HEADER TRANSFERASE 10-DEC-08 2W5H TITLE HUMAN NEK2 KINASE APO COMPND MOL_ID: 1; COMPND 2 MOLECULE: SERINE/THREONINE-PROTEIN KINASE NEK2; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: KINASE DOMAIN, RESIDUES 1-271; COMPND 5 SYNONYM: NIMA-RELATED PROTEIN KINASE 2, NIMA-LIKE PROTEIN COMPND 6 KINASE 1, HSPK 21, NEK2; COMPND 7 EC: 2.7.11.1; COMPND 8 ENGINEERED: YES; COMPND 9 MUTATION: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606; SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008; SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3); SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET22B KEYWDS SER/THR PROTEIN KINASE, KINASE, NUCLEUS, MEIOSIS, MITOSIS, KEYWDS 2 CYTOPLASM, SERINE/THREONINE-PROTEIN KINASE, METAL-BINDING, KEYWDS 3 PHOSPHOPROTEIN, NUCLEOTIDE-BINDING, MAGNESIUM, CELL CYCLE, KEYWDS 4 ATP-BINDING, TRANSFERASE, CENTROSOME SPLITTING, KEYWDS 5 ALTERNATIVE SPLICING, COILED COIL, POLYMORPHISM, CELL KEYWDS 6 DIVISION EXPDTA X-RAY DIFFRACTION AUTHOR R.BAYLISS REVDAT 4 01-SEP-09 2W5H 1 TITLE REVDAT 3 17-FEB-09 2W5H 1 JRNL REVDAT 2 20-JAN-09 2W5H 1 JRNL REVDAT 1 23-DEC-08 2W5H 0 JRNL AUTH I.WESTWOOD,D.M.CHEARY,J.E.BAXTER,M.W.RICHARDS, JRNL AUTH 2 R.L.VAN MONTFORT,A.M.FRY,R.BAYLISS JRNL TITL INSIGHTS INTO THE CONFORMATIONAL VARIABILITY AND JRNL TITL 2 REGULATION OF HUMAN NEK2 KINASE. JRNL REF J.MOL.BIOL. V. 386 476 2009 JRNL REFN ISSN 0022-2836 JRNL PMID 19124027 JRNL DOI 10.1016/J.JMB.2008.12.033 REMARK 2 REMARK 2 RESOLUTION. 2.33 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE) REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE- REMARK 3 : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO, REMARK 3 : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL REMARK 3 : MORIARTY,REETAL PAI,RANDY READ,JANE REMARK 3 : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM REMARK 3 : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH, REMARK 3 : LAURENT STORONI,TOM TERWILLIGER,PETER REMARK 3 : ZWART REMARK 3 REMARK 3 REFINEMENT TARGET : ML REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.33 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 58.61 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.010 REMARK 3 COMPLETENESS FOR RANGE (%) : 88.1 REMARK 3 NUMBER OF REFLECTIONS : 12529 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.197 REMARK 3 R VALUE (WORKING SET) : 0.195 REMARK 3 FREE R VALUE : 0.254 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.700 REMARK 3 FREE R VALUE TEST SET COUNT : 587 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS). REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE REMARK 3 1 58.6261 - 3.6985 0.94 3236 158 0.1806 0.2292 REMARK 3 2 3.6985 - 2.9356 0.94 3175 160 0.1865 0.2536 REMARK 3 3 2.9356 - 2.5645 0.90 3047 150 0.2059 0.2616 REMARK 3 4 2.5645 - 2.3300 0.74 2484 119 0.2170 0.3020 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL REMARK 3 SOLVENT RADIUS : 1.11 REMARK 3 SHRINKAGE RADIUS : 0.90 REMARK 3 K_SOL : 0.34 REMARK 3 B_SOL : 36.42 REMARK 3 REMARK 3 ERROR ESTIMATES. REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.360 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 23.880 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 21.14 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 31.73 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 1.15370 REMARK 3 B22 (A**2) : -4.28670 REMARK 3 B33 (A**2) : 3.13300 REMARK 3 B12 (A**2) : -0.00000 REMARK 3 B13 (A**2) : -6.17790 REMARK 3 B23 (A**2) : 0.00000 REMARK 3 REMARK 3 TWINNING INFORMATION. REMARK 3 FRACTION: NULL REMARK 3 OPERATOR: NULL REMARK 3 REMARK 3 DEVIATIONS FROM IDEAL VALUES. REMARK 3 RMSD COUNT REMARK 3 BOND : 0.006 2209 REMARK 3 ANGLE : 0.964 2983 REMARK 3 CHIRALITY : 0.060 324 REMARK 3 PLANARITY : 0.004 383 REMARK 3 DIHEDRAL : 17.549 820 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 1 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: CHAIN A REMARK 3 ORIGIN FOR THE GROUP (A): -11.8774 0.5080 12.6833 REMARK 3 T TENSOR REMARK 3 T11: 0.0774 T22: 0.1032 REMARK 3 T33: 0.0581 T12: 0.0132 REMARK 3 T13: 0.0197 T23: 0.0105 REMARK 3 L TENSOR REMARK 3 L11: 0.8959 L22: 0.9991 REMARK 3 L33: 0.2125 L12: -0.5467 REMARK 3 L13: 0.1119 L23: -0.0528 REMARK 3 S TENSOR REMARK 3 S11: -0.0941 S12: -0.1266 S13: -0.0530 REMARK 3 S21: 0.1092 S22: 0.0862 S23: -0.0223 REMARK 3 S31: -0.0415 S32: 0.0616 S33: 0.0180 REMARK 3 REMARK 3 NCS DETAILS REMARK 3 NUMBER OF NCS GROUPS : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 2W5H COMPLIES WITH FORMAT V. 3.20, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 11-DEC-08. REMARK 100 THE PDBE ID CODE IS EBI-38313. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : NULL REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : NULL REMARK 200 NUMBER OF CRYSTALS USED : NULL REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : DIAMOND REMARK 200 BEAMLINE : I03 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.92 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : ADSC REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL REMARK 200 DATA SCALING SOFTWARE : NULL REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 12969 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.33 REMARK 200 RESOLUTION RANGE LOW (A) : 58.60 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 3.0 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 91.3 REMARK 200 DATA REDUNDANCY : 3.7 REMARK 200 R MERGE (I) : 0.11 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 6.10 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL REMARK 200 COMPLETENESS FOR SHELL (%) : NULL REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : NULL REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: OTHER REMARK 200 SOFTWARE USED: NULL REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NONE REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 51.85 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.55 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 50 MM TRIS, PH 8.5 2-10% REMARK 280 PEG8000 REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,Y,-Z REMARK 290 3555 X+1/2,Y+1/2,Z REMARK 290 4555 -X+1/2,Y+1/2,-Z REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 49.86950 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 28.48100 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 49.86950 REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 28.48100 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 GENERATING THE BIOMOLECULE REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC REMARK 350 SOFTWARE USED: PQS REMARK 350 APPLY THE FOLLOWING TO CHAINS: A REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 375 REMARK 375 SPECIAL POSITION REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL REMARK 375 POSITIONS. REMARK 375 REMARK 375 ATOM RES CSSEQI REMARK 375 HOH A2067 LIES ON A SPECIAL POSITION. REMARK 400 REMARK 400 COMPOUND REMARK 400 ENGINEERED RESIDUE IN CHAIN A, THR 175 TO ALA REMARK 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 MET A 1 REMARK 465 PRO A 2 REMARK 465 ASP A 132 REMARK 465 GLY A 133 REMARK 465 GLY A 134 REMARK 465 HIS A 135 REMARK 465 THR A 136 REMARK 465 VAL A 137 REMARK 465 LEU A 138 REMARK 465 ILE A 165 REMARK 465 LEU A 166 REMARK 465 ASN A 167 REMARK 465 ARG A 190 REMARK 465 MET A 191 REMARK 470 REMARK 470 MISSING ATOM REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 470 I=INSERTION CODE): REMARK 470 M RES CSSEQI ATOMS REMARK 470 SER A 3 OG REMARK 470 ARG A 4 CG CD NE CZ NH1 NH2 REMARK 470 LYS A 37 CD CE NZ REMARK 470 GLU A 46 CG CD OE1 OE2 REMARK 470 LEU A 58 CG CD1 CD2 REMARK 470 ARG A 60 CG CD NE CZ NH1 NH2 REMARK 470 ASN A 79 CG OD1 ND2 REMARK 470 LYS A 103 CG CD CE NZ REMARK 470 ARG A 164 CG CD NE CZ NH1 NH2 REMARK 470 LYS A 174 CG CD CE NZ 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; REMARK 480 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 480 I=INSERTION CODE): REMARK 480 M RES CSSEQI ATOMS REMARK 480 ARG A 69 CA CB CG CD NE CZ NH1 NH2 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 OG SER A 192 - O HOH A 2067 2.20 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS REMARK 500 REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15 REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375 REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS. REMARK 500 REMARK 500 DISTANCE CUTOFF: REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE REMARK 500 REMARK 500 OG SER A 192 O HOH A 2067 2556 2.20 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 ARG A 140 52.97 -140.73 REMARK 500 LEU A 142 48.23 -96.68 REMARK 500 ASN A 194 102.06 -164.61 REMARK 500 REMARK 500 REMARK: NULL REMARK 525 REMARK 525 SOLVENT REMARK 525 REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER; REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE REMARK 525 NUMBER; I=INSERTION CODE): REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 2W5B RELATED DB: PDB REMARK 900 HUMAN NEK2 KINASE ATPGAMMAS-BOUND REMARK 900 RELATED ID: 2W5A RELATED DB: PDB REMARK 900 HUMAN NEK2 KINASE ADP-BOUND REMARK 900 RELATED ID: 2JAV RELATED DB: PDB REMARK 900 HUMAN KINASE WITH PYRROLE-INDOLINONE LIGAND REMARK 999 REMARK 999 SEQUENCE REMARK 999 C-TERMINAL LEHHHHHH FROM VECTOR SEQUENCE T175A MUTATION DBREF 2W5H A 1 271 UNP P51955 NEK2_HUMAN 1 271 DBREF 2W5H A 272 279 PDB 2W5H 2W5H 272 279 SEQADV 2W5H ALA A 175 UNP P51955 THR 175 ENGINEERED MUTATION SEQRES 1 A 279 MET PRO SER ARG ALA GLU ASP TYR GLU VAL LEU TYR THR SEQRES 2 A 279 ILE GLY THR GLY SER TYR GLY ARG CYS GLN LYS ILE ARG SEQRES 3 A 279 ARG LYS SER ASP GLY LYS ILE LEU VAL TRP LYS GLU LEU SEQRES 4 A 279 ASP TYR GLY SER MET THR GLU ALA GLU LYS GLN MET LEU SEQRES 5 A 279 VAL SER GLU VAL ASN LEU LEU ARG GLU LEU LYS HIS PRO SEQRES 6 A 279 ASN ILE VAL ARG TYR TYR ASP ARG ILE ILE ASP ARG THR SEQRES 7 A 279 ASN THR THR LEU TYR ILE VAL MET GLU TYR CYS GLU GLY SEQRES 8 A 279 GLY ASP LEU ALA SER VAL ILE THR LYS GLY THR LYS GLU SEQRES 9 A 279 ARG GLN TYR LEU ASP GLU GLU PHE VAL LEU ARG VAL MET SEQRES 10 A 279 THR GLN LEU THR LEU ALA LEU LYS GLU CYS HIS ARG ARG SEQRES 11 A 279 SER ASP GLY GLY HIS THR VAL LEU HIS ARG ASP LEU LYS SEQRES 12 A 279 PRO ALA ASN VAL PHE LEU ASP GLY LYS GLN ASN VAL LYS SEQRES 13 A 279 LEU GLY ASP PHE GLY LEU ALA ARG ILE LEU ASN HIS ASP SEQRES 14 A 279 THR SER PHE ALA LYS ALA PHE VAL GLY THR PRO TYR TYR SEQRES 15 A 279 MET SER PRO GLU GLN MET ASN ARG MET SER TYR ASN GLU SEQRES 16 A 279 LYS SER ASP ILE TRP SER LEU GLY CYS LEU LEU TYR GLU SEQRES 17 A 279 LEU CYS ALA LEU MET PRO PRO PHE THR ALA PHE SER GLN SEQRES 18 A 279 LYS GLU LEU ALA GLY LYS ILE ARG GLU GLY LYS PHE ARG SEQRES 19 A 279 ARG ILE PRO TYR ARG TYR SER ASP GLU LEU ASN GLU ILE SEQRES 20 A 279 ILE THR ARG MET LEU ASN LEU LYS ASP TYR HIS ARG PRO SEQRES 21 A 279 SER VAL GLU GLU ILE LEU GLU ASN PRO LEU ILE LEU GLU SEQRES 22 A 279 HIS HIS HIS HIS HIS HIS FORMUL 2 HOH *120(H2 O1) HELIX 1 1 ARG A 4 GLU A 6 5 3 HELIX 2 2 GLY A 42 MET A 44 5 3 HELIX 3 3 ALA A 47 LEU A 62 1 16 HELIX 4 4 LEU A 94 GLU A 104 1 11 HELIX 5 5 ASP A 109 ARG A 130 1 22 HELIX 6 6 LYS A 143 ALA A 145 5 3 HELIX 7 7 PHE A 160 ARG A 164 5 5 HELIX 8 8 HIS A 168 VAL A 177 1 10 HELIX 9 9 SER A 184 ASN A 189 1 6 HELIX 10 10 ASN A 194 LEU A 212 1 19 HELIX 11 11 SER A 220 GLY A 231 1 12 HELIX 12 12 SER A 241 LEU A 252 1 12 HELIX 13 13 LYS A 255 ARG A 259 5 5 HELIX 14 14 SER A 261 GLU A 267 1 7 HELIX 15 15 LEU A 272 HIS A 276 5 5 SHEET 1 AA 5 TYR A 8 GLY A 17 0 SHEET 2 AA 5 GLY A 20 ARG A 27 -1 O GLY A 20 N GLY A 17 SHEET 3 AA 5 ILE A 33 ASP A 40 -1 O LEU A 34 N ILE A 25 SHEET 4 AA 5 THR A 81 GLU A 87 -1 O LEU A 82 N LEU A 39 SHEET 5 AA 5 TYR A 70 ASP A 76 -1 N TYR A 71 O VAL A 85 SHEET 1 AB 3 GLY A 92 ASP A 93 0 SHEET 2 AB 3 VAL A 147 LEU A 149 -1 N LEU A 149 O GLY A 92 SHEET 3 AB 3 VAL A 155 LEU A 157 -1 O LYS A 156 N PHE A 148 CRYST1 99.739 56.962 80.612 90.00 133.36 90.00 C 1 2 1 4 ORIGX1 1.000000 0.000000 0.000000 0.00000 ORIGX2 0.000000 1.000000 0.000000 0.00000 ORIGX3 0.000000 0.000000 1.000000 0.00000 SCALE1 0.010026 0.000000 0.009468 0.00000 SCALE2 0.000000 0.017556 0.000000 0.00000 SCALE3 0.000000 0.000000 0.017062 0.00000 ATOM 1 N SER A 3 2.089 -21.031 20.303 1.00 42.05 N ANISOU 1 N SER A 3 4835 5540 5604 721 124 660 N ATOM 2 CA SER A 3 2.410 -21.019 21.719 1.00 44.83 C ANISOU 2 CA SER A 3 5220 5933 5879 793 95 713 C ATOM 3 C SER A 3 3.804 -20.470 21.975 1.00 46.84 C ANISOU 3 C SER A 3 5466 6232 6101 804 19 657 C ATOM 4 O SER A 3 4.022 -19.849 23.006 1.00 54.07 O ANISOU 4 O SER A 3 6422 7197 6927 850 -23 663 O ATOM 5 CB SER A 3 2.286 -22.416 22.319 1.00 45.75 C ANISOU 5 CB SER A 3 5325 6017 6042 847 123 804 C ATOM 6 N ARG A 4 4.739 -20.688 21.049 1.00 40.66 N ANISOU 6 N ARG A 4 4628 5430 5390 765 1 600 N ATOM 7 CA ARG A 4 6.113 -20.193 21.202 1.00 36.92 C ANISOU 7 CA ARG A 4 4130 4989 4907 770 -70 546 C ATOM 8 C ARG A 4 6.524 -19.142 20.150 1.00 33.44 C ANISOU 8 C ARG A 4 3665 4554 4485 700 -80 459 C ATOM 9 O ARG A 4 6.064 -19.183 19.003 1.00 34.70 O ANISOU 9 O ARG A 4 3809 4684 4692 648 -32 435 O ATOM 10 CB ARG A 4 7.084 -21.378 21.172 1.00 38.44 C ANISOU 10 CB ARG A 4 4273 5157 5174 797 -85 563 C ATOM 11 N ALA A 5 7.393 -18.214 20.555 1.00 34.66 N ANISOU 11 N ALA A 5 3816 4746 4607 704 -145 414 N ATOM 12 CA ALA A 5 7.886 -17.160 19.677 1.00 38.29 C ANISOU 12 CA ALA A 5 4247 5210 5090 642 -158 341 C ATOM 13 C ALA A 5 8.746 -17.755 18.565 1.00 37.55 C ANISOU 13 C ALA A 5 4085 5088 5094 610 -137 312 C ATOM 14 O ALA A 5 8.862 -17.169 17.497 1.00 37.58 O ANISOU 14 O ALA A 5 4066 5084 5129 555 -112 267 O ATOM 15 CB ALA A 5 8.674 -16.145 20.466 1.00 41.16 C ANISOU 15 CB ALA A 5 4614 5611 5413 660 -239 302 C ATOM 16 N GLU A 6 9.346 -18.920 18.821 1.00 31.92 N ANISOU 16 N GLU A 6 3341 4360 4426 649 -146 341 N ATOM 17 CA GLU A 6 10.216 -19.579 17.842 1.00 34.95 C ANISOU 17 CA GLU A 6 3659 4717 4903 629 -127 315 C ATOM 18 C GLU A 6 9.418 -20.204 16.700 1.00 34.20 C ANISOU 18 C GLU A 6 3564 4584 4848 598 -53 316 C ATOM 19 O GLU A 6 9.980 -20.614 15.688 1.00 35.31 O ANISOU 19 O GLU A 6 3658 4704 5054 578 -27 284 O ATOM 20 CB GLU A 6 11.114 -20.632 18.512 1.00 47.39 C ANISOU 20 CB GLU A 6 5201 6286 6518 684 -165 344 C ATOM 21 CG GLU A 6 10.368 -21.833 19.096 1.00 58.96 C ANISOU 21 CG GLU A 6 6696 7728 7978 732 -140 417 C ATOM 22 CD GLU A 6 11.309 -22.822 19.759 1.00 70.92 C ANISOU 22 CD GLU A 6 8177 9237 9532 789 -180 448 C ATOM 23 OE1 GLU A 6 12.522 -22.722 19.484 1.00 74.90 O ANISOU 23 OE1 GLU A 6 8627 9747 10087 783 -216 405 O ATOM 24 OE2 GLU A 6 10.846 -23.685 20.543 1.00 75.12 O ANISOU 24 OE2 GLU A 6 8736 9757 10050 841 -174 519 O ATOM 25 N ASP A 7 8.102 -20.266 16.859 1.00 34.54 N ANISOU 25 N ASP A 7 3658 4617 4851 597 -20 350 N ATOM 26 CA ASP A 7 7.241 -20.839 15.833 1.00 29.28 C ANISOU 26 CA ASP A 7 2993 3909 4225 571 39 347 C ATOM 27 C ASP A 7 6.999 -19.845 14.699 1.00 29.22 C ANISOU 27 C ASP A 7 2989 3909 4204 513 65 290 C ATOM 28 O ASP A 7 6.349 -20.174 13.702 1.00 30.31 O ANISOU 28 O ASP A 7 3129 4017 4370 490 107 274 O ATOM 29 CB ASP A 7 5.900 -21.247 16.440 1.00 30.39 C ANISOU 29 CB ASP A 7 3177 4030 4338 591 64 408 C ATOM 30 CG ASP A 7 6.047 -22.205 17.595 1.00 38.53 C ANISOU 30 CG ASP A 7 4210 5055 5376 653 48 478 C ATOM 31 OD1 ASP A 7 7.030 -22.980 17.597 1.00 43.53 O ANISOU 31 OD1 ASP A 7 4801 5676 6062 676 28 477 O ATOM 32 OD2 ASP A 7 5.171 -22.181 18.489 1.00 41.61 O ANISOU 32 OD2 ASP A 7 4643 5451 5717 681 58 536 O ATOM 33 N TYR A 8 7.511 -18.626 14.866 1.00 23.49 N ANISOU 33 N TYR A 8 2265 3221 3440 493 35 260 N ATOM 34 CA TYR A 8 7.358 -17.566 13.869 1.00 22.21 C ANISOU 34 CA TYR A 8 2107 3067 3265 441 58 214 C ATOM 35 C TYR A 8 8.692 -16.880 13.575 1.00 20.43 C ANISOU 35 C TYR A 8 1834 2862 3068 423 35 174 C ATOM 36 O TYR A 8 9.610 -16.912 14.392 1.00 15.45 O ANISOU 36 O TYR A 8 1175 2245 2449 449 -15 178 O ATOM 37 CB TYR A 8 6.367 -16.501 14.358 1.00 19.81 C ANISOU 37 CB TYR A 8 1858 2781 2886 427 51 221 C ATOM 38 CG TYR A 8 5.028 -17.034 14.794 1.00 22.77 C ANISOU 38 CG TYR A 8 2277 3138 3234 446 75 267 C ATOM 39 CD1 TYR A 8 4.833 -17.514 16.085 1.00 18.45 C ANISOU 39 CD1 TYR A 8 1752 2599 2660 496 53 321 C ATOM 40 CD2 TYR A 8 3.946 -17.042 13.920 1.00 23.67 C ANISOU 40 CD2 TYR A 8 2412 3229 3354 417 119 260 C ATOM 41 CE1 TYR A 8 3.596 -18.003 16.488 1.00 15.59 C ANISOU 41 CE1 TYR A 8 1424 2218 2283 515 84 373 C ATOM 42 CE2 TYR A 8 2.707 -17.529 14.318 1.00 18.78 C ANISOU 42 CE2 TYR A 8 1824 2586 2726 433 142 305 C ATOM 43 CZ TYR A 8 2.541 -18.003 15.602 1.00 17.44 C ANISOU 43 CZ TYR A 8 1669 2422 2535 481 128 364 C ATOM 44 OH TYR A 8 1.320 -18.479 16.002 1.00 25.32 O ANISOU 44 OH TYR A 8 2692 3396 3534 497 159 416 O ATOM 45 N GLU A 9 8.787 -16.245 12.411 1.00 22.59 N ANISOU 45 N GLU A 9 2095 3135 3354 381 72 138 N ATOM 46 CA GLU A 9 9.933 -15.408 12.104 1.00 21.86 C ANISOU 46 CA GLU A 9 1955 3059 3293 358 59 107 C ATOM 47 C GLU A 9 9.503 -13.997 11.745 1.00 21.58 C ANISOU 47 C GLU A 9 1944 3036 3220 314 68 88 C ATOM 48 O GLU A 9 8.686 -13.800 10.852 1.00 24.05 O ANISOU 48 O GLU A 9 2287 3341 3510 291 115 82 O ATOM 49 CB GLU A 9 10.730 -15.998 10.958 1.00 21.85 C ANISOU 49 CB GLU A 9 1901 3046 3355 354 105 87 C ATOM 50 CG GLU A 9 11.964 -15.193 10.637 1.00 33.99 C ANISOU 50 CG GLU A 9 3379 4595 4940 332 101 64 C ATOM 51 CD GLU A 9 12.692 -15.728 9.428 1.00 46.34 C ANISOU 51 CD GLU A 9 4895 6152 6560 333 160 48 C ATOM 52 OE1 GLU A 9 12.017 -16.072 8.432 1.00 52.66 O ANISOU 52 OE1 GLU A 9 5725 6945 7339 331 215 39 O ATOM 53 OE2 GLU A 9 13.939 -15.800 9.472 1.00 45.45 O ANISOU 53 OE2 GLU A 9 4714 6040 6513 341 150 41 O ATOM 54 N VAL A 10 10.055 -13.019 12.453 1.00 23.83 N ANISOU 54 N VAL A 10 2215 3335 3503 306 16 78 N ATOM 55 CA VAL A 10 9.804 -11.627 12.130 1.00 19.70 C ANISOU 55 CA VAL A 10 1706 2818 2960 263 19 59 C ATOM 56 C VAL A 10 10.419 -11.309 10.768 1.00 16.33 C ANISOU 56 C VAL A 10 1235 2384 2585 229 77 43 C ATOM 57 O VAL A 10 11.624 -11.469 10.562 1.00 23.43 O ANISOU 57 O VAL A 10 2067 3281 3553 231 76 35 O ATOM 58 CB VAL A 10 10.391 -10.665 13.205 1.00 18.82 C ANISOU 58 CB VAL A 10 1582 2719 2852 265 -59 44 C ATOM 59 CG1 VAL A 10 10.296 -9.202 12.743 1.00 18.34 C ANISOU 59 CG1 VAL A 10 1521 2654 2793 217 -53 22 C ATOM 60 CG2 VAL A 10 9.678 -10.842 14.529 1.00 18.61 C ANISOU 60 CG2 VAL A 10 1612 2705 2753 307 -110 60 C ATOM 61 N LEU A 11 9.577 -10.876 9.837 1.00 14.69 N ANISOU 61 N LEU A 11 1064 2174 2343 202 129 41 N ATOM 62 CA LEU A 11 10.038 -10.356 8.558 1.00 19.81 C ANISOU 62 CA LEU A 11 1683 2821 3024 173 187 31 C ATOM 63 C LEU A 11 10.558 -8.936 8.744 1.00 30.72 C ANISOU 63 C LEU A 11 3038 4203 4433 137 164 25 C ATOM 64 O LEU A 11 11.696 -8.628 8.381 1.00 37.87 O ANISOU 64 O LEU A 11 3875 5103 5409 124 177 22 O ATOM 65 CB LEU A 11 8.904 -10.377 7.531 1.00 19.33 C ANISOU 65 CB LEU A 11 1677 2758 2909 164 243 31 C ATOM 66 CG LEU A 11 8.610 -11.783 6.997 1.00 25.40 C ANISOU 66 CG LEU A 11 2456 3519 3676 197 275 29 C ATOM 67 CD1 LEU A 11 7.350 -11.842 6.135 1.00 17.87 C ANISOU 67 CD1 LEU A 11 1561 2559 2669 193 311 22 C ATOM 68 CD2 LEU A 11 9.819 -12.278 6.230 1.00 24.37 C ANISOU 68 CD2 LEU A 11 2266 3391 3604 209 314 20 C ATOM 69 N TYR A 12 9.724 -8.080 9.330 1.00 26.69 N ANISOU 69 N TYR A 12 2575 3693 3873 123 129 22 N ATOM 70 CA TYR A 12 10.096 -6.690 9.565 1.00 23.47 C ANISOU 70 CA TYR A 12 2146 3278 3494 90 98 11 C ATOM 71 C TYR A 12 9.000 -5.927 10.304 1.00 19.19 C ANISOU 71 C TYR A 12 1669 2738 2884 85 56 5 C ATOM 72 O TYR A 12 7.848 -6.345 10.334 1.00 19.02 O ANISOU 72 O TYR A 12 1709 2723 2794 99 72 15 O ATOM 73 CB TYR A 12 10.452 -5.985 8.246 1.00 18.26 C ANISOU 73 CB TYR A 12 1456 2610 2873 53 167 19 C ATOM 74 CG TYR A 12 9.290 -5.885 7.285 1.00 20.73 C ANISOU 74 CG TYR A 12 1832 2926 3118 44 227 29 C ATOM 75 CD1 TYR A 12 8.363 -4.855 7.388 1.00 15.97 C ANISOU 75 CD1 TYR A 12 1278 2319 2472 21 214 27 C ATOM 76 CD2 TYR A 12 9.116 -6.826 6.280 1.00 20.62 C ANISOU 76 CD2 TYR A 12 1828 2920 3085 63 290 35 C ATOM 77 CE1 TYR A 12 7.298 -4.765 6.518 1.00 13.44 C ANISOU 77 CE1 TYR A 12 1014 2002 2092 15 262 35 C ATOM 78 CE2 TYR A 12 8.062 -6.740 5.402 1.00 13.98 C ANISOU 78 CE2 TYR A 12 1046 2082 2184 60 334 37 C ATOM 79 CZ TYR A 12 7.156 -5.708 5.525 1.00 15.86 C ANISOU 79 CZ TYR A 12 1330 2316 2381 35 319 39 C ATOM 80 OH TYR A 12 6.105 -5.631 4.647 1.00 20.07 O ANISOU 80 OH TYR A 12 1918 2851 2856 34 358 41 O ATOM 81 N THR A 13 9.380 -4.801 10.893 1.00 19.20 N ANISOU 81 N THR A 13 1652 2729 2912 67 2 -13 N ATOM 82 CA THR A 13 8.459 -3.959 11.642 1.00 19.15 C ANISOU 82 CA THR A 13 1704 2725 2848 66 -42 -26 C ATOM 83 C THR A 13 7.600 -3.147 10.690 1.00 19.36 C ANISOU 83 C THR A 13 1765 2742 2850 29 12 -18 C ATOM 84 O THR A 13 8.108 -2.478 9.801 1.00 20.66 O ANISOU 84 O THR A 13 1890 2891 3068 -6 48 -13 O ATOM 85 CB THR A 13 9.225 -3.013 12.572 1.00 22.81 C ANISOU 85 CB THR A 13 2133 3177 3357 63 -128 -58 C ATOM 86 OG1 THR A 13 10.046 -3.791 13.450 1.00 24.95 O ANISOU 86 OG1 THR A 13 2373 3458 3649 102 -184 -67 O ATOM 87 CG2 THR A 13 8.270 -2.167 13.396 1.00 23.94 C ANISOU 87 CG2 THR A 13 2339 3323 3433 70 -176 -77 C ATOM 88 N ILE A 14 6.289 -3.226 10.870 1.00 19.86 N ANISOU 88 N ILE A 14 1899 2815 2834 41 20 -11 N ATOM 89 CA ILE A 14 5.359 -2.563 9.977 1.00 24.41 C ANISOU 89 CA ILE A 14 2512 3382 3379 12 67 -3 C ATOM 90 C ILE A 14 5.177 -1.144 10.456 1.00 36.12 C ANISOU 90 C ILE A 14 4007 4852 4866 -10 23 -22 C ATOM 91 O ILE A 14 5.230 -0.186 9.685 1.00 43.18 O ANISOU 91 O ILE A 14 4889 5728 5790 -47 50 -19 O ATOM 92 CB ILE A 14 3.995 -3.261 9.976 1.00 27.09 C ANISOU 92 CB ILE A 14 2916 3732 3645 34 91 10 C ATOM 93 CG1 ILE A 14 4.087 -4.594 9.228 1.00 29.60 C ANISOU 93 CG1 ILE A 14 3223 4054 3970 50 140 24 C ATOM 94 CG2 ILE A 14 2.951 -2.384 9.326 1.00 27.21 C ANISOU 94 CG2 ILE A 14 2975 3738 3626 8 119 12 C ATOM 95 CD1 ILE A 14 2.800 -5.361 9.197 1.00 23.37 C ANISOU 95 CD1 ILE A 14 2485 3265 3129 71 159 36 C ATOM 96 N GLY A 15 4.958 -1.021 11.752 1.00 40.19 N ANISOU 96 N GLY A 15 4547 5375 5349 19 -44 -41 N ATOM 97 CA GLY A 15 4.803 0.275 12.361 1.00 48.12 C ANISOU 97 CA GLY A 15 5564 6366 6354 7 -98 -69 C ATOM 98 C GLY A 15 4.871 0.128 13.857 1.00 53.85 C ANISOU 98 C GLY A 15 6310 7109 7043 55 -178 -93 C ATOM 99 O GLY A 15 4.432 -0.879 14.411 1.00 58.80 O ANISOU 99 O GLY A 15 6969 7761 7612 98 -174 -77 O ATOM 100 N THR A 16 5.439 1.130 14.510 1.00 52.42 N ANISOU 100 N THR A 16 6108 6912 6898 52 -251 -133 N ATOM 101 CA THR A 16 5.445 1.174 15.957 1.00 53.83 C ANISOU 101 CA THR A 16 6316 7108 7030 105 -336 -165 C ATOM 102 C THR A 16 4.139 1.796 16.441 1.00 62.60 C ANISOU 102 C THR A 16 7502 8227 8056 123 -341 -173 C ATOM 103 O THR A 16 3.831 2.941 16.114 1.00 63.66 O ANISOU 103 O THR A 16 7641 8336 8211 89 -345 -192 O ATOM 104 CB THR A 16 6.632 1.989 16.480 1.00 51.52 C ANISOU 104 CB THR A 16 5968 6792 6817 99 -425 -214 C ATOM 105 OG1 THR A 16 7.835 1.542 15.841 1.00 50.02 O ANISOU 105 OG1 THR A 16 5696 6587 6723 72 -408 -201 O ATOM 106 CG2 THR A 16 6.766 1.819 17.981 1.00 52.63 C ANISOU 106 CG2 THR A 16 6139 6957 6900 167 -519 -249 C ATOM 107 N GLY A 17 3.363 1.029 17.198 1.00 70.58 N ANISOU 107 N GLY A 17 8569 9271 8976 177 -335 -154 N ATOM 108 CA GLY A 17 2.131 1.533 17.773 1.00 76.23 C ANISOU 108 CA GLY A 17 9355 9999 9609 204 -336 -159 C ATOM 109 C GLY A 17 2.437 2.420 18.961 1.00 80.70 C ANISOU 109 C GLY A 17 9940 10569 10154 243 -433 -215 C ATOM 110 O GLY A 17 3.599 2.568 19.355 1.00 82.92 O ANISOU 110 O GLY A 17 10178 10843 10486 250 -504 -251 O ATOM 111 N SER A 18 1.399 3.024 19.532 1.00 80.19 N ANISOU 111 N SER A 18 9938 10515 10016 272 -440 -228 N ATOM 112 CA SER A 18 1.582 3.866 20.709 1.00 78.76 C ANISOU 112 CA SER A 18 9785 10341 9800 321 -535 -288 C ATOM 113 C SER A 18 1.973 2.996 21.894 1.00 75.90 C ANISOU 113 C SER A 18 9445 10021 9372 401 -581 -287 C ATOM 114 O SER A 18 2.574 3.469 22.868 1.00 75.39 O ANISOU 114 O SER A 18 9389 9964 9293 448 -678 -343 O ATOM 115 CB SER A 18 0.299 4.637 21.033 1.00 79.60 C ANISOU 115 CB SER A 18 9958 10452 9836 341 -521 -298 C ATOM 116 OG SER A 18 -0.118 5.438 19.932 1.00 78.84 O ANISOU 116 OG SER A 18 9844 10316 9796 271 -479 -295 O ATOM 117 N TYR A 19 1.638 1.714 21.785 1.00 71.81 N ANISOU 117 N TYR A 19 8937 9528 8820 419 -513 -222 N ATOM 118 CA TYR A 19 1.831 0.771 22.874 1.00 66.69 C ANISOU 118 CA TYR A 19 8317 8922 8101 500 -538 -203 C ATOM 119 C TYR A 19 2.629 -0.446 22.435 1.00 57.01 C ANISOU 119 C TYR A 19 7039 7695 6928 486 -513 -163 C ATOM 120 O TYR A 19 2.347 -1.561 22.867 1.00 56.07 O ANISOU 120 O TYR A 19 6943 7602 6758 533 -479 -111 O ATOM 121 CB TYR A 19 0.478 0.321 23.428 1.00 69.38 C ANISOU 121 CB TYR A 19 8730 9295 8335 555 -477 -152 C ATOM 122 CG TYR A 19 -0.491 1.451 23.712 1.00 73.29 C ANISOU 122 CG TYR A 19 9278 9791 8780 566 -481 -183 C ATOM 123 CD1 TYR A 19 -0.523 2.079 24.957 1.00 77.24 C ANISOU 123 CD1 TYR A 19 9831 10319 9198 643 -555 -229 C ATOM 124 CD2 TYR A 19 -1.389 1.877 22.740 1.00 70.80 C ANISOU 124 CD2 TYR A 19 8960 9447 8494 505 -413 -166 C ATOM 125 CE1 TYR A 19 -1.418 3.106 25.215 1.00 77.77 C ANISOU 125 CE1 TYR A 19 9946 10385 9219 657 -557 -260 C ATOM 126 CE2 TYR A 19 -2.279 2.898 22.990 1.00 72.88 C ANISOU 126 CE2 TYR A 19 9268 9708 8715 516 -416 -193 C ATOM 127 CZ TYR A 19 -2.290 3.510 24.225 1.00 76.73 C ANISOU 127 CZ TYR A 19 9806 10222 9126 591 -486 -240 C ATOM 128 OH TYR A 19 -3.185 4.526 24.456 1.00 79.75 O ANISOU 128 OH TYR A 19 10233 10601 9468 605 -487 -269 O ATOM 129 N GLY A 20 3.627 -0.226 21.586 1.00 50.71 N ANISOU 129 N GLY A 20 6168 6863 6236 423 -527 -186 N ATOM 130 CA GLY A 20 4.509 -1.295 21.156 1.00 44.85 C ANISOU 130 CA GLY A 20 5371 6119 5553 411 -509 -157 C ATOM 131 C GLY A 20 4.522 -1.484 19.655 1.00 44.45 C ANISOU 131 C GLY A 20 5272 6037 5580 333 -428 -131 C ATOM 132 O GLY A 20 3.688 -0.928 18.939 1.00 46.96 O ANISOU 132 O GLY A 20 5608 6340 5896 293 -377 -125 O ATOM 133 N ARG A 21 5.474 -2.277 19.177 1.00 43.00 N ANISOU 133 N ARG A 21 5028 5845 5463 318 -417 -117 N ATOM 134 CA ARG A 21 5.630 -2.498 17.745 1.00 37.52 C ANISOU 134 CA ARG A 21 4288 5127 4840 254 -342 -96 C ATOM 135 C ARG A 21 4.618 -3.473 17.154 1.00 36.60 C ANISOU 135 C ARG A 21 4203 5017 4686 254 -253 -44 C ATOM 136 O ARG A 21 4.209 -4.445 17.789 1.00 29.79 O ANISOU 136 O ARG A 21 3371 4173 3773 303 -244 -12 O ATOM 137 CB ARG A 21 7.043 -2.976 17.412 1.00 34.27 C ANISOU 137 CB ARG A 21 3798 4704 4519 241 -358 -102 C ATOM 138 CG ARG A 21 8.130 -1.961 17.714 1.00 40.13 C ANISOU 138 CG ARG A 21 4488 5426 5333 226 -439 -154 C ATOM 139 CD ARG A 21 9.482 -2.451 17.238 1.00 38.54 C ANISOU 139 CD ARG A 21 4200 5209 5234 208 -441 -153 C ATOM 140 NE ARG A 21 9.814 -3.742 17.826 1.00 36.86 N ANISOU 140 NE ARG A 21 3988 5021 4997 261 -455 -132 N ATOM 141 CZ ARG A 21 10.967 -4.379 17.641 1.00 35.54 C ANISOU 141 CZ ARG A 21 3750 4846 4906 262 -465 -130 C ATOM 142 NH1 ARG A 21 11.164 -5.549 18.226 1.00 30.57 N ANISOU 142 NH1 ARG A 21 3129 4239 4248 315 -478 -108 N ATOM 143 NH2 ARG A 21 11.920 -3.853 16.877 1.00 37.53 N ANISOU 143 NH2 ARG A 21 3923 5069 5269 213 -458 -146 N ATOM 144 N CYS A 22 4.226 -3.194 15.920 1.00 34.09 N ANISOU 144 N CYS A 22 3877 4679 4398 201 -190 -36 N ATOM 145 CA CYS A 22 3.488 -4.143 15.112 1.00 28.00 C ANISOU 145 CA CYS A 22 3118 3904 3616 194 -113 2 C ATOM 146 C CYS A 22 4.473 -4.739 14.097 1.00 22.66 C ANISOU 146 C CYS A 22 2380 3216 3014 167 -80 6 C ATOM 147 O CYS A 22 5.221 -4.012 13.455 1.00 20.76 O ANISOU 147 O CYS A 22 2096 2960 2830 129 -80 -14 O ATOM 148 CB CYS A 22 2.336 -3.428 14.406 1.00 21.93 C ANISOU 148 CB CYS A 22 2387 3123 2822 161 -70 5 C ATOM 149 SG CYS A 22 1.433 -4.467 13.265 1.00 35.99 S ANISOU 149 SG CYS A 22 4180 4894 4602 149 13 39 S ATOM 150 N GLN A 23 4.498 -6.058 13.962 1.00 19.75 N ANISOU 150 N GLN A 23 2003 2850 2650 191 -50 32 N ATOM 151 CA GLN A 23 5.477 -6.673 13.065 1.00 16.47 C ANISOU 151 CA GLN A 23 1529 2425 2302 175 -20 32 C ATOM 152 C GLN A 23 4.875 -7.680 12.102 1.00 13.71 C ANISOU 152 C GLN A 23 1189 2066 1952 173 47 53 C ATOM 153 O GLN A 23 3.970 -8.427 12.454 1.00 13.68 O ANISOU 153 O GLN A 23 1222 2062 1914 199 58 76 O ATOM 154 CB GLN A 23 6.628 -7.310 13.856 1.00 17.31 C ANISOU 154 CB GLN A 23 1593 2540 2443 209 -69 30 C ATOM 155 CG GLN A 23 7.457 -6.319 14.645 1.00 17.00 C ANISOU 155 CG GLN A 23 1530 2504 2424 209 -145 -2 C ATOM 156 CD GLN A 23 8.528 -6.975 15.490 1.00 26.85 C ANISOU 156 CD GLN A 23 2739 3760 3702 249 -203 -6 C ATOM 157 OE1 GLN A 23 8.239 -7.815 16.342 1.00 39.70 O ANISOU 157 OE1 GLN A 23 4397 5403 5282 300 -222 16 O ATOM 158 NE2 GLN A 23 9.776 -6.579 15.268 1.00 18.72 N ANISOU 158 NE2 GLN A 23 1639 2718 2755 228 -232 -31 N ATOM 159 N LYS A 24 5.384 -7.688 10.877 1.00 18.31 N ANISOU 159 N LYS A 24 1738 2641 2579 146 91 44 N ATOM 160 CA LYS A 24 4.950 -8.668 9.896 1.00 23.45 C ANISOU 160 CA LYS A 24 2396 3282 3233 151 147 53 C ATOM 161 C LYS A 24 5.750 -9.923 10.167 1.00 24.61 C ANISOU 161 C LYS A 24 2503 3427 3419 183 140 61 C ATOM 162 O LYS A 24 6.975 -9.873 10.227 1.00 25.09 O ANISOU 162 O LYS A 24 2512 3493 3529 183 125 52 O ATOM 163 CB LYS A 24 5.208 -8.162 8.484 1.00 23.50 C ANISOU 163 CB LYS A 24 2386 3284 3258 119 198 41 C ATOM 164 CG LYS A 24 4.658 -9.042 7.380 1.00 20.66 C ANISOU 164 CG LYS A 24 2044 2916 2890 129 249 39 C ATOM 165 CD LYS A 24 4.274 -8.150 6.222 1.00 30.01 C ANISOU 165 CD LYS A 24 3249 4102 4052 101 290 31 C ATOM 166 CE LYS A 24 4.664 -8.745 4.899 1.00 33.96 C ANISOU 166 CE LYS A 24 3735 4603 4566 112 344 21 C ATOM 167 NZ LYS A 24 4.496 -7.732 3.825 1.00 32.65 N ANISOU 167 NZ LYS A 24 3587 4444 4376 90 385 21 N ATOM 168 N ILE A 25 5.060 -11.046 10.348 1.00 24.68 N ANISOU 168 N ILE A 25 2534 3426 3417 212 150 79 N ATOM 169 CA ILE A 25 5.726 -12.292 10.711 1.00 19.01 C ANISOU 169 CA ILE A 25 1783 2702 2738 247 141 91 C ATOM 170 C ILE A 25 5.292 -13.469 9.840 1.00 12.72 C ANISOU 170 C ILE A 25 988 1883 1964 259 184 91 C ATOM 171 O ILE A 25 4.218 -13.458 9.249 1.00 15.10 O ANISOU 171 O ILE A 25 1325 2171 2243 248 210 88 O ATOM 172 CB ILE A 25 5.481 -12.647 12.185 1.00 13.25 C ANISOU 172 CB ILE A 25 1073 1979 1981 284 95 121 C ATOM 173 CG1 ILE A 25 3.982 -12.770 12.459 1.00 13.29 C ANISOU 173 CG1 ILE A 25 1134 1975 1941 291 112 146 C ATOM 174 CG2 ILE A 25 6.131 -11.606 13.100 1.00 10.79 C ANISOU 174 CG2 ILE A 25 756 1691 1653 284 38 109 C ATOM 175 CD1 ILE A 25 3.649 -13.080 13.881 1.00 17.93 C ANISOU 175 CD1 ILE A 25 1747 2572 2493 334 80 184 C ATOM 176 N ARG A 26 6.138 -14.491 9.779 1.00 16.40 N ANISOU 176 N ARG A 26 1411 2340 2479 284 185 91 N ATOM 177 CA ARG A 26 5.837 -15.690 9.016 1.00 22.33 C ANISOU 177 CA ARG A 26 2158 3064 3262 302 217 85 C ATOM 178 C ARG A 26 5.835 -16.919 9.922 1.00 23.66 C ANISOU 178 C ARG A 26 2316 3212 3460 341 195 118 C ATOM 179 O ARG A 26 6.826 -17.218 10.577 1.00 31.80 O ANISOU 179 O ARG A 26 3312 4253 4518 362 168 128 O ATOM 180 CB ARG A 26 6.844 -15.861 7.879 1.00 28.78 C ANISOU 180 CB ARG A 26 2934 3885 4117 300 251 53 C ATOM 181 CG ARG A 26 6.698 -17.184 7.141 1.00 41.02 C ANISOU 181 CG ARG A 26 4476 5406 5704 328 276 38 C ATOM 182 CD ARG A 26 7.956 -17.529 6.365 1.00 46.07 C ANISOU 182 CD ARG A 26 5065 6053 6387 341 303 13 C ATOM 183 NE ARG A 26 8.372 -18.902 6.638 1.00 51.13 N ANISOU 183 NE ARG A 26 5675 6669 7084 379 292 17 N ATOM 184 CZ ARG A 26 8.386 -19.878 5.737 1.00 49.42 C ANISOU 184 CZ ARG A 26 5450 6430 6898 405 318 -13 C ATOM 185 NH1 ARG A 26 8.020 -19.642 4.488 1.00 52.09 N ANISOU 185 NH1 ARG A 26 5813 6771 7208 401 355 -50 N ATOM 186 NH2 ARG A 26 8.774 -21.094 6.086 1.00 50.22 N ANISOU 186 NH2 ARG A 26 5521 6504 7058 439 303 -7 N ATOM 187 N ARG A 27 4.712 -17.625 9.961 1.00 20.86 N ANISOU 187 N ARG A 27 1989 2828 3108 353 206 136 N ATOM 188 CA ARG A 27 4.612 -18.842 10.751 1.00 24.70 C ANISOU 188 CA ARG A 27 2465 3288 3632 391 193 175 C ATOM 189 C ARG A 27 5.383 -19.980 10.071 1.00 28.48 C ANISOU 189 C ARG A 27 2899 3742 4180 411 205 154 C ATOM 190 O ARG A 27 5.172 -20.273 8.891 1.00 29.58 O ANISOU 190 O ARG A 27 3037 3862 4340 404 232 114 O ATOM 191 CB ARG A 27 3.147 -19.216 10.934 1.00 25.19 C ANISOU 191 CB ARG A 27 2561 3318 3691 394 206 204 C ATOM 192 CG ARG A 27 2.922 -20.569 11.567 1.00 30.62 C ANISOU 192 CG ARG A 27 3234 3967 4435 431 204 250 C ATOM 193 CD ARG A 27 1.552 -21.075 11.183 1.00 36.04 C ANISOU 193 CD ARG A 27 3936 4604 5152 426 226 260 C ATOM 194 NE ARG A 27 0.508 -20.405 11.942 1.00 34.17 N ANISOU 194 NE ARG A 27 3738 4378 4866 420 231 300 N ATOM 195 CZ ARG A 27 -0.765 -20.354 11.573 1.00 31.42 C ANISOU 195 CZ ARG A 27 3408 3999 4530 403 249 302 C ATOM 196 NH1 ARG A 27 -1.147 -20.917 10.439 1.00 28.80 N ANISOU 196 NH1 ARG A 27 3062 3625 4254 392 256 260 N ATOM 197 NH2 ARG A 27 -1.653 -19.726 12.329 1.00 29.59 N ANISOU 197 NH2 ARG A 27 3209 3781 4254 402 256 342 N ATOM 198 N LYS A 28 6.272 -20.624 10.819 1.00 24.17 N ANISOU 198 N LYS A 28 2320 3196 3667 442 181 177 N ATOM 199 CA LYS A 28 7.211 -21.577 10.226 1.00 28.29 C ANISOU 199 CA LYS A 28 2794 3701 4255 463 190 154 C ATOM 200 C LYS A 28 6.563 -22.825 9.620 1.00 31.35 C ANISOU 200 C LYS A 28 3179 4033 4698 481 209 147 C ATOM 201 O LYS A 28 6.974 -23.288 8.556 1.00 34.49 O ANISOU 201 O LYS A 28 3555 4418 5133 487 229 101 O ATOM 202 CB LYS A 28 8.286 -21.970 11.238 1.00 24.07 C ANISOU 202 CB LYS A 28 2224 3177 3746 495 153 183 C ATOM 203 CG LYS A 28 9.184 -20.819 11.661 1.00 25.34 C ANISOU 203 CG LYS A 28 2370 3384 3873 480 125 173 C ATOM 204 CD LYS A 28 10.311 -21.301 12.565 1.00 27.55 C ANISOU 204 CD LYS A 28 2609 3672 4188 517 82 194 C ATOM 205 CE LYS A 28 11.440 -20.297 12.590 1.00 25.56 C ANISOU 205 CE LYS A 28 2320 3453 3937 499 57 165 C ATOM 206 NZ LYS A 28 12.594 -20.796 13.373 1.00 24.46 N ANISOU 206 NZ LYS A 28 2134 3318 3841 537 9 178 N ATOM 207 N SER A 29 5.552 -23.359 10.297 1.00 26.11 N ANISOU 207 N SER A 29 2537 3337 4046 493 203 193 N ATOM 208 CA SER A 29 4.895 -24.590 9.860 1.00 32.95 C ANISOU 208 CA SER A 29 3394 4141 4985 510 214 191 C ATOM 209 C SER A 29 4.416 -24.549 8.409 1.00 37.94 C ANISOU 209 C SER A 29 4036 4755 5624 492 234 124 C ATOM 210 O SER A 29 4.659 -25.487 7.648 1.00 40.12 O ANISOU 210 O SER A 29 4288 4995 5961 512 238 86 O ATOM 211 CB SER A 29 3.731 -24.942 10.783 1.00 29.80 C ANISOU 211 CB SER A 29 3016 3709 4596 518 212 258 C ATOM 212 OG SER A 29 2.724 -23.953 10.747 1.00 33.52 O ANISOU 212 OG SER A 29 3530 4198 5008 487 222 258 O ATOM 213 N ASP A 30 3.743 -23.469 8.022 1.00 36.32 N ANISOU 213 N ASP A 30 3869 4575 5355 459 244 106 N ATOM 214 CA ASP A 30 3.203 -23.369 6.666 1.00 35.42 C ANISOU 214 CA ASP A 30 3774 4448 5238 448 258 44 C ATOM 215 C ASP A 30 3.604 -22.102 5.912 1.00 34.01 C ANISOU 215 C ASP A 30 3614 4324 4984 422 277 6 C ATOM 216 O ASP A 30 3.247 -21.936 4.749 1.00 36.49 O ANISOU 216 O ASP A 30 3949 4636 5281 419 290 -44 O ATOM 217 CB ASP A 30 1.680 -23.530 6.667 1.00 31.52 C ANISOU 217 CB ASP A 30 3305 3910 4760 437 252 55 C ATOM 218 CG ASP A 30 0.991 -22.583 7.625 1.00 36.99 C ANISOU 218 CG ASP A 30 4029 4628 5399 414 252 107 C ATOM 219 OD1 ASP A 30 1.698 -21.849 8.348 1.00 37.27 O ANISOU 219 OD1 ASP A 30 4066 4712 5383 408 249 133 O ATOM 220 OD2 ASP A 30 -0.260 -22.574 7.661 1.00 35.23 O ANISOU 220 OD2 ASP A 30 3825 4374 5188 403 252 121 O ATOM 221 N GLY A 31 4.345 -21.213 6.566 1.00 32.07 N ANISOU 221 N GLY A 31 3363 4126 4698 408 275 31 N ATOM 222 CA GLY A 31 4.761 -19.970 5.935 1.00 31.76 C ANISOU 222 CA GLY A 31 3334 4131 4600 381 294 6 C ATOM 223 C GLY A 31 3.639 -18.947 5.839 1.00 25.42 C ANISOU 223 C GLY A 31 2580 3338 3740 350 295 9 C ATOM 224 O GLY A 31 3.696 -18.019 5.034 1.00 25.08 O ANISOU 224 O GLY A 31 2554 3322 3653 330 315 -17 O ATOM 225 N LYS A 32 2.617 -19.124 6.669 1.00 24.27 N ANISOU 225 N LYS A 32 2456 3170 3597 348 276 45 N ATOM 226 CA LYS A 32 1.465 -18.229 6.702 1.00 22.89 C ANISOU 226 CA LYS A 32 2324 2999 3375 321 276 52 C ATOM 227 C LYS A 32 1.907 -16.836 7.123 1.00 26.41 C ANISOU 227 C LYS A 32 2780 3492 3761 296 273 62 C ATOM 228 O LYS A 32 2.385 -16.654 8.238 1.00 26.21 O ANISOU 228 O LYS A 32 2744 3484 3729 301 253 95 O ATOM 229 CB LYS A 32 0.441 -18.764 7.703 1.00 23.87 C ANISOU 229 CB LYS A 32 2457 3090 3523 331 263 100 C ATOM 230 CG LYS A 32 -0.978 -18.811 7.193 1.00 29.81 C ANISOU 230 CG LYS A 32 3235 3807 4284 321 266 90 C ATOM 231 CD LYS A 32 -1.696 -17.482 7.287 1.00 34.02 C ANISOU 231 CD LYS A 32 3808 4367 4752 291 269 94 C ATOM 232 CE LYS A 32 -3.158 -17.663 6.873 1.00 38.96 C ANISOU 232 CE LYS A 32 4451 4950 5401 285 268 88 C ATOM 233 NZ LYS A 32 -3.826 -16.379 6.559 1.00 41.08 N ANISOU 233 NZ LYS A 32 4758 5242 5608 257 270 75 N ATOM 234 N ILE A 33 1.769 -15.856 6.234 1.00 21.61 N ANISOU 234 N ILE A 33 2195 2905 3113 271 290 33 N ATOM 235 CA ILE A 33 2.060 -14.474 6.600 1.00 12.64 C ANISOU 235 CA ILE A 33 1068 1804 1930 243 285 42 C ATOM 236 C ILE A 33 1.017 -13.891 7.562 1.00 24.29 C ANISOU 236 C ILE A 33 2579 3279 3372 232 265 72 C ATOM 237 O ILE A 33 -0.194 -13.968 7.322 1.00 25.13 O ANISOU 237 O ILE A 33 2715 3363 3471 229 270 72 O ATOM 238 CB ILE A 33 2.226 -13.573 5.368 1.00 16.01 C ANISOU 238 CB ILE A 33 1507 2249 2327 221 314 11 C ATOM 239 CG1 ILE A 33 3.366 -14.104 4.507 1.00 19.14 C ANISOU 239 CG1 ILE A 33 1867 2653 2753 238 342 -13 C ATOM 240 CG2 ILE A 33 2.600 -12.182 5.805 1.00 16.69 C ANISOU 240 CG2 ILE A 33 1595 2363 2384 191 306 22 C ATOM 241 CD1 ILE A 33 4.662 -14.220 5.301 1.00 15.78 C ANISOU 241 CD1 ILE A 33 1390 2241 2364 244 328 4 C ATOM 242 N LEU A 34 1.507 -13.313 8.657 1.00 25.04 N ANISOU 242 N LEU A 34 2669 3397 3448 232 240 94 N ATOM 243 CA LEU A 34 0.674 -12.782 9.731 1.00 15.27 C ANISOU 243 CA LEU A 34 1465 2166 2173 233 220 123 C ATOM 244 C LEU A 34 1.314 -11.531 10.334 1.00 18.42 C ANISOU 244 C LEU A 34 1866 2597 2538 219 192 117 C ATOM 245 O LEU A 34 2.376 -11.089 9.891 1.00 22.79 O ANISOU 245 O LEU A 34 2388 3163 3108 203 191 95 O ATOM 246 CB LEU A 34 0.531 -13.844 10.829 1.00 13.98 C ANISOU 246 CB LEU A 34 1295 1989 2028 272 207 165 C ATOM 247 CG LEU A 34 -0.269 -15.113 10.514 1.00 17.40 C ANISOU 247 CG LEU A 34 1725 2380 2508 289 228 181 C ATOM 248 CD1 LEU A 34 0.279 -16.294 11.297 1.00 16.75 C ANISOU 248 CD1 LEU A 34 1614 2285 2466 327 219 216 C ATOM 249 CD2 LEU A 34 -1.765 -14.916 10.782 1.00 17.64 C ANISOU 249 CD2 LEU A 34 1789 2391 2522 285 240 205 C ATOM 250 N VAL A 35 0.682 -10.968 11.358 1.00 13.88 N ANISOU 250 N VAL A 35 1322 2031 1919 227 171 137 N ATOM 251 CA VAL A 35 1.331 -9.924 12.135 1.00 19.90 C ANISOU 251 CA VAL A 35 2085 2821 2655 224 131 127 C ATOM 252 C VAL A 35 1.228 -10.255 13.613 1.00 19.69 C ANISOU 252 C VAL A 35 2076 2808 2598 270 98 159 C ATOM 253 O VAL A 35 0.453 -11.121 14.011 1.00 17.02 O ANISOU 253 O VAL A 35 1754 2458 2256 298 117 196 O ATOM 254 CB VAL A 35 0.719 -8.530 11.873 1.00 21.62 C ANISOU 254 CB VAL A 35 2334 3044 2837 192 130 109 C ATOM 255 CG1 VAL A 35 0.813 -8.169 10.394 1.00 17.61 C ANISOU 255 CG1 VAL A 35 1814 2525 2351 153 166 85 C ATOM 256 CG2 VAL A 35 -0.723 -8.486 12.351 1.00 17.31 C ANISOU 256 CG2 VAL A 35 1836 2492 2250 205 141 132 C ATOM 257 N TRP A 36 2.034 -9.592 14.428 1.00 17.16 N ANISOU 257 N TRP A 36 1748 2510 2259 281 48 145 N ATOM 258 CA TRP A 36 1.804 -9.639 15.862 1.00 19.18 C ANISOU 258 CA TRP A 36 2037 2788 2464 331 13 170 C ATOM 259 C TRP A 36 2.022 -8.273 16.474 1.00 18.90 C ANISOU 259 C TRP A 36 2020 2773 2389 329 -38 137 C ATOM 260 O TRP A 36 2.737 -7.430 15.923 1.00 17.85 O ANISOU 260 O TRP A 36 1858 2636 2288 290 -57 97 O ATOM 261 CB TRP A 36 2.623 -10.723 16.598 1.00 15.43 C ANISOU 261 CB TRP A 36 1538 2320 2006 378 -11 195 C ATOM 262 CG TRP A 36 4.125 -10.551 16.620 1.00 13.62 C ANISOU 262 CG TRP A 36 1259 2099 1816 375 -59 162 C ATOM 263 CD1 TRP A 36 4.827 -9.395 16.457 1.00 11.07 C ANISOU 263 CD1 TRP A 36 917 1782 1507 345 -96 116 C ATOM 264 CD2 TRP A 36 5.095 -11.589 16.831 1.00 11.38 C ANISOU 264 CD2 TRP A 36 935 1814 1576 403 -75 175 C ATOM 265 NE1 TRP A 36 6.182 -9.648 16.535 1.00 11.53 N ANISOU 265 NE1 TRP A 36 921 1843 1619 351 -134 99 N ATOM 266 CE2 TRP A 36 6.373 -10.981 16.763 1.00 13.80 C ANISOU 266 CE2 TRP A 36 1195 2127 1922 388 -122 133 C ATOM 267 CE3 TRP A 36 5.020 -12.966 17.055 1.00 19.53 C ANISOU 267 CE3 TRP A 36 1960 2834 2625 440 -54 218 C ATOM 268 CZ2 TRP A 36 7.555 -11.714 16.926 1.00 22.81 C ANISOU 268 CZ2 TRP A 36 2285 3267 3115 409 -150 132 C ATOM 269 CZ3 TRP A 36 6.204 -13.693 17.212 1.00 22.97 C ANISOU 269 CZ3 TRP A 36 2348 3268 3109 462 -82 218 C ATOM 270 CH2 TRP A 36 7.449 -13.061 17.146 1.00 20.13 C ANISOU 270 CH2 TRP A 36 1945 2920 2785 447 -129 174 C ATOM 271 N LYS A 37 1.376 -8.053 17.609 1.00 22.69 N ANISOU 271 N LYS A 37 2548 3273 2801 372 -57 154 N ATOM 272 CA LYS A 37 1.521 -6.806 18.333 1.00 22.94 C ANISOU 272 CA LYS A 37 2605 3325 2789 382 -114 118 C ATOM 273 C LYS A 37 2.364 -7.066 19.571 1.00 26.78 C ANISOU 273 C LYS A 37 3092 3837 3246 443 -180 116 C ATOM 274 O LYS A 37 2.078 -7.975 20.348 1.00 27.93 O ANISOU 274 O LYS A 37 3261 3998 3354 499 -170 163 O ATOM 275 CB LYS A 37 0.149 -6.237 18.697 1.00 20.72 C ANISOU 275 CB LYS A 37 2381 3049 2442 394 -90 131 C ATOM 276 CG LYS A 37 -0.718 -5.929 17.492 1.00 25.75 C ANISOU 276 CG LYS A 37 3019 3659 3107 338 -34 130 C ATOM 277 N GLU A 38 3.413 -6.268 19.727 1.00 31.58 N ANISOU 277 N GLU A 38 3671 4448 3878 432 -248 64 N ATOM 278 CA GLU A 38 4.386 -6.429 20.798 1.00 37.13 C ANISOU 278 CA GLU A 38 4368 5173 4567 487 -327 49 C ATOM 279 C GLU A 38 4.039 -5.557 22.001 1.00 38.70 C ANISOU 279 C GLU A 38 4624 5399 4680 539 -389 23 C ATOM 280 O GLU A 38 4.084 -4.331 21.923 1.00 40.18 O ANISOU 280 O GLU A 38 4814 5578 4873 513 -427 -30 O ATOM 281 CB GLU A 38 5.764 -6.053 20.268 1.00 43.35 C ANISOU 281 CB GLU A 38 5083 5942 5446 446 -372 2 C ATOM 282 CG GLU A 38 6.909 -6.649 21.031 1.00 52.12 C ANISOU 282 CG GLU A 38 6163 7066 6574 493 -440 -4 C ATOM 283 CD GLU A 38 8.243 -6.252 20.454 1.00 59.45 C ANISOU 283 CD GLU A 38 7010 7970 7607 449 -478 -47 C ATOM 284 OE1 GLU A 38 8.525 -5.032 20.424 1.00 61.61 O ANISOU 284 OE1 GLU A 38 7269 8231 7908 421 -525 -98 O ATOM 285 OE2 GLU A 38 9.004 -7.160 20.051 1.00 61.84 O ANISOU 285 OE2 GLU A 38 7261 8265 7971 445 -461 -30 O ATOM 286 N LEU A 39 3.702 -6.199 23.114 1.00 38.92 N ANISOU 286 N LEU A 39 4700 5460 4627 619 -397 60 N ATOM 287 CA LEU A 39 3.220 -5.492 24.291 1.00 34.21 C ANISOU 287 CA LEU A 39 4171 4897 3930 684 -444 42 C ATOM 288 C LEU A 39 4.059 -5.817 25.517 1.00 37.86 C ANISOU 288 C LEU A 39 4648 5392 4343 768 -529 33 C ATOM 289 O LEU A 39 4.059 -6.952 25.998 1.00 40.81 O ANISOU 289 O LEU A 39 5033 5783 4688 820 -506 93 O ATOM 290 CB LEU A 39 1.753 -5.841 24.544 1.00 33.24 C ANISOU 290 CB LEU A 39 4108 4788 3735 714 -362 105 C ATOM 291 CG LEU A 39 0.861 -5.840 23.292 1.00 42.88 C ANISOU 291 CG LEU A 39 5311 5972 5009 637 -274 126 C ATOM 292 CD1 LEU A 39 -0.572 -6.274 23.609 1.00 41.25 C ANISOU 292 CD1 LEU A 39 5154 5775 4746 671 -196 192 C ATOM 293 CD2 LEU A 39 0.873 -4.471 22.608 1.00 40.96 C ANISOU 293 CD2 LEU A 39 5056 5709 4799 574 -297 61 C ATOM 294 N ASP A 40 4.766 -4.809 26.021 1.00 39.18 N ANISOU 294 N ASP A 40 4815 5566 4506 782 -630 -44 N ATOM 295 CA ASP A 40 5.624 -4.978 27.189 1.00 41.18 C ANISOU 295 CA ASP A 40 5082 5850 4713 866 -730 -68 C ATOM 296 C ASP A 40 4.837 -4.754 28.465 1.00 34.55 C ANISOU 296 C ASP A 40 4338 5060 3730 965 -749 -59 C ATOM 297 O ASP A 40 4.621 -3.620 28.877 1.00 40.27 O ANISOU 297 O ASP A 40 5098 5792 4412 982 -803 -122 O ATOM 298 CB ASP A 40 6.795 -3.997 27.142 1.00 49.65 C ANISOU 298 CB ASP A 40 6103 6900 5860 838 -841 -162 C ATOM 299 CG ASP A 40 7.833 -4.267 28.218 1.00 53.29 C ANISOU 299 CG ASP A 40 6565 7387 6296 918 -955 -193 C ATOM 300 OD1 ASP A 40 9.025 -4.389 27.866 1.00 57.19 O ANISOU 300 OD1 ASP A 40 6981 7855 6894 885 -1007 -223 O ATOM 301 OD2 ASP A 40 7.469 -4.366 29.408 1.00 51.13 O ANISOU 301 OD2 ASP A 40 6368 7160 5898 1018 -992 -186 O ATOM 302 N TYR A 41 4.420 -5.848 29.092 1.00 26.05 N ANISOU 302 N TYR A 41 3302 4015 2581 1036 -701 21 N ATOM 303 CA TYR A 41 3.640 -5.795 30.328 1.00 28.68 C ANISOU 303 CA TYR A 41 3729 4401 2769 1143 -701 48 C ATOM 304 C TYR A 41 4.496 -5.652 31.585 1.00 27.20 C ANISOU 304 C TYR A 41 3577 4254 2502 1246 -823 3 C ATOM 305 O TYR A 41 4.004 -5.851 32.688 1.00 32.15 O ANISOU 305 O TYR A 41 4283 4933 2999 1353 -823 37 O ATOM 306 CB TYR A 41 2.750 -7.037 30.459 1.00 32.42 C ANISOU 306 CB TYR A 41 4228 4886 3203 1177 -586 166 C ATOM 307 CG TYR A 41 3.515 -8.346 30.526 1.00 36.75 C ANISOU 307 CG TYR A 41 4740 5432 3791 1198 -585 221 C ATOM 308 CD1 TYR A 41 3.899 -8.900 31.746 1.00 38.30 C ANISOU 308 CD1 TYR A 41 4983 5675 3895 1311 -633 251 C ATOM 309 CD2 TYR A 41 3.838 -9.039 29.366 1.00 39.71 C ANISOU 309 CD2 TYR A 41 5037 5759 4291 1110 -537 242 C ATOM 310 CE1 TYR A 41 4.591 -10.097 31.801 1.00 39.46 C ANISOU 310 CE1 TYR A 41 5095 5816 4082 1331 -633 304 C ATOM 311 CE2 TYR A 41 4.528 -10.231 29.411 1.00 39.64 C ANISOU 311 CE2 TYR A 41 4994 5745 4323 1130 -536 289 C ATOM 312 CZ TYR A 41 4.900 -10.758 30.629 1.00 41.66 C ANISOU 312 CZ TYR A 41 5293 6043 4494 1238 -584 322 C ATOM 313 OH TYR A 41 5.582 -11.951 30.665 1.00 47.75 O ANISOU 313 OH TYR A 41 6028 6804 5310 1258 -584 371 O ATOM 314 N GLY A 42 5.769 -5.309 31.414 1.00 28.53 N ANISOU 314 N GLY A 42 3687 4402 2752 1217 -928 -73 N ATOM 315 CA GLY A 42 6.710 -5.249 32.521 1.00 29.20 C ANISOU 315 CA GLY A 42 3793 4519 2781 1310 -1058 -122 C ATOM 316 C GLY A 42 6.337 -4.331 33.678 1.00 34.72 C ANISOU 316 C GLY A 42 4583 5264 3346 1408 -1134 -179 C ATOM 317 O GLY A 42 6.711 -4.587 34.820 1.00 39.40 O ANISOU 317 O GLY A 42 5229 5904 3839 1522 -1211 -186 O ATOM 318 N SER A 43 5.607 -3.258 33.387 1.00 33.68 N ANISOU 318 N SER A 43 4470 5117 3208 1369 -1115 -223 N ATOM 319 CA SER A 43 5.224 -2.283 34.412 1.00 40.35 C ANISOU 319 CA SER A 43 5399 6000 3933 1459 -1188 -289 C ATOM 320 C SER A 43 3.770 -2.398 34.856 1.00 36.99 C ANISOU 320 C SER A 43 5062 5616 3377 1518 -1080 -218 C ATOM 321 O SER A 43 3.256 -1.527 35.554 1.00 36.81 O ANISOU 321 O SER A 43 5109 5622 3255 1584 -1116 -269 O ATOM 322 CB SER A 43 5.501 -0.853 33.940 1.00 49.42 C ANISOU 322 CB SER A 43 6511 7102 5166 1389 -1265 -402 C ATOM 323 OG SER A 43 6.893 -0.602 33.834 1.00 58.02 O ANISOU 323 OG SER A 43 7527 8157 6361 1361 -1389 -479 O ATOM 324 N MET A 44 3.112 -3.480 34.465 1.00 33.35 N ANISOU 324 N MET A 44 4594 5156 2920 1499 -947 -101 N ATOM 325 CA MET A 44 1.712 -3.673 34.809 1.00 34.39 C ANISOU 325 CA MET A 44 4796 5321 2952 1547 -831 -22 C ATOM 326 C MET A 44 1.536 -4.373 36.143 1.00 35.04 C ANISOU 326 C MET A 44 4961 5472 2880 1695 -827 41 C ATOM 327 O MET A 44 2.389 -5.159 36.551 1.00 34.39 O ANISOU 327 O MET A 44 4870 5406 2791 1741 -876 63 O ATOM 328 CB MET A 44 1.016 -4.499 33.733 1.00 35.65 C ANISOU 328 CB MET A 44 4903 5441 3202 1455 -690 74 C ATOM 329 CG MET A 44 1.101 -3.912 32.341 1.00 37.29 C ANISOU 329 CG MET A 44 5033 5583 3551 1315 -677 27 C ATOM 330 SD MET A 44 -0.062 -4.709 31.222 1.00 38.39 S ANISOU 330 SD MET A 44 5138 5686 3763 1230 -512 131 S ATOM 331 CE MET A 44 0.575 -4.169 29.640 1.00 97.47 C ANISOU 331 CE MET A 44 12524 13099 11410 1082 -531 65 C ATOM 332 N THR A 45 0.414 -4.101 36.804 1.00 34.73 N ANISOU 332 N THR A 45 5003 5474 2718 1772 -764 76 N ATOM 333 CA THR A 45 0.051 -4.797 38.034 1.00 37.83 C ANISOU 333 CA THR A 45 5481 5936 2957 1918 -730 158 C ATOM 334 C THR A 45 -0.646 -6.124 37.744 1.00 36.50 C ANISOU 334 C THR A 45 5292 5758 2819 1903 -579 309 C ATOM 335 O THR A 45 -1.117 -6.355 36.629 1.00 36.65 O ANISOU 335 O THR A 45 5245 5721 2961 1787 -494 344 O ATOM 336 CB THR A 45 -0.873 -3.932 38.918 1.00 41.77 C ANISOU 336 CB THR A 45 6078 6487 3306 2018 -719 135 C ATOM 337 OG1 THR A 45 -2.111 -3.703 38.231 1.00 44.08 O ANISOU 337 OG1 THR A 45 6356 6750 3642 1948 -593 180 O ATOM 338 CG2 THR A 45 -0.215 -2.613 39.229 1.00 37.81 C ANISOU 338 CG2 THR A 45 5596 5988 2780 2036 -874 -20 C ATOM 339 N GLU A 46 -0.695 -6.989 38.757 1.00 34.21 N ANISOU 339 N GLU A 46 5060 5521 2419 2025 -551 398 N ATOM 340 CA GLU A 46 -1.361 -8.279 38.642 1.00 36.16 C ANISOU 340 CA GLU A 46 5291 5758 2692 2028 -410 550 C ATOM 341 C GLU A 46 -2.815 -8.097 38.225 1.00 43.28 C ANISOU 341 C GLU A 46 6193 6640 3610 1988 -273 608 C ATOM 342 O GLU A 46 -3.419 -8.988 37.630 1.00 41.12 O ANISOU 342 O GLU A 46 5871 6325 3426 1932 -157 709 O ATOM 343 CB GLU A 46 -1.299 -9.036 39.969 1.00 36.47 C ANISOU 343 CB GLU A 46 5409 5865 2584 2187 -400 637 C ATOM 344 N ALA A 47 -3.367 -6.929 38.537 1.00 44.81 N ANISOU 344 N ALA A 47 6441 6860 3726 2017 -291 540 N ATOM 345 CA ALA A 47 -4.758 -6.625 38.233 1.00 47.75 C ANISOU 345 CA ALA A 47 6820 7219 4106 1990 -170 587 C ATOM 346 C ALA A 47 -4.937 -6.207 36.778 1.00 53.66 C ANISOU 346 C ALA A 47 7482 7891 5016 1827 -157 536 C ATOM 347 O ALA A 47 -5.870 -6.652 36.104 1.00 52.89 O ANISOU 347 O ALA A 47 7344 7753 4998 1764 -40 612 O ATOM 348 CB ALA A 47 -5.264 -5.538 39.154 1.00 47.38 C ANISOU 348 CB ALA A 47 6864 7230 3908 2093 -196 532 C ATOM 349 N GLU A 48 -4.036 -5.353 36.298 1.00 51.67 N ANISOU 349 N GLU A 48 7201 7617 4814 1763 -277 409 N ATOM 350 CA GLU A 48 -4.085 -4.894 34.917 1.00 45.73 C ANISOU 350 CA GLU A 48 6372 6796 4209 1615 -272 358 C ATOM 351 C GLU A 48 -3.905 -6.060 33.964 1.00 41.81 C ANISOU 351 C GLU A 48 5794 6249 3844 1528 -210 429 C ATOM 352 O GLU A 48 -4.559 -6.127 32.927 1.00 44.23 O ANISOU 352 O GLU A 48 6050 6504 4250 1432 -137 451 O ATOM 353 CB GLU A 48 -3.025 -3.822 34.665 1.00 43.30 C ANISOU 353 CB GLU A 48 6044 6474 3934 1572 -414 218 C ATOM 354 CG GLU A 48 -3.130 -2.649 35.623 1.00 49.51 C ANISOU 354 CG GLU A 48 6910 7305 4597 1662 -491 134 C ATOM 355 CD GLU A 48 -2.204 -1.501 35.264 1.00 55.36 C ANISOU 355 CD GLU A 48 7619 8016 5398 1606 -626 -6 C ATOM 356 OE1 GLU A 48 -0.970 -1.705 35.206 1.00 51.07 O ANISOU 356 OE1 GLU A 48 7037 7462 4907 1590 -721 -49 O ATOM 357 OE2 GLU A 48 -2.717 -0.382 35.053 1.00 60.75 O ANISOU 357 OE2 GLU A 48 8315 8683 6083 1578 -638 -70 O ATOM 358 N LYS A 49 -3.033 -6.988 34.339 1.00 34.75 N ANISOU 358 N LYS A 49 4890 5367 2946 1568 -243 464 N ATOM 359 CA LYS A 49 -2.748 -8.151 33.517 1.00 36.40 C ANISOU 359 CA LYS A 49 5025 5529 3278 1497 -195 526 C ATOM 360 C LYS A 49 -3.900 -9.160 33.492 1.00 39.08 C ANISOU 360 C LYS A 49 5362 5854 3634 1509 -53 659 C ATOM 361 O LYS A 49 -3.993 -9.973 32.578 1.00 45.08 O ANISOU 361 O LYS A 49 6054 6559 4514 1430 2 703 O ATOM 362 CB LYS A 49 -1.450 -8.816 33.982 1.00 39.84 C ANISOU 362 CB LYS A 49 5450 5981 3705 1542 -278 522 C ATOM 363 CG LYS A 49 -0.267 -7.864 34.031 1.00 39.09 C ANISOU 363 CG LYS A 49 5348 5894 3610 1531 -423 392 C ATOM 364 CD LYS A 49 1.031 -8.595 34.297 1.00 41.46 C ANISOU 364 CD LYS A 49 5619 6199 3933 1559 -502 389 C ATOM 365 CE LYS A 49 1.069 -9.132 35.705 1.00 43.17 C ANISOU 365 CE LYS A 49 5914 6480 4007 1707 -517 448 C ATOM 366 NZ LYS A 49 2.456 -9.435 36.115 1.00 40.44 N ANISOU 366 NZ LYS A 49 5553 6148 3666 1746 -635 406 N ATOM 367 N GLN A 50 -4.775 -9.107 34.492 1.00 41.96 N ANISOU 367 N GLN A 50 5797 6265 3883 1611 5 721 N ATOM 368 CA GLN A 50 -5.933 -9.997 34.543 1.00 52.08 C ANISOU 368 CA GLN A 50 7072 7530 5187 1627 145 853 C ATOM 369 C GLN A 50 -7.049 -9.438 33.675 1.00 50.08 C ANISOU 369 C GLN A 50 6789 7234 5004 1542 214 841 C ATOM 370 O GLN A 50 -7.708 -10.176 32.943 1.00 50.23 O ANISOU 370 O GLN A 50 6752 7199 5134 1480 301 909 O ATOM 371 CB GLN A 50 -6.419 -10.178 35.983 1.00 64.76 C ANISOU 371 CB GLN A 50 8764 9204 6639 1777 191 935 C ATOM 372 CG GLN A 50 -7.576 -11.151 36.136 1.00 74.53 C ANISOU 372 CG GLN A 50 9989 10422 7906 1804 342 1085 C ATOM 373 CD GLN A 50 -7.230 -12.558 35.687 1.00 80.27 C ANISOU 373 CD GLN A 50 10650 11098 8752 1764 378 1168 C ATOM 374 OE1 GLN A 50 -6.426 -13.252 36.320 1.00 81.81 O ANISOU 374 OE1 GLN A 50 10862 11318 8903 1832 343 1205 O ATOM 375 NE2 GLN A 50 -7.853 -12.996 34.598 1.00 79.72 N ANISOU 375 NE2 GLN A 50 10503 10954 8833 1658 447 1196 N ATOM 376 N MET A 51 -7.246 -8.126 33.765 1.00 47.42 N ANISOU 376 N MET A 51 6491 6920 4608 1543 168 751 N ATOM 377 CA MET A 51 -8.192 -7.417 32.914 1.00 44.17 C ANISOU 377 CA MET A 51 6054 6469 4260 1461 213 723 C ATOM 378 C MET A 51 -7.699 -7.451 31.468 1.00 43.21 C ANISOU 378 C MET A 51 5851 6283 4285 1324 180 666 C ATOM 379 O MET A 51 -8.491 -7.423 30.527 1.00 42.40 O ANISOU 379 O MET A 51 5706 6132 4273 1244 239 677 O ATOM 380 CB MET A 51 -8.364 -5.977 33.410 1.00 44.92 C ANISOU 380 CB MET A 51 6211 6604 4254 1502 157 632 C ATOM 381 CG MET A 51 -9.300 -5.122 32.577 1.00 50.54 C ANISOU 381 CG MET A 51 6901 7277 5024 1422 193 595 C ATOM 382 SD MET A 51 -9.629 -3.494 33.293 1.00120.10 S ANISOU 382 SD MET A 51 15788 16132 13711 1485 138 499 S ATOM 383 CE MET A 51 -10.479 -3.939 34.808 1.00 83.15 C ANISOU 383 CE MET A 51 11191 11524 8880 1647 228 604 C ATOM 384 N LEU A 52 -6.383 -7.532 31.302 1.00 42.98 N ANISOU 384 N LEU A 52 5801 6254 4278 1303 86 608 N ATOM 385 CA LEU A 52 -5.775 -7.650 29.984 1.00 42.64 C ANISOU 385 CA LEU A 52 5681 6155 4365 1186 58 560 C ATOM 386 C LEU A 52 -5.997 -9.041 29.390 1.00 45.19 C ANISOU 386 C LEU A 52 5948 6433 4788 1149 135 648 C ATOM 387 O LEU A 52 -6.160 -9.182 28.179 1.00 44.21 O ANISOU 387 O LEU A 52 5767 6255 4775 1053 158 633 O ATOM 388 CB LEU A 52 -4.282 -7.363 30.072 1.00 42.70 C ANISOU 388 CB LEU A 52 5678 6176 4370 1184 -61 478 C ATOM 389 CG LEU A 52 -3.455 -7.593 28.810 1.00 42.66 C ANISOU 389 CG LEU A 52 5595 6121 4495 1077 -89 437 C ATOM 390 CD1 LEU A 52 -3.815 -6.593 27.735 1.00 41.06 C ANISOU 390 CD1 LEU A 52 5366 5882 4353 982 -88 371 C ATOM 391 CD2 LEU A 52 -2.003 -7.463 29.176 1.00 46.91 C ANISOU 391 CD2 LEU A 52 6124 6678 5022 1099 -199 375 C ATOM 392 N VAL A 53 -5.992 -10.064 30.243 1.00 43.89 N ANISOU 392 N VAL A 53 5801 6289 4585 1230 171 739 N ATOM 393 CA VAL A 53 -6.340 -11.420 29.830 1.00 42.44 C ANISOU 393 CA VAL A 53 5568 6059 4498 1207 251 834 C ATOM 394 C VAL A 53 -7.809 -11.525 29.418 1.00 43.58 C ANISOU 394 C VAL A 53 5697 6166 4695 1177 355 892 C ATOM 395 O VAL A 53 -8.133 -12.109 28.386 1.00 42.32 O ANISOU 395 O VAL A 53 5476 5945 4659 1099 394 907 O ATOM 396 CB VAL A 53 -6.082 -12.434 30.963 1.00 47.58 C ANISOU 396 CB VAL A 53 6248 6741 5090 1312 272 930 C ATOM 397 CG1 VAL A 53 -6.849 -13.731 30.714 1.00 49.57 C ANISOU 397 CG1 VAL A 53 6455 6941 5437 1302 379 1047 C ATOM 398 CG2 VAL A 53 -4.597 -12.705 31.130 1.00 46.52 C ANISOU 398 CG2 VAL A 53 6105 6624 4948 1326 175 885 C ATOM 399 N SER A 54 -8.692 -10.967 30.243 1.00 45.54 N ANISOU 399 N SER A 54 6001 6452 4851 1245 399 923 N ATOM 400 CA SER A 54 -10.131 -10.971 29.976 1.00 47.44 C ANISOU 400 CA SER A 54 6227 6660 5137 1226 498 980 C ATOM 401 C SER A 54 -10.455 -10.500 28.566 1.00 45.60 C ANISOU 401 C SER A 54 5943 6372 5013 1107 488 910 C ATOM 402 O SER A 54 -11.384 -10.998 27.930 1.00 48.42 O ANISOU 402 O SER A 54 6254 6675 5469 1062 558 958 O ATOM 403 CB SER A 54 -10.862 -10.077 30.979 1.00 52.36 C ANISOU 403 CB SER A 54 6922 7339 5632 1310 525 988 C ATOM 404 OG SER A 54 -10.546 -10.457 32.310 1.00 58.17 O ANISOU 404 OG SER A 54 7716 8135 6250 1432 531 1050 O ATOM 405 N GLU A 55 -9.678 -9.535 28.087 1.00 44.24 N ANISOU 405 N GLU A 55 5776 6211 4823 1060 398 798 N ATOM 406 CA GLU A 55 -9.915 -8.915 26.785 1.00 47.78 C ANISOU 406 CA GLU A 55 6185 6614 5353 957 382 728 C ATOM 407 C GLU A 55 -9.336 -9.719 25.628 1.00 44.59 C ANISOU 407 C GLU A 55 5715 6158 5068 877 369 715 C ATOM 408 O GLU A 55 -9.938 -9.807 24.559 1.00 42.08 O ANISOU 408 O GLU A 55 5356 5791 4842 805 398 706 O ATOM 409 CB GLU A 55 -9.357 -7.488 26.758 1.00 49.02 C ANISOU 409 CB GLU A 55 6376 6803 5448 942 298 620 C ATOM 410 CG GLU A 55 -10.045 -6.550 27.728 1.00 58.43 C ANISOU 410 CG GLU A 55 7633 8038 6529 1013 307 615 C ATOM 411 CD GLU A 55 -10.241 -5.158 27.167 1.00 69.16 C ANISOU 411 CD GLU A 55 9001 9390 7887 961 266 524 C ATOM 412 OE1 GLU A 55 -10.573 -5.046 25.964 1.00 74.46 O ANISOU 412 OE1 GLU A 55 9627 10012 8653 871 280 503 O ATOM 413 OE2 GLU A 55 -10.089 -4.184 27.941 1.00 70.92 O ANISOU 413 OE2 GLU A 55 9278 9655 8014 1014 217 473 O ATOM 414 N VAL A 56 -8.152 -10.280 25.837 1.00 41.39 N ANISOU 414 N VAL A 56 5300 5767 4660 893 321 708 N ATOM 415 CA VAL A 56 -7.548 -11.148 24.843 1.00 45.20 C ANISOU 415 CA VAL A 56 5721 6202 5249 831 312 701 C ATOM 416 C VAL A 56 -8.487 -12.324 24.589 1.00 46.00 C ANISOU 416 C VAL A 56 5785 6253 5438 826 397 789 C ATOM 417 O VAL A 56 -8.561 -12.841 23.477 1.00 46.24 O ANISOU 417 O VAL A 56 5765 6231 5575 759 407 775 O ATOM 418 CB VAL A 56 -6.180 -11.685 25.316 1.00 48.70 C ANISOU 418 CB VAL A 56 6161 6670 5673 866 254 696 C ATOM 419 CG1 VAL A 56 -5.545 -12.568 24.242 1.00 42.65 C ANISOU 419 CG1 VAL A 56 5329 5855 5020 804 248 683 C ATOM 420 CG2 VAL A 56 -5.256 -10.537 25.684 1.00 51.79 C ANISOU 420 CG2 VAL A 56 6584 7107 5986 878 164 609 C ATOM 421 N ASN A 57 -9.199 -12.743 25.633 1.00 46.63 N ANISOU 421 N ASN A 57 5892 6349 5477 901 458 881 N ATOM 422 CA ASN A 57 -10.122 -13.864 25.532 1.00 45.32 C ANISOU 422 CA ASN A 57 5686 6129 5403 903 542 976 C ATOM 423 C ASN A 57 -11.382 -13.489 24.765 1.00 47.78 C ANISOU 423 C ASN A 57 5975 6398 5782 848 588 969 C ATOM 424 O ASN A 57 -11.862 -14.269 23.944 1.00 50.19 O ANISOU 424 O ASN A 57 6224 6637 6210 800 618 989 O ATOM 425 CB ASN A 57 -10.475 -14.401 26.917 1.00 45.35 C ANISOU 425 CB ASN A 57 5725 6164 5342 1006 601 1086 C ATOM 426 CG ASN A 57 -9.320 -15.152 27.568 1.00 51.80 C ANISOU 426 CG ASN A 57 6552 7007 6125 1060 564 1114 C ATOM 427 OD1 ASN A 57 -8.494 -15.774 26.893 1.00 49.63 O ANISOU 427 OD1 ASN A 57 6233 6700 5925 1015 525 1084 O ATOM 428 ND2 ASN A 57 -9.266 -15.102 28.892 1.00 56.40 N ANISOU 428 ND2 ASN A 57 7191 7647 6589 1162 578 1171 N ATOM 429 N LEU A 58 -11.911 -12.296 25.036 1.00 45.65 N ANISOU 429 N LEU A 58 5748 6163 5435 859 586 935 N ATOM 430 CA LEU A 58 -13.051 -11.770 24.286 1.00 47.17 C ANISOU 430 CA LEU A 58 5921 6319 5684 806 618 916 C ATOM 431 C LEU A 58 -12.669 -11.574 22.824 1.00 42.70 C ANISOU 431 C LEU A 58 5317 5713 5193 712 565 828 C ATOM 432 O LEU A 58 -13.435 -11.909 21.926 1.00 47.54 O ANISOU 432 O LEU A 58 5887 6269 5908 661 591 831 O ATOM 433 CB LEU A 58 -13.535 -10.448 24.884 1.00 50.43 C ANISOU 433 CB LEU A 58 6391 6780 5989 840 617 888 C ATOM 434 N LEU A 59 -11.479 -11.028 22.600 1.00 37.71 N ANISOU 434 N LEU A 59 4701 5113 4513 693 490 750 N ATOM 435 CA LEU A 59 -10.911 -10.894 21.265 1.00 38.24 C ANISOU 435 CA LEU A 59 4735 5151 4643 613 443 673 C ATOM 436 C LEU A 59 -10.849 -12.256 20.589 1.00 43.44 C ANISOU 436 C LEU A 59 5338 5754 5413 588 464 704 C ATOM 437 O LEU A 59 -11.251 -12.417 19.438 1.00 46.79 O ANISOU 437 O LEU A 59 5728 6130 5919 530 466 673 O ATOM 438 CB LEU A 59 -9.501 -10.303 21.368 1.00 40.21 C ANISOU 438 CB LEU A 59 5004 5444 4831 612 368 606 C ATOM 439 CG LEU A 59 -8.535 -10.523 20.199 1.00 43.80 C ANISOU 439 CG LEU A 59 5419 5875 5349 549 327 546 C ATOM 440 CD1 LEU A 59 -8.979 -9.716 18.986 1.00 40.54 C ANISOU 440 CD1 LEU A 59 4998 5439 4969 480 320 486 C ATOM 441 CD2 LEU A 59 -7.113 -10.156 20.593 1.00 46.54 C ANISOU 441 CD2 LEU A 59 5777 6263 5644 564 261 502 C ATOM 442 N ARG A 60 -10.348 -13.238 21.327 1.00 44.88 N ANISOU 442 N ARG A 60 5514 5942 5598 637 476 763 N ATOM 443 CA ARG A 60 -10.253 -14.597 20.828 1.00 45.00 C ANISOU 443 CA ARG A 60 5476 5901 5722 622 494 798 C ATOM 444 C ARG A 60 -11.607 -15.079 20.314 1.00 48.82 C ANISOU 444 C ARG A 60 5922 6319 6307 597 549 836 C ATOM 445 O ARG A 60 -11.676 -15.922 19.419 1.00 50.08 O ANISOU 445 O ARG A 60 6033 6420 6575 559 548 826 O ATOM 446 CB ARG A 60 -9.731 -15.534 21.924 1.00 43.90 C ANISOU 446 CB ARG A 60 5340 5777 5563 691 510 876 C ATOM 447 N GLU A 61 -12.680 -14.520 20.872 1.00 53.55 N ANISOU 447 N GLU A 61 6544 6929 6875 620 594 875 N ATOM 448 CA GLU A 61 -14.033 -15.027 20.638 1.00 63.33 C ANISOU 448 CA GLU A 61 7742 8105 8216 610 654 930 C ATOM 449 C GLU A 61 -14.749 -14.439 19.416 1.00 60.63 C ANISOU 449 C GLU A 61 7381 7727 7929 542 635 860 C ATOM 450 O GLU A 61 -15.769 -14.973 18.977 1.00 59.28 O ANISOU 450 O GLU A 61 7164 7491 7867 523 668 888 O ATOM 451 CB GLU A 61 -14.896 -14.856 21.896 1.00 73.85 C ANISOU 451 CB GLU A 61 9100 9462 9499 677 725 1021 C ATOM 452 CG GLU A 61 -16.059 -15.831 21.987 1.00 84.93 C ANISOU 452 CG GLU A 61 10447 10796 11028 685 801 1115 C ATOM 453 CD GLU A 61 -15.596 -17.276 22.017 1.00 92.72 C ANISOU 453 CD GLU A 61 11389 11736 12107 695 812 1171 C ATOM 454 OE1 GLU A 61 -14.445 -17.521 22.433 1.00 93.87 O ANISOU 454 OE1 GLU A 61 11559 11920 12187 724 780 1167 O ATOM 455 OE2 GLU A 61 -16.377 -18.166 21.617 1.00 95.96 O ANISOU 455 OE2 GLU A 61 11735 12065 12661 675 848 1216 O ATOM 456 N LEU A 62 -14.224 -13.349 18.868 1.00 56.59 N ANISOU 456 N LEU A 62 6901 7252 7347 509 581 771 N ATOM 457 CA LEU A 62 -14.755 -12.818 17.616 1.00 53.41 C ANISOU 457 CA LEU A 62 6485 6818 6991 447 556 702 C ATOM 458 C LEU A 62 -14.292 -13.625 16.410 1.00 53.94 C ANISOU 458 C LEU A 62 6512 6839 7146 404 522 656 C ATOM 459 O LEU A 62 -13.098 -13.764 16.150 1.00 59.04 O ANISOU 459 O LEU A 62 7162 7506 7764 396 484 618 O ATOM 460 CB LEU A 62 -14.342 -11.366 17.421 1.00 52.35 C ANISOU 460 CB LEU A 62 6398 6736 6756 428 513 629 C ATOM 461 CG LEU A 62 -14.712 -10.393 18.535 1.00 55.61 C ANISOU 461 CG LEU A 62 6859 7199 7071 472 534 653 C ATOM 462 CD1 LEU A 62 -13.970 -9.088 18.316 1.00 55.16 C ANISOU 462 CD1 LEU A 62 6843 7188 6928 451 477 573 C ATOM 463 CD2 LEU A 62 -16.217 -10.168 18.594 1.00 58.62 C ANISOU 463 CD2 LEU A 62 7230 7551 7493 475 584 689 C ATOM 464 N LYS A 63 -15.253 -14.159 15.675 1.00 48.67 N ANISOU 464 N LYS A 63 5802 6105 6586 378 533 658 N ATOM 465 CA LYS A 63 -14.957 -14.772 14.399 1.00 44.40 C ANISOU 465 CA LYS A 63 5229 5519 6122 339 494 599 C ATOM 466 C LYS A 63 -15.909 -14.243 13.344 1.00 33.39 C ANISOU 466 C LYS A 63 3828 4092 4767 300 474 546 C ATOM 467 O LYS A 63 -17.055 -14.679 13.228 1.00 34.32 O ANISOU 467 O LYS A 63 3909 4152 4981 298 495 575 O ATOM 468 CB LYS A 63 -15.007 -16.292 14.486 1.00 51.91 C ANISOU 468 CB LYS A 63 6127 6409 7187 354 512 647 C ATOM 469 CG LYS A 63 -13.810 -16.896 15.188 1.00 54.93 C ANISOU 469 CG LYS A 63 6515 6821 7534 387 513 679 C ATOM 470 CD LYS A 63 -13.770 -18.400 15.004 1.00 60.16 C ANISOU 470 CD LYS A 63 7122 7414 8321 394 519 710 C ATOM 471 CE LYS A 63 -12.807 -19.042 15.984 1.00 63.61 C ANISOU 471 CE LYS A 63 7564 7878 8729 438 533 768 C ATOM 472 NZ LYS A 63 -12.513 -20.458 15.641 1.00 65.67 N ANISOU 472 NZ LYS A 63 7773 8073 9107 441 528 782 N ATOM 473 N HIS A 64 -15.406 -13.289 12.576 1.00 19.80 N ANISOU 473 N HIS A 64 2141 2407 2975 272 434 471 N ATOM 474 CA HIS A 64 -16.189 -12.629 11.547 1.00 16.31 C ANISOU 474 CA HIS A 64 1704 1944 2549 239 410 417 C ATOM 475 C HIS A 64 -15.280 -12.231 10.386 1.00 12.61 C ANISOU 475 C HIS A 64 1257 1498 2037 211 363 336 C ATOM 476 O HIS A 64 -14.180 -11.720 10.609 1.00 13.93 O ANISOU 476 O HIS A 64 1452 1719 2123 212 354 321 O ATOM 477 CB HIS A 64 -16.870 -11.401 12.148 1.00 12.42 C ANISOU 477 CB HIS A 64 1244 1485 1991 243 430 434 C ATOM 478 CG HIS A 64 -17.939 -10.845 11.291 1.00 11.56 C ANISOU 478 CG HIS A 64 1132 1345 1917 217 413 398 C ATOM 479 ND1 HIS A 64 -17.673 -10.040 10.204 1.00 10.19 N ANISOU 479 ND1 HIS A 64 986 1186 1700 187 370 326 N ATOM 480 CD2 HIS A 64 -19.287 -10.983 11.328 1.00 17.02 C ANISOU 480 CD2 HIS A 64 1792 1987 2687 219 433 427 C ATOM 481 CE1 HIS A 64 -18.800 -9.707 9.618 1.00 14.70 C ANISOU 481 CE1 HIS A 64 1548 1722 2314 173 359 308 C ATOM 482 NE2 HIS A 64 -19.799 -10.269 10.282 1.00 18.31 N ANISOU 482 NE2 HIS A 64 1967 2139 2850 190 395 366 N ATOM 483 N PRO A 65 -15.725 -12.472 9.138 1.00 15.40 N ANISOU 483 N PRO A 65 1596 1811 2445 190 332 283 N ATOM 484 CA PRO A 65 -14.926 -12.114 7.959 1.00 7.74 C ANISOU 484 CA PRO A 65 649 862 1429 172 295 210 C ATOM 485 C PRO A 65 -14.557 -10.637 7.924 1.00 9.83 C ANISOU 485 C PRO A 65 961 1185 1590 156 291 189 C ATOM 486 O PRO A 65 -13.592 -10.266 7.263 1.00 13.00 O ANISOU 486 O PRO A 65 1381 1617 1940 145 275 148 O ATOM 487 CB PRO A 65 -15.876 -12.432 6.785 1.00 11.00 C ANISOU 487 CB PRO A 65 1046 1220 1912 162 262 164 C ATOM 488 CG PRO A 65 -17.241 -12.519 7.407 1.00 9.57 C ANISOU 488 CG PRO A 65 839 997 1801 165 282 211 C ATOM 489 CD PRO A 65 -16.961 -13.161 8.734 1.00 15.01 C ANISOU 489 CD PRO A 65 1506 1689 2509 188 327 287 C ATOM 490 N ASN A 66 -15.331 -9.805 8.611 1.00 8.02 N ANISOU 490 N ASN A 66 747 966 1335 157 308 219 N ATOM 491 CA ASN A 66 -15.117 -8.369 8.558 1.00 10.32 C ANISOU 491 CA ASN A 66 1080 1301 1540 141 300 197 C ATOM 492 C ASN A 66 -14.558 -7.825 9.867 1.00 17.76 C ANISOU 492 C ASN A 66 2041 2290 2418 158 318 232 C ATOM 493 O ASN A 66 -14.670 -6.632 10.143 1.00 16.74 O ANISOU 493 O ASN A 66 1942 2188 2230 152 315 224 O ATOM 494 CB ASN A 66 -16.405 -7.640 8.176 1.00 8.35 C ANISOU 494 CB ASN A 66 841 1031 1303 130 294 187 C ATOM 495 CG ASN A 66 -16.895 -8.008 6.784 1.00 7.63 C ANISOU 495 CG ASN A 66 739 899 1260 117 262 140 C ATOM 496 OD1 ASN A 66 -18.039 -8.410 6.612 1.00 14.07 O ANISOU 496 OD1 ASN A 66 1530 1667 2149 120 257 145 O ATOM 497 ND2 ASN A 66 -16.030 -7.872 5.790 1.00 8.60 N ANISOU 497 ND2 ASN A 66 880 1041 1345 107 239 93 N ATOM 498 N ILE A 67 -13.962 -8.709 10.665 1.00 11.49 N ANISOU 498 N ILE A 67 1229 1501 1636 183 333 268 N ATOM 499 CA ILE A 67 -13.246 -8.318 11.873 1.00 15.91 C ANISOU 499 CA ILE A 67 1808 2108 2130 207 340 294 C ATOM 500 C ILE A 67 -11.859 -8.944 11.851 1.00 14.49 C ANISOU 500 C ILE A 67 1615 1945 1946 212 325 285 C ATOM 501 O ILE A 67 -11.715 -10.132 11.560 1.00 16.19 O ANISOU 501 O ILE A 67 1799 2130 2223 218 330 295 O ATOM 502 CB ILE A 67 -13.995 -8.766 13.130 1.00 19.80 C ANISOU 502 CB ILE A 67 2295 2594 2633 248 378 364 C ATOM 503 CG1 ILE A 67 -15.225 -7.881 13.347 1.00 17.24 C ANISOU 503 CG1 ILE A 67 1989 2266 2296 249 395 373 C ATOM 504 CG2 ILE A 67 -13.088 -8.705 14.333 1.00 17.51 C ANISOU 504 CG2 ILE A 67 2024 2351 2277 285 378 389 C ATOM 505 CD1 ILE A 67 -16.242 -8.474 14.280 1.00 16.05 C ANISOU 505 CD1 ILE A 67 1821 2094 2183 286 445 445 C ATOM 506 N VAL A 68 -10.836 -8.142 12.134 1.00 9.56 N ANISOU 506 N VAL A 68 1011 1365 1258 209 303 262 N ATOM 507 CA VAL A 68 -9.470 -8.648 12.084 1.00 10.61 C ANISOU 507 CA VAL A 68 1126 1514 1392 211 287 250 C ATOM 508 C VAL A 68 -9.338 -9.919 12.927 1.00 15.91 C ANISOU 508 C VAL A 68 1775 2174 2094 250 303 301 C ATOM 509 O VAL A 68 -9.623 -9.921 14.119 1.00 20.29 O ANISOU 509 O VAL A 68 2344 2746 2620 286 316 346 O ATOM 510 CB VAL A 68 -8.435 -7.606 12.511 1.00 13.17 C ANISOU 510 CB VAL A 68 1467 1881 1655 208 258 225 C ATOM 511 CG1 VAL A 68 -7.053 -8.201 12.390 1.00 12.75 C ANISOU 511 CG1 VAL A 68 1388 1840 1618 210 242 214 C ATOM 512 CG2 VAL A 68 -8.559 -6.367 11.637 1.00 9.54 C ANISOU 512 CG2 VAL A 68 1025 1424 1174 169 247 182 C ATOM 513 N ARG A 69 -8.930 -11.000 12.285 0.50 7.89 N ANISOU 513 N ARG A 69 727 1132 1139 246 304 295 N ATOM 514 C ARG A 69 -7.730 -12.420 13.936 0.50 8.57 C ANISOU 514 C ARG A 69 790 1236 1229 312 306 366 C ATOM 515 O ARG A 69 -6.583 -12.138 13.620 0.50 8.50 O ANISOU 515 O ARG A 69 776 1252 1202 299 278 327 O ATOM 516 CA AARG A 69 -8.878 -12.298 12.940 0.00 9.79 C ANISOU 516 CA AARG A 69 942 1352 1426 280 320 346 C ATOM 517 CB AARG A 69 -8.828 -13.424 11.899 0.00 11.14 C ANISOU 517 CB AARG A 69 1077 1476 1682 268 320 325 C ATOM 518 CG AARG A 69 -10.046 -14.334 11.913 0.00 14.03 C ANISOU 518 CG AARG A 69 1418 1782 2130 277 344 363 C ATOM 519 CD AARG A 69 -9.730 -15.625 12.653 0.00 15.01 C ANISOU 519 CD AARG A 69 1512 1884 2309 312 360 420 C ATOM 520 NE AARG A 69 -9.295 -16.696 11.760 0.00 17.73 N ANISOU 520 NE AARG A 69 1820 2186 2730 306 345 388 N ATOM 521 CZ AARG A 69 -8.510 -17.701 12.136 0.00 21.72 C ANISOU 521 CZ AARG A 69 2301 2682 3271 330 345 413 C ATOM 522 NH1AARG A 69 -8.054 -17.758 13.380 0.00 23.27 N ANISOU 522 NH1AARG A 69 2505 2910 3426 364 357 472 N ATOM 523 NH2AARG A 69 -8.166 -18.643 11.273 0.00 23.18 N ANISOU 523 NH2AARG A 69 2453 2826 3528 326 330 378 N ATOM 524 CA BARG A 69 -8.882 -12.301 12.934 0.50 8.28 C ANISOU 524 CA BARG A 69 751 1161 1236 280 320 345 C ATOM 525 CB BARG A 69 -8.767 -13.411 11.884 0.50 8.33 C ANISOU 525 CB BARG A 69 720 1121 1324 268 319 323 C ATOM 526 CG BARG A 69 -8.846 -14.810 12.451 0.50 12.04 C ANISOU 526 CG BARG A 69 1157 1555 1862 299 336 377 C ATOM 527 CD BARG A 69 -10.053 -15.575 11.937 0.50 15.66 C ANISOU 527 CD BARG A 69 1589 1946 2414 293 352 389 C ATOM 528 NE BARG A 69 -11.314 -14.962 12.336 0.50 17.91 N ANISOU 528 NE BARG A 69 1889 2225 2692 291 374 419 N ATOM 529 CZ BARG A 69 -12.162 -14.384 11.491 0.50 14.61 C ANISOU 529 CZ BARG A 69 1478 1788 2285 263 365 380 C ATOM 530 NH1BARG A 69 -11.895 -14.332 10.191 0.50 11.21 N ANISOU 530 NH1BARG A 69 1046 1347 1865 236 334 309 N ATOM 531 NH2BARG A 69 -13.285 -13.857 11.944 0.50 15.41 N ANISOU 531 NH2BARG A 69 1589 1884 2384 265 388 412 N ATOM 532 N TYR A 70 -8.061 -12.843 15.146 1.00 19.32 N ANISOU 532 N TYR A 70 2159 2604 2579 356 326 430 N ATOM 533 CA TYR A 70 -7.068 -13.155 16.158 1.00 23.49 C ANISOU 533 CA TYR A 70 2690 3165 3070 398 310 456 C ATOM 534 C TYR A 70 -6.547 -14.556 15.857 1.00 25.25 C ANISOU 534 C TYR A 70 2870 3353 3370 405 315 474 C ATOM 535 O TYR A 70 -7.311 -15.414 15.422 1.00 26.75 O ANISOU 535 O TYR A 70 3034 3491 3637 399 343 497 O ATOM 536 CB TYR A 70 -7.691 -13.113 17.551 1.00 29.75 C ANISOU 536 CB TYR A 70 3512 3978 3814 452 335 524 C ATOM 537 CG TYR A 70 -6.877 -13.855 18.580 1.00 35.77 C ANISOU 537 CG TYR A 70 4273 4762 4555 507 327 570 C ATOM 538 CD1 TYR A 70 -7.215 -15.149 18.966 1.00 33.75 C ANISOU 538 CD1 TYR A 70 3994 4472 4358 539 365 644 C ATOM 539 CD2 TYR A 70 -5.765 -13.265 19.160 1.00 38.41 C ANISOU 539 CD2 TYR A 70 4628 5147 4819 528 277 541 C ATOM 540 CE1 TYR A 70 -6.463 -15.832 19.901 1.00 36.89 C ANISOU 540 CE1 TYR A 70 4392 4888 4734 594 357 690 C ATOM 541 CE2 TYR A 70 -5.009 -13.937 20.092 1.00 37.11 C ANISOU 541 CE2 TYR A 70 4464 5002 4633 582 263 580 C ATOM 542 CZ TYR A 70 -5.363 -15.216 20.461 1.00 36.60 C ANISOU 542 CZ TYR A 70 4381 4907 4618 616 304 657 C ATOM 543 OH TYR A 70 -4.616 -15.892 21.387 1.00 40.13 O ANISOU 543 OH TYR A 70 4831 5375 5042 674 290 701 O ATOM 544 N TYR A 71 -5.252 -14.791 16.064 1.00 25.25 N ANISOU 544 N TYR A 71 2859 3376 3358 419 284 460 N ATOM 545 CA TYR A 71 -4.674 -16.113 15.781 1.00 22.70 C ANISOU 545 CA TYR A 71 2495 3021 3109 429 286 473 C ATOM 546 C TYR A 71 -4.025 -16.826 16.969 1.00 28.54 C ANISOU 546 C TYR A 71 3232 3776 3835 485 280 531 C ATOM 547 O TYR A 71 -4.116 -18.044 17.090 1.00 30.45 O ANISOU 547 O TYR A 71 3446 3980 4145 507 300 576 O ATOM 548 CB TYR A 71 -3.654 -16.042 14.635 1.00 22.37 C ANISOU 548 CB TYR A 71 2428 2979 3091 393 261 402 C ATOM 549 CG TYR A 71 -4.252 -16.183 13.248 1.00 20.67 C ANISOU 549 CG TYR A 71 2199 2724 2929 353 275 359 C ATOM 550 CD1 TYR A 71 -4.770 -15.078 12.582 1.00 18.73 C ANISOU 550 CD1 TYR A 71 1979 2490 2648 318 274 319 C ATOM 551 CD2 TYR A 71 -4.296 -17.415 12.603 1.00 23.09 C ANISOU 551 CD2 TYR A 71 2472 2981 3322 356 284 357 C ATOM 552 CE1 TYR A 71 -5.318 -15.196 11.320 1.00 21.17 C ANISOU 552 CE1 TYR A 71 2281 2766 2997 289 281 278 C ATOM 553 CE2 TYR A 71 -4.845 -17.537 11.338 1.00 26.95 C ANISOU 553 CE2 TYR A 71 2953 3435 3853 328 287 309 C ATOM 554 CZ TYR A 71 -5.352 -16.426 10.705 1.00 26.34 C ANISOU 554 CZ TYR A 71 2904 3374 3731 296 285 271 C ATOM 555 OH TYR A 71 -5.895 -16.545 9.449 1.00 33.09 O ANISOU 555 OH TYR A 71 3755 4197 4619 276 283 223 O ATOM 556 N ASP A 72 -3.344 -16.085 17.831 1.00 29.52 N ANISOU 556 N ASP A 72 3383 3955 3877 511 247 526 N ATOM 557 CA ASP A 72 -2.491 -16.740 18.809 1.00 31.95 C ANISOU 557 CA ASP A 72 3687 4282 4170 565 227 566 C ATOM 558 C ASP A 72 -1.984 -15.755 19.849 1.00 33.39 C ANISOU 558 C ASP A 72 3911 4526 4251 600 184 556 C ATOM 559 O ASP A 72 -1.920 -14.552 19.603 1.00 36.53 O ANISOU 559 O ASP A 72 4326 4948 4606 570 159 500 O ATOM 560 CB ASP A 72 -1.314 -17.410 18.084 1.00 31.28 C ANISOU 560 CB ASP A 72 3555 4180 4148 547 202 529 C ATOM 561 CG ASP A 72 -0.585 -18.442 18.941 1.00 36.95 C ANISOU 561 CG ASP A 72 4259 4900 4882 603 189 581 C ATOM 562 OD1 ASP A 72 -1.068 -18.779 20.042 1.00 36.33 O ANISOU 562 OD1 ASP A 72 4206 4830 4769 657 207 654 O ATOM 563 OD2 ASP A 72 0.486 -18.913 18.497 1.00 37.54 O ANISOU 563 OD2 ASP A 72 4296 4968 5001 596 164 550 O ATOM 564 N ARG A 73 -1.658 -16.285 21.023 1.00 34.61 N ANISOU 564 N ARG A 73 4080 4702 4369 667 174 612 N ATOM 565 CA ARG A 73 -0.981 -15.541 22.074 1.00 37.50 C ANISOU 565 CA ARG A 73 4483 5126 4641 714 118 598 C ATOM 566 C ARG A 73 0.401 -16.130 22.236 1.00 40.41 C ANISOU 566 C ARG A 73 4819 5501 5033 734 68 586 C ATOM 567 O ARG A 73 0.598 -17.328 22.040 1.00 45.78 O ANISOU 567 O ARG A 73 5465 6148 5782 742 90 625 O ATOM 568 CB ARG A 73 -1.687 -15.738 23.410 1.00 43.50 C ANISOU 568 CB ARG A 73 5292 5912 5325 793 144 678 C ATOM 569 CG ARG A 73 -3.017 -15.050 23.584 1.00 48.90 C ANISOU 569 CG ARG A 73 6015 6601 5964 792 191 696 C ATOM 570 CD ARG A 73 -3.696 -15.543 24.858 1.00 53.61 C ANISOU 570 CD ARG A 73 6652 7217 6502 878 235 794 C ATOM 571 NE ARG A 73 -4.030 -16.963 24.816 1.00 52.26 N ANISOU 571 NE ARG A 73 6445 6998 6413 892 292 879 N ATOM 572 CZ ARG A 73 -5.194 -17.463 25.221 1.00 51.78 C ANISOU 572 CZ ARG A 73 6392 6916 6367 921 370 968 C ATOM 573 NH1 ARG A 73 -6.144 -16.660 25.694 1.00 49.20 N ANISOU 573 NH1 ARG A 73 6107 6615 5971 942 403 984 N ATOM 574 NH2 ARG A 73 -5.406 -18.770 25.155 1.00 51.42 N ANISOU 574 NH2 ARG A 73 6306 6819 6413 930 416 1044 N ATOM 575 N ILE A 74 1.348 -15.288 22.622 1.00 39.82 N ANISOU 575 N ILE A 74 4753 5466 4910 744 -3 532 N ATOM 576 CA ILE A 74 2.683 -15.736 22.974 1.00 41.37 C ANISOU 576 CA ILE A 74 4921 5675 5122 774 -61 520 C ATOM 577 C ILE A 74 3.229 -14.863 24.093 1.00 44.11 C ANISOU 577 C ILE A 74 5308 6076 5377 827 -137 493 C ATOM 578 O ILE A 74 3.143 -13.639 24.031 1.00 40.98 O ANISOU 578 O ILE A 74 4930 5697 4943 803 -167 435 O ATOM 579 CB ILE A 74 3.663 -15.622 21.792 1.00 41.92 C ANISOU 579 CB ILE A 74 4929 5723 5277 708 -82 452 C ATOM 580 CG1 ILE A 74 3.262 -16.545 20.639 1.00 37.79 C ANISOU 580 CG1 ILE A 74 4366 5147 4844 663 -17 467 C ATOM 581 CG2 ILE A 74 5.074 -15.936 22.255 1.00 43.38 C ANISOU 581 CG2 ILE A 74 5081 5922 5477 741 -150 436 C ATOM 582 CD1 ILE A 74 4.190 -16.422 19.443 1.00 40.36 C ANISOU 582 CD1 ILE A 74 4636 5457 5243 606 -28 402 C ATOM 583 N ILE A 75 3.797 -15.495 25.114 1.00 50.45 N ANISOU 583 N ILE A 75 6123 6902 6145 903 -174 532 N ATOM 584 CA ILE A 75 4.491 -14.765 26.168 1.00 50.94 C ANISOU 584 CA ILE A 75 6218 7013 6123 961 -264 496 C ATOM 585 C ILE A 75 5.988 -15.046 26.144 1.00 53.79 C ANISOU 585 C ILE A 75 6527 7373 6537 965 -340 456 C ATOM 586 O ILE A 75 6.413 -16.201 26.091 1.00 48.84 O ANISOU 586 O ILE A 75 5867 6726 5962 983 -326 501 O ATOM 587 CB ILE A 75 3.943 -15.096 27.563 1.00 51.24 C ANISOU 587 CB ILE A 75 6327 7092 6052 1065 -258 569 C ATOM 588 CG1 ILE A 75 4.819 -14.454 28.639 1.00 58.73 C ANISOU 588 CG1 ILE A 75 7309 8091 6915 1136 -366 522 C ATOM 589 CG2 ILE A 75 3.899 -16.594 27.777 1.00 54.49 C ANISOU 589 CG2 ILE A 75 6724 7482 6499 1105 -209 663 C ATOM 590 CD1 ILE A 75 4.451 -14.864 30.050 1.00 65.49 C ANISOU 590 CD1 ILE A 75 8238 8993 7652 1254 -367 596 C ATOM 591 N ASP A 76 6.775 -13.974 26.169 1.00 57.50 N ANISOU 591 N ASP A 76 6984 7859 7004 948 -421 373 N ATOM 592 CA ASP A 76 8.216 -14.063 26.341 1.00 62.67 C ANISOU 592 CA ASP A 76 7591 8517 7705 962 -509 330 C ATOM 593 C ASP A 76 8.565 -13.378 27.649 1.00 63.90 C ANISOU 593 C ASP A 76 7796 8720 7762 1041 -609 299 C ATOM 594 O ASP A 76 8.816 -12.174 27.680 1.00 61.73 O ANISOU 594 O ASP A 76 7523 8453 7478 1021 -670 222 O ATOM 595 CB ASP A 76 8.940 -13.364 25.190 1.00 70.21 C ANISOU 595 CB ASP A 76 8474 9442 8760 871 -524 254 C ATOM 596 CG ASP A 76 10.376 -13.004 25.533 1.00 76.33 C ANISOU 596 CG ASP A 76 9201 10224 9576 885 -632 193 C ATOM 597 OD1 ASP A 76 11.144 -13.921 25.898 1.00 77.19 O ANISOU 597 OD1 ASP A 76 9284 10334 9711 929 -662 217 O ATOM 598 OD2 ASP A 76 10.733 -11.807 25.432 1.00 76.94 O ANISOU 598 OD2 ASP A 76 9265 10301 9668 853 -687 121 O ATOM 599 N ARG A 77 8.571 -14.142 28.732 1.00 66.72 N ANISOU 599 N ARG A 77 8197 9108 8047 1137 -627 358 N ATOM 600 CA ARG A 77 8.809 -13.573 30.055 1.00 70.02 C ANISOU 600 CA ARG A 77 8676 9576 8351 1231 -721 332 C ATOM 601 C ARG A 77 10.193 -12.942 30.239 1.00 63.77 C ANISOU 601 C ARG A 77 7840 8788 7601 1232 -852 239 C ATOM 602 O ARG A 77 10.381 -12.115 31.129 1.00 56.92 O ANISOU 602 O ARG A 77 7018 7955 6653 1291 -945 186 O ATOM 603 CB ARG A 77 8.549 -14.623 31.136 1.00 75.78 C ANISOU 603 CB ARG A 77 9462 10339 8994 1339 -705 427 C ATOM 604 CG ARG A 77 9.121 -14.279 32.488 1.00 85.13 C ANISOU 604 CG ARG A 77 10701 11577 10067 1450 -819 399 C ATOM 605 CD ARG A 77 8.157 -14.681 33.574 1.00 93.53 C ANISOU 605 CD ARG A 77 11860 12686 10989 1556 -771 490 C ATOM 606 NE ARG A 77 7.265 -15.749 33.140 1.00 97.80 N ANISOU 606 NE ARG A 77 12393 13198 11567 1534 -636 600 N ATOM 607 CZ ARG A 77 6.226 -16.169 33.847 1.00100.36 C ANISOU 607 CZ ARG A 77 12786 13547 11798 1606 -558 697 C ATOM 608 NH1 ARG A 77 5.959 -15.608 35.018 1.00102.48 N ANISOU 608 NH1 ARG A 77 13143 13879 11917 1709 -598 696 N ATOM 609 NH2 ARG A 77 5.457 -17.142 33.385 1.00 99.36 N ANISOU 609 NH2 ARG A 77 12639 13383 11730 1578 -440 793 N ATOM 610 N THR A 78 11.148 -13.318 29.395 1.00 66.31 N ANISOU 610 N THR A 78 8072 9071 8052 1171 -861 217 N ATOM 611 CA THR A 78 12.510 -12.818 29.517 1.00 66.56 C ANISOU 611 CA THR A 78 8046 9097 8146 1169 -980 135 C ATOM 612 C THR A 78 12.575 -11.320 29.258 1.00 65.26 C ANISOU 612 C THR A 78 7871 8924 8000 1117 -1031 43 C ATOM 613 O THR A 78 13.303 -10.591 29.935 1.00 63.39 O ANISOU 613 O THR A 78 7632 8700 7754 1154 -1153 -29 O ATOM 614 CB THR A 78 13.449 -13.552 28.561 1.00 65.87 C ANISOU 614 CB THR A 78 7858 8967 8202 1109 -959 137 C ATOM 615 OG1 THR A 78 13.213 -14.963 28.658 1.00 63.68 O ANISOU 615 OG1 THR A 78 7590 8687 7917 1147 -895 227 O ATOM 616 CG2 THR A 78 14.900 -13.249 28.912 1.00 70.13 C ANISOU 616 CG2 THR A 78 8337 9504 8806 1128 -1087 68 C ATOM 617 N ASN A 79 11.806 -10.867 28.275 1.00 66.00 N ANISOU 617 N ASN A 79 7958 8993 8125 1033 -942 44 N ATOM 618 CA ASN A 79 11.701 -9.444 27.983 1.00 64.32 C ANISOU 618 CA ASN A 79 7741 8769 7929 982 -975 -32 C ATOM 619 C ASN A 79 10.357 -8.893 28.453 1.00 60.60 C ANISOU 619 C ASN A 79 7363 8325 7335 1011 -937 -17 C ATOM 620 O ASN A 79 10.034 -7.737 28.197 1.00 62.71 O ANISOU 620 O ASN A 79 7639 8583 7606 970 -950 -71 O ATOM 621 CB ASN A 79 11.907 -9.177 26.488 1.00 62.88 C ANISOU 621 CB ASN A 79 7478 8537 7876 867 -909 -48 C ATOM 622 N THR A 80 9.599 -9.731 29.161 1.00 56.05 N ANISOU 622 N THR A 80 6857 7784 6657 1086 -890 60 N ATOM 623 CA THR A 80 8.253 -9.400 29.635 1.00 49.93 C ANISOU 623 CA THR A 80 6170 7037 5766 1122 -836 93 C ATOM 624 C THR A 80 7.388 -8.895 28.493 1.00 45.23 C ANISOU 624 C THR A 80 5559 6408 5220 1025 -745 92 C ATOM 625 O THR A 80 6.679 -7.895 28.628 1.00 47.62 O ANISOU 625 O THR A 80 5904 6719 5470 1021 -745 59 O ATOM 626 CB THR A 80 8.265 -8.344 30.751 1.00 51.62 C ANISOU 626 CB THR A 80 6447 7289 5875 1196 -939 27 C ATOM 627 OG1 THR A 80 8.596 -7.063 30.202 1.00 56.65 O ANISOU 627 OG1 THR A 80 7047 7897 6582 1125 -992 -67 O ATOM 628 CG2 THR A 80 9.276 -8.714 31.822 1.00 45.54 C ANISOU 628 CG2 THR A 80 5687 6551 5064 1292 -1052 9 C ATOM 629 N THR A 81 7.460 -9.586 27.362 1.00 41.00 N ANISOU 629 N THR A 81 4961 5833 4783 952 -669 124 N ATOM 630 CA THR A 81 6.721 -9.178 26.180 1.00 34.26 C ANISOU 630 CA THR A 81 4090 4947 3981 862 -587 122 C ATOM 631 C THR A 81 5.610 -10.159 25.847 1.00 31.74 C ANISOU 631 C THR A 81 3792 4619 3648 859 -473 209 C ATOM 632 O THR A 81 5.820 -11.369 25.772 1.00 33.85 O ANISOU 632 O THR A 81 4036 4876 3948 875 -440 264 O ATOM 633 CB THR A 81 7.637 -9.004 24.959 1.00 28.87 C ANISOU 633 CB THR A 81 3318 4223 3430 772 -589 79 C ATOM 634 OG1 THR A 81 8.505 -7.880 25.170 1.00 32.84 O ANISOU 634 OG1 THR A 81 3794 4722 3960 762 -687 -2 O ATOM 635 CG2 THR A 81 6.801 -8.762 23.708 1.00 23.61 C ANISOU 635 CG2 THR A 81 2640 3526 2804 690 -495 89 C ATOM 636 N LEU A 82 4.415 -9.614 25.672 1.00 23.42 N ANISOU 636 N LEU A 82 2780 3565 2553 841 -417 219 N ATOM 637 CA LEU A 82 3.288 -10.370 25.161 1.00 25.41 C ANISOU 637 CA LEU A 82 3041 3797 2815 822 -310 289 C ATOM 638 C LEU A 82 3.115 -10.064 23.677 1.00 26.47 C ANISOU 638 C LEU A 82 3129 3890 3040 721 -264 260 C ATOM 639 O LEU A 82 3.021 -8.900 23.289 1.00 26.67 O ANISOU 639 O LEU A 82 3156 3911 3067 678 -283 204 O ATOM 640 CB LEU A 82 2.026 -9.994 25.925 1.00 22.32 C ANISOU 640 CB LEU A 82 2724 3432 2323 871 -275 324 C ATOM 641 CG LEU A 82 0.679 -10.432 25.354 1.00 30.26 C ANISOU 641 CG LEU A 82 3737 4411 3347 841 -169 384 C ATOM 642 CD1 LEU A 82 0.470 -11.934 25.470 1.00 24.21 C ANISOU 642 CD1 LEU A 82 2957 3629 2611 871 -110 473 C ATOM 643 CD2 LEU A 82 -0.421 -9.682 26.080 1.00 32.62 C ANISOU 643 CD2 LEU A 82 4105 4739 3550 884 -148 396 C ATOM 644 N TYR A 83 3.098 -11.108 22.853 1.00 25.70 N ANISOU 644 N TYR A 83 2989 3759 3015 689 -206 296 N ATOM 645 CA TYR A 83 2.827 -10.961 21.428 1.00 26.56 C ANISOU 645 CA TYR A 83 3063 3832 3198 606 -155 275 C ATOM 646 C TYR A 83 1.406 -11.416 21.106 1.00 19.75 C ANISOU 646 C TYR A 83 2226 2949 2330 598 -73 327 C ATOM 647 O TYR A 83 0.956 -12.481 21.529 1.00 21.14 O ANISOU 647 O TYR A 83 2410 3119 2504 638 -36 392 O ATOM 648 CB TYR A 83 3.816 -11.768 20.586 1.00 30.11 C ANISOU 648 CB TYR A 83 3445 4255 3739 575 -151 267 C ATOM 649 CG TYR A 83 5.274 -11.472 20.847 1.00 31.37 C ANISOU 649 CG TYR A 83 3565 4428 3927 582 -227 222 C ATOM 650 CD1 TYR A 83 6.031 -12.294 21.677 1.00 35.35 C ANISOU 650 CD1 TYR A 83 4058 4945 4428 641 -269 245 C ATOM 651 CD2 TYR A 83 5.906 -10.388 20.246 1.00 33.09 C ANISOU 651 CD2 TYR A 83 3750 4640 4183 530 -259 158 C ATOM 652 CE1 TYR A 83 7.373 -12.036 21.910 1.00 38.42 C ANISOU 652 CE1 TYR A 83 4405 5342 4852 648 -345 201 C ATOM 653 CE2 TYR A 83 7.245 -10.125 20.475 1.00 37.58 C ANISOU 653 CE2 TYR A 83 4272 5213 4794 534 -330 118 C ATOM 654 CZ TYR A 83 7.973 -10.950 21.306 1.00 43.17 C ANISOU 654 CZ TYR A 83 4969 5935 5500 593 -375 137 C ATOM 655 OH TYR A 83 9.305 -10.678 21.529 1.00 54.07 O ANISOU 655 OH TYR A 83 6297 7316 6931 597 -452 94 O ATOM 656 N ILE A 84 0.688 -10.599 20.360 1.00 13.93 N ANISOU 656 N ILE A 84 1497 2199 1596 546 -46 299 N ATOM 657 CA ILE A 84 -0.639 -10.996 19.930 1.00 14.69 C ANISOU 657 CA ILE A 84 1609 2271 1702 532 26 341 C ATOM 658 C ILE A 84 -0.645 -11.171 18.423 1.00 16.68 C ANISOU 658 C ILE A 84 1821 2485 2033 464 59 314 C ATOM 659 O ILE A 84 -0.468 -10.209 17.683 1.00 14.71 O ANISOU 659 O ILE A 84 1564 2233 1791 416 47 263 O ATOM 660 CB ILE A 84 -1.698 -9.985 20.366 1.00 18.09 C ANISOU 660 CB ILE A 84 2091 2717 2065 541 36 339 C ATOM 661 CG1 ILE A 84 -1.725 -9.895 21.892 1.00 29.49 C ANISOU 661 CG1 ILE A 84 3582 4203 3420 622 8 368 C ATOM 662 CG2 ILE A 84 -3.056 -10.407 19.860 1.00 11.25 C ANISOU 662 CG2 ILE A 84 1231 1820 1225 523 108 380 C ATOM 663 CD1 ILE A 84 -2.616 -8.815 22.402 1.00 39.32 C ANISOU 663 CD1 ILE A 84 4879 5468 4591 639 10 356 C ATOM 664 N VAL A 85 -0.824 -12.418 17.987 1.00 21.72 N ANISOU 664 N VAL A 85 2432 3092 2729 465 98 349 N ATOM 665 CA VAL A 85 -0.744 -12.764 16.577 1.00 17.47 C ANISOU 665 CA VAL A 85 1857 2519 2261 413 124 320 C ATOM 666 C VAL A 85 -2.077 -12.494 15.903 1.00 22.50 C ANISOU 666 C VAL A 85 2514 3132 2904 383 166 322 C ATOM 667 O VAL A 85 -3.133 -12.890 16.400 1.00 23.95 O ANISOU 667 O VAL A 85 2716 3302 3081 407 196 370 O ATOM 668 CB VAL A 85 -0.341 -14.234 16.368 1.00 14.92 C ANISOU 668 CB VAL A 85 1495 2167 2005 431 140 348 C ATOM 669 CG1 VAL A 85 -0.130 -14.522 14.891 1.00 10.00 C ANISOU 669 CG1 VAL A 85 838 1515 1446 385 160 306 C ATOM 670 CG2 VAL A 85 0.918 -14.558 17.160 1.00 19.08 C ANISOU 670 CG2 VAL A 85 2004 2719 2526 469 96 354 C ATOM 671 N MET A 86 -2.021 -11.807 14.771 1.00 18.55 N ANISOU 671 N MET A 86 2006 2625 2418 333 168 272 N ATOM 672 C MET A 86 -3.079 -11.543 12.560 1.00 14.34 C ANISOU 672 C MET A 86 1469 2047 1931 264 213 224 C ATOM 673 O MET A 86 -1.970 -11.625 12.030 1.00 15.05 O ANISOU 673 O MET A 86 1532 2145 2041 253 202 196 O ATOM 674 CA AMET A 86 -3.225 -11.401 14.068 0.50 15.97 C ANISOU 674 CA AMET A 86 1699 2277 2092 304 198 265 C ATOM 675 CB AMET A 86 -3.566 -9.953 14.415 0.50 18.03 C ANISOU 675 CB AMET A 86 1996 2564 2292 292 181 246 C ATOM 676 CG AMET A 86 -3.590 -9.673 15.908 0.50 19.63 C ANISOU 676 CG AMET A 86 2228 2798 2434 340 159 274 C ATOM 677 SD AMET A 86 -5.111 -10.217 16.698 0.50 25.15 S ANISOU 677 SD AMET A 86 2954 3483 3116 380 205 342 S ATOM 678 CE AMET A 86 -6.230 -8.898 16.214 0.50 17.52 C ANISOU 678 CE AMET A 86 2020 2514 2123 344 216 313 C ATOM 679 CA BMET A 86 -3.225 -11.396 14.064 0.50 15.96 C ANISOU 679 CA BMET A 86 1698 2276 2091 303 198 264 C ATOM 680 CB BMET A 86 -3.560 -9.935 14.377 0.50 17.76 C ANISOU 680 CB BMET A 86 1961 2529 2258 290 181 244 C ATOM 681 CG BMET A 86 -3.987 -9.662 15.808 0.50 20.02 C ANISOU 681 CG BMET A 86 2282 2840 2484 336 171 279 C ATOM 682 SD BMET A 86 -4.239 -7.898 16.121 0.50 39.46 S ANISOU 682 SD BMET A 86 4784 5329 4880 323 142 241 S ATOM 683 CE BMET A 86 -5.772 -7.596 15.244 0.50 83.55 C ANISOU 683 CE BMET A 86 10384 10882 10480 289 188 244 C ATOM 684 N GLU A 87 -4.224 -11.563 11.894 1.00 14.15 N ANISOU 684 N GLU A 87 1458 1996 1921 247 237 222 N ATOM 685 CA GLU A 87 -4.350 -11.564 10.449 1.00 14.53 C ANISOU 685 CA GLU A 87 1500 2025 1997 216 248 181 C ATOM 686 C GLU A 87 -3.548 -10.407 9.844 1.00 14.05 C ANISOU 686 C GLU A 87 1442 1992 1903 187 238 141 C ATOM 687 O GLU A 87 -3.518 -9.318 10.399 1.00 16.99 O ANISOU 687 O GLU A 87 1834 2388 2234 178 223 141 O ATOM 688 CB GLU A 87 -5.843 -11.418 10.137 1.00 18.16 C ANISOU 688 CB GLU A 87 1981 2456 2463 207 264 187 C ATOM 689 CG GLU A 87 -6.213 -11.175 8.707 1.00 25.11 C ANISOU 689 CG GLU A 87 2867 3320 3353 180 268 142 C ATOM 690 CD GLU A 87 -7.707 -10.961 8.525 1.00 28.03 C ANISOU 690 CD GLU A 87 3257 3663 3732 173 274 148 C ATOM 691 OE1 GLU A 87 -8.452 -10.917 9.535 1.00 14.26 O ANISOU 691 OE1 GLU A 87 1519 1913 1985 187 282 190 O ATOM 692 OE2 GLU A 87 -8.128 -10.841 7.358 1.00 37.47 O ANISOU 692 OE2 GLU A 87 4459 4841 4936 158 271 111 O ATOM 693 N TYR A 88 -2.891 -10.638 8.713 1.00 15.10 N ANISOU 693 N TYR A 88 1556 2122 2060 174 248 109 N ATOM 694 CA TYR A 88 -2.179 -9.559 8.040 1.00 14.45 C ANISOU 694 CA TYR A 88 1474 2062 1956 147 250 81 C ATOM 695 C TYR A 88 -3.089 -8.956 6.985 1.00 21.57 C ANISOU 695 C TYR A 88 2405 2953 2838 126 266 62 C ATOM 696 O TYR A 88 -3.687 -9.673 6.186 1.00 25.51 O ANISOU 696 O TYR A 88 2908 3429 3354 133 277 48 O ATOM 697 CB TYR A 88 -0.879 -10.051 7.409 1.00 12.19 C ANISOU 697 CB TYR A 88 1148 1782 1700 150 260 64 C ATOM 698 CG TYR A 88 -0.212 -9.019 6.540 1.00 17.33 C ANISOU 698 CG TYR A 88 1794 2452 2339 123 276 43 C ATOM 699 CD1 TYR A 88 0.188 -7.797 7.061 1.00 18.73 C ANISOU 699 CD1 TYR A 88 1971 2646 2501 102 258 46 C ATOM 700 CD2 TYR A 88 0.017 -9.262 5.196 1.00 17.26 C ANISOU 700 CD2 TYR A 88 1782 2441 2336 124 309 21 C ATOM 701 CE1 TYR A 88 0.797 -6.849 6.264 1.00 17.96 C ANISOU 701 CE1 TYR A 88 1862 2556 2404 76 277 36 C ATOM 702 CE2 TYR A 88 0.625 -8.318 4.394 1.00 13.73 C ANISOU 702 CE2 TYR A 88 1329 2010 1878 103 333 13 C ATOM 703 CZ TYR A 88 1.014 -7.121 4.931 1.00 12.35 C ANISOU 703 CZ TYR A 88 1147 1846 1698 77 319 24 C ATOM 704 OH TYR A 88 1.612 -6.197 4.117 1.00 18.96 O ANISOU 704 OH TYR A 88 1973 2693 2537 56 348 24 O ATOM 705 N CYS A 89 -3.207 -7.636 7.002 1.00 18.40 N ANISOU 705 N CYS A 89 2024 2566 2402 102 261 58 N ATOM 706 CA CYS A 89 -4.075 -6.938 6.073 1.00 11.99 C ANISOU 706 CA CYS A 89 1243 1746 1566 83 272 43 C ATOM 707 C CYS A 89 -3.230 -6.118 5.113 1.00 16.32 C ANISOU 707 C CYS A 89 1786 2310 2104 63 290 28 C ATOM 708 O CYS A 89 -2.794 -5.008 5.424 1.00 18.92 O ANISOU 708 O CYS A 89 2114 2652 2424 42 282 32 O ATOM 709 CB CYS A 89 -5.065 -6.053 6.824 1.00 10.06 C ANISOU 709 CB CYS A 89 1030 1500 1294 75 257 56 C ATOM 710 SG CYS A 89 -6.286 -6.953 7.846 1.00 17.09 S ANISOU 710 SG CYS A 89 1927 2368 2197 102 252 86 S ATOM 711 N GLU A 90 -3.019 -6.700 3.941 1.00 14.79 N ANISOU 711 N GLU A 90 1589 2115 1917 73 314 10 N ATOM 712 CA GLU A 90 -2.114 -6.203 2.922 1.00 25.08 C ANISOU 712 CA GLU A 90 2882 3435 3213 65 345 2 C ATOM 713 C GLU A 90 -2.388 -4.787 2.410 1.00 27.22 C ANISOU 713 C GLU A 90 3178 3711 3451 40 355 8 C ATOM 714 O GLU A 90 -1.468 -4.114 1.949 1.00 30.36 O ANISOU 714 O GLU A 90 3559 4123 3855 27 381 17 O ATOM 715 CB GLU A 90 -2.113 -7.187 1.752 1.00 33.49 C ANISOU 715 CB GLU A 90 3951 4496 4276 94 367 -22 C ATOM 716 CG GLU A 90 -1.891 -6.550 0.401 1.00 40.85 C ANISOU 716 CG GLU A 90 4904 5445 5174 96 403 -29 C ATOM 717 CD GLU A 90 -2.055 -7.541 -0.728 1.00 39.06 C ANISOU 717 CD GLU A 90 4691 5215 4934 134 417 -62 C ATOM 718 OE1 GLU A 90 -1.894 -8.755 -0.482 1.00 31.17 O ANISOU 718 OE1 GLU A 90 3671 4203 3970 157 405 -78 O ATOM 719 OE2 GLU A 90 -2.340 -7.105 -1.862 1.00 38.55 O ANISOU 719 OE2 GLU A 90 4662 5161 4825 147 437 -73 O ATOM 720 N GLY A 91 -3.638 -4.337 2.478 1.00 21.25 N ANISOU 720 N GLY A 91 2462 2943 2671 33 338 7 N ATOM 721 CA GLY A 91 -3.993 -3.040 1.928 1.00 7.67 C ANISOU 721 CA GLY A 91 769 1224 922 12 347 14 C ATOM 722 C GLY A 91 -3.782 -1.886 2.891 1.00 13.53 C ANISOU 722 C GLY A 91 1504 1966 1673 -16 327 29 C ATOM 723 O GLY A 91 -3.971 -0.724 2.523 1.00 14.57 O ANISOU 723 O GLY A 91 1651 2094 1790 -36 333 37 O ATOM 724 N GLY A 92 -3.387 -2.202 4.123 1.00 12.47 N ANISOU 724 N GLY A 92 1344 1833 1560 -13 301 31 N ATOM 725 CA GLY A 92 -3.161 -1.183 5.133 1.00 8.60 C ANISOU 725 CA GLY A 92 848 1342 1076 -31 271 35 C ATOM 726 C GLY A 92 -4.456 -0.680 5.743 1.00 19.30 C ANISOU 726 C GLY A 92 2243 2688 2403 -30 248 35 C ATOM 727 O GLY A 92 -5.484 -1.344 5.654 1.00 23.10 O ANISOU 727 O GLY A 92 2746 3161 2869 -14 252 35 O ATOM 728 N ASP A 93 -4.394 0.494 6.372 1.00 19.86 N ANISOU 728 N ASP A 93 2317 2754 2472 -46 223 32 N ATOM 729 CA ASP A 93 -5.552 1.107 7.019 1.00 18.20 C ANISOU 729 CA ASP A 93 2144 2537 2235 -43 202 30 C ATOM 730 C ASP A 93 -6.188 2.192 6.163 1.00 15.55 C ANISOU 730 C ASP A 93 1834 2185 1888 -65 213 30 C ATOM 731 O ASP A 93 -5.585 2.666 5.201 1.00 13.92 O ANISOU 731 O ASP A 93 1617 1976 1697 -85 235 36 O ATOM 732 CB ASP A 93 -5.171 1.679 8.383 1.00 25.86 C ANISOU 732 CB ASP A 93 3109 3512 3204 -36 160 19 C ATOM 733 CG ASP A 93 -4.092 2.751 8.291 1.00 30.80 C ANISOU 733 CG ASP A 93 3708 4130 3866 -63 142 8 C ATOM 734 OD1 ASP A 93 -3.103 2.681 9.052 1.00 36.43 O ANISOU 734 OD1 ASP A 93 4389 4850 4601 -57 111 -3 O ATOM 735 OD2 ASP A 93 -4.220 3.664 7.450 1.00 34.89 O ANISOU 735 OD2 ASP A 93 4231 4632 4394 -91 158 12 O ATOM 736 N LEU A 94 -7.395 2.598 6.545 1.00 16.69 N ANISOU 736 N LEU A 94 2012 2321 2010 -59 201 28 N ATOM 737 CA LEU A 94 -8.153 3.612 5.809 1.00 22.88 C ANISOU 737 CA LEU A 94 2823 3087 2782 -76 206 29 C ATOM 738 C LEU A 94 -7.614 5.049 5.941 1.00 26.09 C ANISOU 738 C LEU A 94 3225 3481 3206 -102 190 25 C ATOM 739 O LEU A 94 -7.881 5.891 5.092 1.00 27.79 O ANISOU 739 O LEU A 94 3454 3682 3422 -120 202 33 O ATOM 740 CB LEU A 94 -9.627 3.567 6.218 1.00 17.07 C ANISOU 740 CB LEU A 94 2119 2342 2025 -60 198 28 C ATOM 741 CG LEU A 94 -10.442 2.407 5.648 1.00 15.40 C ANISOU 741 CG LEU A 94 1913 2127 1813 -42 215 33 C ATOM 742 CD1 LEU A 94 -11.921 2.579 5.988 1.00 15.64 C ANISOU 742 CD1 LEU A 94 1966 2141 1836 -30 208 35 C ATOM 743 CD2 LEU A 94 -10.250 2.309 4.150 1.00 14.08 C ANISOU 743 CD2 LEU A 94 1750 1956 1643 -51 234 31 C ATOM 744 N ALA A 95 -6.879 5.336 7.012 1.00 21.16 N ANISOU 744 N ALA A 95 2580 2860 2598 -101 158 12 N ATOM 745 CA ALA A 95 -6.275 6.662 7.175 1.00 26.14 C ANISOU 745 CA ALA A 95 3197 3472 3262 -126 134 2 C ATOM 746 C ALA A 95 -5.260 6.908 6.064 1.00 24.08 C ANISOU 746 C ALA A 95 2903 3202 3042 -155 166 22 C ATOM 747 O ALA A 95 -5.194 7.996 5.493 1.00 33.70 O ANISOU 747 O ALA A 95 4121 4397 4286 -180 174 33 O ATOM 748 CB ALA A 95 -5.610 6.791 8.530 1.00 23.69 C ANISOU 748 CB ALA A 95 2870 3167 2965 -113 85 -24 C ATOM 749 N SER A 96 -4.463 5.888 5.767 1.00 20.15 N ANISOU 749 N SER A 96 2377 2724 2554 -147 189 30 N ATOM 750 CA SER A 96 -3.476 5.976 4.694 1.00 23.21 C ANISOU 750 CA SER A 96 2732 3110 2978 -166 230 53 C ATOM 751 C SER A 96 -4.149 6.130 3.333 1.00 22.48 C ANISOU 751 C SER A 96 2672 3015 2853 -167 276 77 C ATOM 752 O SER A 96 -3.657 6.847 2.463 1.00 15.39 O ANISOU 752 O SER A 96 1762 2106 1979 -185 309 103 O ATOM 753 CB SER A 96 -2.550 4.758 4.712 1.00 20.45 C ANISOU 753 CB SER A 96 2347 2782 2641 -151 245 54 C ATOM 754 OG SER A 96 -1.696 4.825 5.842 1.00 23.16 O ANISOU 754 OG SER A 96 2652 3123 3024 -152 201 35 O ATOM 755 N VAL A 97 -5.279 5.453 3.156 1.00 21.40 N ANISOU 755 N VAL A 97 2576 2889 2665 -144 277 69 N ATOM 756 CA VAL A 97 -6.046 5.572 1.918 1.00 20.09 C ANISOU 756 CA VAL A 97 2448 2722 2463 -138 306 83 C ATOM 757 C VAL A 97 -6.553 6.996 1.759 1.00 18.45 C ANISOU 757 C VAL A 97 2261 2489 2260 -158 298 94 C ATOM 758 O VAL A 97 -6.492 7.587 0.683 1.00 27.90 O ANISOU 758 O VAL A 97 3469 3680 3450 -164 330 121 O ATOM 759 CB VAL A 97 -7.261 4.635 1.924 1.00 21.54 C ANISOU 759 CB VAL A 97 2665 2912 2607 -111 294 65 C ATOM 760 CG1 VAL A 97 -8.265 5.035 0.851 1.00 14.10 C ANISOU 760 CG1 VAL A 97 1765 1961 1630 -104 304 71 C ATOM 761 CG2 VAL A 97 -6.823 3.186 1.760 1.00 21.77 C ANISOU 761 CG2 VAL A 97 2676 2960 2634 -88 308 56 C ATOM 762 N ILE A 98 -7.077 7.527 2.850 1.00 16.38 N ANISOU 762 N ILE A 98 2006 2213 2006 -164 256 76 N ATOM 763 CA ILE A 98 -7.637 8.867 2.879 1.00 19.26 C ANISOU 763 CA ILE A 98 2389 2549 2379 -181 239 80 C ATOM 764 C ILE A 98 -6.553 9.924 2.689 1.00 24.36 C ANISOU 764 C ILE A 98 3000 3172 3083 -212 248 99 C ATOM 765 O ILE A 98 -6.779 10.943 2.039 1.00 21.06 O ANISOU 765 O ILE A 98 2595 2731 2677 -227 260 122 O ATOM 766 CB ILE A 98 -8.353 9.102 4.214 1.00 20.22 C ANISOU 766 CB ILE A 98 2524 2664 2495 -172 192 49 C ATOM 767 CG1 ILE A 98 -9.649 8.286 4.236 1.00 17.97 C ANISOU 767 CG1 ILE A 98 2272 2390 2164 -145 193 42 C ATOM 768 CG2 ILE A 98 -8.607 10.588 4.431 1.00 17.79 C ANISOU 768 CG2 ILE A 98 2225 2322 2212 -191 169 46 C ATOM 769 CD1 ILE A 98 -10.291 8.190 5.590 1.00 13.32 C ANISOU 769 CD1 ILE A 98 1692 1803 1564 -126 161 20 C ATOM 770 N THR A 99 -5.373 9.666 3.250 1.00 27.40 N ANISOU 770 N THR A 99 3338 3561 3511 -220 240 92 N ATOM 771 CA THR A 99 -4.228 10.553 3.083 1.00 30.66 C ANISOU 771 CA THR A 99 3703 3947 3999 -251 248 111 C ATOM 772 C THR A 99 -3.815 10.576 1.626 1.00 35.16 C ANISOU 772 C THR A 99 4268 4522 4570 -255 317 160 C ATOM 773 O THR A 99 -3.549 11.632 1.055 1.00 39.74 O ANISOU 773 O THR A 99 4836 5071 5191 -277 339 195 O ATOM 774 CB THR A 99 -3.033 10.077 3.915 1.00 36.16 C ANISOU 774 CB THR A 99 4346 4650 4744 -253 224 91 C ATOM 775 OG1 THR A 99 -3.231 10.429 5.288 1.00 28.03 O ANISOU 775 OG1 THR A 99 3318 3609 3722 -249 154 47 O ATOM 776 CG2 THR A 99 -1.747 10.714 3.410 1.00 42.67 C ANISOU 776 CG2 THR A 99 5110 5449 5655 -284 250 122 C ATOM 777 N LYS A 100 -3.757 9.386 1.042 1.00 39.80 N ANISOU 777 N LYS A 100 4865 5145 5111 -229 351 165 N ATOM 778 CA LYS A 100 -3.414 9.204 -0.361 1.00 37.95 C ANISOU 778 CA LYS A 100 4636 4926 4858 -218 419 206 C ATOM 779 C LYS A 100 -4.365 9.959 -1.279 1.00 41.50 C ANISOU 779 C LYS A 100 5136 5366 5265 -213 437 232 C ATOM 780 O LYS A 100 -3.944 10.555 -2.267 1.00 47.14 O ANISOU 780 O LYS A 100 5848 6074 5990 -215 489 281 O ATOM 781 CB LYS A 100 -3.441 7.715 -0.708 1.00 36.08 C ANISOU 781 CB LYS A 100 4411 4729 4569 -183 438 190 C ATOM 782 CG LYS A 100 -2.911 7.404 -2.088 1.00 41.37 C ANISOU 782 CG LYS A 100 5084 5421 5214 -162 508 226 C ATOM 783 CD LYS A 100 -2.694 5.914 -2.329 1.00 45.02 C ANISOU 783 CD LYS A 100 5547 5918 5642 -127 521 203 C ATOM 784 CE LYS A 100 -2.360 5.705 -3.809 1.00 55.99 C ANISOU 784 CE LYS A 100 6954 7332 6988 -94 591 234 C ATOM 785 NZ LYS A 100 -2.338 4.256 -4.230 1.00 62.21 N ANISOU 785 NZ LYS A 100 7754 8151 7731 -52 601 204 N ATOM 786 N GLY A 101 -5.653 9.917 -0.953 1.00 38.30 N ANISOU 786 N GLY A 101 4778 4959 4815 -201 397 204 N ATOM 787 CA GLY A 101 -6.655 10.650 -1.703 1.00 32.34 C ANISOU 787 CA GLY A 101 4072 4193 4024 -195 401 222 C ATOM 788 C GLY A 101 -6.426 12.154 -1.662 1.00 35.17 C ANISOU 788 C GLY A 101 4416 4509 4439 -227 402 253 C ATOM 789 O GLY A 101 -6.697 12.843 -2.639 1.00 30.42 O ANISOU 789 O GLY A 101 3839 3897 3821 -222 433 294 O ATOM 790 N THR A 102 -5.927 12.664 -0.538 1.00 39.71 N ANISOU 790 N THR A 102 4949 5057 5081 -255 364 233 N ATOM 791 CA THR A 102 -5.587 14.082 -0.422 1.00 50.49 C ANISOU 791 CA THR A 102 6290 6373 6521 -288 358 256 C ATOM 792 C THR A 102 -4.320 14.422 -1.209 1.00 52.72 C ANISOU 792 C THR A 102 6525 6644 6863 -305 418 313 C ATOM 793 O THR A 102 -4.328 15.303 -2.071 1.00 53.76 O ANISOU 793 O THR A 102 6663 6753 7012 -312 458 367 O ATOM 794 CB THR A 102 -5.416 14.512 1.050 1.00 49.86 C ANISOU 794 CB THR A 102 6181 6266 6496 -308 289 207 C ATOM 795 OG1 THR A 102 -6.701 14.771 1.627 1.00 48.75 O ANISOU 795 OG1 THR A 102 6088 6120 6315 -295 244 172 O ATOM 796 CG2 THR A 102 -4.602 15.778 1.138 1.00 51.15 C ANISOU 796 CG2 THR A 102 6297 6376 6764 -344 284 229 C ATOM 797 N LYS A 103 -3.235 13.720 -0.906 1.00 51.20 N ANISOU 797 N LYS A 103 6281 6467 6704 -309 429 306 N ATOM 798 CA LYS A 103 -1.978 13.929 -1.609 1.00 59.31 C ANISOU 798 CA LYS A 103 7255 7485 7796 -322 493 361 C ATOM 799 C LYS A 103 -2.215 14.027 -3.114 1.00 66.09 C ANISOU 799 C LYS A 103 8151 8361 8598 -297 571 425 C ATOM 800 O LYS A 103 -1.878 15.036 -3.733 1.00 69.47 O ANISOU 800 O LYS A 103 8562 8757 9077 -313 614 485 O ATOM 801 CB LYS A 103 -1.001 12.790 -1.315 1.00 54.11 C ANISOU 801 CB LYS A 103 6552 6858 7150 -313 503 343 C ATOM 802 N GLU A 104 -2.825 12.988 -3.685 1.00 67.51 N ANISOU 802 N GLU A 104 8384 8592 8674 -255 586 410 N ATOM 803 CA GLU A 104 -3.039 12.885 -5.131 1.00 68.79 C ANISOU 803 CA GLU A 104 8591 8782 8764 -218 655 460 C ATOM 804 C GLU A 104 -4.339 13.538 -5.583 1.00 65.16 C ANISOU 804 C GLU A 104 8199 8312 8246 -204 635 467 C ATOM 805 O GLU A 104 -4.782 13.365 -6.724 1.00 63.40 O ANISOU 805 O GLU A 104 8030 8118 7942 -163 673 494 O ATOM 806 CB GLU A 104 -2.983 11.421 -5.560 1.00 72.75 C ANISOU 806 CB GLU A 104 9114 9339 9188 -174 674 433 C ATOM 807 CG GLU A 104 -1.636 10.775 -5.248 1.00 80.58 C ANISOU 807 CG GLU A 104 10038 10341 10238 -182 702 433 C ATOM 808 CD GLU A 104 -1.761 9.315 -4.831 1.00 84.77 C ANISOU 808 CD GLU A 104 10576 10908 10724 -158 671 373 C ATOM 809 OE1 GLU A 104 -2.865 8.910 -4.421 1.00 89.29 O ANISOU 809 OE1 GLU A 104 11193 11486 11247 -148 615 326 O ATOM 810 OE2 GLU A 104 -0.761 8.568 -4.906 1.00 83.54 O ANISOU 810 OE2 GLU A 104 10379 10772 10590 -148 705 375 O ATOM 811 N ARG A 105 -4.922 14.314 -4.675 1.00 64.58 N ANISOU 811 N ARG A 105 8124 8199 8215 -235 573 440 N ATOM 812 CA ARG A 105 -6.106 15.126 -4.960 1.00 66.10 C ANISOU 812 CA ARG A 105 8370 8371 8374 -230 549 447 C ATOM 813 C ARG A 105 -7.184 14.400 -5.759 1.00 62.16 C ANISOU 813 C ARG A 105 7943 7912 7764 -181 546 432 C ATOM 814 O ARG A 105 -7.833 14.988 -6.627 1.00 60.04 O ANISOU 814 O ARG A 105 7720 7639 7453 -160 560 467 O ATOM 815 CB ARG A 105 -5.735 16.467 -5.616 1.00 70.91 C ANISOU 815 CB ARG A 105 8966 8939 9038 -247 594 523 C ATOM 816 CG ARG A 105 -4.292 16.572 -6.079 1.00 76.82 C ANISOU 816 CG ARG A 105 9655 9683 9849 -258 668 583 C ATOM 817 CD ARG A 105 -3.659 17.863 -5.606 1.00 81.08 C ANISOU 817 CD ARG A 105 10133 10154 10520 -309 664 616 C ATOM 818 NE ARG A 105 -3.781 18.015 -4.163 1.00 84.06 N ANISOU 818 NE ARG A 105 10481 10500 10956 -342 576 543 N ATOM 819 CZ ARG A 105 -4.777 18.655 -3.562 1.00 87.27 C ANISOU 819 CZ ARG A 105 10919 10878 11361 -351 512 505 C ATOM 820 NH1 ARG A 105 -5.749 19.208 -4.280 1.00 87.41 N ANISOU 820 NH1 ARG A 105 10994 10891 11328 -333 521 535 N ATOM 821 NH2 ARG A 105 -4.798 18.738 -2.240 1.00 87.71 N ANISOU 821 NH2 ARG A 105 10950 10912 11463 -373 437 438 N ATOM 822 N GLN A 106 -7.413 13.137 -5.412 1.00 57.45 N ANISOU 822 N GLN A 106 7354 7350 7126 -161 521 378 N ATOM 823 CA GLN A 106 -8.392 12.316 -6.108 1.00 52.86 C ANISOU 823 CA GLN A 106 6831 6801 6452 -115 509 353 C ATOM 824 C GLN A 106 -9.293 11.570 -5.127 1.00 43.40 C ANISOU 824 C GLN A 106 5638 5604 5247 -116 442 286 C ATOM 825 O GLN A 106 -8.832 11.005 -4.129 1.00 41.20 O ANISOU 825 O GLN A 106 5320 5327 5006 -134 425 255 O ATOM 826 CB GLN A 106 -7.694 11.324 -7.039 1.00 53.48 C ANISOU 826 CB GLN A 106 6915 6925 6482 -76 561 364 C ATOM 827 CG GLN A 106 -8.545 10.103 -7.386 1.00 59.12 C ANISOU 827 CG GLN A 106 7672 7669 7121 -31 529 311 C ATOM 828 CD GLN A 106 -7.711 8.908 -7.833 1.00 65.87 C ANISOU 828 CD GLN A 106 8515 8563 7950 0 566 300 C ATOM 829 OE1 GLN A 106 -6.481 8.987 -7.909 1.00 69.53 O ANISOU 829 OE1 GLN A 106 8937 9035 8448 -11 621 335 O ATOM 830 NE2 GLN A 106 -8.379 7.791 -8.122 1.00 64.63 N ANISOU 830 NE2 GLN A 106 8390 8427 7740 38 534 249 N ATOM 831 N TYR A 107 -10.582 11.576 -5.438 1.00 29.72 N ANISOU 831 N TYR A 107 3954 3868 3469 -93 408 267 N ATOM 832 CA TYR A 107 -11.598 10.981 -4.597 1.00 27.18 C ANISOU 832 CA TYR A 107 3637 3541 3147 -92 351 213 C ATOM 833 C TYR A 107 -11.716 9.469 -4.820 1.00 26.76 C ANISOU 833 C TYR A 107 3589 3519 3059 -60 345 176 C ATOM 834 O TYR A 107 -11.452 8.956 -5.916 1.00 27.27 O ANISOU 834 O TYR A 107 3676 3609 3075 -25 372 184 O ATOM 835 CB TYR A 107 -12.935 11.663 -4.870 1.00 26.76 C ANISOU 835 CB TYR A 107 3626 3467 3074 -81 316 210 C ATOM 836 CG TYR A 107 -13.034 13.090 -4.359 1.00 31.45 C ANISOU 836 CG TYR A 107 4212 4022 3715 -114 307 233 C ATOM 837 CD1 TYR A 107 -13.248 14.152 -5.230 1.00 30.80 C ANISOU 837 CD1 TYR A 107 4159 3923 3620 -109 322 277 C ATOM 838 CD2 TYR A 107 -12.936 13.371 -3.000 1.00 35.17 C ANISOU 838 CD2 TYR A 107 4650 4474 4241 -145 281 209 C ATOM 839 CE1 TYR A 107 -13.356 15.460 -4.766 1.00 30.27 C ANISOU 839 CE1 TYR A 107 4082 3813 3605 -139 311 295 C ATOM 840 CE2 TYR A 107 -13.044 14.670 -2.517 1.00 32.69 C ANISOU 840 CE2 TYR A 107 4329 4120 3972 -171 266 220 C ATOM 841 CZ TYR A 107 -13.252 15.714 -3.405 1.00 37.41 C ANISOU 841 CZ TYR A 107 4951 4696 4567 -170 280 263 C ATOM 842 OH TYR A 107 -13.362 17.008 -2.938 1.00 36.90 O ANISOU 842 OH TYR A 107 4878 4586 4557 -195 263 273 O ATOM 843 N LEU A 108 -12.107 8.764 -3.765 1.00 20.29 N ANISOU 843 N LEU A 108 2749 2695 2265 -68 311 137 N ATOM 844 CA LEU A 108 -12.278 7.316 -3.814 1.00 18.91 C ANISOU 844 CA LEU A 108 2572 2539 2075 -41 300 102 C ATOM 845 C LEU A 108 -13.563 6.937 -4.545 1.00 16.82 C ANISOU 845 C LEU A 108 2347 2269 1776 -8 266 77 C ATOM 846 O LEU A 108 -14.591 7.596 -4.387 1.00 16.20 O ANISOU 846 O LEU A 108 2285 2166 1702 -12 236 75 O ATOM 847 CB LEU A 108 -12.288 6.731 -2.396 1.00 20.76 C ANISOU 847 CB LEU A 108 2769 2766 2352 -59 278 79 C ATOM 848 CG LEU A 108 -10.942 6.602 -1.669 1.00 24.34 C ANISOU 848 CG LEU A 108 3178 3230 2839 -80 300 88 C ATOM 849 CD1 LEU A 108 -9.952 5.782 -2.490 1.00 27.86 C ANISOU 849 CD1 LEU A 108 3614 3703 3268 -62 337 93 C ATOM 850 CD2 LEU A 108 -10.361 7.967 -1.335 1.00 20.16 C ANISOU 850 CD2 LEU A 108 2636 2686 2339 -112 308 115 C ATOM 851 N ASP A 109 -13.494 5.871 -5.341 1.00 14.96 N ANISOU 851 N ASP A 109 2123 2051 1508 28 267 55 N ATOM 852 CA ASP A 109 -14.650 5.366 -6.085 1.00 12.73 C ANISOU 852 CA ASP A 109 1876 1762 1201 65 224 21 C ATOM 853 C ASP A 109 -15.824 5.128 -5.141 1.00 12.55 C ANISOU 853 C ASP A 109 1833 1706 1227 52 178 -4 C ATOM 854 O ASP A 109 -15.646 4.628 -4.033 1.00 14.77 O ANISOU 854 O ASP A 109 2076 1982 1553 31 181 -9 O ATOM 855 CB ASP A 109 -14.317 4.056 -6.822 1.00 20.40 C ANISOU 855 CB ASP A 109 2852 2753 2146 106 224 -13 C ATOM 856 CG ASP A 109 -13.315 4.247 -7.945 0.50 25.13 C ANISOU 856 CG ASP A 109 3477 3388 2683 134 273 11 C ATOM 857 OD1 ASP A 109 -12.985 5.408 -8.268 0.50 22.85 O ANISOU 857 OD1 ASP A 109 3205 3105 2372 124 306 58 O ATOM 858 OD2 ASP A 109 -12.853 3.230 -8.505 0.50 28.21 O ANISOU 858 OD2 ASP A 109 3871 3799 3049 170 281 -15 O ATOM 859 N GLU A 110 -17.023 5.496 -5.578 1.00 15.19 N ANISOU 859 N GLU A 110 2195 2021 1555 67 139 -16 N ATOM 860 CA GLU A 110 -18.216 5.243 -4.785 1.00 17.15 C ANISOU 860 CA GLU A 110 2422 2236 1856 59 100 -37 C ATOM 861 C GLU A 110 -18.332 3.755 -4.445 1.00 15.02 C ANISOU 861 C GLU A 110 2121 1959 1627 71 85 -70 C ATOM 862 O GLU A 110 -18.748 3.403 -3.348 1.00 15.69 O ANISOU 862 O GLU A 110 2170 2026 1767 54 81 -69 O ATOM 863 CB GLU A 110 -19.471 5.754 -5.504 1.00 16.81 C ANISOU 863 CB GLU A 110 2411 2172 1803 81 55 -49 C ATOM 864 CG GLU A 110 -20.785 5.488 -4.781 1.00 20.77 C ANISOU 864 CG GLU A 110 2886 2635 2370 76 16 -69 C ATOM 865 CD GLU A 110 -21.888 6.467 -5.189 1.00 18.28 C ANISOU 865 CD GLU A 110 2596 2297 2051 84 -18 -66 C ATOM 866 OE1 GLU A 110 -21.565 7.528 -5.767 1.00 18.24 O ANISOU 866 OE1 GLU A 110 2628 2305 1998 84 -5 -40 O ATOM 867 OE2 GLU A 110 -23.076 6.176 -4.924 1.00 13.86 O ANISOU 867 OE2 GLU A 110 2015 1704 1545 90 -56 -87 O ATOM 868 N GLU A 111 -17.954 2.887 -5.382 1.00 18.24 N ANISOU 868 N GLU A 111 2542 2382 2008 103 79 -96 N ATOM 869 CA GLU A 111 -17.981 1.438 -5.153 1.00 12.58 C ANISOU 869 CA GLU A 111 1793 1653 1335 116 63 -129 C ATOM 870 C GLU A 111 -17.178 1.036 -3.924 1.00 13.68 C ANISOU 870 C GLU A 111 1889 1799 1510 86 101 -107 C ATOM 871 O GLU A 111 -17.576 0.140 -3.182 1.00 17.84 O ANISOU 871 O GLU A 111 2379 2302 2096 84 89 -116 O ATOM 872 CB GLU A 111 -17.472 0.693 -6.385 1.00 9.57 C ANISOU 872 CB GLU A 111 1437 1291 907 159 56 -162 C ATOM 873 CG GLU A 111 -18.514 0.626 -7.477 1.00 16.44 C ANISOU 873 CG GLU A 111 2343 2145 1758 200 -3 -203 C ATOM 874 CD GLU A 111 -19.665 -0.269 -7.082 1.00 21.54 C ANISOU 874 CD GLU A 111 2953 2741 2490 202 -59 -240 C ATOM 875 OE1 GLU A 111 -19.435 -1.480 -6.945 1.00 26.53 O ANISOU 875 OE1 GLU A 111 3556 3361 3165 212 -67 -268 O ATOM 876 OE2 GLU A 111 -20.790 0.233 -6.908 1.00 24.54 O ANISOU 876 OE2 GLU A 111 3329 3091 2903 195 -93 -240 O ATOM 877 N PHE A 112 -16.053 1.713 -3.718 1.00 9.52 N ANISOU 877 N PHE A 112 1365 1302 952 67 144 -75 N ATOM 878 CA PHE A 112 -15.210 1.478 -2.553 1.00 14.17 C ANISOU 878 CA PHE A 112 1916 1899 1569 42 173 -55 C ATOM 879 C PHE A 112 -15.905 1.895 -1.259 1.00 15.55 C ANISOU 879 C PHE A 112 2072 2055 1783 20 165 -39 C ATOM 880 O PHE A 112 -15.808 1.210 -0.234 1.00 12.64 O ANISOU 880 O PHE A 112 1670 1681 1450 15 171 -34 O ATOM 881 CB PHE A 112 -13.875 2.207 -2.699 1.00 14.22 C ANISOU 881 CB PHE A 112 1925 1936 1542 27 215 -28 C ATOM 882 CG PHE A 112 -12.984 2.091 -1.494 1.00 17.48 C ANISOU 882 CG PHE A 112 2300 2358 1985 3 234 -11 C ATOM 883 CD1 PHE A 112 -12.358 0.894 -1.195 1.00 19.32 C ANISOU 883 CD1 PHE A 112 2503 2598 2238 13 242 -22 C ATOM 884 CD2 PHE A 112 -12.764 3.183 -0.668 1.00 17.40 C ANISOU 884 CD2 PHE A 112 2283 2346 1982 -26 240 12 C ATOM 885 CE1 PHE A 112 -11.530 0.783 -0.101 1.00 21.88 C ANISOU 885 CE1 PHE A 112 2795 2932 2587 -4 255 -7 C ATOM 886 CE2 PHE A 112 -11.933 3.082 0.427 1.00 24.24 C ANISOU 886 CE2 PHE A 112 3117 3220 2872 -41 248 21 C ATOM 887 CZ PHE A 112 -11.312 1.876 0.713 1.00 18.88 C ANISOU 887 CZ PHE A 112 2411 2552 2209 -30 256 13 C ATOM 888 N VAL A 113 -16.606 3.023 -1.314 1.00 13.98 N ANISOU 888 N VAL A 113 1895 1845 1572 10 154 -30 N ATOM 889 CA VAL A 113 -17.329 3.535 -0.153 1.00 12.06 C ANISOU 889 CA VAL A 113 1639 1584 1358 -4 149 -17 C ATOM 890 C VAL A 113 -18.458 2.576 0.225 1.00 5.96 C ANISOU 890 C VAL A 113 843 783 637 11 128 -30 C ATOM 891 O VAL A 113 -18.709 2.317 1.398 1.00 7.39 O ANISOU 891 O VAL A 113 1000 959 851 8 139 -15 O ATOM 892 CB VAL A 113 -17.874 4.967 -0.395 1.00 8.08 C ANISOU 892 CB VAL A 113 1164 1071 835 -14 139 -7 C ATOM 893 CG1 VAL A 113 -18.611 5.479 0.836 1.00 5.82 C ANISOU 893 CG1 VAL A 113 866 769 578 -23 136 2 C ATOM 894 CG2 VAL A 113 -16.729 5.912 -0.751 1.00 6.87 C ANISOU 894 CG2 VAL A 113 1025 937 647 -31 163 12 C ATOM 895 N LEU A 114 -19.125 2.042 -0.787 1.00 7.17 N ANISOU 895 N LEU A 114 1005 919 800 31 99 -56 N ATOM 896 CA LEU A 114 -20.185 1.075 -0.581 1.00 6.24 C ANISOU 896 CA LEU A 114 857 764 748 45 75 -70 C ATOM 897 C LEU A 114 -19.644 -0.196 0.065 1.00 7.37 C ANISOU 897 C LEU A 114 963 907 929 48 93 -66 C ATOM 898 O LEU A 114 -20.283 -0.747 0.958 1.00 9.39 O ANISOU 898 O LEU A 114 1184 1138 1244 49 99 -50 O ATOM 899 CB LEU A 114 -20.891 0.793 -1.903 1.00 10.33 C ANISOU 899 CB LEU A 114 1393 1262 1269 69 28 -108 C ATOM 900 CG LEU A 114 -21.641 2.014 -2.466 1.00 6.63 C ANISOU 900 CG LEU A 114 958 787 772 70 5 -108 C ATOM 901 CD1 LEU A 114 -22.339 1.663 -3.754 1.00 7.03 C ANISOU 901 CD1 LEU A 114 1029 819 822 102 -50 -150 C ATOM 902 CD2 LEU A 114 -22.643 2.506 -1.457 1.00 6.46 C ANISOU 902 CD2 LEU A 114 913 740 799 57 8 -88 C ATOM 903 N ARG A 115 -18.450 -0.630 -0.346 1.00 6.27 N ANISOU 903 N ARG A 115 831 795 758 51 106 -74 N ATOM 904 CA ARG A 115 -17.800 -1.787 0.271 1.00 12.24 C ANISOU 904 CA ARG A 115 1552 1553 1547 55 124 -68 C ATOM 905 C ARG A 115 -17.528 -1.560 1.752 1.00 9.15 C ANISOU 905 C ARG A 115 1141 1173 1163 41 155 -28 C ATOM 906 O ARG A 115 -17.873 -2.390 2.591 1.00 10.93 O ANISOU 906 O ARG A 115 1334 1379 1439 48 164 -11 O ATOM 907 CB ARG A 115 -16.489 -2.133 -0.439 1.00 16.60 C ANISOU 907 CB ARG A 115 2115 2135 2058 62 137 -83 C ATOM 908 CG ARG A 115 -16.695 -2.834 -1.772 1.00 16.85 C ANISOU 908 CG ARG A 115 2160 2154 2086 91 106 -127 C ATOM 909 CD ARG A 115 -15.412 -3.429 -2.323 1.00 18.20 C ANISOU 909 CD ARG A 115 2334 2354 2227 106 126 -141 C ATOM 910 NE ARG A 115 -15.706 -4.347 -3.416 1.00 24.23 N ANISOU 910 NE ARG A 115 3107 3101 3000 142 90 -191 N ATOM 911 CZ ARG A 115 -15.910 -3.979 -4.676 1.00 25.94 C ANISOU 911 CZ ARG A 115 3367 3328 3161 169 69 -221 C ATOM 912 NH1 ARG A 115 -15.852 -2.698 -5.018 1.00 24.40 N ANISOU 912 NH1 ARG A 115 3208 3158 2904 160 85 -199 N ATOM 913 NH2 ARG A 115 -16.164 -4.897 -5.597 1.00 33.03 N ANISOU 913 NH2 ARG A 115 4274 4210 4067 209 29 -275 N ATOM 914 N VAL A 116 -16.908 -0.432 2.072 1.00 8.03 N ANISOU 914 N VAL A 116 1020 1060 972 24 171 -14 N ATOM 915 CA VAL A 116 -16.658 -0.087 3.468 1.00 10.63 C ANISOU 915 CA VAL A 116 1338 1402 1298 18 191 15 C ATOM 916 C VAL A 116 -17.956 0.031 4.262 1.00 14.26 C ANISOU 916 C VAL A 116 1790 1838 1791 26 191 32 C ATOM 917 O VAL A 116 -18.040 -0.423 5.403 1.00 12.96 O ANISOU 917 O VAL A 116 1605 1675 1645 37 211 58 O ATOM 918 CB VAL A 116 -15.902 1.241 3.588 1.00 11.36 C ANISOU 918 CB VAL A 116 1453 1520 1342 -1 196 19 C ATOM 919 CG1 VAL A 116 -15.676 1.579 5.052 1.00 5.64 C ANISOU 919 CG1 VAL A 116 721 809 612 0 206 38 C ATOM 920 CG2 VAL A 116 -14.603 1.170 2.817 1.00 5.79 C ANISOU 920 CG2 VAL A 116 749 837 612 -9 205 10 C ATOM 921 N MET A 117 -18.969 0.647 3.662 1.00 6.79 N ANISOU 921 N MET A 117 857 870 851 24 173 20 N ATOM 922 CA MET A 117 -20.231 0.834 4.360 1.00 8.70 C ANISOU 922 CA MET A 117 1088 1088 1130 32 176 37 C ATOM 923 C MET A 117 -20.844 -0.521 4.683 1.00 5.97 C ANISOU 923 C MET A 117 700 711 856 48 184 51 C ATOM 924 O MET A 117 -21.279 -0.771 5.796 1.00 11.50 O ANISOU 924 O MET A 117 1379 1406 1583 61 212 85 O ATOM 925 CB MET A 117 -21.192 1.682 3.522 1.00 5.81 C ANISOU 925 CB MET A 117 742 701 765 28 149 19 C ATOM 926 CG MET A 117 -22.614 1.748 4.072 1.00 19.74 C ANISOU 926 CG MET A 117 2485 2433 2583 39 151 34 C ATOM 927 SD MET A 117 -23.610 3.024 3.262 1.00 24.43 S ANISOU 927 SD MET A 117 3105 3007 3168 35 118 16 S ATOM 928 CE MET A 117 -23.920 2.267 1.673 1.00 35.74 C ANISOU 928 CE MET A 117 4538 4414 4627 42 69 -23 C ATOM 929 N THR A 118 -20.855 -1.396 3.689 1.00 9.14 N ANISOU 929 N THR A 118 1090 1092 1291 51 159 24 N ATOM 930 CA THR A 118 -21.489 -2.702 3.806 1.00 11.64 C ANISOU 930 CA THR A 118 1361 1366 1694 64 156 31 C ATOM 931 C THR A 118 -20.740 -3.562 4.819 1.00 14.58 C ANISOU 931 C THR A 118 1711 1752 2078 72 192 65 C ATOM 932 O THR A 118 -21.319 -4.079 5.770 1.00 9.83 O ANISOU 932 O THR A 118 1077 1131 1529 84 220 106 O ATOM 933 CB THR A 118 -21.497 -3.413 2.430 1.00 6.56 C ANISOU 933 CB THR A 118 717 699 1075 70 112 -18 C ATOM 934 OG1 THR A 118 -22.255 -2.627 1.500 1.00 16.90 O ANISOU 934 OG1 THR A 118 2051 1997 2371 70 74 -48 O ATOM 935 CG2 THR A 118 -22.100 -4.812 2.520 1.00 6.90 C ANISOU 935 CG2 THR A 118 707 689 1224 82 102 -17 C ATOM 936 N GLN A 119 -19.438 -3.687 4.618 1.00 12.22 N ANISOU 936 N GLN A 119 1427 1487 1728 68 194 53 N ATOM 937 CA GLN A 119 -18.626 -4.590 5.409 1.00 6.34 C ANISOU 937 CA GLN A 119 660 753 994 78 219 79 C ATOM 938 C GLN A 119 -18.405 -4.081 6.842 1.00 12.14 C ANISOU 938 C GLN A 119 1401 1519 1692 86 253 122 C ATOM 939 O GLN A 119 -18.406 -4.873 7.789 1.00 11.59 O ANISOU 939 O GLN A 119 1307 1444 1653 104 280 162 O ATOM 940 CB GLN A 119 -17.337 -4.906 4.658 1.00 6.30 C ANISOU 940 CB GLN A 119 666 773 955 73 208 49 C ATOM 941 CG GLN A 119 -17.615 -5.595 3.317 1.00 6.49 C ANISOU 941 CG GLN A 119 686 766 1015 79 174 4 C ATOM 942 CD GLN A 119 -16.362 -6.091 2.629 1.00 11.71 C ANISOU 942 CD GLN A 119 1353 1450 1647 84 172 -23 C ATOM 943 OE1 GLN A 119 -15.495 -6.708 3.257 1.00 12.77 O ANISOU 943 OE1 GLN A 119 1468 1597 1787 88 192 -4 O ATOM 944 NE2 GLN A 119 -16.263 -5.838 1.325 1.00 8.87 N ANISOU 944 NE2 GLN A 119 1021 1096 1255 88 148 -67 N ATOM 945 N LEU A 120 -18.280 -2.768 7.014 1.00 13.92 N ANISOU 945 N LEU A 120 1661 1773 1855 76 251 115 N ATOM 946 CA LEU A 120 -18.236 -2.207 8.370 1.00 13.86 C ANISOU 946 CA LEU A 120 1664 1791 1810 91 275 147 C ATOM 947 C LEU A 120 -19.561 -2.343 9.129 1.00 9.05 C ANISOU 947 C LEU A 120 1039 1158 1243 113 302 184 C ATOM 948 O LEU A 120 -19.570 -2.621 10.320 1.00 11.64 O ANISOU 948 O LEU A 120 1360 1499 1562 141 334 225 O ATOM 949 CB LEU A 120 -17.748 -0.751 8.383 1.00 18.40 C ANISOU 949 CB LEU A 120 2276 2396 2317 77 261 125 C ATOM 950 CG LEU A 120 -16.227 -0.540 8.267 1.00 26.23 C ANISOU 950 CG LEU A 120 3277 3421 3267 64 249 107 C ATOM 951 CD1 LEU A 120 -15.868 0.928 8.476 1.00 23.18 C ANISOU 951 CD1 LEU A 120 2920 3054 2832 52 234 90 C ATOM 952 CD2 LEU A 120 -15.428 -1.435 9.229 1.00 19.88 C ANISOU 952 CD2 LEU A 120 2456 2636 2462 86 262 130 C ATOM 953 N THR A 121 -20.682 -2.156 8.448 1.00 9.81 N ANISOU 953 N THR A 121 1125 1218 1383 104 290 173 N ATOM 954 CA THR A 121 -21.980 -2.331 9.100 1.00 10.94 C ANISOU 954 CA THR A 121 1243 1332 1582 124 320 211 C ATOM 955 C THR A 121 -22.149 -3.756 9.608 1.00 7.63 C ANISOU 955 C THR A 121 778 886 1235 143 350 255 C ATOM 956 O THR A 121 -22.646 -3.976 10.708 1.00 10.05 O ANISOU 956 O THR A 121 1070 1193 1557 171 396 309 O ATOM 957 CB THR A 121 -23.148 -1.973 8.164 1.00 9.49 C ANISOU 957 CB THR A 121 1049 1107 1449 110 294 187 C ATOM 958 OG1 THR A 121 -23.105 -0.573 7.892 1.00 9.24 O ANISOU 958 OG1 THR A 121 1060 1098 1352 98 274 159 O ATOM 959 CG2 THR A 121 -24.477 -2.313 8.809 1.00 6.95 C ANISOU 959 CG2 THR A 121 687 748 1206 130 327 231 C ATOM 960 N LEU A 122 -21.725 -4.714 8.792 1.00 11.74 N ANISOU 960 N LEU A 122 1278 1384 1800 130 325 233 N ATOM 961 CA LEU A 122 -21.751 -6.121 9.169 1.00 12.96 C ANISOU 961 CA LEU A 122 1387 1507 2030 145 347 271 C ATOM 962 C LEU A 122 -20.812 -6.405 10.350 1.00 13.22 C ANISOU 962 C LEU A 122 1430 1582 2011 169 383 314 C ATOM 963 O LEU A 122 -21.133 -7.203 11.224 1.00 11.59 O ANISOU 963 O LEU A 122 1194 1360 1851 195 425 374 O ATOM 964 CB LEU A 122 -21.429 -7.011 7.959 1.00 12.07 C ANISOU 964 CB LEU A 122 1255 1361 1970 129 304 225 C ATOM 965 CG LEU A 122 -22.540 -7.118 6.899 1.00 17.81 C ANISOU 965 CG LEU A 122 1959 2032 2776 118 265 189 C ATOM 966 CD1 LEU A 122 -21.995 -7.617 5.572 1.00 17.79 C ANISOU 966 CD1 LEU A 122 1962 2017 2780 108 211 124 C ATOM 967 CD2 LEU A 122 -23.698 -8.001 7.369 1.00 17.95 C ANISOU 967 CD2 LEU A 122 1914 1986 2922 129 287 235 C ATOM 968 N ALA A 123 -19.661 -5.742 10.374 1.00 13.52 N ANISOU 968 N ALA A 123 1509 1672 1956 163 366 285 N ATOM 969 CA ALA A 123 -18.768 -5.834 11.520 1.00 17.11 C ANISOU 969 CA ALA A 123 1978 2169 2352 189 389 318 C ATOM 970 C ALA A 123 -19.440 -5.302 12.794 1.00 16.80 C ANISOU 970 C ALA A 123 1954 2150 2280 225 429 365 C ATOM 971 O ALA A 123 -19.428 -5.968 13.829 1.00 16.96 O ANISOU 971 O ALA A 123 1963 2177 2303 262 468 423 O ATOM 972 CB ALA A 123 -17.456 -5.086 11.240 1.00 11.23 C ANISOU 972 CB ALA A 123 1269 1470 1526 172 355 272 C ATOM 973 N LEU A 124 -20.037 -4.114 12.712 1.00 15.91 N ANISOU 973 N LEU A 124 1866 2045 2133 218 422 344 N ATOM 974 CA LEU A 124 -20.780 -3.559 13.843 1.00 13.76 C ANISOU 974 CA LEU A 124 1608 1789 1829 256 463 383 C ATOM 975 C LEU A 124 -21.872 -4.495 14.351 1.00 17.82 C ANISOU 975 C LEU A 124 2079 2266 2426 283 518 452 C ATOM 976 O LEU A 124 -22.026 -4.663 15.551 1.00 22.68 O ANISOU 976 O LEU A 124 2700 2904 3013 331 567 508 O ATOM 977 CB LEU A 124 -21.418 -2.214 13.490 1.00 13.25 C ANISOU 977 CB LEU A 124 1569 1727 1739 241 445 346 C ATOM 978 CG LEU A 124 -20.522 -0.981 13.393 1.00 22.40 C ANISOU 978 CG LEU A 124 2776 2925 2811 226 403 292 C ATOM 979 CD1 LEU A 124 -21.374 0.255 13.131 1.00 16.12 C ANISOU 979 CD1 LEU A 124 1999 2121 2005 217 394 268 C ATOM 980 CD2 LEU A 124 -19.689 -0.801 14.657 1.00 28.37 C ANISOU 980 CD2 LEU A 124 3562 3731 3488 267 411 305 C ATOM 981 N LYS A 125 -22.635 -5.095 13.443 1.00 8.00 N ANISOU 981 N LYS A 125 790 964 1287 256 511 448 N ATOM 982 CA LYS A 125 -23.746 -5.939 13.854 1.00 17.00 C ANISOU 982 CA LYS A 125 1877 2056 2527 277 562 513 C ATOM 983 C LYS A 125 -23.241 -7.144 14.647 1.00 19.95 C ANISOU 983 C LYS A 125 2229 2430 2923 307 601 577 C ATOM 984 O LYS A 125 -23.880 -7.591 15.592 1.00 22.58 O ANISOU 984 O LYS A 125 2538 2753 3288 347 666 654 O ATOM 985 CB LYS A 125 -24.559 -6.354 12.631 1.00 17.92 C ANISOU 985 CB LYS A 125 1946 2103 2759 240 529 483 C ATOM 986 CG LYS A 125 -25.473 -7.547 12.796 1.00 23.58 C ANISOU 986 CG LYS A 125 2591 2753 3616 250 566 542 C ATOM 987 CD LYS A 125 -26.249 -7.743 11.495 1.00 31.50 C ANISOU 987 CD LYS A 125 3554 3690 4724 214 512 492 C ATOM 988 CE LYS A 125 -26.919 -9.107 11.414 1.00 36.45 C ANISOU 988 CE LYS A 125 4101 4236 5510 215 527 532 C ATOM 989 NZ LYS A 125 -27.412 -9.399 10.035 1.00 32.94 N ANISOU 989 NZ LYS A 125 3625 3731 5160 182 453 463 N ATOM 990 N GLU A 126 -22.080 -7.657 14.260 1.00 15.39 N ANISOU 990 N GLU A 126 1658 1863 2324 292 565 547 N ATOM 991 CA GLU A 126 -21.434 -8.713 15.013 1.00 17.56 C ANISOU 991 CA GLU A 126 1921 2145 2607 322 595 602 C ATOM 992 C GLU A 126 -21.005 -8.221 16.398 1.00 21.44 C ANISOU 992 C GLU A 126 2458 2703 2986 375 630 643 C ATOM 993 O GLU A 126 -21.282 -8.863 17.405 1.00 23.21 O ANISOU 993 O GLU A 126 2669 2927 3223 422 690 724 O ATOM 994 CB GLU A 126 -20.241 -9.245 14.230 1.00 19.86 C ANISOU 994 CB GLU A 126 2211 2437 2896 295 543 551 C ATOM 995 CG GLU A 126 -19.463 -10.271 14.977 1.00 23.85 C ANISOU 995 CG GLU A 126 2706 2951 3403 326 566 602 C ATOM 996 CD GLU A 126 -20.303 -11.482 15.324 1.00 31.67 C ANISOU 996 CD GLU A 126 3638 3881 4515 344 616 679 C ATOM 997 OE1 GLU A 126 -21.297 -11.759 14.619 1.00 31.50 O ANISOU 997 OE1 GLU A 126 3572 3796 4601 320 613 672 O ATOM 998 OE2 GLU A 126 -19.965 -12.166 16.307 1.00 37.58 O ANISOU 998 OE2 GLU A 126 4383 4641 5256 386 657 749 O ATOM 999 N CYS A 127 -20.344 -7.068 16.450 1.00 22.61 N ANISOU 999 N CYS A 127 2661 2905 3025 371 593 588 N ATOM 1000 CA CYS A 127 -19.950 -6.474 17.727 1.00 25.00 C ANISOU 1000 CA CYS A 127 3012 3270 3215 425 613 610 C ATOM 1001 C CYS A 127 -21.140 -6.243 18.656 1.00 28.63 C ANISOU 1001 C CYS A 127 3473 3732 3672 474 681 674 C ATOM 1002 O CYS A 127 -21.091 -6.587 19.838 1.00 31.84 O ANISOU 1002 O CYS A 127 3895 4169 4033 537 729 739 O ATOM 1003 CB CYS A 127 -19.211 -5.154 17.506 1.00 23.20 C ANISOU 1003 CB CYS A 127 2835 3086 2894 406 555 531 C ATOM 1004 SG CYS A 127 -17.572 -5.344 16.796 1.00 28.35 S ANISOU 1004 SG CYS A 127 3491 3754 3527 368 488 472 S ATOM 1005 N HIS A 128 -22.199 -5.648 18.114 1.00 20.03 N ANISOU 1005 N HIS A 128 2370 2612 2628 450 686 656 N ATOM 1006 CA HIS A 128 -23.427 -5.440 18.864 1.00 21.11 C ANISOU 1006 CA HIS A 128 2497 2743 2779 492 755 716 C ATOM 1007 C HIS A 128 -24.016 -6.745 19.396 1.00 26.47 C ANISOU 1007 C HIS A 128 3124 3385 3549 524 829 816 C ATOM 1008 O HIS A 128 -24.537 -6.784 20.507 1.00 31.27 O ANISOU 1008 O HIS A 128 3739 4014 4128 587 901 890 O ATOM 1009 CB HIS A 128 -24.460 -4.715 18.009 1.00 13.29 C ANISOU 1009 CB HIS A 128 1488 1715 1847 453 740 677 C ATOM 1010 CG HIS A 128 -24.088 -3.297 17.691 1.00 21.62 C ANISOU 1010 CG HIS A 128 2598 2806 2813 434 684 596 C ATOM 1011 ND1 HIS A 128 -24.578 -2.640 16.590 1.00 25.93 N ANISOU 1011 ND1 HIS A 128 3134 3319 3399 384 642 540 N ATOM 1012 CD2 HIS A 128 -23.277 -2.423 18.327 1.00 26.67 C ANISOU 1012 CD2 HIS A 128 3298 3506 3331 460 660 563 C ATOM 1013 CE1 HIS A 128 -24.092 -1.403 16.561 1.00 30.56 C ANISOU 1013 CE1 HIS A 128 3773 3944 3896 378 601 481 C ATOM 1014 NE2 HIS A 128 -23.297 -1.257 17.613 1.00 34.46 N ANISOU 1014 NE2 HIS A 128 4307 4491 4294 423 609 491 N ATOM 1015 N ARG A 129 -23.932 -7.808 18.607 1.00 28.17 N ANISOU 1015 N ARG A 129 3284 3542 3875 484 812 820 N ATOM 1016 CA ARG A 129 -24.531 -9.077 18.996 1.00 37.93 C ANISOU 1016 CA ARG A 129 4459 4728 5224 506 877 914 C ATOM 1017 C ARG A 129 -23.848 -9.624 20.241 1.00 41.45 C ANISOU 1017 C ARG A 129 4933 5221 5597 571 925 987 C ATOM 1018 O ARG A 129 -24.496 -10.211 21.107 1.00 42.78 O ANISOU 1018 O ARG A 129 5075 5376 5804 621 1009 1088 O ATOM 1019 CB ARG A 129 -24.426 -10.091 17.862 1.00 37.37 C ANISOU 1019 CB ARG A 129 4330 4586 5283 450 834 888 C ATOM 1020 CG ARG A 129 -25.634 -10.994 17.745 1.00 42.90 C ANISOU 1020 CG ARG A 129 4946 5201 6152 446 883 954 C ATOM 1021 CD ARG A 129 -25.219 -12.435 17.738 1.00 46.13 C ANISOU 1021 CD ARG A 129 5309 5564 6655 446 891 999 C ATOM 1022 NE ARG A 129 -23.995 -12.631 16.976 1.00 47.71 N ANISOU 1022 NE ARG A 129 5534 5779 6815 413 813 920 N ATOM 1023 CZ ARG A 129 -23.040 -13.484 17.324 1.00 53.63 C ANISOU 1023 CZ ARG A 129 6286 6539 7553 431 815 947 C ATOM 1024 NH1 ARG A 129 -21.956 -13.604 16.576 1.00 56.38 N ANISOU 1024 NH1 ARG A 129 6654 6900 7868 400 745 871 N ATOM 1025 NH2 ARG A 129 -23.167 -14.210 18.425 1.00 51.61 N ANISOU 1025 NH2 ARG A 129 6012 6279 7317 482 889 1054 N ATOM 1026 N ARG A 130 -22.540 -9.400 20.327 1.00 43.22 N ANISOU 1026 N ARG A 130 5207 5498 5715 573 871 937 N ATOM 1027 CA ARG A 130 -21.720 -9.928 21.412 1.00 45.95 C ANISOU 1027 CA ARG A 130 5583 5890 5986 634 896 994 C ATOM 1028 C ARG A 130 -21.679 -9.045 22.663 1.00 51.79 C ANISOU 1028 C ARG A 130 6392 6708 6579 709 926 1013 C ATOM 1029 O ARG A 130 -20.890 -9.290 23.574 1.00 50.71 O ANISOU 1029 O ARG A 130 6294 6621 6353 765 931 1044 O ATOM 1030 CB ARG A 130 -20.305 -10.204 20.907 1.00 39.79 C ANISOU 1030 CB ARG A 130 4817 5125 5176 603 820 931 C ATOM 1031 CG ARG A 130 -20.230 -11.366 19.939 1.00 46.72 C ANISOU 1031 CG ARG A 130 5630 5931 6191 553 803 930 C ATOM 1032 CD ARG A 130 -18.815 -11.918 19.882 1.00 58.61 C ANISOU 1032 CD ARG A 130 7149 7459 7663 551 757 906 C ATOM 1033 NE ARG A 130 -18.745 -13.218 19.220 1.00 63.53 N ANISOU 1033 NE ARG A 130 7710 8014 8416 522 754 922 N ATOM 1034 CZ ARG A 130 -18.728 -14.381 19.862 1.00 62.79 C ANISOU 1034 CZ ARG A 130 7586 7895 8378 559 800 1010 C ATOM 1035 NH1 ARG A 130 -18.777 -14.409 21.190 1.00 59.49 N ANISOU 1035 NH1 ARG A 130 7196 7519 7888 630 859 1095 N ATOM 1036 NH2 ARG A 130 -18.667 -15.514 19.177 1.00 65.55 N ANISOU 1036 NH2 ARG A 130 7878 8175 8854 530 789 1014 N ATOM 1037 N SER A 131 -22.535 -8.029 22.709 1.00 52.62 N ANISOU 1037 N SER A 131 6513 6821 6658 713 942 993 N ATOM 1038 CA SER A 131 -22.639 -7.182 23.893 1.00 54.32 C ANISOU 1038 CA SER A 131 6793 7106 6739 791 973 1009 C ATOM 1039 C SER A 131 -23.609 -7.784 24.903 1.00 56.51 C ANISOU 1039 C SER A 131 7052 7380 7039 865 1087 1133 C ATOM 1040 O SER A 131 -23.462 -7.598 26.112 1.00 57.30 O ANISOU 1040 O SER A 131 7206 7543 7022 953 1127 1177 O ATOM 1041 CB SER A 131 -23.088 -5.772 23.510 1.00 57.53 C ANISOU 1041 CB SER A 131 7227 7525 7105 768 938 929 C ATOM 1042 OG SER A 131 -22.166 -5.181 22.608 1.00 57.06 O ANISOU 1042 OG SER A 131 7185 7469 7024 704 840 825 O ATOM 1043 N HIS A 139 -14.514 -2.345 22.468 1.00 56.19 N ANISOU 1043 N HIS A 139 7255 7553 6543 639 381 418 N ATOM 1044 CA HIS A 139 -13.617 -1.702 21.515 1.00 60.14 C ANISOU 1044 CA HIS A 139 7741 8039 7072 570 312 340 C ATOM 1045 C HIS A 139 -14.156 -1.737 20.087 1.00 59.55 C ANISOU 1045 C HIS A 139 7626 7912 7089 491 328 330 C ATOM 1046 O HIS A 139 -13.850 -2.658 19.323 1.00 59.22 O ANISOU 1046 O HIS A 139 7544 7844 7113 454 336 345 O ATOM 1047 CB HIS A 139 -12.251 -2.393 21.498 1.00 65.30 C ANISOU 1047 CB HIS A 139 8375 8702 7732 564 271 332 C ATOM 1048 CG HIS A 139 -11.530 -2.385 22.809 1.00 75.61 C ANISOU 1048 CG HIS A 139 9720 10058 8950 640 238 332 C ATOM 1049 ND1 HIS A 139 -11.469 -1.277 23.625 1.00 81.23 N ANISOU 1049 ND1 HIS A 139 10481 10804 9580 685 197 286 N ATOM 1050 CD2 HIS A 139 -10.797 -3.345 23.420 1.00 80.00 C ANISOU 1050 CD2 HIS A 139 10273 10636 9489 682 233 367 C ATOM 1051 CE1 HIS A 139 -10.747 -1.561 24.694 1.00 83.86 C ANISOU 1051 CE1 HIS A 139 10842 11179 9842 755 165 291 C ATOM 1052 NE2 HIS A 139 -10.327 -2.810 24.595 1.00 82.90 N ANISOU 1052 NE2 HIS A 139 10689 11051 9757 755 187 343 N ATOM 1053 N ARG A 140 -14.940 -0.734 19.718 1.00 59.46 N ANISOU 1053 N ARG A 140 7627 7887 7079 470 329 302 N ATOM 1054 CA ARG A 140 -15.388 -0.614 18.341 1.00 63.34 C ANISOU 1054 CA ARG A 140 8087 8333 7645 400 332 284 C ATOM 1055 C ARG A 140 -15.364 0.855 17.954 1.00 61.90 C ANISOU 1055 C ARG A 140 7928 8149 7443 370 290 221 C ATOM 1056 O ARG A 140 -16.366 1.411 17.506 1.00 62.27 O ANISOU 1056 O ARG A 140 7976 8173 7512 353 307 217 O ATOM 1057 CB ARG A 140 -16.784 -1.222 18.157 1.00 67.80 C ANISOU 1057 CB ARG A 140 8630 8866 8266 404 395 338 C ATOM 1058 CG ARG A 140 -17.859 -0.583 19.025 1.00 70.40 C ANISOU 1058 CG ARG A 140 8986 9208 8554 453 432 360 C ATOM 1059 CD ARG A 140 -18.565 -1.617 19.890 1.00 72.68 C ANISOU 1059 CD ARG A 140 9263 9500 8853 510 503 444 C ATOM 1060 NE ARG A 140 -19.922 -1.207 20.240 1.00 75.40 N ANISOU 1060 NE ARG A 140 9611 9835 9204 538 555 475 N ATOM 1061 CZ ARG A 140 -20.232 -0.103 20.920 1.00 79.78 C ANISOU 1061 CZ ARG A 140 10210 10420 9683 578 552 451 C ATOM 1062 NH1 ARG A 140 -21.505 0.174 21.183 1.00 81.49 N ANISOU 1062 NH1 ARG A 140 10423 10624 9916 604 607 483 N ATOM 1063 NH2 ARG A 140 -19.280 0.732 21.326 1.00 81.19 N ANISOU 1063 NH2 ARG A 140 10434 10637 9779 592 493 391 N ATOM 1064 N ASP A 141 -14.215 1.486 18.165 1.00 59.01 N ANISOU 1064 N ASP A 141 7576 7804 7042 367 233 173 N ATOM 1065 CA ASP A 141 -14.032 2.891 17.830 1.00 61.63 C ANISOU 1065 CA ASP A 141 7924 8128 7364 338 188 114 C ATOM 1066 C ASP A 141 -13.650 2.980 16.353 1.00 48.52 C ANISOU 1066 C ASP A 141 6233 6435 5768 263 176 94 C ATOM 1067 O ASP A 141 -12.667 2.374 15.894 1.00 42.22 O ANISOU 1067 O ASP A 141 5408 5637 4996 240 164 92 O ATOM 1068 CB ASP A 141 -13.020 3.534 18.797 1.00 73.40 C ANISOU 1068 CB ASP A 141 9441 9650 8798 372 129 71 C ATOM 1069 CG ASP A 141 -12.151 4.599 18.152 1.00 82.30 C ANISOU 1069 CG ASP A 141 10559 10759 9953 321 70 10 C ATOM 1070 OD1 ASP A 141 -12.685 5.495 17.465 1.00 83.83 O ANISOU 1070 OD1 ASP A 141 10755 10925 10172 284 70 -10 O ATOM 1071 OD2 ASP A 141 -10.919 4.549 18.369 1.00 85.87 O ANISOU 1071 OD2 ASP A 141 10999 11222 10407 319 24 -15 O ATOM 1072 N LEU A 142 -14.473 3.714 15.613 1.00 41.42 N ANISOU 1072 N LEU A 142 5337 5508 4891 233 184 82 N ATOM 1073 CA LEU A 142 -14.486 3.622 14.165 1.00 38.65 C ANISOU 1073 CA LEU A 142 4963 5128 4596 175 188 78 C ATOM 1074 C LEU A 142 -13.664 4.678 13.449 1.00 35.55 C ANISOU 1074 C LEU A 142 4569 4724 4214 132 148 36 C ATOM 1075 O LEU A 142 -14.143 5.290 12.503 1.00 48.16 O ANISOU 1075 O LEU A 142 6168 6296 5834 98 150 28 O ATOM 1076 CB LEU A 142 -15.929 3.677 13.654 1.00 37.13 C ANISOU 1076 CB LEU A 142 4771 4908 4429 170 220 96 C ATOM 1077 CG LEU A 142 -16.694 2.365 13.509 1.00 37.64 C ANISOU 1077 CG LEU A 142 4810 4958 4532 181 263 141 C ATOM 1078 CD1 LEU A 142 -16.637 1.554 14.783 1.00 46.22 C ANISOU 1078 CD1 LEU A 142 5897 6070 5593 234 288 179 C ATOM 1079 CD2 LEU A 142 -18.128 2.629 13.113 1.00 37.30 C ANISOU 1079 CD2 LEU A 142 4765 4885 4521 178 284 152 C ATOM 1080 N LYS A 143 -12.428 4.889 13.873 1.00 31.23 N ANISOU 1080 N LYS A 143 4017 4194 3657 132 112 13 N ATOM 1081 CA LYS A 143 -11.551 5.772 13.120 1.00 25.59 C ANISOU 1081 CA LYS A 143 3290 3463 2971 87 82 -18 C ATOM 1082 C LYS A 143 -10.895 5.015 11.966 1.00 23.21 C ANISOU 1082 C LYS A 143 2956 3155 2709 51 101 -3 C ATOM 1083 O LYS A 143 -10.736 3.796 12.025 1.00 18.68 O ANISOU 1083 O LYS A 143 2367 2593 2138 66 121 19 O ATOM 1084 CB LYS A 143 -10.501 6.408 14.027 1.00 28.25 C ANISOU 1084 CB LYS A 143 3626 3811 3295 101 29 -53 C ATOM 1085 CG LYS A 143 -9.818 5.439 14.959 1.00 32.77 C ANISOU 1085 CG LYS A 143 4193 4416 3844 141 19 -45 C ATOM 1086 CD LYS A 143 -8.814 6.159 15.846 1.00 33.34 C ANISOU 1086 CD LYS A 143 4265 4497 3905 159 -47 -90 C ATOM 1087 CE LYS A 143 -7.860 5.176 16.508 1.00 43.13 C ANISOU 1087 CE LYS A 143 5489 5764 5133 189 -64 -83 C ATOM 1088 NZ LYS A 143 -6.720 5.877 17.167 1.00 50.50 N ANISOU 1088 NZ LYS A 143 6412 6699 6075 198 -139 -133 N ATOM 1089 N PRO A 144 -10.542 5.738 10.896 1.00 19.78 N ANISOU 1089 N PRO A 144 2512 2699 2303 8 98 -13 N ATOM 1090 CA PRO A 144 -9.827 5.213 9.730 1.00 18.80 C ANISOU 1090 CA PRO A 144 2362 2572 2211 -22 119 -2 C ATOM 1091 C PRO A 144 -8.647 4.313 10.102 1.00 23.18 C ANISOU 1091 C PRO A 144 2886 3147 2776 -12 113 0 C ATOM 1092 O PRO A 144 -8.426 3.287 9.460 1.00 27.95 O ANISOU 1092 O PRO A 144 3473 3755 3393 -14 139 15 O ATOM 1093 CB PRO A 144 -9.316 6.483 9.057 1.00 22.44 C ANISOU 1093 CB PRO A 144 2817 3013 2697 -59 106 -15 C ATOM 1094 CG PRO A 144 -10.374 7.473 9.341 1.00 22.00 C ANISOU 1094 CG PRO A 144 2793 2940 2626 -54 94 -24 C ATOM 1095 CD PRO A 144 -10.913 7.151 10.714 1.00 16.78 C ANISOU 1095 CD PRO A 144 2150 2297 1929 -10 80 -32 C ATOM 1096 N ALA A 145 -7.909 4.695 11.135 1.00 24.33 N ANISOU 1096 N ALA A 145 3024 3302 2917 2 74 -20 N ATOM 1097 CA ALA A 145 -6.706 3.974 11.530 1.00 26.66 C ANISOU 1097 CA ALA A 145 3288 3615 3228 12 59 -22 C ATOM 1098 C ALA A 145 -7.005 2.581 12.088 1.00 21.52 C ANISOU 1098 C ALA A 145 2640 2984 2553 50 78 3 C ATOM 1099 O ALA A 145 -6.118 1.735 12.140 1.00 22.00 O ANISOU 1099 O ALA A 145 2672 3056 2631 57 77 9 O ATOM 1100 CB ALA A 145 -5.894 4.808 12.540 1.00 19.26 C ANISOU 1100 CB ALA A 145 2344 2680 2294 22 1 -55 C ATOM 1101 N ASN A 146 -8.256 2.356 12.493 1.00 18.96 N ANISOU 1101 N ASN A 146 2346 2661 2196 76 97 19 N ATOM 1102 CA ASN A 146 -8.698 1.083 13.058 1.00 11.44 C ANISOU 1102 CA ASN A 146 1395 1721 1230 114 121 52 C ATOM 1103 C ASN A 146 -9.407 0.203 12.027 1.00 15.46 C ANISOU 1103 C ASN A 146 1894 2211 1770 99 163 75 C ATOM 1104 O ASN A 146 -9.945 -0.853 12.355 1.00 14.49 O ANISOU 1104 O ASN A 146 1767 2086 1652 125 187 105 O ATOM 1105 CB ASN A 146 -9.630 1.313 14.254 1.00 26.69 C ANISOU 1105 CB ASN A 146 3362 3666 3114 160 121 63 C ATOM 1106 CG ASN A 146 -8.923 1.926 15.449 1.00 39.20 C ANISOU 1106 CG ASN A 146 4962 5275 4659 193 72 37 C ATOM 1107 OD1 ASN A 146 -7.694 1.954 15.510 1.00 46.07 O ANISOU 1107 OD1 ASN A 146 5808 6151 5544 184 36 16 O ATOM 1108 ND2 ASN A 146 -9.705 2.414 16.417 1.00 37.40 N ANISOU 1108 ND2 ASN A 146 4770 5059 4380 235 69 37 N ATOM 1109 N VAL A 147 -9.412 0.641 10.775 1.00 16.63 N ANISOU 1109 N VAL A 147 2037 2341 1940 59 170 60 N ATOM 1110 CA VAL A 147 -10.082 -0.120 9.723 1.00 12.78 C ANISOU 1110 CA VAL A 147 1544 1834 1478 50 199 71 C ATOM 1111 C VAL A 147 -9.101 -0.514 8.634 1.00 13.85 C ANISOU 1111 C VAL A 147 1656 1970 1638 28 206 60 C ATOM 1112 O VAL A 147 -8.406 0.337 8.085 1.00 14.25 O ANISOU 1112 O VAL A 147 1704 2023 1688 3 199 45 O ATOM 1113 CB VAL A 147 -11.222 0.667 9.080 1.00 14.42 C ANISOU 1113 CB VAL A 147 1775 2021 1681 34 204 65 C ATOM 1114 CG1 VAL A 147 -11.983 -0.222 8.108 1.00 10.83 C ANISOU 1114 CG1 VAL A 147 1315 1545 1256 33 223 71 C ATOM 1115 CG2 VAL A 147 -12.143 1.227 10.155 1.00 11.48 C ANISOU 1115 CG2 VAL A 147 1426 1651 1285 57 200 73 C ATOM 1116 N PHE A 148 -9.069 -1.803 8.310 1.00 8.13 N ANISOU 1116 N PHE A 148 913 1239 936 41 222 69 N ATOM 1117 CA PHE A 148 -8.045 -2.341 7.424 1.00 8.83 C ANISOU 1117 CA PHE A 148 978 1332 1045 31 231 58 C ATOM 1118 C PHE A 148 -8.606 -2.944 6.143 1.00 11.53 C ANISOU 1118 C PHE A 148 1324 1656 1401 30 247 48 C ATOM 1119 O PHE A 148 -9.775 -3.325 6.074 1.00 18.16 O ANISOU 1119 O PHE A 148 2174 2473 2251 39 247 52 O ATOM 1120 CB PHE A 148 -7.180 -3.366 8.190 1.00 6.63 C ANISOU 1120 CB PHE A 148 671 1066 784 53 227 70 C ATOM 1121 CG PHE A 148 -6.487 -2.775 9.386 1.00 10.18 C ANISOU 1121 CG PHE A 148 1117 1535 1214 61 201 72 C ATOM 1122 CD1 PHE A 148 -7.115 -2.732 10.618 1.00 11.19 C ANISOU 1122 CD1 PHE A 148 1264 1670 1318 89 190 89 C ATOM 1123 CD2 PHE A 148 -5.234 -2.208 9.263 1.00 11.25 C ANISOU 1123 CD2 PHE A 148 1232 1684 1361 44 186 56 C ATOM 1124 CE1 PHE A 148 -6.493 -2.161 11.716 1.00 14.36 C ANISOU 1124 CE1 PHE A 148 1670 2093 1694 104 157 83 C ATOM 1125 CE2 PHE A 148 -4.603 -1.641 10.354 1.00 7.27 C ANISOU 1125 CE2 PHE A 148 723 1194 846 53 150 49 C ATOM 1126 CZ PHE A 148 -5.228 -1.615 11.580 1.00 9.86 C ANISOU 1126 CZ PHE A 148 1077 1532 1140 85 132 59 C ATOM 1127 N LEU A 149 -7.755 -3.025 5.132 1.00 8.68 N ANISOU 1127 N LEU A 149 952 1302 1042 21 259 34 N ATOM 1128 CA LEU A 149 -8.094 -3.668 3.881 1.00 11.56 C ANISOU 1128 CA LEU A 149 1324 1655 1413 30 270 16 C ATOM 1129 C LEU A 149 -7.155 -4.849 3.643 1.00 17.59 C ANISOU 1129 C LEU A 149 2058 2424 2201 47 281 9 C ATOM 1130 O LEU A 149 -5.947 -4.729 3.837 1.00 20.21 O ANISOU 1130 O LEU A 149 2367 2776 2537 42 290 14 O ATOM 1131 CB LEU A 149 -7.932 -2.669 2.749 1.00 9.91 C ANISOU 1131 CB LEU A 149 1136 1454 1173 15 282 7 C ATOM 1132 CG LEU A 149 -8.526 -1.291 3.029 1.00 14.25 C ANISOU 1132 CG LEU A 149 1711 2001 1703 -6 272 16 C ATOM 1133 CD1 LEU A 149 -8.033 -0.337 1.956 1.00 16.70 C ANISOU 1133 CD1 LEU A 149 2034 2320 1990 -21 291 17 C ATOM 1134 CD2 LEU A 149 -10.047 -1.367 3.050 1.00 15.96 C ANISOU 1134 CD2 LEU A 149 1951 2194 1919 2 256 12 C ATOM 1135 N ASP A 150 -7.703 -5.989 3.232 1.00 6.79 N ANISOU 1135 N ASP A 150 686 1034 859 68 278 -4 N ATOM 1136 CA ASP A 150 -6.873 -7.112 2.820 1.00 11.08 C ANISOU 1136 CA ASP A 150 1204 1578 1427 88 287 -18 C ATOM 1137 C ASP A 150 -6.617 -7.034 1.306 1.00 15.56 C ANISOU 1137 C ASP A 150 1790 2155 1969 97 302 -49 C ATOM 1138 O ASP A 150 -6.774 -5.965 0.703 1.00 14.60 O ANISOU 1138 O ASP A 150 1695 2045 1806 85 310 -49 O ATOM 1139 CB ASP A 150 -7.491 -8.448 3.251 1.00 13.65 C ANISOU 1139 CB ASP A 150 1512 1870 1804 109 274 -16 C ATOM 1140 CG ASP A 150 -8.656 -8.871 2.380 1.00 23.46 C ANISOU 1140 CG ASP A 150 2770 3079 3064 120 258 -44 C ATOM 1141 OD1 ASP A 150 -9.129 -8.054 1.561 1.00 25.63 O ANISOU 1141 OD1 ASP A 150 3077 3360 3302 113 254 -62 O ATOM 1142 OD2 ASP A 150 -9.089 -10.035 2.522 1.00 20.01 O ANISOU 1142 OD2 ASP A 150 2312 2607 2684 138 246 -48 O ATOM 1143 N GLY A 151 -6.206 -8.133 0.683 1.00 9.53 N ANISOU 1143 N GLY A 151 1013 1385 1224 124 306 -74 N ATOM 1144 CA GLY A 151 -5.853 -8.066 -0.727 1.00 16.31 C ANISOU 1144 CA GLY A 151 1891 2259 2046 144 325 -103 C ATOM 1145 C GLY A 151 -6.947 -8.495 -1.686 1.00 18.57 C ANISOU 1145 C GLY A 151 2209 2521 2324 169 299 -143 C ATOM 1146 O GLY A 151 -6.718 -8.640 -2.883 1.00 17.14 O ANISOU 1146 O GLY A 151 2051 2353 2107 199 308 -174 O ATOM 1147 N LYS A 152 -8.139 -8.708 -1.144 1.00 13.44 N ANISOU 1147 N LYS A 152 1560 1837 1709 162 265 -141 N ATOM 1148 CA LYS A 152 -9.264 -9.219 -1.912 1.00 12.41 C ANISOU 1148 CA LYS A 152 1449 1673 1593 184 229 -182 C ATOM 1149 C LYS A 152 -10.485 -8.297 -1.821 1.00 15.18 C ANISOU 1149 C LYS A 152 1825 2011 1931 166 208 -172 C ATOM 1150 O LYS A 152 -11.623 -8.750 -1.926 1.00 11.78 O ANISOU 1150 O LYS A 152 1394 1539 1542 174 171 -193 O ATOM 1151 CB LYS A 152 -9.603 -10.627 -1.417 1.00 26.05 C ANISOU 1151 CB LYS A 152 3140 3355 3403 198 205 -193 C ATOM 1152 CG LYS A 152 -8.630 -11.693 -1.921 1.00 31.82 C ANISOU 1152 CG LYS A 152 3854 4088 4148 230 212 -224 C ATOM 1153 CD LYS A 152 -8.103 -12.569 -0.802 1.00 39.84 C ANISOU 1153 CD LYS A 152 4822 5088 5228 224 221 -193 C ATOM 1154 CE LYS A 152 -9.199 -13.308 -0.076 1.00 45.64 C ANISOU 1154 CE LYS A 152 5531 5766 6044 221 193 -180 C ATOM 1155 NZ LYS A 152 -8.575 -14.220 0.919 1.00 47.27 N ANISOU 1155 NZ LYS A 152 5695 5960 6307 224 205 -146 N ATOM 1156 N GLN A 153 -10.234 -7.004 -1.625 1.00 7.43 N ANISOU 1156 N GLN A 153 861 1059 901 140 230 -142 N ATOM 1157 CA GLN A 153 -11.291 -5.996 -1.476 1.00 16.34 C ANISOU 1157 CA GLN A 153 2014 2178 2016 122 215 -129 C ATOM 1158 C GLN A 153 -12.151 -6.262 -0.256 1.00 16.66 C ANISOU 1158 C GLN A 153 2029 2188 2114 107 201 -106 C ATOM 1159 O GLN A 153 -13.326 -5.910 -0.223 1.00 13.71 O ANISOU 1159 O GLN A 153 1665 1789 1753 102 179 -106 O ATOM 1160 CB GLN A 153 -12.168 -5.888 -2.727 1.00 10.64 C ANISOU 1160 CB GLN A 153 1329 1444 1269 145 184 -168 C ATOM 1161 CG GLN A 153 -11.411 -5.423 -3.971 1.00 18.08 C ANISOU 1161 CG GLN A 153 2308 2424 2137 167 206 -182 C ATOM 1162 CD GLN A 153 -12.309 -5.255 -5.188 1.00 23.89 C ANISOU 1162 CD GLN A 153 3089 3153 2837 199 171 -220 C ATOM 1163 OE1 GLN A 153 -13.148 -6.106 -5.477 1.00 22.68 O ANISOU 1163 OE1 GLN A 153 2933 2964 2722 222 123 -262 O ATOM 1164 NE2 GLN A 153 -12.123 -4.162 -5.913 1.00 27.11 N ANISOU 1164 NE2 GLN A 153 3537 3591 3174 203 191 -205 N ATOM 1165 N ASN A 154 -11.558 -6.897 0.748 1.00 12.75 N ANISOU 1165 N ASN A 154 1499 1693 1652 104 215 -82 N ATOM 1166 CA ASN A 154 -12.255 -7.087 2.003 1.00 13.19 C ANISOU 1166 CA ASN A 154 1534 1727 1752 96 214 -48 C ATOM 1167 C ASN A 154 -11.898 -6.026 3.023 1.00 16.89 C ANISOU 1167 C ASN A 154 2008 2224 2183 76 231 -12 C ATOM 1168 O ASN A 154 -10.758 -5.567 3.114 1.00 11.10 O ANISOU 1168 O ASN A 154 1276 1525 1417 67 245 -7 O ATOM 1169 CB ASN A 154 -12.004 -8.482 2.563 1.00 16.29 C ANISOU 1169 CB ASN A 154 1887 2096 2206 112 216 -38 C ATOM 1170 CG ASN A 154 -12.469 -9.569 1.627 1.00 23.26 C ANISOU 1170 CG ASN A 154 2760 2940 3140 134 190 -79 C ATOM 1171 OD1 ASN A 154 -13.522 -9.449 0.997 1.00 23.78 O ANISOU 1171 OD1 ASN A 154 2837 2977 3220 137 162 -104 O ATOM 1172 ND2 ASN A 154 -11.686 -10.640 1.524 1.00 18.59 N ANISOU 1172 ND2 ASN A 154 2143 2341 2577 151 193 -91 N ATOM 1173 N VAL A 155 -12.903 -5.640 3.790 1.00 17.94 N ANISOU 1173 N VAL A 155 2144 2342 2329 71 228 11 N ATOM 1174 CA VAL A 155 -12.756 -4.604 4.788 1.00 12.16 C ANISOU 1174 CA VAL A 155 1424 1636 1562 59 238 37 C ATOM 1175 C VAL A 155 -12.933 -5.222 6.166 1.00 13.09 C ANISOU 1175 C VAL A 155 1519 1747 1706 75 249 75 C ATOM 1176 O VAL A 155 -13.887 -5.955 6.413 1.00 16.83 O ANISOU 1176 O VAL A 155 1977 2189 2230 88 253 91 O ATOM 1177 CB VAL A 155 -13.797 -3.484 4.581 1.00 13.33 C ANISOU 1177 CB VAL A 155 1599 1775 1691 47 228 34 C ATOM 1178 CG1 VAL A 155 -13.653 -2.418 5.640 1.00 7.56 C ANISOU 1178 CG1 VAL A 155 880 1066 925 39 234 54 C ATOM 1179 CG2 VAL A 155 -13.672 -2.891 3.174 1.00 6.05 C ANISOU 1179 CG2 VAL A 155 703 858 739 38 218 3 C ATOM 1180 N LYS A 156 -12.000 -4.923 7.061 1.00 18.84 N ANISOU 1180 N LYS A 156 2247 2508 2404 77 255 91 N ATOM 1181 CA LYS A 156 -12.023 -5.492 8.393 1.00 20.76 C ANISOU 1181 CA LYS A 156 2476 2754 2657 102 266 129 C ATOM 1182 C LYS A 156 -11.837 -4.433 9.458 1.00 15.80 C ANISOU 1182 C LYS A 156 1870 2157 1977 107 262 141 C ATOM 1183 O LYS A 156 -10.995 -3.548 9.331 1.00 18.59 O ANISOU 1183 O LYS A 156 2234 2534 2295 90 247 118 O ATOM 1184 CB LYS A 156 -10.939 -6.554 8.512 1.00 21.31 C ANISOU 1184 CB LYS A 156 2519 2831 2747 114 268 134 C ATOM 1185 CG LYS A 156 -10.779 -7.359 7.241 1.00 23.64 C ANISOU 1185 CG LYS A 156 2799 3103 3081 108 265 104 C ATOM 1186 CD LYS A 156 -10.521 -8.794 7.549 1.00 25.51 C ANISOU 1186 CD LYS A 156 3003 3320 3370 130 271 122 C ATOM 1187 CE LYS A 156 -10.673 -9.618 6.298 1.00 24.41 C ANISOU 1187 CE LYS A 156 2850 3148 3275 131 262 86 C ATOM 1188 NZ LYS A 156 -10.594 -11.048 6.667 1.00 31.16 N ANISOU 1188 NZ LYS A 156 3669 3972 4197 153 266 106 N ATOM 1189 N LEU A 157 -12.638 -4.530 10.507 1.00 15.48 N ANISOU 1189 N LEU A 157 1834 2113 1933 132 277 175 N ATOM 1190 CA LEU A 157 -12.494 -3.656 11.651 1.00 18.08 C ANISOU 1190 CA LEU A 157 2188 2473 2207 151 272 184 C ATOM 1191 C LEU A 157 -11.457 -4.232 12.605 1.00 20.46 C ANISOU 1191 C LEU A 157 2481 2802 2491 179 266 202 C ATOM 1192 O LEU A 157 -11.452 -5.426 12.893 1.00 14.21 O ANISOU 1192 O LEU A 157 1667 2000 1731 201 284 235 O ATOM 1193 CB LEU A 157 -13.842 -3.489 12.357 1.00 14.81 C ANISOU 1193 CB LEU A 157 1786 2050 1793 175 296 216 C ATOM 1194 CG LEU A 157 -13.786 -2.710 13.675 1.00 20.39 C ANISOU 1194 CG LEU A 157 2523 2791 2435 209 294 226 C ATOM 1195 CD1 LEU A 157 -13.081 -1.378 13.468 1.00 20.21 C ANISOU 1195 CD1 LEU A 157 2522 2786 2369 185 255 177 C ATOM 1196 CD2 LEU A 157 -15.166 -2.520 14.288 1.00 15.99 C ANISOU 1196 CD2 LEU A 157 1977 2223 1875 236 327 259 C ATOM 1197 N GLY A 158 -10.561 -3.376 13.075 1.00 30.00 N ANISOU 1197 N GLY A 158 3704 4041 3654 180 236 178 N ATOM 1198 CA GLY A 158 -9.518 -3.813 13.974 1.00 35.06 C ANISOU 1198 CA GLY A 158 4338 4708 4275 209 219 188 C ATOM 1199 C GLY A 158 -9.140 -2.776 15.008 1.00 41.04 C ANISOU 1199 C GLY A 158 5124 5497 4973 232 186 170 C ATOM 1200 O GLY A 158 -8.014 -2.271 15.012 1.00 43.48 O ANISOU 1200 O GLY A 158 5426 5820 5276 220 147 137 O ATOM 1201 N ASP A 159 -10.083 -2.452 15.886 1.00 48.17 N ANISOU 1201 N ASP A 159 6057 6409 5836 268 199 191 N ATOM 1202 CA ASP A 159 -9.776 -1.600 17.022 1.00 55.23 C ANISOU 1202 CA ASP A 159 6985 7336 6666 306 165 172 C ATOM 1203 C ASP A 159 -9.035 -2.447 18.044 1.00 54.89 C ANISOU 1203 C ASP A 159 6940 7320 6594 358 153 197 C ATOM 1204 O ASP A 159 -9.541 -3.471 18.494 1.00 49.81 O ANISOU 1204 O ASP A 159 6295 6678 5953 393 194 253 O ATOM 1205 CB ASP A 159 -11.046 -1.012 17.640 1.00 57.45 C ANISOU 1205 CB ASP A 159 7302 7621 6906 337 189 187 C ATOM 1206 CG ASP A 159 -10.756 -0.161 18.875 1.00 64.71 C ANISOU 1206 CG ASP A 159 8261 8576 7749 388 150 162 C ATOM 1207 OD1 ASP A 159 -11.665 0.555 19.336 1.00 70.13 O ANISOU 1207 OD1 ASP A 159 8980 9267 8398 413 162 160 O ATOM 1208 OD2 ASP A 159 -9.621 -0.206 19.392 1.00 65.51 O ANISOU 1208 OD2 ASP A 159 8361 8699 7829 407 103 140 O ATOM 1209 N PHE A 160 -7.833 -2.013 18.405 1.00 60.37 N ANISOU 1209 N PHE A 160 7633 8034 7270 363 96 158 N ATOM 1210 CA PHE A 160 -6.989 -2.766 19.320 1.00 69.13 C ANISOU 1210 CA PHE A 160 8740 9171 8354 412 73 176 C ATOM 1211 C PHE A 160 -6.851 -2.039 20.656 1.00 67.03 C ANISOU 1211 C PHE A 160 8519 8942 8006 475 28 155 C ATOM 1212 O PHE A 160 -5.747 -1.887 21.178 1.00 67.90 O ANISOU 1212 O PHE A 160 8627 9072 8100 495 -34 123 O ATOM 1213 CB PHE A 160 -5.613 -2.988 18.691 1.00 75.37 C ANISOU 1213 CB PHE A 160 9486 9954 9197 375 37 146 C ATOM 1214 CG PHE A 160 -4.846 -4.127 19.301 1.00 78.58 C ANISOU 1214 CG PHE A 160 9878 10377 9603 416 27 176 C ATOM 1215 CD1 PHE A 160 -5.192 -5.435 19.029 1.00 76.70 C ANISOU 1215 CD1 PHE A 160 9620 10123 9399 421 79 230 C ATOM 1216 CD2 PHE A 160 -3.783 -3.893 20.156 1.00 81.02 C ANISOU 1216 CD2 PHE A 160 10190 10713 9881 451 -38 148 C ATOM 1217 CE1 PHE A 160 -4.485 -6.487 19.595 1.00 77.78 C ANISOU 1217 CE1 PHE A 160 9742 10272 9540 460 71 260 C ATOM 1218 CE2 PHE A 160 -3.076 -4.945 20.722 1.00 80.56 C ANISOU 1218 CE2 PHE A 160 10118 10670 9822 493 -49 177 C ATOM 1219 CZ PHE A 160 -3.426 -6.239 20.439 1.00 79.84 C ANISOU 1219 CZ PHE A 160 10009 10564 9764 496 7 236 C ATOM 1220 N GLY A 161 -7.979 -1.583 21.193 1.00 61.64 N ANISOU 1220 N GLY A 161 7878 8269 7273 509 56 170 N ATOM 1221 CA GLY A 161 -8.003 -0.858 22.451 1.00 58.33 C ANISOU 1221 CA GLY A 161 7510 7887 6765 578 17 147 C ATOM 1222 C GLY A 161 -7.358 -1.605 23.604 1.00 58.38 C ANISOU 1222 C GLY A 161 7535 7934 6714 655 -5 172 C ATOM 1223 O GLY A 161 -6.953 -0.990 24.588 1.00 56.29 O ANISOU 1223 O GLY A 161 7309 7703 6378 713 -64 133 O ATOM 1224 N LEU A 162 -7.298 -2.933 23.498 1.00 60.73 N ANISOU 1224 N LEU A 162 7807 8226 7042 661 39 236 N ATOM 1225 CA LEU A 162 -6.522 -3.761 24.423 1.00 61.07 C ANISOU 1225 CA LEU A 162 7858 8301 7045 726 15 264 C ATOM 1226 C LEU A 162 -5.320 -2.985 24.920 1.00 62.47 C ANISOU 1226 C LEU A 162 8045 8501 7189 744 -87 188 C ATOM 1227 O LEU A 162 -5.151 -2.744 26.119 1.00 60.70 O ANISOU 1227 O LEU A 162 7870 8320 6875 827 -128 178 O ATOM 1228 CB LEU A 162 -5.988 -4.996 23.695 1.00 59.58 C ANISOU 1228 CB LEU A 162 7613 8085 6939 687 39 300 C ATOM 1229 CG LEU A 162 -6.722 -6.324 23.627 1.00 60.54 C ANISOU 1229 CG LEU A 162 7720 8189 7095 701 121 389 C ATOM 1230 CD1 LEU A 162 -5.992 -7.265 22.672 1.00 61.86 C ANISOU 1230 CD1 LEU A 162 7827 8322 7355 647 122 393 C ATOM 1231 CD2 LEU A 162 -6.785 -6.919 25.009 1.00 63.15 C ANISOU 1231 CD2 LEU A 162 8089 8559 7345 799 133 450 C ATOM 1232 N ALA A 163 -4.490 -2.600 23.956 1.00 64.16 N ANISOU 1232 N ALA A 163 8211 8685 7482 668 -127 135 N ATOM 1233 CA ALA A 163 -3.188 -1.997 24.204 1.00 62.36 C ANISOU 1233 CA ALA A 163 7969 8464 7262 668 -224 65 C ATOM 1234 C ALA A 163 -3.205 -0.790 25.136 1.00 66.03 C ANISOU 1234 C ALA A 163 8483 8953 7654 718 -294 3 C ATOM 1235 O ALA A 163 -2.164 -0.416 25.673 1.00 68.14 O ANISOU 1235 O ALA A 163 8747 9232 7914 743 -385 -53 O ATOM 1236 CB ALA A 163 -2.506 -1.650 22.880 1.00 55.63 C ANISOU 1236 CB ALA A 163 7053 7569 6515 572 -235 27 C ATOM 1237 N ARG A 164 -4.375 -0.195 25.338 1.00 64.22 N ANISOU 1237 N ARG A 164 8298 8729 7374 736 -256 8 N ATOM 1238 CA ARG A 164 -4.500 0.956 26.218 1.00 64.69 C ANISOU 1238 CA ARG A 164 8410 8810 7361 789 -318 -54 C ATOM 1239 C ARG A 164 -3.938 0.675 27.605 1.00 64.68 C ANISOU 1239 C ARG A 164 8452 8859 7264 894 -380 -63 C ATOM 1240 O ARG A 164 -3.116 1.435 28.115 1.00 64.89 O ANISOU 1240 O ARG A 164 8487 8891 7276 919 -483 -142 O ATOM 1241 CB ARG A 164 -5.963 1.371 26.331 1.00 65.56 C ANISOU 1241 CB ARG A 164 8563 8924 7422 808 -250 -28 C ATOM 1242 N HIS A 168 -0.181 4.308 30.473 1.00 97.01 N ANISOU 1242 N HIS A 168 12592 12971 11296 1054 -920 -468 N ATOM 1243 CA HIS A 168 -1.295 5.202 30.760 1.00 95.55 C ANISOU 1243 CA HIS A 168 12468 12794 11044 1084 -897 -491 C ATOM 1244 C HIS A 168 -0.871 6.650 30.586 1.00 93.42 C ANISOU 1244 C HIS A 168 12175 12474 10844 1046 -998 -601 C ATOM 1245 O HIS A 168 -1.706 7.550 30.583 1.00 93.81 O ANISOU 1245 O HIS A 168 12259 12512 10871 1047 -984 -630 O ATOM 1246 CB HIS A 168 -1.830 4.974 32.172 1.00 98.15 C ANISOU 1246 CB HIS A 168 12895 13195 11204 1226 -904 -483 C ATOM 1247 CG HIS A 168 -2.026 3.533 32.522 1.00100.16 C ANISOU 1247 CG HIS A 168 13168 13496 11392 1278 -824 -377 C ATOM 1248 ND1 HIS A 168 -1.205 2.866 33.406 1.00101.46 N ANISOU 1248 ND1 HIS A 168 13353 13702 11494 1362 -889 -376 N ATOM 1249 CD2 HIS A 168 -2.961 2.634 32.127 1.00101.54 C ANISOU 1249 CD2 HIS A 168 13344 13679 11559 1260 -687 -266 C ATOM 1250 CE1 HIS A 168 -1.621 1.619 33.534 1.00103.91 C ANISOU 1250 CE1 HIS A 168 13676 14043 11761 1392 -791 -266 C ATOM 1251 NE2 HIS A 168 -2.682 1.452 32.769 1.00103.67 N ANISOU 1251 NE2 HIS A 168 13631 13991 11767 1331 -668 -199 N ATOM 1252 N ASP A 169 0.433 6.866 30.440 1.00 92.62 N ANISOU 1252 N ASP A 169 12013 12340 10839 1011 -1099 -661 N ATOM 1253 CA ASP A 169 0.963 8.187 30.132 1.00 94.30 C ANISOU 1253 CA ASP A 169 12184 12490 11155 959 -1193 -758 C ATOM 1254 C ASP A 169 0.719 8.463 28.657 1.00 88.99 C ANISOU 1254 C ASP A 169 11444 11759 10608 829 -1108 -718 C ATOM 1255 O ASP A 169 0.477 9.599 28.251 1.00 86.59 O ANISOU 1255 O ASP A 169 11128 11407 10365 783 -1127 -765 O ATOM 1256 CB ASP A 169 2.461 8.260 30.455 1.00 98.32 C ANISOU 1256 CB ASP A 169 12639 12978 11739 964 -1326 -827 C ATOM 1257 CG ASP A 169 2.751 8.062 31.932 1.00100.96 C ANISOU 1257 CG ASP A 169 13044 13371 11945 1101 -1427 -878 C ATOM 1258 OD1 ASP A 169 1.832 7.649 32.672 1.00100.41 O ANISOU 1258 OD1 ASP A 169 13064 13366 11722 1192 -1373 -838 O ATOM 1259 OD2 ASP A 169 3.898 8.324 32.352 1.00104.16 O ANISOU 1259 OD2 ASP A 169 13414 13757 12404 1120 -1560 -956 O ATOM 1260 N THR A 170 0.772 7.398 27.866 1.00 85.84 N ANISOU 1260 N THR A 170 11006 11365 10246 777 -1014 -630 N ATOM 1261 CA THR A 170 0.597 7.501 26.427 1.00 81.48 C ANISOU 1261 CA THR A 170 10393 10763 9802 663 -931 -586 C ATOM 1262 C THR A 170 -0.871 7.279 26.087 1.00 73.38 C ANISOU 1262 C THR A 170 9415 9756 8710 660 -813 -520 C ATOM 1263 O THR A 170 -1.314 7.519 24.962 1.00 71.53 O ANISOU 1263 O THR A 170 9150 9485 8542 578 -743 -489 O ATOM 1264 CB THR A 170 1.491 6.501 25.689 1.00 83.07 C ANISOU 1264 CB THR A 170 10522 10956 10085 609 -899 -536 C ATOM 1265 OG1 THR A 170 1.266 6.591 24.276 1.00 81.75 O ANISOU 1265 OG1 THR A 170 10306 10748 10009 508 -813 -493 O ATOM 1266 CG2 THR A 170 1.215 5.078 26.168 1.00 84.23 C ANISOU 1266 CG2 THR A 170 10704 11160 10139 669 -843 -465 C ATOM 1267 N SER A 171 -1.627 6.822 27.078 1.00 67.36 N ANISOU 1267 N SER A 171 8727 9050 7815 754 -791 -496 N ATOM 1268 CA SER A 171 -3.062 6.670 26.918 1.00 62.32 C ANISOU 1268 CA SER A 171 8135 8428 7115 762 -685 -437 C ATOM 1269 C SER A 171 -3.768 7.910 27.458 1.00 61.53 C ANISOU 1269 C SER A 171 8088 8325 6965 802 -721 -500 C ATOM 1270 O SER A 171 -4.899 8.205 27.079 1.00 60.87 O ANISOU 1270 O SER A 171 8026 8234 6868 784 -648 -471 O ATOM 1271 CB SER A 171 -3.548 5.400 27.618 1.00 58.32 C ANISOU 1271 CB SER A 171 7672 7981 6508 839 -621 -360 C ATOM 1272 OG SER A 171 -4.947 5.255 27.490 1.00 56.24 O ANISOU 1272 OG SER A 171 7444 7728 6197 848 -519 -301 O ATOM 1273 N PHE A 172 -3.088 8.639 28.338 1.00 61.45 N ANISOU 1273 N PHE A 172 8099 8319 6933 857 -840 -590 N ATOM 1274 CA PHE A 172 -3.612 9.902 28.846 1.00 58.28 C ANISOU 1274 CA PHE A 172 7743 7906 6494 895 -892 -665 C ATOM 1275 C PHE A 172 -3.518 11.006 27.796 1.00 54.77 C ANISOU 1275 C PHE A 172 7243 7386 6180 792 -908 -704 C ATOM 1276 O PHE A 172 -4.471 11.751 27.586 1.00 49.32 O ANISOU 1276 O PHE A 172 6579 6679 5482 782 -873 -711 O ATOM 1277 CB PHE A 172 -2.874 10.331 30.119 1.00 55.28 C ANISOU 1277 CB PHE A 172 7402 7550 6052 992 -1027 -760 C ATOM 1278 CG PHE A 172 -3.054 11.782 30.454 1.00 53.25 C ANISOU 1278 CG PHE A 172 7169 7259 5802 1011 -1111 -862 C ATOM 1279 CD1 PHE A 172 -4.262 12.247 30.937 1.00 57.78 C ANISOU 1279 CD1 PHE A 172 7817 7860 6278 1073 -1069 -866 C ATOM 1280 CD2 PHE A 172 -2.023 12.683 30.266 1.00 52.52 C ANISOU 1280 CD2 PHE A 172 7022 7106 5828 966 -1229 -953 C ATOM 1281 CE1 PHE A 172 -4.438 13.583 31.235 1.00 61.08 C ANISOU 1281 CE1 PHE A 172 8257 8244 6706 1092 -1147 -964 C ATOM 1282 CE2 PHE A 172 -2.193 14.024 30.565 1.00 52.77 C ANISOU 1282 CE2 PHE A 172 7073 7098 5878 982 -1310 -1049 C ATOM 1283 CZ PHE A 172 -3.402 14.470 31.051 1.00 58.07 C ANISOU 1283 CZ PHE A 172 7822 7798 6443 1046 -1270 -1057 C ATOM 1284 N ALA A 173 -2.357 11.099 27.150 1.00 56.32 N ANISOU 1284 N ALA A 173 7362 7537 6501 718 -957 -724 N ATOM 1285 CA ALA A 173 -2.095 12.119 26.138 1.00 60.68 C ANISOU 1285 CA ALA A 173 7853 8013 7189 620 -973 -752 C ATOM 1286 C ALA A 173 -2.970 11.919 24.903 1.00 62.33 C ANISOU 1286 C ALA A 173 8045 8205 7431 543 -847 -670 C ATOM 1287 O ALA A 173 -3.399 12.881 24.270 1.00 60.82 O ANISOU 1287 O ALA A 173 7843 7967 7298 491 -836 -685 O ATOM 1288 CB ALA A 173 -0.623 12.117 25.754 1.00 61.02 C ANISOU 1288 CB ALA A 173 7812 8016 7357 565 -1042 -779 C ATOM 1289 N LYS A 174 -3.219 10.662 24.557 1.00 65.85 N ANISOU 1289 N LYS A 174 8489 8688 7843 537 -757 -586 N ATOM 1290 CA LYS A 174 -4.027 10.341 23.389 1.00 64.07 C ANISOU 1290 CA LYS A 174 8248 8449 7647 470 -645 -512 C ATOM 1291 C LYS A 174 -5.497 10.641 23.652 1.00 63.77 C ANISOU 1291 C LYS A 174 8273 8427 7528 507 -591 -496 C ATOM 1292 O LYS A 174 -6.240 11.008 22.741 1.00 66.82 O ANISOU 1292 O LYS A 174 8651 8784 7953 452 -531 -468 O ATOM 1293 CB LYS A 174 -3.852 8.870 23.001 1.00 62.11 C ANISOU 1293 CB LYS A 174 7979 8230 7392 459 -575 -434 C ATOM 1294 N ALA A 175 -5.924 10.470 24.897 1.00 59.90 N ANISOU 1294 N ALA A 175 7847 7987 6925 606 -608 -511 N ATOM 1295 CA ALA A 175 -7.306 10.761 25.252 1.00 54.14 C ANISOU 1295 CA ALA A 175 7177 7276 6118 652 -554 -496 C ATOM 1296 C ALA A 175 -7.495 12.265 25.416 1.00 55.04 C ANISOU 1296 C ALA A 175 7307 7353 6251 654 -619 -578 C ATOM 1297 O ALA A 175 -8.601 12.796 25.286 1.00 52.41 O ANISOU 1297 O ALA A 175 7003 7012 5898 658 -574 -571 O ATOM 1298 CB ALA A 175 -7.689 10.028 26.540 1.00 51.06 C ANISOU 1298 CB ALA A 175 6850 6955 5595 765 -539 -475 C ATOM 1299 N PHE A 176 -6.395 12.953 25.694 1.00 57.88 N ANISOU 1299 N PHE A 176 7645 7686 6662 650 -729 -657 N ATOM 1300 CA PHE A 176 -6.455 14.370 26.040 1.00 58.36 C ANISOU 1300 CA PHE A 176 7723 7709 6743 664 -811 -747 C ATOM 1301 C PHE A 176 -6.053 15.315 24.901 1.00 60.46 C ANISOU 1301 C PHE A 176 7924 7894 7156 558 -831 -766 C ATOM 1302 O PHE A 176 -6.684 16.355 24.691 1.00 62.35 O ANISOU 1302 O PHE A 176 8175 8094 7421 544 -836 -796 O ATOM 1303 CB PHE A 176 -5.588 14.639 27.275 1.00 55.79 C ANISOU 1303 CB PHE A 176 7422 7401 6374 747 -936 -837 C ATOM 1304 CG PHE A 176 -5.506 16.086 27.648 1.00 55.77 C ANISOU 1304 CG PHE A 176 7432 7351 6407 762 -1036 -943 C ATOM 1305 CD1 PHE A 176 -6.565 16.712 28.272 1.00 54.66 C ANISOU 1305 CD1 PHE A 176 7362 7229 6179 832 -1029 -975 C ATOM 1306 CD2 PHE A 176 -4.376 16.825 27.363 1.00 56.30 C ANISOU 1306 CD2 PHE A 176 7435 7352 6603 708 -1137 -1009 C ATOM 1307 CE1 PHE A 176 -6.493 18.045 28.604 1.00 56.64 C ANISOU 1307 CE1 PHE A 176 7622 7431 6467 848 -1125 -1077 C ATOM 1308 CE2 PHE A 176 -4.303 18.156 27.697 1.00 57.13 C ANISOU 1308 CE2 PHE A 176 7546 7405 6754 721 -1234 -1107 C ATOM 1309 CZ PHE A 176 -5.360 18.763 28.318 1.00 58.49 C ANISOU 1309 CZ PHE A 176 7792 7595 6835 792 -1230 -1144 C ATOM 1310 N VAL A 177 -4.996 14.960 24.178 1.00 54.00 N ANISOU 1310 N VAL A 177 7034 7048 6434 488 -840 -746 N ATOM 1311 CA VAL A 177 -4.520 15.789 23.078 1.00 51.32 C ANISOU 1311 CA VAL A 177 6629 6634 6238 391 -850 -751 C ATOM 1312 C VAL A 177 -5.355 15.541 21.824 1.00 52.78 C ANISOU 1312 C VAL A 177 6802 6809 6443 324 -733 -666 C ATOM 1313 O VAL A 177 -5.580 16.450 21.028 1.00 50.03 O ANISOU 1313 O VAL A 177 6431 6406 6173 266 -723 -666 O ATOM 1314 CB VAL A 177 -3.029 15.526 22.776 1.00 42.79 C ANISOU 1314 CB VAL A 177 5472 5528 5259 345 -900 -759 C ATOM 1315 CG1 VAL A 177 -2.544 16.382 21.610 1.00 31.96 C ANISOU 1315 CG1 VAL A 177 4028 4078 4039 247 -897 -752 C ATOM 1316 CG2 VAL A 177 -2.181 15.781 24.001 1.00 49.20 C ANISOU 1316 CG2 VAL A 177 6291 6345 6057 413 -1028 -849 C ATOM 1317 N GLY A 178 -5.808 14.300 21.661 1.00 53.75 N ANISOU 1317 N GLY A 178 6941 6983 6499 336 -649 -594 N ATOM 1318 CA GLY A 178 -6.588 13.892 20.504 1.00 53.92 C ANISOU 1318 CA GLY A 178 6952 6999 6535 281 -545 -517 C ATOM 1319 C GLY A 178 -7.966 14.519 20.382 1.00 53.22 C ANISOU 1319 C GLY A 178 6907 6902 6411 291 -503 -510 C ATOM 1320 O GLY A 178 -8.681 14.703 21.369 1.00 54.67 O ANISOU 1320 O GLY A 178 7146 7114 6511 364 -516 -538 O ATOM 1321 N THR A 179 -8.348 14.837 19.151 1.00 53.80 N ANISOU 1321 N THR A 179 6955 6938 6547 221 -452 -472 N ATOM 1322 CA THR A 179 -9.649 15.443 18.887 1.00 56.98 C ANISOU 1322 CA THR A 179 7393 7328 6931 223 -413 -462 C ATOM 1323 C THR A 179 -10.717 14.415 18.491 1.00 56.06 C ANISOU 1323 C THR A 179 7294 7246 6762 229 -318 -390 C ATOM 1324 O THR A 179 -10.520 13.633 17.558 1.00 59.93 O ANISOU 1324 O THR A 179 7752 7736 7281 183 -269 -338 O ATOM 1325 CB THR A 179 -9.546 16.521 17.787 1.00 55.93 C ANISOU 1325 CB THR A 179 7226 7128 6897 149 -417 -463 C ATOM 1326 OG1 THR A 179 -8.456 17.406 18.080 1.00 59.30 O ANISOU 1326 OG1 THR A 179 7621 7513 7396 135 -504 -523 O ATOM 1327 CG2 THR A 179 -10.830 17.324 17.706 1.00 49.82 C ANISOU 1327 CG2 THR A 179 6489 6336 6105 160 -397 -467 C ATOM 1328 N PRO A 180 -11.856 14.423 19.205 1.00 51.62 N ANISOU 1328 N PRO A 180 6780 6709 6124 289 -293 -390 N ATOM 1329 CA PRO A 180 -12.974 13.483 19.031 1.00 48.43 C ANISOU 1329 CA PRO A 180 6390 6333 5676 306 -208 -326 C ATOM 1330 C PRO A 180 -13.896 13.833 17.861 1.00 37.72 C ANISOU 1330 C PRO A 180 5024 4941 4366 254 -161 -293 C ATOM 1331 O PRO A 180 -15.093 14.050 18.073 1.00 28.96 O ANISOU 1331 O PRO A 180 3941 3834 3227 284 -127 -284 O ATOM 1332 CB PRO A 180 -13.750 13.609 20.357 1.00 52.69 C ANISOU 1332 CB PRO A 180 6984 6909 6127 397 -208 -346 C ATOM 1333 CG PRO A 180 -12.843 14.364 21.285 1.00 54.48 C ANISOU 1333 CG PRO A 180 7228 7137 6336 435 -301 -424 C ATOM 1334 CD PRO A 180 -12.036 15.254 20.402 1.00 54.42 C ANISOU 1334 CD PRO A 180 7177 7070 6429 357 -351 -457 C ATOM 1335 N TYR A 181 -13.347 13.869 16.649 1.00 38.80 N ANISOU 1335 N TYR A 181 5122 5047 4573 182 -156 -275 N ATOM 1336 CA TYR A 181 -14.118 14.192 15.446 1.00 37.09 C ANISOU 1336 CA TYR A 181 4897 4797 4397 135 -117 -244 C ATOM 1337 C TYR A 181 -15.416 13.393 15.314 1.00 31.55 C ANISOU 1337 C TYR A 181 4209 4115 3663 156 -52 -197 C ATOM 1338 O TYR A 181 -16.399 13.884 14.768 1.00 24.10 O ANISOU 1338 O TYR A 181 3274 3148 2736 144 -31 -187 O ATOM 1339 CB TYR A 181 -13.262 13.977 14.195 1.00 37.25 C ANISOU 1339 CB TYR A 181 4877 4798 4479 68 -108 -218 C ATOM 1340 CG TYR A 181 -12.032 14.845 14.125 1.00 42.10 C ANISOU 1340 CG TYR A 181 5465 5381 5150 37 -164 -253 C ATOM 1341 CD1 TYR A 181 -10.811 14.395 14.602 1.00 38.68 C ANISOU 1341 CD1 TYR A 181 5008 4964 4726 41 -196 -270 C ATOM 1342 CD2 TYR A 181 -12.093 16.118 13.571 1.00 45.37 C ANISOU 1342 CD2 TYR A 181 5874 5744 5619 2 -185 -267 C ATOM 1343 CE1 TYR A 181 -9.683 15.195 14.527 1.00 43.68 C ANISOU 1343 CE1 TYR A 181 5607 5562 5428 10 -249 -301 C ATOM 1344 CE2 TYR A 181 -10.974 16.921 13.495 1.00 45.76 C ANISOU 1344 CE2 TYR A 181 5890 5756 5738 -29 -234 -295 C ATOM 1345 CZ TYR A 181 -9.775 16.454 13.969 1.00 49.77 C ANISOU 1345 CZ TYR A 181 6370 6280 6261 -26 -266 -312 C ATOM 1346 OH TYR A 181 -8.669 17.261 13.889 1.00 59.29 O ANISOU 1346 OH TYR A 181 7534 7441 7551 -59 -316 -339 O ATOM 1347 N TYR A 182 -15.408 12.167 15.826 1.00 33.53 N ANISOU 1347 N TYR A 182 4459 4404 3876 189 -22 -169 N ATOM 1348 CA TYR A 182 -16.498 11.212 15.614 1.00 33.34 C ANISOU 1348 CA TYR A 182 4434 4392 3842 202 42 -118 C ATOM 1349 C TYR A 182 -17.445 11.099 16.809 1.00 37.80 C ANISOU 1349 C TYR A 182 5028 4982 4351 274 67 -111 C ATOM 1350 O TYR A 182 -18.201 10.132 16.911 1.00 39.56 O ANISOU 1350 O TYR A 182 5245 5219 4568 295 122 -63 O ATOM 1351 CB TYR A 182 -15.931 9.818 15.308 1.00 25.98 C ANISOU 1351 CB TYR A 182 3474 3478 2918 190 67 -80 C ATOM 1352 CG TYR A 182 -15.294 9.664 13.946 1.00 20.76 C ANISOU 1352 CG TYR A 182 2783 2795 2310 126 65 -72 C ATOM 1353 CD1 TYR A 182 -14.682 10.742 13.310 1.00 27.39 C ANISOU 1353 CD1 TYR A 182 3617 3607 3184 84 30 -100 C ATOM 1354 CD2 TYR A 182 -15.280 8.429 13.302 1.00 14.14 C ANISOU 1354 CD2 TYR A 182 1922 1962 1490 111 100 -35 C ATOM 1355 CE1 TYR A 182 -14.089 10.597 12.053 1.00 27.50 C ANISOU 1355 CE1 TYR A 182 3605 3604 3239 33 38 -85 C ATOM 1356 CE2 TYR A 182 -14.685 8.274 12.057 1.00 15.24 C ANISOU 1356 CE2 TYR A 182 2037 2085 1667 62 101 -30 C ATOM 1357 CZ TYR A 182 -14.095 9.360 11.439 1.00 22.08 C ANISOU 1357 CZ TYR A 182 2902 2930 2558 25 73 -52 C ATOM 1358 OH TYR A 182 -13.509 9.210 10.208 1.00 20.75 O ANISOU 1358 OH TYR A 182 2713 2750 2421 -16 83 -40 O ATOM 1359 N MET A 183 -17.398 12.072 17.713 1.00 36.43 N ANISOU 1359 N MET A 183 4886 4814 4140 314 30 -158 N ATOM 1360 CA MET A 183 -18.200 12.001 18.929 1.00 35.93 C ANISOU 1360 CA MET A 183 4858 4784 4011 394 57 -153 C ATOM 1361 C MET A 183 -19.658 12.366 18.675 1.00 34.81 C ANISOU 1361 C MET A 183 4721 4622 3885 401 102 -133 C ATOM 1362 O MET A 183 -19.964 13.499 18.319 1.00 37.67 O ANISOU 1362 O MET A 183 5091 4952 4272 382 75 -168 O ATOM 1363 CB MET A 183 -17.627 12.912 20.011 1.00 42.00 C ANISOU 1363 CB MET A 183 5663 5567 4727 444 -6 -219 C ATOM 1364 CG MET A 183 -18.292 12.721 21.363 1.00 48.92 C ANISOU 1364 CG MET A 183 6583 6489 5517 542 23 -213 C ATOM 1365 SD MET A 183 -17.889 11.124 22.101 1.00115.21 S ANISOU 1365 SD MET A 183 14978 14939 13858 590 64 -155 S ATOM 1366 CE MET A 183 -16.316 11.506 22.866 1.00 69.36 C ANISOU 1366 CE MET A 183 9190 9153 8009 616 -35 -227 C ATOM 1367 N SER A 184 -20.556 11.406 18.871 1.00 35.88 N ANISOU 1367 N SER A 184 4847 4773 4014 429 171 -74 N ATOM 1368 CA SER A 184 -21.983 11.657 18.691 1.00 30.86 C ANISOU 1368 CA SER A 184 4207 4118 3402 440 217 -51 C ATOM 1369 C SER A 184 -22.451 12.703 19.688 1.00 31.38 C ANISOU 1369 C SER A 184 4315 4195 3414 504 208 -91 C ATOM 1370 O SER A 184 -21.812 12.912 20.715 1.00 38.52 O ANISOU 1370 O SER A 184 5253 5133 4249 558 179 -124 O ATOM 1371 CB SER A 184 -22.787 10.371 18.870 1.00 31.08 C ANISOU 1371 CB SER A 184 4210 4157 3441 465 294 22 C ATOM 1372 OG SER A 184 -22.603 9.845 20.171 1.00 36.10 O ANISOU 1372 OG SER A 184 4871 4841 4005 540 321 42 O ATOM 1373 N PRO A 185 -23.568 13.374 19.380 1.00 32.64 N ANISOU 1373 N PRO A 185 4473 4327 3604 503 228 -91 N ATOM 1374 CA PRO A 185 -24.184 14.344 20.292 1.00 30.44 C ANISOU 1374 CA PRO A 185 4231 4057 3279 570 228 -127 C ATOM 1375 C PRO A 185 -24.566 13.732 21.648 1.00 29.57 C ANISOU 1375 C PRO A 185 4146 4000 3089 665 285 -96 C ATOM 1376 O PRO A 185 -24.322 14.357 22.676 1.00 34.53 O ANISOU 1376 O PRO A 185 4822 4658 3642 733 260 -143 O ATOM 1377 CB PRO A 185 -25.449 14.777 19.539 1.00 28.69 C ANISOU 1377 CB PRO A 185 3987 3793 3121 545 258 -109 C ATOM 1378 CG PRO A 185 -25.168 14.493 18.104 1.00 28.40 C ANISOU 1378 CG PRO A 185 3912 3718 3159 455 237 -94 C ATOM 1379 CD PRO A 185 -24.288 13.281 18.097 1.00 28.71 C ANISOU 1379 CD PRO A 185 3937 3784 3188 441 245 -63 C ATOM 1380 N GLU A 186 -25.152 12.535 21.647 1.00 29.35 N ANISOU 1380 N GLU A 186 4089 3984 3081 674 361 -18 N ATOM 1381 CA GLU A 186 -25.543 11.857 22.890 1.00 34.61 C ANISOU 1381 CA GLU A 186 4774 4699 3677 766 429 29 C ATOM 1382 C GLU A 186 -24.352 11.580 23.790 1.00 32.19 C ANISOU 1382 C GLU A 186 4507 4442 3283 812 392 7 C ATOM 1383 O GLU A 186 -24.415 11.779 25.004 1.00 36.14 O ANISOU 1383 O GLU A 186 5055 4988 3689 906 406 -3 O ATOM 1384 CB GLU A 186 -26.239 10.518 22.606 1.00 33.24 C ANISOU 1384 CB GLU A 186 4549 4517 3562 755 512 123 C ATOM 1385 CG GLU A 186 -27.201 10.534 21.453 1.00 39.34 C ANISOU 1385 CG GLU A 186 5270 5233 4443 691 530 144 C ATOM 1386 CD GLU A 186 -26.504 10.411 20.117 1.00 35.46 C ANISOU 1386 CD GLU A 186 4752 4706 4016 594 469 120 C ATOM 1387 OE1 GLU A 186 -26.023 9.302 19.790 1.00 26.98 O ANISOU 1387 OE1 GLU A 186 3651 3633 2968 566 478 157 O ATOM 1388 OE2 GLU A 186 -26.447 11.428 19.394 1.00 35.04 O ANISOU 1388 OE2 GLU A 186 4705 4621 3986 550 415 68 O ATOM 1389 N GLN A 187 -23.273 11.095 23.187 1.00 32.98 N ANISOU 1389 N GLN A 187 4587 4533 3410 750 346 0 N ATOM 1390 CA GLN A 187 -22.106 10.690 23.956 1.00 41.65 C ANISOU 1390 CA GLN A 187 5713 5674 4438 788 309 -16 C ATOM 1391 C GLN A 187 -21.372 11.908 24.502 1.00 45.55 C ANISOU 1391 C GLN A 187 6254 6178 4876 817 220 -111 C ATOM 1392 O GLN A 187 -20.581 11.800 25.441 1.00 46.74 O ANISOU 1392 O GLN A 187 6440 6370 4948 877 183 -137 O ATOM 1393 CB GLN A 187 -21.169 9.814 23.123 1.00 43.43 C ANISOU 1393 CB GLN A 187 5898 5886 4720 714 286 4 C ATOM 1394 CG GLN A 187 -21.806 8.522 22.623 1.00 45.78 C ANISOU 1394 CG GLN A 187 6148 6170 5077 690 364 92 C ATOM 1395 CD GLN A 187 -22.346 7.643 23.742 1.00 45.51 C ANISOU 1395 CD GLN A 187 6127 6177 4989 777 443 163 C ATOM 1396 OE1 GLN A 187 -21.809 7.624 24.849 1.00 45.98 O ANISOU 1396 OE1 GLN A 187 6231 6285 4954 852 431 153 O ATOM 1397 NE2 GLN A 187 -23.408 6.903 23.452 1.00 43.13 N ANISOU 1397 NE2 GLN A 187 5785 5853 4749 770 523 236 N ATOM 1398 N MET A 188 -21.638 13.063 23.900 1.00 43.96 N ANISOU 1398 N MET A 188 6049 5933 4720 775 181 -163 N ATOM 1399 CA MET A 188 -21.173 14.338 24.435 1.00 48.75 C ANISOU 1399 CA MET A 188 6697 6537 5288 807 100 -256 C ATOM 1400 C MET A 188 -21.859 14.678 25.761 1.00 51.72 C ANISOU 1400 C MET A 188 7131 6959 5564 924 128 -271 C ATOM 1401 O MET A 188 -21.243 15.260 26.653 1.00 54.02 O ANISOU 1401 O MET A 188 7468 7274 5783 987 62 -341 O ATOM 1402 CB MET A 188 -21.431 15.458 23.429 1.00 50.13 C ANISOU 1402 CB MET A 188 6851 6649 5545 735 63 -297 C ATOM 1403 CG MET A 188 -20.231 15.839 22.587 1.00 51.30 C ANISOU 1403 CG MET A 188 6973 6759 5759 651 -15 -337 C ATOM 1404 SD MET A 188 -20.710 16.896 21.207 1.00 70.28 S ANISOU 1404 SD MET A 188 9346 9089 8267 563 -31 -350 S ATOM 1405 CE MET A 188 -22.232 17.605 21.839 1.00 49.35 C ANISOU 1405 CE MET A 188 6728 6440 5581 634 12 -359 C ATOM 1406 N ASN A 189 -23.133 14.313 25.883 1.00 53.51 N ANISOU 1406 N ASN A 189 7350 7194 5787 957 224 -206 N ATOM 1407 CA ASN A 189 -23.939 14.695 27.035 1.00 56.07 C ANISOU 1407 CA ASN A 189 7725 7558 6023 1070 266 -213 C ATOM 1408 C ASN A 189 -24.228 13.502 27.945 1.00 63.96 C ANISOU 1408 C ASN A 189 8738 8617 6947 1152 354 -129 C ATOM 1409 O ASN A 189 -25.353 12.997 28.001 1.00 70.81 O ANISOU 1409 O ASN A 189 9585 9488 7832 1176 456 -51 O ATOM 1410 CB ASN A 189 -25.248 15.346 26.583 1.00 55.03 C ANISOU 1410 CB ASN A 189 7574 7388 5945 1057 313 -203 C ATOM 1411 CG ASN A 189 -25.107 16.117 25.278 1.00 60.78 C ANISOU 1411 CG ASN A 189 8267 8047 6782 948 253 -244 C ATOM 1412 OD1 ASN A 189 -24.012 16.530 24.891 1.00 67.06 O ANISOU 1412 OD1 ASN A 189 9061 8821 7598 896 165 -300 O ATOM 1413 ND2 ASN A 189 -26.226 16.310 24.590 1.00 54.30 N ANISOU 1413 ND2 ASN A 189 7412 7188 6031 915 302 -211 N ATOM 1414 N SER A 192 -23.619 6.145 27.946 1.00 69.02 N ANISOU 1414 N SER A 192 9214 9321 7690 1126 664 346 N ATOM 1415 CA SER A 192 -23.761 4.700 28.046 1.00 71.43 C ANISOU 1415 CA SER A 192 9481 9626 8033 1133 740 451 C ATOM 1416 C SER A 192 -23.709 4.037 26.680 1.00 62.75 C ANISOU 1416 C SER A 192 8307 8463 7073 1017 730 468 C ATOM 1417 O SER A 192 -23.616 4.706 25.650 1.00 55.56 O ANISOU 1417 O SER A 192 7377 7512 6223 935 671 403 O ATOM 1418 CB SER A 192 -25.100 4.372 28.682 1.00 78.54 C ANISOU 1418 CB SER A 192 10372 10535 8933 1204 862 543 C ATOM 1419 OG SER A 192 -26.062 5.296 28.199 1.00 80.68 O ANISOU 1419 OG SER A 192 10629 10773 9253 1177 871 510 O ATOM 1420 N TYR A 193 -23.769 2.708 26.696 1.00 59.56 N ANISOU 1420 N TYR A 193 7864 8050 6717 1017 789 556 N ATOM 1421 CA TYR A 193 -23.980 1.899 25.498 1.00 55.35 C ANISOU 1421 CA TYR A 193 7255 7453 6321 924 798 586 C ATOM 1422 C TYR A 193 -25.160 2.456 24.689 1.00 49.65 C ANISOU 1422 C TYR A 193 6495 6680 5689 876 818 576 C ATOM 1423 O TYR A 193 -26.218 2.770 25.238 1.00 51.95 O ANISOU 1423 O TYR A 193 6790 6977 5972 929 886 612 O ATOM 1424 CB TYR A 193 -24.236 0.439 25.918 1.00 54.24 C ANISOU 1424 CB TYR A 193 7078 7308 6222 956 882 698 C ATOM 1425 CG TYR A 193 -24.269 -0.605 24.808 1.00 53.84 C ANISOU 1425 CG TYR A 193 6952 7193 6310 871 883 728 C ATOM 1426 CD1 TYR A 193 -25.452 -1.271 24.490 1.00 55.88 C ANISOU 1426 CD1 TYR A 193 7147 7400 6687 856 960 802 C ATOM 1427 CD2 TYR A 193 -23.116 -0.954 24.109 1.00 54.79 C ANISOU 1427 CD2 TYR A 193 7064 7304 6448 811 808 682 C ATOM 1428 CE1 TYR A 193 -25.490 -2.232 23.490 1.00 56.24 C ANISOU 1428 CE1 TYR A 193 7124 7383 6861 784 952 820 C ATOM 1429 CE2 TYR A 193 -23.147 -1.917 23.108 1.00 56.77 C ANISOU 1429 CE2 TYR A 193 7252 7499 6821 742 808 704 C ATOM 1430 CZ TYR A 193 -24.337 -2.552 22.807 1.00 57.88 C ANISOU 1430 CZ TYR A 193 7332 7586 7074 730 876 770 C ATOM 1431 OH TYR A 193 -24.397 -3.509 21.817 1.00 57.55 O ANISOU 1431 OH TYR A 193 7227 7484 7157 666 867 783 O ATOM 1432 N ASN A 194 -24.963 2.599 23.386 1.00 40.13 N ANISOU 1432 N ASN A 194 5255 5427 4567 780 760 527 N ATOM 1433 CA ASN A 194 -26.010 3.076 22.490 1.00 33.77 C ANISOU 1433 CA ASN A 194 4412 4570 3850 730 766 514 C ATOM 1434 C ASN A 194 -25.572 2.752 21.086 1.00 26.44 C ANISOU 1434 C ASN A 194 3444 3594 3008 634 708 481 C ATOM 1435 O ASN A 194 -24.725 3.436 20.530 1.00 30.15 O ANISOU 1435 O ASN A 194 3937 4068 3449 592 631 408 O ATOM 1436 CB ASN A 194 -26.224 4.589 22.648 1.00 33.74 C ANISOU 1436 CB ASN A 194 4454 4581 3786 746 731 444 C ATOM 1437 CG ASN A 194 -27.363 5.128 21.780 1.00 34.88 C ANISOU 1437 CG ASN A 194 4561 4673 4019 702 738 433 C ATOM 1438 OD1 ASN A 194 -27.848 4.459 20.872 1.00 38.21 O ANISOU 1438 OD1 ASN A 194 4924 5044 4549 648 749 461 O ATOM 1439 ND2 ASN A 194 -27.772 6.357 22.050 1.00 30.75 N ANISOU 1439 ND2 ASN A 194 4073 4159 3452 728 725 387 N ATOM 1440 N GLU A 195 -26.145 1.695 20.528 1.00 21.14 N ANISOU 1440 N GLU A 195 2710 2877 2444 604 745 535 N ATOM 1441 CA GLU A 195 -25.750 1.201 19.226 1.00 19.87 C ANISOU 1441 CA GLU A 195 2514 2674 2363 525 694 507 C ATOM 1442 C GLU A 195 -25.902 2.263 18.144 1.00 17.51 C ANISOU 1442 C GLU A 195 2221 2350 2082 468 632 433 C ATOM 1443 O GLU A 195 -25.130 2.293 17.193 1.00 15.52 O ANISOU 1443 O GLU A 195 1969 2087 1840 413 572 387 O ATOM 1444 CB GLU A 195 -26.547 -0.058 18.889 1.00 23.85 C ANISOU 1444 CB GLU A 195 2946 3125 2989 512 744 574 C ATOM 1445 CG GLU A 195 -26.281 -1.216 19.855 1.00 28.82 C ANISOU 1445 CG GLU A 195 3566 3774 3612 563 805 654 C ATOM 1446 CD GLU A 195 -27.239 -2.375 19.663 1.00 37.75 C ANISOU 1446 CD GLU A 195 4620 4844 4878 557 864 730 C ATOM 1447 OE1 GLU A 195 -28.226 -2.221 18.916 1.00 41.19 O ANISOU 1447 OE1 GLU A 195 5013 5228 5410 523 862 721 O ATOM 1448 OE2 GLU A 195 -27.007 -3.444 20.260 1.00 42.95 O ANISOU 1448 OE2 GLU A 195 5261 5505 5555 588 910 799 O ATOM 1449 N LYS A 196 -26.884 3.146 18.298 1.00 15.82 N ANISOU 1449 N LYS A 196 2013 2128 1869 486 650 427 N ATOM 1450 CA LYS A 196 -27.089 4.236 17.344 1.00 18.40 C ANISOU 1450 CA LYS A 196 2350 2432 2210 439 594 363 C ATOM 1451 C LYS A 196 -25.935 5.238 17.361 1.00 20.06 C ANISOU 1451 C LYS A 196 2616 2676 2332 428 529 295 C ATOM 1452 O LYS A 196 -25.781 6.030 16.434 1.00 20.42 O ANISOU 1452 O LYS A 196 2669 2701 2389 380 476 243 O ATOM 1453 CB LYS A 196 -28.410 4.968 17.621 1.00 20.14 C ANISOU 1453 CB LYS A 196 2564 2637 2453 468 631 373 C ATOM 1454 CG LYS A 196 -29.634 4.186 17.204 1.00 14.69 C ANISOU 1454 CG LYS A 196 1804 1893 1882 458 675 425 C ATOM 1455 CD LYS A 196 -29.542 3.822 15.741 1.00 19.46 C ANISOU 1455 CD LYS A 196 2376 2451 2566 386 616 394 C ATOM 1456 CE LYS A 196 -30.753 3.021 15.285 1.00 22.10 C ANISOU 1456 CE LYS A 196 2638 2726 3033 376 646 437 C ATOM 1457 NZ LYS A 196 -31.934 3.869 15.090 1.00 21.89 N ANISOU 1457 NZ LYS A 196 2597 2671 3048 381 651 428 N ATOM 1458 N SER A 197 -25.135 5.214 18.421 1.00 22.93 N ANISOU 1458 N SER A 197 3016 3088 2610 475 533 296 N ATOM 1459 CA SER A 197 -23.957 6.071 18.477 1.00 18.59 C ANISOU 1459 CA SER A 197 2510 2564 1990 464 466 230 C ATOM 1460 C SER A 197 -22.896 5.525 17.534 1.00 19.36 C ANISOU 1460 C SER A 197 2588 2650 2117 403 422 213 C ATOM 1461 O SER A 197 -22.075 6.266 17.011 1.00 18.47 O ANISOU 1461 O SER A 197 2492 2536 1989 365 363 160 O ATOM 1462 CB SER A 197 -23.399 6.171 19.895 1.00 22.86 C ANISOU 1462 CB SER A 197 3095 3159 2432 538 473 230 C ATOM 1463 OG SER A 197 -24.339 6.766 20.765 1.00 26.56 O ANISOU 1463 OG SER A 197 3586 3642 2861 602 514 240 O ATOM 1464 N ASP A 198 -22.919 4.221 17.302 1.00 19.16 N ANISOU 1464 N ASP A 198 2525 2613 2141 394 452 261 N ATOM 1465 CA ASP A 198 -21.951 3.638 16.392 1.00 17.29 C ANISOU 1465 CA ASP A 198 2271 2367 1933 342 415 244 C ATOM 1466 C ASP A 198 -22.311 3.948 14.937 1.00 17.59 C ANISOU 1466 C ASP A 198 2289 2362 2034 280 387 216 C ATOM 1467 O ASP A 198 -21.430 4.033 14.085 1.00 16.16 O ANISOU 1467 O ASP A 198 2108 2176 1855 237 345 183 O ATOM 1468 CB ASP A 198 -21.837 2.124 16.612 1.00 18.65 C ANISOU 1468 CB ASP A 198 2410 2536 2141 355 453 300 C ATOM 1469 CG ASP A 198 -21.125 1.754 17.914 1.00 26.56 C ANISOU 1469 CG ASP A 198 3436 3586 3070 413 469 325 C ATOM 1470 OD1 ASP A 198 -20.481 2.615 18.547 1.00 26.80 O ANISOU 1470 OD1 ASP A 198 3509 3652 3021 438 435 287 O ATOM 1471 OD2 ASP A 198 -21.208 0.571 18.294 1.00 28.65 O ANISOU 1471 OD2 ASP A 198 3676 3849 3361 437 511 383 O ATOM 1472 N ILE A 199 -23.608 4.102 14.665 1.00 11.15 N ANISOU 1472 N ILE A 199 1455 1514 1268 281 411 232 N ATOM 1473 CA ILE A 199 -24.098 4.498 13.342 1.00 13.12 C ANISOU 1473 CA ILE A 199 1692 1724 1570 233 379 204 C ATOM 1474 C ILE A 199 -23.611 5.914 12.995 1.00 12.71 C ANISOU 1474 C ILE A 199 1678 1680 1471 211 332 151 C ATOM 1475 O ILE A 199 -23.230 6.198 11.856 1.00 15.82 O ANISOU 1475 O ILE A 199 2074 2058 1880 167 294 123 O ATOM 1476 CB ILE A 199 -25.660 4.417 13.236 1.00 9.09 C ANISOU 1476 CB ILE A 199 1150 1176 1129 245 411 231 C ATOM 1477 CG1 ILE A 199 -26.160 3.010 13.575 1.00 13.44 C ANISOU 1477 CG1 ILE A 199 1653 1709 1744 264 460 289 C ATOM 1478 CG2 ILE A 199 -26.127 4.804 11.852 1.00 6.92 C ANISOU 1478 CG2 ILE A 199 865 862 902 201 369 199 C ATOM 1479 CD1 ILE A 199 -25.573 1.921 12.672 1.00 11.83 C ANISOU 1479 CD1 ILE A 199 1423 1486 1587 228 435 285 C ATOM 1480 N TRP A 200 -23.615 6.793 13.996 1.00 11.89 N ANISOU 1480 N TRP A 200 1606 1600 1312 247 336 139 N ATOM 1481 CA TRP A 200 -23.102 8.155 13.835 1.00 9.87 C ANISOU 1481 CA TRP A 200 1384 1346 1020 230 289 89 C ATOM 1482 C TRP A 200 -21.606 8.143 13.509 1.00 16.71 C ANISOU 1482 C TRP A 200 2258 2228 1864 199 250 63 C ATOM 1483 O TRP A 200 -21.179 8.772 12.542 1.00 20.58 O ANISOU 1483 O TRP A 200 2751 2700 2368 155 215 37 O ATOM 1484 CB TRP A 200 -23.389 9.004 15.081 1.00 9.45 C ANISOU 1484 CB TRP A 200 1363 1314 912 284 298 75 C ATOM 1485 CG TRP A 200 -22.717 10.345 15.063 1.00 12.09 C ANISOU 1485 CG TRP A 200 1729 1648 1215 270 243 20 C ATOM 1486 CD1 TRP A 200 -21.391 10.597 15.261 1.00 18.24 C ANISOU 1486 CD1 TRP A 200 2523 2445 1964 260 201 -12 C ATOM 1487 CD2 TRP A 200 -23.336 11.619 14.838 1.00 11.85 C ANISOU 1487 CD2 TRP A 200 1715 1592 1195 266 223 -10 C ATOM 1488 NE1 TRP A 200 -21.144 11.948 15.171 1.00 24.31 N ANISOU 1488 NE1 TRP A 200 3312 3196 2727 247 156 -59 N ATOM 1489 CE2 TRP A 200 -22.322 12.596 14.913 1.00 20.61 C ANISOU 1489 CE2 TRP A 200 2848 2702 2282 251 169 -59 C ATOM 1490 CE3 TRP A 200 -24.649 12.031 14.585 1.00 17.87 C ANISOU 1490 CE3 TRP A 200 2471 2327 1990 273 244 0 C ATOM 1491 CZ2 TRP A 200 -22.580 13.952 14.742 1.00 23.49 C ANISOU 1491 CZ2 TRP A 200 3230 3038 2655 243 137 -96 C ATOM 1492 CZ3 TRP A 200 -24.899 13.386 14.407 1.00 17.69 C ANISOU 1492 CZ3 TRP A 200 2470 2281 1971 267 212 -38 C ATOM 1493 CH2 TRP A 200 -23.872 14.326 14.493 1.00 19.81 C ANISOU 1493 CH2 TRP A 200 2762 2548 2216 252 159 -85 C ATOM 1494 N SER A 201 -20.824 7.415 14.308 1.00 11.21 N ANISOU 1494 N SER A 201 1562 1564 1135 224 258 75 N ATOM 1495 CA SER A 201 -19.402 7.209 14.017 1.00 11.40 C ANISOU 1495 CA SER A 201 1582 1601 1148 197 225 57 C ATOM 1496 C SER A 201 -19.169 6.658 12.610 1.00 11.37 C ANISOU 1496 C SER A 201 1552 1574 1193 145 221 62 C ATOM 1497 O SER A 201 -18.279 7.123 11.902 1.00 19.31 O ANISOU 1497 O SER A 201 2559 2575 2202 109 190 37 O ATOM 1498 CB SER A 201 -18.753 6.291 15.052 1.00 15.19 C ANISOU 1498 CB SER A 201 2062 2117 1594 237 238 77 C ATOM 1499 OG SER A 201 -18.926 6.783 16.364 1.00 29.43 O ANISOU 1499 OG SER A 201 3896 3947 3338 295 240 70 O ATOM 1500 N LEU A 202 -19.962 5.668 12.202 1.00 10.78 N ANISOU 1500 N LEU A 202 1452 1482 1160 146 251 94 N ATOM 1501 CA LEU A 202 -19.833 5.119 10.854 1.00 9.22 C ANISOU 1501 CA LEU A 202 1235 1263 1005 107 242 92 C ATOM 1502 C LEU A 202 -20.129 6.202 9.828 1.00 13.51 C ANISOU 1502 C LEU A 202 1794 1785 1556 76 216 66 C ATOM 1503 O LEU A 202 -19.430 6.323 8.825 1.00 21.47 O ANISOU 1503 O LEU A 202 2803 2789 2566 44 197 51 O ATOM 1504 CB LEU A 202 -20.784 3.946 10.648 1.00 12.68 C ANISOU 1504 CB LEU A 202 1642 1679 1498 117 271 123 C ATOM 1505 CG LEU A 202 -20.770 3.240 9.288 1.00 16.55 C ANISOU 1505 CG LEU A 202 2112 2144 2032 87 256 115 C ATOM 1506 CD1 LEU A 202 -19.370 2.747 8.904 1.00 9.02 C ANISOU 1506 CD1 LEU A 202 1156 1210 1060 71 244 103 C ATOM 1507 CD2 LEU A 202 -21.770 2.089 9.301 1.00 13.09 C ANISOU 1507 CD2 LEU A 202 1637 1676 1661 102 280 144 C ATOM 1508 N GLY A 203 -21.171 6.990 10.089 1.00 9.88 N ANISOU 1508 N GLY A 203 1345 1310 1100 89 219 64 N ATOM 1509 CA GLY A 203 -21.537 8.079 9.203 1.00 10.23 C ANISOU 1509 CA GLY A 203 1405 1330 1151 64 194 44 C ATOM 1510 C GLY A 203 -20.385 9.046 9.018 1.00 11.11 C ANISOU 1510 C GLY A 203 1536 1450 1234 40 166 19 C ATOM 1511 O GLY A 203 -20.080 9.441 7.898 1.00 16.52 O ANISOU 1511 O GLY A 203 2227 2122 1928 10 150 13 O ATOM 1512 N CYS A 204 -19.751 9.419 10.129 1.00 9.36 N ANISOU 1512 N CYS A 204 1326 1250 982 58 160 7 N ATOM 1513 CA CYS A 204 -18.566 10.281 10.128 1.00 8.63 C ANISOU 1513 CA CYS A 204 1241 1160 876 37 128 -18 C ATOM 1514 C CYS A 204 -17.416 9.653 9.356 1.00 9.78 C ANISOU 1514 C CYS A 204 1369 1315 1033 7 127 -12 C ATOM 1515 O CYS A 204 -16.707 10.331 8.616 1.00 11.48 O ANISOU 1515 O CYS A 204 1584 1518 1261 -25 112 -20 O ATOM 1516 CB CYS A 204 -18.082 10.552 11.559 1.00 9.38 C ANISOU 1516 CB CYS A 204 1348 1279 937 71 115 -38 C ATOM 1517 SG CYS A 204 -19.124 11.622 12.540 1.00 15.53 S ANISOU 1517 SG CYS A 204 2156 2050 1694 112 109 -59 S ATOM 1518 N LEU A 205 -17.205 8.358 9.560 1.00 10.13 N ANISOU 1518 N LEU A 205 1395 1378 1074 20 147 5 N ATOM 1519 CA LEU A 205 -16.153 7.657 8.831 1.00 13.49 C ANISOU 1519 CA LEU A 205 1802 1813 1510 -2 150 10 C ATOM 1520 C LEU A 205 -16.418 7.680 7.324 1.00 10.35 C ANISOU 1520 C LEU A 205 1405 1396 1131 -29 155 16 C ATOM 1521 O LEU A 205 -15.518 7.973 6.537 1.00 17.52 O ANISOU 1521 O LEU A 205 2311 2305 2043 -54 152 14 O ATOM 1522 CB LEU A 205 -16.001 6.215 9.331 1.00 17.06 C ANISOU 1522 CB LEU A 205 2235 2285 1963 20 170 28 C ATOM 1523 CG LEU A 205 -14.956 5.281 8.713 1.00 21.40 C ANISOU 1523 CG LEU A 205 2762 2845 2524 6 176 33 C ATOM 1524 CD1 LEU A 205 -14.593 4.193 9.724 1.00 24.42 C ANISOU 1524 CD1 LEU A 205 3129 3249 2901 35 186 48 C ATOM 1525 CD2 LEU A 205 -15.445 4.644 7.427 1.00 24.44 C ANISOU 1525 CD2 LEU A 205 3141 3213 2932 -7 188 39 C ATOM 1526 N LEU A 206 -17.642 7.365 6.912 1.00 9.87 N ANISOU 1526 N LEU A 206 1348 1319 1082 -19 163 24 N ATOM 1527 CA LEU A 206 -17.914 7.241 5.480 1.00 10.80 C ANISOU 1527 CA LEU A 206 1471 1422 1211 -34 160 24 C ATOM 1528 C LEU A 206 -17.904 8.604 4.815 1.00 9.16 C ANISOU 1528 C LEU A 206 1285 1199 995 -53 146 20 C ATOM 1529 O LEU A 206 -17.523 8.736 3.650 1.00 8.34 O ANISOU 1529 O LEU A 206 1191 1094 885 -67 147 24 O ATOM 1530 CB LEU A 206 -19.249 6.551 5.235 1.00 8.16 C ANISOU 1530 CB LEU A 206 1130 1068 902 -17 162 29 C ATOM 1531 CG LEU A 206 -19.353 5.123 5.756 1.00 11.94 C ANISOU 1531 CG LEU A 206 1581 1551 1405 2 179 40 C ATOM 1532 CD1 LEU A 206 -20.806 4.659 5.735 1.00 9.71 C ANISOU 1532 CD1 LEU A 206 1284 1240 1166 18 180 47 C ATOM 1533 CD2 LEU A 206 -18.485 4.211 4.904 1.00 15.08 C ANISOU 1533 CD2 LEU A 206 1968 1958 1803 -6 178 33 C ATOM 1534 N TYR A 207 -18.323 9.615 5.572 1.00 10.67 N ANISOU 1534 N TYR A 207 1488 1379 1186 -50 135 13 N ATOM 1535 CA TYR A 207 -18.315 10.990 5.086 1.00 17.59 C ANISOU 1535 CA TYR A 207 2383 2235 2064 -68 120 11 C ATOM 1536 C TYR A 207 -16.876 11.383 4.774 1.00 16.06 C ANISOU 1536 C TYR A 207 2182 2048 1871 -94 121 14 C ATOM 1537 O TYR A 207 -16.591 11.990 3.743 1.00 18.43 O ANISOU 1537 O TYR A 207 2491 2335 2175 -112 124 28 O ATOM 1538 CB TYR A 207 -18.914 11.954 6.128 1.00 11.16 C ANISOU 1538 CB TYR A 207 1579 1407 1252 -55 106 -4 C ATOM 1539 CG TYR A 207 -18.955 13.417 5.688 1.00 13.50 C ANISOU 1539 CG TYR A 207 1894 1675 1562 -74 87 -7 C ATOM 1540 CD1 TYR A 207 -17.810 14.212 5.714 1.00 17.60 C ANISOU 1540 CD1 TYR A 207 2408 2186 2092 -97 76 -11 C ATOM 1541 CD2 TYR A 207 -20.142 13.999 5.250 1.00 11.52 C ANISOU 1541 CD2 TYR A 207 1660 1399 1320 -67 80 -4 C ATOM 1542 CE1 TYR A 207 -17.842 15.549 5.314 1.00 12.78 C ANISOU 1542 CE1 TYR A 207 1809 1542 1505 -115 60 -9 C ATOM 1543 CE2 TYR A 207 -20.195 15.332 4.851 1.00 8.33 C ANISOU 1543 CE2 TYR A 207 1271 964 931 -81 63 -4 C ATOM 1544 CZ TYR A 207 -19.035 16.105 4.883 1.00 10.97 C ANISOU 1544 CZ TYR A 207 1600 1289 1278 -106 54 -5 C ATOM 1545 OH TYR A 207 -19.056 17.421 4.477 1.00 8.85 O ANISOU 1545 OH TYR A 207 1342 983 1036 -122 39 1 O ATOM 1546 N GLU A 208 -15.964 11.021 5.669 1.00 16.29 N ANISOU 1546 N GLU A 208 2193 2096 1900 -92 120 5 N ATOM 1547 CA GLU A 208 -14.564 11.402 5.507 1.00 13.32 C ANISOU 1547 CA GLU A 208 1800 1723 1540 -116 118 7 C ATOM 1548 C GLU A 208 -13.950 10.637 4.338 1.00 12.59 C ANISOU 1548 C GLU A 208 1697 1643 1444 -126 146 28 C ATOM 1549 O GLU A 208 -13.105 11.152 3.617 1.00 13.03 O ANISOU 1549 O GLU A 208 1745 1693 1515 -148 157 43 O ATOM 1550 CB GLU A 208 -13.776 11.202 6.813 1.00 14.41 C ANISOU 1550 CB GLU A 208 1919 1876 1679 -106 101 -13 C ATOM 1551 CG GLU A 208 -12.367 11.809 6.793 1.00 20.92 C ANISOU 1551 CG GLU A 208 2719 2693 2537 -133 88 -17 C ATOM 1552 CD GLU A 208 -11.601 11.628 8.092 1.00 24.15 C ANISOU 1552 CD GLU A 208 3111 3117 2948 -118 58 -44 C ATOM 1553 OE1 GLU A 208 -12.178 11.136 9.086 1.00 24.41 O ANISOU 1553 OE1 GLU A 208 3159 3169 2948 -83 50 -57 O ATOM 1554 OE2 GLU A 208 -10.405 11.977 8.119 1.00 28.73 O ANISOU 1554 OE2 GLU A 208 3662 3689 3566 -138 43 -51 O ATOM 1555 N LEU A 209 -14.415 9.414 4.133 1.00 14.49 N ANISOU 1555 N LEU A 209 1937 1899 1668 -107 158 29 N ATOM 1556 CA LEU A 209 -13.997 8.619 2.989 1.00 13.75 C ANISOU 1556 CA LEU A 209 1841 1819 1565 -107 180 40 C ATOM 1557 C LEU A 209 -14.451 9.275 1.683 1.00 21.85 C ANISOU 1557 C LEU A 209 2893 2830 2578 -111 185 54 C ATOM 1558 O LEU A 209 -13.808 9.120 0.650 1.00 22.22 O ANISOU 1558 O LEU A 209 2942 2887 2611 -112 207 69 O ATOM 1559 CB LEU A 209 -14.601 7.228 3.109 1.00 18.98 C ANISOU 1559 CB LEU A 209 2497 2490 2223 -83 182 32 C ATOM 1560 CG LEU A 209 -13.822 6.018 2.633 1.00 20.12 C ANISOU 1560 CG LEU A 209 2623 2654 2366 -76 200 33 C ATOM 1561 CD1 LEU A 209 -12.434 6.030 3.225 1.00 20.80 C ANISOU 1561 CD1 LEU A 209 2683 2757 2462 -88 208 36 C ATOM 1562 CD2 LEU A 209 -14.573 4.779 3.065 1.00 17.17 C ANISOU 1562 CD2 LEU A 209 2240 2279 2005 -53 195 25 C ATOM 1563 N CYS A 210 -15.567 9.999 1.730 1.00 20.34 N ANISOU 1563 N CYS A 210 2723 2617 2386 -107 167 51 N ATOM 1564 CA CYS A 210 -16.087 10.681 0.547 1.00 12.88 C ANISOU 1564 CA CYS A 210 1808 1658 1427 -106 166 66 C ATOM 1565 C CYS A 210 -15.471 12.073 0.333 1.00 15.47 C ANISOU 1565 C CYS A 210 2140 1968 1769 -130 172 88 C ATOM 1566 O CYS A 210 -14.976 12.364 -0.756 1.00 9.03 O ANISOU 1566 O CYS A 210 1336 1156 941 -132 194 116 O ATOM 1567 CB CYS A 210 -17.611 10.805 0.624 1.00 6.22 C ANISOU 1567 CB CYS A 210 982 794 586 -89 140 53 C ATOM 1568 SG CYS A 210 -18.514 9.250 0.530 1.00 12.23 S ANISOU 1568 SG CYS A 210 1735 1562 1350 -62 130 33 S ATOM 1569 N ALA A 211 -15.516 12.920 1.367 1.00 17.78 N ANISOU 1569 N ALA A 211 2424 2241 2090 -143 153 77 N ATOM 1570 CA ALA A 211 -15.075 14.314 1.269 1.00 17.13 C ANISOU 1570 CA ALA A 211 2341 2129 2037 -166 151 94 C ATOM 1571 C ALA A 211 -13.594 14.477 1.573 1.00 18.05 C ANISOU 1571 C ALA A 211 2423 2248 2188 -190 163 101 C ATOM 1572 O ALA A 211 -13.013 15.545 1.349 1.00 21.50 O ANISOU 1572 O ALA A 211 2849 2656 2665 -213 166 122 O ATOM 1573 CB ALA A 211 -15.888 15.184 2.211 1.00 13.72 C ANISOU 1573 CB ALA A 211 1918 1671 1625 -164 118 71 C ATOM 1574 N LEU A 212 -12.987 13.406 2.073 1.00 21.95 N ANISOU 1574 N LEU A 212 2894 2771 2675 -184 168 86 N ATOM 1575 CA LEU A 212 -11.583 13.422 2.459 1.00 18.81 C ANISOU 1575 CA LEU A 212 2457 2377 2315 -203 173 88 C ATOM 1576 C LEU A 212 -11.319 14.371 3.622 1.00 19.46 C ANISOU 1576 C LEU A 212 2523 2431 2440 -216 133 61 C ATOM 1577 O LEU A 212 -10.183 14.768 3.865 1.00 19.25 O ANISOU 1577 O LEU A 212 2460 2391 2462 -237 127 62 O ATOM 1578 CB LEU A 212 -10.694 13.765 1.268 1.00 13.77 C ANISOU 1578 CB LEU A 212 1806 1733 1694 -221 214 131 C ATOM 1579 CG LEU A 212 -10.706 12.721 0.160 1.00 10.59 C ANISOU 1579 CG LEU A 212 1418 1362 1242 -199 253 150 C ATOM 1580 CD1 LEU A 212 -9.899 13.169 -1.064 1.00 20.96 C ANISOU 1580 CD1 LEU A 212 2726 2674 2564 -207 302 201 C ATOM 1581 CD2 LEU A 212 -10.191 11.402 0.688 1.00 9.86 C ANISOU 1581 CD2 LEU A 212 1302 1302 1141 -188 254 127 C ATOM 1582 N MET A 213 -12.380 14.749 4.326 1.00 22.26 N ANISOU 1582 N MET A 213 2903 2776 2780 -201 104 35 N ATOM 1583 CA MET A 213 -12.259 15.490 5.574 1.00 23.18 C ANISOU 1583 CA MET A 213 3012 2874 2922 -199 59 -2 C ATOM 1584 C MET A 213 -13.455 15.081 6.428 1.00 23.61 C ANISOU 1584 C MET A 213 3095 2945 2931 -162 46 -28 C ATOM 1585 O MET A 213 -14.473 14.648 5.890 1.00 24.99 O ANISOU 1585 O MET A 213 3292 3127 3076 -150 66 -13 O ATOM 1586 CB MET A 213 -12.248 16.997 5.316 1.00 25.79 C ANISOU 1586 CB MET A 213 3343 3154 3303 -222 42 3 C ATOM 1587 CG MET A 213 -13.498 17.520 4.637 1.00 36.91 C ANISOU 1587 CG MET A 213 4787 4544 4692 -215 51 20 C ATOM 1588 SD MET A 213 -13.448 19.284 4.245 1.00 83.62 S ANISOU 1588 SD MET A 213 10702 10396 10676 -242 34 34 S ATOM 1589 CE MET A 213 -12.388 19.292 2.803 1.00 64.92 C ANISOU 1589 CE MET A 213 8309 8022 8335 -272 86 100 C ATOM 1590 N PRO A 214 -13.336 15.194 7.757 1.00 19.50 N ANISOU 1590 N PRO A 214 2574 2431 2406 -142 12 -67 N ATOM 1591 CA PRO A 214 -14.453 14.837 8.638 1.00 14.10 C ANISOU 1591 CA PRO A 214 1916 1765 1678 -101 8 -84 C ATOM 1592 C PRO A 214 -15.590 15.839 8.453 1.00 18.77 C ANISOU 1592 C PRO A 214 2533 2325 2274 -97 1 -88 C ATOM 1593 O PRO A 214 -15.321 16.960 8.032 1.00 20.13 O ANISOU 1593 O PRO A 214 2702 2459 2486 -122 -16 -90 O ATOM 1594 CB PRO A 214 -13.850 14.959 10.050 1.00 9.95 C ANISOU 1594 CB PRO A 214 1386 1251 1144 -76 -31 -125 C ATOM 1595 CG PRO A 214 -12.369 15.198 9.854 1.00 13.09 C ANISOU 1595 CG PRO A 214 1749 1637 1590 -108 -51 -130 C ATOM 1596 CD PRO A 214 -12.212 15.793 8.492 1.00 15.56 C ANISOU 1596 CD PRO A 214 2050 1917 1946 -151 -28 -96 C ATOM 1597 N PRO A 215 -16.839 15.444 8.762 1.00 10.00 N ANISOU 1597 N PRO A 215 1442 1226 1132 -65 16 -87 N ATOM 1598 CA PRO A 215 -18.034 16.284 8.631 1.00 14.26 C ANISOU 1598 CA PRO A 215 2003 1737 1676 -56 11 -91 C ATOM 1599 C PRO A 215 -17.966 17.534 9.511 1.00 18.45 C ANISOU 1599 C PRO A 215 2545 2244 2222 -44 -28 -131 C ATOM 1600 O PRO A 215 -18.415 18.599 9.097 1.00 19.44 O ANISOU 1600 O PRO A 215 2680 2331 2375 -56 -42 -134 O ATOM 1601 CB PRO A 215 -19.164 15.349 9.099 1.00 12.46 C ANISOU 1601 CB PRO A 215 1783 1534 1418 -18 38 -83 C ATOM 1602 CG PRO A 215 -18.465 14.298 9.898 1.00 12.93 C ANISOU 1602 CG PRO A 215 1830 1633 1451 0 46 -85 C ATOM 1603 CD PRO A 215 -17.204 14.076 9.155 1.00 14.24 C ANISOU 1603 CD PRO A 215 1976 1800 1635 -38 43 -75 C ATOM 1604 N PHE A 216 -17.412 17.391 10.710 1.00 24.43 N ANISOU 1604 N PHE A 216 3302 3022 2958 -17 -50 -165 N ATOM 1605 CA PHE A 216 -17.243 18.509 11.639 1.00 24.38 C ANISOU 1605 CA PHE A 216 3308 2995 2962 2 -97 -215 C ATOM 1606 C PHE A 216 -15.771 18.705 11.989 1.00 23.21 C ANISOU 1606 C PHE A 216 3136 2840 2841 -15 -138 -242 C ATOM 1607 O PHE A 216 -15.067 17.756 12.349 1.00 21.15 O ANISOU 1607 O PHE A 216 2863 2616 2557 -7 -133 -239 O ATOM 1608 CB PHE A 216 -18.035 18.270 12.931 1.00 21.67 C ANISOU 1608 CB PHE A 216 2991 2681 2561 66 -95 -241 C ATOM 1609 CG PHE A 216 -19.433 17.786 12.705 1.00 15.57 C ANISOU 1609 CG PHE A 216 2230 1920 1768 87 -47 -209 C ATOM 1610 CD1 PHE A 216 -20.449 18.683 12.422 1.00 12.41 C ANISOU 1610 CD1 PHE A 216 1842 1485 1387 90 -48 -214 C ATOM 1611 CD2 PHE A 216 -19.733 16.436 12.771 1.00 14.20 C ANISOU 1611 CD2 PHE A 216 2048 1783 1564 102 -3 -174 C ATOM 1612 CE1 PHE A 216 -21.740 18.245 12.205 1.00 15.89 C ANISOU 1612 CE1 PHE A 216 2286 1931 1819 108 -8 -185 C ATOM 1613 CE2 PHE A 216 -21.024 15.997 12.563 1.00 22.30 C ANISOU 1613 CE2 PHE A 216 3075 2811 2587 119 37 -145 C ATOM 1614 CZ PHE A 216 -22.030 16.900 12.280 1.00 18.40 C ANISOU 1614 CZ PHE A 216 2592 2285 2115 122 35 -151 C ATOM 1615 N THR A 217 -15.313 19.942 11.889 1.00 23.34 N ANISOU 1615 N THR A 217 3144 2808 2916 -38 -180 -268 N ATOM 1616 CA THR A 217 -13.914 20.245 12.130 1.00 24.10 C ANISOU 1616 CA THR A 217 3209 2887 3062 -60 -224 -293 C ATOM 1617 C THR A 217 -13.806 21.543 12.902 1.00 26.60 C ANISOU 1617 C THR A 217 3531 3159 3416 -45 -291 -356 C ATOM 1618 O THR A 217 -14.636 22.440 12.762 1.00 27.31 O ANISOU 1618 O THR A 217 3640 3215 3521 -41 -297 -365 O ATOM 1619 CB THR A 217 -13.128 20.379 10.818 1.00 27.65 C ANISOU 1619 CB THR A 217 3620 3307 3578 -122 -201 -245 C ATOM 1620 OG1 THR A 217 -13.636 21.494 10.073 1.00 31.26 O ANISOU 1620 OG1 THR A 217 4083 3713 4083 -147 -199 -229 O ATOM 1621 CG2 THR A 217 -13.260 19.105 9.981 1.00 24.94 C ANISOU 1621 CG2 THR A 217 3275 3007 3195 -132 -138 -189 C ATOM 1622 N ALA A 218 -12.775 21.635 13.725 1.00 30.94 N ANISOU 1622 N ALA A 218 4063 3707 3984 -34 -348 -405 N ATOM 1623 CA ALA A 218 -12.608 22.780 14.601 1.00 35.65 C ANISOU 1623 CA ALA A 218 4666 4263 4615 -10 -426 -479 C ATOM 1624 C ALA A 218 -11.195 22.800 15.158 1.00 36.25 C ANISOU 1624 C ALA A 218 4706 4329 4738 -16 -491 -522 C ATOM 1625 O ALA A 218 -10.487 21.787 15.138 1.00 26.42 O ANISOU 1625 O ALA A 218 3441 3123 3475 -21 -474 -499 O ATOM 1626 CB ALA A 218 -13.605 22.701 15.733 1.00 39.26 C ANISOU 1626 CB ALA A 218 5178 4758 4980 66 -435 -522 C ATOM 1627 N PHE A 219 -10.790 23.962 15.653 1.00 46.75 N ANISOU 1627 N PHE A 219 6025 5602 6137 -13 -569 -587 N ATOM 1628 CA PHE A 219 -9.480 24.106 16.271 1.00 56.30 C ANISOU 1628 CA PHE A 219 7195 6791 7404 -14 -648 -641 C ATOM 1629 C PHE A 219 -9.562 24.038 17.794 1.00 57.06 C ANISOU 1629 C PHE A 219 7335 6923 7421 71 -719 -728 C ATOM 1630 O PHE A 219 -8.590 24.313 18.490 1.00 58.16 O ANISOU 1630 O PHE A 219 7451 7043 7603 85 -805 -793 O ATOM 1631 CB PHE A 219 -8.802 25.398 15.810 1.00 55.24 C ANISOU 1631 CB PHE A 219 7009 6562 7418 -68 -698 -659 C ATOM 1632 CG PHE A 219 -8.458 25.405 14.345 1.00 55.05 C ANISOU 1632 CG PHE A 219 6937 6506 7473 -145 -628 -568 C ATOM 1633 CD1 PHE A 219 -9.116 26.247 13.462 1.00 52.41 C ANISOU 1633 CD1 PHE A 219 6605 6123 7186 -179 -593 -527 C ATOM 1634 CD2 PHE A 219 -7.485 24.550 13.849 1.00 56.66 C ANISOU 1634 CD2 PHE A 219 7096 6733 7700 -179 -595 -521 C ATOM 1635 CE1 PHE A 219 -8.796 26.245 12.116 1.00 50.43 C ANISOU 1635 CE1 PHE A 219 6317 5848 6996 -240 -526 -440 C ATOM 1636 CE2 PHE A 219 -7.168 24.537 12.507 1.00 53.18 C ANISOU 1636 CE2 PHE A 219 6616 6269 7321 -240 -524 -437 C ATOM 1637 CZ PHE A 219 -7.826 25.384 11.638 1.00 49.06 C ANISOU 1637 CZ PHE A 219 6101 5701 6838 -269 -489 -395 C ATOM 1638 N SER A 220 -10.728 23.653 18.302 1.00 55.27 N ANISOU 1638 N SER A 220 7171 6751 7079 130 -681 -727 N ATOM 1639 CA SER A 220 -10.957 23.581 19.739 1.00 49.92 C ANISOU 1639 CA SER A 220 6545 6116 6307 223 -734 -800 C ATOM 1640 C SER A 220 -12.113 22.626 20.016 1.00 42.66 C ANISOU 1640 C SER A 220 5679 5272 5260 275 -651 -754 C ATOM 1641 O SER A 220 -13.084 22.605 19.272 1.00 41.03 O ANISOU 1641 O SER A 220 5479 5062 5050 251 -579 -699 O ATOM 1642 CB SER A 220 -11.263 24.978 20.279 1.00 44.93 C ANISOU 1642 CB SER A 220 5933 5427 5710 253 -809 -884 C ATOM 1643 OG SER A 220 -12.032 24.912 21.462 1.00 49.74 O ANISOU 1643 OG SER A 220 6610 6087 6200 351 -823 -935 O ATOM 1644 N GLN A 221 -12.012 21.837 21.078 1.00 34.23 N ANISOU 1644 N GLN A 221 4645 4269 4093 348 -661 -775 N ATOM 1645 CA GLN A 221 -13.035 20.836 21.362 1.00 34.98 C ANISOU 1645 CA GLN A 221 4782 4433 4078 398 -576 -721 C ATOM 1646 C GLN A 221 -14.389 21.446 21.676 1.00 35.39 C ANISOU 1646 C GLN A 221 4879 4484 4083 445 -548 -733 C ATOM 1647 O GLN A 221 -15.438 20.815 21.478 1.00 32.81 O ANISOU 1647 O GLN A 221 4569 4191 3707 458 -461 -671 O ATOM 1648 CB GLN A 221 -12.604 19.907 22.497 1.00 39.71 C ANISOU 1648 CB GLN A 221 5409 5100 4580 473 -593 -735 C ATOM 1649 CG GLN A 221 -13.522 18.702 22.680 1.00 47.78 C ANISOU 1649 CG GLN A 221 6459 6188 5506 514 -495 -661 C ATOM 1650 CD GLN A 221 -12.862 17.555 23.448 1.00 54.40 C ANISOU 1650 CD GLN A 221 7307 7088 6274 563 -499 -647 C ATOM 1651 OE1 GLN A 221 -13.505 16.899 24.275 1.00 53.42 O ANISOU 1651 OE1 GLN A 221 7228 7022 6048 641 -454 -623 O ATOM 1652 NE2 GLN A 221 -11.582 17.297 23.160 1.00 53.70 N ANISOU 1652 NE2 GLN A 221 7174 6984 6243 518 -547 -657 N ATOM 1653 N LYS A 222 -14.356 22.685 22.151 1.00 31.42 N ANISOU 1653 N LYS A 222 4392 3939 3606 470 -624 -815 N ATOM 1654 CA LYS A 222 -15.577 23.415 22.481 1.00 33.59 C ANISOU 1654 CA LYS A 222 4709 4207 3845 518 -606 -839 C ATOM 1655 C LYS A 222 -16.272 23.945 21.248 1.00 29.93 C ANISOU 1655 C LYS A 222 4218 3690 3463 445 -559 -791 C ATOM 1656 O LYS A 222 -17.506 24.000 21.174 1.00 29.39 O ANISOU 1656 O LYS A 222 4174 3632 3360 469 -500 -763 O ATOM 1657 CB LYS A 222 -15.253 24.559 23.446 1.00 35.72 C ANISOU 1657 CB LYS A 222 5008 4449 4117 576 -712 -952 C ATOM 1658 CG LYS A 222 -16.326 25.615 23.580 1.00 40.92 C ANISOU 1658 CG LYS A 222 5696 5074 4776 608 -712 -989 C ATOM 1659 CD LYS A 222 -15.837 26.795 24.438 1.00 50.86 C ANISOU 1659 CD LYS A 222 6976 6292 6057 658 -832 -1112 C ATOM 1660 CE LYS A 222 -17.022 27.527 25.070 1.00 55.59 C ANISOU 1660 CE LYS A 222 7631 6894 6597 739 -823 -1157 C ATOM 1661 NZ LYS A 222 -17.440 26.889 26.352 1.00 58.73 N ANISOU 1661 NZ LYS A 222 8096 7382 6838 860 -802 -1178 N ATOM 1662 N GLU A 223 -15.451 24.347 20.271 1.00 29.05 N ANISOU 1662 N GLU A 223 4055 3520 3463 358 -587 -778 N ATOM 1663 C GLU A 223 -16.443 23.648 18.171 1.00 27.97 C ANISOU 1663 C GLU A 223 3880 3372 3373 255 -449 -630 C ATOM 1664 O GLU A 223 -17.443 23.715 17.457 1.00 26.35 O ANISOU 1664 O GLU A 223 3679 3158 3176 237 -394 -585 O ATOM 1665 CA AGLU A 223 -15.946 24.851 18.983 0.50 30.95 C ANISOU 1665 CA AGLU A 223 4268 3707 3784 285 -546 -726 C ATOM 1666 CB AGLU A 223 -14.880 25.592 18.205 0.50 33.37 C ANISOU 1666 CB AGLU A 223 4521 3941 4216 207 -596 -732 C ATOM 1667 CG AGLU A 223 -13.872 26.320 19.103 0.50 37.22 C ANISOU 1667 CG AGLU A 223 5001 4396 4746 232 -704 -826 C ATOM 1668 CD AGLU A 223 -13.117 27.461 18.441 0.50 36.81 C ANISOU 1668 CD AGLU A 223 4897 4249 4841 163 -760 -843 C ATOM 1669 OE1AGLU A 223 -11.872 27.418 18.364 0.50 35.92 O ANISOU 1669 OE1AGLU A 223 4737 4112 4800 127 -805 -854 O ATOM 1670 OE2AGLU A 223 -13.765 28.372 17.912 0.50 38.26 O ANISOU 1670 OE2AGLU A 223 5082 4379 5078 142 -751 -835 O ATOM 1671 CA BGLU A 223 -15.957 24.847 18.985 0.50 30.97 C ANISOU 1671 CA BGLU A 223 4271 3710 3786 285 -545 -726 C ATOM 1672 CB BGLU A 223 -14.906 25.614 18.208 0.50 33.39 C ANISOU 1672 CB BGLU A 223 4525 3943 4219 208 -596 -732 C ATOM 1673 CG BGLU A 223 -14.728 25.167 16.765 0.50 35.22 C ANISOU 1673 CG BGLU A 223 4715 4162 4504 126 -531 -641 C ATOM 1674 CD BGLU A 223 -13.983 26.187 15.895 0.50 36.10 C ANISOU 1674 CD BGLU A 223 4778 4190 4747 54 -564 -635 C ATOM 1675 OE1BGLU A 223 -12.745 26.303 15.997 0.50 36.07 O ANISOU 1675 OE1BGLU A 223 4734 4162 4809 28 -614 -658 O ATOM 1676 OE2BGLU A 223 -14.632 26.817 15.038 0.50 31.86 O ANISOU 1676 OE2BGLU A 223 4240 3612 4254 22 -535 -599 O ATOM 1677 N LEU A 224 -15.787 22.513 18.368 1.00 22.96 N ANISOU 1677 N LEU A 224 3236 2788 2700 259 -433 -606 N ATOM 1678 CA LEU A 224 -16.186 21.251 17.739 1.00 25.12 C ANISOU 1678 CA LEU A 224 3501 3104 2940 239 -350 -525 C ATOM 1679 C LEU A 224 -17.518 20.772 18.339 1.00 27.35 C ANISOU 1679 C LEU A 224 3822 3430 3138 305 -293 -507 C ATOM 1680 O LEU A 224 -18.413 20.366 17.610 1.00 27.54 O ANISOU 1680 O LEU A 224 3841 3456 3167 284 -229 -449 O ATOM 1681 CB LEU A 224 -15.089 20.220 17.964 1.00 25.06 C ANISOU 1681 CB LEU A 224 3474 3134 2915 235 -357 -513 C ATOM 1682 CG LEU A 224 -15.321 18.838 17.382 1.00 30.76 C ANISOU 1682 CG LEU A 224 4183 3897 3609 218 -280 -437 C ATOM 1683 CD1 LEU A 224 -15.560 18.919 15.889 1.00 29.23 C ANISOU 1683 CD1 LEU A 224 3959 3667 3479 145 -239 -384 C ATOM 1684 CD2 LEU A 224 -14.144 17.917 17.686 1.00 26.73 C ANISOU 1684 CD2 LEU A 224 3651 3418 3086 218 -296 -434 C ATOM 1685 N ALA A 225 -17.668 20.854 19.661 1.00 24.50 N ANISOU 1685 N ALA A 225 3502 3104 2704 387 -317 -556 N ATOM 1686 CA ALA A 225 -18.944 20.494 20.284 1.00 23.89 C ANISOU 1686 CA ALA A 225 3460 3066 2551 456 -256 -535 C ATOM 1687 C ALA A 225 -20.105 21.328 19.739 1.00 21.88 C ANISOU 1687 C ALA A 225 3209 2771 2335 443 -232 -529 C ATOM 1688 O ALA A 225 -21.171 20.797 19.457 1.00 22.18 O ANISOU 1688 O ALA A 225 3244 2824 2359 450 -160 -474 O ATOM 1689 CB ALA A 225 -18.873 20.607 21.801 1.00 20.82 C ANISOU 1689 CB ALA A 225 3119 2720 2071 556 -288 -593 C ATOM 1690 N GLY A 226 -19.899 22.632 19.601 1.00 24.22 N ANISOU 1690 N GLY A 226 3505 3011 2685 426 -294 -585 N ATOM 1691 CA GLY A 226 -20.922 23.497 19.047 1.00 19.22 C ANISOU 1691 CA GLY A 226 2873 2333 2095 412 -279 -581 C ATOM 1692 C GLY A 226 -21.307 23.064 17.644 1.00 17.24 C ANISOU 1692 C GLY A 226 2588 2063 1899 338 -227 -504 C ATOM 1693 O GLY A 226 -22.485 22.946 17.328 1.00 26.78 O ANISOU 1693 O GLY A 226 3799 3273 3105 347 -174 -468 O ATOM 1694 N LYS A 227 -20.306 22.833 16.803 1.00 16.81 N ANISOU 1694 N LYS A 227 2501 1992 1894 270 -242 -481 N ATOM 1695 CA LYS A 227 -20.529 22.370 15.434 1.00 26.55 C ANISOU 1695 CA LYS A 227 3706 3212 3170 206 -197 -411 C ATOM 1696 C LYS A 227 -21.341 21.079 15.391 1.00 27.37 C ANISOU 1696 C LYS A 227 3810 3364 3226 226 -126 -356 C ATOM 1697 O LYS A 227 -22.307 20.971 14.647 1.00 29.29 O ANISOU 1697 O LYS A 227 4046 3594 3489 211 -88 -317 O ATOM 1698 CB LYS A 227 -19.197 22.125 14.722 1.00 31.01 C ANISOU 1698 CB LYS A 227 4238 3765 3779 144 -217 -394 C ATOM 1699 CG LYS A 227 -18.290 23.328 14.626 1.00 30.83 C ANISOU 1699 CG LYS A 227 4201 3685 3827 113 -284 -437 C ATOM 1700 CD LYS A 227 -18.196 23.856 13.221 1.00 31.32 C ANISOU 1700 CD LYS A 227 4239 3697 3966 45 -272 -392 C ATOM 1701 CE LYS A 227 -16.864 24.564 13.037 1.00 31.25 C ANISOU 1701 CE LYS A 227 4197 3642 4036 2 -324 -412 C ATOM 1702 NZ LYS A 227 -16.305 24.325 11.683 1.00 30.08 N ANISOU 1702 NZ LYS A 227 4016 3478 3935 -62 -288 -345 N ATOM 1703 N ILE A 228 -20.921 20.098 16.181 1.00 29.75 N ANISOU 1703 N ILE A 228 4116 3718 3471 261 -112 -353 N ATOM 1704 CA ILE A 228 -21.591 18.806 16.251 1.00 25.16 C ANISOU 1704 CA ILE A 228 3528 3178 2853 282 -46 -299 C ATOM 1705 C ILE A 228 -23.040 18.916 16.711 1.00 24.97 C ANISOU 1705 C ILE A 228 3520 3159 2807 334 -2 -289 C ATOM 1706 O ILE A 228 -23.899 18.194 16.223 1.00 27.98 O ANISOU 1706 O ILE A 228 3884 3545 3203 327 51 -238 O ATOM 1707 CB ILE A 228 -20.845 17.835 17.190 1.00 26.59 C ANISOU 1707 CB ILE A 228 3716 3412 2975 320 -42 -299 C ATOM 1708 CG1 ILE A 228 -19.550 17.337 16.544 1.00 22.24 C ANISOU 1708 CG1 ILE A 228 3137 2859 2454 264 -65 -289 C ATOM 1709 CG2 ILE A 228 -21.737 16.660 17.550 1.00 30.63 C ANISOU 1709 CG2 ILE A 228 4227 3963 3450 360 31 -245 C ATOM 1710 CD1 ILE A 228 -18.680 16.523 17.490 1.00 17.68 C ANISOU 1710 CD1 ILE A 228 2566 2329 1825 301 -75 -297 C ATOM 1711 N ARG A 229 -23.308 19.829 17.641 1.00 27.18 N ANISOU 1711 N ARG A 229 3833 3438 3058 389 -26 -341 N ATOM 1712 CA ARG A 229 -24.658 20.017 18.183 1.00 27.62 C ANISOU 1712 CA ARG A 229 3903 3500 3089 448 18 -335 C ATOM 1713 C ARG A 229 -25.636 20.614 17.180 1.00 26.47 C ANISOU 1713 C ARG A 229 3739 3306 3010 411 29 -317 C ATOM 1714 O ARG A 229 -26.830 20.316 17.224 1.00 32.90 O ANISOU 1714 O ARG A 229 4546 4125 3829 438 83 -283 O ATOM 1715 CB ARG A 229 -24.631 20.841 19.480 1.00 33.99 C ANISOU 1715 CB ARG A 229 4754 4323 3839 526 -13 -402 C ATOM 1716 CG ARG A 229 -24.487 19.972 20.721 1.00 42.30 C ANISOU 1716 CG ARG A 229 5831 5441 4799 603 19 -394 C ATOM 1717 CD ARG A 229 -24.458 20.768 22.021 1.00 47.92 C ANISOU 1717 CD ARG A 229 6594 6173 5440 693 -16 -466 C ATOM 1718 NE ARG A 229 -23.109 21.236 22.337 1.00 59.23 N ANISOU 1718 NE ARG A 229 8041 7600 6864 686 -107 -535 N ATOM 1719 CZ ARG A 229 -22.765 22.515 22.464 1.00 63.47 C ANISOU 1719 CZ ARG A 229 8593 8094 7427 687 -185 -614 C ATOM 1720 NH1 ARG A 229 -23.678 23.465 22.318 1.00 64.93 N ANISOU 1720 NH1 ARG A 229 8786 8243 7641 698 -182 -636 N ATOM 1721 NH2 ARG A 229 -21.510 22.849 22.746 1.00 61.05 N ANISOU 1721 NH2 ARG A 229 8290 7778 7126 679 -270 -674 N ATOM 1722 N GLU A 230 -25.133 21.463 16.284 1.00 22.18 N ANISOU 1722 N GLU A 230 3188 2714 2524 351 -22 -336 N ATOM 1723 CA GLU A 230 -25.951 22.004 15.201 1.00 23.51 C ANISOU 1723 CA GLU A 230 3343 2836 2755 313 -18 -314 C ATOM 1724 C GLU A 230 -26.293 20.939 14.143 1.00 24.10 C ANISOU 1724 C GLU A 230 3386 2916 2856 271 23 -249 C ATOM 1725 O GLU A 230 -27.358 20.982 13.525 1.00 28.51 O ANISOU 1725 O GLU A 230 3931 3452 3449 265 44 -223 O ATOM 1726 CB GLU A 230 -25.273 23.216 14.554 1.00 27.04 C ANISOU 1726 CB GLU A 230 3791 3228 3255 265 -80 -345 C ATOM 1727 CG GLU A 230 -25.526 24.519 15.285 1.00 38.21 C ANISOU 1727 CG GLU A 230 5231 4613 4675 305 -119 -408 C ATOM 1728 CD GLU A 230 -27.004 24.889 15.324 1.00 50.66 C ANISOU 1728 CD GLU A 230 6812 6176 6260 341 -87 -400 C ATOM 1729 OE1 GLU A 230 -27.688 24.727 14.288 1.00 54.24 O ANISOU 1729 OE1 GLU A 230 7246 6609 6756 306 -64 -353 O ATOM 1730 OE2 GLU A 230 -27.480 25.344 16.389 1.00 50.97 O ANISOU 1730 OE2 GLU A 230 6877 6226 6265 409 -87 -444 O ATOM 1731 N GLY A 231 -25.390 19.982 13.949 1.00 19.11 N ANISOU 1731 N GLY A 231 2742 2311 2209 245 28 -228 N ATOM 1732 CA GLY A 231 -25.626 18.873 13.040 1.00 16.12 C ANISOU 1732 CA GLY A 231 2335 1939 1850 212 61 -175 C ATOM 1733 C GLY A 231 -25.629 19.303 11.591 1.00 19.04 C ANISOU 1733 C GLY A 231 2696 2269 2271 155 39 -159 C ATOM 1734 O GLY A 231 -26.367 18.761 10.773 1.00 21.03 O ANISOU 1734 O GLY A 231 2930 2513 2547 142 59 -125 O ATOM 1735 N LYS A 232 -24.798 20.286 11.271 1.00 21.43 N ANISOU 1735 N LYS A 232 3008 2544 2590 125 -4 -183 N ATOM 1736 CA LYS A 232 -24.724 20.804 9.912 1.00 20.80 C ANISOU 1736 CA LYS A 232 2924 2426 2553 76 -21 -161 C ATOM 1737 C LYS A 232 -23.350 20.534 9.317 1.00 16.04 C ANISOU 1737 C LYS A 232 2311 1829 1953 32 -32 -149 C ATOM 1738 O LYS A 232 -22.330 20.724 9.972 1.00 15.69 O ANISOU 1738 O LYS A 232 2267 1793 1903 31 -53 -176 O ATOM 1739 CB LYS A 232 -25.003 22.307 9.887 1.00 21.66 C ANISOU 1739 CB LYS A 232 3047 2487 2696 76 -55 -187 C ATOM 1740 CG LYS A 232 -26.436 22.717 10.150 1.00 21.72 C ANISOU 1740 CG LYS A 232 3061 2478 2712 114 -45 -194 C ATOM 1741 CD LYS A 232 -26.487 24.233 10.350 1.00 30.30 C ANISOU 1741 CD LYS A 232 4164 3517 3832 119 -85 -230 C ATOM 1742 CE LYS A 232 -27.907 24.758 10.500 1.00 32.95 C ANISOU 1742 CE LYS A 232 4504 3831 4184 155 -76 -237 C ATOM 1743 NZ LYS A 232 -27.934 26.252 10.573 1.00 36.02 N ANISOU 1743 NZ LYS A 232 4907 4165 4612 156 -118 -271 N ATOM 1744 N PHE A 233 -23.338 20.108 8.062 1.00 17.32 N ANISOU 1744 N PHE A 233 2466 1988 2129 1 -20 -110 N ATOM 1745 CA PHE A 233 -22.111 19.730 7.389 1.00 8.09 C ANISOU 1745 CA PHE A 233 1285 828 960 -36 -19 -91 C ATOM 1746 C PHE A 233 -22.314 19.953 5.915 1.00 12.73 C ANISOU 1746 C PHE A 233 1877 1393 1565 -63 -15 -55 C ATOM 1747 O PHE A 233 -23.440 20.128 5.469 1.00 7.25 O ANISOU 1747 O PHE A 233 1193 684 877 -50 -16 -45 O ATOM 1748 CB PHE A 233 -21.767 18.266 7.666 1.00 7.05 C ANISOU 1748 CB PHE A 233 1139 743 796 -28 8 -82 C ATOM 1749 CG PHE A 233 -22.947 17.333 7.592 1.00 12.50 C ANISOU 1749 CG PHE A 233 1826 1448 1476 -3 34 -66 C ATOM 1750 CD1 PHE A 233 -23.304 16.745 6.389 1.00 17.03 C ANISOU 1750 CD1 PHE A 233 2395 2019 2058 -18 42 -39 C ATOM 1751 CD2 PHE A 233 -23.695 17.040 8.728 1.00 13.99 C ANISOU 1751 CD2 PHE A 233 2013 1651 1650 38 49 -79 C ATOM 1752 CE1 PHE A 233 -24.387 15.887 6.309 1.00 11.96 C ANISOU 1752 CE1 PHE A 233 1741 1381 1422 3 58 -28 C ATOM 1753 CE2 PHE A 233 -24.781 16.187 8.658 1.00 13.72 C ANISOU 1753 CE2 PHE A 233 1966 1623 1624 58 76 -58 C ATOM 1754 CZ PHE A 233 -25.128 15.608 7.443 1.00 10.68 C ANISOU 1754 CZ PHE A 233 1571 1229 1260 38 77 -35 C ATOM 1755 N ARG A 234 -21.225 19.957 5.154 1.00 8.32 N ANISOU 1755 N ARG A 234 1312 835 1014 -95 -11 -32 N ATOM 1756 CA ARG A 234 -21.356 20.127 3.723 1.00 7.36 C ANISOU 1756 CA ARG A 234 1201 699 896 -112 -3 8 C ATOM 1757 C ARG A 234 -21.846 18.820 3.129 1.00 18.40 C ANISOU 1757 C ARG A 234 2600 2131 2261 -98 15 21 C ATOM 1758 O ARG A 234 -21.654 17.759 3.718 1.00 17.18 O ANISOU 1758 O ARG A 234 2431 2009 2088 -88 28 9 O ATOM 1759 CB ARG A 234 -20.031 20.551 3.086 1.00 7.62 C ANISOU 1759 CB ARG A 234 1224 721 948 -145 5 35 C ATOM 1760 CG ARG A 234 -19.492 21.857 3.621 1.00 8.03 C ANISOU 1760 CG ARG A 234 1268 730 1053 -162 -19 21 C ATOM 1761 CD ARG A 234 -18.234 22.289 2.880 1.00 14.58 C ANISOU 1761 CD ARG A 234 2080 1542 1918 -198 -4 58 C ATOM 1762 NE ARG A 234 -18.464 22.479 1.448 1.00 15.55 N ANISOU 1762 NE ARG A 234 2221 1656 2030 -202 20 114 N ATOM 1763 CZ ARG A 234 -19.175 23.474 0.921 1.00 25.11 C ANISOU 1763 CZ ARG A 234 3452 2827 3261 -199 10 134 C ATOM 1764 NH1 ARG A 234 -19.738 24.386 1.708 1.00 23.84 N ANISOU 1764 NH1 ARG A 234 3293 2628 3137 -194 -25 101 N ATOM 1765 NH2 ARG A 234 -19.328 23.556 -0.399 1.00 25.55 N ANISOU 1765 NH2 ARG A 234 3530 2883 3296 -196 32 188 N ATOM 1766 N ARG A 235 -22.508 18.897 1.981 1.00 15.16 N ANISOU 1766 N ARG A 235 2207 1709 1844 -93 12 44 N ATOM 1767 CA ARG A 235 -22.813 17.689 1.239 1.00 11.76 C ANISOU 1767 CA ARG A 235 1777 1305 1386 -81 21 53 C ATOM 1768 C ARG A 235 -21.488 17.092 0.799 1.00 13.33 C ANISOU 1768 C ARG A 235 1970 1532 1564 -98 44 68 C ATOM 1769 O ARG A 235 -20.546 17.823 0.517 1.00 9.18 O ANISOU 1769 O ARG A 235 1445 996 1047 -119 54 89 O ATOM 1770 CB ARG A 235 -23.672 17.979 0.007 1.00 10.42 C ANISOU 1770 CB ARG A 235 1632 1118 1209 -68 4 71 C ATOM 1771 CG ARG A 235 -24.079 16.707 -0.752 1.00 15.54 C ANISOU 1771 CG ARG A 235 2281 1789 1833 -48 0 67 C ATOM 1772 CD ARG A 235 -24.456 16.978 -2.204 1.00 15.86 C ANISOU 1772 CD ARG A 235 2355 1822 1849 -33 -19 88 C ATOM 1773 NE ARG A 235 -25.094 15.825 -2.837 1.00 13.92 N ANISOU 1773 NE ARG A 235 2110 1590 1590 -7 -39 70 N ATOM 1774 CZ ARG A 235 -24.439 14.819 -3.410 1.00 13.43 C ANISOU 1774 CZ ARG A 235 2050 1558 1494 0 -28 68 C ATOM 1775 NH1 ARG A 235 -23.113 14.800 -3.419 1.00 14.21 N ANISOU 1775 NH1 ARG A 235 2149 1679 1570 -19 9 86 N ATOM 1776 NH2 ARG A 235 -25.114 13.821 -3.961 1.00 9.23 N ANISOU 1776 NH2 ARG A 235 1518 1030 960 26 -56 44 N ATOM 1777 N ILE A 236 -21.407 15.770 0.732 1.00 8.70 N ANISOU 1777 N ILE A 236 1372 976 958 -87 55 61 N ATOM 1778 CA ILE A 236 -20.219 15.143 0.171 1.00 12.29 C ANISOU 1778 CA ILE A 236 1821 1457 1390 -98 79 76 C ATOM 1779 C ILE A 236 -20.088 15.581 -1.292 1.00 12.20 C ANISOU 1779 C ILE A 236 1838 1441 1356 -95 84 108 C ATOM 1780 O ILE A 236 -21.035 16.113 -1.852 1.00 12.86 O ANISOU 1780 O ILE A 236 1946 1505 1437 -81 63 113 O ATOM 1781 CB ILE A 236 -20.284 13.609 0.315 1.00 14.77 C ANISOU 1781 CB ILE A 236 2119 1800 1692 -83 85 59 C ATOM 1782 CG1 ILE A 236 -21.456 13.037 -0.476 1.00 15.24 C ANISOU 1782 CG1 ILE A 236 2192 1853 1745 -58 65 51 C ATOM 1783 CG2 ILE A 236 -20.410 13.218 1.792 1.00 10.25 C ANISOU 1783 CG2 ILE A 236 1523 1234 1139 -80 86 38 C ATOM 1784 CD1 ILE A 236 -21.661 11.569 -0.231 1.00 13.93 C ANISOU 1784 CD1 ILE A 236 2003 1703 1585 -43 66 33 C ATOM 1785 N PRO A 237 -18.914 15.383 -1.905 1.00 16.62 N ANISOU 1785 N PRO A 237 2397 2021 1899 -104 114 131 N ATOM 1786 CA PRO A 237 -18.760 15.803 -3.303 1.00 13.01 C ANISOU 1786 CA PRO A 237 1970 1564 1409 -93 128 169 C ATOM 1787 C PRO A 237 -19.861 15.262 -4.219 1.00 15.48 C ANISOU 1787 C PRO A 237 2315 1884 1683 -55 102 158 C ATOM 1788 O PRO A 237 -20.372 14.150 -3.991 1.00 12.53 O ANISOU 1788 O PRO A 237 1931 1523 1305 -40 84 123 O ATOM 1789 CB PRO A 237 -17.410 15.213 -3.690 1.00 7.74 C ANISOU 1789 CB PRO A 237 1289 927 725 -99 170 188 C ATOM 1790 CG PRO A 237 -16.667 15.138 -2.404 1.00 10.74 C ANISOU 1790 CG PRO A 237 1627 1305 1149 -128 173 170 C ATOM 1791 CD PRO A 237 -17.677 14.801 -1.357 1.00 7.11 C ANISOU 1791 CD PRO A 237 1161 839 702 -121 138 128 C ATOM 1792 N TYR A 238 -20.181 16.041 -5.252 1.00 9.92 N ANISOU 1792 N TYR A 238 1647 1168 954 -39 98 189 N ATOM 1793 CA TYR A 238 -21.261 15.745 -6.190 1.00 10.80 C ANISOU 1793 CA TYR A 238 1795 1282 1029 2 62 178 C ATOM 1794 C TYR A 238 -21.028 14.527 -7.086 1.00 15.70 C ANISOU 1794 C TYR A 238 2432 1940 1595 36 64 163 C ATOM 1795 O TYR A 238 -21.960 14.011 -7.709 1.00 15.48 O ANISOU 1795 O TYR A 238 2425 1912 1544 72 21 135 O ATOM 1796 CB TYR A 238 -21.614 16.998 -7.019 1.00 10.20 C ANISOU 1796 CB TYR A 238 1755 1182 936 14 57 219 C ATOM 1797 CG TYR A 238 -22.186 18.101 -6.152 1.00 13.09 C ANISOU 1797 CG TYR A 238 2106 1505 1361 -11 39 219 C ATOM 1798 CD1 TYR A 238 -21.395 19.166 -5.719 1.00 8.70 C ANISOU 1798 CD1 TYR A 238 1536 925 843 -45 67 252 C ATOM 1799 CD2 TYR A 238 -23.506 18.050 -5.728 1.00 8.34 C ANISOU 1799 CD2 TYR A 238 1501 882 785 1 -7 183 C ATOM 1800 CE1 TYR A 238 -21.918 20.166 -4.902 1.00 14.77 C ANISOU 1800 CE1 TYR A 238 2293 1652 1667 -63 46 244 C ATOM 1801 CE2 TYR A 238 -24.032 19.027 -4.919 1.00 10.19 C ANISOU 1801 CE2 TYR A 238 1722 1079 1070 -17 -21 180 C ATOM 1802 CZ TYR A 238 -23.232 20.088 -4.501 1.00 15.60 C ANISOU 1802 CZ TYR A 238 2399 1743 1786 -47 4 207 C ATOM 1803 OH TYR A 238 -23.737 21.071 -3.684 1.00 17.49 O ANISOU 1803 OH TYR A 238 2627 1942 2076 -60 -14 196 O ATOM 1804 N ARG A 239 -19.792 14.055 -7.145 1.00 16.43 N ANISOU 1804 N ARG A 239 2511 2060 1671 27 109 176 N ATOM 1805 CA ARG A 239 -19.523 12.802 -7.840 1.00 21.76 C ANISOU 1805 CA ARG A 239 3197 2770 2300 61 110 153 C ATOM 1806 C ARG A 239 -20.188 11.615 -7.155 1.00 20.96 C ANISOU 1806 C ARG A 239 3068 2665 2232 62 73 96 C ATOM 1807 O ARG A 239 -20.353 10.563 -7.760 1.00 20.45 O ANISOU 1807 O ARG A 239 3013 2617 2141 96 54 65 O ATOM 1808 CB ARG A 239 -18.025 12.556 -7.976 1.00 24.26 C ANISOU 1808 CB ARG A 239 3500 3116 2601 51 171 181 C ATOM 1809 CG ARG A 239 -17.218 13.024 -6.806 1.00 31.16 C ANISOU 1809 CG ARG A 239 4327 3976 3535 -1 199 196 C ATOM 1810 CD ARG A 239 -15.860 12.360 -6.810 1.00 45.40 C ANISOU 1810 CD ARG A 239 6106 5809 5335 -8 246 205 C ATOM 1811 NE ARG A 239 -15.975 10.921 -6.598 1.00 55.57 N ANISOU 1811 NE ARG A 239 7381 7118 6615 9 229 157 N ATOM 1812 CZ ARG A 239 -15.368 10.004 -7.342 1.00 54.13 C ANISOU 1812 CZ ARG A 239 7207 6968 6392 39 251 151 C ATOM 1813 NH1 ARG A 239 -15.540 8.719 -7.072 1.00 55.34 N ANISOU 1813 NH1 ARG A 239 7345 7130 6550 51 230 105 N ATOM 1814 NH2 ARG A 239 -14.585 10.370 -8.348 1.00 50.24 N ANISOU 1814 NH2 ARG A 239 6736 6496 5855 58 299 193 N ATOM 1815 N TYR A 240 -20.567 11.790 -5.893 1.00 20.52 N ANISOU 1815 N TYR A 240 2975 2586 2236 30 65 85 N ATOM 1816 CA TYR A 240 -21.266 10.736 -5.164 1.00 11.28 C ANISOU 1816 CA TYR A 240 1774 1407 1106 32 38 43 C ATOM 1817 C TYR A 240 -22.773 10.883 -5.297 1.00 18.90 C ANISOU 1817 C TYR A 240 2746 2342 2096 50 -14 22 C ATOM 1818 O TYR A 240 -23.314 11.991 -5.234 1.00 22.98 O ANISOU 1818 O TYR A 240 3274 2836 2621 44 -24 39 O ATOM 1819 CB TYR A 240 -20.862 10.711 -3.696 1.00 7.85 C ANISOU 1819 CB TYR A 240 1298 969 717 -2 60 44 C ATOM 1820 CG TYR A 240 -19.377 10.538 -3.515 1.00 8.87 C ANISOU 1820 CG TYR A 240 1413 1125 832 -20 104 61 C ATOM 1821 CD1 TYR A 240 -18.559 11.621 -3.213 1.00 11.60 C ANISOU 1821 CD1 TYR A 240 1757 1468 1184 -47 130 91 C ATOM 1822 CD2 TYR A 240 -18.787 9.290 -3.651 1.00 11.83 C ANISOU 1822 CD2 TYR A 240 1774 1523 1198 -10 115 45 C ATOM 1823 CE1 TYR A 240 -17.197 11.457 -3.057 1.00 21.20 C ANISOU 1823 CE1 TYR A 240 2952 2703 2400 -64 166 106 C ATOM 1824 CE2 TYR A 240 -17.436 9.116 -3.489 1.00 10.79 C ANISOU 1824 CE2 TYR A 240 1626 1415 1059 -24 154 60 C ATOM 1825 CZ TYR A 240 -16.641 10.195 -3.198 1.00 17.95 C ANISOU 1825 CZ TYR A 240 2527 2319 1975 -52 179 91 C ATOM 1826 OH TYR A 240 -15.290 9.993 -3.055 1.00 23.11 O ANISOU 1826 OH TYR A 240 3157 2992 2633 -66 215 105 O ATOM 1827 N SER A 241 -23.438 9.747 -5.486 1.00 11.62 N ANISOU 1827 N SER A 241 1809 1413 1192 73 -48 -16 N ATOM 1828 CA SER A 241 -24.866 9.709 -5.774 1.00 11.07 C ANISOU 1828 CA SER A 241 1739 1311 1154 95 -103 -41 C ATOM 1829 C SER A 241 -25.667 10.314 -4.637 1.00 15.32 C ANISOU 1829 C SER A 241 2247 1820 1754 73 -102 -33 C ATOM 1830 O SER A 241 -25.214 10.343 -3.486 1.00 8.11 O ANISOU 1830 O SER A 241 1306 911 862 46 -64 -21 O ATOM 1831 CB SER A 241 -25.319 8.272 -6.011 1.00 10.23 C ANISOU 1831 CB SER A 241 1610 1197 1080 118 -139 -84 C ATOM 1832 OG SER A 241 -25.283 7.520 -4.811 1.00 16.30 O ANISOU 1832 OG SER A 241 2328 1957 1910 94 -115 -87 O ATOM 1833 N ASP A 242 -26.859 10.799 -4.977 1.00 13.00 N ANISOU 1833 N ASP A 242 1960 1497 1484 89 -145 -42 N ATOM 1834 CA ASP A 242 -27.784 11.356 -4.000 1.00 12.25 C ANISOU 1834 CA ASP A 242 1836 1371 1449 77 -146 -37 C ATOM 1835 C ASP A 242 -28.175 10.286 -2.984 1.00 10.63 C ANISOU 1835 C ASP A 242 1575 1154 1309 71 -134 -52 C ATOM 1836 O ASP A 242 -28.421 10.577 -1.820 1.00 15.93 O ANISOU 1836 O ASP A 242 2220 1818 2015 57 -105 -39 O ATOM 1837 CB ASP A 242 -29.029 11.891 -4.709 1.00 10.35 C ANISOU 1837 CB ASP A 242 1608 1098 1227 101 -202 -48 C ATOM 1838 CG ASP A 242 -28.815 13.285 -5.317 1.00 16.64 C ANISOU 1838 CG ASP A 242 2453 1897 1973 103 -203 -20 C ATOM 1839 OD1 ASP A 242 -27.738 13.886 -5.098 1.00 17.40 O ANISOU 1839 OD1 ASP A 242 2566 2013 2032 81 -158 10 O ATOM 1840 OD2 ASP A 242 -29.732 13.780 -6.008 1.00 14.13 O ANISOU 1840 OD2 ASP A 242 2153 1556 1659 128 -250 -25 O ATOM 1841 N GLU A 243 -28.224 9.040 -3.436 1.00 12.05 N ANISOU 1841 N GLU A 243 1739 1333 1506 85 -155 -77 N ATOM 1842 CA GLU A 243 -28.547 7.921 -2.554 1.00 12.91 C ANISOU 1842 CA GLU A 243 1793 1427 1685 81 -141 -84 C ATOM 1843 C GLU A 243 -27.494 7.737 -1.484 1.00 8.35 C ANISOU 1843 C GLU A 243 1204 879 1088 59 -81 -60 C ATOM 1844 O GLU A 243 -27.814 7.584 -0.313 1.00 12.66 O ANISOU 1844 O GLU A 243 1716 1417 1678 52 -50 -45 O ATOM 1845 CB GLU A 243 -28.711 6.621 -3.354 1.00 13.40 C ANISOU 1845 CB GLU A 243 1841 1477 1773 102 -183 -119 C ATOM 1846 CG GLU A 243 -29.930 6.612 -4.291 1.00 14.79 C ANISOU 1846 CG GLU A 243 2017 1616 1988 130 -256 -152 C ATOM 1847 CD GLU A 243 -29.760 7.489 -5.527 1.00 22.75 C ANISOU 1847 CD GLU A 243 3090 2642 2913 151 -291 -159 C ATOM 1848 OE1 GLU A 243 -28.613 7.874 -5.848 1.00 19.82 O ANISOU 1848 OE1 GLU A 243 2763 2312 2456 146 -258 -141 O ATOM 1849 OE2 GLU A 243 -30.785 7.774 -6.189 1.00 27.28 O ANISOU 1849 OE2 GLU A 243 3669 3186 3509 175 -352 -181 O ATOM 1850 N LEU A 244 -26.231 7.754 -1.894 1.00 13.10 N ANISOU 1850 N LEU A 244 1836 1516 1625 51 -63 -56 N ATOM 1851 CA LEU A 244 -25.143 7.613 -0.948 1.00 8.89 C ANISOU 1851 CA LEU A 244 1293 1011 1074 31 -14 -37 C ATOM 1852 C LEU A 244 -25.181 8.800 0.007 1.00 10.31 C ANISOU 1852 C LEU A 244 1477 1190 1249 17 9 -16 C ATOM 1853 O LEU A 244 -24.994 8.637 1.202 1.00 9.50 O ANISOU 1853 O LEU A 244 1352 1095 1161 11 39 -6 O ATOM 1854 CB LEU A 244 -23.793 7.548 -1.666 1.00 11.46 C ANISOU 1854 CB LEU A 244 1647 1370 1337 27 -1 -35 C ATOM 1855 CG LEU A 244 -22.543 7.271 -0.809 1.00 11.20 C ANISOU 1855 CG LEU A 244 1599 1365 1290 8 43 -20 C ATOM 1856 CD1 LEU A 244 -22.757 6.098 0.104 1.00 12.83 C ANISOU 1856 CD1 LEU A 244 1764 1567 1545 12 54 -24 C ATOM 1857 CD2 LEU A 244 -21.326 7.046 -1.687 1.00 9.01 C ANISOU 1857 CD2 LEU A 244 1342 1118 964 8 56 -19 C ATOM 1858 N ASN A 245 -25.430 9.993 -0.522 1.00 10.53 N ANISOU 1858 N ASN A 245 1536 1209 1255 15 -8 -12 N ATOM 1859 CA ASN A 245 -25.444 11.176 0.333 1.00 13.90 C ANISOU 1859 CA ASN A 245 1969 1631 1682 3 8 2 C ATOM 1860 C ASN A 245 -26.565 11.106 1.357 1.00 10.79 C ANISOU 1860 C ASN A 245 1544 1216 1339 15 13 -1 C ATOM 1861 O ASN A 245 -26.403 11.525 2.493 1.00 15.19 O ANISOU 1861 O ASN A 245 2095 1780 1896 13 39 5 O ATOM 1862 CB ASN A 245 -25.545 12.474 -0.465 1.00 6.45 C ANISOU 1862 CB ASN A 245 1062 675 715 0 -11 11 C ATOM 1863 CG ASN A 245 -25.631 13.691 0.439 1.00 17.77 C ANISOU 1863 CG ASN A 245 2497 2094 2158 -10 -1 17 C ATOM 1864 OD1 ASN A 245 -24.650 14.081 1.082 1.00 15.63 O ANISOU 1864 OD1 ASN A 245 2228 1838 1874 -27 21 23 O ATOM 1865 ND2 ASN A 245 -26.808 14.288 0.506 1.00 13.06 N ANISOU 1865 ND2 ASN A 245 1901 1470 1593 3 -21 13 N ATOM 1866 N GLU A 246 -27.702 10.561 0.939 1.00 16.25 N ANISOU 1866 N GLU A 246 2217 1882 2077 32 -12 -10 N ATOM 1867 CA GLU A 246 -28.863 10.415 1.812 1.00 19.73 C ANISOU 1867 CA GLU A 246 2619 2297 2578 46 -2 -6 C ATOM 1868 C GLU A 246 -28.572 9.507 3.007 1.00 11.52 C ANISOU 1868 C GLU A 246 1547 1273 1555 49 43 7 C ATOM 1869 O GLU A 246 -28.862 9.857 4.141 1.00 18.88 O ANISOU 1869 O GLU A 246 2469 2208 2495 60 75 21 O ATOM 1870 CB GLU A 246 -30.062 9.881 1.018 1.00 26.43 C ANISOU 1870 CB GLU A 246 3444 3109 3487 62 -43 -21 C ATOM 1871 CG GLU A 246 -31.361 9.750 1.817 1.00 36.19 C ANISOU 1871 CG GLU A 246 4633 4313 4804 77 -31 -12 C ATOM 1872 CD GLU A 246 -32.451 9.001 1.054 1.00 58.63 C ANISOU 1872 CD GLU A 246 7439 7114 7725 90 -77 -29 C ATOM 1873 OE1 GLU A 246 -32.116 8.251 0.108 1.00 62.13 O ANISOU 1873 OE1 GLU A 246 7889 7557 8161 91 -113 -51 O ATOM 1874 OE2 GLU A 246 -33.643 9.162 1.403 1.00 69.32 O ANISOU 1874 OE2 GLU A 246 8754 8433 9151 103 -78 -23 O ATOM 1875 N ILE A 247 -28.002 8.338 2.743 1.00 14.72 N ANISOU 1875 N ILE A 247 1939 1690 1964 46 45 5 N ATOM 1876 CA ILE A 247 -27.783 7.351 3.795 1.00 10.17 C ANISOU 1876 CA ILE A 247 1330 1125 1410 53 86 24 C ATOM 1877 C ILE A 247 -26.745 7.886 4.787 1.00 9.63 C ANISOU 1877 C ILE A 247 1283 1094 1282 48 119 34 C ATOM 1878 O ILE A 247 -26.949 7.849 6.004 1.00 11.52 O ANISOU 1878 O ILE A 247 1509 1342 1526 65 155 52 O ATOM 1879 CB ILE A 247 -27.401 5.961 3.215 1.00 23.91 C ANISOU 1879 CB ILE A 247 3049 2861 3173 51 75 16 C ATOM 1880 CG1 ILE A 247 -27.110 4.940 4.326 1.00 30.99 C ANISOU 1880 CG1 ILE A 247 3912 3769 4095 59 120 42 C ATOM 1881 CG2 ILE A 247 -26.193 6.073 2.309 1.00 20.46 C ANISOU 1881 CG2 ILE A 247 2650 2453 2671 37 58 -2 C ATOM 1882 CD1 ILE A 247 -28.229 4.727 5.313 1.00 29.78 C ANISOU 1882 CD1 ILE A 247 3718 3591 4005 79 153 71 C ATOM 1883 N ILE A 248 -25.647 8.420 4.266 1.00 7.16 N ANISOU 1883 N ILE A 248 1005 803 914 29 106 23 N ATOM 1884 CA ILE A 248 -24.669 9.073 5.125 1.00 12.48 C ANISOU 1884 CA ILE A 248 1696 1504 1541 23 124 26 C ATOM 1885 C ILE A 248 -25.286 10.209 5.950 1.00 10.58 C ANISOU 1885 C ILE A 248 1466 1255 1298 36 129 24 C ATOM 1886 O ILE A 248 -25.011 10.326 7.141 1.00 14.92 O ANISOU 1886 O ILE A 248 2016 1823 1828 52 152 28 O ATOM 1887 CB ILE A 248 -23.463 9.604 4.331 1.00 15.78 C ANISOU 1887 CB ILE A 248 2141 1937 1918 -2 110 17 C ATOM 1888 CG1 ILE A 248 -22.779 8.452 3.584 1.00 15.75 C ANISOU 1888 CG1 ILE A 248 2127 1946 1910 -7 110 16 C ATOM 1889 CG2 ILE A 248 -22.505 10.317 5.277 1.00 14.19 C ANISOU 1889 CG2 ILE A 248 1950 1756 1686 -8 120 15 C ATOM 1890 CD1 ILE A 248 -21.493 8.833 2.847 1.00 9.58 C ANISOU 1890 CD1 ILE A 248 1366 1184 1089 -27 109 15 C ATOM 1891 N THR A 249 -26.113 11.042 5.322 1.00 9.02 N ANISOU 1891 N THR A 249 1280 1030 1117 34 106 18 N ATOM 1892 CA THR A 249 -26.761 12.138 6.031 1.00 9.98 C ANISOU 1892 CA THR A 249 1410 1139 1241 49 109 13 C ATOM 1893 C THR A 249 -27.669 11.607 7.129 1.00 11.86 C ANISOU 1893 C THR A 249 1622 1378 1509 82 144 27 C ATOM 1894 O THR A 249 -27.734 12.163 8.225 1.00 18.52 O ANISOU 1894 O THR A 249 2474 2232 2332 105 164 25 O ATOM 1895 CB THR A 249 -27.571 13.041 5.088 1.00 14.03 C ANISOU 1895 CB THR A 249 1937 1619 1774 44 77 7 C ATOM 1896 OG1 THR A 249 -26.687 13.638 4.135 1.00 13.18 O ANISOU 1896 OG1 THR A 249 1858 1513 1635 18 53 3 O ATOM 1897 CG2 THR A 249 -28.269 14.156 5.883 1.00 6.50 C ANISOU 1897 CG2 THR A 249 991 651 829 62 81 0 C ATOM 1898 N ARG A 250 -28.364 10.520 6.824 1.00 8.84 N ANISOU 1898 N ARG A 250 1204 980 1176 88 152 42 N ATOM 1899 CA ARG A 250 -29.238 9.869 7.790 1.00 11.71 C ANISOU 1899 CA ARG A 250 1530 1337 1580 119 195 67 C ATOM 1900 C ARG A 250 -28.461 9.354 9.009 1.00 16.44 C ANISOU 1900 C ARG A 250 2132 1975 2138 138 236 84 C ATOM 1901 O ARG A 250 -28.933 9.486 10.137 1.00 22.09 O ANISOU 1901 O ARG A 250 2843 2701 2849 174 276 101 O ATOM 1902 CB ARG A 250 -30.054 8.744 7.130 1.00 26.41 C ANISOU 1902 CB ARG A 250 3347 3167 3521 117 189 79 C ATOM 1903 CG ARG A 250 -31.444 8.523 7.732 1.00 40.45 C ANISOU 1903 CG ARG A 250 5080 4916 5374 145 222 105 C ATOM 1904 CD ARG A 250 -32.367 9.697 7.402 1.00 49.91 C ANISOU 1904 CD ARG A 250 6286 6088 6588 150 198 89 C ATOM 1905 NE ARG A 250 -33.297 10.018 8.485 1.00 60.36 N ANISOU 1905 NE ARG A 250 7587 7406 7939 186 248 113 N ATOM 1906 CZ ARG A 250 -34.506 9.483 8.623 1.00 66.84 C ANISOU 1906 CZ ARG A 250 8351 8191 8852 204 271 138 C ATOM 1907 NH1 ARG A 250 -35.274 9.840 9.643 1.00 67.79 N ANISOU 1907 NH1 ARG A 250 8456 8313 8990 241 325 164 N ATOM 1908 NH2 ARG A 250 -34.945 8.589 7.744 1.00 72.56 N ANISOU 1908 NH2 ARG A 250 9034 8879 9657 186 240 138 N ATOM 1909 N MET A 251 -27.273 8.786 8.797 1.00 7.95 N ANISOU 1909 N MET A 251 1065 923 1032 120 227 80 N ATOM 1910 CA MET A 251 -26.458 8.323 9.927 1.00 12.91 C ANISOU 1910 CA MET A 251 1699 1589 1618 140 258 94 C ATOM 1911 C MET A 251 -25.967 9.499 10.771 1.00 10.66 C ANISOU 1911 C MET A 251 1452 1328 1271 155 253 72 C ATOM 1912 O MET A 251 -25.688 9.341 11.951 1.00 9.53 O ANISOU 1912 O MET A 251 1318 1214 1091 190 279 82 O ATOM 1913 CB MET A 251 -25.248 7.485 9.479 1.00 6.27 C ANISOU 1913 CB MET A 251 856 765 761 116 246 91 C ATOM 1914 CG MET A 251 -25.545 6.272 8.612 1.00 6.21 C ANISOU 1914 CG MET A 251 814 734 812 103 242 102 C ATOM 1915 SD MET A 251 -23.989 5.432 8.234 1.00 17.27 S ANISOU 1915 SD MET A 251 2218 2161 2183 82 232 94 S ATOM 1916 CE MET A 251 -24.451 4.412 6.831 1.00 12.92 C ANISOU 1916 CE MET A 251 1640 1574 1695 66 207 85 C ATOM 1917 N LEU A 252 -25.864 10.676 10.169 1.00 16.01 N ANISOU 1917 N LEU A 252 2154 1991 1939 133 216 43 N ATOM 1918 CA LEU A 252 -25.407 11.859 10.888 1.00 15.94 C ANISOU 1918 CA LEU A 252 2178 1994 1884 146 201 15 C ATOM 1919 C LEU A 252 -26.565 12.694 11.447 1.00 16.57 C ANISOU 1919 C LEU A 252 2265 2059 1972 179 213 10 C ATOM 1920 O LEU A 252 -26.413 13.886 11.698 1.00 16.87 O ANISOU 1920 O LEU A 252 2329 2090 1989 183 189 -21 O ATOM 1921 CB LEU A 252 -24.505 12.711 9.986 1.00 7.91 C ANISOU 1921 CB LEU A 252 1180 965 859 103 157 -10 C ATOM 1922 CG LEU A 252 -23.184 12.012 9.666 1.00 13.78 C ANISOU 1922 CG LEU A 252 1918 1731 1588 78 150 -8 C ATOM 1923 CD1 LEU A 252 -22.324 12.879 8.792 1.00 18.42 C ANISOU 1923 CD1 LEU A 252 2519 2305 2175 38 117 -24 C ATOM 1924 CD2 LEU A 252 -22.458 11.643 10.955 1.00 17.79 C ANISOU 1924 CD2 LEU A 252 2430 2274 2057 106 161 -12 C ATOM 1925 N ASN A 253 -27.716 12.063 11.655 1.00 13.21 N ANISOU 1925 N ASN A 253 1811 1623 1585 204 252 40 N ATOM 1926 CA ASN A 253 -28.868 12.747 12.248 1.00 12.70 C ANISOU 1926 CA ASN A 253 1747 1546 1533 242 274 41 C ATOM 1927 C ASN A 253 -28.659 13.045 13.734 1.00 20.04 C ANISOU 1927 C ASN A 253 2702 2512 2400 297 302 34 C ATOM 1928 O ASN A 253 -28.082 12.236 14.455 1.00 21.36 O ANISOU 1928 O ASN A 253 2870 2713 2533 319 327 53 O ATOM 1929 CB ASN A 253 -30.140 11.908 12.052 1.00 10.09 C ANISOU 1929 CB ASN A 253 1368 1191 1274 253 311 80 C ATOM 1930 CG ASN A 253 -31.408 12.710 12.267 1.00 14.12 C ANISOU 1930 CG ASN A 253 1871 1677 1818 281 325 79 C ATOM 1931 OD1 ASN A 253 -31.766 13.027 13.401 1.00 20.32 O ANISOU 1931 OD1 ASN A 253 2666 2481 2574 332 366 85 O ATOM 1932 ND2 ASN A 253 -32.098 13.042 11.174 1.00 10.50 N ANISOU 1932 ND2 ASN A 253 1396 1176 1416 253 292 71 N ATOM 1933 N LEU A 254 -29.128 14.204 14.188 1.00 23.02 N ANISOU 1933 N LEU A 254 3103 2882 2762 325 295 7 N ATOM 1934 CA LEU A 254 -29.032 14.579 15.605 1.00 22.08 C ANISOU 1934 CA LEU A 254 3015 2799 2577 390 318 -8 C ATOM 1935 C LEU A 254 -29.745 13.613 16.555 1.00 25.59 C ANISOU 1935 C LEU A 254 3439 3268 3014 447 395 44 C ATOM 1936 O LEU A 254 -29.281 13.378 17.667 1.00 28.91 O ANISOU 1936 O LEU A 254 3886 3733 3367 499 418 47 O ATOM 1937 CB LEU A 254 -29.551 16.002 15.819 1.00 21.72 C ANISOU 1937 CB LEU A 254 2994 2733 2526 411 296 -50 C ATOM 1938 CG LEU A 254 -28.659 17.062 15.170 1.00 24.56 C ANISOU 1938 CG LEU A 254 3378 3069 2884 365 223 -100 C ATOM 1939 CD1 LEU A 254 -29.141 18.487 15.471 1.00 18.83 C ANISOU 1939 CD1 LEU A 254 2678 2319 2157 390 199 -145 C ATOM 1940 CD2 LEU A 254 -27.203 16.854 15.620 1.00 17.70 C ANISOU 1940 CD2 LEU A 254 2530 2232 1962 360 194 -123 C ATOM 1941 N LYS A 255 -30.879 13.075 16.117 1.00 24.40 N ANISOU 1941 N LYS A 255 3243 3090 2939 442 434 87 N ATOM 1942 CA LYS A 255 -31.614 12.089 16.895 1.00 14.93 C ANISOU 1942 CA LYS A 255 2012 1905 1757 491 514 148 C ATOM 1943 C LYS A 255 -31.086 10.679 16.633 1.00 17.01 C ANISOU 1943 C LYS A 255 2246 2173 2044 465 527 189 C ATOM 1944 O LYS A 255 -31.092 10.184 15.506 1.00 14.38 O ANISOU 1944 O LYS A 255 1881 1807 1778 408 498 192 O ATOM 1945 CB LYS A 255 -33.110 12.153 16.591 1.00 20.39 C ANISOU 1945 CB LYS A 255 2657 2555 2535 498 550 177 C ATOM 1946 CG LYS A 255 -33.894 13.133 17.457 1.00 33.59 C ANISOU 1946 CG LYS A 255 4349 4235 4178 561 584 165 C ATOM 1947 CD LYS A 255 -33.775 14.569 16.990 1.00 41.11 C ANISOU 1947 CD LYS A 255 5337 5169 5116 541 516 98 C ATOM 1948 CE LYS A 255 -34.541 15.493 17.928 1.00 40.92 C ANISOU 1948 CE LYS A 255 5334 5153 5060 612 551 83 C ATOM 1949 NZ LYS A 255 -34.055 15.341 19.319 1.00 35.52 N ANISOU 1949 NZ LYS A 255 4690 4528 4276 686 592 86 N ATOM 1950 N ASP A 256 -30.618 10.038 17.691 1.00 17.30 N ANISOU 1950 N ASP A 256 2297 2253 2024 512 569 219 N ATOM 1951 CA ASP A 256 -30.172 8.662 17.594 1.00 22.32 C ANISOU 1951 CA ASP A 256 2902 2893 2684 496 590 264 C ATOM 1952 C ASP A 256 -31.235 7.785 16.932 1.00 23.99 C ANISOU 1952 C ASP A 256 3045 3056 3016 473 624 313 C ATOM 1953 O ASP A 256 -30.909 6.937 16.101 1.00 30.08 O ANISOU 1953 O ASP A 256 3786 3804 3840 425 599 320 O ATOM 1954 CB ASP A 256 -29.750 8.112 18.968 1.00 24.12 C ANISOU 1954 CB ASP A 256 3154 3174 2836 566 643 302 C ATOM 1955 CG ASP A 256 -30.709 8.492 20.089 1.00 30.21 C ANISOU 1955 CG ASP A 256 3936 3966 3576 647 714 332 C ATOM 1956 OD1 ASP A 256 -30.569 7.909 21.179 1.00 35.75 O ANISOU 1956 OD1 ASP A 256 4652 4709 4223 712 771 378 O ATOM 1957 OD2 ASP A 256 -31.595 9.357 19.905 1.00 34.12 O ANISOU 1957 OD2 ASP A 256 4426 4438 4099 652 716 312 O ATOM 1958 N TYR A 257 -32.502 8.022 17.275 1.00 20.45 N ANISOU 1958 N TYR A 257 2569 2589 2614 508 675 343 N ATOM 1959 CA TYR A 257 -33.616 7.234 16.738 1.00 22.78 C ANISOU 1959 CA TYR A 257 2789 2830 3037 490 707 390 C ATOM 1960 C TYR A 257 -34.011 7.556 15.292 1.00 25.78 C ANISOU 1960 C TYR A 257 3144 3157 3495 427 637 348 C ATOM 1961 O TYR A 257 -34.829 6.848 14.719 1.00 33.69 O ANISOU 1961 O TYR A 257 4082 4109 4609 407 645 376 O ATOM 1962 CB TYR A 257 -34.843 7.304 17.659 1.00 18.67 C ANISOU 1962 CB TYR A 257 2239 2306 2549 554 796 445 C ATOM 1963 CG TYR A 257 -35.295 8.704 17.995 1.00 24.35 C ANISOU 1963 CG TYR A 257 2996 3037 3217 587 791 405 C ATOM 1964 CD1 TYR A 257 -34.959 9.296 19.204 1.00 21.31 C ANISOU 1964 CD1 TYR A 257 2670 2709 2717 656 825 398 C ATOM 1965 CD2 TYR A 257 -36.047 9.439 17.094 1.00 28.08 C ANISOU 1965 CD2 TYR A 257 3448 3464 3757 553 748 370 C ATOM 1966 CE1 TYR A 257 -35.370 10.580 19.508 1.00 28.94 C ANISOU 1966 CE1 TYR A 257 3671 3684 3642 689 816 355 C ATOM 1967 CE2 TYR A 257 -36.465 10.724 17.388 1.00 28.23 C ANISOU 1967 CE2 TYR A 257 3500 3490 3737 583 743 332 C ATOM 1968 CZ TYR A 257 -36.126 11.288 18.595 1.00 29.79 C ANISOU 1968 CZ TYR A 257 3754 3742 3825 650 777 324 C ATOM 1969 OH TYR A 257 -36.531 12.568 18.889 1.00 37.94 O ANISOU 1969 OH TYR A 257 4819 4777 4821 683 768 280 O ATOM 1970 N HIS A 258 -33.431 8.601 14.700 1.00 20.63 N ANISOU 1970 N HIS A 258 2540 2511 2787 397 567 283 N ATOM 1971 CA HIS A 258 -33.646 8.877 13.271 1.00 20.18 C ANISOU 1971 CA HIS A 258 2470 2411 2787 341 497 246 C ATOM 1972 C HIS A 258 -32.576 8.248 12.386 1.00 18.43 C ANISOU 1972 C HIS A 258 2257 2191 2554 292 446 225 C ATOM 1973 O HIS A 258 -32.767 8.101 11.184 1.00 15.78 O ANISOU 1973 O HIS A 258 1904 1820 2272 252 396 204 O ATOM 1974 CB HIS A 258 -33.716 10.376 12.981 1.00 22.86 C ANISOU 1974 CB HIS A 258 2852 2748 3087 335 453 195 C ATOM 1975 CG HIS A 258 -34.980 11.014 13.481 1.00 25.99 C ANISOU 1975 CG HIS A 258 3229 3126 3520 376 491 207 C ATOM 1976 ND1 HIS A 258 -36.131 10.319 13.662 1.00 20.28 N ANISOU 1976 ND1 HIS A 258 2441 2373 2891 396 543 256 N ATOM 1977 CD2 HIS A 258 -35.235 12.311 13.816 1.00 22.35 C ANISOU 1977 CD2 HIS A 258 2802 2670 3019 400 483 176 C ATOM 1978 CE1 HIS A 258 -37.081 11.148 14.110 1.00 25.46 C ANISOU 1978 CE1 HIS A 258 3092 3019 3562 433 572 257 C ATOM 1979 NE2 HIS A 258 -36.555 12.344 14.208 1.00 25.32 N ANISOU 1979 NE2 HIS A 258 3135 3023 3461 437 535 207 N ATOM 1980 N ARG A 259 -31.448 7.889 12.982 1.00 14.19 N ANISOU 1980 N ARG A 259 1749 1697 1946 299 457 229 N ATOM 1981 CA ARG A 259 -30.409 7.171 12.261 1.00 16.66 C ANISOU 1981 CA ARG A 259 2064 2014 2250 260 419 215 C ATOM 1982 C ARG A 259 -30.860 5.756 11.897 1.00 14.75 C ANISOU 1982 C ARG A 259 1764 1739 2101 250 437 252 C ATOM 1983 O ARG A 259 -31.635 5.137 12.623 1.00 11.91 O ANISOU 1983 O ARG A 259 1364 1368 1795 283 496 303 O ATOM 1984 CB ARG A 259 -29.145 7.123 13.111 1.00 13.45 C ANISOU 1984 CB ARG A 259 1697 1660 1752 276 428 213 C ATOM 1985 CG ARG A 259 -28.748 8.494 13.617 1.00 16.11 C ANISOU 1985 CG ARG A 259 2087 2024 2009 292 409 174 C ATOM 1986 CD ARG A 259 -27.573 8.436 14.567 1.00 22.96 C ANISOU 1986 CD ARG A 259 2991 2941 2793 316 412 168 C ATOM 1987 NE ARG A 259 -27.428 9.701 15.278 1.00 23.24 N ANISOU 1987 NE ARG A 259 3071 2997 2763 346 397 131 N ATOM 1988 CZ ARG A 259 -26.855 9.829 16.466 1.00 20.83 C ANISOU 1988 CZ ARG A 259 2799 2735 2382 395 409 126 C ATOM 1989 NH1 ARG A 259 -26.358 8.764 17.076 1.00 16.04 N ANISOU 1989 NH1 ARG A 259 2186 2157 1752 419 439 161 N ATOM 1990 NH2 ARG A 259 -26.792 11.020 17.044 1.00 21.83 N ANISOU 1990 NH2 ARG A 259 2965 2873 2455 424 387 83 N ATOM 1991 N PRO A 260 -30.368 5.239 10.768 1.00 13.24 N ANISOU 1991 N PRO A 260 1566 1531 1934 209 387 227 N ATOM 1992 CA PRO A 260 -30.720 3.876 10.359 1.00 15.68 C ANISOU 1992 CA PRO A 260 1819 1802 2336 200 392 251 C ATOM 1993 C PRO A 260 -30.100 2.859 11.320 1.00 15.29 C ANISOU 1993 C PRO A 260 1758 1777 2273 222 443 296 C ATOM 1994 O PRO A 260 -29.001 3.088 11.837 1.00 16.53 O ANISOU 1994 O PRO A 260 1959 1983 2338 229 445 289 O ATOM 1995 CB PRO A 260 -30.075 3.741 8.972 1.00 12.36 C ANISOU 1995 CB PRO A 260 1414 1372 1910 159 321 202 C ATOM 1996 CG PRO A 260 -29.421 5.059 8.677 1.00 16.40 C ANISOU 1996 CG PRO A 260 1986 1915 2330 145 289 163 C ATOM 1997 CD PRO A 260 -29.294 5.812 9.947 1.00 11.65 C ANISOU 1997 CD PRO A 260 1410 1348 1667 175 330 179 C ATOM 1998 N SER A 261 -30.809 1.766 11.576 1.00 10.85 N ANISOU 1998 N SER A 261 1136 1178 1807 235 482 345 N ATOM 1999 CA SER A 261 -30.218 0.630 12.260 1.00 11.76 C ANISOU 1999 CA SER A 261 1235 1307 1927 251 523 390 C ATOM 2000 C SER A 261 -29.353 -0.088 11.244 1.00 15.76 C ANISOU 2000 C SER A 261 1741 1803 2445 213 467 353 C ATOM 2001 O SER A 261 -29.469 0.175 10.043 1.00 15.10 O ANISOU 2001 O SER A 261 1661 1695 2382 181 405 301 O ATOM 2002 CB SER A 261 -31.299 -0.328 12.753 1.00 13.66 C ANISOU 2002 CB SER A 261 1402 1500 2287 274 583 459 C ATOM 2003 OG SER A 261 -32.003 -0.898 11.662 1.00 19.18 O ANISOU 2003 OG SER A 261 2046 2132 3109 242 540 439 O ATOM 2004 N VAL A 262 -28.503 -0.991 11.733 1.00 18.02 N ANISOU 2004 N VAL A 262 2025 2107 2714 222 489 380 N ATOM 2005 CA VAL A 262 -27.722 -1.904 10.896 1.00 15.14 C ANISOU 2005 CA VAL A 262 1651 1729 2374 194 448 353 C ATOM 2006 C VAL A 262 -28.581 -2.591 9.828 1.00 15.25 C ANISOU 2006 C VAL A 262 1610 1673 2512 172 410 335 C ATOM 2007 O VAL A 262 -28.209 -2.635 8.658 1.00 20.63 O ANISOU 2007 O VAL A 262 2304 2344 3191 145 347 277 O ATOM 2008 CB VAL A 262 -27.029 -2.985 11.761 1.00 16.25 C ANISOU 2008 CB VAL A 262 1777 1884 2513 217 491 404 C ATOM 2009 CG1 VAL A 262 -26.726 -4.221 10.931 1.00 25.04 C ANISOU 2009 CG1 VAL A 262 2852 2956 3706 194 459 390 C ATOM 2010 CG2 VAL A 262 -25.760 -2.433 12.390 1.00 16.58 C ANISOU 2010 CG2 VAL A 262 1878 1995 2425 229 492 393 C ATOM 2011 N GLU A 263 -29.725 -3.130 10.244 1.00 14.16 N ANISOU 2011 N GLU A 263 1411 1486 2484 188 449 384 N ATOM 2012 CA GLU A 263 -30.661 -3.782 9.329 1.00 17.35 C ANISOU 2012 CA GLU A 263 1753 1814 3025 170 410 366 C ATOM 2013 C GLU A 263 -31.195 -2.836 8.239 1.00 17.33 C ANISOU 2013 C GLU A 263 1771 1799 3016 151 342 301 C ATOM 2014 O GLU A 263 -31.267 -3.203 7.074 1.00 20.71 O ANISOU 2014 O GLU A 263 2187 2191 3489 132 273 248 O ATOM 2015 CB GLU A 263 -31.826 -4.391 10.114 1.00 22.58 C ANISOU 2015 CB GLU A 263 2340 2425 3814 192 474 440 C ATOM 2016 CG GLU A 263 -31.472 -5.645 10.914 1.00 27.83 C ANISOU 2016 CG GLU A 263 2968 3079 4528 210 531 508 C ATOM 2017 CD GLU A 263 -30.666 -5.356 12.178 1.00 38.63 C ANISOU 2017 CD GLU A 263 4386 4521 5771 244 598 558 C ATOM 2018 OE1 GLU A 263 -30.664 -4.199 12.659 1.00 27.36 O ANISOU 2018 OE1 GLU A 263 3009 3145 4240 261 616 552 O ATOM 2019 OE2 GLU A 263 -30.032 -6.298 12.700 1.00 50.70 O ANISOU 2019 OE2 GLU A 263 5904 6054 7305 257 630 600 O ATOM 2020 N GLU A 264 -31.559 -1.620 8.626 1.00 9.56 N ANISOU 2020 N GLU A 264 818 844 1971 160 360 304 N ATOM 2021 CA GLU A 264 -32.112 -0.636 7.695 1.00 9.95 C ANISOU 2021 CA GLU A 264 886 881 2012 146 302 251 C ATOM 2022 C GLU A 264 -31.044 -0.203 6.702 1.00 10.91 C ANISOU 2022 C GLU A 264 1071 1038 2035 124 240 189 C ATOM 2023 O GLU A 264 -31.336 0.099 5.549 1.00 15.25 O ANISOU 2023 O GLU A 264 1631 1567 2596 111 174 139 O ATOM 2024 CB GLU A 264 -32.673 0.583 8.457 1.00 8.44 C ANISOU 2024 CB GLU A 264 716 714 1776 166 342 273 C ATOM 2025 CG GLU A 264 -34.058 0.333 9.069 1.00 21.38 C ANISOU 2025 CG GLU A 264 2285 2306 3534 188 392 324 C ATOM 2026 CD GLU A 264 -34.462 1.321 10.152 1.00 26.23 C ANISOU 2026 CD GLU A 264 2919 2954 4094 220 455 359 C ATOM 2027 OE1 GLU A 264 -35.595 1.189 10.655 1.00 35.12 O ANISOU 2027 OE1 GLU A 264 3988 4044 5313 242 503 405 O ATOM 2028 OE2 GLU A 264 -33.661 2.209 10.516 1.00 23.57 O ANISOU 2028 OE2 GLU A 264 2651 2675 3628 226 458 341 O ATOM 2029 N ILE A 265 -29.799 -0.178 7.169 1.00 9.55 N ANISOU 2029 N ILE A 265 941 919 1767 124 263 196 N ATOM 2030 CA ILE A 265 -28.679 0.188 6.322 1.00 10.58 C ANISOU 2030 CA ILE A 265 1126 1085 1809 105 218 147 C ATOM 2031 C ILE A 265 -28.513 -0.859 5.220 1.00 12.71 C ANISOU 2031 C ILE A 265 1375 1322 2131 94 169 112 C ATOM 2032 O ILE A 265 -28.489 -0.520 4.041 1.00 10.95 O ANISOU 2032 O ILE A 265 1178 1095 1888 85 111 62 O ATOM 2033 CB ILE A 265 -27.382 0.289 7.127 1.00 17.98 C ANISOU 2033 CB ILE A 265 2099 2080 2653 108 254 164 C ATOM 2034 CG1 ILE A 265 -27.374 1.544 7.998 1.00 11.18 C ANISOU 2034 CG1 ILE A 265 1274 1255 1719 120 282 176 C ATOM 2035 CG2 ILE A 265 -26.209 0.347 6.200 1.00 20.21 C ANISOU 2035 CG2 ILE A 265 2420 2389 2872 88 214 121 C ATOM 2036 CD1 ILE A 265 -26.185 1.591 8.946 1.00 12.89 C ANISOU 2036 CD1 ILE A 265 1519 1524 1854 130 311 192 C ATOM 2037 N LEU A 266 -28.424 -2.129 5.615 1.00 10.47 N ANISOU 2037 N LEU A 266 1047 1015 1916 101 191 138 N ATOM 2038 CA LEU A 266 -28.208 -3.236 4.681 1.00 10.19 C ANISOU 2038 CA LEU A 266 989 946 1937 95 144 102 C ATOM 2039 C LEU A 266 -29.370 -3.455 3.710 1.00 16.57 C ANISOU 2039 C LEU A 266 1762 1691 2844 95 83 64 C ATOM 2040 O LEU A 266 -29.187 -4.056 2.656 1.00 17.19 O ANISOU 2040 O LEU A 266 1840 1747 2943 95 23 11 O ATOM 2041 CB LEU A 266 -27.913 -4.529 5.438 1.00 11.93 C ANISOU 2041 CB LEU A 266 1163 1148 2220 103 185 145 C ATOM 2042 CG LEU A 266 -26.745 -4.467 6.413 1.00 14.41 C ANISOU 2042 CG LEU A 266 1509 1523 2445 109 237 181 C ATOM 2043 CD1 LEU A 266 -26.619 -5.759 7.197 1.00 14.86 C ANISOU 2043 CD1 LEU A 266 1517 1555 2573 123 279 233 C ATOM 2044 CD2 LEU A 266 -25.462 -4.164 5.672 1.00 14.25 C ANISOU 2044 CD2 LEU A 266 1543 1548 2323 97 204 133 C ATOM 2045 N GLU A 267 -30.558 -2.969 4.069 1.00 15.35 N ANISOU 2045 N GLU A 267 1576 1506 2749 100 94 87 N ATOM 2046 CA GLU A 267 -31.714 -3.029 3.176 1.00 22.79 C ANISOU 2046 CA GLU A 267 2484 2387 3786 101 30 48 C ATOM 2047 C GLU A 267 -31.668 -1.946 2.100 1.00 22.12 C ANISOU 2047 C GLU A 267 2461 2328 3616 99 -31 -8 C ATOM 2048 O GLU A 267 -32.538 -1.887 1.235 1.00 16.98 O ANISOU 2048 O GLU A 267 1794 1634 3024 105 -97 -48 O ATOM 2049 CB GLU A 267 -33.027 -2.910 3.961 1.00 27.20 C ANISOU 2049 CB GLU A 267 2979 2902 4452 108 68 97 C ATOM 2050 CG GLU A 267 -33.252 -4.042 4.939 1.00 48.60 C ANISOU 2050 CG GLU A 267 5620 5576 7269 115 131 161 C ATOM 2051 CD GLU A 267 -34.329 -3.738 5.965 1.00 66.22 C ANISOU 2051 CD GLU A 267 7802 7786 9573 128 199 229 C ATOM 2052 OE1 GLU A 267 -35.338 -3.089 5.611 1.00 70.59 O ANISOU 2052 OE1 GLU A 267 8337 8310 10172 129 171 212 O ATOM 2053 OE2 GLU A 267 -34.166 -4.166 7.129 1.00 71.74 O ANISOU 2053 OE2 GLU A 267 8479 8497 10281 142 283 301 O ATOM 2054 N ASN A 268 -30.663 -1.085 2.146 1.00 19.38 N ANISOU 2054 N ASN A 268 2182 2047 3133 93 -12 -9 N ATOM 2055 CA ASN A 268 -30.586 -0.028 1.143 1.00 13.02 C ANISOU 2055 CA ASN A 268 1436 1265 2247 93 -61 -50 C ATOM 2056 C ASN A 268 -30.233 -0.602 -0.240 1.00 15.69 C ANISOU 2056 C ASN A 268 1796 1595 2572 102 -132 -112 C ATOM 2057 O ASN A 268 -29.329 -1.432 -0.356 1.00 17.74 O ANISOU 2057 O ASN A 268 2059 1869 2813 103 -126 -121 O ATOM 2058 CB ASN A 268 -29.608 1.071 1.593 1.00 15.39 C ANISOU 2058 CB ASN A 268 1797 1631 2422 83 -18 -31 C ATOM 2059 CG ASN A 268 -29.702 2.322 0.739 1.00 16.26 C ANISOU 2059 CG ASN A 268 1959 1756 2462 83 -57 -57 C ATOM 2060 OD1 ASN A 268 -29.212 2.355 -0.387 1.00 15.35 O ANISOU 2060 OD1 ASN A 268 1883 1654 2295 87 -100 -93 O ATOM 2061 ND2 ASN A 268 -30.337 3.355 1.271 1.00 10.70 N ANISOU 2061 ND2 ASN A 268 1258 1050 1756 82 -39 -36 N ATOM 2062 N PRO A 269 -30.963 -0.175 -1.288 1.00 15.16 N ANISOU 2062 N PRO A 269 1743 1505 2512 115 -202 -155 N ATOM 2063 CA PRO A 269 -30.772 -0.628 -2.675 1.00 14.33 C ANISOU 2063 CA PRO A 269 1666 1393 2386 136 -279 -219 C ATOM 2064 C PRO A 269 -29.356 -0.412 -3.205 1.00 15.43 C ANISOU 2064 C PRO A 269 1874 1597 2393 139 -264 -230 C ATOM 2065 O PRO A 269 -28.979 -1.037 -4.189 1.00 18.92 O ANISOU 2065 O PRO A 269 2337 2040 2813 161 -310 -278 O ATOM 2066 CB PRO A 269 -31.773 0.232 -3.461 1.00 22.55 C ANISOU 2066 CB PRO A 269 2724 2414 3429 152 -342 -247 C ATOM 2067 CG PRO A 269 -32.829 0.586 -2.488 1.00 8.93 C ANISOU 2067 CG PRO A 269 944 654 1794 139 -311 -206 C ATOM 2068 CD PRO A 269 -32.107 0.749 -1.172 1.00 22.78 C ANISOU 2068 CD PRO A 269 2697 2447 3513 117 -214 -145 C ATOM 2069 N LEU A 270 -28.583 0.452 -2.553 1.00 13.33 N ANISOU 2069 N LEU A 270 1639 1380 2044 120 -200 -187 N ATOM 2070 CA LEU A 270 -27.183 0.666 -2.918 1.00 12.19 C ANISOU 2070 CA LEU A 270 1549 1294 1791 118 -175 -187 C ATOM 2071 C LEU A 270 -26.311 -0.565 -2.669 1.00 8.51 C ANISOU 2071 C LEU A 270 1059 833 1340 118 -154 -191 C ATOM 2072 O LEU A 270 -25.346 -0.807 -3.389 1.00 8.15 O ANISOU 2072 O LEU A 270 1048 819 1228 129 -158 -213 O ATOM 2073 CB LEU A 270 -26.605 1.842 -2.124 1.00 15.06 C ANISOU 2073 CB LEU A 270 1937 1697 2087 95 -116 -141 C ATOM 2074 CG LEU A 270 -26.930 3.254 -2.594 1.00 15.58 C ANISOU 2074 CG LEU A 270 2047 1774 2100 95 -131 -137 C ATOM 2075 CD1 LEU A 270 -26.406 4.257 -1.597 1.00 12.46 C ANISOU 2075 CD1 LEU A 270 1663 1407 1664 71 -75 -95 C ATOM 2076 CD2 LEU A 270 -26.334 3.489 -3.948 1.00 16.27 C ANISOU 2076 CD2 LEU A 270 2189 1887 2104 115 -161 -163 C ATOM 2077 N ILE A 271 -26.652 -1.320 -1.631 1.00 9.30 N ANISOU 2077 N ILE A 271 1101 903 1528 107 -126 -164 N ATOM 2078 CA ILE A 271 -25.831 -2.417 -1.135 1.00 16.12 C ANISOU 2078 CA ILE A 271 1939 1772 2413 104 -95 -153 C ATOM 2079 C ILE A 271 -26.117 -3.730 -1.881 1.00 16.06 C ANISOU 2079 C ILE A 271 1901 1718 2482 125 -149 -202 C ATOM 2080 O ILE A 271 -27.197 -4.300 -1.766 1.00 16.12 O ANISOU 2080 O ILE A 271 1857 1665 2604 128 -178 -208 O ATOM 2081 CB ILE A 271 -26.027 -2.565 0.397 1.00 9.80 C ANISOU 2081 CB ILE A 271 1095 964 1664 89 -33 -92 C ATOM 2082 CG1 ILE A 271 -25.612 -1.250 1.082 1.00 9.33 C ANISOU 2082 CG1 ILE A 271 1073 954 1518 75 12 -58 C ATOM 2083 CG2 ILE A 271 -25.266 -3.783 0.948 1.00 9.57 C ANISOU 2083 CG2 ILE A 271 1035 933 1666 90 -3 -76 C ATOM 2084 CD1 ILE A 271 -25.450 -1.320 2.576 1.00 13.39 C ANISOU 2084 CD1 ILE A 271 1564 1481 2044 71 74 -3 C ATOM 2085 N LEU A 272 -25.138 -4.190 -2.653 1.00 15.56 N ANISOU 2085 N LEU A 272 1869 1681 2362 140 -163 -237 N ATOM 2086 CA LEU A 272 -25.285 -5.395 -3.459 1.00 17.00 C ANISOU 2086 CA LEU A 272 2033 1823 2605 165 -222 -295 C ATOM 2087 C LEU A 272 -24.327 -6.475 -2.968 1.00 17.87 C ANISOU 2087 C LEU A 272 2117 1937 2736 163 -186 -283 C ATOM 2088 O LEU A 272 -23.453 -6.207 -2.150 1.00 8.12 O ANISOU 2088 O LEU A 272 890 745 1452 144 -121 -235 O ATOM 2089 CB LEU A 272 -25.046 -5.075 -4.938 1.00 20.12 C ANISOU 2089 CB LEU A 272 2490 2243 2911 199 -277 -356 C ATOM 2090 CG LEU A 272 -26.029 -4.046 -5.504 1.00 17.59 C ANISOU 2090 CG LEU A 272 2196 1915 2570 207 -320 -369 C ATOM 2091 CD1 LEU A 272 -25.661 -3.619 -6.920 1.00 10.01 C ANISOU 2091 CD1 LEU A 272 1310 993 1501 247 -363 -417 C ATOM 2092 CD2 LEU A 272 -27.448 -4.615 -5.452 1.00 18.05 C ANISOU 2092 CD2 LEU A 272 2195 1896 2768 212 -380 -394 C ATOM 2093 N GLU A 273 -24.496 -7.691 -3.473 1.00 12.49 N ANISOU 2093 N GLU A 273 1405 1208 2132 184 -234 -331 N ATOM 2094 CA GLU A 273 -23.701 -8.832 -3.023 1.00 16.59 C ANISOU 2094 CA GLU A 273 1893 1719 2691 184 -207 -321 C ATOM 2095 C GLU A 273 -22.193 -8.580 -3.118 1.00 17.95 C ANISOU 2095 C GLU A 273 2113 1965 2744 185 -162 -313 C ATOM 2096 O GLU A 273 -21.452 -8.861 -2.180 1.00 15.14 O ANISOU 2096 O GLU A 273 1737 1626 2389 169 -105 -266 O ATOM 2097 CB GLU A 273 -24.077 -10.087 -3.816 1.00 9.75 C ANISOU 2097 CB GLU A 273 997 790 1919 212 -281 -391 C ATOM 2098 CG GLU A 273 -23.686 -11.411 -3.161 1.00 15.63 C ANISOU 2098 CG GLU A 273 1683 1495 2759 209 -259 -373 C ATOM 2099 CD GLU A 273 -22.192 -11.691 -3.222 1.00 23.06 C ANISOU 2099 CD GLU A 273 2657 2492 3612 217 -221 -374 C ATOM 2100 OE1 GLU A 273 -21.685 -12.385 -2.318 1.00 21.06 O ANISOU 2100 OE1 GLU A 273 2366 2230 3406 205 -175 -329 O ATOM 2101 OE2 GLU A 273 -21.530 -11.217 -4.171 1.00 28.53 O ANISOU 2101 OE2 GLU A 273 3412 3237 4191 239 -234 -416 O ATOM 2102 N HIS A 274 -21.750 -8.046 -4.253 1.00 16.32 N ANISOU 2102 N HIS A 274 1966 1798 2435 208 -185 -357 N ATOM 2103 CA HIS A 274 -20.331 -7.828 -4.519 1.00 13.29 C ANISOU 2103 CA HIS A 274 1625 1480 1946 215 -143 -352 C ATOM 2104 C HIS A 274 -19.665 -6.798 -3.600 1.00 13.08 C ANISOU 2104 C HIS A 274 1609 1503 1857 180 -73 -284 C ATOM 2105 O HIS A 274 -18.444 -6.721 -3.560 1.00 12.05 O ANISOU 2105 O HIS A 274 1495 1418 1665 178 -32 -270 O ATOM 2106 CB HIS A 274 -20.113 -7.463 -5.999 1.00 11.74 C ANISOU 2106 CB HIS A 274 1491 1314 1656 255 -180 -408 C ATOM 2107 CG HIS A 274 -20.474 -6.052 -6.339 1.00 15.56 C ANISOU 2107 CG HIS A 274 2022 1829 2064 249 -178 -390 C ATOM 2108 ND1 HIS A 274 -21.773 -5.642 -6.559 1.00 9.00 N ANISOU 2108 ND1 HIS A 274 1188 960 1269 252 -229 -405 N ATOM 2109 CD2 HIS A 274 -19.702 -4.947 -6.503 1.00 13.13 C ANISOU 2109 CD2 HIS A 274 1758 1578 1651 241 -130 -356 C ATOM 2110 CE1 HIS A 274 -21.785 -4.349 -6.823 1.00 19.26 C ANISOU 2110 CE1 HIS A 274 2534 2297 2487 246 -213 -381 C ATOM 2111 NE2 HIS A 274 -20.546 -3.904 -6.800 1.00 13.86 N ANISOU 2111 NE2 HIS A 274 1878 1669 1719 239 -153 -350 N ATOM 2112 N HIS A 275 -20.463 -6.013 -2.872 1.00 10.74 N ANISOU 2112 N HIS A 275 1303 1197 1581 155 -62 -245 N ATOM 2113 CA HIS A 275 -19.930 -5.102 -1.853 1.00 14.12 C ANISOU 2113 CA HIS A 275 1737 1664 1964 125 -3 -187 C ATOM 2114 C HIS A 275 -19.547 -5.841 -0.563 1.00 17.62 C ANISOU 2114 C HIS A 275 2134 2100 2460 112 37 -145 C ATOM 2115 O HIS A 275 -18.866 -5.289 0.295 1.00 17.37 O ANISOU 2115 O HIS A 275 2109 2105 2388 95 81 -104 O ATOM 2116 CB HIS A 275 -20.928 -3.986 -1.522 1.00 10.44 C ANISOU 2116 CB HIS A 275 1279 1189 1497 110 -6 -164 C ATOM 2117 CG HIS A 275 -21.244 -3.084 -2.678 1.00 13.99 C ANISOU 2117 CG HIS A 275 1778 1651 1885 122 -40 -194 C ATOM 2118 ND1 HIS A 275 -22.530 -2.839 -3.096 1.00 10.42 N ANISOU 2118 ND1 HIS A 275 1324 1162 1472 131 -88 -215 N ATOM 2119 CD2 HIS A 275 -20.431 -2.372 -3.497 1.00 7.29 C ANISOU 2119 CD2 HIS A 275 980 848 942 130 -31 -201 C ATOM 2120 CE1 HIS A 275 -22.503 -2.004 -4.126 1.00 9.19 C ANISOU 2120 CE1 HIS A 275 1222 1030 1241 146 -111 -235 C ATOM 2121 NE2 HIS A 275 -21.247 -1.718 -4.393 1.00 9.54 N ANISOU 2121 NE2 HIS A 275 1297 1123 1203 146 -74 -224 N ATOM 2122 N HIS A 276 -19.995 -7.086 -0.432 1.00 18.60 N ANISOU 2122 N HIS A 276 2214 2174 2678 123 19 -155 N ATOM 2123 CA HIS A 276 -19.705 -7.898 0.753 1.00 16.18 C ANISOU 2123 CA HIS A 276 1863 1855 2428 118 56 -109 C ATOM 2124 C HIS A 276 -18.343 -8.538 0.637 1.00 7.45 C ANISOU 2124 C HIS A 276 761 778 1291 126 72 -118 C ATOM 2125 O HIS A 276 -17.693 -8.448 -0.396 1.00 14.34 O ANISOU 2125 O HIS A 276 1666 1676 2106 138 56 -161 O ATOM 2126 CB HIS A 276 -20.760 -9.004 0.946 1.00 10.03 C ANISOU 2126 CB HIS A 276 1028 1003 1781 126 34 -108 C ATOM 2127 CG HIS A 276 -22.107 -8.484 1.322 1.00 7.88 C ANISOU 2127 CG HIS A 276 736 698 1561 117 30 -85 C ATOM 2128 ND1 HIS A 276 -22.874 -7.727 0.462 1.00 8.45 N ANISOU 2128 ND1 HIS A 276 832 762 1615 119 -14 -124 N ATOM 2129 CD2 HIS A 276 -22.821 -8.589 2.468 1.00 7.93 C ANISOU 2129 CD2 HIS A 276 701 679 1633 111 68 -25 C ATOM 2130 CE1 HIS A 276 -24.000 -7.389 1.061 1.00 9.91 C ANISOU 2130 CE1 HIS A 276 988 916 1860 111 -4 -91 C ATOM 2131 NE2 HIS A 276 -23.993 -7.898 2.279 1.00 12.91 N ANISOU 2131 NE2 HIS A 276 1328 1285 2290 107 48 -30 N ATOM 2132 N HIS A 277 -17.930 -9.211 1.700 1.00 14.14 N ANISOU 2132 N HIS A 277 1575 1622 2177 124 106 -75 N ATOM 2133 CA HIS A 277 -16.634 -9.876 1.723 1.00 11.47 C ANISOU 2133 CA HIS A 277 1232 1307 1818 132 122 -79 C ATOM 2134 C HIS A 277 -16.614 -11.019 0.717 1.00 17.01 C ANISOU 2134 C HIS A 277 1920 1971 2572 155 83 -135 C ATOM 2135 O HIS A 277 -17.646 -11.632 0.425 1.00 13.10 O ANISOU 2135 O HIS A 277 1397 1416 2163 163 46 -156 O ATOM 2136 CB HIS A 277 -16.315 -10.395 3.125 1.00 11.65 C ANISOU 2136 CB HIS A 277 1222 1329 1875 130 162 -17 C ATOM 2137 CG HIS A 277 -16.997 -11.684 3.464 1.00 10.29 C ANISOU 2137 CG HIS A 277 998 1092 1821 142 156 0 C ATOM 2138 ND1 HIS A 277 -16.421 -12.918 3.244 1.00 11.69 N ANISOU 2138 ND1 HIS A 277 1148 1244 2051 158 146 -16 N ATOM 2139 CD2 HIS A 277 -18.214 -11.926 4.018 1.00 11.82 C ANISOU 2139 CD2 HIS A 277 1157 1236 2098 141 161 34 C ATOM 2140 CE1 HIS A 277 -17.259 -13.867 3.642 1.00 13.83 C ANISOU 2140 CE1 HIS A 277 1368 1448 2437 164 143 8 C ATOM 2141 NE2 HIS A 277 -18.348 -13.293 4.109 1.00 12.19 N ANISOU 2141 NE2 HIS A 277 1154 1226 2252 154 154 41 N ATOM 2142 N HIS A 278 -15.433 -11.274 0.172 1.00 10.98 N ANISOU 2142 N HIS A 278 1173 1240 1761 168 88 -162 N ATOM 2143 CA HIS A 278 -15.201 -12.456 -0.645 1.00 17.88 C ANISOU 2143 CA HIS A 278 2032 2082 2679 196 56 -215 C ATOM 2144 C HIS A 278 -13.831 -12.988 -0.303 1.00 23.96 C ANISOU 2144 C HIS A 278 2791 2881 3431 202 89 -201 C ATOM 2145 O HIS A 278 -12.824 -12.336 -0.560 1.00 20.82 O ANISOU 2145 O HIS A 278 2422 2541 2948 201 116 -201 O ATOM 2146 CB HIS A 278 -15.269 -12.114 -2.123 1.00 17.94 C ANISOU 2146 CB HIS A 278 2084 2104 2627 220 19 -284 C ATOM 2147 CG HIS A 278 -16.626 -11.672 -2.564 1.00 20.89 C ANISOU 2147 CG HIS A 278 2469 2445 3024 219 -26 -306 C ATOM 2148 ND1 HIS A 278 -17.003 -10.344 -2.594 1.00 17.11 N ANISOU 2148 ND1 HIS A 278 2025 1998 2479 202 -16 -286 N ATOM 2149 CD2 HIS A 278 -17.702 -12.379 -2.964 1.00 19.84 C ANISOU 2149 CD2 HIS A 278 2311 2246 2983 234 -84 -346 C ATOM 2150 CE1 HIS A 278 -18.252 -10.257 -3.016 1.00 23.63 C ANISOU 2150 CE1 HIS A 278 2849 2782 3349 208 -65 -313 C ATOM 2151 NE2 HIS A 278 -18.701 -11.485 -3.245 1.00 23.96 N ANISOU 2151 NE2 HIS A 278 2852 2762 3488 227 -109 -351 N ATOM 2152 N HIS A 279 -13.795 -14.158 0.314 1.00 29.65 N ANISOU 2152 N HIS A 279 3465 3560 4241 209 90 -183 N ATOM 2153 CA HIS A 279 -12.529 -14.738 0.727 1.00 42.30 C ANISOU 2153 CA HIS A 279 5051 5184 5836 217 119 -167 C ATOM 2154 C HIS A 279 -12.263 -15.965 -0.115 1.00 50.60 C ANISOU 2154 C HIS A 279 6085 6198 6940 249 88 -225 C ATOM 2155 O HIS A 279 -12.880 -17.005 0.112 1.00 54.94 O ANISOU 2155 O HIS A 279 6595 6682 7599 257 64 -226 O ATOM 2156 CB HIS A 279 -12.556 -15.111 2.216 1.00 44.93 C ANISOU 2156 CB HIS A 279 5347 5504 6221 206 150 -92 C ATOM 2157 CG HIS A 279 -12.417 -13.941 3.143 1.00 41.94 C ANISOU 2157 CG HIS A 279 4988 5175 5771 184 184 -38 C ATOM 2158 ND1 HIS A 279 -13.494 -13.195 3.574 1.00 34.42 N ANISOU 2158 ND1 HIS A 279 4045 4215 4818 169 187 -11 N ATOM 2159 CD2 HIS A 279 -11.320 -13.390 3.731 1.00 41.44 C ANISOU 2159 CD2 HIS A 279 4936 5167 5640 178 212 -12 C ATOM 2160 CE1 HIS A 279 -13.068 -12.232 4.382 1.00 33.54 C ANISOU 2160 CE1 HIS A 279 3953 4154 4637 156 215 27 C ATOM 2161 NE2 HIS A 279 -11.764 -12.336 4.493 1.00 39.98 N ANISOU 2161 NE2 HIS A 279 4771 5006 5414 161 227 26 N ATOM 2162 OXT HIS A 279 -11.439 -15.944 -1.030 1.00 52.44 O ANISOU 2162 OXT HIS A 279 6345 6464 7115 270 86 -272 O TER 2163 HIS A 279 HETATM 2164 O HOH A2001 10.621 -15.194 16.755 1.00 25.61 O HETATM 2165 O HOH A2002 15.215 -13.739 10.663 1.00 24.57 O HETATM 2166 O HOH A2003 -5.558 5.047 23.846 1.00 53.22 O HETATM 2167 O HOH A2004 4.386 -1.809 25.019 1.00 46.16 O HETATM 2168 O HOH A2005 1.204 -2.147 17.536 1.00 51.26 O HETATM 2169 O HOH A2006 10.534 -9.151 17.943 1.00 39.32 O HETATM 2170 O HOH A2007 3.427 -10.204 2.595 1.00 44.70 O HETATM 2171 O HOH A2008 -21.400 -10.874 4.825 1.00 19.22 O HETATM 2172 O HOH A2009 -1.236 -19.126 14.597 1.00 27.41 O HETATM 2173 O HOH A2010 0.274 -24.260 12.190 1.00 42.80 O HETATM 2174 O HOH A2011 5.200 -22.430 12.792 1.00 44.24 O HETATM 2175 O HOH A2012 0.196 -15.974 3.794 1.00 25.90 O HETATM 2176 O HOH A2013 -2.683 -13.108 7.583 1.00 16.74 O HETATM 2177 O HOH A2014 -20.332 4.087 -8.798 1.00 24.72 O HETATM 2178 O HOH A2015 4.314 -1.982 31.308 1.00 41.79 O HETATM 2179 O HOH A2016 4.067 -6.964 35.544 1.00 29.53 O HETATM 2180 O HOH A2017 -11.949 -16.638 25.031 1.00 45.64 O HETATM 2181 O HOH A2018 -13.960 -17.092 18.078 1.00 52.74 O HETATM 2182 O HOH A2019 -10.846 -12.782 16.203 1.00 37.13 O HETATM 2183 O HOH A2020 -19.226 -8.880 4.269 1.00 19.00 O HETATM 2184 O HOH A2021 -12.214 -12.137 13.230 1.00 22.44 O HETATM 2185 O HOH A2022 -8.161 -18.654 8.920 1.00 46.97 O HETATM 2186 O HOH A2023 -5.056 -18.828 21.327 1.00 31.82 O HETATM 2187 O HOH A2024 4.491 -16.031 36.843 1.00 51.98 O HETATM 2188 O HOH A2025 -3.968 -6.521 11.018 1.00 23.62 O HETATM 2189 O HOH A2026 -32.160 13.417 6.830 1.00 27.77 O HETATM 2190 O HOH A2027 -2.010 -5.637 9.134 1.00 15.07 O HETATM 2191 O HOH A2028 -3.998 -8.998 3.517 1.00 12.75 O HETATM 2192 O HOH A2029 -2.305 -10.324 1.572 1.00 33.40 O HETATM 2193 O HOH A2030 -0.859 -1.177 0.859 1.00 31.01 O HETATM 2194 O HOH A2031 -3.504 1.855 3.214 1.00 24.95 O HETATM 2195 O HOH A2032 -0.921 0.355 9.886 1.00 53.40 O HETATM 2196 O HOH A2033 -35.479 3.105 6.053 1.00 26.91 O HETATM 2197 O HOH A2034 -0.791 7.368 2.134 1.00 36.14 O HETATM 2198 O HOH A2035 -8.856 5.945 -6.004 1.00 38.48 O HETATM 2199 O HOH A2036 -13.704 17.575 -0.327 1.00 26.73 O HETATM 2200 O HOH A2037 -12.886 7.935 -7.836 1.00 32.22 O HETATM 2201 O HOH A2038 -10.350 3.549 -9.424 1.00 28.22 O HETATM 2202 O HOH A2039 -10.877 3.806 -4.966 1.00 26.30 O HETATM 2203 O HOH A2040 -24.272 3.520 -6.722 1.00 30.51 O HETATM 2204 O HOH A2041 -17.416 3.685 -8.396 1.00 28.13 O HETATM 2205 O HOH A2042 -17.746 -2.293 -9.363 1.00 44.65 O HETATM 2206 O HOH A2043 -21.522 2.625 -7.055 1.00 22.16 O HETATM 2207 O HOH A2044 -23.150 -1.094 -7.523 1.00 17.77 O HETATM 2208 O HOH A2045 -13.404 -1.119 -4.309 1.00 34.60 O HETATM 2209 O HOH A2046 -16.158 -6.415 -1.972 1.00 13.56 O HETATM 2210 O HOH A2047 -22.558 -9.601 10.632 1.00 14.62 O HETATM 2211 O HOH A2048 -29.175 -11.638 10.794 1.00 35.38 O HETATM 2212 O HOH A2049 -25.129 -10.819 9.244 1.00 28.67 O HETATM 2213 O HOH A2050 -23.397 -10.585 13.148 1.00 29.31 O HETATM 2214 O HOH A2051 -12.729 -5.911 17.385 1.00 36.41 O HETATM 2215 O HOH A2052 -21.474 3.177 22.431 1.00 31.42 O HETATM 2216 O HOH A2053 -3.544 2.004 11.788 1.00 31.73 O HETATM 2217 O HOH A2054 -7.626 7.750 12.050 1.00 46.81 O HETATM 2218 O HOH A2055 -7.317 -12.320 3.755 1.00 42.09 O HETATM 2219 O HOH A2056 -8.293 -4.825 -1.503 1.00 36.80 O HETATM 2220 O HOH A2057 -5.519 -10.820 1.064 1.00 40.15 O HETATM 2221 O HOH A2058 -11.801 -11.069 -3.768 1.00 37.82 O HETATM 2222 O HOH A2059 -13.812 -8.959 -4.692 1.00 17.77 O HETATM 2223 O HOH A2060 -14.582 -8.704 -1.637 1.00 22.94 O HETATM 2224 O HOH A2061 -11.205 -11.718 9.248 1.00 23.51 O HETATM 2225 O HOH A2062 -5.479 -0.770 15.646 1.00 39.55 O HETATM 2226 O HOH A2063 -5.152 2.264 30.237 1.00 33.35 O HETATM 2227 O HOH A2064 -18.893 13.742 15.463 1.00 27.84 O HETATM 2228 O HOH A2065 -13.671 10.496 17.421 1.00 25.24 O HETATM 2229 O HOH A2066 -20.441 8.248 19.349 1.00 38.17 O HETATM 2230 O HOH A2067 -27.673 4.290 29.305 0.50 28.86 O HETATM 2231 O HOH A2068 -28.660 0.164 21.844 1.00 31.65 O HETATM 2232 O HOH A2069 -28.625 -0.463 15.442 1.00 31.71 O HETATM 2233 O HOH A2070 -34.155 2.585 13.939 1.00 37.61 O HETATM 2234 O HOH A2071 -16.700 4.878 17.829 1.00 38.19 O HETATM 2235 O HOH A2072 -10.331 11.538 11.698 1.00 27.58 O HETATM 2236 O HOH A2073 -8.681 13.703 6.504 1.00 33.91 O HETATM 2237 O HOH A2074 -9.334 13.605 10.737 1.00 38.83 O HETATM 2238 O HOH A2075 -18.589 20.193 6.769 1.00 13.10 O HETATM 2239 O HOH A2076 -15.981 15.356 12.567 1.00 33.71 O HETATM 2240 O HOH A2077 -6.541 22.454 17.539 1.00 39.45 O HETATM 2241 O HOH A2078 -18.835 25.993 17.283 1.00 23.85 O HETATM 2242 O HOH A2079 -22.706 22.061 12.314 1.00 14.69 O HETATM 2243 O HOH A2080 -27.719 16.535 11.220 1.00 21.72 O HETATM 2244 O HOH A2081 -27.736 18.948 8.204 1.00 10.69 O HETATM 2245 O HOH A2082 -19.604 21.041 10.056 1.00 25.06 O HETATM 2246 O HOH A2083 -19.629 19.849 -1.665 1.00 19.08 O HETATM 2247 O HOH A2084 -28.201 15.935 -2.353 1.00 20.03 O HETATM 2248 O HOH A2085 -18.114 17.211 1.535 1.00 20.42 O HETATM 2249 O HOH A2086 -18.106 18.060 -5.542 1.00 17.35 O HETATM 2250 O HOH A2087 -24.760 13.546 -7.781 1.00 32.52 O HETATM 2251 O HOH A2088 -17.494 7.355 -8.120 1.00 18.83 O HETATM 2252 O HOH A2089 -17.455 16.250 -7.252 1.00 17.42 O HETATM 2253 O HOH A2090 -28.963 13.213 -1.170 1.00 24.08 O HETATM 2254 O HOH A2091 -29.032 15.825 -7.648 1.00 44.16 O HETATM 2255 O HOH A2092 -30.151 6.186 0.411 1.00 23.54 O HETATM 2256 O HOH A2093 -27.729 4.750 -7.083 1.00 46.52 O HETATM 2257 O HOH A2094 -30.903 11.841 4.509 1.00 29.18 O HETATM 2258 O HOH A2095 -28.406 15.118 9.014 1.00 33.17 O HETATM 2259 O HOH A2096 -34.564 5.959 8.508 1.00 33.16 O HETATM 2260 O HOH A2097 -30.338 13.457 8.887 1.00 23.36 O HETATM 2261 O HOH A2098 -33.165 15.405 13.961 1.00 45.08 O HETATM 2262 O HOH A2099 -30.341 16.089 12.344 1.00 17.86 O HETATM 2263 O HOH A2100 -29.010 15.616 19.568 1.00 32.07 O HETATM 2264 O HOH A2101 -38.020 14.568 15.021 1.00 12.65 O HETATM 2265 O HOH A2102 -34.335 5.062 11.563 1.00 43.68 O HETATM 2266 O HOH A2103 -34.301 -2.254 12.229 1.00 29.78 O HETATM 2267 O HOH A2104 -31.124 -6.163 6.611 1.00 25.91 O HETATM 2268 O HOH A2105 -31.258 2.794 4.338 1.00 14.64 O HETATM 2269 O HOH A2106 -33.892 0.703 4.931 1.00 39.33 O HETATM 2270 O HOH A2107 -27.882 -6.263 1.857 1.00 11.28 O HETATM 2271 O HOH A2108 -34.400 -6.657 8.234 1.00 42.38 O HETATM 2272 O HOH A2109 -36.474 -3.484 2.968 1.00 52.63 O HETATM 2273 O HOH A2110 -33.985 -4.446 -0.094 1.00 48.16 O HETATM 2274 O HOH A2111 -30.398 3.678 -2.741 1.00 38.62 O HETATM 2275 O HOH A2112 -25.099 -0.215 -5.914 1.00 21.80 O HETATM 2276 O HOH A2113 -27.363 -6.805 -0.599 1.00 6.91 O HETATM 2277 O HOH A2114 -19.857 -14.772 -2.559 1.00 22.14 O HETATM 2278 O HOH A2115 -23.536 -7.576 -6.677 1.00 13.59 O HETATM 2279 O HOH A2116 -16.757 -8.073 -5.002 1.00 29.28 O HETATM 2280 O HOH A2117 -18.720 -14.316 -0.036 1.00 18.58 O HETATM 2281 O HOH A2118 -20.342 -12.078 0.261 1.00 19.73 O HETATM 2282 O HOH A2119 -17.663 -10.519 -6.481 1.00 27.41 O HETATM 2283 O HOH A2120 -16.168 -15.958 -0.548 1.00 29.63 O MASTER 336 0 0 15 8 0 0 6 2282 1 0 22 END