Browse entries in the PDBbind-CN Database
HEADER APOPTOSIS 07-MAY-18 6DCN TITLE BCL-XL COMPLEX WITH BECLIN 1 BH3 DOMAIN T108PTHR COMPND MOL_ID: 1; COMPND 2 MOLECULE: BCL-XL PROTEIN; COMPND 3 CHAIN: A, B; COMPND 4 SYNONYM: BCL2-L-1,APOPTOSIS REGULATOR BCL-X,BCL2-L-1,APOPTOSIS COMPND 5 REGULATOR BCL-X; COMPND 6 ENGINEERED: YES; COMPND 7 MOL_ID: 2; COMPND 8 MOLECULE: BECLIN-1; COMPND 9 CHAIN: D, C; COMPND 10 SYNONYM: COILED-COIL MYOSIN-LIKE BCL2-INTERACTING PROTEIN,PROTEIN COMPND 11 GT197; COMPND 12 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 SYNTHETIC: YES; SOURCE 3 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 4 ORGANISM_COMMON: HUMAN; SOURCE 5 ORGANISM_TAXID: 9606; SOURCE 6 MOL_ID: 2; SOURCE 7 SYNTHETIC: YES; SOURCE 8 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 9 ORGANISM_COMMON: HUMAN; SOURCE 10 ORGANISM_TAXID: 9606 KEYWDS APOPTOSIS, BCL-2, AUTOPHAGY, BECLIN 1 EXPDTA X-RAY DIFFRACTION AUTHOR E.F.LEE,B.J.SMITH,N.A.SMITH,S.YAO,W.D.FAIRLIE REVDAT 4 01-JAN-20 6DCN 1 REMARK REVDAT 3 17-APR-19 6DCN 1 JRNL REVDAT 2 23-JAN-19 6DCN 1 JRNL REVDAT 1 23-MAY-18 6DCN 0 SPRSDE 23-MAY-18 6DCN 5VB1 JRNL AUTH E.F.LEE,N.A.SMITH,T.P.SOARES DA COSTA,N.MEFTAHI,S.YAO, JRNL AUTH 2 T.J.HARRIS,S.TRAN,A.PETTIKIRIARACHCHI,M.A.PERUGINI, JRNL AUTH 3 D.W.KEIZER,M.EVANGELISTA,B.J.SMITH,W.D.FAIRLIE JRNL TITL STRUCTURAL INSIGHTS INTO BCL2 PRO-SURVIVAL PROTEIN JRNL TITL 2 INTERACTIONS WITH THE KEY AUTOPHAGY REGULATOR BECN1 JRNL TITL 3 FOLLOWING PHOSPHORYLATION BY STK4/MST1. JRNL REF AUTOPHAGY V. 15 785 2019 JRNL REFN ESSN 1554-8635 JRNL PMID 30626284 JRNL DOI 10.1080/15548627.2018.1564557 REMARK 2 REMARK 2 RESOLUTION. 2.44 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX (1.13_2998) REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE, REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER, REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY, REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON, REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI, REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART REMARK 3 REMARK 3 REFINEMENT TARGET : NULL REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.44 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 48.93 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340 REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7 REMARK 3 NUMBER OF REFLECTIONS : 22378 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.192 REMARK 3 R VALUE (WORKING SET) : 0.189 REMARK 3 FREE R VALUE : 0.229 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 8.930 REMARK 3 FREE R VALUE TEST SET COUNT : 1998 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 48.9435 - 5.8867 1.00 1603 158 0.1728 0.2176 REMARK 3 2 5.8867 - 4.6736 1.00 1506 147 0.1721 0.2101 REMARK 3 3 4.6736 - 4.0832 1.00 1468 144 0.1497 0.1660 REMARK 3 4 4.0832 - 3.7100 1.00 1472 144 0.1694 0.2041 REMARK 3 5 3.7100 - 3.4442 1.00 1455 144 0.1872 0.2141 REMARK 3 6 3.4442 - 3.2412 1.00 1455 142 0.1961 0.2628 REMARK 3 7 3.2412 - 3.0789 1.00 1456 143 0.2132 0.2459 REMARK 3 8 3.0789 - 2.9449 1.00 1426 140 0.2279 0.2988 REMARK 3 9 2.9449 - 2.8315 1.00 1448 142 0.2067 0.2623 REMARK 3 10 2.8315 - 2.7338 1.00 1434 140 0.2183 0.2728 REMARK 3 11 2.7338 - 2.6483 1.00 1424 141 0.2167 0.2657 REMARK 3 12 2.6483 - 2.5726 1.00 1431 139 0.2417 0.2894 REMARK 3 13 2.5726 - 2.5049 1.00 1428 140 0.2686 0.3179 REMARK 3 14 2.5049 - 2.4438 0.97 1374 134 0.2941 0.3584 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : NULL REMARK 3 SOLVENT RADIUS : 1.11 REMARK 3 SHRINKAGE RADIUS : 0.90 REMARK 3 K_SOL : NULL REMARK 3 B_SOL : NULL REMARK 3 REMARK 3 ERROR ESTIMATES. REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.320 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 22.600 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : NULL REMARK 3 B22 (A**2) : NULL REMARK 3 B33 (A**2) : NULL REMARK 3 B12 (A**2) : NULL REMARK 3 B13 (A**2) : NULL REMARK 3 B23 (A**2) : NULL REMARK 3 REMARK 3 TWINNING INFORMATION. REMARK 3 FRACTION: NULL REMARK 3 OPERATOR: NULL REMARK 3 REMARK 3 DEVIATIONS FROM IDEAL VALUES. REMARK 3 RMSD COUNT REMARK 3 BOND : 0.007 2677 REMARK 3 ANGLE : 0.796 3625 REMARK 3 CHIRALITY : 0.044 391 REMARK 3 PLANARITY : 0.004 462 REMARK 3 DIHEDRAL : 18.299 1555 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 1 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: ALL REMARK 3 ORIGIN FOR THE GROUP (A): 14.8036 2.5550 24.0815 REMARK 3 T TENSOR REMARK 3 T11: 0.2548 T22: 0.4625 REMARK 3 T33: 0.3409 T12: 0.0218 REMARK 3 T13: 0.0091 T23: 0.0387 REMARK 3 L TENSOR REMARK 3 L11: 0.5814 L22: 2.9838 REMARK 3 L33: 1.4304 L12: 0.3172 REMARK 3 L13: 0.3265 L23: 0.5972 REMARK 3 S TENSOR REMARK 3 S11: -0.0782 S12: -0.0114 S13: -0.0158 REMARK 3 S21: 0.0005 S22: 0.0281 S23: -0.2726 REMARK 3 S31: -0.0519 S32: 0.3274 S33: 0.0421 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 6DCN COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-MAY-18. REMARK 100 THE DEPOSITION ID IS D_1000234378. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 09-OCT-14 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : NULL REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : AUSTRALIAN SYNCHROTRON REMARK 200 BEAMLINE : MX2 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.9537 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 270 REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS VNOV 11, 2017 REMARK 200 DATA SCALING SOFTWARE : XDS VNOV 11, 2017 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 22390 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.444 REMARK 200 RESOLUTION RANGE LOW (A) : 48.934 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7 REMARK 200 DATA REDUNDANCY : 10.80 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.1300 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.44 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.50 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 <I/SIGMA(I)> FOR SHELL : NULL REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: PHASER REMARK 200 STARTING MODEL: 2P1L REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 65.09 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.52 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 2M NACL, 10% GLYCEROL, VAPOR REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 4 21 2 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 -Y+1/2,X+1/2,Z REMARK 290 4555 Y+1/2,-X+1/2,Z REMARK 290 5555 -X+1/2,Y+1/2,-Z REMARK 290 6555 X+1/2,-Y+1/2,-Z REMARK 290 7555 Y,X,-Z REMARK 290 8555 -Y,-X,-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 0.000000 -1.000000 0.000000 54.70950 REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 54.70950 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 54.70950 REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 54.70950 REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 54.70950 REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 54.70950 REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 54.70950 REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 54.70950 REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1, 2 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, D, C 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 350 REMARK 350 BIOMOLECULE: 2 REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: OCTAMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 19390 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 27740 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -155.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, D, C 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 350 BIOMT1 2 -1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000 REMARK 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 ASN A 198 REMARK 465 ALA A 199 REMARK 465 ALA A 200 REMARK 465 ALA A 201 REMARK 465 GLU A 202 REMARK 465 SER A 203 REMARK 465 ARG A 204 REMARK 465 LYS A 205 REMARK 465 GLY A 206 REMARK 465 GLN A 207 REMARK 465 GLU A 208 REMARK 465 ASN B 198 REMARK 465 ALA B 199 REMARK 465 ALA B 200 REMARK 465 ALA B 201 REMARK 465 GLU B 202 REMARK 465 SER B 203 REMARK 465 ARG B 204 REMARK 465 LYS B 205 REMARK 465 GLY B 206 REMARK 465 GLN B 207 REMARK 465 GLU B 208 REMARK 465 ASP D 105 REMARK 465 GLY D 106 REMARK 465 GLY D 128 REMARK 465 GLN D 129 REMARK 465 THR D 130 REMARK 465 ASP C 105 REMARK 465 GLY C 106 REMARK 465 GLY C 128 REMARK 465 GLN C 129 REMARK 465 THR C 130 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 LYS A 20 CG CD CE NZ REMARK 470 GLN A 26 CG CD OE1 NE2 REMARK 470 SER A 106 OG REMARK 470 HIS A 113 CG ND1 CD2 CE1 NE2 REMARK 470 GLU A 129 CG CD OE1 OE2 REMARK 470 GLU A 184 CG CD OE1 OE2 REMARK 470 LYS B 20 CG CD CE NZ REMARK 470 SER B 23 OG REMARK 470 GLN B 88 CG CD OE1 NE2 REMARK 470 ASP B 107 CG OD1 OD2 REMARK 470 GLN B 111 CG CD OE1 NE2 REMARK 470 HIS B 113 CG ND1 CD2 CE1 NE2 REMARK 470 GLN B 121 CG CD OE1 NE2 REMARK 470 GLN B 125 CG CD OE1 NE2 REMARK 470 GLU B 129 CG CD OE1 OE2 REMARK 470 GLU D 110 CG CD OE1 OE2 REMARK 470 GLU C 110 CG CD OE1 OE2 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 PHE A 105 -149.95 -132.64 REMARK 500 GLU A 184 1.15 -66.80 REMARK 500 PHE B 105 -159.84 -122.71 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 5VAX RELATED DB: PDB REMARK 900 RELATED ID: 5VAU RELATED DB: PDB REMARK 900 RELATED ID: 5VAY RELATED DB: PDB DBREF 6DCN A 1 26 UNP Q07817 B2CL1_HUMAN 1 26 DBREF 6DCN A 83 208 UNP Q07817 B2CL1_HUMAN 83 208 DBREF 6DCN B 1 26 UNP Q07817 B2CL1_HUMAN 1 26 DBREF 6DCN B 83 208 UNP Q07817 B2CL1_HUMAN 83 208 DBREF 6DCN D 105 130 UNP Q14457 BECN1_HUMAN 105 130 DBREF 6DCN C 105 130 UNP Q14457 BECN1_HUMAN 105 130 SEQADV 6DCN PRO A -3 UNP Q07817 EXPRESSION TAG SEQADV 6DCN LEU A -2 UNP Q07817 EXPRESSION TAG SEQADV 6DCN GLY A -1 UNP Q07817 EXPRESSION TAG SEQADV 6DCN SER A 0 UNP Q07817 EXPRESSION TAG SEQADV 6DCN PRO B -3 UNP Q07817 EXPRESSION TAG SEQADV 6DCN LEU B -2 UNP Q07817 EXPRESSION TAG SEQADV 6DCN GLY B -1 UNP Q07817 EXPRESSION TAG SEQADV 6DCN SER B 0 UNP Q07817 EXPRESSION TAG SEQRES 1 A 156 PRO LEU GLY SER MET SER GLN SER ASN ARG GLU LEU VAL SEQRES 2 A 156 VAL ASP PHE LEU SER TYR LYS LEU SER GLN LYS GLY TYR SEQRES 3 A 156 SER TRP SER GLN MET ALA ALA VAL LYS GLN ALA LEU ARG SEQRES 4 A 156 GLU ALA GLY ASP GLU PHE GLU LEU ARG TYR ARG ARG ALA SEQRES 5 A 156 PHE SER ASP LEU THR SER GLN LEU HIS ILE THR PRO GLY SEQRES 6 A 156 THR ALA TYR GLN SER PHE GLU GLN VAL VAL ASN GLU LEU SEQRES 7 A 156 PHE ARG ASP GLY VAL ASN TRP GLY ARG ILE VAL ALA PHE SEQRES 8 A 156 PHE SER PHE GLY GLY ALA LEU CYS VAL GLU SER VAL ASP SEQRES 9 A 156 LYS GLU MET GLN VAL LEU VAL SER ARG ILE ALA ALA TRP SEQRES 10 A 156 MET ALA THR TYR LEU ASN ASP HIS LEU GLU PRO TRP ILE SEQRES 11 A 156 GLN GLU ASN GLY GLY TRP ASP THR PHE VAL GLU LEU TYR SEQRES 12 A 156 GLY ASN ASN ALA ALA ALA GLU SER ARG LYS GLY GLN GLU SEQRES 1 B 156 PRO LEU GLY SER MET SER GLN SER ASN ARG GLU LEU VAL SEQRES 2 B 156 VAL ASP PHE LEU SER TYR LYS LEU SER GLN LYS GLY TYR SEQRES 3 B 156 SER TRP SER GLN MET ALA ALA VAL LYS GLN ALA LEU ARG SEQRES 4 B 156 GLU ALA GLY ASP GLU PHE GLU LEU ARG TYR ARG ARG ALA SEQRES 5 B 156 PHE SER ASP LEU THR SER GLN LEU HIS ILE THR PRO GLY SEQRES 6 B 156 THR ALA TYR GLN SER PHE GLU GLN VAL VAL ASN GLU LEU SEQRES 7 B 156 PHE ARG ASP GLY VAL ASN TRP GLY ARG ILE VAL ALA PHE SEQRES 8 B 156 PHE SER PHE GLY GLY ALA LEU CYS VAL GLU SER VAL ASP SEQRES 9 B 156 LYS GLU MET GLN VAL LEU VAL SER ARG ILE ALA ALA TRP SEQRES 10 B 156 MET ALA THR TYR LEU ASN ASP HIS LEU GLU PRO TRP ILE SEQRES 11 B 156 GLN GLU ASN GLY GLY TRP ASP THR PHE VAL GLU LEU TYR SEQRES 12 B 156 GLY ASN ASN ALA ALA ALA GLU SER ARG LYS GLY GLN GLU SEQRES 1 D 26 ASP GLY GLY TPO MET GLU ASN LEU SER ARG ARG LEU LYS SEQRES 2 D 26 VAL THR GLY ASP LEU PHE ASP ILE MET SER GLY GLN THR SEQRES 1 C 26 ASP GLY GLY TPO MET GLU ASN LEU SER ARG ARG LEU LYS SEQRES 2 C 26 VAL THR GLY ASP LEU PHE ASP ILE MET SER GLY GLN THR MODRES 6DCN TPO D 108 THR MODIFIED RESIDUE MODRES 6DCN TPO C 108 THR MODIFIED RESIDUE HET TPO D 108 11 HET TPO C 108 11 HETNAM TPO PHOSPHOTHREONINE HETSYN TPO PHOSPHONOTHREONINE FORMUL 3 TPO 2(C4 H10 N O6 P) FORMUL 5 HOH *44(H2 O) HELIX 1 AA1 SER A 4 LYS A 20 1 17 HELIX 2 AA2 SER A 25 PHE A 105 1 25 HELIX 3 AA3 THR A 118 ARG A 132 1 15 HELIX 4 AA4 ASN A 136 LYS A 157 1 22 HELIX 5 AA5 VAL A 161 LEU A 178 1 18 HELIX 6 AA6 LEU A 178 GLU A 184 1 7 HELIX 7 AA7 GLY A 186 GLY A 196 1 11 HELIX 8 AA8 GLY B -1 LYS B 20 1 22 HELIX 9 AA9 SER B 25 PHE B 105 1 25 HELIX 10 AB1 THR B 115 ARG B 132 1 18 HELIX 11 AB2 ASN B 136 LYS B 157 1 22 HELIX 12 AB3 VAL B 161 LEU B 178 1 18 HELIX 13 AB4 LEU B 178 ASN B 185 1 8 HELIX 14 AB5 GLY B 186 GLY B 196 1 11 HELIX 15 AB6 TPO D 108 MET D 126 1 19 HELIX 16 AB7 TPO C 108 MET C 126 1 19 LINK C GLY D 107 N TPO D 108 1555 1555 1.33 LINK C TPO D 108 N MET D 109 1555 1555 1.33 LINK C GLY C 107 N TPO C 108 1555 1555 1.33 LINK C TPO C 108 N MET C 109 1555 1555 1.33 CRYST1 109.419 109.419 97.127 90.00 90.00 90.00 P 4 21 2 16 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 0.009139 0.000000 0.000000 0.00000 SCALE2 0.000000 0.009139 0.000000 0.00000 SCALE3 0.000000 0.000000 0.010296 0.00000 ATOM 1 N PRO A -3 3.403 1.324 11.918 1.00 89.53 N ANISOU 1 N PRO A -3 11448 11454 11116 229 -523 197 N ATOM 2 CA PRO A -3 4.165 0.167 12.404 1.00 97.04 C ANISOU 2 CA PRO A -3 12318 12502 12052 246 -360 208 C ATOM 3 C PRO A -3 4.355 0.244 13.917 1.00103.73 C ANISOU 3 C PRO A -3 12985 13442 12987 268 -277 210 C ATOM 4 O PRO A -3 3.394 0.548 14.629 1.00113.95 O ANISOU 4 O PRO A -3 14188 14711 14397 290 -337 177 O ATOM 5 CB PRO A -3 5.500 0.292 11.662 1.00 89.06 C ANISOU 5 CB PRO A -3 11423 11529 10887 199 -256 247 C ATOM 6 CG PRO A -3 5.679 1.787 11.521 1.00 86.93 C ANISOU 6 CG PRO A -3 11220 11233 10576 147 -313 268 C ATOM 7 CD PRO A -3 4.286 2.394 11.416 1.00 85.68 C ANISOU 7 CD PRO A -3 11086 10965 10503 170 -507 237 C ATOM 8 N LEU A -2 5.567 -0.017 14.402 1.00 91.09 N ANISOU 8 N LEU A -2 11338 11939 11334 263 -142 240 N ATOM 9 CA LEU A -2 5.842 0.151 15.822 1.00 85.57 C ANISOU 9 CA LEU A -2 10502 11317 10694 278 -81 246 C ATOM 10 C LEU A -2 5.719 1.617 16.220 1.00 97.13 C ANISOU 10 C LEU A -2 11958 12772 12175 249 -140 246 C ATOM 11 O LEU A -2 6.250 2.504 15.538 1.00 96.48 O ANISOU 11 O LEU A -2 11966 12674 12018 201 -163 268 O ATOM 12 CB LEU A -2 7.242 -0.355 16.161 1.00 62.82 C ANISOU 12 CB LEU A -2 7579 8532 7759 281 43 276 C ATOM 13 CG LEU A -2 7.544 -1.815 15.869 1.00 52.98 C ANISOU 13 CG LEU A -2 6337 7297 6497 322 112 275 C ATOM 14 CD1 LEU A -2 8.923 -2.138 16.384 1.00 50.08 C ANISOU 14 CD1 LEU A -2 5898 7021 6108 338 215 296 C ATOM 15 CD2 LEU A -2 6.494 -2.731 16.488 1.00 48.36 C ANISOU 15 CD2 LEU A -2 5704 6676 5993 362 89 252 C ATOM 16 N GLY A -1 5.000 1.864 17.318 1.00100.10 N ANISOU 16 N GLY A -1 12239 13150 12645 272 -157 219 N ATOM 17 CA GLY A -1 4.952 3.177 17.953 1.00 99.65 C ANISOU 17 CA GLY A -1 12161 13090 12609 255 -194 213 C ATOM 18 C GLY A -1 4.407 4.299 17.097 1.00100.70 C ANISOU 18 C GLY A -1 12388 13131 12742 235 -322 201 C ATOM 19 O GLY A -1 4.819 5.453 17.269 1.00 96.13 O ANISOU 19 O GLY A -1 11842 12551 12132 202 -347 214 O ATOM 20 N SER A 0 3.476 3.997 16.187 1.00104.49 N ANISOU 20 N SER A 0 12922 13523 13257 254 -420 175 N ATOM 21 CA SER A 0 2.923 4.987 15.266 1.00 99.40 C ANISOU 21 CA SER A 0 12392 12768 12606 243 -574 166 C ATOM 22 C SER A 0 2.101 6.070 15.960 1.00 90.51 C ANISOU 22 C SER A 0 11204 11592 11592 272 -659 121 C ATOM 23 O SER A 0 1.731 7.056 15.312 1.00 76.18 O ANISOU 23 O SER A 0 9490 9680 9774 268 -799 115 O ATOM 24 CB SER A 0 2.067 4.277 14.216 1.00 99.10 C ANISOU 24 CB SER A 0 12420 12642 12592 265 -678 142 C ATOM 25 OG SER A 0 1.150 3.386 14.832 1.00 97.50 O ANISOU 25 OG SER A 0 12074 12445 12527 312 -663 92 O ATOM 26 N MET A 1 1.817 5.922 17.252 1.00 90.18 N ANISOU 26 N MET A 1 11016 11605 11643 301 -577 87 N ATOM 27 CA MET A 1 0.967 6.856 17.965 1.00 87.06 C ANISOU 27 CA MET A 1 10552 11162 11367 335 -634 29 C ATOM 28 C MET A 1 1.711 7.741 18.949 1.00 85.26 C ANISOU 28 C MET A 1 10315 10989 11092 311 -566 45 C ATOM 29 O MET A 1 1.100 8.661 19.501 1.00 95.36 O ANISOU 29 O MET A 1 11560 12219 12453 339 -613 -5 O ATOM 30 CB MET A 1 -0.130 6.097 18.717 1.00 84.90 C ANISOU 30 CB MET A 1 10124 10887 11247 381 -587 -40 C ATOM 31 CG MET A 1 -1.434 6.843 18.737 1.00 82.48 C ANISOU 31 CG MET A 1 9752 10479 11108 432 -705 -123 C ATOM 32 SD MET A 1 -2.803 5.772 19.149 1.00 76.60 S ANISOU 32 SD MET A 1 8830 9715 10561 468 -663 -209 S ATOM 33 CE MET A 1 -2.644 4.488 17.908 1.00 73.81 C ANISOU 33 CE MET A 1 8553 9351 10142 445 -713 -163 C ATOM 34 N SER A 2 3.000 7.495 19.184 1.00 73.95 N ANISOU 34 N SER A 2 8908 9651 9540 264 -465 105 N ATOM 35 CA SER A 2 3.762 8.238 20.191 1.00 63.13 C ANISOU 35 CA SER A 2 7523 8335 8128 236 -408 119 C ATOM 36 C SER A 2 4.460 9.434 19.541 1.00 60.38 C ANISOU 36 C SER A 2 7296 7951 7697 179 -480 156 C ATOM 37 O SER A 2 5.682 9.495 19.419 1.00 66.19 O ANISOU 37 O SER A 2 8066 8749 8335 118 -423 209 O ATOM 38 CB SER A 2 4.760 7.319 20.879 1.00 63.21 C ANISOU 38 CB SER A 2 7481 8458 8077 219 -279 157 C ATOM 39 OG SER A 2 4.102 6.451 21.784 1.00 70.26 O ANISOU 39 OG SER A 2 8285 9372 9037 262 -209 121 O ATOM 40 N GLN A 3 3.651 10.414 19.141 1.00 51.71 N ANISOU 40 N GLN A 3 6257 6742 6649 198 -608 123 N ATOM 41 CA GLN A 3 4.131 11.506 18.304 1.00 53.43 C ANISOU 41 CA GLN A 3 6627 6892 6783 141 -697 161 C ATOM 42 C GLN A 3 4.020 12.865 18.979 1.00 54.49 C ANISOU 42 C GLN A 3 6784 6975 6945 139 -755 135 C ATOM 43 O GLN A 3 4.227 13.889 18.321 1.00 58.09 O ANISOU 43 O GLN A 3 7380 7347 7345 96 -850 159 O ATOM 44 CB GLN A 3 3.386 11.514 16.962 1.00 55.36 C ANISOU 44 CB GLN A 3 6983 7020 7030 159 -836 158 C ATOM 45 CG GLN A 3 3.824 10.381 16.034 1.00 68.64 C ANISOU 45 CG GLN A 3 8711 8741 8629 131 -781 199 C ATOM 46 CD GLN A 3 2.952 10.263 14.810 1.00 84.07 C ANISOU 46 CD GLN A 3 10780 10573 10591 157 -932 187 C ATOM 47 OE1 GLN A 3 2.322 11.238 14.382 1.00 86.51 O ANISOU 47 OE1 GLN A 3 11187 10758 10926 173 -1095 170 O ATOM 48 NE2 GLN A 3 2.899 9.061 14.236 1.00 88.17 N ANISOU 48 NE2 GLN A 3 11297 11115 11087 165 -895 193 N ATOM 49 N SER A 4 3.727 12.903 20.270 1.00 43.01 N ANISOU 49 N SER A 4 5217 5561 5564 179 -695 86 N ATOM 50 CA SER A 4 3.569 14.165 20.970 1.00 37.17 C ANISOU 50 CA SER A 4 4504 4766 4853 185 -744 50 C ATOM 51 C SER A 4 4.905 14.676 21.494 1.00 42.72 C ANISOU 51 C SER A 4 5248 5537 5448 99 -684 100 C ATOM 52 O SER A 4 5.837 13.907 21.763 1.00 44.93 O ANISOU 52 O SER A 4 5477 5928 5667 58 -580 142 O ATOM 53 CB SER A 4 2.612 14.001 22.139 1.00 41.32 C ANISOU 53 CB SER A 4 4904 5294 5501 264 -693 -35 C ATOM 54 OG SER A 4 3.231 13.209 23.134 1.00 47.60 O ANISOU 54 OG SER A 4 5627 6209 6252 243 -548 -19 O ATOM 55 N ASN A 5 4.980 16.001 21.655 1.00 38.03 N ANISOU 55 N ASN A 5 4742 4867 4843 75 -762 89 N ATOM 56 CA ASN A 5 6.102 16.595 22.373 1.00 43.93 C ANISOU 56 CA ASN A 5 5512 5667 5514 -4 -718 118 C ATOM 57 C ASN A 5 6.297 15.955 23.741 1.00 45.06 C ANISOU 57 C ASN A 5 5539 5910 5670 21 -609 92 C ATOM 58 O ASN A 5 7.437 15.733 24.166 1.00 44.04 O ANISOU 58 O ASN A 5 5389 5871 5473 -44 -550 135 O ATOM 59 CB ASN A 5 5.900 18.102 22.518 1.00 43.20 C ANISOU 59 CB ASN A 5 5529 5459 5428 -17 -824 92 C ATOM 60 CG ASN A 5 6.209 18.840 21.247 1.00 51.82 C ANISOU 60 CG ASN A 5 6779 6459 6453 -87 -922 145 C ATOM 61 OD1 ASN A 5 7.014 18.378 20.435 1.00 52.63 O ANISOU 61 OD1 ASN A 5 6915 6611 6473 -165 -876 212 O ATOM 62 ND2 ASN A 5 5.589 19.996 21.065 1.00 51.62 N ANISOU 62 ND2 ASN A 5 6864 6292 6458 -61 -1054 114 N ATOM 63 N ARG A 6 5.198 15.646 24.447 1.00 39.17 N ANISOU 63 N ARG A 6 4723 5146 5015 110 -581 20 N ATOM 64 CA ARG A 6 5.336 15.009 25.755 1.00 35.07 C ANISOU 64 CA ARG A 6 4130 4708 4488 126 -471 -2 C ATOM 65 C ARG A 6 6.052 13.673 25.627 1.00 37.58 C ANISOU 65 C ARG A 6 4387 5135 4757 105 -391 56 C ATOM 66 O ARG A 6 6.863 13.307 26.488 1.00 43.38 O ANISOU 66 O ARG A 6 5102 5947 5434 78 -335 77 O ATOM 67 CB ARG A 6 3.964 14.840 26.422 1.00 33.55 C ANISOU 67 CB ARG A 6 3874 4468 4403 215 -428 -95 C ATOM 68 CG ARG A 6 4.008 14.213 27.826 1.00 33.21 C ANISOU 68 CG ARG A 6 3794 4492 4334 224 -302 -121 C ATOM 69 CD ARG A 6 2.661 14.279 28.539 1.00 42.24 C ANISOU 69 CD ARG A 6 4888 5578 5585 296 -236 -226 C ATOM 70 NE ARG A 6 2.281 15.648 28.907 1.00 57.25 N ANISOU 70 NE ARG A 6 6844 7387 7520 318 -289 -293 N ATOM 71 CZ ARG A 6 2.356 16.146 30.140 1.00 63.83 C ANISOU 71 CZ ARG A 6 7730 8213 8308 313 -227 -340 C ATOM 72 NH1 ARG A 6 2.798 15.395 31.154 1.00 54.68 N ANISOU 72 NH1 ARG A 6 6587 7130 7058 284 -117 -324 N ATOM 73 NH2 ARG A 6 1.985 17.403 30.358 1.00 74.55 N ANISOU 73 NH2 ARG A 6 9143 9477 9705 340 -283 -406 N ATOM 74 N GLU A 7 5.801 12.951 24.534 1.00 39.79 N ANISOU 74 N GLU A 7 4646 5414 5058 119 -399 80 N ATOM 75 CA GLU A 7 6.488 11.682 24.316 1.00 42.77 C ANISOU 75 CA GLU A 7 4973 5885 5394 106 -325 130 C ATOM 76 C GLU A 7 7.962 11.899 24.012 1.00 41.74 C ANISOU 76 C GLU A 7 4868 5814 5178 24 -322 194 C ATOM 77 O GLU A 7 8.816 11.106 24.431 1.00 49.19 O ANISOU 77 O GLU A 7 5755 6846 6089 12 -260 224 O ATOM 78 CB GLU A 7 5.825 10.909 23.177 1.00 53.12 C ANISOU 78 CB GLU A 7 6272 7166 6744 139 -339 133 C ATOM 79 CG GLU A 7 5.287 9.559 23.583 1.00 74.11 C ANISOU 79 CG GLU A 7 8847 9865 9447 190 -258 115 C ATOM 80 CD GLU A 7 6.331 8.675 24.237 1.00 78.03 C ANISOU 80 CD GLU A 7 9308 10462 9877 173 -171 157 C ATOM 81 OE1 GLU A 7 7.335 8.324 23.558 1.00 73.80 O ANISOU 81 OE1 GLU A 7 8780 9974 9285 138 -162 210 O ATOM 82 OE2 GLU A 7 6.134 8.346 25.432 1.00 71.00 O ANISOU 82 OE2 GLU A 7 8388 9595 8993 194 -113 134 O ATOM 83 N LEU A 8 8.277 12.947 23.252 1.00 37.64 N ANISOU 83 N LEU A 8 4433 5240 4629 -36 -390 214 N ATOM 84 CA LEU A 8 9.674 13.306 23.025 1.00 37.19 C ANISOU 84 CA LEU A 8 4391 5234 4506 -131 -374 265 C ATOM 85 C LEU A 8 10.412 13.502 24.349 1.00 36.17 C ANISOU 85 C LEU A 8 4213 5165 4366 -152 -360 259 C ATOM 86 O LEU A 8 11.507 12.960 24.558 1.00 38.29 O ANISOU 86 O LEU A 8 4412 5521 4615 -186 -315 290 O ATOM 87 CB LEU A 8 9.743 14.576 22.183 1.00 42.95 C ANISOU 87 CB LEU A 8 5244 5872 5201 -202 -451 281 C ATOM 88 CG LEU A 8 10.986 14.618 21.319 1.00 58.12 C ANISOU 88 CG LEU A 8 7190 7834 7058 -308 -404 337 C ATOM 89 CD1 LEU A 8 10.804 13.607 20.199 1.00 64.06 C ANISOU 89 CD1 LEU A 8 7950 8596 7792 -285 -356 356 C ATOM 90 CD2 LEU A 8 11.168 16.014 20.775 1.00 63.89 C ANISOU 90 CD2 LEU A 8 8062 8470 7745 -399 -474 354 C ATOM 91 N VAL A 9 9.812 14.268 25.266 1.00 30.41 N ANISOU 91 N VAL A 9 3520 4382 3651 -127 -403 214 N ATOM 92 CA VAL A 9 10.396 14.410 26.601 1.00 33.61 C ANISOU 92 CA VAL A 9 3906 4831 4032 -141 -399 202 C ATOM 93 C VAL A 9 10.552 13.043 27.245 1.00 31.60 C ANISOU 93 C VAL A 9 3572 4659 3776 -91 -330 209 C ATOM 94 O VAL A 9 11.652 12.661 27.658 1.00 40.27 O ANISOU 94 O VAL A 9 4623 5829 4848 -122 -327 240 O ATOM 95 CB VAL A 9 9.546 15.343 27.486 1.00 35.14 C ANISOU 95 CB VAL A 9 4169 4944 4239 -109 -437 139 C ATOM 96 CG1 VAL A 9 10.152 15.440 28.881 1.00 35.88 C ANISOU 96 CG1 VAL A 9 4273 5075 4285 -127 -437 126 C ATOM 97 CG2 VAL A 9 9.409 16.730 26.863 1.00 32.61 C ANISOU 97 CG2 VAL A 9 3944 4526 3922 -154 -523 132 C ATOM 98 N VAL A 10 9.444 12.284 27.336 1.00 34.91 N ANISOU 98 N VAL A 10 3974 5060 4230 -12 -281 179 N ATOM 99 CA VAL A 10 9.471 10.992 28.028 1.00 35.08 C ANISOU 99 CA VAL A 10 3948 5140 4242 33 -214 185 C ATOM 100 C VAL A 10 10.558 10.097 27.446 1.00 38.57 C ANISOU 100 C VAL A 10 4323 5660 4670 16 -198 241 C ATOM 101 O VAL A 10 11.313 9.445 28.183 1.00 40.50 O ANISOU 101 O VAL A 10 4539 5962 4889 23 -192 261 O ATOM 102 CB VAL A 10 8.095 10.296 27.958 1.00 38.15 C ANISOU 102 CB VAL A 10 4319 5490 4685 103 -155 144 C ATOM 103 CG1 VAL A 10 8.231 8.843 28.424 1.00 32.22 C ANISOU 103 CG1 VAL A 10 3532 4794 3916 136 -84 165 C ATOM 104 CG2 VAL A 10 7.045 11.016 28.816 1.00 29.71 C ANISOU 104 CG2 VAL A 10 3292 4352 3645 130 -141 72 C ATOM 105 N ASP A 11 10.658 10.061 26.115 1.00 37.82 N ANISOU 105 N ASP A 11 4215 5561 4592 -4 -195 264 N ATOM 106 CA ASP A 11 11.659 9.223 25.466 1.00 38.13 C ANISOU 106 CA ASP A 11 4191 5671 4627 -18 -158 306 C ATOM 107 C ASP A 11 13.074 9.671 25.807 1.00 42.42 C ANISOU 107 C ASP A 11 4692 6270 5157 -83 -184 328 C ATOM 108 O ASP A 11 13.947 8.837 26.101 1.00 47.58 O ANISOU 108 O ASP A 11 5267 6991 5822 -67 -167 346 O ATOM 109 CB ASP A 11 11.454 9.232 23.951 1.00 36.50 C ANISOU 109 CB ASP A 11 4011 5434 4422 -38 -142 319 C ATOM 110 CG ASP A 11 12.404 8.306 23.241 1.00 53.31 C ANISOU 110 CG ASP A 11 6080 7630 6547 -46 -78 350 C ATOM 111 OD1 ASP A 11 12.091 7.100 23.144 1.00 70.39 O ANISOU 111 OD1 ASP A 11 8213 9809 8722 19 -36 349 O ATOM 112 OD2 ASP A 11 13.473 8.779 22.803 1.00 63.37 O ANISOU 112 OD2 ASP A 11 7333 8935 7809 -119 -64 370 O ATOM 113 N PHE A 12 13.332 10.978 25.762 1.00 39.62 N ANISOU 113 N PHE A 12 4383 5881 4790 -158 -234 325 N ATOM 114 CA PHE A 12 14.689 11.446 26.045 1.00 44.27 C ANISOU 114 CA PHE A 12 4918 6520 5384 -235 -263 342 C ATOM 115 C PHE A 12 15.092 11.108 27.478 1.00 35.27 C ANISOU 115 C PHE A 12 3746 5415 4239 -201 -311 332 C ATOM 116 O PHE A 12 16.193 10.600 27.717 1.00 34.73 O ANISOU 116 O PHE A 12 3583 5413 4201 -210 -324 347 O ATOM 117 CB PHE A 12 14.818 12.947 25.776 1.00 29.88 C ANISOU 117 CB PHE A 12 3169 4639 3544 -330 -313 340 C ATOM 118 CG PHE A 12 16.212 13.466 25.959 1.00 33.64 C ANISOU 118 CG PHE A 12 3581 5161 4040 -428 -337 353 C ATOM 119 CD1 PHE A 12 17.078 13.543 24.893 1.00 31.41 C ANISOU 119 CD1 PHE A 12 3247 4908 3778 -512 -277 377 C ATOM 120 CD2 PHE A 12 16.664 13.864 27.214 1.00 32.93 C ANISOU 120 CD2 PHE A 12 3481 5081 3951 -442 -419 337 C ATOM 121 CE1 PHE A 12 18.358 14.015 25.069 1.00 48.50 C ANISOU 121 CE1 PHE A 12 5327 7116 5984 -611 -290 381 C ATOM 122 CE2 PHE A 12 17.950 14.336 27.395 1.00 42.31 C ANISOU 122 CE2 PHE A 12 4593 6308 5176 -536 -458 344 C ATOM 123 CZ PHE A 12 18.793 14.419 26.329 1.00 47.19 C ANISOU 123 CZ PHE A 12 5135 6960 5836 -622 -391 364 C ATOM 124 N LEU A 13 14.200 11.354 28.442 1.00 33.34 N ANISOU 124 N LEU A 13 3586 5121 3961 -160 -339 302 N ATOM 125 CA LEU A 13 14.546 11.095 29.841 1.00 36.78 C ANISOU 125 CA LEU A 13 4036 5573 4364 -137 -390 294 C ATOM 126 C LEU A 13 14.681 9.605 30.112 1.00 41.55 C ANISOU 126 C LEU A 13 4592 6224 4971 -62 -357 312 C ATOM 127 O LEU A 13 15.495 9.197 30.946 1.00 50.29 O ANISOU 127 O LEU A 13 5679 7363 6067 -52 -419 323 O ATOM 128 CB LEU A 13 13.501 11.695 30.774 1.00 30.50 C ANISOU 128 CB LEU A 13 3363 4706 3521 -114 -398 250 C ATOM 129 CG LEU A 13 13.228 13.189 30.653 1.00 35.78 C ANISOU 129 CG LEU A 13 4102 5308 4185 -171 -441 223 C ATOM 130 CD1 LEU A 13 12.109 13.562 31.595 1.00 30.10 C ANISOU 130 CD1 LEU A 13 3489 4519 3430 -127 -423 166 C ATOM 131 CD2 LEU A 13 14.498 13.960 30.992 1.00 34.00 C ANISOU 131 CD2 LEU A 13 3865 5102 3950 -259 -533 237 C ATOM 132 N SER A 14 13.870 8.777 29.445 1.00 43.18 N ANISOU 132 N SER A 14 4789 6424 5193 -8 -275 314 N ATOM 133 CA SER A 14 14.008 7.329 29.607 1.00 41.24 C ANISOU 133 CA SER A 14 4507 6212 4951 60 -243 333 C ATOM 134 C SER A 14 15.369 6.868 29.121 1.00 40.46 C ANISOU 134 C SER A 14 4290 6181 4901 52 -264 360 C ATOM 135 O SER A 14 16.072 6.109 29.804 1.00 41.42 O ANISOU 135 O SER A 14 4380 6331 5027 92 -312 373 O ATOM 136 CB SER A 14 12.905 6.595 28.847 1.00 37.69 C ANISOU 136 CB SER A 14 4066 5737 4519 107 -155 327 C ATOM 137 OG SER A 14 11.621 6.973 29.293 1.00 44.14 O ANISOU 137 OG SER A 14 4961 6491 5320 119 -128 291 O ATOM 138 N TYR A 15 15.759 7.331 27.932 1.00 41.77 N ANISOU 138 N TYR A 15 4397 6367 5108 -1 -229 365 N ATOM 139 CA TYR A 15 17.073 7.023 27.396 1.00 45.29 C ANISOU 139 CA TYR A 15 4716 6878 5616 -22 -222 377 C ATOM 140 C TYR A 15 18.173 7.387 28.392 1.00 50.26 C ANISOU 140 C TYR A 15 5287 7537 6272 -50 -328 375 C ATOM 141 O TYR A 15 19.087 6.595 28.643 1.00 45.89 O ANISOU 141 O TYR A 15 4632 7028 5774 -8 -361 378 O ATOM 142 CB TYR A 15 17.248 7.769 26.077 1.00 45.72 C ANISOU 142 CB TYR A 15 4755 6931 5686 -105 -159 379 C ATOM 143 CG TYR A 15 18.600 7.611 25.459 1.00 51.13 C ANISOU 143 CG TYR A 15 5303 7680 6442 -148 -119 381 C ATOM 144 CD1 TYR A 15 19.065 6.367 25.078 1.00 50.67 C ANISOU 144 CD1 TYR A 15 5154 7666 6431 -80 -62 379 C ATOM 145 CD2 TYR A 15 19.414 8.712 25.243 1.00 57.03 C ANISOU 145 CD2 TYR A 15 6010 8440 7219 -262 -130 377 C ATOM 146 CE1 TYR A 15 20.313 6.221 24.496 1.00 54.10 C ANISOU 146 CE1 TYR A 15 5445 8161 6950 -116 -7 366 C ATOM 147 CE2 TYR A 15 20.662 8.576 24.663 1.00 59.22 C ANISOU 147 CE2 TYR A 15 6144 8779 7580 -312 -71 368 C ATOM 148 CZ TYR A 15 21.106 7.327 24.296 1.00 56.38 C ANISOU 148 CZ TYR A 15 5680 8466 7276 -235 -6 359 C ATOM 149 OH TYR A 15 22.340 7.185 23.722 1.00 58.39 O ANISOU 149 OH TYR A 15 5775 8781 7630 -280 69 337 O ATOM 150 N LYS A 16 18.079 8.580 28.995 1.00 48.22 N ANISOU 150 N LYS A 16 5096 7245 5980 -115 -396 364 N ATOM 151 CA LYS A 16 19.138 9.057 29.887 1.00 43.60 C ANISOU 151 CA LYS A 16 4465 6680 5422 -157 -514 358 C ATOM 152 C LYS A 16 19.190 8.257 31.177 1.00 41.83 C ANISOU 152 C LYS A 16 4286 6447 5161 -76 -605 360 C ATOM 153 O LYS A 16 20.273 7.932 31.658 1.00 53.41 O ANISOU 153 O LYS A 16 5664 7947 6684 -66 -703 361 O ATOM 154 CB LYS A 16 18.945 10.543 30.193 1.00 41.83 C ANISOU 154 CB LYS A 16 4328 6408 5159 -248 -565 343 C ATOM 155 CG LYS A 16 19.335 11.410 29.024 1.00 55.35 C ANISOU 155 CG LYS A 16 5990 8127 6915 -351 -509 347 C ATOM 156 CD LYS A 16 20.825 11.280 28.798 1.00 63.86 C ANISOU 156 CD LYS A 16 6892 9274 8098 -405 -528 346 C ATOM 157 CE LYS A 16 21.212 11.559 27.372 1.00 58.42 C ANISOU 157 CE LYS A 16 6135 8606 7454 -487 -406 353 C ATOM 158 NZ LYS A 16 22.688 11.634 27.359 1.00 58.32 N ANISOU 158 NZ LYS A 16 5940 8656 7561 -557 -427 338 N ATOM 159 N LEU A 17 18.033 7.944 31.757 1.00 41.04 N ANISOU 159 N LEU A 17 4328 6295 4969 -23 -578 359 N ATOM 160 CA LEU A 17 18.010 7.150 32.975 1.00 48.06 C ANISOU 160 CA LEU A 17 5302 7162 5798 44 -649 366 C ATOM 161 C LEU A 17 18.598 5.759 32.738 1.00 51.29 C ANISOU 161 C LEU A 17 5617 7608 6263 123 -653 387 C ATOM 162 O LEU A 17 19.466 5.298 33.491 1.00 50.33 O ANISOU 162 O LEU A 17 5476 7492 6157 158 -776 395 O ATOM 163 CB LEU A 17 16.579 7.069 33.496 1.00 42.51 C ANISOU 163 CB LEU A 17 4762 6394 4994 71 -575 354 C ATOM 164 CG LEU A 17 16.170 8.406 34.102 1.00 45.96 C ANISOU 164 CG LEU A 17 5307 6783 5372 9 -604 322 C ATOM 165 CD1 LEU A 17 14.667 8.529 34.281 1.00 43.53 C ANISOU 165 CD1 LEU A 17 5116 6416 5007 29 -493 292 C ATOM 166 CD2 LEU A 17 16.889 8.605 35.428 1.00 50.14 C ANISOU 166 CD2 LEU A 17 5922 7292 5837 -4 -747 320 C ATOM 167 N SER A 18 18.153 5.082 31.685 1.00 49.21 N ANISOU 167 N SER A 18 5302 7362 6035 157 -531 394 N ATOM 168 CA SER A 18 18.634 3.728 31.452 1.00 52.40 C ANISOU 168 CA SER A 18 5632 7789 6488 241 -528 409 C ATOM 169 C SER A 18 20.073 3.727 30.953 1.00 53.89 C ANISOU 169 C SER A 18 5631 8042 6802 232 -574 400 C ATOM 170 O SER A 18 20.818 2.774 31.208 1.00 54.52 O ANISOU 170 O SER A 18 5642 8136 6939 308 -639 403 O ATOM 171 CB SER A 18 17.707 3.013 30.473 1.00 50.98 C ANISOU 171 CB SER A 18 5465 7601 6304 276 -387 413 C ATOM 172 OG SER A 18 17.806 3.588 29.207 1.00 47.61 O ANISOU 172 OG SER A 18 4954 7206 5930 222 -306 402 O ATOM 173 N GLN A 19 20.485 4.787 30.260 1.00 54.52 N ANISOU 173 N GLN A 19 5626 8155 6933 139 -541 384 N ATOM 174 CA GLN A 19 21.885 4.924 29.853 1.00 49.43 C ANISOU 174 CA GLN A 19 4788 7572 6422 109 -570 366 C ATOM 175 C GLN A 19 22.815 4.945 31.053 1.00 58.45 C ANISOU 175 C GLN A 19 5890 8714 7606 126 -757 359 C ATOM 176 O GLN A 19 23.953 4.475 30.968 1.00 71.94 O ANISOU 176 O GLN A 19 7425 10464 9445 159 -812 340 O ATOM 177 CB GLN A 19 22.038 6.202 29.030 1.00 51.96 C ANISOU 177 CB GLN A 19 5068 7910 6764 -19 -500 355 C ATOM 178 CG GLN A 19 23.352 6.469 28.398 1.00 57.72 C ANISOU 178 CG GLN A 19 5598 8701 7632 -83 -476 330 C ATOM 179 CD GLN A 19 23.324 7.794 27.672 1.00 67.37 C ANISOU 179 CD GLN A 19 6839 9919 8841 -224 -404 327 C ATOM 180 OE1 GLN A 19 22.890 8.807 28.231 1.00 67.10 O ANISOU 180 OE1 GLN A 19 6920 9840 8736 -285 -474 335 O ATOM 181 NE2 GLN A 19 23.759 7.794 26.412 1.00 69.24 N ANISOU 181 NE2 GLN A 19 6983 10190 9134 -278 -258 316 N ATOM 182 N LYS A 20 22.356 5.498 32.172 1.00 57.47 N ANISOU 182 N LYS A 20 5923 8537 7376 107 -861 367 N ATOM 183 CA LYS A 20 23.102 5.486 33.420 1.00 62.85 C ANISOU 183 CA LYS A 20 6619 9197 8063 127 -1062 364 C ATOM 184 C LYS A 20 22.645 4.367 34.338 1.00 65.35 C ANISOU 184 C LYS A 20 7087 9458 8284 235 -1129 389 C ATOM 185 O LYS A 20 22.970 4.380 35.526 1.00 69.62 O ANISOU 185 O LYS A 20 7725 9954 8773 252 -1301 393 O ATOM 186 CB LYS A 20 22.982 6.843 34.129 1.00 63.40 C ANISOU 186 CB LYS A 20 6794 9232 8062 28 -1143 354 C ATOM 187 N GLY A 21 21.870 3.419 33.824 1.00 65.44 N ANISOU 187 N GLY A 21 7141 9461 8261 301 -1000 406 N ATOM 188 CA GLY A 21 21.563 2.214 34.565 1.00 65.52 C ANISOU 188 CA GLY A 21 7280 9416 8198 400 -1052 432 C ATOM 189 C GLY A 21 20.408 2.294 35.532 1.00 66.97 C ANISOU 189 C GLY A 21 7719 9524 8204 388 -1037 449 C ATOM 190 O GLY A 21 20.256 1.387 36.358 1.00 72.25 O ANISOU 190 O GLY A 21 8528 10131 8791 453 -1103 474 O ATOM 191 N TYR A 22 19.575 3.327 35.453 1.00 60.27 N ANISOU 191 N TYR A 22 6941 8667 7291 308 -946 434 N ATOM 192 CA TYR A 22 18.494 3.521 36.408 1.00 53.75 C ANISOU 192 CA TYR A 22 6344 7768 6308 291 -914 435 C ATOM 193 C TYR A 22 17.150 3.175 35.776 1.00 52.90 C ANISOU 193 C TYR A 22 6277 7649 6174 297 -720 432 C ATOM 194 O TYR A 22 16.859 3.561 34.636 1.00 45.56 O ANISOU 194 O TYR A 22 5231 6759 5320 271 -618 418 O ATOM 195 CB TYR A 22 18.455 4.962 36.925 1.00 60.91 C ANISOU 195 CB TYR A 22 7315 8660 7167 204 -960 406 C ATOM 196 CG TYR A 22 19.748 5.513 37.537 1.00 72.48 C ANISOU 196 CG TYR A 22 8738 10134 8668 176 -1164 401 C ATOM 197 CD1 TYR A 22 20.693 6.171 36.749 1.00 71.75 C ANISOU 197 CD1 TYR A 22 8436 10107 8718 127 -1201 386 C ATOM 198 CD2 TYR A 22 19.997 5.420 38.912 1.00 73.92 C ANISOU 198 CD2 TYR A 22 9101 10250 8737 188 -1319 407 C ATOM 199 CE1 TYR A 22 21.853 6.701 37.304 1.00 71.17 C ANISOU 199 CE1 TYR A 22 8304 10039 8697 91 -1390 374 C ATOM 200 CE2 TYR A 22 21.157 5.952 39.475 1.00 73.92 C ANISOU 200 CE2 TYR A 22 9062 10249 8777 159 -1529 397 C ATOM 201 CZ TYR A 22 22.079 6.588 38.661 1.00 76.09 C ANISOU 201 CZ TYR A 22 9097 10596 9217 111 -1564 378 C ATOM 202 OH TYR A 22 23.230 7.116 39.196 1.00 82.99 O ANISOU 202 OH TYR A 22 9909 11469 10154 74 -1773 362 O ATOM 203 N SER A 23 16.324 2.462 36.528 1.00 47.68 N ANISOU 203 N SER A 23 5789 6923 5404 325 -673 443 N ATOM 204 CA SER A 23 14.973 2.146 36.109 1.00 54.11 C ANISOU 204 CA SER A 23 6647 7715 6199 323 -496 432 C ATOM 205 C SER A 23 13.980 2.940 36.944 1.00 58.92 C ANISOU 205 C SER A 23 7413 8269 6705 270 -429 398 C ATOM 206 O SER A 23 14.198 3.183 38.132 1.00 69.65 O ANISOU 206 O SER A 23 8927 9581 7954 253 -507 397 O ATOM 207 CB SER A 23 14.693 0.643 36.230 1.00 63.64 C ANISOU 207 CB SER A 23 7919 8886 7377 385 -458 464 C ATOM 208 OG SER A 23 15.016 0.153 37.518 1.00 69.97 O ANISOU 208 OG SER A 23 8898 9624 8062 404 -558 489 O ATOM 209 N TRP A 24 12.889 3.355 36.304 1.00 53.58 N ANISOU 209 N TRP A 24 6698 7590 6068 246 -290 363 N ATOM 210 CA TRP A 24 11.848 4.140 36.948 1.00 51.62 C ANISOU 210 CA TRP A 24 6565 7290 5757 205 -202 314 C ATOM 211 C TRP A 24 10.576 3.350 37.202 1.00 55.70 C ANISOU 211 C TRP A 24 7164 7757 6243 212 -43 297 C ATOM 212 O TRP A 24 9.589 3.935 37.651 1.00 66.21 O ANISOU 212 O TRP A 24 8565 9045 7546 182 61 243 O ATOM 213 CB TRP A 24 11.516 5.359 36.090 1.00 54.00 C ANISOU 213 CB TRP A 24 6758 7613 6146 173 -176 275 C ATOM 214 CG TRP A 24 11.182 4.972 34.703 1.00 54.15 C ANISOU 214 CG TRP A 24 6631 7667 6278 195 -115 282 C ATOM 215 CD1 TRP A 24 9.934 4.763 34.183 1.00 58.74 C ANISOU 215 CD1 TRP A 24 7187 8221 6909 205 6 251 C ATOM 216 CD2 TRP A 24 12.108 4.692 33.651 1.00 48.05 C ANISOU 216 CD2 TRP A 24 5721 6955 5581 208 -173 318 C ATOM 217 NE1 TRP A 24 10.028 4.383 32.863 1.00 52.43 N ANISOU 217 NE1 TRP A 24 6264 7458 6199 223 10 270 N ATOM 218 CE2 TRP A 24 11.355 4.337 32.513 1.00 50.27 C ANISOU 218 CE2 TRP A 24 5926 7239 5936 224 -85 311 C ATOM 219 CE3 TRP A 24 13.503 4.689 33.563 1.00 49.24 C ANISOU 219 CE3 TRP A 24 5801 7155 5752 207 -286 350 C ATOM 220 CZ2 TRP A 24 11.955 4.005 31.298 1.00 52.20 C ANISOU 220 CZ2 TRP A 24 6054 7531 6250 236 -97 336 C ATOM 221 CZ3 TRP A 24 14.093 4.365 32.355 1.00 45.83 C ANISOU 221 CZ3 TRP A 24 5228 6776 5409 218 -281 369 C ATOM 222 CH2 TRP A 24 13.323 4.029 31.242 1.00 47.90 C ANISOU 222 CH2 TRP A 24 5444 7037 5720 231 -182 363 C ATOM 223 N SER A 25 10.561 2.053 36.900 1.00 51.66 N ANISOU 223 N SER A 25 6637 7246 5746 250 -16 335 N ATOM 224 CA SER A 25 9.398 1.197 37.098 1.00 48.67 C ANISOU 224 CA SER A 25 6329 6817 5348 245 137 322 C ATOM 225 C SER A 25 9.841 -0.248 36.925 1.00 51.41 C ANISOU 225 C SER A 25 6688 7159 5687 290 105 380 C ATOM 226 O SER A 25 10.906 -0.522 36.363 1.00 49.22 O ANISOU 226 O SER A 25 6315 6928 5458 335 -13 417 O ATOM 227 CB SER A 25 8.270 1.531 36.114 1.00 46.60 C ANISOU 227 CB SER A 25 5935 6563 5208 235 256 272 C ATOM 228 OG SER A 25 8.667 1.239 34.779 1.00 55.09 O ANISOU 228 OG SER A 25 6852 7691 6389 268 208 296 O ATOM 229 N GLN A 26 9.011 -1.173 37.417 1.00 55.62 N ANISOU 229 N GLN A 26 7339 7629 6164 275 220 383 N ATOM 230 CA GLN A 26 9.314 -2.588 37.229 1.00 59.86 C ANISOU 230 CA GLN A 26 7904 8146 6696 317 197 436 C ATOM 231 C GLN A 26 9.385 -2.926 35.746 1.00 52.00 C ANISOU 231 C GLN A 26 6708 7204 5844 357 196 437 C ATOM 232 O GLN A 26 10.288 -3.646 35.303 1.00 49.52 O ANISOU 232 O GLN A 26 6347 6911 5557 417 102 478 O ATOM 233 CB GLN A 26 8.275 -3.462 37.941 1.00 58.11 C ANISOU 233 CB GLN A 26 7846 7838 6395 274 344 434 C ATOM 234 N MET A 83 8.449 -2.393 34.959 1.00 53.77 N ANISOU 234 N MET A 83 6819 7446 6163 330 294 389 N ATOM 235 CA MET A 83 8.491 -2.608 33.516 1.00 55.87 C ANISOU 235 CA MET A 83 6924 7756 6549 361 285 387 C ATOM 236 C MET A 83 9.806 -2.105 32.930 1.00 51.65 C ANISOU 236 C MET A 83 6288 7291 6046 395 158 409 C ATOM 237 O MET A 83 10.440 -2.795 32.120 1.00 47.91 O ANISOU 237 O MET A 83 5739 6844 5620 442 120 434 O ATOM 238 CB MET A 83 7.288 -1.922 32.863 1.00 56.94 C ANISOU 238 CB MET A 83 6972 7887 6774 325 377 328 C ATOM 239 CG MET A 83 7.027 -2.268 31.395 1.00 68.92 C ANISOU 239 CG MET A 83 8363 9422 8400 346 380 321 C ATOM 240 SD MET A 83 6.598 -4.000 31.030 1.00 75.12 S ANISOU 240 SD MET A 83 9176 10161 9203 366 437 344 S ATOM 241 CE MET A 83 5.782 -4.547 32.531 1.00 71.74 C ANISOU 241 CE MET A 83 8906 9659 8694 316 550 338 C ATOM 242 N ALA A 84 10.247 -0.917 33.356 1.00 44.10 N ANISOU 242 N ALA A 84 5330 6360 5066 369 98 396 N ATOM 243 CA ALA A 84 11.480 -0.352 32.824 1.00 36.88 C ANISOU 243 CA ALA A 84 4309 5509 4194 383 -11 410 C ATOM 244 C ALA A 84 12.657 -1.268 33.088 1.00 41.85 C ANISOU 244 C ALA A 84 4940 6151 4811 440 -109 453 C ATOM 245 O ALA A 84 13.533 -1.431 32.226 1.00 45.91 O ANISOU 245 O ALA A 84 5326 6716 5402 471 -151 462 O ATOM 246 CB ALA A 84 11.749 1.027 33.433 1.00 38.30 C ANISOU 246 CB ALA A 84 4512 5699 4340 336 -67 389 C ATOM 247 N ALA A 85 12.696 -1.875 34.281 1.00 42.31 N ANISOU 247 N ALA A 85 5148 6154 4773 454 -146 476 N ATOM 248 CA ALA A 85 13.800 -2.766 34.613 1.00 44.62 C ANISOU 248 CA ALA A 85 5455 6441 5059 521 -267 515 C ATOM 249 C ALA A 85 13.759 -4.026 33.757 1.00 35.69 C ANISOU 249 C ALA A 85 4270 5303 3987 581 -222 530 C ATOM 250 O ALA A 85 14.808 -4.565 33.392 1.00 43.23 O ANISOU 250 O ALA A 85 5138 6283 5006 648 -307 544 O ATOM 251 CB ALA A 85 13.779 -3.099 36.106 1.00 32.60 C ANISOU 251 CB ALA A 85 4149 4841 3398 519 -329 540 C ATOM 252 N VAL A 86 12.565 -4.492 33.410 1.00 35.30 N ANISOU 252 N VAL A 86 4263 5218 3932 558 -89 521 N ATOM 253 CA VAL A 86 12.456 -5.625 32.504 1.00 36.24 C ANISOU 253 CA VAL A 86 4335 5326 4110 606 -45 529 C ATOM 254 C VAL A 86 12.963 -5.246 31.117 1.00 43.98 C ANISOU 254 C VAL A 86 5133 6381 5198 623 -39 507 C ATOM 255 O VAL A 86 13.755 -5.984 30.514 1.00 43.98 O ANISOU 255 O VAL A 86 5062 6396 5252 689 -72 515 O ATOM 256 CB VAL A 86 11.008 -6.142 32.471 1.00 39.17 C ANISOU 256 CB VAL A 86 4788 5636 4458 563 91 518 C ATOM 257 CG1 VAL A 86 10.903 -7.358 31.544 1.00 34.61 C ANISOU 257 CG1 VAL A 86 4178 5037 3935 610 124 526 C ATOM 258 CG2 VAL A 86 10.555 -6.514 33.890 1.00 34.12 C ANISOU 258 CG2 VAL A 86 4350 4918 3698 532 109 538 C ATOM 259 N LYS A 87 12.530 -4.085 30.594 1.00 40.45 N ANISOU 259 N LYS A 87 4618 5972 4779 562 7 477 N ATOM 260 CA LYS A 87 12.967 -3.682 29.256 1.00 35.19 C ANISOU 260 CA LYS A 87 3813 5364 4193 562 22 460 C ATOM 261 C LYS A 87 14.478 -3.562 29.190 1.00 39.48 C ANISOU 261 C LYS A 87 4257 5963 4780 597 -64 467 C ATOM 262 O LYS A 87 15.109 -4.107 28.283 1.00 46.42 O ANISOU 262 O LYS A 87 5047 6869 5722 640 -46 461 O ATOM 263 CB LYS A 87 12.316 -2.367 28.826 1.00 32.00 C ANISOU 263 CB LYS A 87 3381 4976 3801 490 59 431 C ATOM 264 CG LYS A 87 10.825 -2.482 28.572 1.00 35.25 C ANISOU 264 CG LYS A 87 3842 5337 4217 464 142 408 C ATOM 265 CD LYS A 87 10.214 -1.114 28.337 1.00 44.27 C ANISOU 265 CD LYS A 87 4964 6481 5377 406 151 375 C ATOM 266 CE LYS A 87 8.726 -1.201 28.024 1.00 44.90 C ANISOU 266 CE LYS A 87 5061 6506 5492 388 219 340 C ATOM 267 NZ LYS A 87 8.135 0.174 27.873 1.00 47.88 N ANISOU 267 NZ LYS A 87 5420 6874 5897 347 209 303 N ATOM 268 N GLN A 88 15.079 -2.866 30.161 1.00 45.90 N ANISOU 268 N GLN A 88 5082 6790 5568 579 -156 474 N ATOM 269 CA GLN A 88 16.532 -2.724 30.182 1.00 51.16 C ANISOU 269 CA GLN A 88 5632 7506 6299 608 -252 473 C ATOM 270 C GLN A 88 17.211 -4.087 30.234 1.00 50.18 C ANISOU 270 C GLN A 88 5490 7364 6213 710 -300 486 C ATOM 271 O GLN A 88 18.174 -4.348 29.498 1.00 42.78 O ANISOU 271 O GLN A 88 4409 6472 5375 752 -304 468 O ATOM 272 CB GLN A 88 16.969 -1.875 31.381 1.00 55.06 C ANISOU 272 CB GLN A 88 6171 7999 6750 574 -369 478 C ATOM 273 CG GLN A 88 16.588 -0.407 31.297 1.00 64.49 C ANISOU 273 CG GLN A 88 7361 9215 7927 480 -342 459 C ATOM 274 CD GLN A 88 16.590 0.284 32.661 1.00 65.40 C ANISOU 274 CD GLN A 88 7591 9298 7958 446 -437 461 C ATOM 275 OE1 GLN A 88 17.131 -0.237 33.639 1.00 69.49 O ANISOU 275 OE1 GLN A 88 8177 9787 8439 488 -549 480 O ATOM 276 NE2 GLN A 88 15.964 1.453 32.730 1.00 59.42 N ANISOU 276 NE2 GLN A 88 6874 8535 7167 373 -400 440 N ATOM 277 N ALA A 89 16.734 -4.961 31.125 1.00 35.80 N ANISOU 277 N ALA A 89 3820 5468 4314 748 -333 514 N ATOM 278 CA ALA A 89 17.309 -6.297 31.223 1.00 37.30 C ANISOU 278 CA ALA A 89 4021 5619 4532 851 -393 529 C ATOM 279 C ALA A 89 17.181 -7.040 29.901 1.00 41.01 C ANISOU 279 C ALA A 89 4410 6100 5070 889 -284 510 C ATOM 280 O ALA A 89 18.126 -7.694 29.444 1.00 36.56 O ANISOU 280 O ALA A 89 3743 5551 4595 972 -316 495 O ATOM 281 CB ALA A 89 16.624 -7.078 32.341 1.00 41.49 C ANISOU 281 CB ALA A 89 4768 6051 4944 864 -424 568 C ATOM 282 N LEU A 90 16.023 -6.915 29.255 1.00 38.56 N ANISOU 282 N LEU A 90 4144 5781 4727 832 -158 503 N ATOM 283 CA LEU A 90 15.784 -7.658 28.034 1.00 36.70 C ANISOU 283 CA LEU A 90 3870 5540 4535 862 -64 485 C ATOM 284 C LEU A 90 16.678 -7.144 26.908 1.00 46.51 C ANISOU 284 C LEU A 90 4946 6861 5866 862 -28 450 C ATOM 285 O LEU A 90 17.341 -7.934 26.219 1.00 49.90 O ANISOU 285 O LEU A 90 5307 7294 6359 933 -5 430 O ATOM 286 CB LEU A 90 14.299 -7.575 27.686 1.00 34.92 C ANISOU 286 CB LEU A 90 3731 5277 4259 794 35 482 C ATOM 287 CG LEU A 90 13.851 -8.633 26.695 1.00 41.82 C ANISOU 287 CG LEU A 90 4625 6112 5155 828 107 471 C ATOM 288 CD1 LEU A 90 14.558 -9.964 26.964 1.00 41.21 C ANISOU 288 CD1 LEU A 90 4576 5990 5092 931 56 485 C ATOM 289 CD2 LEU A 90 12.343 -8.780 26.728 1.00 37.50 C ANISOU 289 CD2 LEU A 90 4175 5506 4566 767 172 471 C ATOM 290 N ARG A 91 16.750 -5.817 26.743 1.00 40.29 N ANISOU 290 N ARG A 91 4098 6127 5081 780 -16 440 N ATOM 291 CA ARG A 91 17.665 -5.235 25.765 1.00 41.02 C ANISOU 291 CA ARG A 91 4046 6291 5251 759 28 409 C ATOM 292 C ARG A 91 19.101 -5.699 25.989 1.00 49.45 C ANISOU 292 C ARG A 91 4982 7390 6417 837 -37 392 C ATOM 293 O ARG A 91 19.812 -6.033 25.033 1.00 55.65 O ANISOU 293 O ARG A 91 5657 8207 7280 868 35 356 O ATOM 294 CB ARG A 91 17.608 -3.715 25.829 1.00 46.32 C ANISOU 294 CB ARG A 91 4693 7002 5905 655 22 407 C ATOM 295 CG ARG A 91 16.231 -3.116 25.673 1.00 43.86 C ANISOU 295 CG ARG A 91 4492 6654 5518 587 66 414 C ATOM 296 CD ARG A 91 16.362 -1.632 25.663 1.00 43.10 C ANISOU 296 CD ARG A 91 4367 6591 5418 497 51 409 C ATOM 297 NE ARG A 91 15.141 -0.950 26.056 1.00 52.91 N ANISOU 297 NE ARG A 91 5713 7791 6599 448 49 412 N ATOM 298 CZ ARG A 91 15.085 -0.009 26.997 1.00 53.86 C ANISOU 298 CZ ARG A 91 5863 7910 6691 405 -13 414 C ATOM 299 NH1 ARG A 91 16.189 0.372 27.643 1.00 57.23 N ANISOU 299 NH1 ARG A 91 6229 8374 7141 399 -92 418 N ATOM 300 NH2 ARG A 91 13.927 0.562 27.279 1.00 50.08 N ANISOU 300 NH2 ARG A 91 5469 7388 6170 370 2 405 N ATOM 301 N GLU A 92 19.559 -5.708 27.241 1.00 47.58 N ANISOU 301 N GLU A 92 4755 7140 6183 869 -176 411 N ATOM 302 CA GLU A 92 20.947 -6.077 27.485 1.00 46.02 C ANISOU 302 CA GLU A 92 4414 6968 6104 948 -267 388 C ATOM 303 C GLU A 92 21.185 -7.550 27.188 1.00 45.17 C ANISOU 303 C GLU A 92 4306 6815 6041 1072 -260 376 C ATOM 304 O GLU A 92 22.189 -7.907 26.554 1.00 44.70 O ANISOU 304 O GLU A 92 4086 6791 6109 1133 -233 330 O ATOM 305 CB GLU A 92 21.345 -5.753 28.919 1.00 50.44 C ANISOU 305 CB GLU A 92 5010 7509 6646 955 -448 412 C ATOM 306 CG GLU A 92 21.673 -4.297 29.135 1.00 71.21 C ANISOU 306 CG GLU A 92 7572 10197 9289 850 -478 403 C ATOM 307 CD GLU A 92 21.521 -3.879 30.583 1.00 93.62 C ANISOU 307 CD GLU A 92 10539 12993 12041 831 -632 434 C ATOM 308 OE1 GLU A 92 21.894 -4.675 31.475 1.00100.94 O ANISOU 308 OE1 GLU A 92 11526 13865 12961 917 -773 452 O ATOM 309 OE2 GLU A 92 21.011 -2.761 30.825 1.00 99.91 O ANISOU 309 OE2 GLU A 92 11394 13801 12768 731 -614 441 O ATOM 310 N ALA A 93 20.272 -8.421 27.625 1.00 38.04 N ANISOU 310 N ALA A 93 3581 5829 5042 1108 -275 413 N ATOM 311 CA ALA A 93 20.421 -9.837 27.303 1.00 41.82 C ANISOU 311 CA ALA A 93 4084 6250 5556 1222 -268 403 C ATOM 312 C ALA A 93 20.483 -10.060 25.790 1.00 41.69 C ANISOU 312 C ALA A 93 3979 6268 5594 1225 -106 356 C ATOM 313 O ALA A 93 21.268 -10.881 25.308 1.00 44.33 O ANISOU 313 O ALA A 93 4224 6596 6025 1325 -92 316 O ATOM 314 CB ALA A 93 19.278 -10.632 27.926 1.00 36.66 C ANISOU 314 CB ALA A 93 3652 5497 4778 1226 -283 452 C ATOM 315 N GLY A 94 19.679 -9.325 25.024 1.00 38.11 N ANISOU 315 N GLY A 94 3559 5844 5079 1119 14 355 N ATOM 316 CA GLY A 94 19.688 -9.504 23.580 1.00 44.80 C ANISOU 316 CA GLY A 94 4363 6710 5949 1112 161 313 C ATOM 317 C GLY A 94 21.015 -9.117 22.960 1.00 52.68 C ANISOU 317 C GLY A 94 5165 7785 7068 1123 214 258 C ATOM 318 O GLY A 94 21.580 -9.861 22.149 1.00 50.78 O ANISOU 318 O GLY A 94 4859 7543 6894 1194 296 210 O ATOM 319 N ASP A 95 21.531 -7.942 23.337 1.00 46.96 N ANISOU 319 N ASP A 95 4340 7125 6376 1049 176 260 N ATOM 320 CA ASP A 95 22.867 -7.552 22.909 1.00 43.21 C ANISOU 320 CA ASP A 95 3656 6723 6038 1049 220 205 C ATOM 321 C ASP A 95 23.876 -8.642 23.240 1.00 53.06 C ANISOU 321 C ASP A 95 4785 7954 7422 1198 150 167 C ATOM 322 O ASP A 95 24.647 -9.082 22.378 1.00 62.54 O ANISOU 322 O ASP A 95 5857 9179 8727 1248 260 101 O ATOM 323 CB ASP A 95 23.274 -6.228 23.568 1.00 44.91 C ANISOU 323 CB ASP A 95 3792 6993 6277 954 143 219 C ATOM 324 CG ASP A 95 22.443 -5.045 23.082 1.00 55.09 C ANISOU 324 CG ASP A 95 5177 8299 7457 810 222 244 C ATOM 325 OD1 ASP A 95 21.801 -5.161 22.014 1.00 46.63 O ANISOU 325 OD1 ASP A 95 4192 7209 6316 778 351 238 O ATOM 326 OD2 ASP A 95 22.439 -3.997 23.774 1.00 61.42 O ANISOU 326 OD2 ASP A 95 5975 9121 8240 733 141 267 O ATOM 327 N GLU A 96 23.877 -9.100 24.491 1.00 50.01 N ANISOU 327 N GLU A 96 4451 7518 7034 1272 -34 203 N ATOM 328 CA GLU A 96 24.872 -10.084 24.892 1.00 52.65 C ANISOU 328 CA GLU A 96 4677 7824 7506 1423 -140 168 C ATOM 329 C GLU A 96 24.622 -11.409 24.185 1.00 51.54 C ANISOU 329 C GLU A 96 4604 7619 7361 1527 -56 144 C ATOM 330 O GLU A 96 25.567 -12.065 23.733 1.00 60.05 O ANISOU 330 O GLU A 96 5531 8700 8584 1633 -26 76 O ATOM 331 CB GLU A 96 24.874 -10.227 26.417 1.00 53.62 C ANISOU 331 CB GLU A 96 4886 7889 7597 1469 -374 220 C ATOM 332 CG GLU A 96 25.909 -11.193 26.995 1.00 78.07 C ANISOU 332 CG GLU A 96 7890 10938 10837 1633 -539 191 C ATOM 333 CD GLU A 96 27.360 -10.687 26.968 1.00 97.82 C ANISOU 333 CD GLU A 96 10100 13513 13555 1659 -594 120 C ATOM 334 OE1 GLU A 96 27.966 -10.644 25.875 1.00101.60 O ANISOU 334 OE1 GLU A 96 10389 14056 14160 1660 -426 45 O ATOM 335 OE2 GLU A 96 27.903 -10.354 28.050 1.00103.50 O ANISOU 335 OE2 GLU A 96 10783 14222 14321 1676 -805 134 O ATOM 336 N PHE A 97 23.353 -11.786 24.017 1.00 46.90 N ANISOU 336 N PHE A 97 4231 6971 6617 1493 -7 191 N ATOM 337 CA PHE A 97 23.041 -12.971 23.226 1.00 51.55 C ANISOU 337 CA PHE A 97 4898 7497 7193 1572 83 166 C ATOM 338 C PHE A 97 23.616 -12.857 21.819 1.00 53.14 C ANISOU 338 C PHE A 97 4968 7755 7467 1562 275 88 C ATOM 339 O PHE A 97 24.323 -13.755 21.350 1.00 55.11 O ANISOU 339 O PHE A 97 5138 7982 7821 1680 318 25 O ATOM 340 CB PHE A 97 21.529 -13.188 23.156 1.00 47.38 C ANISOU 340 CB PHE A 97 4602 6905 6495 1503 119 222 C ATOM 341 CG PHE A 97 21.136 -14.393 22.357 1.00 46.53 C ANISOU 341 CG PHE A 97 4592 6723 6365 1571 199 198 C ATOM 342 CD1 PHE A 97 20.916 -14.297 20.983 1.00 52.46 C ANISOU 342 CD1 PHE A 97 5344 7496 7093 1525 368 154 C ATOM 343 CD2 PHE A 97 21.008 -15.629 22.968 1.00 46.41 C ANISOU 343 CD2 PHE A 97 4687 6603 6344 1678 99 219 C ATOM 344 CE1 PHE A 97 20.568 -15.411 20.236 1.00 50.24 C ANISOU 344 CE1 PHE A 97 5166 7138 6785 1587 435 127 C ATOM 345 CE2 PHE A 97 20.657 -16.749 22.231 1.00 50.28 C ANISOU 345 CE2 PHE A 97 5275 7015 6815 1739 168 194 C ATOM 346 CZ PHE A 97 20.435 -16.641 20.867 1.00 50.65 C ANISOU 346 CZ PHE A 97 5316 7089 6842 1694 335 146 C ATOM 347 N GLU A 98 23.313 -11.754 21.130 1.00 50.62 N ANISOU 347 N GLU A 98 4642 7502 7090 1422 395 88 N ATOM 348 CA GLU A 98 23.717 -11.605 19.736 1.00 47.91 C ANISOU 348 CA GLU A 98 4230 7200 6774 1388 597 21 C ATOM 349 C GLU A 98 25.233 -11.555 19.580 1.00 57.68 C ANISOU 349 C GLU A 98 5211 8501 8204 1446 643 -60 C ATOM 350 O GLU A 98 25.770 -12.091 18.600 1.00 60.40 O ANISOU 350 O GLU A 98 5492 8847 8611 1495 798 -136 O ATOM 351 CB GLU A 98 23.051 -10.363 19.143 1.00 43.88 C ANISOU 351 CB GLU A 98 3793 6732 6149 1220 687 48 C ATOM 352 CG GLU A 98 21.529 -10.539 19.038 1.00 50.49 C ANISOU 352 CG GLU A 98 4863 7498 6822 1175 665 105 C ATOM 353 CD GLU A 98 20.735 -9.249 19.215 1.00 54.56 C ANISOU 353 CD GLU A 98 5449 8038 7243 1036 639 156 C ATOM 354 OE1 GLU A 98 21.303 -8.150 19.014 1.00 58.46 O ANISOU 354 OE1 GLU A 98 5846 8600 7766 949 683 145 O ATOM 355 OE2 GLU A 98 19.534 -9.344 19.555 1.00 49.74 O ANISOU 355 OE2 GLU A 98 4989 7373 6538 1011 576 203 O ATOM 356 N LEU A 99 25.942 -10.940 20.530 1.00 54.50 N ANISOU 356 N LEU A 99 4657 8145 7905 1441 513 -52 N ATOM 357 CA LEU A 99 27.399 -10.950 20.458 1.00 54.46 C ANISOU 357 CA LEU A 99 4379 8195 8117 1503 536 -137 C ATOM 358 C LEU A 99 27.943 -12.359 20.651 1.00 57.67 C ANISOU 358 C LEU A 99 4730 8538 8646 1699 469 -186 C ATOM 359 O LEU A 99 28.893 -12.767 19.969 1.00 63.84 O ANISOU 359 O LEU A 99 5329 9341 9584 1771 590 -284 O ATOM 360 CB LEU A 99 27.991 -9.998 21.497 1.00 63.15 C ANISOU 360 CB LEU A 99 5340 9349 9303 1453 377 -116 C ATOM 361 CG LEU A 99 29.517 -9.985 21.516 1.00 76.34 C ANISOU 361 CG LEU A 99 6699 11076 11232 1515 375 -210 C ATOM 362 CD1 LEU A 99 30.040 -9.505 20.164 1.00 81.78 C ANISOU 362 CD1 LEU A 99 7258 11836 11977 1421 656 -288 C ATOM 363 CD2 LEU A 99 30.058 -9.135 22.656 1.00 76.38 C ANISOU 363 CD2 LEU A 99 6582 11116 11320 1474 173 -187 C ATOM 364 N ARG A 100 27.356 -13.117 21.581 1.00 53.26 N ANISOU 364 N ARG A 100 4329 7890 8018 1787 281 -123 N ATOM 365 CA ARG A 100 27.738 -14.517 21.730 1.00 53.77 C ANISOU 365 CA ARG A 100 4388 7869 8174 1974 208 -161 C ATOM 366 C ARG A 100 27.425 -15.291 20.459 1.00 62.59 C ANISOU 366 C ARG A 100 5586 8951 9246 2006 414 -212 C ATOM 367 O ARG A 100 28.238 -16.101 19.996 1.00 70.59 O ANISOU 367 O ARG A 100 6474 9942 10405 2139 473 -302 O ATOM 368 CB ARG A 100 27.009 -15.134 22.923 1.00 55.35 C ANISOU 368 CB ARG A 100 4800 7966 8265 2031 -14 -70 C ATOM 369 CG ARG A 100 27.883 -15.851 23.912 1.00 69.39 C ANISOU 369 CG ARG A 100 6494 9683 10190 2196 -241 -85 C ATOM 370 CD ARG A 100 27.045 -16.437 25.033 1.00 87.46 C ANISOU 370 CD ARG A 100 9047 11856 12327 2226 -435 14 C ATOM 371 NE ARG A 100 27.620 -16.170 26.351 1.00100.95 N ANISOU 371 NE ARG A 100 10720 13547 14091 2266 -689 45 N ATOM 372 CZ ARG A 100 27.601 -14.976 26.938 1.00105.17 C ANISOU 372 CZ ARG A 100 11223 14151 14587 2143 -748 82 C ATOM 373 NH1 ARG A 100 28.140 -14.808 28.140 1.00108.93 N ANISOU 373 NH1 ARG A 100 11688 14595 15106 2186 -995 107 N ATOM 374 NH2 ARG A 100 27.052 -13.942 26.315 1.00 98.74 N ANISOU 374 NH2 ARG A 100 10401 13428 13688 1980 -569 90 N ATOM 375 N TYR A 101 26.250 -15.035 19.869 1.00 62.20 N ANISOU 375 N TYR A 101 5744 8890 8999 1888 520 -162 N ATOM 376 CA TYR A 101 25.821 -15.789 18.698 1.00 59.53 C ANISOU 376 CA TYR A 101 5527 8502 8591 1910 689 -203 C ATOM 377 C TYR A 101 26.711 -15.493 17.497 1.00 64.00 C ANISOU 377 C TYR A 101 5929 9138 9251 1890 920 -308 C ATOM 378 O TYR A 101 27.161 -16.415 16.808 1.00 66.46 O ANISOU 378 O TYR A 101 6212 9408 9631 1999 1027 -390 O ATOM 379 CB TYR A 101 24.358 -15.477 18.372 1.00 54.41 C ANISOU 379 CB TYR A 101 5126 7825 7723 1778 724 -129 C ATOM 380 CG TYR A 101 23.786 -16.308 17.231 1.00 53.95 C ANISOU 380 CG TYR A 101 5227 7696 7574 1797 861 -164 C ATOM 381 CD1 TYR A 101 23.025 -17.451 17.487 1.00 46.14 C ANISOU 381 CD1 TYR A 101 4419 6592 6518 1872 775 -133 C ATOM 382 CD2 TYR A 101 24.013 -15.956 15.898 1.00 50.43 C ANISOU 382 CD2 TYR A 101 4769 7290 7102 1732 1075 -229 C ATOM 383 CE1 TYR A 101 22.505 -18.220 16.443 1.00 44.20 C ANISOU 383 CE1 TYR A 101 4327 6276 6192 1885 887 -168 C ATOM 384 CE2 TYR A 101 23.509 -16.722 14.856 1.00 45.95 C ANISOU 384 CE2 TYR A 101 4368 6649 6441 1749 1188 -264 C ATOM 385 CZ TYR A 101 22.754 -17.851 15.133 1.00 49.81 C ANISOU 385 CZ TYR A 101 5024 7026 6874 1828 1087 -235 C ATOM 386 OH TYR A 101 22.250 -18.609 14.095 1.00 57.97 O ANISOU 386 OH TYR A 101 6230 7980 7815 1840 1188 -274 O ATOM 387 N ARG A 102 26.964 -14.211 17.217 1.00 61.40 N ANISOU 387 N ARG A 102 5503 8906 8920 1744 1012 -309 N ATOM 388 CA ARG A 102 27.633 -13.880 15.966 1.00 67.02 C ANISOU 388 CA ARG A 102 6113 9673 9677 1689 1267 -400 C ATOM 389 C ARG A 102 29.112 -14.229 16.002 1.00 72.61 C ANISOU 389 C ARG A 102 6526 10421 10643 1806 1315 -511 C ATOM 390 O ARG A 102 29.734 -14.329 14.943 1.00 74.60 O ANISOU 390 O ARG A 102 6692 10697 10954 1801 1550 -609 O ATOM 391 CB ARG A 102 27.450 -12.402 15.617 1.00 64.13 C ANISOU 391 CB ARG A 102 5755 9387 9224 1487 1357 -365 C ATOM 392 CG ARG A 102 28.386 -11.460 16.347 1.00 74.91 C ANISOU 392 CG ARG A 102 6874 10841 10748 1441 1290 -373 C ATOM 393 CD ARG A 102 28.312 -10.056 15.766 1.00 79.56 C ANISOU 393 CD ARG A 102 7479 11497 11254 1238 1422 -355 C ATOM 394 NE ARG A 102 26.952 -9.526 15.807 1.00 81.41 N ANISOU 394 NE ARG A 102 7972 11694 11266 1135 1353 -254 N ATOM 395 CZ ARG A 102 26.438 -8.870 16.843 1.00 87.08 C ANISOU 395 CZ ARG A 102 8727 12418 11941 1089 1164 -172 C ATOM 396 NH1 ARG A 102 27.170 -8.660 17.931 1.00 90.27 N ANISOU 396 NH1 ARG A 102 8947 12861 12491 1131 1015 -172 N ATOM 397 NH2 ARG A 102 25.190 -8.424 16.796 1.00 90.08 N ANISOU 397 NH2 ARG A 102 9328 12761 12136 1004 1121 -96 N ATOM 398 N ARG A 103 29.686 -14.425 17.187 1.00 71.00 N ANISOU 398 N ARG A 103 6166 10215 10596 1911 1097 -502 N ATOM 399 CA ARG A 103 31.062 -14.898 17.256 1.00 68.54 C ANISOU 399 CA ARG A 103 5562 9924 10557 2050 1110 -616 C ATOM 400 C ARG A 103 31.143 -16.378 16.905 1.00 75.20 C ANISOU 400 C ARG A 103 6458 10669 11446 2239 1133 -680 C ATOM 401 O ARG A 103 31.971 -16.789 16.084 1.00 81.64 O ANISOU 401 O ARG A 103 7117 11497 12405 2309 1324 -804 O ATOM 402 CB ARG A 103 31.638 -14.635 18.651 1.00 70.24 C ANISOU 402 CB ARG A 103 5610 10154 10923 2106 834 -587 C ATOM 403 CG ARG A 103 31.960 -13.175 18.913 1.00 72.84 C ANISOU 403 CG ARG A 103 5805 10589 11282 1935 835 -564 C ATOM 404 CD ARG A 103 32.481 -12.950 20.318 1.00 87.96 C ANISOU 404 CD ARG A 103 7587 12505 13329 1992 539 -534 C ATOM 405 NE ARG A 103 32.630 -11.523 20.598 1.00101.58 N ANISOU 405 NE ARG A 103 9228 14318 15048 1814 529 -501 N ATOM 406 CZ ARG A 103 33.101 -11.026 21.737 1.00109.33 C ANISOU 406 CZ ARG A 103 10094 15315 16131 1816 290 -477 C ATOM 407 NH1 ARG A 103 33.472 -11.843 22.714 1.00114.82 N ANISOU 407 NH1 ARG A 103 10750 15940 16934 1989 33 -478 N ATOM 408 NH2 ARG A 103 33.206 -9.713 21.898 1.00107.11 N ANISOU 408 NH2 ARG A 103 9753 15109 15835 1645 299 -451 N ATOM 409 N ALA A 104 30.286 -17.197 17.519 1.00 78.34 N ANISOU 409 N ALA A 104 7080 10962 11724 2320 949 -601 N ATOM 410 CA ALA A 104 30.322 -18.633 17.261 1.00 75.94 C ANISOU 410 CA ALA A 104 6851 10547 11457 2501 946 -654 C ATOM 411 C ALA A 104 29.865 -18.965 15.849 1.00 77.70 C ANISOU 411 C ALA A 104 7226 10748 11549 2456 1211 -704 C ATOM 412 O ALA A 104 30.270 -19.993 15.297 1.00 81.49 O ANISOU 412 O ALA A 104 7690 11162 12110 2598 1299 -798 O ATOM 413 CB ALA A 104 29.451 -19.372 18.277 1.00 72.24 C ANISOU 413 CB ALA A 104 6613 9964 10872 2570 690 -547 C ATOM 414 N PHE A 105 29.023 -18.115 15.258 1.00 74.38 N ANISOU 414 N PHE A 105 6965 10370 10926 2265 1330 -646 N ATOM 415 CA PHE A 105 28.435 -18.359 13.946 1.00 74.37 C ANISOU 415 CA PHE A 105 7162 10334 10762 2204 1548 -678 C ATOM 416 C PHE A 105 28.560 -17.118 13.074 1.00 79.50 C ANISOU 416 C PHE A 105 7779 11082 11344 2015 1763 -695 C ATOM 417 O PHE A 105 29.513 -16.348 13.215 1.00 94.90 O ANISOU 417 O PHE A 105 9483 13128 13446 1974 1820 -738 O ATOM 418 CB PHE A 105 26.962 -18.749 14.087 1.00 68.85 C ANISOU 418 CB PHE A 105 6778 9544 9839 2163 1430 -573 C ATOM 419 CG PHE A 105 26.712 -19.802 15.126 1.00 66.08 C ANISOU 419 CG PHE A 105 6490 9092 9525 2309 1198 -528 C ATOM 420 CD1 PHE A 105 27.203 -21.092 14.963 1.00 66.82 C ANISOU 420 CD1 PHE A 105 6573 9095 9722 2494 1200 -606 C ATOM 421 CD2 PHE A 105 25.985 -19.508 16.263 1.00 66.17 C ANISOU 421 CD2 PHE A 105 6588 9090 9462 2261 985 -411 C ATOM 422 CE1 PHE A 105 26.974 -22.066 15.917 1.00 64.32 C ANISOU 422 CE1 PHE A 105 6341 8669 9427 2624 979 -560 C ATOM 423 CE2 PHE A 105 25.749 -20.483 17.220 1.00 68.70 C ANISOU 423 CE2 PHE A 105 6999 9307 9798 2382 781 -366 C ATOM 424 CZ PHE A 105 26.247 -21.765 17.043 1.00 63.46 C ANISOU 424 CZ PHE A 105 6334 8546 9231 2562 773 -436 C ATOM 425 N SER A 106 27.619 -16.920 12.162 1.00 76.95 N ANISOU 425 N SER A 106 7709 10730 10800 1897 1875 -664 N ATOM 426 CA SER A 106 27.479 -15.648 11.470 1.00 82.48 C ANISOU 426 CA SER A 106 8449 11502 11388 1699 2023 -646 C ATOM 427 C SER A 106 26.417 -14.824 12.184 1.00 87.31 C ANISOU 427 C SER A 106 9186 12122 11866 1582 1834 -513 C ATOM 428 O SER A 106 25.676 -15.341 13.023 1.00 88.50 O ANISOU 428 O SER A 106 9430 12215 11982 1645 1629 -442 O ATOM 429 CB SER A 106 27.110 -15.865 9.998 1.00 79.32 C ANISOU 429 CB SER A 106 8269 11051 10817 1637 2249 -696 C ATOM 430 N ASP A 107 26.360 -13.526 11.870 1.00 89.15 N ANISOU 430 N ASP A 107 9422 12423 12028 1410 1909 -483 N ATOM 431 CA ASP A 107 25.265 -12.712 12.388 1.00 89.53 C ANISOU 431 CA ASP A 107 9611 12468 11938 1298 1751 -367 C ATOM 432 C ASP A 107 23.943 -13.309 11.932 1.00 79.83 C ANISOU 432 C ASP A 107 8668 11139 10524 1295 1705 -325 C ATOM 433 O ASP A 107 23.826 -13.793 10.804 1.00 80.37 O ANISOU 433 O ASP A 107 8875 11157 10505 1295 1853 -378 O ATOM 434 CB ASP A 107 25.360 -11.260 11.922 1.00 94.67 C ANISOU 434 CB ASP A 107 10261 13187 12524 1113 1852 -348 C ATOM 435 CG ASP A 107 24.372 -10.352 12.663 1.00101.29 C ANISOU 435 CG ASP A 107 11194 14027 13264 1017 1668 -238 C ATOM 436 OD1 ASP A 107 24.794 -9.644 13.605 1.00102.75 O ANISOU 436 OD1 ASP A 107 11219 14275 13546 992 1567 -210 O ATOM 437 OD2 ASP A 107 23.165 -10.373 12.330 1.00100.46 O ANISOU 437 OD2 ASP A 107 11320 13856 12994 973 1616 -187 O ATOM 438 N LEU A 108 22.943 -13.294 12.815 1.00 72.02 N ANISOU 438 N LEU A 108 7769 10117 9479 1291 1503 -235 N ATOM 439 CA LEU A 108 21.753 -14.072 12.495 1.00 78.52 C ANISOU 439 CA LEU A 108 8825 10838 10171 1309 1447 -207 C ATOM 440 C LEU A 108 20.792 -13.353 11.557 1.00 82.45 C ANISOU 440 C LEU A 108 9527 11308 10491 1166 1492 -179 C ATOM 441 O LEU A 108 19.787 -13.951 11.167 1.00 88.59 O ANISOU 441 O LEU A 108 10498 11998 11166 1169 1445 -164 O ATOM 442 CB LEU A 108 21.018 -14.526 13.764 1.00 70.05 C ANISOU 442 CB LEU A 108 7780 9724 9113 1365 1234 -134 C ATOM 443 CG LEU A 108 20.536 -13.627 14.892 1.00 62.14 C ANISOU 443 CG LEU A 108 6742 8761 8107 1295 1084 -51 C ATOM 444 CD1 LEU A 108 19.554 -14.436 15.714 1.00 49.66 C ANISOU 444 CD1 LEU A 108 5280 7099 6491 1344 934 4 C ATOM 445 CD2 LEU A 108 21.704 -13.165 15.754 1.00 67.87 C ANISOU 445 CD2 LEU A 108 7238 9570 8978 1331 1045 -60 C ATOM 446 N THR A 109 21.074 -12.114 11.156 1.00 79.60 N ANISOU 446 N THR A 109 9139 11011 10096 1040 1573 -173 N ATOM 447 CA THR A 109 20.367 -11.563 10.007 1.00 79.41 C ANISOU 447 CA THR A 109 9332 10942 9898 919 1639 -165 C ATOM 448 C THR A 109 20.901 -12.104 8.688 1.00 87.50 C ANISOU 448 C THR A 109 10451 11931 10864 929 1846 -250 C ATOM 449 O THR A 109 20.178 -12.079 7.686 1.00 99.35 O ANISOU 449 O THR A 109 12190 13357 12201 863 1875 -250 O ATOM 450 CB THR A 109 20.452 -10.035 9.984 1.00 69.95 C ANISOU 450 CB THR A 109 8109 9803 8664 774 1652 -126 C ATOM 451 OG1 THR A 109 21.828 -9.629 10.031 1.00 78.15 O ANISOU 451 OG1 THR A 109 8942 10931 9821 763 1791 -174 O ATOM 452 CG2 THR A 109 19.683 -9.431 11.154 1.00 46.13 C ANISOU 452 CG2 THR A 109 5056 6802 5669 752 1448 -43 C ATOM 453 N SER A 110 22.142 -12.600 8.671 1.00 86.65 N ANISOU 453 N SER A 110 10167 11869 10889 1013 1986 -329 N ATOM 454 CA SER A 110 22.777 -12.989 7.414 1.00 95.47 C ANISOU 454 CA SER A 110 11357 12961 11957 1012 2224 -424 C ATOM 455 C SER A 110 22.162 -14.247 6.814 1.00108.27 C ANISOU 455 C SER A 110 13180 14469 13488 1099 2218 -457 C ATOM 456 O SER A 110 22.178 -14.412 5.589 1.00113.04 O ANISOU 456 O SER A 110 13969 15018 13961 1056 2379 -513 O ATOM 457 CB SER A 110 24.274 -13.203 7.626 1.00 95.20 C ANISOU 457 CB SER A 110 11043 13005 12124 1091 2375 -513 C ATOM 458 OG SER A 110 24.526 -14.410 8.332 1.00 90.26 O ANISOU 458 OG SER A 110 10300 12354 11641 1273 2283 -543 O ATOM 459 N GLN A 111 21.621 -15.140 7.644 1.00114.68 N ANISOU 459 N GLN A 111 13979 15235 14358 1212 2038 -425 N ATOM 460 CA GLN A 111 21.163 -16.442 7.170 1.00119.64 C ANISOU 460 CA GLN A 111 14775 15751 14930 1306 2030 -464 C ATOM 461 C GLN A 111 19.719 -16.443 6.675 1.00112.09 C ANISOU 461 C GLN A 111 14096 14701 13793 1224 1913 -410 C ATOM 462 O GLN A 111 19.320 -17.384 5.974 1.00116.42 O ANISOU 462 O GLN A 111 14829 15147 14259 1266 1932 -451 O ATOM 463 CB GLN A 111 21.328 -17.493 8.283 1.00119.77 C ANISOU 463 CB GLN A 111 14658 15749 15101 1468 1897 -460 C ATOM 464 CG GLN A 111 21.168 -16.968 9.719 1.00113.17 C ANISOU 464 CG GLN A 111 13664 14975 14362 1464 1708 -372 C ATOM 465 CD GLN A 111 22.315 -17.402 10.640 1.00115.44 C ANISOU 465 CD GLN A 111 13699 15309 14855 1603 1685 -406 C ATOM 466 OE1 GLN A 111 22.100 -18.059 11.658 1.00109.98 O ANISOU 466 OE1 GLN A 111 12979 14579 14229 1695 1518 -366 O ATOM 467 NE2 GLN A 111 23.539 -17.026 10.281 1.00122.31 N ANISOU 467 NE2 GLN A 111 14387 16255 15829 1613 1850 -483 N ATOM 468 N LEU A 112 18.948 -15.405 6.982 1.00 96.10 N ANISOU 468 N LEU A 112 12102 12700 11710 1108 1791 -327 N ATOM 469 CA LEU A 112 17.501 -15.447 6.820 1.00 90.19 C ANISOU 469 CA LEU A 112 11557 11865 10848 1050 1628 -272 C ATOM 470 C LEU A 112 17.082 -15.252 5.370 1.00 92.99 C ANISOU 470 C LEU A 112 12177 12141 11014 960 1700 -302 C ATOM 471 O LEU A 112 17.602 -14.380 4.667 1.00102.40 O ANISOU 471 O LEU A 112 13408 13368 12131 871 1834 -319 O ATOM 472 CB LEU A 112 16.866 -14.371 7.692 1.00 88.09 C ANISOU 472 CB LEU A 112 11214 11651 10607 969 1477 -183 C ATOM 473 CG LEU A 112 17.571 -14.255 9.044 1.00 78.75 C ANISOU 473 CG LEU A 112 9771 10561 9588 1034 1440 -159 C ATOM 474 CD1 LEU A 112 17.039 -13.073 9.820 1.00 76.29 C ANISOU 474 CD1 LEU A 112 9398 10302 9287 946 1318 -82 C ATOM 475 CD2 LEU A 112 17.406 -15.539 9.844 1.00 73.33 C ANISOU 475 CD2 LEU A 112 9048 9826 8987 1162 1348 -158 C ATOM 476 N HIS A 113 16.122 -16.072 4.922 1.00 82.14 N ANISOU 476 N HIS A 113 11001 10650 9559 976 1604 -308 N ATOM 477 CA HIS A 113 15.565 -15.975 3.568 1.00 71.45 C ANISOU 477 CA HIS A 113 9936 9198 8013 894 1624 -334 C ATOM 478 C HIS A 113 14.047 -15.837 3.685 1.00 60.66 C ANISOU 478 C HIS A 113 8689 7753 6604 836 1385 -273 C ATOM 479 O HIS A 113 13.316 -16.796 3.455 1.00 70.48 O ANISOU 479 O HIS A 113 10062 8896 7823 871 1293 -290 O ATOM 480 CB HIS A 113 15.956 -17.174 2.734 1.00 67.37 C ANISOU 480 CB HIS A 113 9558 8599 7439 972 1751 -423 C ATOM 481 N ILE A 114 13.576 -14.639 4.021 1.00 49.07 N ANISOU 481 N ILE A 114 7178 6329 5137 747 1285 -208 N ATOM 482 CA ILE A 114 12.158 -14.405 4.272 1.00 59.19 C ANISOU 482 CA ILE A 114 8519 7549 6421 698 1058 -157 C ATOM 483 C ILE A 114 11.524 -13.663 3.107 1.00 51.41 C ANISOU 483 C ILE A 114 7782 6480 5271 592 991 -154 C ATOM 484 O ILE A 114 12.167 -12.882 2.391 1.00 50.05 O ANISOU 484 O ILE A 114 7701 6327 4990 527 1110 -163 O ATOM 485 CB ILE A 114 11.901 -13.617 5.576 1.00 68.92 C ANISOU 485 CB ILE A 114 9530 8870 7786 685 960 -90 C ATOM 486 CG1 ILE A 114 12.595 -12.256 5.517 1.00 63.86 C ANISOU 486 CG1 ILE A 114 8831 8315 7117 612 1041 -67 C ATOM 487 CG2 ILE A 114 12.305 -14.443 6.792 1.00 69.03 C ANISOU 487 CG2 ILE A 114 9341 8938 7949 788 976 -85 C ATOM 488 CD1 ILE A 114 13.198 -11.827 6.817 1.00 60.09 C ANISOU 488 CD1 ILE A 114 8092 7957 6782 643 1059 -33 C ATOM 489 N THR A 115 10.231 -13.929 2.922 1.00 47.38 N ANISOU 489 N THR A 115 7388 5867 4748 571 792 -144 N ATOM 490 CA THR A 115 9.353 -13.195 2.025 1.00 45.99 C ANISOU 490 CA THR A 115 7428 5596 4451 478 646 -132 C ATOM 491 C THR A 115 8.070 -12.966 2.803 1.00 46.51 C ANISOU 491 C THR A 115 7383 5641 4647 467 419 -92 C ATOM 492 O THR A 115 7.879 -13.578 3.862 1.00 46.36 O ANISOU 492 O THR A 115 7173 5665 4777 525 402 -82 O ATOM 493 CB THR A 115 9.057 -13.974 0.744 1.00 46.78 C ANISOU 493 CB THR A 115 7823 5558 4395 469 627 -186 C ATOM 494 OG1 THR A 115 8.351 -15.174 1.085 1.00 46.70 O ANISOU 494 OG1 THR A 115 7783 5486 4475 529 524 -207 O ATOM 495 CG2 THR A 115 10.329 -14.308 -0.003 1.00 41.60 C ANISOU 495 CG2 THR A 115 7272 4918 3616 486 883 -240 C ATOM 496 N PRO A 116 7.164 -12.114 2.331 1.00 46.59 N ANISOU 496 N PRO A 116 7510 5581 4613 396 243 -73 N ATOM 497 CA PRO A 116 5.882 -11.992 3.044 1.00 41.88 C ANISOU 497 CA PRO A 116 6790 4956 4166 392 34 -53 C ATOM 498 C PRO A 116 5.114 -13.295 3.061 1.00 43.62 C ANISOU 498 C PRO A 116 7030 5095 4450 427 -53 -88 C ATOM 499 O PRO A 116 4.460 -13.610 4.062 1.00 48.52 O ANISOU 499 O PRO A 116 7465 5736 5235 447 -118 -78 O ATOM 500 CB PRO A 116 5.143 -10.896 2.259 1.00 41.63 C ANISOU 500 CB PRO A 116 6924 4839 4056 318 -144 -41 C ATOM 501 CG PRO A 116 6.247 -10.101 1.560 1.00 38.82 C ANISOU 501 CG PRO A 116 6708 4514 3527 273 9 -27 C ATOM 502 CD PRO A 116 7.295 -11.135 1.234 1.00 40.86 C ANISOU 502 CD PRO A 116 7015 4800 3711 315 229 -67 C ATOM 503 N GLY A 117 5.205 -14.086 1.991 1.00 44.36 N ANISOU 503 N GLY A 117 7353 5090 4413 430 -41 -133 N ATOM 504 CA GLY A 117 4.455 -15.327 1.929 1.00 41.21 C ANISOU 504 CA GLY A 117 6995 4596 4067 453 -136 -169 C ATOM 505 C GLY A 117 4.988 -16.445 2.800 1.00 42.49 C ANISOU 505 C GLY A 117 7007 4813 4323 530 2 -176 C ATOM 506 O GLY A 117 4.228 -17.340 3.183 1.00 42.62 O ANISOU 506 O GLY A 117 6982 4770 4440 540 -86 -189 O ATOM 507 N THR A 118 6.287 -16.432 3.110 1.00 41.51 N ANISOU 507 N THR A 118 6806 4793 4174 582 212 -170 N ATOM 508 CA THR A 118 6.902 -17.482 3.911 1.00 45.07 C ANISOU 508 CA THR A 118 7128 5287 4710 669 331 -177 C ATOM 509 C THR A 118 7.306 -17.031 5.312 1.00 43.54 C ANISOU 509 C THR A 118 6667 5223 4652 698 385 -126 C ATOM 510 O THR A 118 7.729 -17.870 6.114 1.00 41.30 O ANISOU 510 O THR A 118 6276 4966 4448 771 451 -124 O ATOM 511 CB THR A 118 8.146 -18.032 3.194 1.00 44.56 C ANISOU 511 CB THR A 118 7174 5224 4532 729 526 -227 C ATOM 512 OG1 THR A 118 9.112 -16.983 3.057 1.00 48.15 O ANISOU 512 OG1 THR A 118 7580 5780 4934 711 662 -215 O ATOM 513 CG2 THR A 118 7.789 -18.545 1.822 1.00 42.82 C ANISOU 513 CG2 THR A 118 7247 4866 4158 702 485 -283 C ATOM 514 N ALA A 119 7.207 -15.739 5.617 1.00 35.37 N ANISOU 514 N ALA A 119 5542 4260 3636 646 352 -87 N ATOM 515 CA ALA A 119 7.701 -15.219 6.890 1.00 34.28 C ANISOU 515 CA ALA A 119 5175 4245 3606 669 409 -42 C ATOM 516 C ALA A 119 7.061 -15.935 8.072 1.00 49.64 C ANISOU 516 C ALA A 119 6991 6183 5686 696 347 -22 C ATOM 517 O ALA A 119 7.750 -16.337 9.016 1.00 51.60 O ANISOU 517 O ALA A 119 7113 6494 5997 758 428 -4 O ATOM 518 CB ALA A 119 7.446 -13.708 6.972 1.00 33.69 C ANISOU 518 CB ALA A 119 5052 4220 3528 598 349 -7 C ATOM 519 N TYR A 120 5.737 -16.113 8.030 1.00 50.65 N ANISOU 519 N TYR A 120 7155 6227 5864 645 202 -27 N ATOM 520 CA TYR A 120 5.036 -16.674 9.183 1.00 49.19 C ANISOU 520 CA TYR A 120 6848 6033 5809 646 160 -7 C ATOM 521 C TYR A 120 5.459 -18.114 9.436 1.00 52.36 C ANISOU 521 C TYR A 120 7286 6392 6217 713 227 -19 C ATOM 522 O TYR A 120 5.776 -18.492 10.574 1.00 46.18 O ANISOU 522 O TYR A 120 6395 5652 5501 752 277 12 O ATOM 523 CB TYR A 120 3.523 -16.597 8.987 1.00 38.41 C ANISOU 523 CB TYR A 120 5501 4580 4515 570 -1 -24 C ATOM 524 CG TYR A 120 2.799 -17.168 10.164 1.00 46.02 C ANISOU 524 CG TYR A 120 6341 5532 5613 554 -13 -10 C ATOM 525 CD1 TYR A 120 2.729 -16.465 11.367 1.00 47.02 C ANISOU 525 CD1 TYR A 120 6301 5744 5821 541 19 26 C ATOM 526 CD2 TYR A 120 2.208 -18.430 10.099 1.00 54.54 C ANISOU 526 CD2 TYR A 120 7485 6508 6729 543 -47 -34 C ATOM 527 CE1 TYR A 120 2.073 -17.001 12.472 1.00 55.21 C ANISOU 527 CE1 TYR A 120 7248 6765 6965 515 31 38 C ATOM 528 CE2 TYR A 120 1.543 -18.969 11.196 1.00 53.38 C ANISOU 528 CE2 TYR A 120 7239 6343 6698 512 -39 -19 C ATOM 529 CZ TYR A 120 1.483 -18.249 12.381 1.00 56.91 C ANISOU 529 CZ TYR A 120 7530 6878 7216 496 7 17 C ATOM 530 OH TYR A 120 0.830 -18.774 13.476 1.00 61.55 O ANISOU 530 OH TYR A 120 8043 7442 7903 454 36 30 O ATOM 531 N GLN A 121 5.471 -18.931 8.381 1.00 49.83 N ANISOU 531 N GLN A 121 7138 5977 5818 729 220 -65 N ATOM 532 CA GLN A 121 5.830 -20.334 8.539 1.00 54.80 C ANISOU 532 CA GLN A 121 7823 6546 6452 798 273 -83 C ATOM 533 C GLN A 121 7.260 -20.475 9.037 1.00 50.71 C ANISOU 533 C GLN A 121 7225 6115 5929 899 415 -73 C ATOM 534 O GLN A 121 7.546 -21.327 9.886 1.00 47.85 O ANISOU 534 O GLN A 121 6816 5740 5624 960 441 -57 O ATOM 535 CB GLN A 121 5.634 -21.075 7.215 1.00 66.15 C ANISOU 535 CB GLN A 121 9478 7864 7793 797 242 -142 C ATOM 536 CG GLN A 121 5.152 -22.513 7.376 1.00 89.35 C ANISOU 536 CG GLN A 121 12493 10685 10772 814 203 -161 C ATOM 537 CD GLN A 121 3.966 -22.635 8.335 1.00101.83 C ANISOU 537 CD GLN A 121 13967 12238 12484 739 103 -128 C ATOM 538 OE1 GLN A 121 2.985 -21.890 8.237 1.00100.66 O ANISOU 538 OE1 GLN A 121 13774 12087 12385 652 -3 -126 O ATOM 539 NE2 GLN A 121 4.060 -23.577 9.273 1.00107.06 N ANISOU 539 NE2 GLN A 121 14595 12875 13209 773 141 -106 N ATOM 540 N SER A 122 8.169 -19.643 8.514 1.00 44.77 N ANISOU 540 N SER A 122 6457 5442 5110 913 503 -83 N ATOM 541 CA SER A 122 9.557 -19.663 8.963 1.00 43.05 C ANISOU 541 CA SER A 122 6131 5313 4913 1004 633 -83 C ATOM 542 C SER A 122 9.659 -19.269 10.423 1.00 48.62 C ANISOU 542 C SER A 122 6651 6102 5721 1013 610 -24 C ATOM 543 O SER A 122 10.425 -19.863 11.192 1.00 48.96 O ANISOU 543 O SER A 122 6617 6167 5820 1101 652 -16 O ATOM 544 CB SER A 122 10.394 -18.712 8.117 1.00 39.05 C ANISOU 544 CB SER A 122 5635 4876 4326 988 736 -107 C ATOM 545 OG SER A 122 10.462 -19.166 6.782 1.00 52.72 O ANISOU 545 OG SER A 122 7564 6526 5944 988 784 -168 O ATOM 546 N PHE A 123 8.895 -18.258 10.824 1.00 41.35 N ANISOU 546 N PHE A 123 5666 5221 4825 926 536 15 N ATOM 547 CA PHE A 123 8.951 -17.823 12.203 1.00 37.99 C ANISOU 547 CA PHE A 123 5087 4868 4480 926 519 67 C ATOM 548 C PHE A 123 8.434 -18.922 13.136 1.00 49.81 C ANISOU 548 C PHE A 123 6594 6297 6036 949 477 88 C ATOM 549 O PHE A 123 9.068 -19.249 14.146 1.00 52.56 O ANISOU 549 O PHE A 123 6872 6675 6423 1010 499 117 O ATOM 550 CB PHE A 123 8.156 -16.530 12.355 1.00 37.47 C ANISOU 550 CB PHE A 123 4966 4843 4427 830 453 92 C ATOM 551 CG PHE A 123 7.968 -16.128 13.773 1.00 38.12 C ANISOU 551 CG PHE A 123 4920 4980 4584 817 431 138 C ATOM 552 CD1 PHE A 123 8.946 -15.398 14.429 1.00 38.47 C ANISOU 552 CD1 PHE A 123 4851 5128 4639 845 477 163 C ATOM 553 CD2 PHE A 123 6.849 -16.534 14.472 1.00 39.00 C ANISOU 553 CD2 PHE A 123 5030 5034 4754 773 373 153 C ATOM 554 CE1 PHE A 123 8.790 -15.050 15.766 1.00 42.00 C ANISOU 554 CE1 PHE A 123 5205 5616 5138 833 453 204 C ATOM 555 CE2 PHE A 123 6.692 -16.193 15.803 1.00 41.22 C ANISOU 555 CE2 PHE A 123 5216 5358 5087 757 372 192 C ATOM 556 CZ PHE A 123 7.664 -15.454 16.453 1.00 29.68 C ANISOU 556 CZ PHE A 123 3663 3996 3619 790 407 219 C ATOM 557 N GLU A 124 7.297 -19.530 12.791 1.00 46.99 N ANISOU 557 N GLU A 124 6335 5837 5684 895 411 73 N ATOM 558 CA GLU A 124 6.706 -20.544 13.658 1.00 46.11 C ANISOU 558 CA GLU A 124 6244 5648 5626 891 380 95 C ATOM 559 C GLU A 124 7.548 -21.811 13.700 1.00 54.54 C ANISOU 559 C GLU A 124 7386 6659 6676 998 422 84 C ATOM 560 O GLU A 124 7.653 -22.462 14.749 1.00 50.85 O ANISOU 560 O GLU A 124 6912 6164 6244 1029 418 119 O ATOM 561 CB GLU A 124 5.290 -20.875 13.199 1.00 36.31 C ANISOU 561 CB GLU A 124 5077 4306 4411 797 299 72 C ATOM 562 CG GLU A 124 4.319 -19.729 13.331 1.00 49.82 C ANISOU 562 CG GLU A 124 6698 6056 6175 701 241 78 C ATOM 563 CD GLU A 124 3.947 -19.453 14.777 1.00 56.49 C ANISOU 563 CD GLU A 124 7428 6941 7093 664 260 121 C ATOM 564 OE1 GLU A 124 3.876 -18.266 15.173 1.00 56.61 O ANISOU 564 OE1 GLU A 124 7337 7040 7130 635 259 136 O ATOM 565 OE2 GLU A 124 3.719 -20.430 15.516 1.00 59.50 O ANISOU 565 OE2 GLU A 124 7844 7261 7502 660 280 139 O ATOM 566 N GLN A 125 8.142 -22.199 12.576 1.00 47.94 N ANISOU 566 N GLN A 125 6636 5795 5783 1056 463 32 N ATOM 567 CA GLN A 125 8.929 -23.418 12.614 1.00 48.83 C ANISOU 567 CA GLN A 125 6814 5845 5895 1170 501 11 C ATOM 568 C GLN A 125 10.129 -23.247 13.527 1.00 48.78 C ANISOU 568 C GLN A 125 6681 5923 5931 1266 544 37 C ATOM 569 O GLN A 125 10.395 -24.101 14.379 1.00 48.75 O ANISOU 569 O GLN A 125 6693 5867 5963 1333 518 61 O ATOM 570 CB GLN A 125 9.365 -23.823 11.213 1.00 54.61 C ANISOU 570 CB GLN A 125 7664 6529 6555 1216 555 -62 C ATOM 571 CG GLN A 125 8.244 -24.414 10.404 1.00 77.35 C ANISOU 571 CG GLN A 125 10709 9285 9396 1143 486 -91 C ATOM 572 CD GLN A 125 8.713 -24.906 9.059 1.00 89.88 C ANISOU 572 CD GLN A 125 12446 10810 10893 1194 543 -167 C ATOM 573 OE1 GLN A 125 9.911 -25.104 8.843 1.00 92.22 O ANISOU 573 OE1 GLN A 125 12724 11141 11176 1301 651 -202 O ATOM 574 NE2 GLN A 125 7.771 -25.102 8.139 1.00 92.52 N ANISOU 574 NE2 GLN A 125 12933 11051 11171 1116 470 -198 N ATOM 575 N VAL A 126 10.851 -22.135 13.380 1.00 42.67 N ANISOU 575 N VAL A 126 5788 5270 5156 1270 596 33 N ATOM 576 CA VAL A 126 12.032 -21.916 14.208 1.00 45.56 C ANISOU 576 CA VAL A 126 6016 5717 5577 1359 622 50 C ATOM 577 C VAL A 126 11.643 -21.871 15.679 1.00 48.61 C ANISOU 577 C VAL A 126 6360 6107 6003 1334 542 121 C ATOM 578 O VAL A 126 12.249 -22.553 16.519 1.00 48.80 O ANISOU 578 O VAL A 126 6376 6102 6065 1425 511 140 O ATOM 579 CB VAL A 126 12.771 -20.642 13.771 1.00 41.08 C ANISOU 579 CB VAL A 126 5328 5277 5004 1339 693 33 C ATOM 580 CG1 VAL A 126 13.819 -20.270 14.791 1.00 38.52 C ANISOU 580 CG1 VAL A 126 4841 5039 4755 1405 689 57 C ATOM 581 CG2 VAL A 126 13.416 -20.875 12.413 1.00 36.51 C ANISOU 581 CG2 VAL A 126 4805 4686 4382 1381 801 -44 C ATOM 582 N VAL A 127 10.580 -21.125 16.001 1.00 36.88 N ANISOU 582 N VAL A 127 4865 4642 4506 1213 505 156 N ATOM 583 CA VAL A 127 10.198 -20.943 17.402 1.00 39.20 C ANISOU 583 CA VAL A 127 5124 4945 4825 1176 455 218 C ATOM 584 C VAL A 127 9.675 -22.244 18.010 1.00 48.43 C ANISOU 584 C VAL A 127 6419 5987 5995 1186 418 242 C ATOM 585 O VAL A 127 10.030 -22.595 19.142 1.00 49.87 O ANISOU 585 O VAL A 127 6613 6151 6185 1227 385 286 O ATOM 586 CB VAL A 127 9.174 -19.805 17.532 1.00 39.41 C ANISOU 586 CB VAL A 127 5101 5020 4851 1048 442 235 C ATOM 587 CG1 VAL A 127 8.638 -19.736 18.968 1.00 31.81 C ANISOU 587 CG1 VAL A 127 4132 4049 3906 999 414 289 C ATOM 588 CG2 VAL A 127 9.825 -18.480 17.126 1.00 37.41 C ANISOU 588 CG2 VAL A 127 4736 4887 4593 1042 471 224 C ATOM 589 N ASN A 128 8.817 -22.969 17.281 1.00 39.69 N ANISOU 589 N ASN A 128 5423 4782 4876 1141 415 215 N ATOM 590 CA ASN A 128 8.360 -24.269 17.762 1.00 38.65 C ANISOU 590 CA ASN A 128 5425 4516 4744 1143 386 233 C ATOM 591 C ASN A 128 9.533 -25.188 18.089 1.00 47.46 C ANISOU 591 C ASN A 128 6587 5587 5861 1291 372 236 C ATOM 592 O ASN A 128 9.540 -25.848 19.136 1.00 56.78 O ANISOU 592 O ASN A 128 7840 6697 7038 1309 332 284 O ATOM 593 CB ASN A 128 7.423 -24.926 16.741 1.00 43.12 C ANISOU 593 CB ASN A 128 6100 4981 5303 1082 377 191 C ATOM 594 CG ASN A 128 6.034 -24.276 16.724 1.00 52.85 C ANISOU 594 CG ASN A 128 7296 6220 6566 930 359 193 C ATOM 595 OD1 ASN A 128 5.628 -23.646 17.707 1.00 50.40 O ANISOU 595 OD1 ASN A 128 6911 5959 6282 866 366 233 O ATOM 596 ND2 ASN A 128 5.308 -24.416 15.607 1.00 50.01 N ANISOU 596 ND2 ASN A 128 6988 5805 6207 876 331 144 N ATOM 597 N GLU A 129 10.550 -25.227 17.235 1.00 44.29 N ANISOU 597 N GLU A 129 6144 5219 5464 1399 406 183 N ATOM 598 CA GLU A 129 11.667 -26.112 17.539 1.00 45.57 C ANISOU 598 CA GLU A 129 6329 5332 5654 1554 386 173 C ATOM 599 C GLU A 129 12.485 -25.580 18.708 1.00 46.22 C ANISOU 599 C GLU A 129 6301 5490 5771 1608 341 218 C ATOM 600 O GLU A 129 13.030 -26.369 19.489 1.00 47.82 O ANISOU 600 O GLU A 129 6558 5620 5992 1705 273 243 O ATOM 601 CB GLU A 129 12.546 -26.318 16.303 1.00 38.35 C ANISOU 601 CB GLU A 129 5389 4431 4751 1657 455 89 C ATOM 602 N LEU A 130 12.568 -24.253 18.854 1.00 44.23 N ANISOU 602 N LEU A 130 5909 5373 5524 1546 364 231 N ATOM 603 CA LEU A 130 13.354 -23.677 19.940 1.00 43.37 C ANISOU 603 CA LEU A 130 5697 5336 5446 1590 311 269 C ATOM 604 C LEU A 130 12.817 -24.121 21.296 1.00 45.88 C ANISOU 604 C LEU A 130 6132 5573 5728 1554 231 344 C ATOM 605 O LEU A 130 13.586 -24.465 22.201 1.00 50.71 O ANISOU 605 O LEU A 130 6756 6156 6355 1646 148 373 O ATOM 606 CB LEU A 130 13.355 -22.158 19.824 1.00 42.99 C ANISOU 606 CB LEU A 130 5502 5431 5399 1507 351 270 C ATOM 607 CG LEU A 130 14.015 -21.378 20.967 1.00 48.63 C ANISOU 607 CG LEU A 130 6115 6225 6138 1522 290 311 C ATOM 608 CD1 LEU A 130 15.494 -21.690 21.034 1.00 48.23 C ANISOU 608 CD1 LEU A 130 5965 6194 6166 1674 254 279 C ATOM 609 CD2 LEU A 130 13.798 -19.885 20.777 1.00 39.48 C ANISOU 609 CD2 LEU A 130 4841 5190 4971 1419 333 311 C ATOM 610 N PHE A 131 11.500 -24.185 21.430 1.00 42.22 N ANISOU 610 N PHE A 131 5765 5059 5217 1422 255 371 N ATOM 611 CA PHE A 131 10.860 -24.511 22.693 1.00 46.36 C ANISOU 611 CA PHE A 131 6410 5508 5695 1355 216 438 C ATOM 612 C PHE A 131 10.277 -25.913 22.723 1.00 50.41 C ANISOU 612 C PHE A 131 7114 5857 6183 1347 204 451 C ATOM 613 O PHE A 131 9.581 -26.251 23.682 1.00 51.40 O ANISOU 613 O PHE A 131 7364 5904 6261 1264 196 505 O ATOM 614 CB PHE A 131 9.761 -23.492 22.991 1.00 40.35 C ANISOU 614 CB PHE A 131 5604 4810 4916 1197 268 456 C ATOM 615 CG PHE A 131 10.274 -22.094 23.162 1.00 43.60 C ANISOU 615 CG PHE A 131 5855 5367 5342 1193 270 454 C ATOM 616 CD1 PHE A 131 10.951 -21.726 24.328 1.00 41.12 C ANISOU 616 CD1 PHE A 131 5532 5085 5007 1230 210 497 C ATOM 617 CD2 PHE A 131 10.084 -21.147 22.171 1.00 41.47 C ANISOU 617 CD2 PHE A 131 5463 5192 5101 1150 320 410 C ATOM 618 CE1 PHE A 131 11.433 -20.430 24.495 1.00 42.11 C ANISOU 618 CE1 PHE A 131 5513 5337 5148 1220 205 493 C ATOM 619 CE2 PHE A 131 10.561 -19.844 22.327 1.00 44.26 C ANISOU 619 CE2 PHE A 131 5681 5670 5466 1140 321 410 C ATOM 620 CZ PHE A 131 11.239 -19.487 23.484 1.00 45.73 C ANISOU 620 CZ PHE A 131 5845 5891 5640 1173 267 449 C ATOM 621 N AARG A 132 10.544 -26.723 21.690 0.55 49.36 N ANISOU 621 N AARG A 132 7016 5664 6074 1425 210 399 N ATOM 622 N BARG A 132 10.544 -26.748 21.713 0.45 49.93 N ANISOU 622 N BARG A 132 7092 5733 6145 1425 209 400 N ATOM 623 CA AARG A 132 9.975 -28.066 21.584 0.55 53.09 C ANISOU 623 CA AARG A 132 7675 5970 6524 1413 197 403 C ATOM 624 CA BARG A 132 9.879 -28.049 21.661 0.45 53.07 C ANISOU 624 CA BARG A 132 7680 5966 6519 1400 198 408 C ATOM 625 C AARG A 132 10.212 -28.887 22.844 0.55 58.31 C ANISOU 625 C AARG A 132 8495 6515 7146 1452 120 470 C ATOM 626 C BARG A 132 10.189 -28.888 22.894 0.45 57.99 C ANISOU 626 C BARG A 132 8459 6472 7103 1448 119 473 C ATOM 627 O AARG A 132 9.304 -29.566 23.335 0.55 60.27 O ANISOU 627 O AARG A 132 8906 6644 7350 1351 127 510 O ATOM 628 O BARG A 132 9.313 -29.591 23.409 0.45 60.19 O ANISOU 628 O BARG A 132 8904 6629 7337 1351 124 514 O ATOM 629 CB AARG A 132 10.580 -28.767 20.364 0.55 53.99 C ANISOU 629 CB AARG A 132 7802 6043 6669 1532 205 331 C ATOM 630 CB BARG A 132 10.274 -28.811 20.399 0.45 53.95 C ANISOU 630 CB BARG A 132 7819 6023 6656 1496 209 337 C ATOM 631 CG AARG A 132 10.413 -30.272 20.309 0.55 55.78 C ANISOU 631 CG AARG A 132 8228 6085 6879 1575 166 330 C ATOM 632 CG BARG A 132 9.334 -29.964 20.105 0.45 54.39 C ANISOU 632 CG BARG A 132 8059 5919 6689 1430 208 334 C ATOM 633 CD AARG A 132 11.126 -30.860 19.082 0.55 57.72 C ANISOU 633 CD AARG A 132 8475 6300 7156 1708 185 245 C ATOM 634 CD BARG A 132 9.674 -30.690 18.817 0.45 56.60 C ANISOU 634 CD BARG A 132 8386 6138 6982 1520 221 257 C ATOM 635 NE AARG A 132 12.444 -30.257 18.850 0.55 62.79 N ANISOU 635 NE AARG A 132 8946 7060 7851 1847 199 203 N ATOM 636 NE BARG A 132 9.817 -29.786 17.677 0.45 64.28 N ANISOU 636 NE BARG A 132 9225 7234 7967 1514 284 194 N ATOM 637 CZ AARG A 132 12.785 -29.579 17.750 0.55 59.55 C ANISOU 637 CZ AARG A 132 8412 6756 7459 1859 284 135 C ATOM 638 CZ BARG A 132 8.813 -29.156 17.072 0.45 60.18 C ANISOU 638 CZ BARG A 132 8674 6754 7437 1377 314 178 C ATOM 639 NH1AARG A 132 14.005 -29.065 17.632 0.55 53.07 N ANISOU 639 NH1AARG A 132 7430 6037 6698 1974 308 97 N ATOM 640 NH1BARG A 132 9.065 -28.373 16.034 0.45 58.73 N ANISOU 640 NH1BARG A 132 8401 6667 7248 1384 359 125 N ATOM 641 NH2AARG A 132 11.913 -29.425 16.757 0.55 54.99 N ANISOU 641 NH2AARG A 132 7879 6174 6839 1753 341 101 N ATOM 642 NH2BARG A 132 7.565 -29.297 17.503 0.45 56.80 N ANISOU 642 NH2BARG A 132 8307 6267 7009 1230 298 213 N ATOM 643 N ASP A 133 11.424 -28.826 23.388 1.00 54.30 N ANISOU 643 N ASP A 133 7945 6032 6654 1592 40 483 N ATOM 644 CA ASP A 133 11.834 -29.639 24.519 1.00 55.95 C ANISOU 644 CA ASP A 133 8320 6115 6822 1660 -67 543 C ATOM 645 C ASP A 133 11.993 -28.811 25.789 1.00 58.30 C ANISOU 645 C ASP A 133 8603 6474 7073 1619 -114 607 C ATOM 646 O ASP A 133 12.786 -29.176 26.658 1.00 53.59 O ANISOU 646 O ASP A 133 8088 5814 6458 1721 -237 645 O ATOM 647 CB ASP A 133 13.138 -30.376 24.203 1.00 53.09 C ANISOU 647 CB ASP A 133 7945 5701 6526 1874 -158 503 C ATOM 648 CG ASP A 133 14.280 -29.422 23.865 1.00 68.13 C ANISOU 648 CG ASP A 133 9601 7767 8519 1980 -163 452 C ATOM 649 OD1 ASP A 133 13.996 -28.285 23.407 1.00 68.13 O ANISOU 649 OD1 ASP A 133 9445 7915 8528 1888 -72 431 O ATOM 650 OD2 ASP A 133 15.456 -29.800 24.044 1.00 66.86 O ANISOU 650 OD2 ASP A 133 9397 7579 8427 2153 -261 430 O ATOM 651 N GLY A 134 11.273 -27.705 25.903 1.00 61.28 N ANISOU 651 N GLY A 134 8885 6966 7433 1478 -29 614 N ATOM 652 CA GLY A 134 11.217 -26.955 27.146 1.00 59.36 C ANISOU 652 CA GLY A 134 8664 6763 7127 1413 -55 672 C ATOM 653 C GLY A 134 11.526 -25.476 26.959 1.00 55.78 C ANISOU 653 C GLY A 134 7984 6493 6715 1397 -24 644 C ATOM 654 O GLY A 134 11.960 -25.020 25.907 1.00 59.75 O ANISOU 654 O GLY A 134 8311 7094 7295 1449 7 583 O ATOM 655 N VAL A 135 11.276 -24.733 28.042 1.00 46.88 N ANISOU 655 N VAL A 135 6888 5401 5524 1315 -29 690 N ATOM 656 CA VAL A 135 11.487 -23.292 28.122 1.00 48.27 C ANISOU 656 CA VAL A 135 6887 5732 5721 1283 -10 674 C ATOM 657 C VAL A 135 12.574 -23.002 29.150 1.00 51.03 C ANISOU 657 C VAL A 135 7251 6094 6045 1370 -146 709 C ATOM 658 O VAL A 135 12.702 -23.698 30.162 1.00 57.86 O ANISOU 658 O VAL A 135 8314 6840 6829 1392 -233 765 O ATOM 659 CB VAL A 135 10.177 -22.559 28.514 1.00 47.16 C ANISOU 659 CB VAL A 135 6764 5621 5533 1104 106 685 C ATOM 660 CG1 VAL A 135 10.393 -21.069 28.605 1.00 37.30 C ANISOU 660 CG1 VAL A 135 5348 4520 4304 1076 118 668 C ATOM 661 CG2 VAL A 135 9.042 -22.882 27.541 1.00 44.80 C ANISOU 661 CG2 VAL A 135 6448 5298 5278 1014 216 647 C ATOM 662 N ASN A 136 13.366 -21.970 28.885 1.00 45.79 N ANISOU 662 N ASN A 136 6386 5566 5446 1416 -173 677 N ATOM 663 CA ASN A 136 14.097 -21.304 29.952 1.00 46.37 C ANISOU 663 CA ASN A 136 6455 5674 5489 1443 -287 708 C ATOM 664 C ASN A 136 14.339 -19.866 29.522 1.00 46.81 C ANISOU 664 C ASN A 136 6289 5894 5604 1405 -242 668 C ATOM 665 O ASN A 136 14.020 -19.475 28.400 1.00 48.83 O ANISOU 665 O ASN A 136 6410 6225 5918 1370 -133 621 O ATOM 666 CB ASN A 136 15.405 -22.022 30.293 1.00 46.05 C ANISOU 666 CB ASN A 136 6432 5571 5494 1614 -463 714 C ATOM 667 CG ASN A 136 16.373 -22.052 29.139 1.00 53.69 C ANISOU 667 CG ASN A 136 7174 6612 6612 1738 -464 641 C ATOM 668 OD1 ASN A 136 16.768 -21.005 28.608 1.00 51.93 O ANISOU 668 OD1 ASN A 136 6742 6530 6461 1723 -417 598 O ATOM 669 ND2 ASN A 136 16.786 -23.256 28.752 1.00 51.51 N ANISOU 669 ND2 ASN A 136 6950 6236 6384 1861 -510 623 N ATOM 670 N TRP A 137 14.908 -19.076 30.430 1.00 46.03 N ANISOU 670 N TRP A 137 6170 5840 5480 1407 -335 689 N ATOM 671 CA TRP A 137 15.111 -17.666 30.126 1.00 44.97 C ANISOU 671 CA TRP A 137 5845 5849 5391 1357 -297 657 C ATOM 672 C TRP A 137 16.053 -17.480 28.941 1.00 41.64 C ANISOU 672 C TRP A 137 5198 5518 5106 1442 -286 595 C ATOM 673 O TRP A 137 15.820 -16.616 28.090 1.00 37.81 O ANISOU 673 O TRP A 137 4577 5130 4658 1379 -183 559 O ATOM 674 CB TRP A 137 15.641 -16.928 31.358 1.00 38.94 C ANISOU 674 CB TRP A 137 5116 5103 4576 1349 -418 688 C ATOM 675 CG TRP A 137 14.649 -16.830 32.457 1.00 47.74 C ANISOU 675 CG TRP A 137 6447 6150 5544 1238 -387 737 C ATOM 676 CD1 TRP A 137 14.744 -17.398 33.700 1.00 47.92 C ANISOU 676 CD1 TRP A 137 6698 6057 5452 1251 -494 793 C ATOM 677 CD2 TRP A 137 13.394 -16.132 32.430 1.00 45.69 C ANISOU 677 CD2 TRP A 137 6204 5923 5234 1095 -231 729 C ATOM 678 NE1 TRP A 137 13.634 -17.095 34.440 1.00 47.88 N ANISOU 678 NE1 TRP A 137 6855 6015 5321 1115 -390 819 N ATOM 679 CE2 TRP A 137 12.788 -16.320 33.689 1.00 51.24 C ANISOU 679 CE2 TRP A 137 7139 6533 5796 1023 -228 776 C ATOM 680 CE3 TRP A 137 12.724 -15.383 31.467 1.00 41.33 C ANISOU 680 CE3 TRP A 137 5501 5459 4744 1024 -99 684 C ATOM 681 CZ2 TRP A 137 11.547 -15.774 34.012 1.00 42.44 C ANISOU 681 CZ2 TRP A 137 6084 5421 4620 884 -78 769 C ATOM 682 CZ3 TRP A 137 11.487 -14.840 31.787 1.00 43.37 C ANISOU 682 CZ3 TRP A 137 5815 5715 4949 897 21 680 C ATOM 683 CH2 TRP A 137 10.914 -15.038 33.048 1.00 41.74 C ANISOU 683 CH2 TRP A 137 5815 5424 4620 829 40 718 C ATOM 684 N GLY A 138 17.138 -18.263 28.882 1.00 40.98 N ANISOU 684 N GLY A 138 5075 5395 5099 1586 -389 580 N ATOM 685 CA GLY A 138 18.036 -18.173 27.738 1.00 40.45 C ANISOU 685 CA GLY A 138 4795 5407 5169 1666 -349 511 C ATOM 686 C GLY A 138 17.314 -18.341 26.411 1.00 45.29 C ANISOU 686 C GLY A 138 5388 6036 5785 1618 -182 473 C ATOM 687 O GLY A 138 17.539 -17.577 25.468 1.00 44.03 O ANISOU 687 O GLY A 138 5074 5977 5679 1587 -89 426 O ATOM 688 N ARG A 139 16.413 -19.323 26.330 1.00 36.63 N ANISOU 688 N ARG A 139 4463 4831 4623 1602 -147 494 N ATOM 689 CA ARG A 139 15.713 -19.556 25.077 1.00 35.88 C ANISOU 689 CA ARG A 139 4367 4737 4530 1558 -14 455 C ATOM 690 C ARG A 139 14.744 -18.431 24.773 1.00 42.22 C ANISOU 690 C ARG A 139 5138 5615 5290 1410 79 457 C ATOM 691 O ARG A 139 14.508 -18.123 23.594 1.00 33.78 O ANISOU 691 O ARG A 139 4002 4590 4242 1377 172 414 O ATOM 692 CB ARG A 139 14.988 -20.897 25.111 1.00 38.16 C ANISOU 692 CB ARG A 139 4848 4882 4770 1570 -13 476 C ATOM 693 CG ARG A 139 15.935 -22.069 25.331 1.00 37.97 C ANISOU 693 CG ARG A 139 4871 4765 4793 1730 -113 469 C ATOM 694 CD ARG A 139 15.233 -23.380 25.133 1.00 45.41 C ANISOU 694 CD ARG A 139 6001 5563 5691 1737 -98 480 C ATOM 695 NE ARG A 139 16.187 -24.477 25.195 1.00 46.76 N ANISOU 695 NE ARG A 139 6208 5639 5918 1906 -195 463 N ATOM 696 CZ ARG A 139 15.861 -25.754 25.048 1.00 46.49 C ANISOU 696 CZ ARG A 139 6342 5461 5860 1948 -208 467 C ATOM 697 NH1 ARG A 139 14.597 -26.099 24.831 1.00 46.02 N ANISOU 697 NH1 ARG A 139 6422 5338 5723 1823 -128 489 N ATOM 698 NH2 ARG A 139 16.803 -26.683 25.104 1.00 43.45 N ANISOU 698 NH2 ARG A 139 5979 4989 5541 2117 -307 445 N ATOM 699 N ILE A 140 14.210 -17.782 25.818 1.00 39.71 N ANISOU 699 N ILE A 140 4871 5306 4910 1325 50 503 N ATOM 700 CA ILE A 140 13.298 -16.661 25.612 1.00 39.11 C ANISOU 700 CA ILE A 140 4755 5295 4808 1196 127 498 C ATOM 701 C ILE A 140 14.058 -15.456 25.082 1.00 42.53 C ANISOU 701 C ILE A 140 5013 5852 5294 1194 138 466 C ATOM 702 O ILE A 140 13.582 -14.744 24.187 1.00 41.27 O ANISOU 702 O ILE A 140 4796 5743 5141 1126 214 438 O ATOM 703 CB ILE A 140 12.552 -16.341 26.912 1.00 34.21 C ANISOU 703 CB ILE A 140 4244 4643 4110 1113 108 545 C ATOM 704 CG1 ILE A 140 11.705 -17.555 27.315 1.00 35.70 C ANISOU 704 CG1 ILE A 140 4617 4702 4247 1091 127 574 C ATOM 705 CG2 ILE A 140 11.712 -15.057 26.753 1.00 31.40 C ANISOU 705 CG2 ILE A 140 3823 4359 3749 996 179 529 C ATOM 706 CD1 ILE A 140 10.747 -17.295 28.493 1.00 33.02 C ANISOU 706 CD1 ILE A 140 4402 4321 3825 982 159 611 C ATOM 707 N VAL A 141 15.257 -15.226 25.612 1.00 33.00 N ANISOU 707 N VAL A 141 3724 4687 4128 1266 55 469 N ATOM 708 CA VAL A 141 16.148 -14.224 25.045 1.00 38.24 C ANISOU 708 CA VAL A 141 4210 5461 4860 1266 72 432 C ATOM 709 C VAL A 141 16.416 -14.534 23.573 1.00 44.53 C ANISOU 709 C VAL A 141 4937 6275 5706 1298 173 377 C ATOM 710 O VAL A 141 16.263 -13.665 22.701 1.00 42.65 O ANISOU 710 O VAL A 141 4635 6102 5467 1226 255 352 O ATOM 711 CB VAL A 141 17.447 -14.154 25.874 1.00 42.68 C ANISOU 711 CB VAL A 141 4686 6047 5482 1350 -50 436 C ATOM 712 CG1 VAL A 141 18.436 -13.122 25.316 1.00 38.86 C ANISOU 712 CG1 VAL A 141 4000 5677 5087 1340 -24 393 C ATOM 713 CG2 VAL A 141 17.116 -13.861 27.338 1.00 40.65 C ANISOU 713 CG2 VAL A 141 4543 5756 5146 1311 -154 492 C ATOM 714 N ALA A 142 16.794 -15.791 23.275 1.00 40.67 N ANISOU 714 N ALA A 142 4482 5719 5250 1404 168 357 N ATOM 715 CA ALA A 142 17.015 -16.208 21.887 1.00 46.87 C ANISOU 715 CA ALA A 142 5234 6506 6069 1438 274 299 C ATOM 716 C ALA A 142 15.796 -15.926 21.027 1.00 45.50 C ANISOU 716 C ALA A 142 5146 6319 5821 1330 359 296 C ATOM 717 O ALA A 142 15.912 -15.493 19.872 1.00 39.44 O ANISOU 717 O ALA A 142 4337 5593 5054 1298 451 254 O ATOM 718 CB ALA A 142 17.348 -17.698 21.828 1.00 45.42 C ANISOU 718 CB ALA A 142 5117 6224 5917 1565 246 281 C ATOM 719 N PHE A 143 14.618 -16.176 21.587 1.00 40.10 N ANISOU 719 N PHE A 143 4590 5571 5077 1270 328 338 N ATOM 720 CA PHE A 143 13.368 -15.903 20.902 1.00 39.48 C ANISOU 720 CA PHE A 143 4581 5471 4950 1168 381 332 C ATOM 721 C PHE A 143 13.221 -14.419 20.585 1.00 41.12 C ANISOU 721 C PHE A 143 4707 5768 5150 1078 407 327 C ATOM 722 O PHE A 143 12.849 -14.054 19.467 1.00 40.40 O ANISOU 722 O PHE A 143 4627 5684 5039 1030 460 298 O ATOM 723 CB PHE A 143 12.225 -16.429 21.771 1.00 40.67 C ANISOU 723 CB PHE A 143 4852 5537 5062 1119 345 373 C ATOM 724 CG PHE A 143 10.885 -15.799 21.501 1.00 34.93 C ANISOU 724 CG PHE A 143 4151 4805 4315 1000 375 371 C ATOM 725 CD1 PHE A 143 10.043 -16.318 20.524 1.00 39.43 C ANISOU 725 CD1 PHE A 143 4786 5312 4882 968 404 342 C ATOM 726 CD2 PHE A 143 10.444 -14.740 22.265 1.00 29.72 C ANISOU 726 CD2 PHE A 143 3454 4193 3647 926 363 392 C ATOM 727 CE1 PHE A 143 8.794 -15.764 20.285 1.00 37.64 C ANISOU 727 CE1 PHE A 143 4569 5073 4661 866 409 332 C ATOM 728 CE2 PHE A 143 9.196 -14.171 22.028 1.00 29.06 C ANISOU 728 CE2 PHE A 143 3377 4098 3568 829 385 379 C ATOM 729 CZ PHE A 143 8.371 -14.684 21.036 1.00 29.73 C ANISOU 729 CZ PHE A 143 3509 4121 3666 801 401 349 C ATOM 730 N PHE A 144 13.503 -13.539 21.558 1.00 41.24 N ANISOU 730 N PHE A 144 4658 5841 5171 1052 362 356 N ATOM 731 CA PHE A 144 13.435 -12.101 21.272 1.00 37.37 C ANISOU 731 CA PHE A 144 4097 5429 4675 969 381 350 C ATOM 732 C PHE A 144 14.470 -11.698 20.226 1.00 42.06 C ANISOU 732 C PHE A 144 4598 6085 5297 986 442 312 C ATOM 733 O PHE A 144 14.155 -10.949 19.291 1.00 38.48 O ANISOU 733 O PHE A 144 4154 5652 4816 916 490 294 O ATOM 734 CB PHE A 144 13.623 -11.264 22.545 1.00 30.67 C ANISOU 734 CB PHE A 144 3205 4622 3824 941 318 383 C ATOM 735 CG PHE A 144 12.355 -11.052 23.331 1.00 40.59 C ANISOU 735 CG PHE A 144 4547 5836 5040 872 301 408 C ATOM 736 CD1 PHE A 144 11.565 -9.919 23.112 1.00 37.38 C ANISOU 736 CD1 PHE A 144 4126 5454 4624 783 319 399 C ATOM 737 CD2 PHE A 144 11.947 -11.977 24.295 1.00 35.24 C ANISOU 737 CD2 PHE A 144 3967 5087 4336 893 275 437 C ATOM 738 CE1 PHE A 144 10.377 -9.731 23.810 1.00 32.50 C ANISOU 738 CE1 PHE A 144 3565 4794 3989 724 321 407 C ATOM 739 CE2 PHE A 144 10.763 -11.777 25.012 1.00 39.26 C ANISOU 739 CE2 PHE A 144 4549 5556 4813 818 290 450 C ATOM 740 CZ PHE A 144 9.981 -10.654 24.767 1.00 34.71 C ANISOU 740 CZ PHE A 144 3932 5011 4246 736 318 430 C ATOM 741 N SER A 145 15.714 -12.183 20.364 1.00 31.31 N ANISOU 741 N SER A 145 3153 4749 3996 1077 441 294 N ATOM 742 CA SER A 145 16.757 -11.816 19.405 1.00 37.96 C ANISOU 742 CA SER A 145 3891 5653 4880 1086 527 247 C ATOM 743 C SER A 145 16.431 -12.315 18.003 1.00 39.28 C ANISOU 743 C SER A 145 4144 5779 5004 1082 627 207 C ATOM 744 O SER A 145 16.792 -11.673 17.006 1.00 40.39 O ANISOU 744 O SER A 145 4260 5958 5127 1031 719 176 O ATOM 745 CB SER A 145 18.107 -12.359 19.844 1.00 38.93 C ANISOU 745 CB SER A 145 3888 5801 5103 1197 504 223 C ATOM 746 OG SER A 145 18.566 -11.643 20.953 1.00 54.24 O ANISOU 746 OG SER A 145 5740 7789 7079 1183 410 252 O ATOM 747 N PHE A 146 15.763 -13.467 17.907 1.00 43.14 N ANISOU 747 N PHE A 146 4747 6179 5467 1128 610 207 N ATOM 748 CA PHE A 146 15.353 -13.977 16.601 1.00 45.65 C ANISOU 748 CA PHE A 146 5172 6442 5732 1120 686 168 C ATOM 749 C PHE A 146 14.310 -13.064 15.965 1.00 42.40 C ANISOU 749 C PHE A 146 4842 6023 5245 1001 685 180 C ATOM 750 O PHE A 146 14.454 -12.641 14.810 1.00 36.40 O ANISOU 750 O PHE A 146 4123 5271 4437 957 759 149 O ATOM 751 CB PHE A 146 14.825 -15.410 16.733 1.00 44.35 C ANISOU 751 CB PHE A 146 5117 6173 5562 1189 650 168 C ATOM 752 CG PHE A 146 14.257 -15.967 15.452 1.00 41.60 C ANISOU 752 CG PHE A 146 4902 5752 5151 1173 705 129 C ATOM 753 CD1 PHE A 146 15.030 -16.015 14.295 1.00 40.10 C ANISOU 753 CD1 PHE A 146 4714 5578 4945 1198 818 69 C ATOM 754 CD2 PHE A 146 12.948 -16.425 15.400 1.00 37.46 C ANISOU 754 CD2 PHE A 146 4506 5142 4586 1125 648 146 C ATOM 755 CE1 PHE A 146 14.509 -16.519 13.111 1.00 35.09 C ANISOU 755 CE1 PHE A 146 4232 4868 4234 1180 862 31 C ATOM 756 CE2 PHE A 146 12.421 -16.943 14.224 1.00 42.15 C ANISOU 756 CE2 PHE A 146 5231 5661 5123 1109 676 107 C ATOM 757 CZ PHE A 146 13.206 -16.987 13.074 1.00 38.01 C ANISOU 757 CZ PHE A 146 4733 5147 4562 1138 778 52 C ATOM 758 N GLY A 147 13.260 -12.724 16.719 1.00 39.45 N ANISOU 758 N GLY A 147 4497 5629 4862 946 600 222 N ATOM 759 CA GLY A 147 12.297 -11.746 16.230 1.00 30.97 C ANISOU 759 CA GLY A 147 3475 4549 3744 844 577 228 C ATOM 760 C GLY A 147 12.963 -10.451 15.795 1.00 33.10 C ANISOU 760 C GLY A 147 3686 4894 3996 789 618 224 C ATOM 761 O GLY A 147 12.712 -9.943 14.699 1.00 36.51 O ANISOU 761 O GLY A 147 4197 5307 4368 731 645 207 O ATOM 762 N GLY A 148 13.851 -9.922 16.639 1.00 34.70 N ANISOU 762 N GLY A 148 3764 5173 4247 802 617 240 N ATOM 763 CA GLY A 148 14.566 -8.705 16.283 1.00 30.24 C ANISOU 763 CA GLY A 148 3136 4678 3676 739 661 235 C ATOM 764 C GLY A 148 15.318 -8.820 14.971 1.00 38.23 C ANISOU 764 C GLY A 148 4174 5697 4656 734 783 192 C ATOM 765 O GLY A 148 15.222 -7.934 14.117 1.00 35.36 O ANISOU 765 O GLY A 148 3874 5334 4228 648 822 188 O ATOM 766 N ALA A 149 16.062 -9.925 14.779 1.00 32.10 N ANISOU 766 N ALA A 149 3363 4915 3919 826 848 155 N ATOM 767 CA ALA A 149 16.811 -10.099 13.538 1.00 37.95 C ANISOU 767 CA ALA A 149 4130 5659 4629 825 992 101 C ATOM 768 C ALA A 149 15.878 -10.251 12.333 1.00 42.42 C ANISOU 768 C ALA A 149 4902 6141 5076 775 1009 89 C ATOM 769 O ALA A 149 16.193 -9.765 11.236 1.00 37.13 O ANISOU 769 O ALA A 149 4309 5469 4329 711 1111 63 O ATOM 770 CB ALA A 149 17.764 -11.292 13.649 1.00 34.41 C ANISOU 770 CB ALA A 149 3595 5214 4266 950 1052 54 C ATOM 771 N LEU A 150 14.736 -10.930 12.507 1.00 41.71 N ANISOU 771 N LEU A 150 4911 5974 4964 798 908 107 N ATOM 772 CA LEU A 150 13.741 -10.954 11.435 1.00 47.11 C ANISOU 772 CA LEU A 150 5784 6570 5544 742 883 97 C ATOM 773 C LEU A 150 13.310 -9.546 11.050 1.00 43.79 C ANISOU 773 C LEU A 150 5419 6158 5063 631 845 122 C ATOM 774 O LEU A 150 13.190 -9.230 9.857 1.00 38.01 O ANISOU 774 O LEU A 150 4838 5380 4226 572 882 104 O ATOM 775 CB LEU A 150 12.512 -11.767 11.836 1.00 40.32 C ANISOU 775 CB LEU A 150 4989 5631 4702 768 765 112 C ATOM 776 CG LEU A 150 12.717 -13.270 11.810 1.00 43.70 C ANISOU 776 CG LEU A 150 5447 6006 5152 864 796 82 C ATOM 777 CD1 LEU A 150 11.410 -13.977 12.085 1.00 47.79 C ANISOU 777 CD1 LEU A 150 6045 6435 5679 859 684 96 C ATOM 778 CD2 LEU A 150 13.301 -13.692 10.475 1.00 45.64 C ANISOU 778 CD2 LEU A 150 5803 6219 5320 879 912 24 C ATOM 779 N CYS A 151 13.074 -8.687 12.049 1.00 32.57 N ANISOU 779 N CYS A 151 3894 4785 3697 601 767 164 N ATOM 780 CA CYS A 151 12.625 -7.325 11.763 1.00 41.14 C ANISOU 780 CA CYS A 151 5031 5865 4733 503 715 187 C ATOM 781 C CYS A 151 13.700 -6.520 11.040 1.00 42.77 C ANISOU 781 C CYS A 151 5248 6117 4884 441 835 177 C ATOM 782 O CYS A 151 13.427 -5.858 10.031 1.00 41.17 O ANISOU 782 O CYS A 151 5200 5865 4579 362 837 177 O ATOM 783 CB CYS A 151 12.223 -6.637 13.063 1.00 30.32 C ANISOU 783 CB CYS A 151 3544 4535 3440 494 620 224 C ATOM 784 SG CYS A 151 10.640 -7.170 13.613 1.00 42.07 S ANISOU 784 SG CYS A 151 5065 5947 4971 516 489 232 S ATOM 785 N VAL A 152 14.927 -6.567 11.556 1.00 36.76 N ANISOU 785 N VAL A 152 4328 5444 4195 470 931 166 N ATOM 786 CA VAL A 152 16.060 -5.900 10.926 1.00 38.98 C ANISOU 786 CA VAL A 152 4585 5775 4450 405 1074 146 C ATOM 787 C VAL A 152 16.255 -6.393 9.491 1.00 48.65 C ANISOU 787 C VAL A 152 5975 6944 5566 388 1201 101 C ATOM 788 O VAL A 152 16.429 -5.594 8.558 1.00 45.15 O ANISOU 788 O VAL A 152 5658 6478 5017 286 1274 100 O ATOM 789 CB VAL A 152 17.322 -6.113 11.781 1.00 33.88 C ANISOU 789 CB VAL A 152 3710 5228 3936 461 1141 128 C ATOM 790 CG1 VAL A 152 18.555 -5.617 11.046 1.00 36.29 C ANISOU 790 CG1 VAL A 152 3968 5583 4239 396 1319 89 C ATOM 791 CG2 VAL A 152 17.160 -5.401 13.138 1.00 42.11 C ANISOU 791 CG2 VAL A 152 4629 6317 5055 454 1011 173 C ATOM 792 N GLU A 153 16.254 -7.715 9.290 1.00 42.59 N ANISOU 792 N GLU A 153 5227 6143 4811 483 1235 63 N ATOM 793 CA GLU A 153 16.390 -8.223 7.931 1.00 45.68 C ANISOU 793 CA GLU A 153 5798 6470 5086 469 1355 15 C ATOM 794 C GLU A 153 15.253 -7.718 7.050 1.00 44.64 C ANISOU 794 C GLU A 153 5918 6237 4805 385 1257 40 C ATOM 795 O GLU A 153 15.474 -7.317 5.900 1.00 40.70 O ANISOU 795 O GLU A 153 5597 5696 4172 305 1353 22 O ATOM 796 CB GLU A 153 16.435 -9.748 7.935 1.00 52.12 C ANISOU 796 CB GLU A 153 6608 7252 5943 592 1379 -29 C ATOM 797 CG GLU A 153 16.363 -10.391 6.550 1.00 65.63 C ANISOU 797 CG GLU A 153 8541 8875 7520 585 1479 -83 C ATOM 798 CD GLU A 153 17.718 -10.625 5.918 1.00 82.24 C ANISOU 798 CD GLU A 153 10600 11021 9628 598 1720 -155 C ATOM 799 OE1 GLU A 153 17.931 -11.739 5.390 1.00 87.72 O ANISOU 799 OE1 GLU A 153 11360 11666 10304 676 1805 -216 O ATOM 800 OE2 GLU A 153 18.564 -9.702 5.943 1.00 88.19 O ANISOU 800 OE2 GLU A 153 11249 11852 10408 528 1830 -156 O ATOM 801 N SER A 154 14.038 -7.686 7.590 1.00 39.64 N ANISOU 801 N SER A 154 5303 5560 4198 398 1064 78 N ATOM 802 CA SER A 154 12.886 -7.277 6.800 1.00 44.29 C ANISOU 802 CA SER A 154 6110 6042 4675 335 935 94 C ATOM 803 C SER A 154 13.018 -5.835 6.331 1.00 48.80 C ANISOU 803 C SER A 154 6772 6609 5160 220 937 123 C ATOM 804 O SER A 154 12.742 -5.522 5.167 1.00 41.59 O ANISOU 804 O SER A 154 6097 5606 4098 152 931 119 O ATOM 805 CB SER A 154 11.612 -7.464 7.620 1.00 42.46 C ANISOU 805 CB SER A 154 5825 5776 4531 372 739 121 C ATOM 806 OG SER A 154 11.353 -8.844 7.777 1.00 48.27 O ANISOU 806 OG SER A 154 6549 6481 5311 457 733 94 O ATOM 807 N VAL A 155 13.412 -4.938 7.239 1.00 43.95 N ANISOU 807 N VAL A 155 5989 6079 4631 195 933 156 N ATOM 808 CA VAL A 155 13.588 -3.539 6.888 1.00 38.78 C ANISOU 808 CA VAL A 155 5413 5417 3903 83 934 186 C ATOM 809 C VAL A 155 14.750 -3.381 5.922 1.00 47.27 C ANISOU 809 C VAL A 155 6575 6507 4877 10 1149 158 C ATOM 810 O VAL A 155 14.685 -2.598 4.965 1.00 50.33 O ANISOU 810 O VAL A 155 7178 6826 5120 -95 1166 172 O ATOM 811 CB VAL A 155 13.800 -2.703 8.161 1.00 43.74 C ANISOU 811 CB VAL A 155 5833 6131 4654 77 884 220 C ATOM 812 CG1 VAL A 155 14.098 -1.287 7.791 1.00 47.31 C ANISOU 812 CG1 VAL A 155 6369 6574 5034 -43 899 249 C ATOM 813 CG2 VAL A 155 12.571 -2.752 9.017 1.00 41.33 C ANISOU 813 CG2 VAL A 155 5475 5798 4430 132 692 241 C ATOM 814 N ASP A 156 15.821 -4.140 6.140 1.00 42.98 N ANISOU 814 N ASP A 156 5873 6046 4410 63 1320 115 N ATOM 815 CA ASP A 156 16.975 -4.053 5.262 1.00 45.93 C ANISOU 815 CA ASP A 156 6296 6441 4714 -4 1557 74 C ATOM 816 C ASP A 156 16.630 -4.465 3.833 1.00 51.56 C ANISOU 816 C ASP A 156 7314 7040 5237 -39 1613 45 C ATOM 817 O ASP A 156 17.224 -3.949 2.881 1.00 58.92 O ANISOU 817 O ASP A 156 8400 7946 6040 -147 1774 30 O ATOM 818 CB ASP A 156 18.100 -4.918 5.833 1.00 57.82 C ANISOU 818 CB ASP A 156 7547 8049 6373 88 1705 20 C ATOM 819 CG ASP A 156 19.331 -4.922 4.964 1.00 75.65 C ANISOU 819 CG ASP A 156 9815 10335 8592 29 1976 -42 C ATOM 820 OD1 ASP A 156 20.084 -3.930 5.007 1.00 85.07 O ANISOU 820 OD1 ASP A 156 10933 11584 9807 -76 2074 -34 O ATOM 821 OD2 ASP A 156 19.545 -5.915 4.234 1.00 86.19 O ANISOU 821 OD2 ASP A 156 11236 11634 9880 81 2098 -103 O ATOM 822 N LYS A 157 15.680 -5.385 3.657 1.00 49.68 N ANISOU 822 N LYS A 157 7180 6725 4972 41 1485 37 N ATOM 823 CA LYS A 157 15.302 -5.887 2.341 1.00 49.65 C ANISOU 823 CA LYS A 157 7476 6601 4786 17 1512 5 C ATOM 824 C LYS A 157 14.077 -5.187 1.777 1.00 49.27 C ANISOU 824 C LYS A 157 7684 6429 4608 -51 1296 52 C ATOM 825 O LYS A 157 13.500 -5.680 0.801 1.00 48.44 O ANISOU 825 O LYS A 157 7836 6207 4363 -56 1245 31 O ATOM 826 CB LYS A 157 15.020 -7.391 2.390 1.00 54.69 C ANISOU 826 CB LYS A 157 8094 7213 5472 143 1495 -41 C ATOM 827 CG LYS A 157 16.167 -8.259 2.827 1.00 55.98 C ANISOU 827 CG LYS A 157 8038 7472 5761 233 1687 -98 C ATOM 828 CD LYS A 157 17.353 -8.042 1.956 1.00 49.42 C ANISOU 828 CD LYS A 157 7266 6663 4848 165 1960 -152 C ATOM 829 CE LYS A 157 18.441 -9.045 2.252 1.00 51.48 C ANISOU 829 CE LYS A 157 7316 6999 5245 274 2145 -228 C ATOM 830 NZ LYS A 157 19.727 -8.427 1.839 1.00 68.33 N ANISOU 830 NZ LYS A 157 9382 9202 7380 190 2408 -270 N ATOM 831 N GLU A 158 13.627 -4.096 2.407 1.00 47.89 N ANISOU 831 N GLU A 158 7440 6270 4488 -92 1149 110 N ATOM 832 CA GLU A 158 12.477 -3.322 1.931 1.00 49.65 C ANISOU 832 CA GLU A 158 7882 6369 4612 -147 925 151 C ATOM 833 C GLU A 158 11.201 -4.161 1.958 1.00 44.09 C ANISOU 833 C GLU A 158 7221 5584 3948 -62 713 139 C ATOM 834 O GLU A 158 10.427 -4.207 0.996 1.00 52.84 O ANISOU 834 O GLU A 158 8595 6557 4926 -89 582 135 O ATOM 835 CB GLU A 158 12.733 -2.738 0.535 1.00 48.75 C ANISOU 835 CB GLU A 158 8110 6152 4262 -268 1000 154 C ATOM 836 CG GLU A 158 13.757 -1.621 0.538 1.00 51.65 C ANISOU 836 CG GLU A 158 8454 6578 4594 -383 1167 178 C ATOM 837 CD GLU A 158 14.057 -1.108 -0.857 1.00 73.37 C ANISOU 837 CD GLU A 158 11567 9217 7092 -517 1271 180 C ATOM 838 OE1 GLU A 158 13.263 -1.396 -1.781 1.00 76.58 O ANISOU 838 OE1 GLU A 158 12269 9483 7343 -521 1143 176 O ATOM 839 OE2 GLU A 158 15.086 -0.418 -1.029 1.00 83.20 O ANISOU 839 OE2 GLU A 158 12809 10510 8292 -625 1479 184 O ATOM 840 N MET A 159 10.996 -4.832 3.080 1.00 38.39 N ANISOU 840 N MET A 159 6239 4938 3408 36 676 133 N ATOM 841 CA MET A 159 9.741 -5.475 3.445 1.00 40.33 C ANISOU 841 CA MET A 159 6452 5126 3744 106 474 127 C ATOM 842 C MET A 159 9.306 -4.999 4.827 1.00 40.81 C ANISOU 842 C MET A 159 6259 5260 3985 140 374 158 C ATOM 843 O MET A 159 9.010 -5.792 5.721 1.00 48.22 O ANISOU 843 O MET A 159 7023 6241 5059 216 352 149 O ATOM 844 CB MET A 159 9.883 -6.989 3.409 1.00 39.29 C ANISOU 844 CB MET A 159 6292 4997 3641 188 550 81 C ATOM 845 CG MET A 159 10.144 -7.524 2.030 1.00 40.77 C ANISOU 845 CG MET A 159 6753 5094 3646 161 632 41 C ATOM 846 SD MET A 159 10.510 -9.299 2.034 1.00 48.70 S ANISOU 846 SD MET A 159 7712 6102 4687 266 751 -21 S ATOM 847 CE MET A 159 12.042 -9.316 2.945 1.00 45.97 C ANISOU 847 CE MET A 159 7082 5924 4458 310 994 -28 C ATOM 848 N GLN A 160 9.288 -3.674 5.007 1.00 45.46 N ANISOU 848 N GLN A 160 6847 5857 4569 78 321 195 N ATOM 849 CA GLN A 160 8.973 -3.069 6.300 1.00 46.92 C ANISOU 849 CA GLN A 160 6811 6110 4907 102 246 220 C ATOM 850 C GLN A 160 7.614 -3.515 6.813 1.00 48.26 C ANISOU 850 C GLN A 160 6912 6228 5197 161 65 207 C ATOM 851 O GLN A 160 7.407 -3.586 8.027 1.00 49.30 O ANISOU 851 O GLN A 160 6835 6427 5468 205 54 212 O ATOM 852 CB GLN A 160 9.006 -1.542 6.195 1.00 42.94 C ANISOU 852 CB GLN A 160 6373 5585 4357 22 189 256 C ATOM 853 CG GLN A 160 10.368 -0.940 5.835 1.00 65.23 C ANISOU 853 CG GLN A 160 9235 8466 7083 -59 380 271 C ATOM 854 CD GLN A 160 10.657 -0.787 4.303 1.00 75.34 C ANISOU 854 CD GLN A 160 10821 9650 8156 -144 440 267 C ATOM 855 OE1 GLN A 160 9.956 -1.330 3.427 1.00 58.50 O ANISOU 855 OE1 GLN A 160 8886 7408 5934 -132 348 249 O ATOM 856 NE2 GLN A 160 11.715 -0.033 4.001 1.00 83.44 N ANISOU 856 NE2 GLN A 160 11891 10712 9101 -239 599 283 N ATOM 857 N VAL A 161 6.685 -3.828 5.905 1.00 46.20 N ANISOU 857 N VAL A 161 6827 5843 4883 158 -76 187 N ATOM 858 CA VAL A 161 5.346 -4.263 6.292 1.00 48.80 C ANISOU 858 CA VAL A 161 7085 6115 5343 203 -250 164 C ATOM 859 C VAL A 161 5.388 -5.426 7.285 1.00 51.22 C ANISOU 859 C VAL A 161 7196 6494 5772 269 -165 149 C ATOM 860 O VAL A 161 4.487 -5.569 8.122 1.00 58.46 O ANISOU 860 O VAL A 161 7969 7410 6834 297 -251 138 O ATOM 861 CB VAL A 161 4.540 -4.627 5.025 1.00 49.74 C ANISOU 861 CB VAL A 161 7439 6086 5375 188 -403 137 C ATOM 862 CG1 VAL A 161 5.248 -5.742 4.247 1.00 45.86 C ANISOU 862 CG1 VAL A 161 7084 5585 4757 194 -266 116 C ATOM 863 CG2 VAL A 161 3.129 -5.058 5.388 1.00 52.02 C ANISOU 863 CG2 VAL A 161 7633 6310 5825 226 -590 105 C ATOM 864 N LEU A 162 6.437 -6.258 7.229 1.00 46.07 N ANISOU 864 N LEU A 162 6538 5902 5066 293 10 145 N ATOM 865 CA LEU A 162 6.488 -7.441 8.078 1.00 42.43 C ANISOU 865 CA LEU A 162 5931 5486 4703 359 74 133 C ATOM 866 C LEU A 162 6.816 -7.120 9.530 1.00 38.29 C ANISOU 866 C LEU A 162 5185 5070 4293 383 128 159 C ATOM 867 O LEU A 162 6.575 -7.967 10.396 1.00 40.89 O ANISOU 867 O LEU A 162 5403 5420 4715 430 142 155 O ATOM 868 CB LEU A 162 7.509 -8.448 7.554 1.00 34.98 C ANISOU 868 CB LEU A 162 5053 4559 3677 393 230 112 C ATOM 869 CG LEU A 162 7.326 -8.966 6.134 1.00 50.54 C ANISOU 869 CG LEU A 162 7266 6422 5514 374 208 79 C ATOM 870 CD1 LEU A 162 8.524 -9.828 5.735 1.00 42.47 C ANISOU 870 CD1 LEU A 162 6283 5434 4421 414 403 51 C ATOM 871 CD2 LEU A 162 6.005 -9.740 5.992 1.00 51.93 C ANISOU 871 CD2 LEU A 162 7491 6493 5747 388 43 54 C ATOM 872 N VAL A 163 7.365 -5.938 9.821 1.00 36.77 N ANISOU 872 N VAL A 163 4945 4939 4088 348 157 186 N ATOM 873 CA VAL A 163 7.749 -5.624 11.199 1.00 45.73 C ANISOU 873 CA VAL A 163 5888 6171 5316 369 202 208 C ATOM 874 C VAL A 163 6.552 -5.732 12.134 1.00 43.67 C ANISOU 874 C VAL A 163 5530 5886 5176 387 102 203 C ATOM 875 O VAL A 163 6.627 -6.361 13.197 1.00 35.44 O ANISOU 875 O VAL A 163 4372 4889 4205 426 148 208 O ATOM 876 CB VAL A 163 8.387 -4.231 11.284 1.00 43.98 C ANISOU 876 CB VAL A 163 5649 6000 5061 314 224 234 C ATOM 877 CG1 VAL A 163 8.647 -3.866 12.769 1.00 36.58 C ANISOU 877 CG1 VAL A 163 4528 5150 4220 334 242 254 C ATOM 878 CG2 VAL A 163 9.672 -4.214 10.477 1.00 35.97 C ANISOU 878 CG2 VAL A 163 4703 5021 3944 287 363 234 C ATOM 879 N SER A 164 5.432 -5.114 11.757 1.00 44.68 N ANISOU 879 N SER A 164 5709 5936 5332 357 -36 188 N ATOM 880 CA SER A 164 4.257 -5.158 12.620 1.00 42.81 C ANISOU 880 CA SER A 164 5361 5674 5231 368 -114 169 C ATOM 881 C SER A 164 3.689 -6.567 12.688 1.00 43.96 C ANISOU 881 C SER A 164 5498 5778 5429 395 -110 145 C ATOM 882 O SER A 164 3.190 -6.988 13.740 1.00 43.08 O ANISOU 882 O SER A 164 5270 5681 5416 407 -87 139 O ATOM 883 CB SER A 164 3.191 -4.174 12.133 1.00 36.35 C ANISOU 883 CB SER A 164 4585 4773 4454 340 -275 147 C ATOM 884 OG SER A 164 2.449 -4.731 11.058 1.00 44.96 O ANISOU 884 OG SER A 164 5792 5757 5532 336 -385 117 O ATOM 885 N ARG A 165 3.769 -7.321 11.584 1.00 37.25 N ANISOU 885 N ARG A 165 4783 4868 4503 398 -125 131 N ATOM 886 CA ARG A 165 3.299 -8.703 11.633 1.00 37.13 C ANISOU 886 CA ARG A 165 4770 4804 4531 420 -120 109 C ATOM 887 C ARG A 165 4.172 -9.549 12.549 1.00 44.31 C ANISOU 887 C ARG A 165 5605 5787 5442 465 21 132 C ATOM 888 O ARG A 165 3.657 -10.359 13.331 1.00 39.71 O ANISOU 888 O ARG A 165 4958 5189 4939 475 34 127 O ATOM 889 CB ARG A 165 3.262 -9.306 10.241 1.00 33.56 C ANISOU 889 CB ARG A 165 4501 4266 3985 416 -168 85 C ATOM 890 CG ARG A 165 2.410 -8.513 9.309 1.00 39.32 C ANISOU 890 CG ARG A 165 5332 4905 4703 376 -335 65 C ATOM 891 CD ARG A 165 2.395 -9.152 7.958 1.00 46.35 C ANISOU 891 CD ARG A 165 6431 5700 5478 368 -386 41 C ATOM 892 NE ARG A 165 1.837 -8.257 6.960 1.00 59.10 N ANISOU 892 NE ARG A 165 8190 7225 7039 330 -551 31 N ATOM 893 CZ ARG A 165 1.771 -8.557 5.673 1.00 65.10 C ANISOU 893 CZ ARG A 165 9177 7884 7672 311 -625 13 C ATOM 894 NH1 ARG A 165 2.230 -9.728 5.249 1.00 63.24 N ANISOU 894 NH1 ARG A 165 9036 7633 7360 330 -534 -4 N ATOM 895 NH2 ARG A 165 1.252 -7.690 4.818 1.00 68.35 N ANISOU 895 NH2 ARG A 165 9738 8204 8029 276 -795 9 N ATOM 896 N ILE A 166 5.497 -9.380 12.465 1.00 37.24 N ANISOU 896 N ILE A 166 4722 4966 4463 489 124 154 N ATOM 897 CA ILE A 166 6.390 -10.148 13.328 1.00 39.97 C ANISOU 897 CA ILE A 166 4993 5373 4821 544 232 173 C ATOM 898 C ILE A 166 6.118 -9.811 14.787 1.00 38.71 C ANISOU 898 C ILE A 166 4702 5262 4746 541 232 196 C ATOM 899 O ILE A 166 6.068 -10.697 15.649 1.00 38.00 O ANISOU 899 O ILE A 166 4575 5169 4696 570 264 206 O ATOM 900 CB ILE A 166 7.860 -9.897 12.939 1.00 35.82 C ANISOU 900 CB ILE A 166 4474 4917 4217 568 335 181 C ATOM 901 CG1 ILE A 166 8.136 -10.502 11.553 1.00 36.95 C ANISOU 901 CG1 ILE A 166 4768 5003 4269 576 368 149 C ATOM 902 CG2 ILE A 166 8.820 -10.465 14.021 1.00 31.93 C ANISOU 902 CG2 ILE A 166 3871 4495 3765 632 415 200 C ATOM 903 CD1 ILE A 166 9.407 -10.001 10.887 1.00 34.89 C ANISOU 903 CD1 ILE A 166 4533 4797 3926 570 480 144 C ATOM 904 N ALA A 167 5.891 -8.529 15.071 1.00 34.67 N ANISOU 904 N ALA A 167 4138 4783 4253 502 193 204 N ATOM 905 CA ALA A 167 5.610 -8.092 16.431 1.00 29.65 C ANISOU 905 CA ALA A 167 3394 4186 3683 494 199 219 C ATOM 906 C ALA A 167 4.384 -8.804 16.979 1.00 35.16 C ANISOU 906 C ALA A 167 4070 4822 4468 480 177 199 C ATOM 907 O ALA A 167 4.392 -9.298 18.114 1.00 41.23 O ANISOU 907 O ALA A 167 4795 5607 5263 490 230 214 O ATOM 908 CB ALA A 167 5.421 -6.577 16.452 1.00 29.14 C ANISOU 908 CB ALA A 167 3299 4145 3627 453 149 219 C ATOM 909 N ALA A 168 3.334 -8.902 16.163 1.00 29.51 N ANISOU 909 N ALA A 168 3390 4026 3795 452 96 162 N ATOM 910 CA ALA A 168 2.128 -9.624 16.569 1.00 36.39 C ANISOU 910 CA ALA A 168 4227 4831 4769 427 79 133 C ATOM 911 C ALA A 168 2.410 -11.104 16.808 1.00 46.23 C ANISOU 911 C ALA A 168 5520 6051 5993 450 143 146 C ATOM 912 O ALA A 168 1.940 -11.682 17.799 1.00 46.46 O ANISOU 912 O ALA A 168 5510 6064 6077 431 193 149 O ATOM 913 CB ALA A 168 1.043 -9.462 15.512 1.00 28.46 C ANISOU 913 CB ALA A 168 3251 3739 3823 396 -46 86 C ATOM 914 N TRP A 169 3.152 -11.746 15.890 1.00 42.21 N ANISOU 914 N TRP A 169 5109 5528 5400 488 148 151 N ATOM 915 CA TRP A 169 3.447 -13.164 16.060 1.00 34.10 C ANISOU 915 CA TRP A 169 4139 4464 4354 521 199 160 C ATOM 916 C TRP A 169 4.235 -13.402 17.347 1.00 37.94 C ANISOU 916 C TRP A 169 4582 5009 4825 558 280 202 C ATOM 917 O TRP A 169 4.014 -14.401 18.044 1.00 38.40 O ANISOU 917 O TRP A 169 4664 5022 4902 561 313 214 O ATOM 918 CB TRP A 169 4.216 -13.713 14.856 1.00 34.92 C ANISOU 918 CB TRP A 169 4355 4545 4368 567 203 149 C ATOM 919 CG TRP A 169 3.564 -13.454 13.533 1.00 44.21 C ANISOU 919 CG TRP A 169 5615 5655 5527 531 111 111 C ATOM 920 CD1 TRP A 169 2.250 -13.246 13.302 1.00 41.66 C ANISOU 920 CD1 TRP A 169 5278 5265 5287 474 6 80 C ATOM 921 CD2 TRP A 169 4.220 -13.356 12.251 1.00 44.53 C ANISOU 921 CD2 TRP A 169 5777 5684 5460 550 110 96 C ATOM 922 NE1 TRP A 169 2.031 -13.029 11.954 1.00 41.65 N ANISOU 922 NE1 TRP A 169 5393 5202 5230 460 -86 51 N ATOM 923 CE2 TRP A 169 3.224 -13.089 11.289 1.00 46.12 C ANISOU 923 CE2 TRP A 169 6058 5800 5665 501 -16 63 C ATOM 924 CE3 TRP A 169 5.550 -13.469 11.828 1.00 38.50 C ANISOU 924 CE3 TRP A 169 5061 4968 4599 601 207 103 C ATOM 925 CZ2 TRP A 169 3.514 -12.930 9.911 1.00 41.72 C ANISOU 925 CZ2 TRP A 169 5663 5197 4992 496 -49 43 C ATOM 926 CZ3 TRP A 169 5.843 -13.316 10.453 1.00 41.92 C ANISOU 926 CZ3 TRP A 169 5638 5364 4927 591 203 77 C ATOM 927 CH2 TRP A 169 4.822 -13.046 9.521 1.00 44.62 C ANISOU 927 CH2 TRP A 169 6092 5614 5249 537 74 51 C ATOM 928 N MET A 170 5.168 -12.503 17.675 1.00 34.23 N ANISOU 928 N MET A 170 4061 4629 4317 583 305 226 N ATOM 929 CA MET A 170 5.924 -12.671 18.909 1.00 35.36 C ANISOU 929 CA MET A 170 4170 4820 4446 620 353 265 C ATOM 930 C MET A 170 5.015 -12.493 20.116 1.00 39.49 C ANISOU 930 C MET A 170 4658 5329 5018 566 365 272 C ATOM 931 O MET A 170 5.056 -13.295 21.052 1.00 33.44 O ANISOU 931 O MET A 170 3928 4534 4243 575 400 297 O ATOM 932 CB MET A 170 7.086 -11.680 18.970 1.00 32.14 C ANISOU 932 CB MET A 170 3704 4509 4000 647 364 281 C ATOM 933 CG MET A 170 8.080 -11.855 17.855 1.00 32.52 C ANISOU 933 CG MET A 170 3778 4575 4002 693 387 268 C ATOM 934 SD MET A 170 9.332 -10.594 17.812 1.00 35.27 S ANISOU 934 SD MET A 170 4044 5031 4325 696 411 279 S ATOM 935 CE MET A 170 10.172 -10.866 19.393 1.00 36.33 C ANISOU 935 CE MET A 170 4107 5213 4484 750 413 315 C ATOM 936 N ALA A 171 4.186 -11.440 20.103 1.00 32.36 N ANISOU 936 N ALA A 171 3694 4436 4165 510 340 248 N ATOM 937 CA ALA A 171 3.270 -11.201 21.211 1.00 39.18 C ANISOU 937 CA ALA A 171 4515 5284 5086 456 374 240 C ATOM 938 C ALA A 171 2.331 -12.384 21.393 1.00 40.62 C ANISOU 938 C ALA A 171 4735 5379 5320 417 406 225 C ATOM 939 O ALA A 171 2.087 -12.827 22.525 1.00 36.90 O ANISOU 939 O ALA A 171 4287 4887 4846 389 474 241 O ATOM 940 CB ALA A 171 2.479 -9.904 20.975 1.00 35.48 C ANISOU 940 CB ALA A 171 3966 4828 4685 414 333 201 C ATOM 941 N THR A 172 1.828 -12.929 20.280 1.00 33.90 N ANISOU 941 N THR A 172 3907 4467 4505 409 355 194 N ATOM 942 CA THR A 172 0.912 -14.055 20.345 1.00 29.24 C ANISOU 942 CA THR A 172 3350 3785 3976 361 376 175 C ATOM 943 C THR A 172 1.608 -15.272 20.930 1.00 46.21 C ANISOU 943 C THR A 172 5602 5905 6050 395 430 221 C ATOM 944 O THR A 172 1.083 -15.915 21.856 1.00 38.11 O ANISOU 944 O THR A 172 4608 4830 5044 344 496 231 O ATOM 945 CB THR A 172 0.346 -14.351 18.953 1.00 42.48 C ANISOU 945 CB THR A 172 5047 5399 5697 351 285 132 C ATOM 946 OG1 THR A 172 -0.592 -13.326 18.599 1.00 36.20 O ANISOU 946 OG1 THR A 172 4154 4601 5000 309 220 83 O ATOM 947 CG2 THR A 172 -0.353 -15.720 18.893 1.00 30.39 C ANISOU 947 CG2 THR A 172 3571 3765 4212 308 297 116 C ATOM 948 N TYR A 173 2.811 -15.590 20.426 1.00 29.41 N ANISOU 948 N TYR A 173 3534 3803 3838 480 406 246 N ATOM 949 CA TYR A 173 3.558 -16.702 21.014 1.00 37.80 C ANISOU 949 CA TYR A 173 4691 4833 4839 532 438 288 C ATOM 950 C TYR A 173 3.831 -16.472 22.501 1.00 39.83 C ANISOU 950 C TYR A 173 4954 5119 5062 525 485 330 C ATOM 951 O TYR A 173 3.655 -17.383 23.318 1.00 43.83 O ANISOU 951 O TYR A 173 5552 5557 5546 506 521 358 O ATOM 952 CB TYR A 173 4.875 -16.946 20.278 1.00 39.04 C ANISOU 952 CB TYR A 173 4879 5021 4933 637 412 295 C ATOM 953 CG TYR A 173 5.372 -18.337 20.573 1.00 39.34 C ANISOU 953 CG TYR A 173 5025 4985 4936 695 421 319 C ATOM 954 CD1 TYR A 173 6.295 -18.571 21.586 1.00 32.00 C ANISOU 954 CD1 TYR A 173 4121 4073 3964 758 425 364 C ATOM 955 CD2 TYR A 173 4.865 -19.432 19.876 1.00 46.19 C ANISOU 955 CD2 TYR A 173 5981 5752 5817 685 411 295 C ATOM 956 CE1 TYR A 173 6.730 -19.869 21.886 1.00 43.96 C ANISOU 956 CE1 TYR A 173 5750 5504 5451 820 414 386 C ATOM 957 CE2 TYR A 173 5.295 -20.735 20.158 1.00 41.98 C ANISOU 957 CE2 TYR A 173 5562 5135 5253 741 413 316 C ATOM 958 CZ TYR A 173 6.228 -20.942 21.159 1.00 48.17 C ANISOU 958 CZ TYR A 173 6371 5935 5996 812 413 362 C ATOM 959 OH TYR A 173 6.647 -22.221 21.425 1.00 48.05 O ANISOU 959 OH TYR A 173 6480 5823 5953 876 397 382 O ATOM 960 N LEU A 174 4.261 -15.260 22.866 1.00 34.87 N ANISOU 960 N LEU A 174 4249 4583 4419 534 479 337 N ATOM 961 CA LEU A 174 4.529 -14.939 24.262 1.00 44.41 C ANISOU 961 CA LEU A 174 5477 5816 5582 524 512 373 C ATOM 962 C LEU A 174 3.314 -15.215 25.138 1.00 44.46 C ANISOU 962 C LEU A 174 5520 5757 5618 426 589 365 C ATOM 963 O LEU A 174 3.412 -15.904 26.163 1.00 41.47 O ANISOU 963 O LEU A 174 5252 5326 5178 413 628 404 O ATOM 964 CB LEU A 174 4.939 -13.475 24.387 1.00 41.67 C ANISOU 964 CB LEU A 174 5034 5567 5231 530 491 368 C ATOM 965 CG LEU A 174 6.411 -13.193 24.593 1.00 54.44 C ANISOU 965 CG LEU A 174 6644 7252 6790 612 445 401 C ATOM 966 CD1 LEU A 174 6.573 -11.694 24.552 1.00 60.26 C ANISOU 966 CD1 LEU A 174 7285 8073 7537 591 429 386 C ATOM 967 CD2 LEU A 174 6.858 -13.760 25.933 1.00 56.18 C ANISOU 967 CD2 LEU A 174 6960 7441 6944 632 445 447 C ATOM 968 N ASN A 175 2.159 -14.689 24.739 1.00 36.50 N ANISOU 968 N ASN A 175 4422 4741 4704 353 613 312 N ATOM 969 CA ASN A 175 0.979 -14.714 25.591 1.00 48.49 C ANISOU 969 CA ASN A 175 5934 6213 6277 252 709 288 C ATOM 970 C ASN A 175 0.307 -16.084 25.640 1.00 50.98 C ANISOU 970 C ASN A 175 6333 6420 6617 194 759 289 C ATOM 971 O ASN A 175 -0.227 -16.452 26.689 1.00 55.63 O ANISOU 971 O ASN A 175 6987 6958 7191 117 863 297 O ATOM 972 CB ASN A 175 -0.009 -13.639 25.127 1.00 41.51 C ANISOU 972 CB ASN A 175 4901 5357 5516 206 705 219 C ATOM 973 CG ASN A 175 0.412 -12.251 25.559 1.00 41.35 C ANISOU 973 CG ASN A 175 4822 5422 5467 231 695 218 C ATOM 974 OD1 ASN A 175 1.115 -12.090 26.564 1.00 44.21 O ANISOU 974 OD1 ASN A 175 5254 5813 5731 248 727 260 O ATOM 975 ND2 ASN A 175 -0.016 -11.237 24.815 1.00 40.71 N ANISOU 975 ND2 ASN A 175 4626 5371 5470 233 638 171 N ATOM 976 N ASP A 176 0.340 -16.860 24.544 1.00 49.55 N ANISOU 976 N ASP A 176 6170 6195 6462 222 693 279 N ATOM 977 CA ASP A 176 -0.304 -18.171 24.529 1.00 42.39 C ANISOU 977 CA ASP A 176 5348 5176 5584 161 730 277 C ATOM 978 C ASP A 176 0.616 -19.325 24.914 1.00 45.42 C ANISOU 978 C ASP A 176 5904 5502 5851 219 721 342 C ATOM 979 O ASP A 176 0.135 -20.324 25.449 1.00 53.65 O ANISOU 979 O ASP A 176 7056 6445 6884 152 782 358 O ATOM 980 CB ASP A 176 -0.902 -18.464 23.153 1.00 43.21 C ANISOU 980 CB ASP A 176 5396 5240 5783 151 655 225 C ATOM 981 CG ASP A 176 -2.162 -17.661 22.878 1.00 53.11 C ANISOU 981 CG ASP A 176 6491 6501 7187 70 658 153 C ATOM 982 OD1 ASP A 176 -2.669 -17.000 23.815 1.00 53.38 O ANISOU 982 OD1 ASP A 176 6457 6564 7262 14 747 138 O ATOM 983 OD2 ASP A 176 -2.639 -17.682 21.714 1.00 49.85 O ANISOU 983 OD2 ASP A 176 6027 6060 6854 68 564 106 O ATOM 984 N HIS A 177 1.922 -19.238 24.678 1.00 46.16 N ANISOU 984 N HIS A 177 6027 5647 5864 341 647 375 N ATOM 985 CA HIS A 177 2.771 -20.409 24.858 1.00 38.55 C ANISOU 985 CA HIS A 177 5213 4616 4819 414 615 422 C ATOM 986 C HIS A 177 3.922 -20.227 25.826 1.00 34.19 C ANISOU 986 C HIS A 177 4722 4100 4168 494 588 478 C ATOM 987 O HIS A 177 4.396 -21.224 26.366 1.00 52.56 O ANISOU 987 O HIS A 177 7198 6344 6429 533 567 523 O ATOM 988 CB HIS A 177 3.335 -20.876 23.507 1.00 39.16 C ANISOU 988 CB HIS A 177 5283 4686 4909 504 540 398 C ATOM 989 CG HIS A 177 2.280 -21.344 22.563 1.00 60.91 C ANISOU 989 CG HIS A 177 8028 7373 7744 433 538 349 C ATOM 990 ND1 HIS A 177 1.909 -20.627 21.446 1.00 64.59 N ANISOU 990 ND1 HIS A 177 8385 7885 8270 424 496 296 N ATOM 991 CD2 HIS A 177 1.480 -22.435 22.594 1.00 67.48 C ANISOU 991 CD2 HIS A 177 8951 8084 8605 359 563 343 C ATOM 992 CE1 HIS A 177 0.945 -21.271 20.812 1.00 63.63 C ANISOU 992 CE1 HIS A 177 8285 7676 8217 355 481 257 C ATOM 993 NE2 HIS A 177 0.667 -22.371 21.488 1.00 68.86 N ANISOU 993 NE2 HIS A 177 9058 8238 8866 311 526 283 N ATOM 994 N LEU A 178 4.381 -19.004 26.070 1.00 41.09 N ANISOU 994 N LEU A 178 5495 5083 5033 518 574 477 N ATOM 995 CA LEU A 178 5.441 -18.774 27.042 1.00 40.77 C ANISOU 995 CA LEU A 178 5509 5075 4908 585 530 526 C ATOM 996 C LEU A 178 4.930 -18.252 28.374 1.00 47.23 C ANISOU 996 C LEU A 178 6383 5888 5673 497 596 546 C ATOM 997 O LEU A 178 5.538 -18.534 29.414 1.00 50.67 O ANISOU 997 O LEU A 178 6951 6288 6013 525 564 598 O ATOM 998 CB LEU A 178 6.463 -17.787 26.484 1.00 41.21 C ANISOU 998 CB LEU A 178 5428 5249 4980 671 465 511 C ATOM 999 CG LEU A 178 7.203 -18.262 25.230 1.00 46.88 C ANISOU 999 CG LEU A 178 6104 5977 5733 767 416 488 C ATOM 1000 CD1 LEU A 178 8.053 -17.128 24.668 1.00 42.43 C ANISOU 1000 CD1 LEU A 178 5396 5534 5191 817 386 468 C ATOM 1001 CD2 LEU A 178 8.064 -19.509 25.547 1.00 37.62 C ANISOU 1001 CD2 LEU A 178 5050 4724 4520 867 361 522 C ATOM 1002 N GLU A 179 3.824 -17.514 28.369 1.00 49.35 N ANISOU 1002 N GLU A 179 6565 6183 6003 395 682 503 N ATOM 1003 CA GLU A 179 3.411 -16.813 29.579 1.00 52.67 C ANISOU 1003 CA GLU A 179 7021 6615 6376 320 759 508 C ATOM 1004 C GLU A 179 3.096 -17.736 30.748 1.00 59.19 C ANISOU 1004 C GLU A 179 8055 7328 7107 253 831 552 C ATOM 1005 O GLU A 179 3.417 -17.364 31.891 1.00 51.28 O ANISOU 1005 O GLU A 179 7159 6326 6000 241 843 584 O ATOM 1006 CB GLU A 179 2.212 -15.906 29.296 1.00 39.12 C ANISOU 1006 CB GLU A 179 5158 4938 4769 230 845 439 C ATOM 1007 CG GLU A 179 1.645 -15.304 30.576 1.00 49.18 C ANISOU 1007 CG GLU A 179 6480 6206 6000 143 958 431 C ATOM 1008 CD GLU A 179 2.613 -14.360 31.294 1.00 56.74 C ANISOU 1008 CD GLU A 179 7465 7234 6860 199 900 459 C ATOM 1009 OE1 GLU A 179 3.722 -14.072 30.803 1.00 52.06 O ANISOU 1009 OE1 GLU A 179 6825 6704 6251 300 774 482 O ATOM 1010 OE2 GLU A 179 2.246 -13.878 32.377 1.00 69.07 O ANISOU 1010 OE2 GLU A 179 9095 8784 8363 134 987 453 O ATOM 1011 N PRO A 180 2.486 -18.910 30.562 1.00 54.99 N ANISOU 1011 N PRO A 180 7609 6691 6593 200 878 556 N ATOM 1012 CA PRO A 180 2.323 -19.790 31.727 1.00 52.20 C ANISOU 1012 CA PRO A 180 7491 6219 6124 135 942 609 C ATOM 1013 C PRO A 180 3.660 -20.180 32.333 1.00 56.96 C ANISOU 1013 C PRO A 180 8256 6793 6593 248 810 682 C ATOM 1014 O PRO A 180 3.814 -20.150 33.566 1.00 52.88 O ANISOU 1014 O PRO A 180 7916 6230 5948 213 830 725 O ATOM 1015 CB PRO A 180 1.555 -20.987 31.151 1.00 47.97 C ANISOU 1015 CB PRO A 180 6997 5578 5652 71 990 598 C ATOM 1016 CG PRO A 180 0.805 -20.401 29.997 1.00 51.56 C ANISOU 1016 CG PRO A 180 7215 6103 6271 47 1007 519 C ATOM 1017 CD PRO A 180 1.761 -19.427 29.387 1.00 48.84 C ANISOU 1017 CD PRO A 180 6736 5884 5937 172 889 511 C ATOM 1018 N TRP A 181 4.654 -20.503 31.495 1.00 48.11 N ANISOU 1018 N TRP A 181 7078 5699 5505 385 671 690 N ATOM 1019 CA TRP A 181 5.970 -20.820 32.035 1.00 44.16 C ANISOU 1019 CA TRP A 181 6693 5174 4911 508 528 746 C ATOM 1020 C TRP A 181 6.551 -19.627 32.777 1.00 44.81 C ANISOU 1020 C TRP A 181 6738 5347 4940 529 484 754 C ATOM 1021 O TRP A 181 7.133 -19.782 33.856 1.00 46.74 O ANISOU 1021 O TRP A 181 7157 5537 5065 553 413 806 O ATOM 1022 CB TRP A 181 6.917 -21.276 30.927 1.00 37.87 C ANISOU 1022 CB TRP A 181 5800 4401 4187 654 410 733 C ATOM 1023 CG TRP A 181 8.251 -21.698 31.448 1.00 40.39 C ANISOU 1023 CG TRP A 181 6217 4685 4445 790 254 780 C ATOM 1024 CD1 TRP A 181 8.658 -22.976 31.734 1.00 40.88 C ANISOU 1024 CD1 TRP A 181 6466 4610 4455 855 175 823 C ATOM 1025 CD2 TRP A 181 9.360 -20.841 31.773 1.00 45.88 C ANISOU 1025 CD2 TRP A 181 6825 5472 5134 880 143 785 C ATOM 1026 NE1 TRP A 181 9.951 -22.967 32.225 1.00 43.64 N ANISOU 1026 NE1 TRP A 181 6844 4961 4776 989 11 852 N ATOM 1027 CE2 TRP A 181 10.407 -21.671 32.252 1.00 48.32 C ANISOU 1027 CE2 TRP A 181 7261 5696 5401 1003 -10 827 C ATOM 1028 CE3 TRP A 181 9.577 -19.458 31.690 1.00 38.32 C ANISOU 1028 CE3 TRP A 181 5693 4654 4213 868 149 755 C ATOM 1029 CZ2 TRP A 181 11.649 -21.156 32.657 1.00 42.60 C ANISOU 1029 CZ2 TRP A 181 6479 5027 4682 1112 -159 836 C ATOM 1030 CZ3 TRP A 181 10.809 -18.950 32.090 1.00 41.52 C ANISOU 1030 CZ3 TRP A 181 6051 5113 4612 966 13 767 C ATOM 1031 CH2 TRP A 181 11.831 -19.801 32.572 1.00 44.15 C ANISOU 1031 CH2 TRP A 181 6496 5364 4915 1086 -142 805 C ATOM 1032 N ILE A 182 6.389 -18.428 32.222 1.00 41.42 N ANISOU 1032 N ILE A 182 6098 5045 4593 517 515 702 N ATOM 1033 CA ILE A 182 6.905 -17.230 32.876 1.00 40.73 C ANISOU 1033 CA ILE A 182 5970 5042 4463 528 475 703 C ATOM 1034 C ILE A 182 6.278 -17.069 34.252 1.00 47.47 C ANISOU 1034 C ILE A 182 7009 5833 5195 420 564 725 C ATOM 1035 O ILE A 182 6.959 -16.745 35.234 1.00 55.36 O ANISOU 1035 O ILE A 182 8126 6824 6085 446 485 761 O ATOM 1036 CB ILE A 182 6.657 -16.002 31.977 1.00 42.94 C ANISOU 1036 CB ILE A 182 6010 5450 4854 517 507 641 C ATOM 1037 CG1 ILE A 182 7.438 -16.137 30.649 1.00 32.76 C ANISOU 1037 CG1 ILE A 182 4572 4219 3658 623 422 623 C ATOM 1038 CG2 ILE A 182 6.987 -14.705 32.728 1.00 33.27 C ANISOU 1038 CG2 ILE A 182 4758 4299 3583 504 486 637 C ATOM 1039 CD1 ILE A 182 7.017 -15.129 29.580 1.00 31.54 C ANISOU 1039 CD1 ILE A 182 4220 4160 3605 597 461 565 C ATOM 1040 N GLN A 183 4.977 -17.341 34.352 1.00 53.72 N ANISOU 1040 N GLN A 183 7836 6571 6005 294 731 700 N ATOM 1041 CA GLN A 183 4.268 -17.190 35.617 1.00 54.07 C ANISOU 1041 CA GLN A 183 8053 6552 5937 173 861 708 C ATOM 1042 C GLN A 183 4.690 -18.258 36.629 1.00 52.21 C ANISOU 1042 C GLN A 183 8125 6179 5535 172 814 787 C ATOM 1043 O GLN A 183 5.003 -17.939 37.778 1.00 56.20 O ANISOU 1043 O GLN A 183 8810 6651 5892 152 796 820 O ATOM 1044 CB GLN A 183 2.760 -17.225 35.360 1.00 57.72 C ANISOU 1044 CB GLN A 183 8439 6995 6498 37 1062 648 C ATOM 1045 CG GLN A 183 1.952 -16.298 36.252 1.00 70.82 C ANISOU 1045 CG GLN A 183 10112 8671 8126 -74 1222 604 C ATOM 1046 CD GLN A 183 2.345 -14.843 36.087 1.00 87.66 C ANISOU 1046 CD GLN A 183 12076 10931 10300 -16 1161 565 C ATOM 1047 OE1 GLN A 183 2.927 -14.450 35.070 1.00 93.85 O ANISOU 1047 OE1 GLN A 183 12680 11800 11177 81 1036 555 O ATOM 1048 NE2 GLN A 183 2.036 -14.031 37.094 1.00 89.51 N ANISOU 1048 NE2 GLN A 183 12384 11170 10457 -80 1258 543 N ATOM 1049 N GLU A 184 4.739 -19.528 36.215 1.00 50.22 N ANISOU 1049 N GLU A 184 7954 5834 5294 197 779 819 N ATOM 1050 CA GLU A 184 5.217 -20.591 37.096 1.00 53.75 C ANISOU 1050 CA GLU A 184 8704 6133 5583 212 705 899 C ATOM 1051 C GLU A 184 6.705 -20.481 37.439 1.00 55.76 C ANISOU 1051 C GLU A 184 9016 6399 5770 367 470 945 C ATOM 1052 O GLU A 184 7.214 -21.358 38.142 1.00 66.48 O ANISOU 1052 O GLU A 184 10628 7626 7004 404 365 1012 O ATOM 1053 CB GLU A 184 4.950 -21.977 36.474 1.00 41.60 C ANISOU 1053 CB GLU A 184 7230 4487 4088 213 709 916 C ATOM 1054 N ASN A 185 7.433 -19.470 36.964 1.00 54.36 N ANISOU 1054 N ASN A 185 8615 6363 5678 460 374 911 N ATOM 1055 CA ASN A 185 8.876 -19.427 37.184 1.00 50.47 C ANISOU 1055 CA ASN A 185 8136 5881 5160 610 145 945 C ATOM 1056 C ASN A 185 9.331 -18.080 37.709 1.00 44.61 C ANISOU 1056 C ASN A 185 7321 5239 4388 613 93 928 C ATOM 1057 O ASN A 185 10.497 -17.716 37.526 1.00 47.86 O ANISOU 1057 O ASN A 185 7619 5714 4850 734 -81 928 O ATOM 1058 CB ASN A 185 9.656 -19.754 35.909 1.00 49.54 C ANISOU 1058 CB ASN A 185 7801 5823 5198 750 41 919 C ATOM 1059 CG ASN A 185 9.740 -21.229 35.648 1.00 53.07 C ANISOU 1059 CG ASN A 185 8383 6140 5643 804 -3 950 C ATOM 1060 OD1 ASN A 185 9.004 -21.769 34.828 1.00 58.88 O ANISOU 1060 OD1 ASN A 185 9065 6857 6450 760 107 925 O ATOM 1061 ND2 ASN A 185 10.641 -21.896 36.345 1.00 58.05 N ANISOU 1061 ND2 ASN A 185 9196 6667 6193 901 -180 1005 N ATOM 1062 N GLY A 186 8.436 -17.330 38.336 1.00 46.15 N ANISOU 1062 N GLY A 186 7570 5450 4516 481 247 908 N ATOM 1063 CA GLY A 186 8.806 -16.109 39.006 1.00 41.96 C ANISOU 1063 CA GLY A 186 7028 4988 3929 473 201 895 C ATOM 1064 C GLY A 186 8.466 -14.831 38.281 1.00 49.87 C ANISOU 1064 C GLY A 186 7752 6137 5058 448 284 823 C ATOM 1065 O GLY A 186 8.795 -13.755 38.793 1.00 57.28 O ANISOU 1065 O GLY A 186 8674 7134 5958 442 242 808 O ATOM 1066 N GLY A 187 7.814 -14.902 37.117 1.00 47.06 N ANISOU 1066 N GLY A 187 7196 5835 4850 433 389 778 N ATOM 1067 CA GLY A 187 7.493 -13.699 36.370 1.00 35.67 C ANISOU 1067 CA GLY A 187 5507 4518 3528 415 448 713 C ATOM 1068 C GLY A 187 8.752 -12.972 35.917 1.00 44.70 C ANISOU 1068 C GLY A 187 6492 5762 4729 522 281 710 C ATOM 1069 O GLY A 187 9.886 -13.362 36.205 1.00 43.37 O ANISOU 1069 O GLY A 187 6382 5573 4524 614 117 751 O ATOM 1070 N TRP A 188 8.528 -11.872 35.193 1.00 40.60 N ANISOU 1070 N TRP A 188 5768 5348 4311 506 323 657 N ATOM 1071 CA TRP A 188 9.631 -11.119 34.606 1.00 40.16 C ANISOU 1071 CA TRP A 188 5542 5391 4324 584 195 647 C ATOM 1072 C TRP A 188 10.575 -10.514 35.648 1.00 44.47 C ANISOU 1072 C TRP A 188 6169 5946 4783 608 63 671 C ATOM 1073 O TRP A 188 11.757 -10.292 35.347 1.00 42.35 O ANISOU 1073 O TRP A 188 5792 5731 4567 689 -78 677 O ATOM 1074 CB TRP A 188 9.061 -10.034 33.703 1.00 42.12 C ANISOU 1074 CB TRP A 188 5598 5728 4676 543 275 589 C ATOM 1075 CG TRP A 188 8.665 -10.544 32.352 1.00 39.13 C ANISOU 1075 CG TRP A 188 5096 5363 4409 559 324 566 C ATOM 1076 CD1 TRP A 188 7.389 -10.661 31.851 1.00 34.19 C ANISOU 1076 CD1 TRP A 188 4437 4714 3840 492 447 530 C ATOM 1077 CD2 TRP A 188 9.550 -11.011 31.319 1.00 34.58 C ANISOU 1077 CD2 TRP A 188 4417 4820 3901 647 248 571 C ATOM 1078 NE1 TRP A 188 7.437 -11.165 30.565 1.00 36.68 N ANISOU 1078 NE1 TRP A 188 4654 5042 4242 533 435 517 N ATOM 1079 CE2 TRP A 188 8.747 -11.384 30.216 1.00 38.47 C ANISOU 1079 CE2 TRP A 188 4843 5305 4471 627 327 541 C ATOM 1080 CE3 TRP A 188 10.943 -11.140 31.214 1.00 39.05 C ANISOU 1080 CE3 TRP A 188 4934 5420 4481 741 124 591 C ATOM 1081 CZ2 TRP A 188 9.295 -11.882 29.031 1.00 36.58 C ANISOU 1081 CZ2 TRP A 188 4518 5085 4296 694 296 532 C ATOM 1082 CZ3 TRP A 188 11.487 -11.645 30.040 1.00 31.86 C ANISOU 1082 CZ3 TRP A 188 3916 4535 3653 811 109 576 C ATOM 1083 CH2 TRP A 188 10.664 -11.998 28.961 1.00 40.13 C ANISOU 1083 CH2 TRP A 188 4925 5571 4752 785 199 548 C ATOM 1084 N ASP A 189 10.091 -10.256 36.867 1.00 46.20 N ANISOU 1084 N ASP A 189 6578 6107 4871 537 106 681 N ATOM 1085 CA ASP A 189 10.973 -9.786 37.932 1.00 51.92 C ANISOU 1085 CA ASP A 189 7421 6816 5489 557 -40 707 C ATOM 1086 C ASP A 189 12.081 -10.782 38.236 1.00 51.77 C ANISOU 1086 C ASP A 189 7495 6737 5439 658 -226 762 C ATOM 1087 O ASP A 189 13.185 -10.384 38.635 1.00 51.56 O ANISOU 1087 O ASP A 189 7454 6730 5405 716 -408 773 O ATOM 1088 CB ASP A 189 10.161 -9.510 39.194 1.00 58.96 C ANISOU 1088 CB ASP A 189 8547 7635 6222 456 61 706 C ATOM 1089 CG ASP A 189 9.237 -8.340 39.023 1.00 68.39 C ANISOU 1089 CG ASP A 189 9637 8889 7459 375 215 640 C ATOM 1090 OD1 ASP A 189 9.407 -7.590 38.029 1.00 71.58 O ANISOU 1090 OD1 ASP A 189 9806 9393 8000 401 200 604 O ATOM 1091 OD2 ASP A 189 8.330 -8.187 39.857 1.00 71.94 O ANISOU 1091 OD2 ASP A 189 10244 9281 7809 286 358 621 O ATOM 1092 N THR A 190 11.801 -12.077 38.085 1.00 45.59 N ANISOU 1092 N THR A 190 6809 5871 4644 680 -196 793 N ATOM 1093 CA THR A 190 12.835 -13.077 38.312 1.00 52.40 C ANISOU 1093 CA THR A 190 7756 6662 5491 791 -383 840 C ATOM 1094 C THR A 190 13.876 -13.029 37.206 1.00 55.27 C ANISOU 1094 C THR A 190 7850 7118 6031 906 -487 814 C ATOM 1095 O THR A 190 15.084 -13.103 37.474 1.00 51.76 O ANISOU 1095 O THR A 190 7379 6672 5617 1003 -684 827 O ATOM 1096 CB THR A 190 12.206 -14.465 38.401 1.00 57.13 C ANISOU 1096 CB THR A 190 8540 7137 6030 779 -314 878 C ATOM 1097 OG1 THR A 190 11.327 -14.504 39.526 1.00 60.18 O ANISOU 1097 OG1 THR A 190 9195 7430 6242 662 -210 902 O ATOM 1098 CG2 THR A 190 13.274 -15.539 38.540 1.00 44.52 C ANISOU 1098 CG2 THR A 190 7025 5455 4434 911 -519 922 C ATOM 1099 N PHE A 191 13.420 -12.886 35.957 1.00 47.85 N ANISOU 1099 N PHE A 191 6711 6258 5214 892 -354 772 N ATOM 1100 CA PHE A 191 14.337 -12.634 34.852 1.00 47.74 C ANISOU 1100 CA PHE A 191 6440 6341 5356 975 -410 736 C ATOM 1101 C PHE A 191 15.222 -11.423 35.137 1.00 44.29 C ANISOU 1101 C PHE A 191 5887 5990 4951 980 -518 719 C ATOM 1102 O PHE A 191 16.430 -11.457 34.875 1.00 41.97 O ANISOU 1102 O PHE A 191 5458 5734 4755 1073 -651 708 O ATOM 1103 CB PHE A 191 13.551 -12.444 33.544 1.00 39.62 C ANISOU 1103 CB PHE A 191 5258 5378 4419 931 -242 694 C ATOM 1104 CG PHE A 191 14.405 -11.995 32.388 1.00 40.63 C ANISOU 1104 CG PHE A 191 5143 5610 4684 989 -265 653 C ATOM 1105 CD1 PHE A 191 14.412 -10.672 31.986 1.00 36.45 C ANISOU 1105 CD1 PHE A 191 4472 5181 4198 932 -226 620 C ATOM 1106 CD2 PHE A 191 15.217 -12.897 31.716 1.00 41.79 C ANISOU 1106 CD2 PHE A 191 5215 5746 4917 1099 -318 646 C ATOM 1107 CE1 PHE A 191 15.190 -10.265 30.924 1.00 41.90 C ANISOU 1107 CE1 PHE A 191 4961 5958 5002 968 -229 585 C ATOM 1108 CE2 PHE A 191 16.010 -12.491 30.663 1.00 38.01 C ANISOU 1108 CE2 PHE A 191 4521 5361 4561 1142 -311 602 C ATOM 1109 CZ PHE A 191 15.996 -11.177 30.261 1.00 41.54 C ANISOU 1109 CZ PHE A 191 4839 5906 5038 1070 -262 574 C ATOM 1110 N VAL A 192 14.651 -10.351 35.702 1.00 40.19 N ANISOU 1110 N VAL A 192 5415 5496 4357 881 -464 710 N ATOM 1111 CA VAL A 192 15.478 -9.193 36.038 1.00 46.13 C ANISOU 1111 CA VAL A 192 6078 6318 5132 877 -576 694 C ATOM 1112 C VAL A 192 16.493 -9.550 37.120 1.00 51.54 C ANISOU 1112 C VAL A 192 6886 6937 5759 944 -794 729 C ATOM 1113 O VAL A 192 17.658 -9.137 37.050 1.00 55.35 O ANISOU 1113 O VAL A 192 7223 7472 6335 1001 -944 713 O ATOM 1114 CB VAL A 192 14.616 -7.994 36.462 1.00 46.40 C ANISOU 1114 CB VAL A 192 6161 6378 5092 762 -474 672 C ATOM 1115 CG1 VAL A 192 15.532 -6.854 36.962 1.00 40.06 C ANISOU 1115 CG1 VAL A 192 5302 5624 4293 754 -614 660 C ATOM 1116 CG2 VAL A 192 13.740 -7.515 35.300 1.00 40.41 C ANISOU 1116 CG2 VAL A 192 5250 5685 4418 709 -299 631 C ATOM 1117 N GLU A 193 16.071 -10.324 38.131 1.00 43.26 N ANISOU 1117 N GLU A 193 6112 5766 4560 936 -820 775 N ATOM 1118 CA GLU A 193 17.000 -10.761 39.173 1.00 50.95 C ANISOU 1118 CA GLU A 193 7241 6652 5464 1007 -1054 813 C ATOM 1119 C GLU A 193 18.169 -11.537 38.582 1.00 65.04 C ANISOU 1119 C GLU A 193 8866 8442 7404 1151 -1208 809 C ATOM 1120 O GLU A 193 19.304 -11.427 39.061 1.00 68.73 O ANISOU 1120 O GLU A 193 9300 8899 7915 1226 -1433 810 O ATOM 1121 CB GLU A 193 16.285 -11.631 40.215 1.00 52.03 C ANISOU 1121 CB GLU A 193 7727 6639 5403 971 -1036 869 C ATOM 1122 CG GLU A 193 15.646 -10.889 41.379 1.00 72.66 C ANISOU 1122 CG GLU A 193 10574 9208 7825 855 -988 878 C ATOM 1123 CD GLU A 193 14.450 -11.638 41.968 1.00 88.04 C ANISOU 1123 CD GLU A 193 12806 11038 9605 769 -821 911 C ATOM 1124 OE1 GLU A 193 13.354 -11.038 42.073 1.00 91.24 O ANISOU 1124 OE1 GLU A 193 13244 11467 9956 653 -608 882 O ATOM 1125 OE2 GLU A 193 14.602 -12.830 42.314 1.00 94.09 O ANISOU 1125 OE2 GLU A 193 13761 11686 10304 817 -899 963 O ATOM 1126 N LEU A 194 17.917 -12.333 37.543 1.00 61.16 N ANISOU 1126 N LEU A 194 8270 7962 7006 1194 -1096 797 N ATOM 1127 CA LEU A 194 18.970 -13.183 37.004 1.00 55.77 C ANISOU 1127 CA LEU A 194 7453 7268 6467 1340 -1223 785 C ATOM 1128 C LEU A 194 19.781 -12.509 35.912 1.00 56.33 C ANISOU 1128 C LEU A 194 7186 7479 6738 1375 -1204 721 C ATOM 1129 O LEU A 194 20.976 -12.789 35.785 1.00 66.55 O ANISOU 1129 O LEU A 194 8337 8782 8168 1489 -1359 698 O ATOM 1130 CB LEU A 194 18.376 -14.484 36.461 1.00 55.88 C ANISOU 1130 CB LEU A 194 7551 7206 6476 1377 -1122 801 C ATOM 1131 CG LEU A 194 17.761 -15.381 37.532 1.00 56.69 C ANISOU 1131 CG LEU A 194 8000 7147 6393 1355 -1159 868 C ATOM 1132 CD1 LEU A 194 16.741 -16.318 36.902 1.00 49.83 C ANISOU 1132 CD1 LEU A 194 7205 6226 5504 1322 -977 877 C ATOM 1133 CD2 LEU A 194 18.857 -16.160 38.215 1.00 57.24 C ANISOU 1133 CD2 LEU A 194 8170 7111 6469 1492 -1425 897 C ATOM 1134 N TYR A 195 19.177 -11.623 35.123 1.00 49.67 N ANISOU 1134 N TYR A 195 6214 6739 5921 1278 -1020 690 N ATOM 1135 CA TYR A 195 19.858 -11.067 33.966 1.00 52.68 C ANISOU 1135 CA TYR A 195 6303 7240 6473 1297 -969 632 C ATOM 1136 C TYR A 195 20.067 -9.567 34.047 1.00 65.85 C ANISOU 1136 C TYR A 195 7858 9003 8157 1205 -968 609 C ATOM 1137 O TYR A 195 20.760 -9.012 33.186 1.00 75.21 O ANISOU 1137 O TYR A 195 8809 10285 9482 1208 -937 564 O ATOM 1138 CB TYR A 195 19.089 -11.402 32.673 1.00 52.74 C ANISOU 1138 CB TYR A 195 6245 7279 6514 1273 -758 610 C ATOM 1139 CG TYR A 195 19.124 -12.875 32.315 1.00 56.89 C ANISOU 1139 CG TYR A 195 6826 7723 7066 1377 -760 616 C ATOM 1140 CD1 TYR A 195 18.382 -13.802 33.034 1.00 57.17 C ANISOU 1140 CD1 TYR A 195 7112 7636 6976 1377 -774 667 C ATOM 1141 CD2 TYR A 195 19.902 -13.339 31.257 1.00 58.19 C ANISOU 1141 CD2 TYR A 195 6803 7926 7381 1470 -736 567 C ATOM 1142 CE1 TYR A 195 18.415 -15.143 32.722 1.00 64.19 C ANISOU 1142 CE1 TYR A 195 8067 8437 7886 1468 -783 673 C ATOM 1143 CE2 TYR A 195 19.939 -14.683 30.935 1.00 64.04 C ANISOU 1143 CE2 TYR A 195 7604 8582 8146 1571 -740 567 C ATOM 1144 CZ TYR A 195 19.194 -15.583 31.668 1.00 68.49 C ANISOU 1144 CZ TYR A 195 8422 9020 8583 1571 -772 622 C ATOM 1145 OH TYR A 195 19.230 -16.931 31.357 1.00 69.77 O ANISOU 1145 OH TYR A 195 8658 9085 8766 1669 -783 623 O ATOM 1146 N GLY A 196 19.489 -8.891 35.033 1.00 64.52 N ANISOU 1146 N GLY A 196 7856 8807 7850 1120 -989 636 N ATOM 1147 CA GLY A 196 19.757 -7.480 35.192 1.00 62.14 C ANISOU 1147 CA GLY A 196 7464 8581 7563 1039 -1012 613 C ATOM 1148 C GLY A 196 21.194 -7.233 35.609 1.00 64.98 C ANISOU 1148 C GLY A 196 7701 8961 8026 1100 -1226 597 C ATOM 1149 O GLY A 196 21.819 -8.037 36.311 1.00 62.75 O ANISOU 1149 O GLY A 196 7496 8602 7743 1193 -1406 617 O ATOM 1150 N ASN A 197 21.729 -6.106 35.161 1.00 76.43 N ANISOU 1150 N ASN A 197 8958 10508 9574 1043 -1216 558 N ATOM 1151 CA ASN A 197 23.091 -5.751 35.514 1.00 90.99 C ANISOU 1151 CA ASN A 197 10653 12379 11542 1081 -1414 533 C ATOM 1152 C ASN A 197 23.078 -4.811 36.709 1.00 98.11 C ANISOU 1152 C ASN A 197 11698 13251 12330 1008 -1550 549 C ATOM 1153 O ASN A 197 22.928 -5.263 37.848 1.00102.09 O ANISOU 1153 O ASN A 197 12434 13654 12702 1037 -1686 587 O ATOM 1154 CB ASN A 197 23.817 -5.127 34.322 1.00 95.97 C ANISOU 1154 CB ASN A 197 10980 13125 12359 1056 -1325 477 C ATOM 1155 CG ASN A 197 24.294 -6.171 33.324 1.00 98.89 C ANISOU 1155 CG ASN A 197 11190 13512 12871 1160 -1256 447 C ATOM 1156 OD1 ASN A 197 24.626 -7.301 33.697 1.00101.02 O ANISOU 1156 OD1 ASN A 197 11508 13710 13163 1281 -1369 458 O ATOM 1157 ND2 ASN A 197 24.330 -5.798 32.048 1.00 96.03 N ANISOU 1157 ND2 ASN A 197 10654 13235 12597 1114 -1070 409 N TER 1158 ASN A 197 ATOM 1159 N PRO B -3 -4.522 -7.327 37.649 1.00 47.90 N ANISOU 1159 N PRO B -3 6115 6103 5981 -411 2172 -136 N ATOM 1160 CA PRO B -3 -5.758 -6.876 36.986 1.00 50.70 C ANISOU 1160 CA PRO B -3 6196 6465 6603 -427 2249 -255 C ATOM 1161 C PRO B -3 -5.916 -7.396 35.542 1.00 49.32 C ANISOU 1161 C PRO B -3 5837 6305 6598 -384 2095 -245 C ATOM 1162 O PRO B -3 -4.923 -7.547 34.814 1.00 42.58 O ANISOU 1162 O PRO B -3 5010 5492 5678 -299 1889 -161 O ATOM 1163 CB PRO B -3 -5.634 -5.343 37.008 1.00 40.59 C ANISOU 1163 CB PRO B -3 4825 5238 5358 -353 2189 -314 C ATOM 1164 CG PRO B -3 -4.136 -5.062 37.069 1.00 45.36 C ANISOU 1164 CG PRO B -3 5584 5890 5760 -272 1990 -206 C ATOM 1165 CD PRO B -3 -3.409 -6.391 37.405 1.00 46.50 C ANISOU 1165 CD PRO B -3 5944 5999 5726 -300 1966 -93 C ATOM 1166 N LEU B -2 -7.173 -7.668 35.169 1.00 51.55 N ANISOU 1166 N LEU B -2 5936 6551 7101 -447 2204 -336 N ATOM 1167 CA LEU B -2 -7.555 -8.261 33.885 1.00 49.86 C ANISOU 1167 CA LEU B -2 5557 6328 7059 -430 2082 -343 C ATOM 1168 C LEU B -2 -6.786 -7.667 32.715 1.00 52.17 C ANISOU 1168 C LEU B -2 5775 6683 7363 -303 1818 -304 C ATOM 1169 O LEU B -2 -6.885 -6.472 32.437 1.00 49.85 O ANISOU 1169 O LEU B -2 5363 6427 7150 -240 1747 -358 O ATOM 1170 CB LEU B -2 -9.057 -8.065 33.665 1.00 47.21 C ANISOU 1170 CB LEU B -2 4977 5958 7005 -491 2204 -482 C ATOM 1171 CG LEU B -2 -9.710 -8.768 32.475 1.00 47.58 C ANISOU 1171 CG LEU B -2 4852 5972 7254 -503 2103 -509 C ATOM 1172 CD1 LEU B -2 -9.404 -10.258 32.481 1.00 40.10 C ANISOU 1172 CD1 LEU B -2 4066 4975 6194 -571 2125 -421 C ATOM 1173 CD2 LEU B -2 -11.204 -8.549 32.500 1.00 41.76 C ANISOU 1173 CD2 LEU B -2 3870 5195 6804 -574 2244 -657 C ATOM 1174 N GLY B -1 -6.017 -8.511 32.033 1.00 53.69 N ANISOU 1174 N GLY B -1 6048 6879 7472 -267 1679 -213 N ATOM 1175 CA GLY B -1 -5.380 -8.127 30.799 1.00 52.89 C ANISOU 1175 CA GLY B -1 5879 6825 7391 -165 1454 -181 C ATOM 1176 C GLY B -1 -3.999 -7.519 30.920 1.00 56.97 C ANISOU 1176 C GLY B -1 6510 7408 7728 -82 1339 -103 C ATOM 1177 O GLY B -1 -3.382 -7.215 29.885 1.00 53.87 O ANISOU 1177 O GLY B -1 6075 7055 7339 -6 1168 -74 O ATOM 1178 N SER B 0 -3.481 -7.332 32.134 1.00 48.01 N ANISOU 1178 N SER B 0 5525 6282 6436 -99 1424 -71 N ATOM 1179 CA SER B 0 -2.215 -6.621 32.237 1.00 46.18 C ANISOU 1179 CA SER B 0 5371 6112 6064 -24 1299 -11 C ATOM 1180 C SER B 0 -1.018 -7.501 31.868 1.00 43.40 C ANISOU 1180 C SER B 0 5127 5774 5589 27 1180 90 C ATOM 1181 O SER B 0 -0.045 -6.988 31.308 1.00 46.62 O ANISOU 1181 O SER B 0 5515 6240 5957 100 1038 127 O ATOM 1182 CB SER B 0 -2.062 -6.022 33.635 1.00 44.78 C ANISOU 1182 CB SER B 0 5318 5933 5763 -55 1405 -19 C ATOM 1183 OG SER B 0 -2.007 -7.035 34.602 1.00 54.72 O ANISOU 1183 OG SER B 0 6762 7137 6894 -118 1518 24 O ATOM 1184 N MET B 1 -1.060 -8.809 32.145 1.00 38.64 N ANISOU 1184 N MET B 1 4634 5114 4933 -11 1237 131 N ATOM 1185 CA MET B 1 0.009 -9.692 31.671 1.00 50.52 C ANISOU 1185 CA MET B 1 6221 6622 6352 51 1117 213 C ATOM 1186 C MET B 1 0.165 -9.575 30.163 1.00 48.49 C ANISOU 1186 C MET B 1 5825 6402 6198 112 989 203 C ATOM 1187 O MET B 1 1.261 -9.314 29.654 1.00 49.73 O ANISOU 1187 O MET B 1 5981 6614 6302 189 867 244 O ATOM 1188 CB MET B 1 -0.265 -11.155 32.050 1.00 61.44 C ANISOU 1188 CB MET B 1 7736 7917 7690 -3 1195 248 C ATOM 1189 CG MET B 1 -0.068 -11.521 33.509 1.00 85.11 C ANISOU 1189 CG MET B 1 10948 10862 10527 -53 1289 289 C ATOM 1190 SD MET B 1 -1.238 -12.794 34.099 1.00107.22 S ANISOU 1190 SD MET B 1 13860 13541 13338 -189 1485 277 S ATOM 1191 CE MET B 1 -0.648 -14.309 33.337 1.00101.45 C ANISOU 1191 CE MET B 1 13211 12753 12583 -140 1370 350 C ATOM 1192 N SER B 2 -0.941 -9.752 29.435 1.00 49.13 N ANISOU 1192 N SER B 2 5789 6448 6428 72 1018 143 N ATOM 1193 CA SER B 2 -0.914 -9.678 27.978 1.00 41.77 C ANISOU 1193 CA SER B 2 4755 5534 5584 120 893 129 C ATOM 1194 C SER B 2 -0.374 -8.336 27.505 1.00 36.59 C ANISOU 1194 C SER B 2 4027 4949 4926 178 792 121 C ATOM 1195 O SER B 2 0.455 -8.269 26.587 1.00 28.62 O ANISOU 1195 O SER B 2 3019 3975 3882 238 682 153 O ATOM 1196 CB SER B 2 -2.321 -9.903 27.434 1.00 41.18 C ANISOU 1196 CB SER B 2 4562 5402 5685 61 927 52 C ATOM 1197 OG SER B 2 -2.774 -11.204 27.723 1.00 56.53 O ANISOU 1197 OG SER B 2 6572 7273 7633 -2 1013 62 O ATOM 1198 N GLN B 3 -0.842 -7.255 28.124 1.00 29.56 N ANISOU 1198 N GLN B 3 3083 4075 4073 156 840 74 N ATOM 1199 CA GLN B 3 -0.436 -5.921 27.713 1.00 41.25 C ANISOU 1199 CA GLN B 3 4505 5608 5559 201 746 62 C ATOM 1200 C GLN B 3 1.046 -5.703 27.958 1.00 39.76 C ANISOU 1200 C GLN B 3 4404 5480 5222 248 685 135 C ATOM 1201 O GLN B 3 1.751 -5.164 27.095 1.00 45.98 O ANISOU 1201 O GLN B 3 5163 6310 5997 291 581 154 O ATOM 1202 CB GLN B 3 -1.261 -4.876 28.457 1.00 32.36 C ANISOU 1202 CB GLN B 3 3317 4474 4504 171 820 -9 C ATOM 1203 CG GLN B 3 -0.751 -3.470 28.294 1.00 51.50 C ANISOU 1203 CG GLN B 3 5715 6944 6908 212 732 -15 C ATOM 1204 CD GLN B 3 -0.926 -2.933 26.883 1.00 68.83 C ANISOU 1204 CD GLN B 3 7824 9134 9194 247 595 -35 C ATOM 1205 OE1 GLN B 3 -1.673 -3.490 26.073 1.00 73.49 O ANISOU 1205 OE1 GLN B 3 8353 9681 9890 240 565 -64 O ATOM 1206 NE2 GLN B 3 -0.238 -1.832 26.585 1.00 71.40 N ANISOU 1206 NE2 GLN B 3 8159 9497 9474 279 504 -18 N ATOM 1207 N SER B 4 1.543 -6.138 29.116 1.00 37.79 N ANISOU 1207 N SER B 4 4267 5230 4861 237 746 175 N ATOM 1208 CA SER B 4 2.964 -5.977 29.420 1.00 39.30 C ANISOU 1208 CA SER B 4 4530 5473 4930 284 671 238 C ATOM 1209 C SER B 4 3.830 -6.704 28.411 1.00 36.65 C ANISOU 1209 C SER B 4 4187 5157 4582 340 586 282 C ATOM 1210 O SER B 4 4.863 -6.178 27.974 1.00 37.48 O ANISOU 1210 O SER B 4 4264 5319 4657 382 503 306 O ATOM 1211 CB SER B 4 3.273 -6.486 30.817 1.00 38.69 C ANISOU 1211 CB SER B 4 4596 5369 4734 264 730 274 C ATOM 1212 OG SER B 4 2.644 -5.665 31.767 1.00 48.11 O ANISOU 1212 OG SER B 4 5812 6551 5918 215 814 230 O ATOM 1213 N ASN B 5 3.429 -7.918 28.030 1.00 34.65 N ANISOU 1213 N ASN B 5 3959 4852 4355 336 615 288 N ATOM 1214 CA ASN B 5 4.229 -8.664 27.066 1.00 37.05 C ANISOU 1214 CA ASN B 5 4267 5164 4645 394 546 320 C ATOM 1215 C ASN B 5 4.263 -7.965 25.707 1.00 33.34 C ANISOU 1215 C ASN B 5 3705 4728 4234 411 481 294 C ATOM 1216 O ASN B 5 5.302 -7.955 25.041 1.00 39.90 O ANISOU 1216 O ASN B 5 4529 5601 5031 460 427 318 O ATOM 1217 CB ASN B 5 3.708 -10.093 26.966 1.00 41.33 C ANISOU 1217 CB ASN B 5 4873 5631 5202 381 590 327 C ATOM 1218 CG ASN B 5 4.202 -10.949 28.117 1.00 45.19 C ANISOU 1218 CG ASN B 5 5495 6083 5593 389 618 377 C ATOM 1219 OD1 ASN B 5 5.243 -10.647 28.707 1.00 40.22 O ANISOU 1219 OD1 ASN B 5 4903 5492 4885 433 567 414 O ATOM 1220 ND2 ASN B 5 3.464 -12.005 28.452 1.00 37.01 N ANISOU 1220 ND2 ASN B 5 4538 4964 4560 343 689 379 N ATOM 1221 N ARG B 6 3.150 -7.343 25.297 1.00 38.19 N ANISOU 1221 N ARG B 6 4252 5320 4939 370 485 240 N ATOM 1222 CA ARG B 6 3.129 -6.602 24.032 1.00 37.72 C ANISOU 1222 CA ARG B 6 4137 5274 4920 382 406 218 C ATOM 1223 C ARG B 6 4.075 -5.404 24.082 1.00 40.81 C ANISOU 1223 C ARG B 6 4513 5734 5259 398 363 237 C ATOM 1224 O ARG B 6 4.769 -5.102 23.100 1.00 43.84 O ANISOU 1224 O ARG B 6 4896 6145 5617 418 309 250 O ATOM 1225 CB ARG B 6 1.690 -6.173 23.703 1.00 36.51 C ANISOU 1225 CB ARG B 6 3914 5068 4889 342 396 153 C ATOM 1226 CG ARG B 6 0.762 -7.360 23.365 1.00 39.21 C ANISOU 1226 CG ARG B 6 4256 5338 5305 317 419 128 C ATOM 1227 CD ARG B 6 -0.590 -6.925 22.793 1.00 40.67 C ANISOU 1227 CD ARG B 6 4349 5467 5638 286 374 55 C ATOM 1228 NE ARG B 6 -1.432 -6.247 23.785 1.00 47.71 N ANISOU 1228 NE ARG B 6 5162 6352 6614 251 445 4 N ATOM 1229 CZ ARG B 6 -2.328 -6.865 24.560 1.00 54.16 C ANISOU 1229 CZ ARG B 6 5945 7127 7506 198 556 -32 C ATOM 1230 NH1 ARG B 6 -2.503 -8.182 24.458 1.00 58.05 N ANISOU 1230 NH1 ARG B 6 6482 7577 7999 170 594 -16 N ATOM 1231 NH2 ARG B 6 -3.056 -6.168 25.436 1.00 42.34 N ANISOU 1231 NH2 ARG B 6 4377 5626 6086 167 640 -88 N ATOM 1232 N GLU B 7 4.173 -4.757 25.244 1.00 49.58 N ANISOU 1232 N GLU B 7 5627 6869 6344 383 393 239 N ATOM 1233 CA GLU B 7 5.093 -3.635 25.394 1.00 44.18 C ANISOU 1233 CA GLU B 7 4932 6243 5611 389 347 256 C ATOM 1234 C GLU B 7 6.551 -4.082 25.357 1.00 39.78 C ANISOU 1234 C GLU B 7 4395 5737 4981 428 323 307 C ATOM 1235 O GLU B 7 7.412 -3.356 24.842 1.00 43.44 O ANISOU 1235 O GLU B 7 4830 6249 5427 431 279 319 O ATOM 1236 CB GLU B 7 4.781 -2.889 26.689 1.00 38.40 C ANISOU 1236 CB GLU B 7 4213 5512 4866 362 383 238 C ATOM 1237 CG GLU B 7 3.584 -1.983 26.559 1.00 48.35 C ANISOU 1237 CG GLU B 7 5420 6734 6215 336 390 174 C ATOM 1238 CD GLU B 7 2.929 -1.642 27.885 1.00 64.42 C ANISOU 1238 CD GLU B 7 7475 8749 8255 307 473 138 C ATOM 1239 OE1 GLU B 7 3.443 -2.064 28.948 1.00 68.76 O ANISOU 1239 OE1 GLU B 7 8104 9309 8712 301 519 170 O ATOM 1240 OE2 GLU B 7 1.882 -0.951 27.851 1.00 63.29 O ANISOU 1240 OE2 GLU B 7 7272 8569 8207 293 491 72 O ATOM 1241 N LEU B 8 6.854 -5.267 25.900 1.00 38.85 N ANISOU 1241 N LEU B 8 4326 5605 4829 456 350 335 N ATOM 1242 CA LEU B 8 8.215 -5.793 25.801 1.00 33.39 C ANISOU 1242 CA LEU B 8 3637 4952 4097 509 317 373 C ATOM 1243 C LEU B 8 8.600 -6.041 24.347 1.00 38.75 C ANISOU 1243 C LEU B 8 4279 5644 4800 533 308 366 C ATOM 1244 O LEU B 8 9.695 -5.668 23.908 1.00 36.88 O ANISOU 1244 O LEU B 8 3998 5461 4553 551 286 376 O ATOM 1245 CB LEU B 8 8.346 -7.085 26.604 1.00 38.93 C ANISOU 1245 CB LEU B 8 4416 5614 4763 543 333 401 C ATOM 1246 CG LEU B 8 8.116 -7.009 28.107 1.00 45.25 C ANISOU 1246 CG LEU B 8 5297 6389 5506 518 347 416 C ATOM 1247 CD1 LEU B 8 8.478 -8.351 28.745 1.00 44.69 C ANISOU 1247 CD1 LEU B 8 5329 6269 5385 559 340 454 C ATOM 1248 CD2 LEU B 8 8.923 -5.871 28.717 1.00 40.19 C ANISOU 1248 CD2 LEU B 8 4634 5805 4831 514 289 423 C ATOM 1249 N VAL B 9 7.713 -6.696 23.591 1.00 34.93 N ANISOU 1249 N VAL B 9 3820 5106 4348 527 329 346 N ATOM 1250 CA VAL B 9 7.954 -6.925 22.173 1.00 37.36 C ANISOU 1250 CA VAL B 9 4125 5410 4660 542 322 334 C ATOM 1251 C VAL B 9 8.231 -5.608 21.457 1.00 38.44 C ANISOU 1251 C VAL B 9 4230 5585 4791 508 295 324 C ATOM 1252 O VAL B 9 9.275 -5.429 20.815 1.00 33.74 O ANISOU 1252 O VAL B 9 3618 5032 4168 520 304 332 O ATOM 1253 CB VAL B 9 6.756 -7.649 21.541 1.00 39.06 C ANISOU 1253 CB VAL B 9 4380 5548 4914 526 326 307 C ATOM 1254 CG1 VAL B 9 6.921 -7.680 20.024 1.00 30.54 C ANISOU 1254 CG1 VAL B 9 3327 4455 3820 531 306 290 C ATOM 1255 CG2 VAL B 9 6.631 -9.044 22.107 1.00 34.48 C ANISOU 1255 CG2 VAL B 9 3849 4922 4330 554 360 321 C ATOM 1256 N VAL B 10 7.284 -4.669 21.549 1.00 36.28 N ANISOU 1256 N VAL B 10 3949 5289 4548 462 266 302 N ATOM 1257 CA VAL B 10 7.456 -3.369 20.908 1.00 31.58 C ANISOU 1257 CA VAL B 10 3346 4709 3941 426 226 296 C ATOM 1258 C VAL B 10 8.776 -2.730 21.331 1.00 36.53 C ANISOU 1258 C VAL B 10 3937 5411 4530 422 234 322 C ATOM 1259 O VAL B 10 9.556 -2.251 20.492 1.00 36.74 O ANISOU 1259 O VAL B 10 3965 5466 4528 403 238 329 O ATOM 1260 CB VAL B 10 6.253 -2.460 21.225 1.00 39.78 C ANISOU 1260 CB VAL B 10 4374 5707 5035 393 185 264 C ATOM 1261 CG1 VAL B 10 6.573 -1.025 20.888 1.00 33.62 C ANISOU 1261 CG1 VAL B 10 3598 4941 4236 359 137 265 C ATOM 1262 CG2 VAL B 10 5.016 -2.934 20.451 1.00 30.68 C ANISOU 1262 CG2 VAL B 10 3240 4476 3942 391 152 228 C ATOM 1263 N ASP B 11 9.071 -2.748 22.636 1.00 29.64 N ANISOU 1263 N ASP B 11 3039 4568 3656 435 239 336 N ATOM 1264 CA ASP B 11 10.288 -2.085 23.106 1.00 29.23 C ANISOU 1264 CA ASP B 11 2943 4580 3582 426 223 356 C ATOM 1265 C ASP B 11 11.540 -2.757 22.556 1.00 38.24 C ANISOU 1265 C ASP B 11 4044 5765 4719 462 249 369 C ATOM 1266 O ASP B 11 12.509 -2.079 22.178 1.00 41.74 O ANISOU 1266 O ASP B 11 4439 6257 5163 435 253 371 O ATOM 1267 CB ASP B 11 10.331 -2.059 24.633 1.00 26.64 C ANISOU 1267 CB ASP B 11 2621 4260 3240 435 205 367 C ATOM 1268 CG ASP B 11 11.611 -1.422 25.162 1.00 45.09 C ANISOU 1268 CG ASP B 11 4912 6658 5564 427 164 384 C ATOM 1269 OD1 ASP B 11 12.621 -2.137 25.301 1.00 44.49 O ANISOU 1269 OD1 ASP B 11 4797 6613 5494 472 154 400 O ATOM 1270 OD2 ASP B 11 11.614 -0.196 25.410 1.00 47.33 O ANISOU 1270 OD2 ASP B 11 5191 6952 5840 378 133 376 O ATOM 1271 N PHE B 12 11.552 -4.088 22.520 1.00 32.21 N ANISOU 1271 N PHE B 12 3297 4980 3961 521 274 372 N ATOM 1272 CA PHE B 12 12.759 -4.778 22.084 1.00 35.65 C ANISOU 1272 CA PHE B 12 3683 5451 4410 571 301 373 C ATOM 1273 C PHE B 12 12.999 -4.572 20.589 1.00 29.86 C ANISOU 1273 C PHE B 12 2955 4723 3667 545 357 353 C ATOM 1274 O PHE B 12 14.121 -4.269 20.170 1.00 28.12 O ANISOU 1274 O PHE B 12 2669 4555 3460 538 394 346 O ATOM 1275 CB PHE B 12 12.665 -6.257 22.427 1.00 27.60 C ANISOU 1275 CB PHE B 12 2699 4392 3397 647 306 380 C ATOM 1276 CG PHE B 12 13.930 -7.017 22.157 1.00 36.60 C ANISOU 1276 CG PHE B 12 3776 5560 4568 719 324 373 C ATOM 1277 CD1 PHE B 12 14.895 -7.147 23.135 1.00 41.89 C ANISOU 1277 CD1 PHE B 12 4385 6262 5268 766 268 387 C ATOM 1278 CD2 PHE B 12 14.160 -7.592 20.926 1.00 28.74 C ANISOU 1278 CD2 PHE B 12 2787 4554 3578 743 391 347 C ATOM 1279 CE1 PHE B 12 16.062 -7.835 22.892 1.00 42.90 C ANISOU 1279 CE1 PHE B 12 4434 6412 5453 844 275 370 C ATOM 1280 CE2 PHE B 12 15.317 -8.288 20.682 1.00 40.01 C ANISOU 1280 CE2 PHE B 12 4146 6007 5051 817 420 328 C ATOM 1281 CZ PHE B 12 16.267 -8.417 21.660 1.00 39.79 C ANISOU 1281 CZ PHE B 12 4033 6012 5075 871 361 337 C ATOM 1282 N LEU B 13 11.953 -4.717 19.774 1.00 29.74 N ANISOU 1282 N LEU B 13 3023 4649 3628 525 363 341 N ATOM 1283 CA LEU B 13 12.117 -4.517 18.340 1.00 41.87 C ANISOU 1283 CA LEU B 13 4608 6173 5129 494 407 323 C ATOM 1284 C LEU B 13 12.551 -3.089 18.039 1.00 39.86 C ANISOU 1284 C LEU B 13 4341 5952 4853 417 406 329 C ATOM 1285 O LEU B 13 13.451 -2.872 17.221 1.00 40.90 O ANISOU 1285 O LEU B 13 4466 6113 4962 390 475 320 O ATOM 1286 CB LEU B 13 10.819 -4.867 17.598 1.00 38.22 C ANISOU 1286 CB LEU B 13 4250 5627 4646 483 377 309 C ATOM 1287 CG LEU B 13 10.300 -6.292 17.791 1.00 32.36 C ANISOU 1287 CG LEU B 13 3534 4837 3925 543 380 301 C ATOM 1288 CD1 LEU B 13 9.057 -6.500 16.950 1.00 31.22 C ANISOU 1288 CD1 LEU B 13 3483 4608 3773 518 337 280 C ATOM 1289 CD2 LEU B 13 11.378 -7.308 17.419 1.00 33.39 C ANISOU 1289 CD2 LEU B 13 3652 4987 4047 606 450 293 C ATOM 1290 N SER B 14 11.943 -2.106 18.721 1.00 44.14 N ANISOU 1290 N SER B 14 4881 6486 5403 378 338 339 N ATOM 1291 CA SER B 14 12.292 -0.699 18.508 1.00 43.50 C ANISOU 1291 CA SER B 14 4803 6423 5301 301 324 346 C ATOM 1292 C SER B 14 13.738 -0.428 18.880 1.00 39.81 C ANISOU 1292 C SER B 14 4234 6037 4857 287 367 353 C ATOM 1293 O SER B 14 14.477 0.218 18.120 1.00 53.33 O ANISOU 1293 O SER B 14 5948 7770 6547 224 419 351 O ATOM 1294 CB SER B 14 11.366 0.207 19.310 1.00 42.36 C ANISOU 1294 CB SER B 14 4672 6250 5174 279 242 348 C ATOM 1295 OG SER B 14 10.027 -0.022 18.905 1.00 54.56 O ANISOU 1295 OG SER B 14 6286 7718 6726 291 200 330 O ATOM 1296 N TYR B 15 14.159 -0.919 20.042 1.00 30.96 N ANISOU 1296 N TYR B 15 3028 4955 3782 341 343 359 N ATOM 1297 CA TYR B 15 15.562 -0.811 20.427 1.00 39.47 C ANISOU 1297 CA TYR B 15 3988 6104 4906 341 362 358 C ATOM 1298 C TYR B 15 16.461 -1.400 19.352 1.00 49.60 C ANISOU 1298 C TYR B 15 5229 7412 6204 353 466 336 C ATOM 1299 O TYR B 15 17.493 -0.820 18.991 1.00 51.72 O ANISOU 1299 O TYR B 15 5422 7730 6500 299 522 324 O ATOM 1300 CB TYR B 15 15.779 -1.530 21.762 1.00 38.69 C ANISOU 1300 CB TYR B 15 3835 6019 4845 417 299 367 C ATOM 1301 CG TYR B 15 17.216 -1.657 22.192 1.00 42.58 C ANISOU 1301 CG TYR B 15 4194 6576 5408 442 288 360 C ATOM 1302 CD1 TYR B 15 17.920 -0.560 22.672 1.00 48.83 C ANISOU 1302 CD1 TYR B 15 4916 7411 6228 379 245 362 C ATOM 1303 CD2 TYR B 15 17.860 -2.878 22.162 1.00 40.29 C ANISOU 1303 CD2 TYR B 15 3844 6296 5169 534 308 346 C ATOM 1304 CE1 TYR B 15 19.231 -0.673 23.088 1.00 45.11 C ANISOU 1304 CE1 TYR B 15 4303 6993 5843 401 217 348 C ATOM 1305 CE2 TYR B 15 19.171 -3.006 22.583 1.00 47.29 C ANISOU 1305 CE2 TYR B 15 4587 7234 6146 569 279 330 C ATOM 1306 CZ TYR B 15 19.851 -1.897 23.038 1.00 48.60 C ANISOU 1306 CZ TYR B 15 4672 7446 6349 499 232 330 C ATOM 1307 OH TYR B 15 21.155 -2.017 23.438 1.00 50.74 O ANISOU 1307 OH TYR B 15 4781 7765 6731 532 190 307 O ATOM 1308 N LYS B 16 16.050 -2.532 18.799 1.00 39.40 N ANISOU 1308 N LYS B 16 3991 6083 4896 415 505 324 N ATOM 1309 CA LYS B 16 16.901 -3.273 17.891 1.00 46.27 C ANISOU 1309 CA LYS B 16 4826 6972 5784 446 613 293 C ATOM 1310 C LYS B 16 16.960 -2.632 16.509 1.00 41.76 C ANISOU 1310 C LYS B 16 4338 6385 5145 357 707 279 C ATOM 1311 O LYS B 16 18.022 -2.646 15.880 1.00 44.16 O ANISOU 1311 O LYS B 16 4578 6729 5470 336 821 250 O ATOM 1312 CB LYS B 16 16.403 -4.716 17.822 1.00 50.80 C ANISOU 1312 CB LYS B 16 5450 7497 6354 543 613 284 C ATOM 1313 CG LYS B 16 17.438 -5.701 17.395 1.00 58.01 C ANISOU 1313 CG LYS B 16 6289 8432 7320 616 700 246 C ATOM 1314 CD LYS B 16 18.730 -5.478 18.135 1.00 61.85 C ANISOU 1314 CD LYS B 16 6598 8994 7910 640 691 235 C ATOM 1315 CE LYS B 16 18.680 -5.973 19.563 1.00 52.16 C ANISOU 1315 CE LYS B 16 5330 7761 6729 717 561 261 C ATOM 1316 NZ LYS B 16 20.096 -6.155 19.998 1.00 53.02 N ANISOU 1316 NZ LYS B 16 5261 7926 6957 773 552 232 N ATOM 1317 N LEU B 17 15.855 -2.052 16.026 1.00 44.29 N ANISOU 1317 N LEU B 17 4803 6642 5384 302 661 297 N ATOM 1318 CA LEU B 17 15.890 -1.391 14.720 1.00 49.73 C ANISOU 1318 CA LEU B 17 5610 7297 5986 212 730 291 C ATOM 1319 C LEU B 17 16.691 -0.104 14.788 1.00 58.73 C ANISOU 1319 C LEU B 17 6699 8482 7133 112 760 301 C ATOM 1320 O LEU B 17 17.545 0.155 13.932 1.00 63.59 O ANISOU 1320 O LEU B 17 7323 9115 7722 45 886 284 O ATOM 1321 CB LEU B 17 14.483 -1.093 14.220 1.00 43.51 C ANISOU 1321 CB LEU B 17 4992 6416 5122 189 637 306 C ATOM 1322 CG LEU B 17 13.650 -2.306 13.832 1.00 47.36 C ANISOU 1322 CG LEU B 17 5558 6844 5593 261 615 290 C ATOM 1323 CD1 LEU B 17 12.170 -1.997 13.988 1.00 44.73 C ANISOU 1323 CD1 LEU B 17 5306 6435 5253 258 478 301 C ATOM 1324 CD2 LEU B 17 13.980 -2.727 12.401 1.00 46.16 C ANISOU 1324 CD2 LEU B 17 5532 6654 5351 239 718 265 C ATOM 1325 N SER B 18 16.440 0.711 15.813 1.00 60.97 N ANISOU 1325 N SER B 18 6935 8780 7452 93 655 326 N ATOM 1326 CA SER B 18 17.172 1.962 15.915 1.00 57.48 C ANISOU 1326 CA SER B 18 6451 8369 7018 -10 670 335 C ATOM 1327 C SER B 18 18.636 1.697 16.222 1.00 55.96 C ANISOU 1327 C SER B 18 6073 8267 6922 -7 758 310 C ATOM 1328 O SER B 18 19.512 2.444 15.768 1.00 65.11 O ANISOU 1328 O SER B 18 7197 9454 8088 -107 845 302 O ATOM 1329 CB SER B 18 16.524 2.863 16.966 1.00 50.19 C ANISOU 1329 CB SER B 18 5531 7430 6107 -23 533 360 C ATOM 1330 OG SER B 18 16.937 2.485 18.257 1.00 57.64 O ANISOU 1330 OG SER B 18 6333 8431 7135 40 483 358 O ATOM 1331 N GLN B 19 18.921 0.617 16.954 1.00 49.65 N ANISOU 1331 N GLN B 19 5156 7506 6204 105 735 295 N ATOM 1332 CA GLN B 19 20.299 0.166 17.115 1.00 46.88 C ANISOU 1332 CA GLN B 19 4619 7229 5965 133 810 259 C ATOM 1333 C GLN B 19 20.972 -0.050 15.761 1.00 63.70 C ANISOU 1333 C GLN B 19 6758 9366 8078 88 996 219 C ATOM 1334 O GLN B 19 22.114 0.369 15.550 1.00 69.44 O ANISOU 1334 O GLN B 19 7358 10149 8879 23 1097 189 O ATOM 1335 CB GLN B 19 20.320 -1.116 17.938 1.00 54.23 C ANISOU 1335 CB GLN B 19 5472 8169 6965 277 745 250 C ATOM 1336 CG GLN B 19 21.611 -1.399 18.639 1.00 61.26 C ANISOU 1336 CG GLN B 19 6152 9127 7997 324 731 221 C ATOM 1337 CD GLN B 19 21.523 -2.648 19.481 1.00 61.39 C ANISOU 1337 CD GLN B 19 6135 9129 8062 469 640 221 C ATOM 1338 OE1 GLN B 19 21.161 -3.708 18.990 1.00 58.22 O ANISOU 1338 OE1 GLN B 19 5797 8690 7635 545 687 209 O ATOM 1339 NE2 GLN B 19 21.840 -2.526 20.761 1.00 63.28 N ANISOU 1339 NE2 GLN B 19 6296 9386 8361 503 500 237 N ATOM 1340 N LYS B 20 20.278 -0.686 14.822 1.00 70.21 N ANISOU 1340 N LYS B 20 7738 10132 8808 114 1051 214 N ATOM 1341 CA LYS B 20 20.862 -0.929 13.511 1.00 71.11 C ANISOU 1341 CA LYS B 20 7897 10240 8880 70 1239 173 C ATOM 1342 C LYS B 20 20.703 0.255 12.570 1.00 80.68 C ANISOU 1342 C LYS B 20 9272 11411 9971 -84 1303 193 C ATOM 1343 O LYS B 20 21.011 0.125 11.383 1.00 89.49 O ANISOU 1343 O LYS B 20 10489 12502 11011 -138 1462 164 O ATOM 1344 CB LYS B 20 20.257 -2.188 12.881 1.00 62.42 C ANISOU 1344 CB LYS B 20 6912 9083 7721 165 1267 153 C ATOM 1345 N GLY B 21 20.222 1.397 13.060 1.00 74.46 N ANISOU 1345 N GLY B 21 8532 10605 9156 -155 1183 239 N ATOM 1346 CA GLY B 21 20.157 2.611 12.272 1.00 72.19 C ANISOU 1346 CA GLY B 21 8400 10270 8761 -304 1226 263 C ATOM 1347 C GLY B 21 18.818 2.925 11.630 1.00 75.32 C ANISOU 1347 C GLY B 21 9055 10554 9009 -322 1127 299 C ATOM 1348 O GLY B 21 18.658 4.026 11.097 1.00 82.59 O ANISOU 1348 O GLY B 21 10125 11418 9837 -439 1120 327 O ATOM 1349 N TYR B 22 17.849 2.018 11.673 1.00 72.24 N ANISOU 1349 N TYR B 22 8724 10123 8601 -213 1040 298 N ATOM 1350 CA TYR B 22 16.633 2.186 10.884 1.00 72.89 C ANISOU 1350 CA TYR B 22 9045 10092 8557 -227 950 319 C ATOM 1351 C TYR B 22 15.639 3.086 11.615 1.00 80.98 C ANISOU 1351 C TYR B 22 10098 11074 9596 -229 761 355 C ATOM 1352 O TYR B 22 15.160 2.744 12.701 1.00 76.45 O ANISOU 1352 O TYR B 22 9406 10529 9114 -142 663 356 O ATOM 1353 CB TYR B 22 16.016 0.823 10.562 1.00 62.15 C ANISOU 1353 CB TYR B 22 7731 8700 7184 -119 938 295 C ATOM 1354 CG TYR B 22 16.964 -0.089 9.800 1.00 74.97 C ANISOU 1354 CG TYR B 22 9340 10354 8791 -106 1129 250 C ATOM 1355 CD1 TYR B 22 17.648 -1.111 10.449 1.00 81.08 C ANISOU 1355 CD1 TYR B 22 9914 11205 9686 -6 1190 216 C ATOM 1356 CD2 TYR B 22 17.197 0.089 8.436 1.00 75.00 C ANISOU 1356 CD2 TYR B 22 9542 10300 8655 -193 1252 237 C ATOM 1357 CE1 TYR B 22 18.526 -1.947 9.759 1.00 85.60 C ANISOU 1357 CE1 TYR B 22 10461 11802 10262 18 1369 163 C ATOM 1358 CE2 TYR B 22 18.072 -0.742 7.737 1.00 80.50 C ANISOU 1358 CE2 TYR B 22 10227 11021 9337 -181 1450 183 C ATOM 1359 CZ TYR B 22 18.735 -1.757 8.405 1.00 86.30 C ANISOU 1359 CZ TYR B 22 10737 11838 10214 -70 1509 143 C ATOM 1360 OH TYR B 22 19.606 -2.587 7.727 1.00 86.37 O ANISOU 1360 OH TYR B 22 10721 11868 10228 -45 1708 79 O ATOM 1361 N SER B 23 15.335 4.240 11.023 1.00 89.78 N ANISOU 1361 N SER B 23 11381 12113 10618 -328 715 382 N ATOM 1362 CA SER B 23 14.269 5.111 11.512 1.00 91.93 C ANISOU 1362 CA SER B 23 11711 12319 10899 -323 531 406 C ATOM 1363 C SER B 23 13.012 4.782 10.723 1.00 97.20 C ANISOU 1363 C SER B 23 12562 12873 11496 -282 419 404 C ATOM 1364 O SER B 23 12.958 5.011 9.511 1.00100.15 O ANISOU 1364 O SER B 23 13146 13164 11741 -348 436 413 O ATOM 1365 CB SER B 23 14.642 6.585 11.363 1.00 88.18 C ANISOU 1365 CB SER B 23 11319 11811 10375 -447 521 435 C ATOM 1366 N TRP B 24 12.006 4.234 11.404 1.00 99.90 N ANISOU 1366 N TRP B 24 12830 13206 11922 -179 303 391 N ATOM 1367 CA TRP B 24 10.773 3.811 10.749 1.00100.29 C ANISOU 1367 CA TRP B 24 13013 13151 11940 -133 182 379 C ATOM 1368 C TRP B 24 9.653 4.845 10.831 1.00101.84 C ANISOU 1368 C TRP B 24 13291 13249 12154 -136 -6 385 C ATOM 1369 O TRP B 24 8.914 5.016 9.860 1.00107.15 O ANISOU 1369 O TRP B 24 14150 13806 12757 -148 -114 385 O ATOM 1370 CB TRP B 24 10.301 2.467 11.330 1.00 97.38 C ANISOU 1370 CB TRP B 24 12517 12820 11663 -26 180 351 C ATOM 1371 CG TRP B 24 10.069 2.453 12.825 1.00 96.63 C ANISOU 1371 CG TRP B 24 12227 12790 11697 32 147 347 C ATOM 1372 CD1 TRP B 24 8.860 2.467 13.471 1.00 96.02 C ANISOU 1372 CD1 TRP B 24 12106 12673 11706 85 27 330 C ATOM 1373 CD2 TRP B 24 11.069 2.412 13.853 1.00 95.03 C ANISOU 1373 CD2 TRP B 24 11859 12697 11550 38 237 354 C ATOM 1374 NE1 TRP B 24 9.050 2.443 14.835 1.00 93.27 N ANISOU 1374 NE1 TRP B 24 11597 12400 11441 118 53 329 N ATOM 1375 CE2 TRP B 24 10.395 2.408 15.096 1.00 90.66 C ANISOU 1375 CE2 TRP B 24 11198 12159 11090 92 165 346 C ATOM 1376 CE3 TRP B 24 12.465 2.379 13.847 1.00 93.42 C ANISOU 1376 CE3 TRP B 24 11585 12575 11333 2 367 360 C ATOM 1377 CZ2 TRP B 24 11.075 2.378 16.314 1.00 81.29 C ANISOU 1377 CZ2 TRP B 24 9868 11059 9961 111 204 352 C ATOM 1378 CZ3 TRP B 24 13.136 2.346 15.063 1.00 87.81 C ANISOU 1378 CZ3 TRP B 24 10704 11953 10705 27 391 362 C ATOM 1379 CH2 TRP B 24 12.440 2.346 16.275 1.00 77.06 C ANISOU 1379 CH2 TRP B 24 9269 10598 9414 81 302 362 C ATOM 1380 N SER B 25 9.501 5.541 11.957 1.00100.79 N ANISOU 1380 N SER B 25 13032 13150 12115 -122 -55 386 N ATOM 1381 CA SER B 25 8.494 6.582 12.102 1.00 93.42 C ANISOU 1381 CA SER B 25 12158 12122 11215 -115 -224 382 C ATOM 1382 C SER B 25 9.109 7.946 11.792 1.00 92.91 C ANISOU 1382 C SER B 25 12210 12021 11069 -217 -229 416 C ATOM 1383 O SER B 25 10.317 8.074 11.566 1.00 87.48 O ANISOU 1383 O SER B 25 11532 11394 10314 -299 -89 439 O ATOM 1384 CB SER B 25 7.904 6.575 13.514 1.00 88.82 C ANISOU 1384 CB SER B 25 11389 11585 10775 -42 -266 354 C ATOM 1385 OG SER B 25 7.668 5.259 13.986 1.00 86.29 O ANISOU 1385 OG SER B 25 10945 11321 10521 30 -212 332 O ATOM 1386 N GLN B 26 8.273 8.991 11.789 1.00 93.12 N ANISOU 1386 N GLN B 26 12324 11943 11114 -214 -391 413 N ATOM 1387 CA GLN B 26 8.821 10.342 11.731 1.00 89.60 C ANISOU 1387 CA GLN B 26 11975 11459 10608 -307 -405 444 C ATOM 1388 C GLN B 26 9.423 10.729 13.072 1.00 91.39 C ANISOU 1388 C GLN B 26 12015 11790 10919 -312 -339 439 C ATOM 1389 O GLN B 26 10.586 11.147 13.147 1.00 86.12 O ANISOU 1389 O GLN B 26 11336 11181 10207 -405 -230 466 O ATOM 1390 CB GLN B 26 7.756 11.360 11.330 1.00 91.11 C ANISOU 1390 CB GLN B 26 12328 11493 10797 -293 -614 440 C ATOM 1391 CG GLN B 26 8.355 12.755 11.123 1.00 98.40 C ANISOU 1391 CG GLN B 26 13397 12355 11634 -402 -631 480 C ATOM 1392 CD GLN B 26 7.375 13.895 11.362 1.00104.19 C ANISOU 1392 CD GLN B 26 14202 12960 12427 -359 -836 463 C ATOM 1393 OE1 GLN B 26 7.527 14.661 12.316 1.00102.17 O ANISOU 1393 OE1 GLN B 26 13855 12727 12236 -362 -841 453 O ATOM 1394 NE2 GLN B 26 6.384 14.033 10.479 1.00106.61 N ANISOU 1394 NE2 GLN B 26 14679 13119 12710 -319 -1017 456 N ATOM 1395 N MET B 83 8.643 10.589 14.149 1.00 91.80 N ANISOU 1395 N MET B 83 11922 11862 11096 -217 -403 402 N ATOM 1396 CA MET B 83 9.163 10.928 15.463 1.00 86.80 C ANISOU 1396 CA MET B 83 11138 11316 10527 -218 -353 394 C ATOM 1397 C MET B 83 10.307 10.014 15.856 1.00 77.00 C ANISOU 1397 C MET B 83 9760 10210 9285 -233 -196 406 C ATOM 1398 O MET B 83 11.158 10.423 16.654 1.00 72.91 O ANISOU 1398 O MET B 83 9155 9763 8787 -273 -148 413 O ATOM 1399 CB MET B 83 8.053 10.894 16.522 1.00 86.33 C ANISOU 1399 CB MET B 83 10971 11243 10588 -117 -432 345 C ATOM 1400 CG MET B 83 7.136 12.122 16.484 1.00 93.47 C ANISOU 1400 CG MET B 83 11968 12022 11525 -102 -585 322 C ATOM 1401 SD MET B 83 7.990 13.727 16.492 1.00 99.49 S ANISOU 1401 SD MET B 83 12848 12741 12212 -214 -612 357 S ATOM 1402 CE MET B 83 6.766 14.823 15.768 1.00101.35 C ANISOU 1402 CE MET B 83 13264 12784 12461 -181 -822 338 C ATOM 1403 N ALA B 84 10.372 8.807 15.289 1.00 64.85 N ANISOU 1403 N ALA B 84 8208 8704 7729 -200 -127 405 N ATOM 1404 CA ALA B 84 11.521 7.950 15.564 1.00 65.50 C ANISOU 1404 CA ALA B 84 8165 8903 7818 -206 16 411 C ATOM 1405 C ALA B 84 12.821 8.625 15.131 1.00 66.82 C ANISOU 1405 C ALA B 84 8359 9103 7928 -323 109 436 C ATOM 1406 O ALA B 84 13.828 8.573 15.847 1.00 71.92 O ANISOU 1406 O ALA B 84 8864 9843 8621 -344 181 436 O ATOM 1407 CB ALA B 84 11.351 6.598 14.878 1.00 62.45 C ANISOU 1407 CB ALA B 84 7788 8524 7414 -153 72 401 C ATOM 1408 N ALA B 85 12.807 9.280 13.969 1.00 56.93 N ANISOU 1408 N ALA B 85 7292 7764 6574 -407 103 457 N ATOM 1409 CA ALA B 85 13.967 10.042 13.522 1.00 51.00 C ANISOU 1409 CA ALA B 85 6586 7029 5764 -541 202 480 C ATOM 1410 C ALA B 85 14.291 11.174 14.490 1.00 49.48 C ANISOU 1410 C ALA B 85 6330 6849 5622 -591 148 487 C ATOM 1411 O ALA B 85 15.459 11.408 14.810 1.00 53.16 O ANISOU 1411 O ALA B 85 6690 7392 6116 -667 243 490 O ATOM 1412 CB ALA B 85 13.715 10.600 12.115 1.00 35.69 C ANISOU 1412 CB ALA B 85 4908 4968 3686 -626 189 506 C ATOM 1413 N VAL B 86 13.263 11.897 14.948 1.00 50.47 N ANISOU 1413 N VAL B 86 6516 6894 5766 -548 -7 483 N ATOM 1414 CA VAL B 86 13.458 13.009 15.875 1.00 51.06 C ANISOU 1414 CA VAL B 86 6557 6964 5881 -588 -70 483 C ATOM 1415 C VAL B 86 14.034 12.510 17.192 1.00 46.82 C ANISOU 1415 C VAL B 86 5802 6548 5438 -543 -31 463 C ATOM 1416 O VAL B 86 14.994 13.080 17.729 1.00 41.51 O ANISOU 1416 O VAL B 86 5058 5924 4790 -619 -2 468 O ATOM 1417 CB VAL B 86 12.134 13.752 16.107 1.00 48.11 C ANISOU 1417 CB VAL B 86 6284 6475 5523 -527 -239 468 C ATOM 1418 CG1 VAL B 86 12.323 14.830 17.168 1.00 44.00 C ANISOU 1418 CG1 VAL B 86 5726 5948 5044 -556 -298 459 C ATOM 1419 CG2 VAL B 86 11.639 14.341 14.821 1.00 42.03 C ANISOU 1419 CG2 VAL B 86 5746 5567 4656 -574 -310 492 C ATOM 1420 N LYS B 87 13.440 11.448 17.737 1.00 35.77 N ANISOU 1420 N LYS B 87 4308 5190 4094 -422 -40 439 N ATOM 1421 CA LYS B 87 13.930 10.895 18.986 1.00 38.04 C ANISOU 1421 CA LYS B 87 4422 5576 4455 -372 -17 424 C ATOM 1422 C LYS B 87 15.382 10.476 18.850 1.00 49.97 C ANISOU 1422 C LYS B 87 5821 7183 5983 -430 96 433 C ATOM 1423 O LYS B 87 16.208 10.775 19.726 1.00 50.00 O ANISOU 1423 O LYS B 87 5716 7245 6036 -460 89 429 O ATOM 1424 CB LYS B 87 13.069 9.709 19.414 1.00 37.91 C ANISOU 1424 CB LYS B 87 4351 5575 4478 -247 -26 402 C ATOM 1425 CG LYS B 87 11.603 10.062 19.738 1.00 38.47 C ANISOU 1425 CG LYS B 87 4487 5561 4571 -183 -128 376 C ATOM 1426 CD LYS B 87 10.824 8.786 20.108 1.00 55.03 C ANISOU 1426 CD LYS B 87 6519 7676 6713 -79 -110 354 C ATOM 1427 CE LYS B 87 9.304 9.008 20.218 1.00 67.12 C ANISOU 1427 CE LYS B 87 8094 9119 8289 -18 -192 316 C ATOM 1428 NZ LYS B 87 8.590 8.703 18.945 1.00 80.57 N ANISOU 1428 NZ LYS B 87 9883 10751 9981 -5 -229 315 N ATOM 1429 N GLN B 88 15.716 9.808 17.740 1.00 44.80 N ANISOU 1429 N GLN B 88 5190 6539 5293 -446 198 439 N ATOM 1430 CA GLN B 88 17.084 9.348 17.551 1.00 47.96 C ANISOU 1430 CA GLN B 88 5463 7030 5730 -492 324 434 C ATOM 1431 C GLN B 88 18.038 10.534 17.469 1.00 48.52 C ANISOU 1431 C GLN B 88 5529 7105 5802 -636 354 444 C ATOM 1432 O GLN B 88 19.108 10.524 18.088 1.00 46.53 O ANISOU 1432 O GLN B 88 5113 6933 5634 -666 385 431 O ATOM 1433 CB GLN B 88 17.172 8.467 16.297 1.00 40.56 C ANISOU 1433 CB GLN B 88 4579 6088 4743 -484 443 430 C ATOM 1434 N ALA B 89 17.641 11.585 16.752 1.00 46.24 N ANISOU 1434 N ALA B 89 5423 6720 5425 -727 328 467 N ATOM 1435 CA ALA B 89 18.480 12.770 16.636 1.00 45.95 C ANISOU 1435 CA ALA B 89 5409 6669 5380 -880 356 481 C ATOM 1436 C ALA B 89 18.626 13.480 17.976 1.00 50.94 C ANISOU 1436 C ALA B 89 5952 7320 6082 -881 242 473 C ATOM 1437 O ALA B 89 19.680 14.061 18.266 1.00 50.71 O ANISOU 1437 O ALA B 89 5835 7331 6103 -987 273 470 O ATOM 1438 CB ALA B 89 17.890 13.713 15.589 1.00 42.37 C ANISOU 1438 CB ALA B 89 5211 6085 4802 -966 331 512 C ATOM 1439 N LEU B 90 17.589 13.430 18.804 1.00 45.05 N ANISOU 1439 N LEU B 90 5230 6543 5344 -769 114 465 N ATOM 1440 CA LEU B 90 17.624 14.093 20.095 1.00 46.14 C ANISOU 1440 CA LEU B 90 5318 6686 5529 -764 7 452 C ATOM 1441 C LEU B 90 18.515 13.344 21.069 1.00 49.98 C ANISOU 1441 C LEU B 90 5600 7285 6106 -724 20 433 C ATOM 1442 O LEU B 90 19.328 13.964 21.774 1.00 51.63 O ANISOU 1442 O LEU B 90 5734 7521 6362 -793 -21 426 O ATOM 1443 CB LEU B 90 16.205 14.228 20.647 1.00 46.38 C ANISOU 1443 CB LEU B 90 5439 6644 5539 -656 -108 438 C ATOM 1444 CG LEU B 90 16.050 15.437 21.557 1.00 56.01 C ANISOU 1444 CG LEU B 90 6709 7811 6763 -690 -216 426 C ATOM 1445 CD1 LEU B 90 16.887 16.570 21.030 1.00 51.46 C ANISOU 1445 CD1 LEU B 90 6196 7198 6160 -848 -203 449 C ATOM 1446 CD2 LEU B 90 14.602 15.841 21.598 1.00 61.15 C ANISOU 1446 CD2 LEU B 90 7488 8357 7389 -611 -305 409 C ATOM 1447 N ARG B 91 18.388 12.012 21.104 1.00 45.67 N ANISOU 1447 N ARG B 91 4971 6795 5587 -613 63 423 N ATOM 1448 CA ARG B 91 19.244 11.198 21.968 1.00 46.25 C ANISOU 1448 CA ARG B 91 4862 6962 5747 -562 61 406 C ATOM 1449 C ARG B 91 20.715 11.416 21.654 1.00 49.62 C ANISOU 1449 C ARG B 91 5152 7452 6248 -668 135 398 C ATOM 1450 O ARG B 91 21.535 11.563 22.569 1.00 56.37 O ANISOU 1450 O ARG B 91 5880 8355 7183 -684 70 383 O ATOM 1451 CB ARG B 91 18.901 9.718 21.825 1.00 47.12 C ANISOU 1451 CB ARG B 91 4929 7108 5869 -436 109 400 C ATOM 1452 CG ARG B 91 17.512 9.368 22.264 1.00 43.74 C ANISOU 1452 CG ARG B 91 4599 6626 5393 -334 45 401 C ATOM 1453 CD ARG B 91 17.108 8.027 21.727 1.00 47.52 C ANISOU 1453 CD ARG B 91 5069 7118 5870 -242 110 399 C ATOM 1454 NE ARG B 91 16.397 7.260 22.734 1.00 66.26 N ANISOU 1454 NE ARG B 91 7438 9489 8251 -135 55 392 N ATOM 1455 CZ ARG B 91 15.405 6.423 22.473 1.00 81.71 C ANISOU 1455 CZ ARG B 91 9446 11412 10187 -59 73 389 C ATOM 1456 NH1 ARG B 91 14.995 6.257 21.220 1.00 83.86 N ANISOU 1456 NH1 ARG B 91 9786 11650 10429 -71 127 391 N ATOM 1457 NH2 ARG B 91 14.816 5.768 23.470 1.00 89.13 N ANISOU 1457 NH2 ARG B 91 10384 12347 11133 21 36 382 N ATOM 1458 N GLU B 92 21.072 11.437 20.366 1.00 49.58 N ANISOU 1458 N GLU B 92 5173 7444 6221 -746 271 403 N ATOM 1459 CA GLU B 92 22.474 11.613 20.000 1.00 54.47 C ANISOU 1459 CA GLU B 92 5646 8125 6926 -857 375 384 C ATOM 1460 C GLU B 92 22.943 13.041 20.249 1.00 58.20 C ANISOU 1460 C GLU B 92 6143 8564 7405 -1008 329 392 C ATOM 1461 O GLU B 92 24.088 13.258 20.669 1.00 59.03 O ANISOU 1461 O GLU B 92 6076 8728 7625 -1079 333 368 O ATOM 1462 CB GLU B 92 22.689 11.222 18.543 1.00 61.40 C ANISOU 1462 CB GLU B 92 6569 9000 7762 -906 560 382 C ATOM 1463 CG GLU B 92 22.163 9.833 18.250 1.00 81.26 C ANISOU 1463 CG GLU B 92 9081 11532 10260 -759 599 373 C ATOM 1464 CD GLU B 92 22.414 9.399 16.828 1.00 92.02 C ANISOU 1464 CD GLU B 92 10502 12889 11572 -804 784 363 C ATOM 1465 OE1 GLU B 92 23.217 8.457 16.637 1.00 95.65 O ANISOU 1465 OE1 GLU B 92 10802 13421 12120 -761 895 325 O ATOM 1466 OE2 GLU B 92 21.813 10.002 15.907 1.00 91.91 O ANISOU 1466 OE2 GLU B 92 10702 12790 11429 -879 814 391 O ATOM 1467 N ALA B 93 22.081 14.031 19.992 1.00 51.04 N ANISOU 1467 N ALA B 93 5449 7557 6389 -1060 274 421 N ATOM 1468 CA ALA B 93 22.469 15.409 20.276 1.00 45.68 C ANISOU 1468 CA ALA B 93 4816 6832 5710 -1201 216 429 C ATOM 1469 C ALA B 93 22.653 15.620 21.776 1.00 45.33 C ANISOU 1469 C ALA B 93 4674 6815 5736 -1157 60 410 C ATOM 1470 O ALA B 93 23.591 16.309 22.207 1.00 41.80 O ANISOU 1470 O ALA B 93 4136 6386 5361 -1268 28 397 O ATOM 1471 CB ALA B 93 21.434 16.374 19.715 1.00 42.12 C ANISOU 1471 CB ALA B 93 4626 6252 5128 -1243 170 463 C ATOM 1472 N GLY B 94 21.781 15.007 22.584 1.00 42.29 N ANISOU 1472 N GLY B 94 4312 6428 5328 -1002 -36 405 N ATOM 1473 CA GLY B 94 21.991 14.993 24.024 1.00 44.93 C ANISOU 1473 CA GLY B 94 4568 6790 5713 -950 -173 385 C ATOM 1474 C GLY B 94 23.333 14.403 24.423 1.00 49.93 C ANISOU 1474 C GLY B 94 4970 7522 6479 -961 -169 361 C ATOM 1475 O GLY B 94 24.066 14.982 25.232 1.00 50.85 O ANISOU 1475 O GLY B 94 5012 7649 6659 -1024 -270 344 O ATOM 1476 N ASP B 95 23.682 13.248 23.851 1.00 47.68 N ANISOU 1476 N ASP B 95 4566 7303 6247 -897 -63 352 N ATOM 1477 CA ASP B 95 24.968 12.634 24.169 1.00 45.19 C ANISOU 1477 CA ASP B 95 4012 7077 6083 -892 -61 319 C ATOM 1478 C ASP B 95 26.127 13.562 23.826 1.00 50.51 C ANISOU 1478 C ASP B 95 4572 7768 6851 -1069 -14 300 C ATOM 1479 O ASP B 95 27.044 13.751 24.637 1.00 59.83 O ANISOU 1479 O ASP B 95 5597 8986 8151 -1101 -118 272 O ATOM 1480 CB ASP B 95 25.103 11.295 23.444 1.00 44.97 C ANISOU 1480 CB ASP B 95 3890 7102 6093 -796 67 307 C ATOM 1481 CG ASP B 95 24.228 10.201 24.070 1.00 57.79 C ANISOU 1481 CG ASP B 95 5572 8720 7666 -618 -7 318 C ATOM 1482 OD1 ASP B 95 23.846 10.327 25.254 1.00 55.67 O ANISOU 1482 OD1 ASP B 95 5358 8427 7368 -565 -159 324 O ATOM 1483 OD2 ASP B 95 23.929 9.203 23.383 1.00 62.37 O ANISOU 1483 OD2 ASP B 95 6153 9313 8230 -538 95 317 O ATOM 1484 N GLU B 96 26.106 14.160 22.629 1.00 49.78 N ANISOU 1484 N GLU B 96 4565 7644 6707 -1194 137 315 N ATOM 1485 CA GLU B 96 27.204 15.046 22.237 1.00 51.79 C ANISOU 1485 CA GLU B 96 4721 7909 7047 -1385 210 297 C ATOM 1486 C GLU B 96 27.265 16.275 23.135 1.00 50.65 C ANISOU 1486 C GLU B 96 4636 7711 6898 -1476 46 304 C ATOM 1487 O GLU B 96 28.354 16.677 23.570 1.00 55.22 O ANISOU 1487 O GLU B 96 5042 8327 7614 -1575 4 271 O ATOM 1488 CB GLU B 96 27.060 15.462 20.771 1.00 59.35 C ANISOU 1488 CB GLU B 96 5816 8821 7912 -1508 408 319 C ATOM 1489 CG GLU B 96 27.071 14.297 19.793 1.00 80.92 C ANISOU 1489 CG GLU B 96 8506 11598 10641 -1435 586 306 C ATOM 1490 CD GLU B 96 26.332 14.587 18.482 1.00 96.27 C ANISOU 1490 CD GLU B 96 10704 13461 12414 -1497 717 345 C ATOM 1491 OE1 GLU B 96 26.526 13.831 17.507 1.00101.72 O ANISOU 1491 OE1 GLU B 96 11379 14178 13092 -1486 893 329 O ATOM 1492 OE2 GLU B 96 25.549 15.559 18.422 1.00 99.74 O ANISOU 1492 OE2 GLU B 96 11368 13801 12729 -1551 636 387 O ATOM 1493 N PHE B 97 26.100 16.872 23.430 1.00 50.17 N ANISOU 1493 N PHE B 97 4813 7560 6690 -1442 -51 338 N ATOM 1494 CA PHE B 97 26.045 18.056 24.281 1.00 49.35 C ANISOU 1494 CA PHE B 97 4798 7390 6564 -1518 -206 340 C ATOM 1495 C PHE B 97 26.712 17.794 25.624 1.00 52.97 C ANISOU 1495 C PHE B 97 5095 7900 7130 -1468 -370 305 C ATOM 1496 O PHE B 97 27.481 18.627 26.120 1.00 55.08 O ANISOU 1496 O PHE B 97 5301 8156 7469 -1589 -456 286 O ATOM 1497 CB PHE B 97 24.586 18.502 24.492 1.00 46.12 C ANISOU 1497 CB PHE B 97 4648 6879 5996 -1440 -286 367 C ATOM 1498 CG PHE B 97 24.445 19.707 25.402 1.00 47.72 C ANISOU 1498 CG PHE B 97 4963 7003 6167 -1501 -442 361 C ATOM 1499 CD1 PHE B 97 24.430 19.561 26.790 1.00 47.93 C ANISOU 1499 CD1 PHE B 97 4957 7042 6211 -1417 -602 335 C ATOM 1500 CD2 PHE B 97 24.355 20.985 24.874 1.00 48.39 C ANISOU 1500 CD2 PHE B 97 5202 6991 6194 -1646 -432 379 C ATOM 1501 CE1 PHE B 97 24.332 20.672 27.633 1.00 43.74 C ANISOU 1501 CE1 PHE B 97 4542 6433 5644 -1476 -742 322 C ATOM 1502 CE2 PHE B 97 24.249 22.094 25.711 1.00 52.14 C ANISOU 1502 CE2 PHE B 97 5785 7384 6641 -1700 -578 368 C ATOM 1503 CZ PHE B 97 24.237 21.932 27.095 1.00 44.26 C ANISOU 1503 CZ PHE B 97 4748 6405 5663 -1614 -730 337 C ATOM 1504 N GLU B 98 26.414 16.645 26.232 1.00 48.24 N ANISOU 1504 N GLU B 98 4442 7348 6539 -1294 -425 297 N ATOM 1505 CA GLU B 98 26.933 16.354 27.556 1.00 47.75 C ANISOU 1505 CA GLU B 98 4276 7316 6550 -1232 -606 270 C ATOM 1506 C GLU B 98 28.412 16.024 27.500 1.00 54.10 C ANISOU 1506 C GLU B 98 4797 8204 7555 -1291 -600 230 C ATOM 1507 O GLU B 98 29.158 16.349 28.433 1.00 59.40 O ANISOU 1507 O GLU B 98 5372 8881 8317 -1327 -765 202 O ATOM 1508 CB GLU B 98 26.125 15.213 28.187 1.00 50.18 C ANISOU 1508 CB GLU B 98 4642 7633 6790 -1036 -659 278 C ATOM 1509 CG GLU B 98 24.634 15.549 28.346 1.00 59.64 C ANISOU 1509 CG GLU B 98 6096 8747 7816 -977 -667 304 C ATOM 1510 CD GLU B 98 23.732 14.308 28.354 1.00 72.11 C ANISOU 1510 CD GLU B 98 7721 10341 9335 -810 -621 317 C ATOM 1511 OE1 GLU B 98 24.259 13.206 28.635 1.00 78.15 O ANISOU 1511 OE1 GLU B 98 8353 11169 10174 -724 -639 308 O ATOM 1512 OE2 GLU B 98 22.506 14.433 28.075 1.00 58.33 O ANISOU 1512 OE2 GLU B 98 6143 8539 7481 -767 -573 332 O ATOM 1513 N LEU B 99 28.860 15.397 26.412 1.00 52.67 N ANISOU 1513 N LEU B 99 4477 8083 7452 -1302 -413 220 N ATOM 1514 CA LEU B 99 30.286 15.137 26.259 1.00 50.53 C ANISOU 1514 CA LEU B 99 3911 7891 7397 -1365 -379 169 C ATOM 1515 C LEU B 99 31.068 16.445 26.226 1.00 61.29 C ANISOU 1515 C LEU B 99 5220 9230 8836 -1578 -392 152 C ATOM 1516 O LEU B 99 32.059 16.609 26.948 1.00 65.14 O ANISOU 1516 O LEU B 99 5517 9747 9486 -1622 -527 109 O ATOM 1517 CB LEU B 99 30.540 14.295 25.001 1.00 51.74 C ANISOU 1517 CB LEU B 99 3953 8102 7603 -1347 -139 154 C ATOM 1518 CG LEU B 99 32.023 14.011 24.736 1.00 65.12 C ANISOU 1518 CG LEU B 99 5318 9879 9544 -1412 -65 86 C ATOM 1519 CD1 LEU B 99 32.672 13.387 25.965 1.00 74.59 C ANISOU 1519 CD1 LEU B 99 6326 11117 10897 -1293 -293 47 C ATOM 1520 CD2 LEU B 99 32.228 13.127 23.517 1.00 62.81 C ANISOU 1520 CD2 LEU B 99 4933 9639 9292 -1381 187 63 C ATOM 1521 N ARG B 100 30.623 17.403 25.410 1.00 66.64 N ANISOU 1521 N ARG B 100 6076 9844 9398 -1716 -270 185 N ATOM 1522 CA ARG B 100 31.266 18.713 25.420 1.00 68.46 C ANISOU 1522 CA ARG B 100 6298 10034 9680 -1928 -291 176 C ATOM 1523 C ARG B 100 31.128 19.381 26.784 1.00 63.70 C ANISOU 1523 C ARG B 100 5777 9377 9051 -1919 -554 174 C ATOM 1524 O ARG B 100 32.108 19.905 27.329 1.00 69.89 O ANISOU 1524 O ARG B 100 6408 10170 9978 -2029 -663 136 O ATOM 1525 CB ARG B 100 30.673 19.603 24.334 1.00 80.39 C ANISOU 1525 CB ARG B 100 8041 11462 11039 -2062 -133 221 C ATOM 1526 CG ARG B 100 30.642 18.982 22.967 1.00 90.88 C ANISOU 1526 CG ARG B 100 9362 12824 12344 -2069 123 229 C ATOM 1527 CD ARG B 100 30.389 20.049 21.922 1.00 99.52 C ANISOU 1527 CD ARG B 100 10672 13826 13313 -2254 262 269 C ATOM 1528 NE ARG B 100 30.190 19.469 20.599 1.00102.56 N ANISOU 1528 NE ARG B 100 11117 14222 13628 -2254 496 283 N ATOM 1529 CZ ARG B 100 30.058 20.182 19.488 1.00 99.98 C ANISOU 1529 CZ ARG B 100 10984 13818 13187 -2412 653 317 C ATOM 1530 NH1 ARG B 100 29.883 19.565 18.327 1.00101.78 N ANISOU 1530 NH1 ARG B 100 11278 14053 13339 -2402 856 326 N ATOM 1531 NH2 ARG B 100 30.103 21.507 19.540 1.00 96.02 N ANISOU 1531 NH2 ARG B 100 10627 13221 12635 -2583 600 343 N ATOM 1532 N TYR B 101 29.914 19.357 27.356 1.00 54.30 N ANISOU 1532 N TYR B 101 4824 8124 7683 -1790 -658 208 N ATOM 1533 CA TYR B 101 29.664 20.049 28.620 1.00 57.09 C ANISOU 1533 CA TYR B 101 5303 8411 7979 -1783 -886 203 C ATOM 1534 C TYR B 101 30.604 19.560 29.715 1.00 62.07 C ANISOU 1534 C TYR B 101 5732 9095 8756 -1736 -1074 158 C ATOM 1535 O TYR B 101 31.277 20.363 30.377 1.00 64.12 O ANISOU 1535 O TYR B 101 5952 9326 9086 -1848 -1225 132 O ATOM 1536 CB TYR B 101 28.207 19.874 29.049 1.00 58.96 C ANISOU 1536 CB TYR B 101 5796 8586 8020 -1629 -932 233 C ATOM 1537 CG TYR B 101 27.822 20.735 30.231 1.00 57.98 C ANISOU 1537 CG TYR B 101 5847 8375 7808 -1635 -1127 224 C ATOM 1538 CD1 TYR B 101 27.118 21.921 30.053 1.00 56.03 C ANISOU 1538 CD1 TYR B 101 5825 8022 7444 -1714 -1124 239 C ATOM 1539 CD2 TYR B 101 28.172 20.365 31.532 1.00 65.40 C ANISOU 1539 CD2 TYR B 101 6744 9330 8777 -1560 -1323 196 C ATOM 1540 CE1 TYR B 101 26.770 22.717 31.141 1.00 58.96 C ANISOU 1540 CE1 TYR B 101 6362 8307 7734 -1715 -1293 221 C ATOM 1541 CE2 TYR B 101 27.839 21.150 32.624 1.00 62.54 C ANISOU 1541 CE2 TYR B 101 6563 8882 8320 -1570 -1494 181 C ATOM 1542 CZ TYR B 101 27.136 22.322 32.426 1.00 64.56 C ANISOU 1542 CZ TYR B 101 7029 9036 8463 -1646 -1471 191 C ATOM 1543 OH TYR B 101 26.809 23.095 33.515 1.00 68.17 O ANISOU 1543 OH TYR B 101 7672 9404 8828 -1651 -1632 167 O ATOM 1544 N ARG B 102 30.670 18.242 29.919 1.00 65.79 N ANISOU 1544 N ARG B 102 6084 9637 9277 -1571 -1085 149 N ATOM 1545 CA ARG B 102 31.522 17.722 30.980 1.00 75.92 C ANISOU 1545 CA ARG B 102 7197 10955 10693 -1509 -1293 110 C ATOM 1546 C ARG B 102 32.994 17.865 30.639 1.00 82.70 C ANISOU 1546 C ARG B 102 7740 11877 11807 -1638 -1279 57 C ATOM 1547 O ARG B 102 33.826 17.906 31.552 1.00 87.25 O ANISOU 1547 O ARG B 102 8180 12457 12512 -1646 -1494 16 O ATOM 1548 CB ARG B 102 31.188 16.257 31.287 1.00 75.54 C ANISOU 1548 CB ARG B 102 7125 10950 10628 -1295 -1316 116 C ATOM 1549 CG ARG B 102 31.914 15.234 30.430 1.00 81.33 C ANISOU 1549 CG ARG B 102 7593 11777 11534 -1250 -1171 90 C ATOM 1550 CD ARG B 102 31.487 13.808 30.785 1.00 90.35 C ANISOU 1550 CD ARG B 102 8750 12940 12637 -1034 -1209 102 C ATOM 1551 NE ARG B 102 30.064 13.562 30.531 1.00 96.23 N ANISOU 1551 NE ARG B 102 9753 13644 13165 -952 -1104 154 N ATOM 1552 CZ ARG B 102 29.586 12.932 29.459 1.00 95.93 C ANISOU 1552 CZ ARG B 102 9720 13635 13093 -905 -895 171 C ATOM 1553 NH1 ARG B 102 30.414 12.472 28.531 1.00 91.77 N ANISOU 1553 NH1 ARG B 102 8968 13177 12722 -931 -749 139 N ATOM 1554 NH2 ARG B 102 28.277 12.756 29.318 1.00100.11 N ANISOU 1554 NH2 ARG B 102 10477 14120 13439 -833 -831 213 N ATOM 1555 N ARG B 103 33.335 17.954 29.352 1.00 81.51 N ANISOU 1555 N ARG B 103 7471 11768 11731 -1743 -1032 51 N ATOM 1556 CA ARG B 103 34.726 18.183 28.989 1.00 78.18 C ANISOU 1556 CA ARG B 103 6740 11403 11561 -1890 -985 -8 C ATOM 1557 C ARG B 103 35.174 19.593 29.342 1.00 78.95 C ANISOU 1557 C ARG B 103 6869 11439 11690 -2097 -1087 -19 C ATOM 1558 O ARG B 103 36.373 19.823 29.531 1.00 87.74 O ANISOU 1558 O ARG B 103 7718 12587 13032 -2207 -1153 -79 O ATOM 1559 CB ARG B 103 34.931 17.904 27.498 1.00 81.30 C ANISOU 1559 CB ARG B 103 7033 11852 12006 -1958 -664 -13 C ATOM 1560 CG ARG B 103 35.816 16.696 27.218 1.00 94.03 C ANISOU 1560 CG ARG B 103 8321 13566 13841 -1862 -591 -75 C ATOM 1561 CD ARG B 103 35.501 16.026 25.885 1.00105.77 C ANISOU 1561 CD ARG B 103 9821 15092 15277 -1831 -287 -65 C ATOM 1562 NE ARG B 103 35.158 16.991 24.843 1.00119.33 N ANISOU 1562 NE ARG B 103 11714 16760 16864 -2018 -73 -28 N ATOM 1563 CZ ARG B 103 34.771 16.656 23.616 1.00126.46 C ANISOU 1563 CZ ARG B 103 12705 17670 17673 -2027 189 -9 C ATOM 1564 NH1 ARG B 103 34.691 15.378 23.273 1.00131.05 N ANISOU 1564 NH1 ARG B 103 13199 18310 18283 -1861 277 -28 N ATOM 1565 NH2 ARG B 103 34.466 17.597 22.731 1.00125.62 N ANISOU 1565 NH2 ARG B 103 12792 17503 17436 -2203 352 30 N ATOM 1566 N ALA B 104 34.242 20.535 29.457 1.00 76.26 N ANISOU 1566 N ALA B 104 6839 11002 11136 -2150 -1111 30 N ATOM 1567 CA ALA B 104 34.590 21.906 29.802 1.00 75.00 C ANISOU 1567 CA ALA B 104 6744 10766 10986 -2344 -1214 22 C ATOM 1568 C ALA B 104 34.333 22.238 31.261 1.00 75.16 C ANISOU 1568 C ALA B 104 6908 10720 10929 -2279 -1517 16 C ATOM 1569 O ALA B 104 35.065 23.049 31.832 1.00 81.28 O ANISOU 1569 O ALA B 104 7623 11459 11802 -2416 -1674 -18 O ATOM 1570 CB ALA B 104 33.818 22.891 28.914 1.00 70.83 C ANISOU 1570 CB ALA B 104 6476 10154 10280 -2469 -1044 74 C ATOM 1571 N PHE B 105 33.312 21.640 31.877 1.00 76.41 N ANISOU 1571 N PHE B 105 7264 10855 10912 -2082 -1596 45 N ATOM 1572 CA PHE B 105 32.983 21.906 33.275 1.00 83.11 C ANISOU 1572 CA PHE B 105 8289 11633 11656 -2015 -1861 38 C ATOM 1573 C PHE B 105 33.006 20.608 34.072 1.00 92.06 C ANISOU 1573 C PHE B 105 9359 12815 12806 -1811 -1995 29 C ATOM 1574 O PHE B 105 33.611 19.623 33.642 1.00101.80 O ANISOU 1574 O PHE B 105 10345 14138 14196 -1747 -1930 12 O ATOM 1575 CB PHE B 105 31.609 22.577 33.387 1.00 80.86 C ANISOU 1575 CB PHE B 105 8359 11247 11116 -1985 -1829 79 C ATOM 1576 CG PHE B 105 31.396 23.691 32.403 1.00 77.29 C ANISOU 1576 CG PHE B 105 8005 10739 10624 -2154 -1671 101 C ATOM 1577 CD1 PHE B 105 30.274 23.710 31.595 1.00 78.88 C ANISOU 1577 CD1 PHE B 105 8390 10908 10673 -2102 -1494 146 C ATOM 1578 CD2 PHE B 105 32.323 24.715 32.277 1.00 73.44 C ANISOU 1578 CD2 PHE B 105 7430 10220 10253 -2369 -1708 77 C ATOM 1579 CE1 PHE B 105 30.081 24.732 30.676 1.00 78.71 C ANISOU 1579 CE1 PHE B 105 8484 10818 10605 -2254 -1368 170 C ATOM 1580 CE2 PHE B 105 32.135 25.740 31.362 1.00 70.91 C ANISOU 1580 CE2 PHE B 105 7225 9833 9883 -2533 -1563 103 C ATOM 1581 CZ PHE B 105 31.014 25.752 30.568 1.00 76.11 C ANISOU 1581 CZ PHE B 105 8087 10453 10377 -2472 -1400 152 C ATOM 1582 N SER B 106 32.352 20.583 35.226 1.00 96.15 N ANISOU 1582 N SER B 106 10107 13264 13160 -1707 -2176 36 N ATOM 1583 CA SER B 106 32.173 19.331 35.950 1.00105.97 C ANISOU 1583 CA SER B 106 11360 14535 14371 -1510 -2282 40 C ATOM 1584 C SER B 106 31.072 18.517 35.266 1.00110.99 C ANISOU 1584 C SER B 106 12092 15197 14880 -1377 -2062 85 C ATOM 1585 O SER B 106 30.590 18.862 34.183 1.00104.43 O ANISOU 1585 O SER B 106 11288 14374 14016 -1435 -1842 108 O ATOM 1586 CB SER B 106 31.856 19.601 37.420 1.00108.91 C ANISOU 1586 CB SER B 106 11973 14815 14592 -1461 -2535 32 C ATOM 1587 OG SER B 106 30.507 20.014 37.586 1.00113.92 O ANISOU 1587 OG SER B 106 12921 15376 14985 -1421 -2448 61 O ATOM 1588 N ASP B 107 30.664 17.414 35.893 1.00117.76 N ANISOU 1588 N ASP B 107 13017 16062 15665 -1201 -2129 98 N ATOM 1589 CA ASP B 107 29.499 16.680 35.417 1.00111.30 C ANISOU 1589 CA ASP B 107 12326 15253 14711 -1078 -1946 137 C ATOM 1590 C ASP B 107 28.255 17.551 35.539 1.00107.92 C ANISOU 1590 C ASP B 107 12187 14740 14077 -1102 -1882 156 C ATOM 1591 O ASP B 107 28.064 18.256 36.537 1.00108.31 O ANISOU 1591 O ASP B 107 12416 14712 14026 -1130 -2033 141 O ATOM 1592 CB ASP B 107 29.319 15.385 36.210 1.00109.46 C ANISOU 1592 CB ASP B 107 12135 15025 14431 -900 -2049 147 C ATOM 1593 N LEU B 108 27.410 17.507 34.502 1.00100.23 N ANISOU 1593 N LEU B 108 11259 13775 13047 -1089 -1663 183 N ATOM 1594 CA LEU B 108 26.181 18.296 34.507 1.00 92.83 C ANISOU 1594 CA LEU B 108 10574 12756 11943 -1097 -1599 194 C ATOM 1595 C LEU B 108 25.291 17.928 35.689 1.00 97.42 C ANISOU 1595 C LEU B 108 11369 13281 12365 -973 -1682 190 C ATOM 1596 O LEU B 108 24.536 18.773 36.186 1.00 93.50 O ANISOU 1596 O LEU B 108 11083 12700 11744 -992 -1704 176 O ATOM 1597 CB LEU B 108 25.440 18.113 33.173 1.00 77.09 C ANISOU 1597 CB LEU B 108 8580 10781 9930 -1083 -1373 223 C ATOM 1598 CG LEU B 108 24.177 18.928 32.858 1.00 60.71 C ANISOU 1598 CG LEU B 108 6724 8620 7721 -1090 -1290 232 C ATOM 1599 CD1 LEU B 108 24.328 20.396 33.223 1.00 64.16 C ANISOU 1599 CD1 LEU B 108 7277 8972 8129 -1218 -1385 212 C ATOM 1600 CD2 LEU B 108 23.808 18.798 31.397 1.00 55.10 C ANISOU 1600 CD2 LEU B 108 5977 7930 7027 -1107 -1102 260 C ATOM 1601 N THR B 109 25.395 16.684 36.169 1.00106.07 N ANISOU 1601 N THR B 109 12422 14416 13462 -851 -1726 199 N ATOM 1602 CA THR B 109 24.603 16.197 37.293 1.00109.46 C ANISOU 1602 CA THR B 109 13063 14792 13735 -741 -1788 198 C ATOM 1603 C THR B 109 25.098 16.692 38.650 1.00113.91 C ANISOU 1603 C THR B 109 13750 15292 14240 -774 -2018 170 C ATOM 1604 O THR B 109 24.318 16.712 39.609 1.00116.56 O ANISOU 1604 O THR B 109 14326 15556 14408 -721 -2050 161 O ATOM 1605 CB THR B 109 24.587 14.666 37.290 1.00105.29 C ANISOU 1605 CB THR B 109 12464 14316 13226 -608 -1760 222 C ATOM 1606 OG1 THR B 109 25.928 14.171 37.154 1.00105.85 O ANISOU 1606 OG1 THR B 109 12299 14451 13468 -616 -1866 217 O ATOM 1607 CG2 THR B 109 23.724 14.144 36.143 1.00 98.37 C ANISOU 1607 CG2 THR B 109 11552 13476 12348 -557 -1531 246 C ATOM 1608 N SER B 110 26.367 17.083 38.764 1.00115.54 N ANISOU 1608 N SER B 110 13802 15517 14579 -863 -2175 153 N ATOM 1609 CA SER B 110 26.881 17.534 40.050 1.00116.79 C ANISOU 1609 CA SER B 110 14083 15608 14685 -896 -2421 125 C ATOM 1610 C SER B 110 26.567 18.996 40.339 1.00118.36 C ANISOU 1610 C SER B 110 14453 15722 14798 -1010 -2449 96 C ATOM 1611 O SER B 110 26.690 19.423 41.492 1.00121.61 O ANISOU 1611 O SER B 110 15043 16054 15108 -1028 -2631 69 O ATOM 1612 CB SER B 110 28.393 17.311 40.114 1.00120.44 C ANISOU 1612 CB SER B 110 14293 16119 15349 -941 -2607 109 C ATOM 1613 OG SER B 110 28.860 17.394 41.449 1.00124.11 O ANISOU 1613 OG SER B 110 14888 16515 15753 -934 -2878 87 O ATOM 1614 N GLN B 111 26.153 19.763 39.336 1.00119.46 N ANISOU 1614 N GLN B 111 14563 15863 14963 -1084 -2280 100 N ATOM 1615 CA GLN B 111 25.957 21.199 39.483 1.00119.16 C ANISOU 1615 CA GLN B 111 14670 15737 14868 -1199 -2311 73 C ATOM 1616 C GLN B 111 24.604 21.569 40.087 1.00119.33 C ANISOU 1616 C GLN B 111 14988 15666 14687 -1131 -2249 54 C ATOM 1617 O GLN B 111 24.237 22.746 40.042 1.00124.73 O ANISOU 1617 O GLN B 111 15799 16270 15322 -1206 -2237 29 O ATOM 1618 CB GLN B 111 26.118 21.884 38.121 1.00114.16 C ANISOU 1618 CB GLN B 111 13898 15131 14347 -1312 -2166 88 C ATOM 1619 N LEU B 112 23.865 20.619 40.662 1.00109.97 N ANISOU 1619 N LEU B 112 13916 14480 13387 -996 -2206 59 N ATOM 1620 CA LEU B 112 22.468 20.838 41.022 1.00102.85 C ANISOU 1620 CA LEU B 112 13250 13505 12323 -925 -2083 36 C ATOM 1621 C LEU B 112 22.198 20.304 42.422 1.00101.90 C ANISOU 1621 C LEU B 112 13343 13333 12042 -849 -2172 16 C ATOM 1622 O LEU B 112 22.386 19.108 42.676 1.00102.84 O ANISOU 1622 O LEU B 112 13419 13500 12156 -769 -2193 46 O ATOM 1623 CB LEU B 112 21.540 20.157 40.008 1.00 95.25 C ANISOU 1623 CB LEU B 112 12207 12594 11387 -841 -1858 64 C ATOM 1624 CG LEU B 112 22.176 19.606 38.722 1.00 88.58 C ANISOU 1624 CG LEU B 112 11093 11854 10709 -861 -1788 110 C ATOM 1625 CD1 LEU B 112 21.677 18.203 38.419 1.00 83.74 C ANISOU 1625 CD1 LEU B 112 10417 11305 10096 -737 -1669 140 C ATOM 1626 CD2 LEU B 112 21.921 20.519 37.522 1.00 85.57 C ANISOU 1626 CD2 LEU B 112 10663 11460 10390 -941 -1676 115 C ATOM 1627 N HIS B 113 21.732 21.180 43.320 1.00 92.65 N ANISOU 1627 N HIS B 113 12421 12054 10727 -873 -2218 -35 N ATOM 1628 CA HIS B 113 21.340 20.799 44.682 1.00 88.12 C ANISOU 1628 CA HIS B 113 12108 11410 9964 -812 -2273 -62 C ATOM 1629 C HIS B 113 19.829 20.984 44.812 1.00 86.00 C ANISOU 1629 C HIS B 113 12018 11083 9575 -745 -2055 -103 C ATOM 1630 O HIS B 113 19.353 22.089 45.091 1.00 82.39 O ANISOU 1630 O HIS B 113 11714 10538 9054 -781 -2037 -160 O ATOM 1631 CB HIS B 113 22.097 21.617 45.727 1.00 80.44 C ANISOU 1631 CB HIS B 113 11297 10352 8915 -896 -2511 -100 C ATOM 1632 N ILE B 114 19.077 19.893 44.644 1.00 83.01 N ANISOU 1632 N ILE B 114 11619 10748 9174 -646 -1894 -81 N ATOM 1633 CA ILE B 114 17.637 19.961 44.423 1.00 84.78 C ANISOU 1633 CA ILE B 114 11917 10940 9354 -582 -1660 -118 C ATOM 1634 C ILE B 114 16.892 19.031 45.373 1.00 83.91 C ANISOU 1634 C ILE B 114 11994 10799 9088 -505 -1564 -131 C ATOM 1635 O ILE B 114 17.354 17.926 45.681 1.00 81.43 O ANISOU 1635 O ILE B 114 11668 10524 8745 -473 -1625 -82 O ATOM 1636 CB ILE B 114 17.292 19.621 42.964 1.00 82.60 C ANISOU 1636 CB ILE B 114 11396 10748 9240 -553 -1518 -80 C ATOM 1637 CG1 ILE B 114 18.072 18.378 42.532 1.00 78.41 C ANISOU 1637 CG1 ILE B 114 10680 10321 8793 -527 -1562 -8 C ATOM 1638 CG2 ILE B 114 17.601 20.814 42.067 1.00 86.53 C ANISOU 1638 CG2 ILE B 114 11792 11236 9850 -634 -1553 -86 C ATOM 1639 CD1 ILE B 114 17.208 17.173 42.296 1.00 77.06 C ANISOU 1639 CD1 ILE B 114 10482 10187 8609 -430 -1393 12 C ATOM 1640 N THR B 115 15.720 19.484 45.816 1.00 81.74 N ANISOU 1640 N THR B 115 11891 10447 8718 -476 -1404 -202 N ATOM 1641 CA THR B 115 14.797 18.805 46.709 1.00 73.70 C ANISOU 1641 CA THR B 115 11073 9383 7548 -419 -1256 -235 C ATOM 1642 C THR B 115 13.403 18.815 46.092 1.00 79.61 C ANISOU 1642 C THR B 115 11750 10132 8367 -359 -999 -280 C ATOM 1643 O THR B 115 13.088 19.704 45.294 1.00 83.96 O ANISOU 1643 O THR B 115 12189 10675 9035 -363 -966 -310 O ATOM 1644 CB THR B 115 14.768 19.494 48.081 1.00 66.50 C ANISOU 1644 CB THR B 115 10479 8353 6436 -455 -1316 -302 C ATOM 1645 OG1 THR B 115 14.954 18.517 49.103 1.00 74.74 O ANISOU 1645 OG1 THR B 115 11717 9372 7310 -442 -1354 -277 O ATOM 1646 CG2 THR B 115 13.450 20.192 48.317 1.00 60.59 C ANISOU 1646 CG2 THR B 115 9855 7525 5641 -426 -1099 -402 C ATOM 1647 N PRO B 116 12.551 17.834 46.430 1.00 73.73 N ANISOU 1647 N PRO B 116 11067 9388 7561 -304 -822 -288 N ATOM 1648 CA PRO B 116 11.207 17.808 45.816 1.00 65.27 C ANISOU 1648 CA PRO B 116 9897 8317 6586 -247 -585 -338 C ATOM 1649 C PRO B 116 10.424 19.090 46.030 1.00 64.92 C ANISOU 1649 C PRO B 116 9943 8183 6542 -243 -502 -445 C ATOM 1650 O PRO B 116 9.820 19.614 45.085 1.00 66.44 O ANISOU 1650 O PRO B 116 9976 8379 6888 -211 -436 -474 O ATOM 1651 CB PRO B 116 10.539 16.601 46.493 1.00 62.81 C ANISOU 1651 CB PRO B 116 9699 7999 6169 -215 -422 -338 C ATOM 1652 CG PRO B 116 11.696 15.715 46.906 1.00 60.50 C ANISOU 1652 CG PRO B 116 9460 7740 5788 -237 -601 -247 C ATOM 1653 CD PRO B 116 12.772 16.681 47.323 1.00 67.29 C ANISOU 1653 CD PRO B 116 10405 8567 6597 -295 -835 -248 C ATOM 1654 N GLY B 117 10.445 19.633 47.246 1.00 65.26 N ANISOU 1654 N GLY B 117 10249 8133 6412 -273 -519 -507 N ATOM 1655 CA GLY B 117 9.747 20.877 47.497 1.00 68.06 C ANISOU 1655 CA GLY B 117 10702 8392 6766 -263 -445 -617 C ATOM 1656 C GLY B 117 10.326 22.080 46.784 1.00 62.41 C ANISOU 1656 C GLY B 117 9893 7662 6157 -297 -612 -613 C ATOM 1657 O GLY B 117 9.642 23.101 46.663 1.00 74.21 O ANISOU 1657 O GLY B 117 11413 9080 7703 -271 -548 -700 O ATOM 1658 N THR B 118 11.568 21.990 46.315 1.00 56.48 N ANISOU 1658 N THR B 118 9037 6975 5446 -355 -821 -519 N ATOM 1659 CA THR B 118 12.250 23.123 45.699 1.00 60.33 C ANISOU 1659 CA THR B 118 9457 7445 6022 -414 -983 -509 C ATOM 1660 C THR B 118 12.591 22.898 44.230 1.00 65.11 C ANISOU 1660 C THR B 118 9784 8144 6813 -420 -1015 -429 C ATOM 1661 O THR B 118 13.039 23.837 43.560 1.00 68.80 O ANISOU 1661 O THR B 118 10187 8591 7363 -474 -1118 -419 O ATOM 1662 CB THR B 118 13.537 23.437 46.470 1.00 55.75 C ANISOU 1662 CB THR B 118 9006 6843 5333 -504 -1214 -483 C ATOM 1663 OG1 THR B 118 14.486 22.382 46.243 1.00 57.45 O ANISOU 1663 OG1 THR B 118 9089 7161 5578 -523 -1321 -384 O ATOM 1664 CG2 THR B 118 13.239 23.546 47.968 1.00 48.52 C ANISOU 1664 CG2 THR B 118 8405 5829 4202 -501 -1189 -556 C ATOM 1665 N ALA B 119 12.377 21.686 43.717 1.00 62.90 N ANISOU 1665 N ALA B 119 9355 7954 6589 -372 -924 -375 N ATOM 1666 CA ALA B 119 12.791 21.341 42.361 1.00 56.27 C ANISOU 1666 CA ALA B 119 8272 7206 5904 -381 -953 -297 C ATOM 1667 C ALA B 119 12.096 22.205 41.307 1.00 56.43 C ANISOU 1667 C ALA B 119 8206 7186 6048 -363 -898 -326 C ATOM 1668 O ALA B 119 12.747 22.696 40.376 1.00 53.31 O ANISOU 1668 O ALA B 119 7704 6812 5741 -422 -992 -279 O ATOM 1669 CB ALA B 119 12.518 19.856 42.112 1.00 50.07 C ANISOU 1669 CB ALA B 119 7379 6507 5140 -321 -848 -248 C ATOM 1670 N TYR B 120 10.782 22.412 41.438 1.00 51.91 N ANISOU 1670 N TYR B 120 7684 6550 5488 -285 -749 -407 N ATOM 1671 CA TYR B 120 10.043 23.170 40.430 1.00 49.63 C ANISOU 1671 CA TYR B 120 7317 6212 5329 -250 -716 -438 C ATOM 1672 C TYR B 120 10.618 24.570 40.237 1.00 52.52 C ANISOU 1672 C TYR B 120 7755 6500 5700 -322 -862 -447 C ATOM 1673 O TYR B 120 10.985 24.958 39.120 1.00 52.94 O ANISOU 1673 O TYR B 120 7708 6563 5844 -363 -933 -395 O ATOM 1674 CB TYR B 120 8.566 23.263 40.797 1.00 42.94 C ANISOU 1674 CB TYR B 120 6516 5293 4506 -151 -547 -545 C ATOM 1675 CG TYR B 120 7.792 24.007 39.748 1.00 52.93 C ANISOU 1675 CG TYR B 120 7696 6497 5919 -101 -542 -580 C ATOM 1676 CD1 TYR B 120 7.512 23.416 38.521 1.00 57.18 C ANISOU 1676 CD1 TYR B 120 8056 7092 6580 -70 -524 -526 C ATOM 1677 CD2 TYR B 120 7.363 25.305 39.962 1.00 53.49 C ANISOU 1677 CD2 TYR B 120 7877 6443 6004 -81 -573 -666 C ATOM 1678 CE1 TYR B 120 6.815 24.097 37.548 1.00 54.71 C ANISOU 1678 CE1 TYR B 120 7684 6708 6394 -23 -548 -555 C ATOM 1679 CE2 TYR B 120 6.658 25.999 38.991 1.00 52.83 C ANISOU 1679 CE2 TYR B 120 7727 6287 6059 -27 -595 -697 C ATOM 1680 CZ TYR B 120 6.387 25.390 37.790 1.00 58.08 C ANISOU 1680 CZ TYR B 120 8222 7006 6838 1 -589 -639 C ATOM 1681 OH TYR B 120 5.691 26.073 36.822 1.00 62.06 O ANISOU 1681 OH TYR B 120 8682 7426 7472 57 -636 -667 O ATOM 1682 N GLN B 121 10.677 25.351 41.318 1.00 52.16 N ANISOU 1682 N GLN B 121 7902 6367 5551 -343 -901 -516 N ATOM 1683 CA GLN B 121 11.157 26.725 41.221 1.00 55.62 C ANISOU 1683 CA GLN B 121 8431 6713 5988 -413 -1038 -534 C ATOM 1684 C GLN B 121 12.550 26.788 40.594 1.00 56.81 C ANISOU 1684 C GLN B 121 8487 6929 6169 -535 -1196 -433 C ATOM 1685 O GLN B 121 12.822 27.659 39.750 1.00 52.69 O ANISOU 1685 O GLN B 121 7939 6363 5718 -593 -1272 -411 O ATOM 1686 CB GLN B 121 11.141 27.377 42.608 1.00 43.49 C ANISOU 1686 CB GLN B 121 7132 5082 4312 -425 -1063 -621 C ATOM 1687 N SER B 122 13.437 25.858 40.974 1.00 49.06 N ANISOU 1687 N SER B 122 7451 6047 5141 -575 -1242 -373 N ATOM 1688 CA SER B 122 14.795 25.840 40.427 1.00 49.16 C ANISOU 1688 CA SER B 122 7344 6129 5206 -688 -1379 -289 C ATOM 1689 C SER B 122 14.779 25.556 38.928 1.00 53.78 C ANISOU 1689 C SER B 122 7736 6776 5921 -692 -1324 -224 C ATOM 1690 O SER B 122 15.475 26.218 38.146 1.00 58.15 O ANISOU 1690 O SER B 122 8235 7321 6537 -791 -1400 -184 O ATOM 1691 CB SER B 122 15.640 24.789 41.149 1.00 50.56 C ANISOU 1691 CB SER B 122 7489 6394 5326 -702 -1440 -248 C ATOM 1692 OG SER B 122 15.500 24.875 42.564 1.00 63.88 O ANISOU 1692 OG SER B 122 9388 8018 6867 -684 -1474 -308 O ATOM 1693 N PHE B 123 13.986 24.563 38.521 1.00 44.26 N ANISOU 1693 N PHE B 123 6440 5626 4750 -592 -1189 -214 N ATOM 1694 CA PHE B 123 13.874 24.199 37.116 1.00 52.02 C ANISOU 1694 CA PHE B 123 7263 6662 5840 -586 -1134 -157 C ATOM 1695 C PHE B 123 13.342 25.362 36.288 1.00 51.48 C ANISOU 1695 C PHE B 123 7246 6490 5824 -599 -1147 -178 C ATOM 1696 O PHE B 123 13.879 25.668 35.220 1.00 45.33 O ANISOU 1696 O PHE B 123 6400 5721 5102 -677 -1184 -121 O ATOM 1697 CB PHE B 123 12.967 22.973 36.966 1.00 47.65 C ANISOU 1697 CB PHE B 123 6632 6166 5307 -471 -993 -158 C ATOM 1698 CG PHE B 123 12.559 22.688 35.549 1.00 43.64 C ANISOU 1698 CG PHE B 123 5998 5683 4898 -446 -934 -118 C ATOM 1699 CD1 PHE B 123 13.316 21.834 34.759 1.00 42.33 C ANISOU 1699 CD1 PHE B 123 5687 5622 4776 -481 -927 -40 C ATOM 1700 CD2 PHE B 123 11.411 23.259 35.006 1.00 44.51 C ANISOU 1700 CD2 PHE B 123 6144 5706 5061 -383 -891 -165 C ATOM 1701 CE1 PHE B 123 12.947 21.557 33.450 1.00 46.28 C ANISOU 1701 CE1 PHE B 123 6099 6137 5348 -463 -873 -6 C ATOM 1702 CE2 PHE B 123 11.034 22.981 33.695 1.00 44.76 C ANISOU 1702 CE2 PHE B 123 6082 5750 5174 -361 -859 -127 C ATOM 1703 CZ PHE B 123 11.804 22.128 32.916 1.00 40.71 C ANISOU 1703 CZ PHE B 123 5446 5341 4682 -405 -847 -46 C ATOM 1704 N GLU B 124 12.275 26.014 36.761 1.00 49.82 N ANISOU 1704 N GLU B 124 7161 6172 5595 -523 -1114 -263 N ATOM 1705 CA GLU B 124 11.700 27.106 35.982 1.00 51.34 C ANISOU 1705 CA GLU B 124 7411 6250 5847 -517 -1145 -288 C ATOM 1706 C GLU B 124 12.650 28.291 35.895 1.00 55.13 C ANISOU 1706 C GLU B 124 7982 6662 6302 -651 -1282 -267 C ATOM 1707 O GLU B 124 12.680 28.984 34.876 1.00 62.49 O ANISOU 1707 O GLU B 124 8928 7532 7282 -698 -1327 -236 O ATOM 1708 CB GLU B 124 10.364 27.538 36.574 1.00 48.59 C ANISOU 1708 CB GLU B 124 7161 5796 5504 -395 -1079 -398 C ATOM 1709 CG GLU B 124 9.263 26.505 36.436 1.00 52.93 C ANISOU 1709 CG GLU B 124 7606 6394 6113 -270 -936 -426 C ATOM 1710 CD GLU B 124 8.789 26.338 34.998 1.00 57.93 C ANISOU 1710 CD GLU B 124 8128 7025 6857 -237 -936 -385 C ATOM 1711 OE1 GLU B 124 8.532 25.193 34.576 1.00 61.15 O ANISOU 1711 OE1 GLU B 124 8407 7525 7304 -195 -855 -351 O ATOM 1712 OE2 GLU B 124 8.670 27.354 34.288 1.00 58.91 O ANISOU 1712 OE2 GLU B 124 8313 7046 7022 -254 -1024 -387 O ATOM 1713 N GLN B 125 13.458 28.514 36.929 1.00 58.08 N ANISOU 1713 N GLN B 125 8428 7042 6600 -721 -1356 -280 N ATOM 1714 CA GLN B 125 14.408 29.617 36.890 1.00 61.36 C ANISOU 1714 CA GLN B 125 8921 7392 7001 -863 -1491 -263 C ATOM 1715 C GLN B 125 15.517 29.353 35.880 1.00 60.48 C ANISOU 1715 C GLN B 125 8661 7368 6951 -988 -1521 -165 C ATOM 1716 O GLN B 125 15.849 30.226 35.074 1.00 70.07 O ANISOU 1716 O GLN B 125 9910 8516 8197 -1088 -1571 -135 O ATOM 1717 CB GLN B 125 14.988 29.862 38.288 1.00 64.87 C ANISOU 1717 CB GLN B 125 9480 7818 7350 -906 -1578 -307 C ATOM 1718 N VAL B 126 16.112 28.158 35.912 1.00 56.41 N ANISOU 1718 N VAL B 126 7987 6994 6452 -989 -1484 -118 N ATOM 1719 CA VAL B 126 17.233 27.867 35.017 1.00 55.09 C ANISOU 1719 CA VAL B 126 7663 6914 6353 -1107 -1496 -38 C ATOM 1720 C VAL B 126 16.778 27.923 33.569 1.00 57.72 C ANISOU 1720 C VAL B 126 7960 7232 6739 -1105 -1415 4 C ATOM 1721 O VAL B 126 17.466 28.478 32.700 1.00 59.23 O ANISOU 1721 O VAL B 126 8134 7405 6965 -1236 -1435 51 O ATOM 1722 CB VAL B 126 17.850 26.496 35.356 1.00 51.95 C ANISOU 1722 CB VAL B 126 7102 6663 5973 -1078 -1471 -7 C ATOM 1723 CG1 VAL B 126 18.714 25.990 34.197 1.00 48.48 C ANISOU 1723 CG1 VAL B 126 6473 6320 5625 -1159 -1425 65 C ATOM 1724 CG2 VAL B 126 18.645 26.571 36.655 1.00 43.09 C ANISOU 1724 CG2 VAL B 126 6021 5547 4804 -1122 -1598 -35 C ATOM 1725 N VAL B 127 15.605 27.352 33.290 1.00 49.57 N ANISOU 1725 N VAL B 127 6924 6198 5711 -963 -1324 -13 N ATOM 1726 CA VAL B 127 15.090 27.317 31.932 1.00 47.47 C ANISOU 1726 CA VAL B 127 6638 5910 5488 -947 -1267 25 C ATOM 1727 C VAL B 127 14.734 28.722 31.457 1.00 52.74 C ANISOU 1727 C VAL B 127 7473 6418 6149 -993 -1339 10 C ATOM 1728 O VAL B 127 14.986 29.082 30.303 1.00 50.71 O ANISOU 1728 O VAL B 127 7235 6126 5905 -1076 -1341 65 O ATOM 1729 CB VAL B 127 13.882 26.370 31.866 1.00 43.35 C ANISOU 1729 CB VAL B 127 6069 5417 4985 -781 -1172 -1 C ATOM 1730 CG1 VAL B 127 13.198 26.479 30.510 1.00 42.44 C ANISOU 1730 CG1 VAL B 127 5968 5248 4911 -753 -1147 25 C ATOM 1731 CG2 VAL B 127 14.318 24.946 32.141 1.00 40.48 C ANISOU 1731 CG2 VAL B 127 5550 5203 4627 -750 -1102 28 C ATOM 1732 N ASN B 128 14.146 29.537 32.339 1.00 53.80 N ANISOU 1732 N ASN B 128 7746 6443 6252 -941 -1398 -65 N ATOM 1733 CA ASN B 128 13.735 30.879 31.940 1.00 55.23 C ANISOU 1733 CA ASN B 128 8099 6455 6431 -966 -1479 -87 C ATOM 1734 C ASN B 128 14.935 31.752 31.603 1.00 55.31 C ANISOU 1734 C ASN B 128 8167 6428 6422 -1163 -1558 -34 C ATOM 1735 O ASN B 128 14.875 32.555 30.662 1.00 59.46 O ANISOU 1735 O ASN B 128 8799 6845 6950 -1228 -1599 -2 O ATOM 1736 CB ASN B 128 12.880 31.521 33.031 1.00 49.35 C ANISOU 1736 CB ASN B 128 7484 5603 5663 -861 -1512 -192 C ATOM 1737 CG ASN B 128 11.464 30.964 33.045 1.00 63.55 C ANISOU 1737 CG ASN B 128 9245 7390 7509 -674 -1429 -253 C ATOM 1738 OD1 ASN B 128 10.959 30.501 32.014 1.00 68.05 O ANISOU 1738 OD1 ASN B 128 9745 7976 8136 -624 -1393 -218 O ATOM 1739 ND2 ASN B 128 10.823 30.988 34.207 1.00 65.67 N ANISOU 1739 ND2 ASN B 128 9561 7631 7758 -575 -1393 -348 N ATOM 1740 N GLU B 129 16.042 31.591 32.329 1.00 51.50 N ANISOU 1740 N GLU B 129 7616 6027 5925 -1265 -1586 -25 N ATOM 1741 CA GLU B 129 17.242 32.338 31.970 1.00 57.34 C ANISOU 1741 CA GLU B 129 8374 6742 6671 -1467 -1649 22 C ATOM 1742 C GLU B 129 17.890 31.772 30.712 1.00 62.43 C ANISOU 1742 C GLU B 129 8885 7476 7359 -1562 -1563 108 C ATOM 1743 O GLU B 129 18.534 32.515 29.963 1.00 62.83 O ANISOU 1743 O GLU B 129 8990 7467 7413 -1723 -1579 152 O ATOM 1744 CB GLU B 129 18.234 32.354 33.136 1.00 49.08 C ANISOU 1744 CB GLU B 129 7283 5750 5615 -1547 -1726 -2 C ATOM 1745 N LEU B 130 17.706 30.475 30.443 1.00 57.49 N ANISOU 1745 N LEU B 130 8101 6982 6760 -1467 -1461 128 N ATOM 1746 CA LEU B 130 18.334 29.879 29.269 1.00 49.82 C ANISOU 1746 CA LEU B 130 7007 6096 5825 -1551 -1365 200 C ATOM 1747 C LEU B 130 17.722 30.420 27.983 1.00 59.02 C ANISOU 1747 C LEU B 130 8314 7150 6963 -1568 -1342 237 C ATOM 1748 O LEU B 130 18.427 30.616 26.983 1.00 65.23 O ANISOU 1748 O LEU B 130 9100 7934 7749 -1715 -1291 296 O ATOM 1749 CB LEU B 130 18.217 28.360 29.333 1.00 44.11 C ANISOU 1749 CB LEU B 130 6102 5526 5133 -1433 -1271 207 C ATOM 1750 CG LEU B 130 18.622 27.548 28.095 1.00 47.65 C ANISOU 1750 CG LEU B 130 6428 6063 5613 -1474 -1150 268 C ATOM 1751 CD1 LEU B 130 20.128 27.603 27.868 1.00 45.11 C ANISOU 1751 CD1 LEU B 130 5979 5815 5346 -1655 -1123 300 C ATOM 1752 CD2 LEU B 130 18.147 26.107 28.196 1.00 45.29 C ANISOU 1752 CD2 LEU B 130 5997 5878 5332 -1319 -1072 264 C ATOM 1753 N PHE B 131 16.418 30.677 27.991 1.00 52.67 N ANISOU 1753 N PHE B 131 7634 6242 6135 -1422 -1380 199 N ATOM 1754 CA PHE B 131 15.715 31.154 26.813 1.00 54.57 C ANISOU 1754 CA PHE B 131 8022 6361 6352 -1412 -1393 229 C ATOM 1755 C PHE B 131 15.310 32.619 26.923 1.00 65.12 C ANISOU 1755 C PHE B 131 9586 7500 7658 -1438 -1519 201 C ATOM 1756 O PHE B 131 14.643 33.129 26.016 1.00 65.65 O ANISOU 1756 O PHE B 131 9806 7434 7702 -1415 -1564 220 O ATOM 1757 CB PHE B 131 14.470 30.294 26.555 1.00 50.60 C ANISOU 1757 CB PHE B 131 7476 5877 5873 -1217 -1356 205 C ATOM 1758 CG PHE B 131 14.770 28.859 26.216 1.00 48.06 C ANISOU 1758 CG PHE B 131 6963 5724 5574 -1190 -1234 240 C ATOM 1759 CD1 PHE B 131 15.329 28.521 24.995 1.00 46.97 C ANISOU 1759 CD1 PHE B 131 6808 5621 5416 -1289 -1161 311 C ATOM 1760 CD2 PHE B 131 14.461 27.841 27.109 1.00 49.11 C ANISOU 1760 CD2 PHE B 131 6950 5970 5740 -1064 -1187 198 C ATOM 1761 CE1 PHE B 131 15.599 27.190 24.669 1.00 44.25 C ANISOU 1761 CE1 PHE B 131 6293 5425 5096 -1256 -1047 335 C ATOM 1762 CE2 PHE B 131 14.731 26.510 26.799 1.00 42.14 C ANISOU 1762 CE2 PHE B 131 5902 5231 4879 -1035 -1084 229 C ATOM 1763 CZ PHE B 131 15.299 26.182 25.577 1.00 41.95 C ANISOU 1763 CZ PHE B 131 5851 5242 4845 -1125 -1016 295 C ATOM 1764 N ARG B 132 15.710 33.304 28.001 1.00 67.34 N ANISOU 1764 N ARG B 132 9906 7747 7933 -1484 -1590 156 N ATOM 1765 CA ARG B 132 15.315 34.693 28.239 1.00 72.23 C ANISOU 1765 CA ARG B 132 10747 8173 8525 -1497 -1714 117 C ATOM 1766 C ARG B 132 15.582 35.597 27.040 1.00 74.13 C ANISOU 1766 C ARG B 132 11163 8275 8726 -1641 -1755 186 C ATOM 1767 O ARG B 132 14.805 36.516 26.760 1.00 77.46 O ANISOU 1767 O ARG B 132 11788 8514 9130 -1589 -1856 165 O ATOM 1768 CB ARG B 132 16.055 35.231 29.464 1.00 74.66 C ANISOU 1768 CB ARG B 132 11064 8482 8821 -1579 -1776 74 C ATOM 1769 CG ARG B 132 15.798 36.692 29.778 1.00 83.58 C ANISOU 1769 CG ARG B 132 12429 9409 9919 -1611 -1905 31 C ATOM 1770 CD ARG B 132 16.747 37.178 30.863 1.00 94.35 C ANISOU 1770 CD ARG B 132 13800 10783 11267 -1732 -1970 1 C ATOM 1771 NE ARG B 132 18.089 36.623 30.679 1.00100.75 N ANISOU 1771 NE ARG B 132 14435 11742 12105 -1902 -1917 64 N ATOM 1772 CZ ARG B 132 19.052 37.190 29.954 1.00 99.56 C ANISOU 1772 CZ ARG B 132 14310 11558 11960 -2117 -1920 128 C ATOM 1773 NH1 ARG B 132 18.838 38.347 29.334 1.00 95.24 N ANISOU 1773 NH1 ARG B 132 13986 10825 11374 -2196 -1983 147 N ATOM 1774 NH2 ARG B 132 20.235 36.594 29.851 1.00100.76 N ANISOU 1774 NH2 ARG B 132 14264 11857 12163 -2254 -1857 168 N ATOM 1775 N ASP B 133 16.673 35.355 26.321 1.00 72.70 N ANISOU 1775 N ASP B 133 10917 8173 8534 -1823 -1676 263 N ATOM 1776 CA ASP B 133 17.114 36.233 25.244 1.00 71.15 C ANISOU 1776 CA ASP B 133 10903 7847 8283 -2002 -1692 333 C ATOM 1777 C ASP B 133 17.220 35.500 23.911 1.00 71.86 C ANISOU 1777 C ASP B 133 10962 7995 8346 -2042 -1575 408 C ATOM 1778 O ASP B 133 18.032 35.869 23.064 1.00 80.93 O ANISOU 1778 O ASP B 133 12187 9111 9452 -2243 -1518 475 O ATOM 1779 CB ASP B 133 18.459 36.870 25.592 1.00 72.82 C ANISOU 1779 CB ASP B 133 11101 8069 8500 -2235 -1693 350 C ATOM 1780 CG ASP B 133 19.577 35.841 25.682 1.00 85.49 C ANISOU 1780 CG ASP B 133 12430 9888 10164 -2325 -1562 373 C ATOM 1781 OD1 ASP B 133 19.321 34.729 26.201 1.00 89.84 O ANISOU 1781 OD1 ASP B 133 12792 10586 10758 -2174 -1517 342 O ATOM 1782 OD2 ASP B 133 20.701 36.127 25.220 1.00 88.26 O ANISOU 1782 OD2 ASP B 133 12752 10256 10527 -2546 -1500 418 O ATOM 1783 N GLY B 134 16.438 34.455 23.710 1.00 68.13 N ANISOU 1783 N GLY B 134 10386 7606 7896 -1866 -1529 396 N ATOM 1784 CA GLY B 134 16.351 33.820 22.409 1.00 66.66 C ANISOU 1784 CA GLY B 134 10215 7442 7669 -1883 -1441 460 C ATOM 1785 C GLY B 134 16.285 32.310 22.497 1.00 63.56 C ANISOU 1785 C GLY B 134 9577 7245 7327 -1770 -1325 450 C ATOM 1786 O GLY B 134 16.668 31.697 23.495 1.00 65.82 O ANISOU 1786 O GLY B 134 9661 7673 7676 -1731 -1286 411 O ATOM 1787 N VAL B 135 15.792 31.703 21.414 1.00 48.47 N ANISOU 1787 N VAL B 135 7705 5330 5380 -1720 -1279 487 N ATOM 1788 CA VAL B 135 15.708 30.257 21.254 1.00 52.49 C ANISOU 1788 CA VAL B 135 8014 6004 5924 -1625 -1165 487 C ATOM 1789 C VAL B 135 16.558 29.848 20.059 1.00 58.15 C ANISOU 1789 C VAL B 135 8738 6770 6584 -1778 -1025 557 C ATOM 1790 O VAL B 135 16.589 30.548 19.044 1.00 64.15 O ANISOU 1790 O VAL B 135 9722 7396 7255 -1890 -1039 609 O ATOM 1791 CB VAL B 135 14.246 29.803 21.044 1.00 50.82 C ANISOU 1791 CB VAL B 135 7839 5741 5730 -1412 -1236 454 C ATOM 1792 CG1 VAL B 135 14.170 28.289 20.877 1.00 47.62 C ANISOU 1792 CG1 VAL B 135 7236 5499 5358 -1323 -1119 455 C ATOM 1793 CG2 VAL B 135 13.372 30.275 22.194 1.00 44.10 C ANISOU 1793 CG2 VAL B 135 6985 4829 4941 -1265 -1351 373 C ATOM 1794 N ASN B 136 17.239 28.713 20.171 1.00 56.13 N ANISOU 1794 N ASN B 136 8252 6698 6377 -1782 -886 558 N ATOM 1795 CA ASN B 136 17.826 28.081 18.996 1.00 51.92 C ANISOU 1795 CA ASN B 136 7710 6221 5798 -1880 -732 608 C ATOM 1796 C ASN B 136 17.956 26.592 19.287 1.00 51.17 C ANISOU 1796 C ASN B 136 7359 6311 5774 -1767 -630 584 C ATOM 1797 O ASN B 136 17.850 26.156 20.439 1.00 49.20 O ANISOU 1797 O ASN B 136 6940 6150 5606 -1657 -670 537 O ATOM 1798 CB ASN B 136 19.171 28.718 18.625 1.00 50.87 C ANISOU 1798 CB ASN B 136 7594 6087 5646 -2129 -630 645 C ATOM 1799 CG ASN B 136 20.245 28.499 19.686 1.00 55.68 C ANISOU 1799 CG ASN B 136 7941 6841 6373 -2186 -587 609 C ATOM 1800 OD1 ASN B 136 20.455 27.381 20.163 1.00 51.67 O ANISOU 1800 OD1 ASN B 136 7199 6489 5944 -2087 -529 580 O ATOM 1801 ND2 ASN B 136 20.935 29.569 20.049 1.00 53.28 N ANISOU 1801 ND2 ASN B 136 7685 6477 6083 -2346 -627 611 N ATOM 1802 N TRP B 137 18.203 25.813 18.228 1.00 44.15 N ANISOU 1802 N TRP B 137 6461 5470 4843 -1799 -496 617 N ATOM 1803 CA TRP B 137 18.212 24.360 18.383 1.00 47.48 C ANISOU 1803 CA TRP B 137 6669 6047 5325 -1678 -408 595 C ATOM 1804 C TRP B 137 19.192 23.907 19.458 1.00 53.38 C ANISOU 1804 C TRP B 137 7150 6947 6187 -1691 -361 562 C ATOM 1805 O TRP B 137 18.901 22.966 20.201 1.00 50.10 O ANISOU 1805 O TRP B 137 6575 6627 5833 -1544 -376 528 O ATOM 1806 CB TRP B 137 18.527 23.676 17.060 1.00 52.07 C ANISOU 1806 CB TRP B 137 7291 6653 5841 -1738 -254 630 C ATOM 1807 CG TRP B 137 17.393 23.723 16.086 1.00 64.18 C ANISOU 1807 CG TRP B 137 9061 8055 7269 -1670 -324 654 C ATOM 1808 CD1 TRP B 137 17.397 24.315 14.860 1.00 62.93 C ANISOU 1808 CD1 TRP B 137 9162 7768 6982 -1791 -302 704 C ATOM 1809 CD2 TRP B 137 16.080 23.159 16.256 1.00 61.46 C ANISOU 1809 CD2 TRP B 137 8723 7685 6943 -1468 -437 628 C ATOM 1810 NE1 TRP B 137 16.176 24.148 14.249 1.00 68.53 N ANISOU 1810 NE1 TRP B 137 10041 8370 7627 -1669 -417 711 N ATOM 1811 CE2 TRP B 137 15.351 23.440 15.083 1.00 68.96 C ANISOU 1811 CE2 TRP B 137 9929 8490 7783 -1471 -498 661 C ATOM 1812 CE3 TRP B 137 15.457 22.441 17.278 1.00 53.75 C ANISOU 1812 CE3 TRP B 137 7568 6790 6065 -1294 -491 578 C ATOM 1813 CZ2 TRP B 137 14.024 23.032 14.909 1.00 67.43 C ANISOU 1813 CZ2 TRP B 137 9789 8233 7597 -1300 -624 640 C ATOM 1814 CZ3 TRP B 137 14.143 22.032 17.105 1.00 57.45 C ANISOU 1814 CZ3 TRP B 137 8088 7200 6539 -1136 -587 558 C ATOM 1815 CH2 TRP B 137 13.439 22.332 15.931 1.00 62.68 C ANISOU 1815 CH2 TRP B 137 8980 7721 7113 -1137 -659 585 C ATOM 1816 N GLY B 138 20.351 24.567 19.565 1.00 54.03 N ANISOU 1816 N GLY B 138 7187 7044 6300 -1870 -315 569 N ATOM 1817 CA GLY B 138 21.332 24.159 20.561 1.00 41.65 C ANISOU 1817 CA GLY B 138 5362 5610 4853 -1885 -298 534 C ATOM 1818 C GLY B 138 20.843 24.374 21.983 1.00 44.90 C ANISOU 1818 C GLY B 138 5741 6016 5301 -1769 -461 494 C ATOM 1819 O GLY B 138 20.994 23.504 22.845 1.00 46.72 O ANISOU 1819 O GLY B 138 5792 6357 5602 -1664 -476 463 O ATOM 1820 N ARG B 139 20.240 25.532 22.245 1.00 44.32 N ANISOU 1820 N ARG B 139 5861 5806 5174 -1786 -584 492 N ATOM 1821 CA ARG B 139 19.646 25.769 23.551 1.00 44.64 C ANISOU 1821 CA ARG B 139 5905 5825 5233 -1669 -724 446 C ATOM 1822 C ARG B 139 18.481 24.827 23.817 1.00 44.26 C ANISOU 1822 C ARG B 139 5833 5804 5178 -1457 -737 422 C ATOM 1823 O ARG B 139 18.280 24.416 24.965 1.00 41.69 O ANISOU 1823 O ARG B 139 5421 5532 4886 -1353 -787 381 O ATOM 1824 CB ARG B 139 19.193 27.222 23.672 1.00 47.11 C ANISOU 1824 CB ARG B 139 6441 5970 5491 -1724 -844 442 C ATOM 1825 CG ARG B 139 20.300 28.217 23.491 1.00 45.30 C ANISOU 1825 CG ARG B 139 6249 5698 5267 -1945 -840 464 C ATOM 1826 CD ARG B 139 19.772 29.624 23.588 1.00 53.95 C ANISOU 1826 CD ARG B 139 7588 6610 6301 -1986 -967 461 C ATOM 1827 NE ARG B 139 20.858 30.600 23.567 1.00 57.68 N ANISOU 1827 NE ARG B 139 8093 7037 6784 -2209 -972 477 N ATOM 1828 CZ ARG B 139 20.715 31.878 23.904 1.00 56.33 C ANISOU 1828 CZ ARG B 139 8107 6717 6578 -2276 -1093 467 C ATOM 1829 NH1 ARG B 139 19.525 32.325 24.299 1.00 48.19 N ANISOU 1829 NH1 ARG B 139 7235 5570 5504 -2126 -1215 435 N ATOM 1830 NH2 ARG B 139 21.762 32.703 23.854 1.00 54.77 N ANISOU 1830 NH2 ARG B 139 7929 6483 6398 -2495 -1088 484 N ATOM 1831 N ILE B 140 17.713 24.458 22.786 1.00 42.75 N ANISOU 1831 N ILE B 140 5727 5573 4942 -1398 -692 445 N ATOM 1832 CA ILE B 140 16.672 23.450 22.995 1.00 44.70 C ANISOU 1832 CA ILE B 140 5924 5858 5203 -1210 -692 420 C ATOM 1833 C ILE B 140 17.297 22.122 23.399 1.00 45.37 C ANISOU 1833 C ILE B 140 5790 6105 5345 -1164 -604 415 C ATOM 1834 O ILE B 140 16.809 21.446 24.312 1.00 40.93 O ANISOU 1834 O ILE B 140 5150 5592 4811 -1035 -629 380 O ATOM 1835 CB ILE B 140 15.780 23.307 21.749 1.00 45.33 C ANISOU 1835 CB ILE B 140 6136 5856 5230 -1165 -680 445 C ATOM 1836 CG1 ILE B 140 14.951 24.579 21.547 1.00 41.56 C ANISOU 1836 CG1 ILE B 140 5879 5201 4712 -1165 -809 438 C ATOM 1837 CG2 ILE B 140 14.879 22.064 21.878 1.00 40.43 C ANISOU 1837 CG2 ILE B 140 5423 5297 4643 -992 -657 419 C ATOM 1838 CD1 ILE B 140 14.004 24.512 20.380 1.00 37.14 C ANISOU 1838 CD1 ILE B 140 5466 4540 4105 -1110 -841 458 C ATOM 1839 N VAL B 141 18.404 21.742 22.748 1.00 36.82 N ANISOU 1839 N VAL B 141 4609 5100 4282 -1272 -497 444 N ATOM 1840 CA VAL B 141 19.158 20.559 23.163 1.00 43.32 C ANISOU 1840 CA VAL B 141 5213 6070 5178 -1233 -428 434 C ATOM 1841 C VAL B 141 19.650 20.698 24.606 1.00 49.62 C ANISOU 1841 C VAL B 141 5912 6912 6030 -1222 -522 401 C ATOM 1842 O VAL B 141 19.597 19.737 25.389 1.00 48.25 O ANISOU 1842 O VAL B 141 5626 6815 5890 -1109 -535 381 O ATOM 1843 CB VAL B 141 20.332 20.311 22.196 1.00 41.96 C ANISOU 1843 CB VAL B 141 4948 5960 5034 -1365 -290 459 C ATOM 1844 CG1 VAL B 141 21.266 19.220 22.753 1.00 39.98 C ANISOU 1844 CG1 VAL B 141 4449 5853 4888 -1326 -243 437 C ATOM 1845 CG2 VAL B 141 19.820 19.935 20.826 1.00 39.75 C ANISOU 1845 CG2 VAL B 141 4777 5643 4682 -1357 -192 488 C ATOM 1846 N ALA B 142 20.167 21.885 24.974 1.00 43.21 N ANISOU 1846 N ALA B 142 5155 6043 5220 -1345 -594 396 N ATOM 1847 CA ALA B 142 20.593 22.108 26.353 1.00 41.82 C ANISOU 1847 CA ALA B 142 4920 5891 5081 -1339 -706 362 C ATOM 1848 C ALA B 142 19.434 21.908 27.319 1.00 40.97 C ANISOU 1848 C ALA B 142 4895 5746 4925 -1180 -782 328 C ATOM 1849 O ALA B 142 19.611 21.367 28.418 1.00 41.18 O ANISOU 1849 O ALA B 142 4850 5829 4969 -1113 -835 303 O ATOM 1850 CB ALA B 142 21.173 23.516 26.514 1.00 39.53 C ANISOU 1850 CB ALA B 142 4711 5519 4788 -1500 -780 360 C ATOM 1851 N PHE B 143 18.241 22.344 26.918 1.00 42.19 N ANISOU 1851 N PHE B 143 5208 5801 5022 -1121 -787 324 N ATOM 1852 CA PHE B 143 17.063 22.216 27.761 1.00 43.01 C ANISOU 1852 CA PHE B 143 5384 5863 5096 -977 -834 281 C ATOM 1853 C PHE B 143 16.721 20.751 28.014 1.00 45.09 C ANISOU 1853 C PHE B 143 5534 6221 5377 -848 -769 277 C ATOM 1854 O PHE B 143 16.437 20.366 29.153 1.00 34.29 O ANISOU 1854 O PHE B 143 4159 4873 3996 -767 -800 244 O ATOM 1855 CB PHE B 143 15.920 22.987 27.106 1.00 40.14 C ANISOU 1855 CB PHE B 143 5185 5369 4699 -944 -855 273 C ATOM 1856 CG PHE B 143 14.549 22.508 27.462 1.00 39.26 C ANISOU 1856 CG PHE B 143 5101 5229 4588 -780 -849 230 C ATOM 1857 CD1 PHE B 143 13.874 23.043 28.536 1.00 40.81 C ANISOU 1857 CD1 PHE B 143 5374 5360 4772 -714 -906 168 C ATOM 1858 CD2 PHE B 143 13.899 21.583 26.669 1.00 39.10 C ANISOU 1858 CD2 PHE B 143 5036 5236 4584 -700 -781 244 C ATOM 1859 CE1 PHE B 143 12.585 22.617 28.852 1.00 36.68 C ANISOU 1859 CE1 PHE B 143 4861 4810 4267 -572 -878 118 C ATOM 1860 CE2 PHE B 143 12.623 21.162 26.975 1.00 35.65 C ANISOU 1860 CE2 PHE B 143 4608 4769 4167 -561 -772 199 C ATOM 1861 CZ PHE B 143 11.968 21.683 28.073 1.00 38.36 C ANISOU 1861 CZ PHE B 143 5008 5055 4512 -499 -813 134 C ATOM 1862 N PHE B 144 16.812 19.901 26.983 1.00 42.48 N ANISOU 1862 N PHE B 144 5127 5947 5067 -836 -676 312 N ATOM 1863 CA PHE B 144 16.587 18.473 27.209 1.00 45.88 C ANISOU 1863 CA PHE B 144 5451 6464 5517 -723 -617 310 C ATOM 1864 C PHE B 144 17.668 17.877 28.099 1.00 45.12 C ANISOU 1864 C PHE B 144 5225 6463 5456 -733 -642 309 C ATOM 1865 O PHE B 144 17.363 17.120 29.026 1.00 44.83 O ANISOU 1865 O PHE B 144 5169 6456 5407 -637 -659 291 O ATOM 1866 CB PHE B 144 16.510 17.708 25.889 1.00 34.84 C ANISOU 1866 CB PHE B 144 4011 5098 4129 -712 -517 343 C ATOM 1867 CG PHE B 144 15.171 17.806 25.219 1.00 40.06 C ANISOU 1867 CG PHE B 144 4786 5673 4761 -643 -513 336 C ATOM 1868 CD1 PHE B 144 14.185 16.860 25.463 1.00 39.21 C ANISOU 1868 CD1 PHE B 144 4655 5577 4665 -513 -488 314 C ATOM 1869 CD2 PHE B 144 14.894 18.846 24.346 1.00 37.50 C ANISOU 1869 CD2 PHE B 144 4596 5248 4406 -711 -544 349 C ATOM 1870 CE1 PHE B 144 12.950 16.967 24.853 1.00 45.88 C ANISOU 1870 CE1 PHE B 144 5584 6340 5509 -450 -500 299 C ATOM 1871 CE2 PHE B 144 13.649 18.950 23.728 1.00 39.16 C ANISOU 1871 CE2 PHE B 144 4909 5368 4604 -637 -570 338 C ATOM 1872 CZ PHE B 144 12.688 18.017 23.977 1.00 40.57 C ANISOU 1872 CZ PHE B 144 5038 5565 4812 -507 -551 310 C ATOM 1873 N SER B 145 18.938 18.196 27.824 1.00 46.61 N ANISOU 1873 N SER B 145 5325 6694 5692 -852 -647 326 N ATOM 1874 CA SER B 145 20.028 17.633 28.620 1.00 43.99 C ANISOU 1874 CA SER B 145 4848 6446 5419 -858 -695 320 C ATOM 1875 C SER B 145 19.920 18.034 30.081 1.00 43.43 C ANISOU 1875 C SER B 145 4852 6340 5309 -833 -825 288 C ATOM 1876 O SER B 145 20.191 17.221 30.973 1.00 43.84 O ANISOU 1876 O SER B 145 4851 6440 5368 -763 -876 280 O ATOM 1877 CB SER B 145 21.377 18.062 28.067 1.00 43.78 C ANISOU 1877 CB SER B 145 4700 6460 5474 -1004 -678 331 C ATOM 1878 OG SER B 145 21.767 17.195 27.032 1.00 52.74 O ANISOU 1878 OG SER B 145 5715 7664 6660 -999 -550 349 O ATOM 1879 N PHE B 146 19.540 19.287 30.346 1.00 43.95 N ANISOU 1879 N PHE B 146 5059 6312 5326 -889 -885 270 N ATOM 1880 CA PHE B 146 19.327 19.739 31.718 1.00 39.75 C ANISOU 1880 CA PHE B 146 4635 5731 4739 -864 -997 232 C ATOM 1881 C PHE B 146 18.284 18.872 32.414 1.00 43.39 C ANISOU 1881 C PHE B 146 5158 6191 5139 -718 -965 212 C ATOM 1882 O PHE B 146 18.552 18.281 33.464 1.00 43.86 O ANISOU 1882 O PHE B 146 5216 6279 5171 -671 -1024 201 O ATOM 1883 CB PHE B 146 18.904 21.208 31.711 1.00 40.05 C ANISOU 1883 CB PHE B 146 4830 5654 4733 -934 -1044 210 C ATOM 1884 CG PHE B 146 18.475 21.732 33.050 1.00 43.45 C ANISOU 1884 CG PHE B 146 5404 6016 5090 -898 -1136 160 C ATOM 1885 CD1 PHE B 146 17.245 22.349 33.200 1.00 36.77 C ANISOU 1885 CD1 PHE B 146 4714 5069 4187 -837 -1116 121 C ATOM 1886 CD2 PHE B 146 19.307 21.620 34.159 1.00 47.91 C ANISOU 1886 CD2 PHE B 146 5952 6608 5644 -923 -1248 146 C ATOM 1887 CE1 PHE B 146 16.851 22.845 34.425 1.00 48.49 C ANISOU 1887 CE1 PHE B 146 6340 6486 5599 -805 -1179 65 C ATOM 1888 CE2 PHE B 146 18.909 22.108 35.410 1.00 43.51 C ANISOU 1888 CE2 PHE B 146 5559 5976 4996 -895 -1329 97 C ATOM 1889 CZ PHE B 146 17.697 22.713 35.549 1.00 42.24 C ANISOU 1889 CZ PHE B 146 5556 5722 4773 -838 -1282 55 C ATOM 1890 N GLY B 147 17.089 18.776 31.823 1.00 39.81 N ANISOU 1890 N GLY B 147 4764 5698 4666 -648 -874 207 N ATOM 1891 CA GLY B 147 16.059 17.908 32.370 1.00 40.95 C ANISOU 1891 CA GLY B 147 4948 5841 4770 -521 -818 185 C ATOM 1892 C GLY B 147 16.544 16.491 32.583 1.00 43.43 C ANISOU 1892 C GLY B 147 5152 6248 5101 -467 -795 212 C ATOM 1893 O GLY B 147 16.308 15.892 33.634 1.00 38.66 O ANISOU 1893 O GLY B 147 4600 5646 4444 -403 -810 196 O ATOM 1894 N GLY B 148 17.243 15.938 31.587 1.00 42.32 N ANISOU 1894 N GLY B 148 4872 6177 5029 -493 -754 252 N ATOM 1895 CA GLY B 148 17.838 14.621 31.756 1.00 33.17 C ANISOU 1895 CA GLY B 148 3601 5101 3902 -438 -745 274 C ATOM 1896 C GLY B 148 18.753 14.548 32.966 1.00 35.59 C ANISOU 1896 C GLY B 148 3899 5425 4199 -451 -873 266 C ATOM 1897 O GLY B 148 18.716 13.578 33.725 1.00 40.56 O ANISOU 1897 O GLY B 148 4542 6072 4796 -371 -898 270 O ATOM 1898 N ALA B 149 19.586 15.574 33.165 1.00 35.24 N ANISOU 1898 N ALA B 149 3843 5367 4180 -555 -969 257 N ATOM 1899 CA ALA B 149 20.511 15.544 34.290 1.00 38.39 C ANISOU 1899 CA ALA B 149 4232 5775 4579 -572 -1120 247 C ATOM 1900 C ALA B 149 19.757 15.663 35.615 1.00 44.43 C ANISOU 1900 C ALA B 149 5199 6470 5214 -519 -1177 219 C ATOM 1901 O ALA B 149 20.096 14.979 36.588 1.00 41.89 O ANISOU 1901 O ALA B 149 4911 6154 4852 -470 -1268 220 O ATOM 1902 CB ALA B 149 21.557 16.649 34.145 1.00 37.67 C ANISOU 1902 CB ALA B 149 4075 5680 4556 -709 -1209 238 C ATOM 1903 N LEU B 150 18.725 16.517 35.662 1.00 38.99 N ANISOU 1903 N LEU B 150 4654 5705 4456 -525 -1124 190 N ATOM 1904 CA LEU B 150 17.874 16.602 36.842 1.00 44.05 C ANISOU 1904 CA LEU B 150 5489 6276 4973 -471 -1132 152 C ATOM 1905 C LEU B 150 17.333 15.234 37.222 1.00 45.82 C ANISOU 1905 C LEU B 150 5734 6525 5151 -366 -1061 165 C ATOM 1906 O LEU B 150 17.372 14.845 38.394 1.00 48.19 O ANISOU 1906 O LEU B 150 6156 6797 5355 -335 -1122 155 O ATOM 1907 CB LEU B 150 16.718 17.565 36.599 1.00 42.26 C ANISOU 1907 CB LEU B 150 5373 5968 4714 -471 -1049 111 C ATOM 1908 CG LEU B 150 17.014 19.032 36.793 1.00 43.24 C ANISOU 1908 CG LEU B 150 5580 6022 4825 -563 -1140 81 C ATOM 1909 CD1 LEU B 150 15.760 19.841 36.542 1.00 48.71 C ANISOU 1909 CD1 LEU B 150 6381 6627 5498 -533 -1056 35 C ATOM 1910 CD2 LEU B 150 17.503 19.226 38.190 1.00 38.72 C ANISOU 1910 CD2 LEU B 150 5134 5416 4163 -582 -1267 55 C ATOM 1911 N CYS B 151 16.828 14.486 36.237 1.00 40.97 N ANISOU 1911 N CYS B 151 5018 5952 4595 -315 -936 188 N ATOM 1912 CA CYS B 151 16.268 13.171 36.528 1.00 42.89 C ANISOU 1912 CA CYS B 151 5284 6213 4802 -223 -861 201 C ATOM 1913 C CYS B 151 17.335 12.224 37.041 1.00 50.77 C ANISOU 1913 C CYS B 151 6232 7255 5802 -201 -968 235 C ATOM 1914 O CYS B 151 17.119 11.512 38.027 1.00 57.73 O ANISOU 1914 O CYS B 151 7235 8108 6590 -151 -988 237 O ATOM 1915 CB CYS B 151 15.600 12.588 35.289 1.00 39.64 C ANISOU 1915 CB CYS B 151 4767 5833 4463 -182 -725 217 C ATOM 1916 SG CYS B 151 14.069 13.410 34.887 1.00 47.31 S ANISOU 1916 SG CYS B 151 5816 6731 5430 -171 -612 168 S ATOM 1917 N VAL B 152 18.500 12.199 36.388 1.00 44.19 N ANISOU 1917 N VAL B 152 5226 6485 5079 -239 -1037 260 N ATOM 1918 CA VAL B 152 19.576 11.331 36.861 1.00 44.02 C ANISOU 1918 CA VAL B 152 5134 6501 5090 -207 -1160 283 C ATOM 1919 C VAL B 152 19.956 11.690 38.299 1.00 46.31 C ANISOU 1919 C VAL B 152 5579 6734 5283 -224 -1328 267 C ATOM 1920 O VAL B 152 20.052 10.820 39.167 1.00 46.17 O ANISOU 1920 O VAL B 152 5656 6694 5194 -162 -1400 281 O ATOM 1921 CB VAL B 152 20.787 11.403 35.915 1.00 43.94 C ANISOU 1921 CB VAL B 152 4890 6566 5238 -255 -1195 295 C ATOM 1922 CG1 VAL B 152 22.028 10.756 36.569 1.00 37.88 C ANISOU 1922 CG1 VAL B 152 4036 5825 4530 -227 -1367 302 C ATOM 1923 CG2 VAL B 152 20.456 10.723 34.615 1.00 39.67 C ANISOU 1923 CG2 VAL B 152 4229 6076 4767 -219 -1034 314 C ATOM 1924 N GLU B 153 20.160 12.983 38.569 1.00 47.90 N ANISOU 1924 N GLU B 153 5832 6898 5468 -312 -1398 237 N ATOM 1925 CA GLU B 153 20.477 13.430 39.923 1.00 58.42 C ANISOU 1925 CA GLU B 153 7339 8165 6694 -337 -1562 215 C ATOM 1926 C GLU B 153 19.396 13.014 40.920 1.00 66.19 C ANISOU 1926 C GLU B 153 8573 9077 7501 -276 -1499 202 C ATOM 1927 O GLU B 153 19.702 12.644 42.059 1.00 68.91 O ANISOU 1927 O GLU B 153 9071 9375 7739 -256 -1627 204 O ATOM 1928 CB GLU B 153 20.669 14.949 39.924 1.00 62.02 C ANISOU 1928 CB GLU B 153 7825 8582 7157 -444 -1616 180 C ATOM 1929 CG GLU B 153 20.753 15.603 41.294 1.00 80.67 C ANISOU 1929 CG GLU B 153 10412 10856 9384 -477 -1762 145 C ATOM 1930 CD GLU B 153 22.110 15.430 41.971 1.00100.29 C ANISOU 1930 CD GLU B 153 12853 13347 11906 -504 -2008 153 C ATOM 1931 OE1 GLU B 153 22.720 14.343 41.847 1.00102.51 O ANISOU 1931 OE1 GLU B 153 13006 13682 12262 -445 -2063 186 O ATOM 1932 OE2 GLU B 153 22.567 16.393 42.632 1.00108.98 O ANISOU 1932 OE2 GLU B 153 14048 14390 12969 -582 -2158 122 O ATOM 1933 N SER B 154 18.128 13.038 40.499 1.00 60.26 N ANISOU 1933 N SER B 154 7866 8311 6719 -248 -1301 186 N ATOM 1934 CA SER B 154 17.031 12.724 41.410 1.00 58.15 C ANISOU 1934 CA SER B 154 7823 7975 6299 -205 -1204 162 C ATOM 1935 C SER B 154 17.027 11.249 41.796 1.00 56.12 C ANISOU 1935 C SER B 154 7607 7726 5991 -132 -1196 202 C ATOM 1936 O SER B 154 16.931 10.907 42.984 1.00 53.21 O ANISOU 1936 O SER B 154 7455 7292 5472 -120 -1246 199 O ATOM 1937 CB SER B 154 15.698 13.120 40.780 1.00 49.05 C ANISOU 1937 CB SER B 154 6664 6805 5166 -192 -999 125 C ATOM 1938 OG SER B 154 15.535 14.525 40.845 1.00 50.36 O ANISOU 1938 OG SER B 154 6887 6923 5326 -249 -1019 76 O ATOM 1939 N VAL B 155 17.123 10.359 40.808 1.00 47.39 N ANISOU 1939 N VAL B 155 6316 6689 4999 -87 -1134 241 N ATOM 1940 CA VAL B 155 17.183 8.932 41.113 1.00 50.65 C ANISOU 1940 CA VAL B 155 6766 7103 5375 -16 -1139 282 C ATOM 1941 C VAL B 155 18.427 8.607 41.933 1.00 55.98 C ANISOU 1941 C VAL B 155 7484 7764 6023 -7 -1374 307 C ATOM 1942 O VAL B 155 18.382 7.793 42.861 1.00 57.39 O ANISOU 1942 O VAL B 155 7843 7885 6079 33 -1429 328 O ATOM 1943 CB VAL B 155 17.130 8.112 39.816 1.00 49.60 C ANISOU 1943 CB VAL B 155 6420 7045 5381 30 -1038 312 C ATOM 1944 CG1 VAL B 155 17.190 6.635 40.134 1.00 53.67 C ANISOU 1944 CG1 VAL B 155 6983 7549 5858 105 -1048 352 C ATOM 1945 CG2 VAL B 155 15.860 8.436 39.066 1.00 42.75 C ANISOU 1945 CG2 VAL B 155 5528 6177 4537 23 -835 284 C ATOM 1946 N ASP B 156 19.551 9.245 41.620 1.00 62.00 N ANISOU 1946 N ASP B 156 8089 8568 6900 -49 -1524 303 N ATOM 1947 CA ASP B 156 20.773 8.936 42.346 1.00 67.61 C ANISOU 1947 CA ASP B 156 8806 9264 7619 -35 -1771 319 C ATOM 1948 C ASP B 156 20.657 9.334 43.809 1.00 74.59 C ANISOU 1948 C ASP B 156 9988 10045 8308 -62 -1894 302 C ATOM 1949 O ASP B 156 21.160 8.632 44.691 1.00 81.94 O ANISOU 1949 O ASP B 156 11050 10924 9161 -20 -2062 326 O ATOM 1950 CB ASP B 156 21.968 9.632 41.701 1.00 73.05 C ANISOU 1950 CB ASP B 156 9247 10019 8491 -91 -1891 307 C ATOM 1951 CG ASP B 156 23.266 9.285 42.387 1.00 91.14 C ANISOU 1951 CG ASP B 156 11501 12296 10832 -71 -2162 314 C ATOM 1952 OD1 ASP B 156 23.710 8.124 42.251 1.00 99.97 O ANISOU 1952 OD1 ASP B 156 12531 13436 12018 17 -2213 342 O ATOM 1953 OD2 ASP B 156 23.831 10.159 43.080 1.00 94.77 O ANISOU 1953 OD2 ASP B 156 12026 12716 11267 -138 -2336 289 O ATOM 1954 N LYS B 157 19.999 10.457 44.089 1.00 72.85 N ANISOU 1954 N LYS B 157 9894 9783 8001 -128 -1818 258 N ATOM 1955 CA LYS B 157 19.835 10.938 45.453 1.00 64.86 C ANISOU 1955 CA LYS B 157 9185 8667 6791 -161 -1911 231 C ATOM 1956 C LYS B 157 18.510 10.506 46.059 1.00 64.05 C ANISOU 1956 C LYS B 157 9334 8498 6506 -135 -1714 219 C ATOM 1957 O LYS B 157 18.096 11.058 47.082 1.00 72.71 O ANISOU 1957 O LYS B 157 10695 9504 7426 -171 -1714 181 O ATOM 1958 CB LYS B 157 19.991 12.453 45.492 1.00 58.84 C ANISOU 1958 CB LYS B 157 8427 7886 6042 -251 -1958 180 C ATOM 1959 CG LYS B 157 21.335 12.841 44.932 1.00 70.32 C ANISOU 1959 CG LYS B 157 9633 9403 7682 -293 -2145 190 C ATOM 1960 CD LYS B 157 21.814 14.183 45.389 1.00 78.70 C ANISOU 1960 CD LYS B 157 10761 10417 8726 -390 -2288 147 C ATOM 1961 CE LYS B 157 23.300 14.320 45.075 1.00 85.15 C ANISOU 1961 CE LYS B 157 11340 11285 9726 -433 -2510 157 C ATOM 1962 NZ LYS B 157 24.096 13.150 45.586 1.00 88.16 N ANISOU 1962 NZ LYS B 157 11703 11667 10125 -358 -2699 191 N ATOM 1963 N GLU B 158 17.845 9.527 45.444 1.00 55.61 N ANISOU 1963 N GLU B 158 8185 7466 5478 -78 -1538 247 N ATOM 1964 CA GLU B 158 16.690 8.859 46.028 1.00 57.12 C ANISOU 1964 CA GLU B 158 8593 7594 5514 -56 -1355 242 C ATOM 1965 C GLU B 158 15.519 9.824 46.187 1.00 60.61 C ANISOU 1965 C GLU B 158 9137 7998 5892 -100 -1155 171 C ATOM 1966 O GLU B 158 14.974 10.028 47.274 1.00 65.77 O ANISOU 1966 O GLU B 158 10068 8561 6360 -126 -1101 135 O ATOM 1967 CB GLU B 158 17.066 8.207 47.356 1.00 61.94 C ANISOU 1967 CB GLU B 158 9495 8110 5928 -46 -1503 270 C ATOM 1968 CG GLU B 158 17.842 6.922 47.181 1.00 77.88 C ANISOU 1968 CG GLU B 158 11436 10149 8006 24 -1641 339 C ATOM 1969 CD GLU B 158 18.861 6.716 48.274 1.00 95.06 C ANISOU 1969 CD GLU B 158 13804 12246 10068 32 -1935 364 C ATOM 1970 OE1 GLU B 158 20.019 7.134 48.071 1.00103.86 O ANISOU 1970 OE1 GLU B 158 14751 13399 11312 31 -2162 365 O ATOM 1971 OE2 GLU B 158 18.502 6.159 49.337 1.00 94.99 O ANISOU 1971 OE2 GLU B 158 14119 12131 9842 34 -1941 381 O ATOM 1972 N MET B 159 15.164 10.434 45.067 1.00 57.00 N ANISOU 1972 N MET B 159 8456 7605 5595 -105 -1049 147 N ATOM 1973 CA MET B 159 13.978 11.265 44.918 1.00 53.23 C ANISOU 1973 CA MET B 159 8007 7101 5118 -124 -852 77 C ATOM 1974 C MET B 159 13.319 10.913 43.586 1.00 51.06 C ANISOU 1974 C MET B 159 7493 6896 5011 -88 -695 85 C ATOM 1975 O MET B 159 13.022 11.776 42.760 1.00 50.84 O ANISOU 1975 O MET B 159 7330 6890 5096 -101 -650 54 O ATOM 1976 CB MET B 159 14.335 12.747 44.998 1.00 51.08 C ANISOU 1976 CB MET B 159 7744 6805 4858 -179 -949 30 C ATOM 1977 CG MET B 159 14.994 13.126 46.306 1.00 53.71 C ANISOU 1977 CG MET B 159 8323 7061 5022 -220 -1122 18 C ATOM 1978 SD MET B 159 15.672 14.802 46.360 1.00 65.83 S ANISOU 1978 SD MET B 159 9857 8569 6588 -295 -1285 -28 S ATOM 1979 CE MET B 159 16.840 14.739 45.008 1.00 73.88 C ANISOU 1979 CE MET B 159 10525 9703 7841 -308 -1421 35 C ATOM 1980 N GLN B 160 13.135 9.605 43.366 1.00 48.66 N ANISOU 1980 N GLN B 160 7152 6617 4718 -43 -631 131 N ATOM 1981 CA GLN B 160 12.521 9.081 42.152 1.00 43.96 C ANISOU 1981 CA GLN B 160 6354 6080 4268 -7 -495 142 C ATOM 1982 C GLN B 160 11.167 9.730 41.853 1.00 48.70 C ANISOU 1982 C GLN B 160 6939 6653 4912 -11 -303 69 C ATOM 1983 O GLN B 160 10.764 9.816 40.689 1.00 53.79 O ANISOU 1983 O GLN B 160 7397 7340 5700 7 -241 65 O ATOM 1984 CB GLN B 160 12.399 7.553 42.275 1.00 43.93 C ANISOU 1984 CB GLN B 160 6384 6077 4229 35 -448 192 C ATOM 1985 CG GLN B 160 11.796 6.853 41.043 1.00 66.63 C ANISOU 1985 CG GLN B 160 9066 9006 7246 73 -320 206 C ATOM 1986 CD GLN B 160 12.510 5.554 40.660 1.00 81.64 C ANISOU 1986 CD GLN B 160 10892 10945 9182 120 -393 277 C ATOM 1987 OE1 GLN B 160 13.697 5.560 40.324 1.00 85.57 O ANISOU 1987 OE1 GLN B 160 11283 11490 9739 133 -553 312 O ATOM 1988 NE2 GLN B 160 11.780 4.437 40.695 1.00 85.17 N ANISOU 1988 NE2 GLN B 160 11388 11368 9605 144 -268 291 N ATOM 1989 N VAL B 161 10.464 10.218 42.876 1.00 49.23 N ANISOU 1989 N VAL B 161 7200 6642 4861 -33 -213 6 N ATOM 1990 CA VAL B 161 9.185 10.886 42.647 1.00 48.17 C ANISOU 1990 CA VAL B 161 7036 6474 4791 -27 -35 -79 C ATOM 1991 C VAL B 161 9.326 12.046 41.664 1.00 58.50 C ANISOU 1991 C VAL B 161 8185 7807 6236 -30 -105 -100 C ATOM 1992 O VAL B 161 8.376 12.372 40.939 1.00 61.37 O ANISOU 1992 O VAL B 161 8436 8164 6718 -4 4 -147 O ATOM 1993 CB VAL B 161 8.590 11.368 43.985 1.00 54.80 C ANISOU 1993 CB VAL B 161 8124 7223 5476 -54 64 -155 C ATOM 1994 CG1 VAL B 161 9.408 12.517 44.556 1.00 53.76 C ANISOU 1994 CG1 VAL B 161 8109 7056 5261 -91 -101 -172 C ATOM 1995 CG2 VAL B 161 7.149 11.787 43.811 1.00 56.32 C ANISOU 1995 CG2 VAL B 161 8269 7378 5754 -36 282 -252 C ATOM 1996 N LEU B 162 10.498 12.687 41.614 1.00 60.09 N ANISOU 1996 N LEU B 162 8378 8027 6427 -64 -293 -66 N ATOM 1997 CA LEU B 162 10.622 13.901 40.817 1.00 57.10 C ANISOU 1997 CA LEU B 162 7896 7649 6151 -84 -354 -89 C ATOM 1998 C LEU B 162 10.653 13.622 39.321 1.00 51.11 C ANISOU 1998 C LEU B 162 6915 6957 5549 -65 -349 -46 C ATOM 1999 O LEU B 162 10.314 14.515 38.534 1.00 49.16 O ANISOU 1999 O LEU B 162 6595 6692 5391 -70 -347 -73 O ATOM 2000 CB LEU B 162 11.869 14.680 41.223 1.00 49.00 C ANISOU 2000 CB LEU B 162 6928 6618 5073 -144 -549 -69 C ATOM 2001 CG LEU B 162 11.748 15.480 42.521 1.00 55.78 C ANISOU 2001 CG LEU B 162 8020 7388 5788 -172 -571 -133 C ATOM 2002 CD1 LEU B 162 13.060 16.198 42.825 1.00 47.24 C ANISOU 2002 CD1 LEU B 162 6973 6302 4672 -239 -790 -109 C ATOM 2003 CD2 LEU B 162 10.592 16.472 42.435 1.00 50.84 C ANISOU 2003 CD2 LEU B 162 7428 6693 5198 -155 -443 -224 C ATOM 2004 N VAL B 163 11.008 12.402 38.919 1.00 43.30 N ANISOU 2004 N VAL B 163 5836 6031 4584 -42 -346 17 N ATOM 2005 CA VAL B 163 11.237 12.101 37.504 1.00 44.42 C ANISOU 2005 CA VAL B 163 5787 6236 4855 -31 -355 61 C ATOM 2006 C VAL B 163 10.028 12.488 36.650 1.00 53.90 C ANISOU 2006 C VAL B 163 6921 7407 6153 -4 -247 16 C ATOM 2007 O VAL B 163 10.137 13.309 35.729 1.00 49.78 O ANISOU 2007 O VAL B 163 6326 6882 5706 -25 -295 16 O ATOM 2008 CB VAL B 163 11.602 10.618 37.330 1.00 36.47 C ANISOU 2008 CB VAL B 163 4719 5285 3851 4 -342 120 C ATOM 2009 CG1 VAL B 163 11.621 10.234 35.836 1.00 39.63 C ANISOU 2009 CG1 VAL B 163 4942 5740 4376 21 -316 153 C ATOM 2010 CG2 VAL B 163 12.934 10.360 37.954 1.00 37.54 C ANISOU 2010 CG2 VAL B 163 4886 5448 3929 -15 -490 165 C ATOM 2011 N SER B 164 8.859 11.891 36.923 1.00 54.50 N ANISOU 2011 N SER B 164 7020 7454 6234 40 -106 -25 N ATOM 2012 CA SER B 164 7.714 12.174 36.056 1.00 50.12 C ANISOU 2012 CA SER B 164 6376 6869 5799 74 -27 -72 C ATOM 2013 C SER B 164 7.173 13.582 36.273 1.00 44.32 C ANISOU 2013 C SER B 164 5696 6058 5084 71 -34 -148 C ATOM 2014 O SER B 164 6.516 14.131 35.381 1.00 43.10 O ANISOU 2014 O SER B 164 5465 5871 5040 96 -35 -179 O ATOM 2015 CB SER B 164 6.604 11.133 36.233 1.00 47.13 C ANISOU 2015 CB SER B 164 5979 6479 5448 114 127 -101 C ATOM 2016 OG SER B 164 6.175 11.060 37.569 1.00 61.29 O ANISOU 2016 OG SER B 164 7913 8228 7145 107 223 -150 O ATOM 2017 N ARG B 165 7.468 14.210 37.409 1.00 38.34 N ANISOU 2017 N ARG B 165 5082 5263 4221 44 -55 -180 N ATOM 2018 CA ARG B 165 7.171 15.636 37.510 1.00 42.82 C ANISOU 2018 CA ARG B 165 5705 5756 4808 38 -91 -247 C ATOM 2019 C ARG B 165 8.021 16.452 36.539 1.00 44.20 C ANISOU 2019 C ARG B 165 5824 5943 5029 -4 -241 -198 C ATOM 2020 O ARG B 165 7.505 17.331 35.834 1.00 49.89 O ANISOU 2020 O ARG B 165 6514 6607 5834 11 -264 -233 O ATOM 2021 CB ARG B 165 7.381 16.106 38.932 1.00 46.38 C ANISOU 2021 CB ARG B 165 6341 6159 5121 12 -88 -291 C ATOM 2022 CG ARG B 165 6.512 15.367 39.878 1.00 49.49 C ANISOU 2022 CG ARG B 165 6816 6530 5457 39 83 -343 C ATOM 2023 CD ARG B 165 6.634 15.944 41.237 1.00 51.81 C ANISOU 2023 CD ARG B 165 7323 6760 5603 11 94 -396 C ATOM 2024 NE ARG B 165 5.894 15.126 42.177 1.00 61.46 N ANISOU 2024 NE ARG B 165 8650 7959 6743 21 274 -437 N ATOM 2025 CZ ARG B 165 5.932 15.305 43.489 1.00 59.34 C ANISOU 2025 CZ ARG B 165 8605 7633 6308 -8 319 -479 C ATOM 2026 NH1 ARG B 165 6.691 16.274 44.000 1.00 51.30 N ANISOU 2026 NH1 ARG B 165 7719 6576 5196 -43 180 -487 N ATOM 2027 NH2 ARG B 165 5.218 14.510 44.274 1.00 56.42 N ANISOU 2027 NH2 ARG B 165 8338 7238 5861 -10 505 -514 N ATOM 2028 N ILE B 166 9.328 16.166 36.486 1.00 41.24 N ANISOU 2028 N ILE B 166 5434 5633 4603 -59 -343 -121 N ATOM 2029 CA ILE B 166 10.231 16.919 35.620 1.00 45.27 C ANISOU 2029 CA ILE B 166 5892 6156 5153 -121 -464 -76 C ATOM 2030 C ILE B 166 9.815 16.769 34.167 1.00 47.95 C ANISOU 2030 C ILE B 166 6112 6506 5599 -100 -441 -51 C ATOM 2031 O ILE B 166 9.825 17.740 33.400 1.00 45.11 O ANISOU 2031 O ILE B 166 5757 6100 5284 -130 -500 -53 O ATOM 2032 CB ILE B 166 11.683 16.469 35.843 1.00 40.80 C ANISOU 2032 CB ILE B 166 5297 5666 4540 -179 -560 -7 C ATOM 2033 CG1 ILE B 166 12.185 16.946 37.220 1.00 36.93 C ANISOU 2033 CG1 ILE B 166 4951 5140 3940 -214 -635 -34 C ATOM 2034 CG2 ILE B 166 12.567 16.954 34.684 1.00 34.36 C ANISOU 2034 CG2 ILE B 166 4381 4881 3793 -247 -637 44 C ATOM 2035 CD1 ILE B 166 13.407 16.181 37.730 1.00 37.94 C ANISOU 2035 CD1 ILE B 166 5060 5334 4022 -241 -730 22 C ATOM 2036 N ALA B 167 9.411 15.555 33.775 1.00 42.96 N ANISOU 2036 N ALA B 167 5397 5924 5003 -51 -360 -29 N ATOM 2037 CA ALA B 167 8.919 15.342 32.419 1.00 41.83 C ANISOU 2037 CA ALA B 167 5161 5781 4952 -27 -342 -12 C ATOM 2038 C ALA B 167 7.730 16.248 32.117 1.00 46.26 C ANISOU 2038 C ALA B 167 5750 6243 5583 15 -337 -83 C ATOM 2039 O ALA B 167 7.658 16.855 31.039 1.00 45.39 O ANISOU 2039 O ALA B 167 5627 6093 5524 2 -401 -69 O ATOM 2040 CB ALA B 167 8.544 13.879 32.231 1.00 37.80 C ANISOU 2040 CB ALA B 167 4574 5325 4464 23 -253 8 C ATOM 2041 N ALA B 168 6.798 16.368 33.070 1.00 42.78 N ANISOU 2041 N ALA B 168 5354 5752 5146 65 -262 -163 N ATOM 2042 CA ALA B 168 5.651 17.252 32.890 1.00 45.39 C ANISOU 2042 CA ALA B 168 5696 5982 5566 118 -258 -247 C ATOM 2043 C ALA B 168 6.078 18.713 32.785 1.00 46.62 C ANISOU 2043 C ALA B 168 5944 6067 5704 78 -374 -256 C ATOM 2044 O ALA B 168 5.621 19.430 31.885 1.00 46.10 O ANISOU 2044 O ALA B 168 5873 5928 5715 99 -444 -271 O ATOM 2045 CB ALA B 168 4.656 17.065 34.031 1.00 32.61 C ANISOU 2045 CB ALA B 168 4104 4330 3957 171 -126 -341 C ATOM 2046 N TRP B 169 6.938 19.184 33.709 1.00 39.45 N ANISOU 2046 N TRP B 169 5132 5166 4690 20 -409 -249 N ATOM 2047 CA TRP B 169 7.414 20.570 33.615 1.00 39.07 C ANISOU 2047 CA TRP B 169 5178 5045 4622 -32 -524 -255 C ATOM 2048 C TRP B 169 8.102 20.828 32.278 1.00 43.66 C ANISOU 2048 C TRP B 169 5723 5638 5229 -95 -618 -175 C ATOM 2049 O TRP B 169 7.952 21.906 31.691 1.00 50.50 O ANISOU 2049 O TRP B 169 6651 6413 6126 -111 -701 -186 O ATOM 2050 CB TRP B 169 8.371 20.916 34.762 1.00 43.81 C ANISOU 2050 CB TRP B 169 5882 5659 5104 -100 -564 -252 C ATOM 2051 CG TRP B 169 7.848 20.567 36.102 1.00 48.04 C ANISOU 2051 CG TRP B 169 6490 6186 5579 -55 -465 -320 C ATOM 2052 CD1 TRP B 169 6.540 20.472 36.465 1.00 45.21 C ANISOU 2052 CD1 TRP B 169 6132 5775 5271 31 -343 -410 C ATOM 2053 CD2 TRP B 169 8.613 20.237 37.261 1.00 49.34 C ANISOU 2053 CD2 TRP B 169 6744 6387 5616 -99 -475 -306 C ATOM 2054 NE1 TRP B 169 6.442 20.103 37.778 1.00 52.52 N ANISOU 2054 NE1 TRP B 169 7155 6704 6096 34 -253 -452 N ATOM 2055 CE2 TRP B 169 7.699 19.950 38.294 1.00 53.17 C ANISOU 2055 CE2 TRP B 169 7308 6836 6058 -42 -343 -386 C ATOM 2056 CE3 TRP B 169 9.980 20.147 37.527 1.00 55.75 C ANISOU 2056 CE3 TRP B 169 7576 7254 6352 -181 -586 -238 C ATOM 2057 CZ2 TRP B 169 8.107 19.582 39.577 1.00 54.44 C ANISOU 2057 CZ2 TRP B 169 7602 7006 6077 -68 -325 -393 C ATOM 2058 CZ3 TRP B 169 10.388 19.783 38.806 1.00 59.86 C ANISOU 2058 CZ3 TRP B 169 8210 7785 6751 -197 -592 -247 C ATOM 2059 CH2 TRP B 169 9.453 19.511 39.815 1.00 58.29 C ANISOU 2059 CH2 TRP B 169 8123 7540 6484 -142 -465 -320 C ATOM 2060 N MET B 170 8.853 19.847 31.773 1.00 41.67 N ANISOU 2060 N MET B 170 5383 5490 4961 -133 -602 -96 N ATOM 2061 CA MET B 170 9.517 20.028 30.487 1.00 37.62 C ANISOU 2061 CA MET B 170 4842 4989 4464 -201 -660 -24 C ATOM 2062 C MET B 170 8.503 20.102 29.358 1.00 44.16 C ANISOU 2062 C MET B 170 5660 5750 5368 -143 -668 -36 C ATOM 2063 O MET B 170 8.570 21.001 28.509 1.00 41.31 O ANISOU 2063 O MET B 170 5369 5312 5014 -184 -750 -18 O ATOM 2064 CB MET B 170 10.508 18.898 30.250 1.00 39.18 C ANISOU 2064 CB MET B 170 4938 5310 4637 -241 -623 47 C ATOM 2065 CG MET B 170 11.714 18.971 31.169 1.00 39.52 C ANISOU 2065 CG MET B 170 4988 5408 4620 -312 -662 67 C ATOM 2066 SD MET B 170 12.710 17.504 30.934 1.00 40.82 S ANISOU 2066 SD MET B 170 5012 5708 4788 -323 -619 133 S ATOM 2067 CE MET B 170 13.272 17.750 29.228 1.00 39.27 C ANISOU 2067 CE MET B 170 4764 5522 4633 -401 -619 191 C ATOM 2068 N ALA B 171 7.540 19.173 29.350 1.00 37.85 N ANISOU 2068 N ALA B 171 4786 4970 4627 -51 -593 -68 N ATOM 2069 CA ALA B 171 6.554 19.124 28.275 1.00 42.46 C ANISOU 2069 CA ALA B 171 5347 5490 5296 9 -619 -83 C ATOM 2070 C ALA B 171 5.715 20.392 28.240 1.00 44.45 C ANISOU 2070 C ALA B 171 5679 5602 5607 53 -702 -152 C ATOM 2071 O ALA B 171 5.424 20.932 27.159 1.00 41.10 O ANISOU 2071 O ALA B 171 5305 5095 5218 56 -799 -137 O ATOM 2072 CB ALA B 171 5.649 17.897 28.446 1.00 38.38 C ANISOU 2072 CB ALA B 171 4723 5016 4845 93 -521 -116 C ATOM 2073 N THR B 172 5.300 20.866 29.419 1.00 42.12 N ANISOU 2073 N THR B 172 5411 5272 5321 93 -667 -231 N ATOM 2074 CA THR B 172 4.552 22.111 29.508 1.00 47.87 C ANISOU 2074 CA THR B 172 6216 5861 6111 144 -741 -309 C ATOM 2075 C THR B 172 5.373 23.285 28.991 1.00 50.52 C ANISOU 2075 C THR B 172 6684 6128 6383 56 -870 -258 C ATOM 2076 O THR B 172 4.877 24.106 28.208 1.00 52.73 O ANISOU 2076 O THR B 172 7032 6287 6715 83 -980 -272 O ATOM 2077 CB THR B 172 4.116 22.351 30.952 1.00 50.87 C ANISOU 2077 CB THR B 172 6615 6224 6489 189 -654 -405 C ATOM 2078 OG1 THR B 172 3.119 21.382 31.302 1.00 55.60 O ANISOU 2078 OG1 THR B 172 7097 6857 7171 272 -528 -465 O ATOM 2079 CG2 THR B 172 3.548 23.730 31.096 1.00 35.75 C ANISOU 2079 CG2 THR B 172 4793 4163 4627 235 -734 -486 C ATOM 2080 N TYR B 173 6.642 23.379 29.402 1.00 37.39 N ANISOU 2080 N TYR B 173 5062 4533 4611 -55 -866 -200 N ATOM 2081 CA TYR B 173 7.466 24.466 28.879 1.00 38.74 C ANISOU 2081 CA TYR B 173 5352 4639 4728 -159 -976 -150 C ATOM 2082 C TYR B 173 7.688 24.297 27.382 1.00 48.91 C ANISOU 2082 C TYR B 173 6648 5920 6016 -206 -1021 -71 C ATOM 2083 O TYR B 173 7.580 25.264 26.617 1.00 53.46 O ANISOU 2083 O TYR B 173 7346 6375 6591 -234 -1127 -57 O ATOM 2084 CB TYR B 173 8.803 24.555 29.624 1.00 34.97 C ANISOU 2084 CB TYR B 173 4892 4239 4156 -275 -966 -110 C ATOM 2085 CG TYR B 173 9.540 25.829 29.303 1.00 37.38 C ANISOU 2085 CG TYR B 173 5326 4458 4417 -389 -1073 -80 C ATOM 2086 CD1 TYR B 173 9.387 26.967 30.094 1.00 46.57 C ANISOU 2086 CD1 TYR B 173 6611 5516 5566 -388 -1137 -142 C ATOM 2087 CD2 TYR B 173 10.362 25.914 28.180 1.00 39.68 C ANISOU 2087 CD2 TYR B 173 5631 4764 4681 -502 -1100 8 C ATOM 2088 CE1 TYR B 173 10.051 28.164 29.773 1.00 51.51 C ANISOU 2088 CE1 TYR B 173 7369 6049 6152 -502 -1240 -113 C ATOM 2089 CE2 TYR B 173 11.017 27.091 27.852 1.00 54.27 C ANISOU 2089 CE2 TYR B 173 7608 6522 6488 -622 -1186 37 C ATOM 2090 CZ TYR B 173 10.860 28.212 28.649 1.00 57.43 C ANISOU 2090 CZ TYR B 173 8127 6815 6877 -623 -1262 -21 C ATOM 2091 OH TYR B 173 11.521 29.369 28.314 1.00 65.69 O ANISOU 2091 OH TYR B 173 9310 7767 7884 -752 -1350 11 O ATOM 2092 N LEU B 174 7.985 23.072 26.942 1.00 47.41 N ANISOU 2092 N LEU B 174 6348 5846 5819 -215 -943 -19 N ATOM 2093 CA LEU B 174 8.194 22.829 25.517 1.00 47.08 C ANISOU 2093 CA LEU B 174 6329 5798 5762 -260 -969 51 C ATOM 2094 C LEU B 174 6.962 23.228 24.704 1.00 51.89 C ANISOU 2094 C LEU B 174 7004 6272 6440 -171 -1064 16 C ATOM 2095 O LEU B 174 7.082 23.915 23.679 1.00 44.17 O ANISOU 2095 O LEU B 174 6158 5197 5427 -224 -1158 59 O ATOM 2096 CB LEU B 174 8.558 21.355 25.287 1.00 37.23 C ANISOU 2096 CB LEU B 174 4948 4692 4507 -258 -862 93 C ATOM 2097 CG LEU B 174 8.698 20.828 23.861 1.00 46.47 C ANISOU 2097 CG LEU B 174 6131 5869 5656 -290 -858 156 C ATOM 2098 CD1 LEU B 174 9.604 21.722 23.034 1.00 46.16 C ANISOU 2098 CD1 LEU B 174 6221 5778 5540 -426 -903 218 C ATOM 2099 CD2 LEU B 174 9.258 19.435 23.902 1.00 45.51 C ANISOU 2099 CD2 LEU B 174 5876 5892 5523 -293 -744 188 C ATOM 2100 N ASN B 175 5.765 22.859 25.180 1.00 48.03 N ANISOU 2100 N ASN B 175 6431 5764 6054 -37 -1047 -66 N ATOM 2101 CA ASN B 175 4.548 23.120 24.418 1.00 48.72 C ANISOU 2101 CA ASN B 175 6546 5726 6239 62 -1151 -109 C ATOM 2102 C ASN B 175 4.111 24.578 24.475 1.00 52.53 C ANISOU 2102 C ASN B 175 7161 6043 6755 91 -1284 -159 C ATOM 2103 O ASN B 175 3.551 25.084 23.496 1.00 58.31 O ANISOU 2103 O ASN B 175 7988 6646 7523 125 -1423 -156 O ATOM 2104 CB ASN B 175 3.420 22.202 24.904 1.00 40.42 C ANISOU 2104 CB ASN B 175 5334 4712 5311 187 -1077 -190 C ATOM 2105 CG ASN B 175 3.541 20.810 24.328 1.00 51.24 C ANISOU 2105 CG ASN B 175 6609 6191 6671 177 -1004 -138 C ATOM 2106 OD1 ASN B 175 3.731 20.661 23.121 1.00 43.10 O ANISOU 2106 OD1 ASN B 175 5640 5135 5602 141 -1072 -76 O ATOM 2107 ND2 ASN B 175 3.481 19.781 25.186 1.00 55.04 N ANISOU 2107 ND2 ASN B 175 6959 6785 7168 202 -864 -161 N ATOM 2108 N ASP B 176 4.347 25.266 25.590 1.00 50.87 N ANISOU 2108 N ASP B 176 6977 5822 6529 81 -1257 -206 N ATOM 2109 CA ASP B 176 3.919 26.657 25.712 1.00 55.40 C ANISOU 2109 CA ASP B 176 7682 6230 7138 117 -1381 -262 C ATOM 2110 C ASP B 176 4.921 27.648 25.133 1.00 53.96 C ANISOU 2110 C ASP B 176 7688 5976 6840 -20 -1477 -180 C ATOM 2111 O ASP B 176 4.510 28.614 24.487 1.00 48.41 O ANISOU 2111 O ASP B 176 7129 5108 6157 1 -1626 -186 O ATOM 2112 CB ASP B 176 3.676 27.031 27.178 1.00 61.62 C ANISOU 2112 CB ASP B 176 8440 7018 7955 168 -1308 -360 C ATOM 2113 CG ASP B 176 2.542 26.256 27.803 1.00 67.17 C ANISOU 2113 CG ASP B 176 8980 7759 8784 302 -1203 -460 C ATOM 2114 OD1 ASP B 176 1.819 25.547 27.064 1.00 65.96 O ANISOU 2114 OD1 ASP B 176 8729 7610 8722 367 -1215 -463 O ATOM 2115 OD2 ASP B 176 2.391 26.347 29.042 1.00 70.52 O ANISOU 2115 OD2 ASP B 176 9381 8204 9210 332 -1103 -537 O ATOM 2116 N HIS B 177 6.226 27.459 25.374 1.00 52.41 N ANISOU 2116 N HIS B 177 7494 5890 6529 -162 -1401 -106 N ATOM 2117 CA HIS B 177 7.205 28.490 25.051 1.00 50.58 C ANISOU 2117 CA HIS B 177 7426 5589 6201 -307 -1471 -44 C ATOM 2118 C HIS B 177 8.223 28.112 23.987 1.00 50.32 C ANISOU 2118 C HIS B 177 7424 5619 6076 -453 -1440 69 C ATOM 2119 O HIS B 177 8.985 28.983 23.560 1.00 63.83 O ANISOU 2119 O HIS B 177 9282 7260 7711 -587 -1491 123 O ATOM 2120 CB HIS B 177 7.969 28.922 26.307 1.00 49.31 C ANISOU 2120 CB HIS B 177 7265 5474 5996 -374 -1429 -69 C ATOM 2121 CG HIS B 177 7.085 29.344 27.427 1.00 63.46 C ANISOU 2121 CG HIS B 177 9053 7203 7855 -248 -1436 -185 C ATOM 2122 ND1 HIS B 177 6.738 28.498 28.458 1.00 67.60 N ANISOU 2122 ND1 HIS B 177 9438 7835 8412 -168 -1317 -246 N ATOM 2123 CD2 HIS B 177 6.463 30.520 27.675 1.00 66.42 C ANISOU 2123 CD2 HIS B 177 9555 7413 8270 -188 -1538 -257 C ATOM 2124 CE1 HIS B 177 5.945 29.136 29.299 1.00 66.90 C ANISOU 2124 CE1 HIS B 177 9389 7653 8377 -70 -1329 -353 C ATOM 2125 NE2 HIS B 177 5.763 30.365 28.847 1.00 67.63 N ANISOU 2125 NE2 HIS B 177 9634 7580 8481 -74 -1465 -365 N ATOM 2126 N LEU B 178 8.287 26.859 23.560 1.00 49.88 N ANISOU 2126 N LEU B 178 7241 5688 6024 -438 -1347 103 N ATOM 2127 CA LEU B 178 9.244 26.480 22.530 1.00 48.06 C ANISOU 2127 CA LEU B 178 7040 5514 5708 -571 -1296 199 C ATOM 2128 C LEU B 178 8.581 26.084 21.234 1.00 54.46 C ANISOU 2128 C LEU B 178 7915 6263 6514 -527 -1343 228 C ATOM 2129 O LEU B 178 9.145 26.322 20.166 1.00 62.50 O ANISOU 2129 O LEU B 178 9069 7237 7442 -642 -1352 301 O ATOM 2130 CB LEU B 178 10.136 25.325 23.010 1.00 42.13 C ANISOU 2130 CB LEU B 178 6103 4959 4946 -614 -1145 223 C ATOM 2131 CG LEU B 178 11.092 25.655 24.162 1.00 45.78 C ANISOU 2131 CG LEU B 178 6512 5490 5392 -692 -1112 213 C ATOM 2132 CD1 LEU B 178 11.904 24.443 24.595 1.00 47.80 C ANISOU 2132 CD1 LEU B 178 6585 5927 5651 -712 -991 234 C ATOM 2133 CD2 LEU B 178 11.999 26.789 23.755 1.00 46.89 C ANISOU 2133 CD2 LEU B 178 6793 5554 5469 -857 -1160 260 C ATOM 2134 N GLU B 179 7.387 25.510 21.315 1.00 53.30 N ANISOU 2134 N GLU B 179 7685 6104 6464 -369 -1372 168 N ATOM 2135 CA GLU B 179 6.722 25.012 20.121 1.00 48.34 C ANISOU 2135 CA GLU B 179 7105 5422 5841 -320 -1431 189 C ATOM 2136 C GLU B 179 6.408 26.097 19.097 1.00 56.35 C ANISOU 2136 C GLU B 179 8365 6237 6808 -347 -1603 217 C ATOM 2137 O GLU B 179 6.549 25.819 17.894 1.00 60.93 O ANISOU 2137 O GLU B 179 9061 6784 7307 -402 -1626 281 O ATOM 2138 CB GLU B 179 5.460 24.260 20.530 1.00 45.07 C ANISOU 2138 CB GLU B 179 6534 5025 5565 -148 -1439 106 C ATOM 2139 CG GLU B 179 4.670 23.740 19.351 1.00 58.26 C ANISOU 2139 CG GLU B 179 8245 6631 7262 -87 -1527 116 C ATOM 2140 CD GLU B 179 5.435 22.712 18.532 1.00 65.03 C ANISOU 2140 CD GLU B 179 9098 7595 8017 -175 -1424 196 C ATOM 2141 OE1 GLU B 179 6.428 22.124 19.029 1.00 62.33 O ANISOU 2141 OE1 GLU B 179 8652 7404 7627 -250 -1265 227 O ATOM 2142 OE2 GLU B 179 5.031 22.493 17.376 1.00 66.35 O ANISOU 2142 OE2 GLU B 179 9372 7684 8154 -165 -1510 223 O ATOM 2143 N PRO B 180 5.989 27.313 19.466 1.00 57.61 N ANISOU 2143 N PRO B 180 8632 6251 7004 -312 -1730 174 N ATOM 2144 CA PRO B 180 5.856 28.355 18.429 1.00 57.00 C ANISOU 2144 CA PRO B 180 8825 5974 6857 -358 -1900 217 C ATOM 2145 C PRO B 180 7.150 28.600 17.671 1.00 61.65 C ANISOU 2145 C PRO B 180 9574 6574 7275 -568 -1831 326 C ATOM 2146 O PRO B 180 7.142 28.595 16.437 1.00 72.12 O ANISOU 2146 O PRO B 180 11080 7814 8508 -621 -1890 388 O ATOM 2147 CB PRO B 180 5.407 29.590 19.224 1.00 49.06 C ANISOU 2147 CB PRO B 180 7882 4836 5922 -295 -2013 147 C ATOM 2148 CG PRO B 180 4.728 29.030 20.440 1.00 48.50 C ANISOU 2148 CG PRO B 180 7566 4866 5997 -151 -1937 41 C ATOM 2149 CD PRO B 180 5.484 27.773 20.776 1.00 53.63 C ANISOU 2149 CD PRO B 180 8032 5737 6607 -213 -1736 77 C ATOM 2150 N TRP B 181 8.267 28.794 18.381 1.00 55.43 N ANISOU 2150 N TRP B 181 8726 5889 6445 -693 -1705 346 N ATOM 2151 CA TRP B 181 9.557 28.969 17.718 1.00 51.10 C ANISOU 2151 CA TRP B 181 8288 5368 5761 -903 -1609 438 C ATOM 2152 C TRP B 181 9.871 27.800 16.809 1.00 53.02 C ANISOU 2152 C TRP B 181 8484 5715 5945 -940 -1492 489 C ATOM 2153 O TRP B 181 10.368 27.992 15.694 1.00 58.35 O ANISOU 2153 O TRP B 181 9348 6327 6495 -1072 -1472 562 O ATOM 2154 CB TRP B 181 10.680 29.129 18.740 1.00 49.36 C ANISOU 2154 CB TRP B 181 7939 5272 5545 -1013 -1489 436 C ATOM 2155 CG TRP B 181 12.036 29.344 18.095 1.00 57.86 C ANISOU 2155 CG TRP B 181 9097 6377 6510 -1239 -1378 518 C ATOM 2156 CD1 TRP B 181 12.637 30.546 17.846 1.00 56.09 C ANISOU 2156 CD1 TRP B 181 9071 6030 6211 -1399 -1420 559 C ATOM 2157 CD2 TRP B 181 12.953 28.335 17.625 1.00 53.75 C ANISOU 2157 CD2 TRP B 181 8456 6015 5953 -1334 -1196 563 C ATOM 2158 NE1 TRP B 181 13.856 30.351 17.244 1.00 58.61 N ANISOU 2158 NE1 TRP B 181 9393 6423 6453 -1596 -1265 624 N ATOM 2159 CE2 TRP B 181 14.077 29.007 17.095 1.00 55.60 C ANISOU 2159 CE2 TRP B 181 8813 6215 6097 -1554 -1124 624 C ATOM 2160 CE3 TRP B 181 12.936 26.939 17.607 1.00 50.24 C ANISOU 2160 CE3 TRP B 181 7812 5729 5547 -1255 -1083 553 C ATOM 2161 CZ2 TRP B 181 15.171 28.329 16.545 1.00 46.21 C ANISOU 2161 CZ2 TRP B 181 7538 5151 4868 -1692 -933 666 C ATOM 2162 CZ3 TRP B 181 14.020 26.262 17.061 1.00 49.53 C ANISOU 2162 CZ3 TRP B 181 7649 5757 5411 -1382 -909 597 C ATOM 2163 CH2 TRP B 181 15.122 26.959 16.530 1.00 51.70 C ANISOU 2163 CH2 TRP B 181 8035 6000 5608 -1596 -831 650 C ATOM 2164 N ILE B 182 9.609 26.578 17.278 1.00 52.33 N ANISOU 2164 N ILE B 182 8160 5782 5939 -833 -1403 450 N ATOM 2165 CA ILE B 182 9.913 25.395 16.478 1.00 51.40 C ANISOU 2165 CA ILE B 182 7989 5767 5773 -858 -1286 490 C ATOM 2166 C ILE B 182 9.150 25.425 15.163 1.00 51.77 C ANISOU 2166 C ILE B 182 8249 5667 5756 -828 -1407 518 C ATOM 2167 O ILE B 182 9.701 25.115 14.097 1.00 53.64 O ANISOU 2167 O ILE B 182 8610 5902 5871 -936 -1335 581 O ATOM 2168 CB ILE B 182 9.601 24.118 17.269 1.00 41.85 C ANISOU 2168 CB ILE B 182 6508 4722 4670 -731 -1198 438 C ATOM 2169 CG1 ILE B 182 10.443 24.070 18.540 1.00 38.59 C ANISOU 2169 CG1 ILE B 182 5918 4445 4300 -770 -1093 418 C ATOM 2170 CG2 ILE B 182 9.849 22.894 16.386 1.00 43.93 C ANISOU 2170 CG2 ILE B 182 6734 5073 4884 -746 -1090 475 C ATOM 2171 CD1 ILE B 182 10.311 22.750 19.312 1.00 36.15 C ANISOU 2171 CD1 ILE B 182 5367 4298 4071 -667 -992 380 C ATOM 2172 N GLN B 183 7.870 25.792 15.216 1.00 58.65 N ANISOU 2172 N GLN B 183 9168 6408 6709 -678 -1595 466 N ATOM 2173 CA GLN B 183 7.062 25.833 14.001 1.00 63.84 C ANISOU 2173 CA GLN B 183 10029 6909 7319 -633 -1753 485 C ATOM 2174 C GLN B 183 7.567 26.905 13.035 1.00 65.24 C ANISOU 2174 C GLN B 183 10537 6918 7332 -785 -1825 563 C ATOM 2175 O GLN B 183 7.643 26.667 11.823 1.00 59.29 O ANISOU 2175 O GLN B 183 9982 6098 6449 -849 -1841 621 O ATOM 2176 CB GLN B 183 5.594 26.047 14.369 1.00 66.60 C ANISOU 2176 CB GLN B 183 10324 7152 7829 -434 -1948 399 C ATOM 2177 CG GLN B 183 4.921 24.785 14.936 1.00 78.35 C ANISOU 2177 CG GLN B 183 11529 8780 9460 -294 -1880 330 C ATOM 2178 CD GLN B 183 3.594 25.063 15.650 1.00 90.98 C ANISOU 2178 CD GLN B 183 13008 10306 11255 -109 -2016 223 C ATOM 2179 OE1 GLN B 183 3.391 26.135 16.230 1.00 93.31 O ANISOU 2179 OE1 GLN B 183 13349 10506 11600 -80 -2098 184 O ATOM 2180 NE2 GLN B 183 2.687 24.085 15.614 1.00 94.13 N ANISOU 2180 NE2 GLN B 183 13247 10745 11772 13 -2031 169 N ATOM 2181 N GLU B 184 7.967 28.074 13.562 1.00 64.41 N ANISOU 2181 N GLU B 184 10513 6743 7217 -856 -1857 567 N ATOM 2182 CA GLU B 184 8.538 29.137 12.746 1.00 63.80 C ANISOU 2182 CA GLU B 184 10754 6505 6980 -1023 -1907 643 C ATOM 2183 C GLU B 184 9.876 28.764 12.123 1.00 72.18 C ANISOU 2183 C GLU B 184 11865 7667 7893 -1237 -1683 722 C ATOM 2184 O GLU B 184 10.324 29.470 11.214 1.00 86.11 O ANISOU 2184 O GLU B 184 13923 9296 9500 -1392 -1697 793 O ATOM 2185 CB GLU B 184 8.748 30.414 13.561 1.00 72.65 C ANISOU 2185 CB GLU B 184 11926 7542 8134 -1062 -1973 625 C ATOM 2186 CG GLU B 184 7.624 30.800 14.485 1.00 92.94 C ANISOU 2186 CG GLU B 184 14388 10048 10874 -858 -2135 527 C ATOM 2187 CD GLU B 184 6.336 31.103 13.763 1.00111.14 C ANISOU 2187 CD GLU B 184 16862 12152 13216 -711 -2386 504 C ATOM 2188 OE1 GLU B 184 6.395 31.703 12.665 1.00116.92 O ANISOU 2188 OE1 GLU B 184 17911 12706 13808 -797 -2503 574 O ATOM 2189 OE2 GLU B 184 5.266 30.735 14.300 1.00116.63 O ANISOU 2189 OE2 GLU B 184 17372 12859 14081 -513 -2467 412 O ATOM 2190 N ASN B 185 10.538 27.706 12.590 1.00 66.54 N ANISOU 2190 N ASN B 185 10879 7177 7226 -1252 -1474 708 N ATOM 2191 CA ASN B 185 11.899 27.399 12.164 1.00 57.87 C ANISOU 2191 CA ASN B 185 9775 6187 6026 -1451 -1244 764 C ATOM 2192 C ASN B 185 12.011 26.003 11.571 1.00 58.62 C ANISOU 2192 C ASN B 185 9767 6409 6097 -1423 -1105 769 C ATOM 2193 O ASN B 185 13.062 25.359 11.664 1.00 60.67 O ANISOU 2193 O ASN B 185 9867 6830 6353 -1518 -888 778 O ATOM 2194 CB ASN B 185 12.876 27.564 13.321 1.00 51.30 C ANISOU 2194 CB ASN B 185 8712 5499 5279 -1525 -1115 742 C ATOM 2195 CG ASN B 185 13.143 29.010 13.643 1.00 57.43 C ANISOU 2195 CG ASN B 185 9647 6142 6032 -1629 -1205 756 C ATOM 2196 OD1 ASN B 185 14.077 29.594 13.108 1.00 70.28 O ANISOU 2196 OD1 ASN B 185 11423 7725 7555 -1835 -1114 812 O ATOM 2197 ND2 ASN B 185 12.332 29.599 14.519 1.00 52.27 N ANISOU 2197 ND2 ASN B 185 8966 5417 5476 -1493 -1373 700 N ATOM 2198 N GLY B 186 10.929 25.521 10.971 1.00 56.58 N ANISOU 2198 N GLY B 186 9592 6074 5831 -1288 -1238 756 N ATOM 2199 CA GLY B 186 10.970 24.314 10.181 1.00 53.71 C ANISOU 2199 CA GLY B 186 9213 5785 5411 -1275 -1134 768 C ATOM 2200 C GLY B 186 10.516 23.067 10.883 1.00 56.86 C ANISOU 2200 C GLY B 186 9304 6344 5955 -1111 -1094 706 C ATOM 2201 O GLY B 186 10.595 21.987 10.289 1.00 60.79 O ANISOU 2201 O GLY B 186 9772 6912 6414 -1098 -998 711 O ATOM 2202 N GLY B 187 10.051 23.170 12.125 1.00 58.82 N ANISOU 2202 N GLY B 187 9341 6646 6364 -992 -1157 647 N ATOM 2203 CA GLY B 187 9.587 22.000 12.848 1.00 57.23 C ANISOU 2203 CA GLY B 187 8864 6586 6295 -845 -1114 590 C ATOM 2204 C GLY B 187 10.721 21.057 13.211 1.00 53.02 C ANISOU 2204 C GLY B 187 8124 6254 5768 -908 -881 598 C ATOM 2205 O GLY B 187 11.882 21.242 12.846 1.00 54.16 O ANISOU 2205 O GLY B 187 8314 6438 5826 -1065 -740 641 O ATOM 2206 N TRP B 188 10.356 20.012 13.952 1.00 47.27 N ANISOU 2206 N TRP B 188 7160 5649 5153 -782 -842 550 N ATOM 2207 CA TRP B 188 11.338 19.004 14.319 1.00 48.64 C ANISOU 2207 CA TRP B 188 7132 6002 5345 -813 -648 552 C ATOM 2208 C TRP B 188 12.062 18.401 13.115 1.00 55.74 C ANISOU 2208 C TRP B 188 8124 6926 6129 -911 -512 594 C ATOM 2209 O TRP B 188 13.188 17.910 13.267 1.00 50.87 O ANISOU 2209 O TRP B 188 7374 6437 5515 -984 -337 602 O ATOM 2210 CB TRP B 188 10.658 17.920 15.128 1.00 36.65 C ANISOU 2210 CB TRP B 188 5401 4577 3946 -658 -648 500 C ATOM 2211 CG TRP B 188 10.388 18.375 16.522 1.00 53.32 C ANISOU 2211 CG TRP B 188 7383 6715 6162 -595 -698 456 C ATOM 2212 CD1 TRP B 188 9.171 18.685 17.073 1.00 54.79 C ANISOU 2212 CD1 TRP B 188 7557 6827 6435 -475 -828 404 C ATOM 2213 CD2 TRP B 188 11.361 18.609 17.542 1.00 47.92 C ANISOU 2213 CD2 TRP B 188 6573 6130 5506 -653 -620 455 C ATOM 2214 NE1 TRP B 188 9.332 19.083 18.376 1.00 55.34 N ANISOU 2214 NE1 TRP B 188 7516 6943 6568 -457 -818 370 N ATOM 2215 CE2 TRP B 188 10.665 19.041 18.693 1.00 50.87 C ANISOU 2215 CE2 TRP B 188 6885 6480 5961 -565 -704 403 C ATOM 2216 CE3 TRP B 188 12.753 18.486 17.598 1.00 49.03 C ANISOU 2216 CE3 TRP B 188 6639 6371 5617 -771 -489 485 C ATOM 2217 CZ2 TRP B 188 11.315 19.357 19.886 1.00 49.21 C ANISOU 2217 CZ2 TRP B 188 6573 6340 5783 -593 -674 387 C ATOM 2218 CZ3 TRP B 188 13.404 18.800 18.785 1.00 51.29 C ANISOU 2218 CZ3 TRP B 188 6801 6730 5958 -796 -475 468 C ATOM 2219 CH2 TRP B 188 12.682 19.228 19.915 1.00 55.05 C ANISOU 2219 CH2 TRP B 188 7248 7175 6493 -708 -572 422 C ATOM 2220 N ASP B 189 11.450 18.431 11.928 1.00 63.67 N ANISOU 2220 N ASP B 189 9355 7802 7033 -913 -590 616 N ATOM 2221 CA ASP B 189 12.112 17.897 10.738 1.00 70.79 C ANISOU 2221 CA ASP B 189 10384 8711 7802 -1012 -451 652 C ATOM 2222 C ASP B 189 13.388 18.666 10.419 1.00 65.22 C ANISOU 2222 C ASP B 189 9764 8008 7006 -1208 -308 694 C ATOM 2223 O ASP B 189 14.410 18.066 10.074 1.00 63.02 O ANISOU 2223 O ASP B 189 9418 7831 6695 -1294 -100 699 O ATOM 2224 CB ASP B 189 11.159 17.926 9.542 1.00 73.87 C ANISOU 2224 CB ASP B 189 11048 8937 8084 -983 -596 669 C ATOM 2225 CG ASP B 189 10.006 16.958 9.698 1.00 83.79 C ANISOU 2225 CG ASP B 189 12198 10202 9436 -808 -706 623 C ATOM 2226 OD1 ASP B 189 10.149 15.979 10.465 1.00 85.69 O ANISOU 2226 OD1 ASP B 189 12181 10592 9785 -733 -607 588 O ATOM 2227 OD2 ASP B 189 8.955 17.178 9.056 1.00 91.46 O ANISOU 2227 OD2 ASP B 189 13347 11024 10380 -747 -900 620 O ATOM 2228 N THR B 190 13.345 19.995 10.524 1.00 61.51 N ANISOU 2228 N THR B 190 9441 7423 6505 -1283 -411 717 N ATOM 2229 CA THR B 190 14.547 20.793 10.314 1.00 62.35 C ANISOU 2229 CA THR B 190 9621 7529 6542 -1483 -276 755 C ATOM 2230 C THR B 190 15.622 20.432 11.331 1.00 62.98 C ANISOU 2230 C THR B 190 9385 7796 6748 -1514 -119 726 C ATOM 2231 O THR B 190 16.821 20.423 11.012 1.00 54.74 O ANISOU 2231 O THR B 190 8304 6818 5677 -1666 75 739 O ATOM 2232 CB THR B 190 14.200 22.282 10.390 1.00 65.47 C ANISOU 2232 CB THR B 190 10223 7757 6896 -1540 -444 781 C ATOM 2233 OG1 THR B 190 13.442 22.653 9.230 1.00 71.21 O ANISOU 2233 OG1 THR B 190 11284 8293 7478 -1547 -576 818 O ATOM 2234 CG2 THR B 190 15.460 23.139 10.467 1.00 58.42 C ANISOU 2234 CG2 THR B 190 9352 6877 5969 -1750 -308 811 C ATOM 2235 N PHE B 191 15.210 20.117 12.561 1.00 63.28 N ANISOU 2235 N PHE B 191 9196 7917 6931 -1372 -201 682 N ATOM 2236 CA PHE B 191 16.169 19.695 13.573 1.00 58.76 C ANISOU 2236 CA PHE B 191 8337 7513 6478 -1382 -86 654 C ATOM 2237 C PHE B 191 16.818 18.379 13.182 1.00 59.31 C ANISOU 2237 C PHE B 191 8261 7713 6562 -1372 97 641 C ATOM 2238 O PHE B 191 18.036 18.208 13.315 1.00 64.21 O ANISOU 2238 O PHE B 191 8731 8439 7229 -1469 255 634 O ATOM 2239 CB PHE B 191 15.483 19.562 14.927 1.00 46.46 C ANISOU 2239 CB PHE B 191 6612 5998 5043 -1227 -215 610 C ATOM 2240 CG PHE B 191 16.335 18.915 15.968 1.00 41.91 C ANISOU 2240 CG PHE B 191 5758 5586 4579 -1208 -125 581 C ATOM 2241 CD1 PHE B 191 17.211 19.677 16.739 1.00 47.16 C ANISOU 2241 CD1 PHE B 191 6339 6285 5294 -1307 -120 577 C ATOM 2242 CD2 PHE B 191 16.255 17.553 16.194 1.00 35.62 C ANISOU 2242 CD2 PHE B 191 4794 4902 3840 -1092 -64 557 C ATOM 2243 CE1 PHE B 191 18.000 19.087 17.717 1.00 50.71 C ANISOU 2243 CE1 PHE B 191 6542 6876 5851 -1284 -69 549 C ATOM 2244 CE2 PHE B 191 17.045 16.948 17.165 1.00 45.04 C ANISOU 2244 CE2 PHE B 191 5748 6232 5134 -1067 -5 532 C ATOM 2245 CZ PHE B 191 17.916 17.721 17.934 1.00 49.41 C ANISOU 2245 CZ PHE B 191 6219 6816 5739 -1160 -15 527 C ATOM 2246 N VAL B 192 16.010 17.424 12.722 1.00 54.25 N ANISOU 2246 N VAL B 192 7651 7065 5897 -1249 73 631 N ATOM 2247 CA VAL B 192 16.559 16.142 12.295 1.00 60.14 C ANISOU 2247 CA VAL B 192 8282 7919 6650 -1228 241 615 C ATOM 2248 C VAL B 192 17.569 16.348 11.174 1.00 64.10 C ANISOU 2248 C VAL B 192 8904 8406 7046 -1404 429 639 C ATOM 2249 O VAL B 192 18.631 15.713 11.146 1.00 66.55 O ANISOU 2249 O VAL B 192 9044 8835 7408 -1449 617 616 O ATOM 2250 CB VAL B 192 15.426 15.194 11.872 1.00 55.94 C ANISOU 2250 CB VAL B 192 7811 7352 6093 -1082 164 603 C ATOM 2251 CG1 VAL B 192 15.984 14.040 11.102 1.00 51.62 C ANISOU 2251 CG1 VAL B 192 7232 6873 5508 -1088 340 593 C ATOM 2252 CG2 VAL B 192 14.689 14.695 13.085 1.00 54.15 C ANISOU 2252 CG2 VAL B 192 7396 7182 5998 -920 53 568 C ATOM 2253 N GLU B 193 17.277 17.272 10.260 1.00 62.53 N ANISOU 2253 N GLU B 193 9002 8055 6702 -1509 384 681 N ATOM 2254 CA GLU B 193 18.211 17.535 9.174 1.00 75.76 C ANISOU 2254 CA GLU B 193 10829 9702 8256 -1697 580 705 C ATOM 2255 C GLU B 193 19.509 18.133 9.690 1.00 72.91 C ANISOU 2255 C GLU B 193 10302 9422 7979 -1847 718 698 C ATOM 2256 O GLU B 193 20.575 17.862 9.131 1.00 77.21 O ANISOU 2256 O GLU B 193 10798 10028 8511 -1972 950 686 O ATOM 2257 CB GLU B 193 17.573 18.459 8.131 1.00 88.57 C ANISOU 2257 CB GLU B 193 12843 11121 9689 -1782 479 758 C ATOM 2258 CG GLU B 193 16.656 17.756 7.128 1.00 96.04 C ANISOU 2258 CG GLU B 193 14000 11979 10510 -1696 415 764 C ATOM 2259 CD GLU B 193 16.171 18.690 6.028 1.00106.78 C ANISOU 2259 CD GLU B 193 15776 13126 11668 -1797 313 820 C ATOM 2260 OE1 GLU B 193 15.120 19.340 6.221 1.00108.01 O ANISOU 2260 OE1 GLU B 193 16056 13156 11826 -1715 56 836 O ATOM 2261 OE2 GLU B 193 16.848 18.784 4.976 1.00111.44 O ANISOU 2261 OE2 GLU B 193 16576 13669 12099 -1959 490 846 O ATOM 2262 N LEU B 194 19.447 18.924 10.761 1.00 67.28 N ANISOU 2262 N LEU B 194 9492 8710 7360 -1838 581 698 N ATOM 2263 CA LEU B 194 20.636 19.594 11.273 1.00 63.43 C ANISOU 2263 CA LEU B 194 8860 8283 6957 -1990 679 691 C ATOM 2264 C LEU B 194 21.459 18.749 12.236 1.00 65.14 C ANISOU 2264 C LEU B 194 8704 8686 7361 -1926 758 637 C ATOM 2265 O LEU B 194 22.676 18.937 12.311 1.00 79.88 O ANISOU 2265 O LEU B 194 10421 10625 9305 -2064 907 619 O ATOM 2266 CB LEU B 194 20.240 20.890 11.973 1.00 63.40 C ANISOU 2266 CB LEU B 194 8947 8182 6961 -2020 487 712 C ATOM 2267 CG LEU B 194 20.065 22.094 11.071 1.00 63.23 C ANISOU 2267 CG LEU B 194 9272 7976 6776 -2176 456 768 C ATOM 2268 CD1 LEU B 194 19.239 23.114 11.806 1.00 53.48 C ANISOU 2268 CD1 LEU B 194 8135 6631 5556 -2117 211 778 C ATOM 2269 CD2 LEU B 194 21.436 22.650 10.712 1.00 72.48 C ANISOU 2269 CD2 LEU B 194 10426 9169 7942 -2420 664 778 C ATOM 2270 N TYR B 195 20.839 17.829 12.980 1.00 54.98 N ANISOU 2270 N TYR B 195 7265 7469 6154 -1726 658 610 N ATOM 2271 CA TYR B 195 21.527 17.135 14.062 1.00 56.13 C ANISOU 2271 CA TYR B 195 7086 7768 6472 -1654 679 565 C ATOM 2272 C TYR B 195 21.459 15.611 13.990 1.00 61.81 C ANISOU 2272 C TYR B 195 7662 8584 7238 -1505 750 533 C ATOM 2273 O TYR B 195 21.995 14.947 14.885 1.00 72.28 O ANISOU 2273 O TYR B 195 8733 10026 8704 -1429 751 497 O ATOM 2274 CB TYR B 195 20.966 17.581 15.429 1.00 55.29 C ANISOU 2274 CB TYR B 195 6914 7657 6437 -1559 469 558 C ATOM 2275 CG TYR B 195 21.266 19.010 15.805 1.00 56.07 C ANISOU 2275 CG TYR B 195 7087 7685 6531 -1696 395 575 C ATOM 2276 CD1 TYR B 195 20.543 20.052 15.257 1.00 54.83 C ANISOU 2276 CD1 TYR B 195 7210 7371 6250 -1756 308 614 C ATOM 2277 CD2 TYR B 195 22.251 19.314 16.738 1.00 57.28 C ANISOU 2277 CD2 TYR B 195 7036 7917 6810 -1761 391 550 C ATOM 2278 CE1 TYR B 195 20.804 21.368 15.599 1.00 62.78 C ANISOU 2278 CE1 TYR B 195 8303 8301 7251 -1881 235 629 C ATOM 2279 CE2 TYR B 195 22.519 20.627 17.091 1.00 64.57 C ANISOU 2279 CE2 TYR B 195 8036 8767 7729 -1893 315 563 C ATOM 2280 CZ TYR B 195 21.792 21.654 16.517 1.00 71.15 C ANISOU 2280 CZ TYR B 195 9159 9444 8432 -1953 244 603 C ATOM 2281 OH TYR B 195 22.048 22.968 16.854 1.00 75.68 O ANISOU 2281 OH TYR B 195 9825 9931 8997 -2085 165 616 O ATOM 2282 N GLY B 196 20.792 15.037 12.996 1.00 58.69 N ANISOU 2282 N GLY B 196 7435 8135 6731 -1458 789 544 N ATOM 2283 CA GLY B 196 20.762 13.592 12.866 1.00 72.63 C ANISOU 2283 CA GLY B 196 9079 9981 8535 -1327 863 512 C ATOM 2284 C GLY B 196 21.992 13.042 12.163 1.00 90.66 C ANISOU 2284 C GLY B 196 11256 12341 10849 -1413 1109 480 C ATOM 2285 O GLY B 196 22.656 13.727 11.385 1.00 93.37 O ANISOU 2285 O GLY B 196 11697 12648 11131 -1587 1249 489 O ATOM 2286 N ASN B 197 22.283 11.771 12.441 1.00106.77 N ANISOU 2286 N ASN B 197 13098 14483 12989 -1288 1167 437 N ATOM 2287 CA ASN B 197 23.469 11.080 11.918 1.00122.11 C ANISOU 2287 CA ASN B 197 14884 16511 15001 -1333 1398 388 C ATOM 2288 C ASN B 197 24.762 11.795 12.311 1.00128.21 C ANISOU 2288 C ASN B 197 15462 17348 15902 -1475 1486 364 C ATOM 2289 O ASN B 197 25.771 11.158 12.618 1.00129.46 O ANISOU 2289 O ASN B 197 15353 17615 16223 -1450 1589 308 O ATOM 2290 CB ASN B 197 23.397 10.933 10.392 1.00126.48 C ANISOU 2290 CB ASN B 197 15676 16992 15389 -1415 1574 392 C ATOM 2291 CG ASN B 197 22.227 10.070 9.938 1.00128.69 C ANISOU 2291 CG ASN B 197 16125 17213 15560 -1274 1492 403 C ATOM 2292 OD1 ASN B 197 22.145 8.886 10.271 1.00127.99 O ANISOU 2292 OD1 ASN B 197 15893 17189 15550 -1124 1488 369 O ATOM 2293 ND2 ASN B 197 21.329 10.655 9.154 1.00130.59 N ANISOU 2293 ND2 ASN B 197 16677 17319 15621 -1324 1419 449 N TER 2294 ASN B 197 ATOM 2295 N GLY D 107 18.484 -28.875 6.218 1.00106.95 N ANISOU 2295 N GLY D 107 14384 12975 13275 2284 1592 -784 N ATOM 2296 CA GLY D 107 17.346 -27.987 6.395 1.00104.92 C ANISOU 2296 CA GLY D 107 14178 12761 12925 2104 1478 -681 C ATOM 2297 C GLY D 107 17.693 -26.718 7.155 1.00100.01 C ANISOU 2297 C GLY D 107 13322 12301 12375 2046 1469 -615 C ATOM 2298 O GLY D 107 18.078 -26.782 8.323 1.00106.14 O ANISOU 2298 O GLY D 107 13931 13117 13282 2117 1383 -570 O HETATM 2299 N TPO D 108 17.533 -25.574 6.489 1.00 85.76 N ANISOU 2299 N TPO D 108 11531 10578 10477 1915 1546 -608 N HETATM 2300 CA TPO D 108 17.990 -24.267 6.975 1.00 78.85 C ANISOU 2300 CA TPO D 108 10449 9856 9656 1851 1573 -564 C HETATM 2301 CB TPO D 108 17.668 -23.173 5.928 1.00 83.53 C ANISOU 2301 CB TPO D 108 11146 10490 10101 1698 1662 -567 C HETATM 2302 CG2 TPO D 108 17.963 -21.778 6.499 1.00 75.77 C ANISOU 2302 CG2 TPO D 108 9971 9651 9166 1614 1662 -507 C HETATM 2303 OG1 TPO D 108 18.425 -23.362 4.722 1.00 99.36 O ANISOU 2303 OG1 TPO D 108 13236 12475 12041 1725 1876 -675 O HETATM 2304 P TPO D 108 17.475 -23.114 3.437 1.00104.64 P ANISOU 2304 P TPO D 108 14213 13060 12486 1591 1881 -682 P HETATM 2305 O1P TPO D 108 18.419 -22.928 2.146 1.00112.95 O ANISOU 2305 O1P TPO D 108 15354 14120 13443 1583 2153 -791 O HETATM 2306 O2P TPO D 108 16.600 -24.295 3.234 1.00102.17 O ANISOU 2306 O2P TPO D 108 14104 12596 12119 1628 1761 -692 O HETATM 2307 O3P TPO D 108 16.579 -21.779 3.639 1.00 99.64 O ANISOU 2307 O3P TPO D 108 13586 12486 11788 1426 1752 -579 O HETATM 2308 C TPO D 108 17.409 -23.858 8.329 1.00 78.63 C ANISOU 2308 C TPO D 108 10310 9872 9695 1811 1388 -452 C HETATM 2309 O TPO D 108 18.134 -23.398 9.207 1.00 81.87 O ANISOU 2309 O TPO D 108 10509 10377 10222 1852 1376 -428 O ATOM 2310 N MET D 109 16.102 -24.020 8.492 1.00 73.65 N ANISOU 2310 N MET D 109 9823 9169 8993 1726 1247 -389 N ATOM 2311 CA MET D 109 15.444 -23.591 9.709 1.00 70.20 C ANISOU 2311 CA MET D 109 9302 8768 8603 1670 1097 -290 C ATOM 2312 C MET D 109 15.782 -24.485 10.898 1.00 69.97 C ANISOU 2312 C MET D 109 9202 8699 8683 1788 1010 -264 C ATOM 2313 O MET D 109 15.968 -23.982 12.003 1.00 67.76 O ANISOU 2313 O MET D 109 8782 8491 8474 1787 941 -204 O ATOM 2314 CB MET D 109 13.940 -23.540 9.505 1.00 69.01 C ANISOU 2314 CB MET D 109 9310 8545 8363 1544 986 -245 C ATOM 2315 CG MET D 109 13.498 -22.344 8.707 1.00 77.86 C ANISOU 2315 CG MET D 109 10471 9720 9393 1415 1010 -241 C ATOM 2316 SD MET D 109 11.735 -22.460 8.389 1.00 92.81 S ANISOU 2316 SD MET D 109 12542 11506 11214 1290 857 -208 S ATOM 2317 CE MET D 109 11.719 -23.132 6.729 1.00 94.48 C ANISOU 2317 CE MET D 109 13003 11604 11292 1296 924 -298 C ATOM 2318 N GLU D 110 15.856 -25.802 10.677 1.00 68.05 N ANISOU 2318 N GLU D 110 9076 8333 8448 1889 1005 -308 N ATOM 2319 CA GLU D 110 16.248 -26.696 11.763 1.00 69.35 C ANISOU 2319 CA GLU D 110 9199 8440 8711 2011 914 -285 C ATOM 2320 C GLU D 110 17.628 -26.325 12.295 1.00 72.16 C ANISOU 2320 C GLU D 110 9330 8896 9193 2123 952 -308 C ATOM 2321 O GLU D 110 17.850 -26.307 13.513 1.00 75.31 O ANISOU 2321 O GLU D 110 9636 9311 9666 2164 839 -249 O ATOM 2322 CB GLU D 110 16.215 -28.156 11.296 1.00 58.13 C ANISOU 2322 CB GLU D 110 7949 6861 7278 2112 914 -342 C ATOM 2323 N ASN D 111 18.553 -25.980 11.394 1.00 60.80 N ANISOU 2323 N ASN D 111 7801 7522 7778 2163 1111 -396 N ATOM 2324 CA ASN D 111 19.899 -25.611 11.813 1.00 61.49 C ANISOU 2324 CA ASN D 111 7647 7706 8012 2264 1157 -434 C ATOM 2325 C ASN D 111 19.906 -24.300 12.588 1.00 62.38 C ANISOU 2325 C ASN D 111 7605 7951 8147 2163 1104 -359 C ATOM 2326 O ASN D 111 20.617 -24.170 13.592 1.00 65.21 O ANISOU 2326 O ASN D 111 7797 8354 8625 2236 1020 -338 O ATOM 2327 CB ASN D 111 20.809 -25.525 10.594 1.00 65.78 C ANISOU 2327 CB ASN D 111 8135 8285 8573 2306 1372 -554 C ATOM 2328 CG ASN D 111 20.864 -26.834 9.827 1.00 76.75 C ANISOU 2328 CG ASN D 111 9684 9537 9941 2417 1434 -640 C ATOM 2329 OD1 ASN D 111 20.681 -27.906 10.402 1.00 76.67 O ANISOU 2329 OD1 ASN D 111 9750 9412 9969 2519 1309 -624 O ATOM 2330 ND2 ASN D 111 21.108 -26.753 8.523 1.00 81.11 N ANISOU 2330 ND2 ASN D 111 10308 10090 10421 2393 1629 -732 N ATOM 2331 N LEU D 112 19.129 -23.315 12.135 1.00 57.28 N ANISOU 2331 N LEU D 112 7018 7360 7387 1999 1138 -321 N ATOM 2332 CA LEU D 112 19.013 -22.070 12.880 1.00 51.79 C ANISOU 2332 CA LEU D 112 6200 6775 6702 1898 1079 -248 C ATOM 2333 C LEU D 112 18.347 -22.304 14.235 1.00 51.91 C ANISOU 2333 C LEU D 112 6244 6751 6727 1894 895 -155 C ATOM 2334 O LEU D 112 18.763 -21.729 15.245 1.00 55.58 O ANISOU 2334 O LEU D 112 6573 7286 7260 1899 819 -112 O ATOM 2335 CB LEU D 112 18.238 -21.041 12.056 1.00 47.63 C ANISOU 2335 CB LEU D 112 5759 6291 6049 1733 1140 -231 C ATOM 2336 CG LEU D 112 17.858 -19.758 12.807 1.00 53.32 C ANISOU 2336 CG LEU D 112 6392 7104 6762 1618 1064 -152 C ATOM 2337 CD1 LEU D 112 19.090 -18.948 13.170 1.00 44.34 C ANISOU 2337 CD1 LEU D 112 5030 6085 5730 1640 1116 -170 C ATOM 2338 CD2 LEU D 112 16.899 -18.920 11.982 1.00 55.82 C ANISOU 2338 CD2 LEU D 112 6832 7425 6951 1469 1089 -133 C ATOM 2339 N SER D 113 17.312 -23.146 14.273 1.00 45.75 N ANISOU 2339 N SER D 113 5651 5854 5877 1876 826 -125 N ATOM 2340 CA SER D 113 16.721 -23.533 15.545 1.00 52.08 C ANISOU 2340 CA SER D 113 6505 6600 6684 1872 677 -44 C ATOM 2341 C SER D 113 17.766 -24.123 16.478 1.00 55.81 C ANISOU 2341 C SER D 113 6886 7052 7266 2024 599 -45 C ATOM 2342 O SER D 113 17.806 -23.789 17.667 1.00 54.17 O ANISOU 2342 O SER D 113 6630 6870 7082 2015 490 20 O ATOM 2343 CB SER D 113 15.593 -24.536 15.312 1.00 62.99 C ANISOU 2343 CB SER D 113 8099 7844 7992 1839 639 -30 C ATOM 2344 OG SER D 113 14.353 -23.862 15.220 1.00 78.32 O ANISOU 2344 OG SER D 113 10101 9800 9857 1680 622 14 O ATOM 2345 N ARG D 114 18.627 -24.999 15.952 1.00 57.12 N ANISOU 2345 N ARG D 114 7035 7166 7500 2169 647 -124 N ATOM 2346 CA ARG D 114 19.656 -25.616 16.780 1.00 59.73 C ANISOU 2346 CA ARG D 114 7277 7464 7956 2333 552 -136 C ATOM 2347 C ARG D 114 20.636 -24.578 17.318 1.00 57.46 C ANISOU 2347 C ARG D 114 6750 7311 7772 2346 536 -138 C ATOM 2348 O ARG D 114 21.018 -24.629 18.492 1.00 53.41 O ANISOU 2348 O ARG D 114 6187 6787 7319 2405 386 -92 O ATOM 2349 CB ARG D 114 20.386 -26.696 15.981 1.00 62.15 C ANISOU 2349 CB ARG D 114 7594 7687 8331 2490 623 -238 C ATOM 2350 CG ARG D 114 21.154 -27.677 16.846 1.00 72.11 C ANISOU 2350 CG ARG D 114 8835 8854 9710 2674 483 -245 C ATOM 2351 CD ARG D 114 21.358 -29.012 16.147 1.00 84.19 C ANISOU 2351 CD ARG D 114 10479 10246 11264 2810 522 -325 C ATOM 2352 NE ARG D 114 21.835 -30.034 17.079 1.00 95.93 N ANISOU 2352 NE ARG D 114 12006 11607 12838 2975 348 -310 N ATOM 2353 CZ ARG D 114 23.093 -30.470 17.154 1.00102.37 C ANISOU 2353 CZ ARG D 114 12665 12404 13827 3171 320 -393 C ATOM 2354 NH1 ARG D 114 24.023 -29.987 16.338 1.00100.22 N ANISOU 2354 NH1 ARG D 114 12172 12239 13667 3221 481 -503 N ATOM 2355 NH2 ARG D 114 23.423 -31.402 18.042 1.00103.34 N ANISOU 2355 NH2 ARG D 114 12856 12392 14015 3318 130 -369 N ATOM 2356 N ARG D 115 21.041 -23.620 16.481 1.00 56.58 N ANISOU 2356 N ARG D 115 6504 7318 7675 2283 683 -190 N ATOM 2357 CA ARG D 115 22.010 -22.622 16.919 1.00 54.82 C ANISOU 2357 CA ARG D 115 6045 7222 7562 2285 678 -200 C ATOM 2358 C ARG D 115 21.397 -21.673 17.947 1.00 52.95 C ANISOU 2358 C ARG D 115 5816 7039 7263 2163 562 -97 C ATOM 2359 O ARG D 115 22.074 -21.255 18.894 1.00 58.38 O ANISOU 2359 O ARG D 115 6368 7775 8038 2199 454 -76 O ATOM 2360 CB ARG D 115 22.565 -21.866 15.703 1.00 44.33 C ANISOU 2360 CB ARG D 115 4597 5995 6253 2231 887 -281 C ATOM 2361 CG ARG D 115 23.556 -22.667 14.861 1.00 46.46 C ANISOU 2361 CG ARG D 115 4788 6233 6631 2373 1018 -404 C ATOM 2362 CD ARG D 115 23.398 -22.449 13.340 1.00 52.13 C ANISOU 2362 CD ARG D 115 5584 6969 7254 2294 1247 -473 C ATOM 2363 NE ARG D 115 24.556 -22.931 12.572 1.00 62.53 N ANISOU 2363 NE ARG D 115 6775 8289 8696 2415 1414 -605 N ATOM 2364 CZ ARG D 115 24.721 -24.181 12.118 1.00 64.99 C ANISOU 2364 CZ ARG D 115 7173 8488 9032 2553 1452 -679 C ATOM 2365 NH1 ARG D 115 23.806 -25.118 12.343 1.00 68.38 N ANISOU 2365 NH1 ARG D 115 7826 8788 9367 2583 1328 -629 N ATOM 2366 NH2 ARG D 115 25.813 -24.506 11.438 1.00 58.82 N ANISOU 2366 NH2 ARG D 115 6252 7718 8378 2661 1623 -809 N ATOM 2367 N LEU D 116 20.121 -21.322 17.785 1.00 53.83 N ANISOU 2367 N LEU D 116 6084 7140 7231 2021 577 -39 N ATOM 2368 CA LEU D 116 19.451 -20.488 18.781 1.00 52.51 C ANISOU 2368 CA LEU D 116 5937 7010 7005 1911 478 50 C ATOM 2369 C LEU D 116 19.303 -21.229 20.100 1.00 55.06 C ANISOU 2369 C LEU D 116 6349 7243 7330 1975 310 112 C ATOM 2370 O LEU D 116 19.548 -20.671 21.175 1.00 55.63 O ANISOU 2370 O LEU D 116 6365 7353 7419 1962 203 160 O ATOM 2371 CB LEU D 116 18.078 -20.068 18.276 1.00 43.02 C ANISOU 2371 CB LEU D 116 4875 5799 5672 1760 530 84 C ATOM 2372 CG LEU D 116 18.055 -19.156 17.068 1.00 46.90 C ANISOU 2372 CG LEU D 116 5323 6369 6128 1669 668 42 C ATOM 2373 CD1 LEU D 116 16.607 -18.986 16.634 1.00 35.97 C ANISOU 2373 CD1 LEU D 116 4099 4941 4626 1545 673 74 C ATOM 2374 CD2 LEU D 116 18.702 -17.816 17.432 1.00 48.55 C ANISOU 2374 CD2 LEU D 116 5359 6704 6383 1614 673 52 C ATOM 2375 N LYS D 117 18.892 -22.497 20.027 1.00 53.95 N ANISOU 2375 N LYS D 117 6369 6971 7159 2039 283 113 N ATOM 2376 CA LYS D 117 18.579 -23.264 21.228 1.00 54.73 C ANISOU 2376 CA LYS D 117 6608 6961 7227 2077 134 181 C ATOM 2377 C LYS D 117 19.823 -23.507 22.081 1.00 55.78 C ANISOU 2377 C LYS D 117 6638 7083 7472 2225 -2 174 C ATOM 2378 O LYS D 117 19.769 -23.393 23.312 1.00 48.30 O ANISOU 2378 O LYS D 117 5748 6109 6495 2215 -142 243 O ATOM 2379 CB LYS D 117 17.903 -24.573 20.820 1.00 54.47 C ANISOU 2379 CB LYS D 117 6772 6781 7142 2105 146 176 C ATOM 2380 CG LYS D 117 17.963 -25.680 21.840 1.00 53.96 C ANISOU 2380 CG LYS D 117 6857 6575 7072 2195 0 223 C ATOM 2381 CD LYS D 117 16.681 -26.485 21.853 1.00 54.42 C ANISOU 2381 CD LYS D 117 7149 6505 7022 2109 10 266 C ATOM 2382 CE LYS D 117 16.308 -26.990 20.484 1.00 60.75 C ANISOU 2382 CE LYS D 117 7994 7273 7815 2103 127 200 C ATOM 2383 NZ LYS D 117 15.034 -27.758 20.528 1.00 60.22 N ANISOU 2383 NZ LYS D 117 8143 7079 7658 2006 124 240 N ATOM 2384 N VAL D 118 20.962 -23.800 21.443 1.00 50.70 N ANISOU 2384 N VAL D 118 5841 6462 6963 2359 35 86 N ATOM 2385 CA VAL D 118 22.195 -24.058 22.182 1.00 52.29 C ANISOU 2385 CA VAL D 118 5914 6648 7304 2515 -109 65 C ATOM 2386 C VAL D 118 22.802 -22.767 22.724 1.00 57.40 C ANISOU 2386 C VAL D 118 6367 7430 8011 2463 -152 75 C ATOM 2387 O VAL D 118 23.413 -22.764 23.804 1.00 55.88 O ANISOU 2387 O VAL D 118 6137 7215 7878 2534 -335 103 O ATOM 2388 CB VAL D 118 23.182 -24.817 21.280 1.00 57.88 C ANISOU 2388 CB VAL D 118 6502 7331 8160 2680 -38 -49 C ATOM 2389 CG1 VAL D 118 24.546 -24.990 21.956 1.00 54.23 C ANISOU 2389 CG1 VAL D 118 5855 6864 7886 2850 -190 -90 C ATOM 2390 CG2 VAL D 118 22.593 -26.174 20.921 1.00 69.57 C ANISOU 2390 CG2 VAL D 118 8204 8654 9575 2741 -32 -52 C ATOM 2391 N THR D 119 22.671 -21.662 21.991 1.00 52.47 N ANISOU 2391 N THR D 119 5629 6935 7371 2338 1 52 N ATOM 2392 CA THR D 119 23.156 -20.394 22.511 1.00 54.94 C ANISOU 2392 CA THR D 119 5778 7367 7728 2270 -39 66 C ATOM 2393 C THR D 119 22.301 -19.933 23.685 1.00 53.53 C ANISOU 2393 C THR D 119 5752 7170 7418 2166 -161 171 C ATOM 2394 O THR D 119 22.824 -19.392 24.667 1.00 53.11 O ANISOU 2394 O THR D 119 5631 7147 7403 2173 -300 198 O ATOM 2395 CB THR D 119 23.168 -19.344 21.400 1.00 55.07 C ANISOU 2395 CB THR D 119 5670 7510 7743 2153 159 20 C ATOM 2396 OG1 THR D 119 23.835 -19.882 20.258 1.00 65.38 O ANISOU 2396 OG1 THR D 119 6881 8818 9143 2239 302 -80 O ATOM 2397 CG2 THR D 119 23.902 -18.083 21.850 1.00 45.99 C ANISOU 2397 CG2 THR D 119 4321 6479 6672 2096 123 18 C ATOM 2398 N GLY D 120 20.983 -20.139 23.598 1.00 43.46 N ANISOU 2398 N GLY D 120 4681 5840 5991 2066 -108 223 N ATOM 2399 CA GLY D 120 20.118 -19.789 24.711 1.00 46.59 C ANISOU 2399 CA GLY D 120 5229 6207 6264 1968 -195 312 C ATOM 2400 C GLY D 120 20.429 -20.604 25.952 1.00 51.59 C ANISOU 2400 C GLY D 120 5984 6728 6891 2066 -388 359 C ATOM 2401 O GLY D 120 20.416 -20.084 27.066 1.00 46.31 O ANISOU 2401 O GLY D 120 5362 6061 6171 2025 -503 414 O ATOM 2402 N ASP D 121 20.751 -21.886 25.768 1.00 48.63 N ANISOU 2402 N ASP D 121 5675 6241 6561 2200 -432 337 N ATOM 2403 CA ASP D 121 21.026 -22.745 26.908 1.00 47.09 C ANISOU 2403 CA ASP D 121 5631 5913 6349 2299 -629 385 C ATOM 2404 C ASP D 121 22.354 -22.389 27.571 1.00 56.71 C ANISOU 2404 C ASP D 121 6683 7166 7697 2410 -802 364 C ATOM 2405 O ASP D 121 22.455 -22.396 28.802 1.00 58.39 O ANISOU 2405 O ASP D 121 7016 7316 7855 2421 -984 426 O ATOM 2406 CB ASP D 121 21.001 -24.204 26.468 1.00 45.12 C ANISOU 2406 CB ASP D 121 5501 5524 6118 2416 -634 363 C ATOM 2407 CG ASP D 121 19.597 -24.697 26.182 1.00 50.96 C ANISOU 2407 CG ASP D 121 6460 6190 6714 2297 -522 405 C ATOM 2408 OD1 ASP D 121 18.634 -23.986 26.539 1.00 45.40 O ANISOU 2408 OD1 ASP D 121 5827 5526 5896 2135 -466 458 O ATOM 2409 OD2 ASP D 121 19.452 -25.795 25.595 1.00 57.72 O ANISOU 2409 OD2 ASP D 121 7410 6943 7579 2366 -491 378 O ATOM 2410 N LEU D 122 23.384 -22.069 26.785 1.00 58.13 N ANISOU 2410 N LEU D 122 6592 7443 8052 2487 -749 272 N ATOM 2411 CA LEU D 122 24.619 -21.588 27.394 1.00 59.71 C ANISOU 2411 CA LEU D 122 6598 7690 8398 2572 -910 244 C ATOM 2412 C LEU D 122 24.370 -20.290 28.149 1.00 60.02 C ANISOU 2412 C LEU D 122 6631 7818 8357 2427 -952 299 C ATOM 2413 O LEU D 122 24.910 -20.074 29.241 1.00 59.94 O ANISOU 2413 O LEU D 122 6629 7780 8365 2465 -1161 329 O ATOM 2414 CB LEU D 122 25.703 -21.387 26.336 1.00 53.87 C ANISOU 2414 CB LEU D 122 5548 7050 7871 2652 -801 126 C ATOM 2415 CG LEU D 122 27.019 -20.812 26.873 1.00 58.32 C ANISOU 2415 CG LEU D 122 5860 7676 8624 2728 -955 81 C ATOM 2416 CD1 LEU D 122 27.760 -21.820 27.774 1.00 57.80 C ANISOU 2416 CD1 LEU D 122 5837 7470 8655 2923 -1227 81 C ATOM 2417 CD2 LEU D 122 27.926 -20.310 25.767 1.00 64.28 C ANISOU 2417 CD2 LEU D 122 6294 8558 9571 2744 -782 -35 C ATOM 2418 N PHE D 123 23.549 -19.419 27.577 1.00 64.15 N ANISOU 2418 N PHE D 123 7149 8436 8789 2264 -766 309 N ATOM 2419 CA PHE D 123 23.170 -18.182 28.243 1.00 63.56 C ANISOU 2419 CA PHE D 123 7090 8435 8625 2121 -786 358 C ATOM 2420 C PHE D 123 22.488 -18.462 29.575 1.00 60.62 C ANISOU 2420 C PHE D 123 6989 7954 8090 2088 -929 450 C ATOM 2421 O PHE D 123 22.874 -17.915 30.614 1.00 63.76 O ANISOU 2421 O PHE D 123 7403 8352 8468 2078 -1088 482 O ATOM 2422 CB PHE D 123 22.251 -17.395 27.323 1.00 63.40 C ANISOU 2422 CB PHE D 123 7057 8505 8529 1968 -565 353 C ATOM 2423 CG PHE D 123 22.477 -15.937 27.371 1.00 67.88 C ANISOU 2423 CG PHE D 123 7480 9197 9113 1860 -538 346 C ATOM 2424 CD1 PHE D 123 23.625 -15.393 26.827 1.00 75.17 C ANISOU 2424 CD1 PHE D 123 8144 10217 10200 1892 -514 276 C ATOM 2425 CD2 PHE D 123 21.540 -15.100 27.949 1.00 65.80 C ANISOU 2425 CD2 PHE D 123 7340 8951 8711 1721 -527 404 C ATOM 2426 CE1 PHE D 123 23.836 -14.033 26.862 1.00 82.29 C ANISOU 2426 CE1 PHE D 123 8924 11226 11118 1781 -490 271 C ATOM 2427 CE2 PHE D 123 21.746 -13.738 27.990 1.00 73.44 C ANISOU 2427 CE2 PHE D 123 8188 10024 9694 1623 -509 395 C ATOM 2428 CZ PHE D 123 22.894 -13.201 27.448 1.00 77.29 C ANISOU 2428 CZ PHE D 123 8429 10602 10335 1649 -495 333 C ATOM 2429 N ASP D 124 21.471 -19.322 29.557 1.00 57.17 N ANISOU 2429 N ASP D 124 6778 7414 7530 2063 -869 493 N ATOM 2430 CA ASP D 124 20.768 -19.689 30.782 1.00 61.47 C ANISOU 2430 CA ASP D 124 7605 7841 7909 2019 -971 578 C ATOM 2431 C ASP D 124 21.720 -20.256 31.829 1.00 62.17 C ANISOU 2431 C ASP D 124 7765 7827 8028 2154 -1230 601 C ATOM 2432 O ASP D 124 21.600 -19.945 33.016 1.00 68.49 O ANISOU 2432 O ASP D 124 8727 8581 8715 2108 -1359 661 O ATOM 2433 CB ASP D 124 19.673 -20.698 30.451 1.00 63.39 C ANISOU 2433 CB ASP D 124 8051 7980 8053 1984 -860 606 C ATOM 2434 CG ASP D 124 18.668 -20.851 31.564 1.00 68.48 C ANISOU 2434 CG ASP D 124 8982 8526 8510 1878 -883 690 C ATOM 2435 OD1 ASP D 124 18.082 -19.816 31.977 1.00 73.05 O ANISOU 2435 OD1 ASP D 124 9572 9174 9008 1744 -821 711 O ATOM 2436 OD2 ASP D 124 18.458 -22.007 32.001 1.00 63.81 O ANISOU 2436 OD2 ASP D 124 8608 7783 7853 1925 -950 730 O ATOM 2437 N ILE D 125 22.674 -21.087 31.402 1.00 58.74 N ANISOU 2437 N ILE D 125 7220 7350 7747 2325 -1314 549 N ATOM 2438 CA ILE D 125 23.621 -21.702 32.323 1.00 58.30 C ANISOU 2438 CA ILE D 125 7222 7183 7748 2477 -1587 562 C ATOM 2439 C ILE D 125 24.506 -20.651 32.981 1.00 58.11 C ANISOU 2439 C ILE D 125 7040 7241 7798 2478 -1743 549 C ATOM 2440 O ILE D 125 24.885 -20.784 34.149 1.00 64.15 O ANISOU 2440 O ILE D 125 7950 7911 8514 2526 -1986 595 O ATOM 2441 CB ILE D 125 24.455 -22.759 31.580 1.00 61.78 C ANISOU 2441 CB ILE D 125 7534 7568 8371 2669 -1623 489 C ATOM 2442 CG1 ILE D 125 23.593 -23.968 31.251 1.00 57.94 C ANISOU 2442 CG1 ILE D 125 7284 6951 7782 2679 -1537 518 C ATOM 2443 CG2 ILE D 125 25.649 -23.194 32.410 1.00 65.57 C ANISOU 2443 CG2 ILE D 125 7986 7956 8970 2847 -1925 478 C ATOM 2444 CD1 ILE D 125 24.358 -25.039 30.561 1.00 65.05 C ANISOU 2444 CD1 ILE D 125 8088 7780 8847 2872 -1572 445 C ATOM 2445 N MET D 126 24.852 -19.595 32.257 1.00 59.50 N ANISOU 2445 N MET D 126 6936 7584 8088 2419 -1617 487 N ATOM 2446 CA MET D 126 25.673 -18.531 32.831 1.00 74.80 C ANISOU 2446 CA MET D 126 8713 9604 10105 2401 -1756 470 C ATOM 2447 C MET D 126 24.785 -17.470 33.488 1.00 89.03 C ANISOU 2447 C MET D 126 10666 11449 11713 2215 -1707 535 C ATOM 2448 O MET D 126 24.756 -16.306 33.094 1.00 96.77 O ANISOU 2448 O MET D 126 11483 12564 12722 2107 -1591 508 O ATOM 2449 CB MET D 126 26.571 -17.929 31.758 1.00 80.17 C ANISOU 2449 CB MET D 126 9017 10430 11012 2426 -1645 368 C ATOM 2450 CG MET D 126 27.463 -18.954 31.069 1.00 89.62 C ANISOU 2450 CG MET D 126 10047 11589 12416 2613 -1665 287 C ATOM 2451 SD MET D 126 28.276 -18.309 29.591 1.00 94.74 S ANISOU 2451 SD MET D 126 10289 12410 13297 2607 -1435 161 S ATOM 2452 CE MET D 126 29.567 -17.297 30.307 1.00 96.89 C ANISOU 2452 CE MET D 126 10297 12760 13757 2618 -1642 120 C ATOM 2453 N SER D 127 24.043 -17.905 34.506 1.00 93.00 N ANISOU 2453 N SER D 127 11496 11824 12014 2179 -1789 619 N ATOM 2454 CA SER D 127 23.161 -17.028 35.280 1.00 89.06 C ANISOU 2454 CA SER D 127 11180 11341 11319 2013 -1746 678 C ATOM 2455 C SER D 127 22.586 -17.765 36.478 1.00 85.89 C ANISOU 2455 C SER D 127 11156 10769 10710 2004 -1863 763 C ATOM 2456 O SER D 127 22.550 -18.996 36.493 1.00 87.78 O ANISOU 2456 O SER D 127 11536 10882 10935 2097 -1916 785 O ATOM 2457 CB SER D 127 22.024 -16.489 34.413 1.00 87.32 C ANISOU 2457 CB SER D 127 10926 11213 11038 1869 -1454 670 C ATOM 2458 OG SER D 127 22.511 -15.536 33.487 1.00 87.70 O ANISOU 2458 OG SER D 127 10673 11416 11233 1841 -1354 603 O TER 2459 SER D 127 ATOM 2460 N GLY C 107 24.399 34.068 40.687 1.00125.78 N ANISOU 2460 N GLY C 107 17124 15434 15233 -2135 -2786 -233 N ATOM 2461 CA GLY C 107 23.927 33.088 41.651 1.00125.39 C ANISOU 2461 CA GLY C 107 17125 15434 15084 -1970 -2789 -260 C ATOM 2462 C GLY C 107 24.201 31.642 41.272 1.00121.67 C ANISOU 2462 C GLY C 107 16407 15131 14692 -1895 -2708 -206 C ATOM 2463 O GLY C 107 24.928 31.369 40.321 1.00128.68 O ANISOU 2463 O GLY C 107 17059 16108 15726 -1980 -2665 -153 O HETATM 2464 N TPO C 108 23.599 30.719 42.017 1.00108.02 N ANISOU 2464 N TPO C 108 14744 13436 12861 -1739 -2678 -223 N HETATM 2465 CA TPO C 108 23.833 29.284 41.863 1.00 99.16 C ANISOU 2465 CA TPO C 108 13426 12457 11794 -1653 -2626 -178 C HETATM 2466 CB TPO C 108 23.213 28.532 43.071 1.00106.51 C ANISOU 2466 CB TPO C 108 14529 13375 12566 -1509 -2643 -211 C HETATM 2467 CG2 TPO C 108 21.727 28.161 42.925 1.00103.95 C ANISOU 2467 CG2 TPO C 108 14311 13037 12148 -1356 -2429 -225 C HETATM 2468 OG1 TPO C 108 23.953 27.354 43.380 1.00112.13 O ANISOU 2468 OG1 TPO C 108 15092 14189 13323 -1475 -2725 -178 O HETATM 2469 P TPO C 108 24.350 27.596 44.921 1.00114.59 P ANISOU 2469 P TPO C 108 15627 14412 13498 -1492 -2955 -229 P HETATM 2470 O1P TPO C 108 25.113 28.862 45.023 1.00115.89 O ANISOU 2470 O1P TPO C 108 15824 14496 13712 -1654 -3120 -259 O HETATM 2471 O2P TPO C 108 22.999 27.745 45.779 1.00115.37 O ANISOU 2471 O2P TPO C 108 16052 14410 13374 -1380 -2850 -285 O HETATM 2472 O3P TPO C 108 25.227 26.360 45.471 1.00111.16 O ANISOU 2472 O3P TPO C 108 15075 14060 13099 -1450 -3107 -199 O HETATM 2473 C TPO C 108 23.287 28.726 40.549 1.00 90.35 C ANISOU 2473 C TPO C 108 12151 11422 10756 -1595 -2410 -126 C HETATM 2474 O TPO C 108 23.913 27.885 39.893 1.00 84.59 O ANISOU 2474 O TPO C 108 11184 10811 10145 -1605 -2370 -77 O ATOM 2475 N MET C 109 22.116 29.210 40.162 1.00 83.95 N ANISOU 2475 N MET C 109 11476 10539 9882 -1531 -2278 -143 N ATOM 2476 CA MET C 109 21.443 28.663 39.016 1.00 76.42 C ANISOU 2476 CA MET C 109 10412 9643 8980 -1459 -2092 -101 C ATOM 2477 C MET C 109 21.699 29.590 37.832 1.00 74.30 C ANISOU 2477 C MET C 109 10102 9333 8794 -1586 -2060 -71 C ATOM 2478 O MET C 109 21.683 29.161 36.676 1.00 74.58 O ANISOU 2478 O MET C 109 9997 9435 8906 -1590 -1939 -19 O ATOM 2479 CB MET C 109 19.950 28.464 39.312 1.00 84.02 C ANISOU 2479 CB MET C 109 11529 10556 9839 -1296 -1970 -142 C ATOM 2480 CG MET C 109 19.247 29.591 40.060 1.00102.12 C ANISOU 2480 CG MET C 109 14077 12697 12027 -1281 -2011 -219 C ATOM 2481 SD MET C 109 17.590 29.111 40.644 1.00113.84 S ANISOU 2481 SD MET C 109 15703 14143 13409 -1083 -1853 -285 S ATOM 2482 CE MET C 109 16.889 30.705 41.083 1.00114.60 C ANISOU 2482 CE MET C 109 16056 14049 13439 -1088 -1890 -377 C ATOM 2483 N GLU C 110 21.979 30.860 38.132 1.00 71.08 N ANISOU 2483 N GLU C 110 9835 8809 8364 -1700 -2171 -102 N ATOM 2484 CA GLU C 110 22.434 31.771 37.089 1.00 68.84 C ANISOU 2484 CA GLU C 110 9524 8476 8155 -1855 -2161 -68 C ATOM 2485 C GLU C 110 23.699 31.238 36.419 1.00 70.59 C ANISOU 2485 C GLU C 110 9485 8822 8515 -1979 -2149 -13 C ATOM 2486 O GLU C 110 23.835 31.297 35.191 1.00 72.85 O ANISOU 2486 O GLU C 110 9684 9130 8866 -2050 -2035 36 O ATOM 2487 CB GLU C 110 22.662 33.161 37.678 1.00 59.07 C ANISOU 2487 CB GLU C 110 8482 7091 6873 -1968 -2305 -114 C ATOM 2488 N ASN C 111 24.622 30.679 37.210 1.00 62.49 N ANISOU 2488 N ASN C 111 8334 7873 7536 -2002 -2263 -26 N ATOM 2489 CA ASN C 111 25.834 30.097 36.642 1.00 64.25 C ANISOU 2489 CA ASN C 111 8277 8217 7917 -2102 -2251 11 C ATOM 2490 C ASN C 111 25.522 28.850 35.834 1.00 67.06 C ANISOU 2490 C ASN C 111 8473 8695 8311 -1988 -2079 54 C ATOM 2491 O ASN C 111 26.141 28.611 34.787 1.00 69.94 O ANISOU 2491 O ASN C 111 8653 9131 8790 -2074 -1974 91 O ATOM 2492 CB ASN C 111 26.838 29.758 37.741 1.00 68.37 C ANISOU 2492 CB ASN C 111 8704 8782 8491 -2130 -2445 -21 C ATOM 2493 CG ASN C 111 27.290 30.975 38.509 1.00 80.99 C ANISOU 2493 CG ASN C 111 10446 10261 10064 -2263 -2632 -65 C ATOM 2494 OD1 ASN C 111 27.269 32.096 37.994 1.00 86.72 O ANISOU 2494 OD1 ASN C 111 11265 10893 10792 -2392 -2611 -63 O ATOM 2495 ND2 ASN C 111 27.701 30.765 39.752 1.00 85.15 N ANISOU 2495 ND2 ASN C 111 11013 10780 10559 -2235 -2827 -105 N ATOM 2496 N LEU C 112 24.581 28.035 36.315 1.00 60.32 N ANISOU 2496 N LEU C 112 7693 7861 7363 -1802 -2041 45 N ATOM 2497 CA LEU C 112 24.205 26.836 35.587 1.00 45.98 C ANISOU 2497 CA LEU C 112 5745 6150 5576 -1689 -1885 82 C ATOM 2498 C LEU C 112 23.614 27.191 34.226 1.00 55.90 C ANISOU 2498 C LEU C 112 7028 7376 6834 -1715 -1724 118 C ATOM 2499 O LEU C 112 23.974 26.598 33.198 1.00 52.22 O ANISOU 2499 O LEU C 112 6399 6994 6448 -1740 -1604 158 O ATOM 2500 CB LEU C 112 23.212 26.019 36.412 1.00 44.81 C ANISOU 2500 CB LEU C 112 5703 6006 5316 -1500 -1873 62 C ATOM 2501 CG LEU C 112 22.711 24.738 35.730 1.00 52.84 C ANISOU 2501 CG LEU C 112 6603 7119 6354 -1375 -1718 97 C ATOM 2502 CD1 LEU C 112 23.846 23.751 35.540 1.00 46.91 C ANISOU 2502 CD1 LEU C 112 5606 6492 5726 -1394 -1735 123 C ATOM 2503 CD2 LEU C 112 21.579 24.096 36.516 1.00 64.51 C ANISOU 2503 CD2 LEU C 112 8216 8579 7716 -1209 -1686 73 C ATOM 2504 N SER C 113 22.687 28.148 34.196 1.00 52.48 N ANISOU 2504 N SER C 113 6812 6817 6310 -1703 -1723 100 N ATOM 2505 CA SER C 113 22.046 28.442 32.926 1.00 51.45 C ANISOU 2505 CA SER C 113 6732 6644 6173 -1710 -1596 135 C ATOM 2506 C SER C 113 23.018 29.135 31.987 1.00 56.58 C ANISOU 2506 C SER C 113 7322 7280 6896 -1913 -1574 172 C ATOM 2507 O SER C 113 22.923 28.969 30.767 1.00 54.50 O ANISOU 2507 O SER C 113 7025 7032 6650 -1944 -1446 217 O ATOM 2508 CB SER C 113 20.781 29.269 33.140 1.00 48.51 C ANISOU 2508 CB SER C 113 6600 6130 5703 -1630 -1616 99 C ATOM 2509 OG SER C 113 21.073 30.487 33.766 1.00 59.35 O ANISOU 2509 OG SER C 113 8116 7390 7045 -1729 -1744 64 O ATOM 2510 N ARG C 114 23.993 29.859 32.536 1.00 55.47 N ANISOU 2510 N ARG C 114 7164 7112 6798 -2059 -1691 153 N ATOM 2511 CA ARG C 114 25.035 30.424 31.691 1.00 59.22 C ANISOU 2511 CA ARG C 114 7552 7587 7364 -2271 -1652 184 C ATOM 2512 C ARG C 114 25.881 29.328 31.045 1.00 56.13 C ANISOU 2512 C ARG C 114 6884 7350 7092 -2296 -1535 211 C ATOM 2513 O ARG C 114 26.205 29.413 29.854 1.00 55.52 O ANISOU 2513 O ARG C 114 6757 7285 7053 -2405 -1395 250 O ATOM 2514 CB ARG C 114 25.905 31.387 32.499 1.00 60.78 C ANISOU 2514 CB ARG C 114 7773 7722 7598 -2425 -1815 150 C ATOM 2515 CG ARG C 114 26.877 32.158 31.640 1.00 72.48 C ANISOU 2515 CG ARG C 114 9195 9176 9167 -2666 -1767 177 C ATOM 2516 CD ARG C 114 27.325 33.476 32.266 1.00 85.84 C ANISOU 2516 CD ARG C 114 11019 10742 10856 -2824 -1925 146 C ATOM 2517 NE ARG C 114 27.921 34.352 31.254 1.00 98.03 N ANISOU 2517 NE ARG C 114 12582 12220 12444 -3053 -1845 182 N ATOM 2518 CZ ARG C 114 29.200 34.713 31.218 1.00105.69 C ANISOU 2518 CZ ARG C 114 13392 13215 13549 -3268 -1868 174 C ATOM 2519 NH1 ARG C 114 29.631 35.507 30.248 1.00105.92 N ANISOU 2519 NH1 ARG C 114 13469 13173 13601 -3481 -1767 209 N ATOM 2520 NH2 ARG C 114 30.046 34.298 32.156 1.00108.57 N ANISOU 2520 NH2 ARG C 114 13557 13665 14028 -3276 -1998 128 N ATOM 2521 N ARG C 115 26.242 28.287 31.802 1.00 50.40 N ANISOU 2521 N ARG C 115 5992 6736 6421 -2194 -1587 189 N ATOM 2522 CA ARG C 115 26.993 27.186 31.200 1.00 50.39 C ANISOU 2522 CA ARG C 115 5726 6876 6542 -2192 -1477 206 C ATOM 2523 C ARG C 115 26.150 26.452 30.161 1.00 57.19 C ANISOU 2523 C ARG C 115 6611 7769 7348 -2084 -1295 244 C ATOM 2524 O ARG C 115 26.661 26.030 29.114 1.00 53.44 O ANISOU 2524 O ARG C 115 5998 7361 6946 -2148 -1145 269 O ATOM 2525 CB ARG C 115 27.470 26.218 32.277 1.00 48.41 C ANISOU 2525 CB ARG C 115 5323 6717 6355 -2085 -1598 174 C ATOM 2526 CG ARG C 115 28.598 26.737 33.136 1.00 63.75 C ANISOU 2526 CG ARG C 115 7172 8652 8398 -2208 -1781 135 C ATOM 2527 CD ARG C 115 28.688 25.972 34.455 1.00 68.22 C ANISOU 2527 CD ARG C 115 7714 9254 8953 -2070 -1956 104 C ATOM 2528 NE ARG C 115 29.961 26.213 35.130 1.00 82.13 N ANISOU 2528 NE ARG C 115 9322 11032 10853 -2181 -2140 66 N ATOM 2529 CZ ARG C 115 30.251 27.297 35.851 1.00 89.29 C ANISOU 2529 CZ ARG C 115 10346 11842 11738 -2296 -2309 35 C ATOM 2530 NH1 ARG C 115 29.358 28.268 36.012 1.00 88.44 N ANISOU 2530 NH1 ARG C 115 10520 11612 11472 -2308 -2312 36 N ATOM 2531 NH2 ARG C 115 31.445 27.415 36.419 1.00 91.27 N ANISOU 2531 NH2 ARG C 115 10429 12112 12136 -2395 -2486 -2 N ATOM 2532 N LEU C 116 24.856 26.286 30.438 1.00 59.22 N ANISOU 2532 N LEU C 116 7044 7977 7482 -1923 -1305 244 N ATOM 2533 CA LEU C 116 23.959 25.656 29.476 1.00 59.71 C ANISOU 2533 CA LEU C 116 7143 8051 7491 -1820 -1158 276 C ATOM 2534 C LEU C 116 23.804 26.526 28.236 1.00 59.41 C ANISOU 2534 C LEU C 116 7229 7927 7418 -1945 -1067 312 C ATOM 2535 O LEU C 116 23.879 26.036 27.101 1.00 58.92 O ANISOU 2535 O LEU C 116 7113 7906 7368 -1966 -920 346 O ATOM 2536 CB LEU C 116 22.597 25.393 30.129 1.00 53.67 C ANISOU 2536 CB LEU C 116 6530 7240 6621 -1633 -1199 255 C ATOM 2537 CG LEU C 116 22.544 24.357 31.256 1.00 50.40 C ANISOU 2537 CG LEU C 116 6037 6903 6209 -1493 -1259 228 C ATOM 2538 CD1 LEU C 116 21.145 24.286 31.855 1.00 48.72 C ANISOU 2538 CD1 LEU C 116 5996 6626 5889 -1338 -1270 202 C ATOM 2539 CD2 LEU C 116 22.986 22.980 30.746 1.00 43.99 C ANISOU 2539 CD2 LEU C 116 5019 6223 5474 -1436 -1159 252 C ATOM 2540 N LYS C 117 23.613 27.829 28.440 1.00 56.39 N ANISOU 2540 N LYS C 117 7029 7413 6982 -2034 -1156 304 N ATOM 2541 CA LYS C 117 23.410 28.745 27.323 1.00 58.99 C ANISOU 2541 CA LYS C 117 7522 7632 7260 -2153 -1094 342 C ATOM 2542 C LYS C 117 24.617 28.765 26.391 1.00 61.40 C ANISOU 2542 C LYS C 117 7695 7991 7644 -2350 -969 374 C ATOM 2543 O LYS C 117 24.470 28.709 25.163 1.00 58.83 O ANISOU 2543 O LYS C 117 7431 7643 7278 -2399 -835 416 O ATOM 2544 CB LYS C 117 23.118 30.144 27.855 1.00 62.06 C ANISOU 2544 CB LYS C 117 8126 7865 7591 -2216 -1231 322 C ATOM 2545 CG LYS C 117 22.870 31.161 26.785 1.00 65.36 C ANISOU 2545 CG LYS C 117 8748 8142 7945 -2335 -1196 363 C ATOM 2546 CD LYS C 117 21.570 31.878 27.047 1.00 67.20 C ANISOU 2546 CD LYS C 117 9227 8223 8084 -2213 -1300 342 C ATOM 2547 CE LYS C 117 21.617 32.726 28.286 1.00 59.79 C ANISOU 2547 CE LYS C 117 8371 7208 7139 -2224 -1454 287 C ATOM 2548 NZ LYS C 117 20.262 33.289 28.531 1.00 62.70 N ANISOU 2548 NZ LYS C 117 8956 7436 7431 -2075 -1532 253 N ATOM 2549 N VAL C 118 25.824 28.837 26.957 1.00 59.59 N ANISOU 2549 N VAL C 118 7284 7827 7530 -2467 -1010 348 N ATOM 2550 CA VAL C 118 27.005 28.978 26.111 1.00 59.93 C ANISOU 2550 CA VAL C 118 7190 7913 7670 -2675 -879 365 C ATOM 2551 C VAL C 118 27.348 27.660 25.421 1.00 57.41 C ANISOU 2551 C VAL C 118 6659 7735 7418 -2615 -710 372 C ATOM 2552 O VAL C 118 27.824 27.653 24.277 1.00 58.02 O ANISOU 2552 O VAL C 118 6707 7825 7512 -2744 -532 398 O ATOM 2553 CB VAL C 118 28.172 29.535 26.945 1.00 58.21 C ANISOU 2553 CB VAL C 118 6831 7710 7578 -2824 -992 326 C ATOM 2554 CG1 VAL C 118 29.442 29.595 26.134 1.00 53.63 C ANISOU 2554 CG1 VAL C 118 6060 7187 7130 -3040 -840 329 C ATOM 2555 CG2 VAL C 118 27.806 30.922 27.427 1.00 62.95 C ANISOU 2555 CG2 VAL C 118 7678 8148 8092 -2903 -1138 322 C ATOM 2556 N THR C 119 27.100 26.528 26.080 1.00 51.84 N ANISOU 2556 N THR C 119 5824 7130 6745 -2422 -754 349 N ATOM 2557 CA THR C 119 27.357 25.246 25.434 1.00 53.84 C ANISOU 2557 CA THR C 119 5893 7507 7058 -2348 -601 352 C ATOM 2558 C THR C 119 26.364 25.004 24.303 1.00 63.64 C ANISOU 2558 C THR C 119 7310 8702 8169 -2286 -471 396 C ATOM 2559 O THR C 119 26.740 24.498 23.237 1.00 63.89 O ANISOU 2559 O THR C 119 7272 8783 8221 -2338 -290 411 O ATOM 2560 CB THR C 119 27.299 24.119 26.463 1.00 60.73 C ANISOU 2560 CB THR C 119 6613 8477 7984 -2157 -699 320 C ATOM 2561 OG1 THR C 119 28.231 24.393 27.514 1.00 62.71 O ANISOU 2561 OG1 THR C 119 6723 8755 8350 -2218 -850 280 O ATOM 2562 CG2 THR C 119 27.633 22.759 25.826 1.00 57.63 C ANISOU 2562 CG2 THR C 119 6023 8207 7667 -2076 -549 318 C ATOM 2563 N GLY C 120 25.095 25.372 24.513 1.00 65.07 N ANISOU 2563 N GLY C 120 7722 8783 8220 -2176 -563 410 N ATOM 2564 CA GLY C 120 24.113 25.257 23.447 1.00 58.40 C ANISOU 2564 CA GLY C 120 7057 7873 7259 -2121 -476 448 C ATOM 2565 C GLY C 120 24.433 26.146 22.258 1.00 55.13 C ANISOU 2565 C GLY C 120 6790 7367 6789 -2318 -373 488 C ATOM 2566 O GLY C 120 24.317 25.718 21.107 1.00 54.01 O ANISOU 2566 O GLY C 120 6698 7229 6595 -2335 -229 518 O ATOM 2567 N ASP C 121 24.855 27.387 22.518 1.00 50.31 N ANISOU 2567 N ASP C 121 6270 6666 6179 -2478 -445 489 N ATOM 2568 CA ASP C 121 25.197 28.287 21.423 1.00 48.55 C ANISOU 2568 CA ASP C 121 6212 6340 5894 -2686 -347 532 C ATOM 2569 C ASP C 121 26.360 27.738 20.613 1.00 57.10 C ANISOU 2569 C ASP C 121 7107 7529 7058 -2829 -130 534 C ATOM 2570 O ASP C 121 26.310 27.733 19.377 1.00 54.46 O ANISOU 2570 O ASP C 121 6904 7151 6638 -2912 24 572 O ATOM 2571 CB ASP C 121 25.510 29.683 21.955 1.00 49.88 C ANISOU 2571 CB ASP C 121 6496 6393 6062 -2837 -468 528 C ATOM 2572 CG ASP C 121 24.266 30.420 22.458 1.00 62.49 C ANISOU 2572 CG ASP C 121 8344 7845 7555 -2714 -653 528 C ATOM 2573 OD1 ASP C 121 23.138 29.964 22.175 1.00 61.21 O ANISOU 2573 OD1 ASP C 121 8285 7655 7316 -2538 -670 537 O ATOM 2574 OD2 ASP C 121 24.413 31.458 23.145 1.00 64.48 O ANISOU 2574 OD2 ASP C 121 8682 8006 7811 -2792 -782 511 O ATOM 2575 N LEU C 122 27.401 27.237 21.289 1.00 50.51 N ANISOU 2575 N LEU C 122 5970 6829 6392 -2853 -117 487 N ATOM 2576 CA LEU C 122 28.487 26.574 20.571 1.00 54.12 C ANISOU 2576 CA LEU C 122 6205 7398 6957 -2958 98 471 C ATOM 2577 C LEU C 122 27.951 25.418 19.739 1.00 55.48 C ANISOU 2577 C LEU C 122 6387 7626 7066 -2818 235 485 C ATOM 2578 O LEU C 122 28.331 25.239 18.575 1.00 59.28 O ANISOU 2578 O LEU C 122 6894 8112 7517 -2929 447 500 O ATOM 2579 CB LEU C 122 29.555 26.082 21.550 1.00 52.55 C ANISOU 2579 CB LEU C 122 5660 7335 6971 -2952 46 408 C ATOM 2580 CG LEU C 122 30.786 25.401 20.938 1.00 62.01 C ANISOU 2580 CG LEU C 122 6574 8656 8331 -3053 260 371 C ATOM 2581 CD1 LEU C 122 31.435 26.322 19.905 1.00 68.92 C ANISOU 2581 CD1 LEU C 122 7536 9461 9189 -3332 449 390 C ATOM 2582 CD2 LEU C 122 31.826 24.983 21.985 1.00 56.31 C ANISOU 2582 CD2 LEU C 122 5505 8051 7840 -3036 160 303 C ATOM 2583 N PHE C 123 27.044 24.642 20.317 1.00 55.81 N ANISOU 2583 N PHE C 123 6427 7701 7078 -2583 120 478 N ATOM 2584 CA PHE C 123 26.418 23.544 19.598 1.00 61.01 C ANISOU 2584 CA PHE C 123 7110 8400 7672 -2439 221 490 C ATOM 2585 C PHE C 123 25.684 24.046 18.356 1.00 61.82 C ANISOU 2585 C PHE C 123 7522 8371 7596 -2501 295 545 C ATOM 2586 O PHE C 123 25.806 23.464 17.271 1.00 64.79 O ANISOU 2586 O PHE C 123 7925 8769 7925 -2528 473 557 O ATOM 2587 CB PHE C 123 25.466 22.826 20.552 1.00 60.97 C ANISOU 2587 CB PHE C 123 7082 8425 7659 -2195 62 476 C ATOM 2588 CG PHE C 123 25.413 21.362 20.354 1.00 62.35 C ANISOU 2588 CG PHE C 123 7105 8711 7873 -2046 149 459 C ATOM 2589 CD1 PHE C 123 26.526 20.586 20.597 1.00 62.16 C ANISOU 2589 CD1 PHE C 123 6794 8817 8006 -2052 224 418 C ATOM 2590 CD2 PHE C 123 24.241 20.753 19.936 1.00 67.28 C ANISOU 2590 CD2 PHE C 123 7871 9304 8391 -1895 146 480 C ATOM 2591 CE1 PHE C 123 26.482 19.222 20.409 1.00 72.55 C ANISOU 2591 CE1 PHE C 123 7982 10225 9361 -1908 300 401 C ATOM 2592 CE2 PHE C 123 24.182 19.386 19.745 1.00 68.29 C ANISOU 2592 CE2 PHE C 123 7870 9524 8552 -1761 224 464 C ATOM 2593 CZ PHE C 123 25.301 18.616 19.980 1.00 71.49 C ANISOU 2593 CZ PHE C 123 8006 10055 9103 -1765 304 426 C ATOM 2594 N ASP C 124 24.946 25.151 18.495 1.00 52.85 N ANISOU 2594 N ASP C 124 6635 7089 6357 -2526 152 575 N ATOM 2595 CA ASP C 124 24.139 25.672 17.401 1.00 51.25 C ANISOU 2595 CA ASP C 124 6752 6739 5982 -2562 169 627 C ATOM 2596 C ASP C 124 25.007 26.159 16.244 1.00 57.77 C ANISOU 2596 C ASP C 124 7672 7520 6756 -2806 367 658 C ATOM 2597 O ASP C 124 24.713 25.876 15.075 1.00 63.12 O ANISOU 2597 O ASP C 124 8520 8150 7312 -2828 484 690 O ATOM 2598 CB ASP C 124 23.245 26.792 17.929 1.00 55.11 C ANISOU 2598 CB ASP C 124 7462 7076 6402 -2528 -44 641 C ATOM 2599 CG ASP C 124 22.260 27.292 16.896 1.00 66.35 C ANISOU 2599 CG ASP C 124 9221 8333 7658 -2524 -79 691 C ATOM 2600 OD1 ASP C 124 22.408 28.457 16.462 1.00 65.77 O ANISOU 2600 OD1 ASP C 124 9367 8116 7505 -2688 -100 727 O ATOM 2601 OD2 ASP C 124 21.350 26.508 16.514 1.00 73.01 O ANISOU 2601 OD2 ASP C 124 10110 9180 8452 -2359 -96 694 O ATOM 2602 N ILE C 125 26.085 26.881 16.554 1.00 56.30 N ANISOU 2602 N ILE C 125 7385 7346 6660 -3001 409 644 N ATOM 2603 CA ILE C 125 27.021 27.329 15.528 1.00 55.82 C ANISOU 2603 CA ILE C 125 7384 7253 6572 -3257 628 664 C ATOM 2604 C ILE C 125 27.577 26.146 14.745 1.00 65.05 C ANISOU 2604 C ILE C 125 8390 8548 7778 -3252 872 641 C ATOM 2605 O ILE C 125 27.665 26.188 13.513 1.00 80.44 O ANISOU 2605 O ILE C 125 10526 10436 9602 -3373 1055 672 O ATOM 2606 CB ILE C 125 28.146 28.160 16.166 1.00 58.83 C ANISOU 2606 CB ILE C 125 7609 7651 7092 -3455 627 638 C ATOM 2607 CG1 ILE C 125 27.556 29.327 16.950 1.00 56.46 C ANISOU 2607 CG1 ILE C 125 7493 7215 6744 -3451 380 656 C ATOM 2608 CG2 ILE C 125 29.093 28.679 15.100 1.00 64.47 C ANISOU 2608 CG2 ILE C 125 8393 8323 7781 -3742 872 656 C ATOM 2609 CD1 ILE C 125 28.581 30.290 17.455 1.00 66.55 C ANISOU 2609 CD1 ILE C 125 8682 8473 8130 -3670 367 638 C ATOM 2610 N MET C 126 27.932 25.065 15.431 1.00 71.92 N ANISOU 2610 N MET C 126 8934 9583 8810 -3108 875 584 N ATOM 2611 CA MET C 126 28.557 23.916 14.775 1.00 80.37 C ANISOU 2611 CA MET C 126 9817 10776 9944 -3094 1106 548 C ATOM 2612 C MET C 126 27.507 22.974 14.176 1.00 93.74 C ANISOU 2612 C MET C 126 11655 12459 11504 -2902 1110 568 C ATOM 2613 O MET C 126 27.450 21.784 14.477 1.00102.60 O ANISOU 2613 O MET C 126 12579 13697 12708 -2727 1117 531 O ATOM 2614 CB MET C 126 29.457 23.187 15.762 1.00 74.31 C ANISOU 2614 CB MET C 126 8638 10176 9420 -3024 1092 475 C ATOM 2615 CG MET C 126 30.381 24.108 16.516 1.00 75.24 C ANISOU 2615 CG MET C 126 8606 10300 9683 -3189 1029 450 C ATOM 2616 SD MET C 126 31.533 23.205 17.558 1.00 86.54 S ANISOU 2616 SD MET C 126 9550 11917 11413 -3113 1004 359 S ATOM 2617 CE MET C 126 32.470 22.310 16.319 1.00 92.77 C ANISOU 2617 CE MET C 126 10161 12803 12285 -3195 1362 312 C ATOM 2618 N SER C 127 26.675 23.529 13.301 1.00 98.01 N ANISOU 2618 N SER C 127 12556 12847 11836 -2943 1094 629 N ATOM 2619 CA SER C 127 25.629 22.751 12.637 1.00 98.30 C ANISOU 2619 CA SER C 127 12764 12849 11736 -2781 1077 650 C ATOM 2620 C SER C 127 25.071 23.514 11.444 1.00 96.82 C ANISOU 2620 C SER C 127 12985 12479 11321 -2898 1100 715 C ATOM 2621 O SER C 127 25.459 24.658 11.193 1.00 97.44 O ANISOU 2621 O SER C 127 13223 12456 11345 -3100 1124 747 O ATOM 2622 CB SER C 127 24.503 22.404 13.616 1.00 99.51 C ANISOU 2622 CB SER C 127 12885 13009 11915 -2534 824 645 C ATOM 2623 OG SER C 127 23.868 23.572 14.109 1.00101.67 O ANISOU 2623 OG SER C 127 13338 13155 12137 -2549 621 676 O TER 2624 SER C 127 HETATM 2625 O HOH A 301 0.675 10.964 19.330 1.00 47.84 O ANISOU 2625 O HOH A 301 5646 6055 6475 356 -805 -43 O HETATM 2626 O HOH A 302 13.204 -25.723 31.343 1.00 66.07 O ANISOU 2626 O HOH A 302 9745 7596 7763 1510 -427 850 O HETATM 2627 O HOH A 303 7.171 1.692 32.838 1.00 48.54 O ANISOU 2627 O HOH A 303 5817 6866 5761 267 306 233 O HETATM 2628 O HOH A 304 5.756 5.234 23.197 1.00 56.98 O ANISOU 2628 O HOH A 304 6556 7842 7250 248 -52 183 O HETATM 2629 O HOH A 305 3.304 -11.926 5.949 1.00 52.61 O ANISOU 2629 O HOH A 305 7607 6360 6024 410 -268 -17 O HETATM 2630 O HOH A 306 18.155 -9.043 17.376 1.00 45.04 O ANISOU 2630 O HOH A 306 4616 6722 5775 888 745 186 O HETATM 2631 O HOH A 307 -1.616 -20.352 27.399 1.00 47.73 O ANISOU 2631 O HOH A 307 6346 5614 6176 -87 1032 344 O HETATM 2632 O HOH A 308 18.773 -0.022 28.056 1.00 45.82 O ANISOU 2632 O HOH A 308 4566 7014 5830 451 -219 413 O HETATM 2633 O HOH A 309 2.758 -16.643 16.993 1.00 38.09 O ANISOU 2633 O HOH A 309 4780 4785 4907 527 269 167 O HETATM 2634 O HOH A 310 17.199 -4.163 34.565 1.00 51.22 O ANISOU 2634 O HOH A 310 6092 7322 6049 715 -628 561 O HETATM 2635 O HOH A 311 6.323 -25.813 13.476 1.00 68.01 O ANISOU 2635 O HOH A 311 9485 7966 8391 1025 342 44 O HETATM 2636 O HOH A 312 10.666 -25.554 32.838 1.00 52.97 O ANISOU 2636 O HOH A 312 8436 5830 5861 1133 -179 937 O HETATM 2637 O HOH A 313 -1.276 -18.713 19.539 1.00 52.52 O ANISOU 2637 O HOH A 313 6540 6358 7057 214 387 124 O HETATM 2638 O HOH A 314 4.096 -18.383 6.041 1.00 46.40 O ANISOU 2638 O HOH A 314 7013 5374 5244 612 0 -130 O HETATM 2639 O HOH A 315 5.869 -10.997 35.251 1.00 45.93 O ANISOU 2639 O HOH A 315 6387 6014 5049 300 662 557 O HETATM 2640 O HOH A 316 3.803 -15.793 5.709 1.00 42.49 O ANISOU 2640 O HOH A 316 6467 4963 4715 523 -102 -91 O HETATM 2641 O HOH A 317 5.195 -3.085 9.718 1.00 45.24 O ANISOU 2641 O HOH A 317 6079 5879 5233 257 -207 197 O HETATM 2642 O HOH A 318 4.609 6.958 27.398 1.00 44.46 O ANISOU 2642 O HOH A 318 4973 6226 5693 258 56 56 O HETATM 2643 O HOH A 319 1.397 -5.128 15.035 1.00 50.28 O ANISOU 2643 O HOH A 319 5985 6573 6545 373 -212 95 O HETATM 2644 O HOH A 320 -0.515 -13.484 15.630 1.00 55.70 O ANISOU 2644 O HOH A 320 6781 6980 7402 347 -1 39 O HETATM 2645 O HOH A 321 7.196 -10.365 37.570 1.00 44.88 O ANISOU 2645 O HOH A 321 6580 5836 4637 312 516 623 O HETATM 2646 O HOH A 322 6.962 -3.349 2.947 1.00 61.43 O ANISOU 2646 O HOH A 322 9377 7556 6409 27 -106 183 O HETATM 2647 O HOH A 323 1.737 10.693 22.345 1.00 28.65 O ANISOU 2647 O HOH A 323 3063 3829 3995 327 -487 -54 O HETATM 2648 O HOH A 324 9.977 -26.525 30.297 1.00 53.50 O ANISOU 2648 O HOH A 324 8294 5906 6127 1156 -41 832 O HETATM 2649 O HOH A 325 2.296 4.241 19.915 1.00 55.58 O ANISOU 2649 O HOH A 325 6400 7414 7304 321 -269 81 O HETATM 2650 O HOH A 326 5.741 -1.180 36.185 1.00 54.22 O ANISOU 2650 O HOH A 326 6977 7411 6211 205 601 251 O HETATM 2651 O HOH A 327 0.328 -16.350 15.560 1.00 56.78 O ANISOU 2651 O HOH A 327 7122 7019 7431 393 98 70 O HETATM 2652 O HOH A 328 8.583 1.547 30.797 1.00 38.90 O ANISOU 2652 O HOH A 328 4427 5730 4622 303 178 291 O HETATM 2653 O HOH A 329 6.335 -0.270 39.063 1.00 58.13 O ANISOU 2653 O HOH A 329 7875 7826 6385 140 590 247 O HETATM 2654 O HOH A 330 4.979 -20.527 4.091 1.00 56.05 O ANISOU 2654 O HOH A 330 8652 6411 6235 697 104 -238 O HETATM 2655 O HOH A 331 15.256 -26.211 29.562 1.00 57.81 O ANISOU 2655 O HOH A 331 8359 6626 6982 1835 -547 729 O HETATM 2656 O HOH A 332 1.431 -18.599 18.612 1.00 47.79 O ANISOU 2656 O HOH A 332 6067 5864 6227 433 343 184 O HETATM 2657 O HOH A 333 19.534 -8.242 15.239 1.00 51.73 O ANISOU 2657 O HOH A 333 5408 7635 6613 794 1017 101 O HETATM 2658 O HOH A 334 0.408 -16.118 4.015 1.00 63.07 O ANISOU 2658 O HOH A 334 9314 7233 7416 381 -656 -181 O HETATM 2659 O HOH A 335 1.357 -14.263 6.784 1.00 52.99 O ANISOU 2659 O HOH A 335 7533 6273 6329 418 -411 -74 O HETATM 2660 O HOH B 301 9.584 1.334 25.697 1.00 48.32 O ANISOU 2660 O HOH B 301 5385 6996 5979 318 127 326 O HETATM 2661 O HOH B 302 9.380 23.793 43.931 1.00 62.20 O ANISOU 2661 O HOH B 302 9447 7623 6563 -233 -601 -640 O HETATM 2662 O HOH B 303 7.565 19.440 14.249 1.00 49.88 O ANISOU 2662 O HOH B 303 7416 5855 5683 -460 -1132 444 O HETATM 2663 O HOH B 304 -5.380 -11.212 32.843 1.00 51.93 O ANISOU 2663 O HOH B 304 6191 6545 6994 -376 1792 -61 O HETATM 2664 O HOH B 305 -3.417 -11.198 30.641 1.00 33.67 O ANISOU 2664 O HOH B 305 3844 4330 4620 -150 1355 52 O HETATM 2665 O HOH B 306 14.130 33.578 19.669 1.00 48.14 O ANISOU 2665 O HOH B 306 8254 4838 5200 -1689 -1548 534 O HETATM 2666 O HOH B 307 -3.154 -10.091 34.138 1.00 54.18 O ANISOU 2666 O HOH B 307 6761 6918 6907 -252 1670 61 O HETATM 2667 O HOH D 201 15.790 -20.358 33.133 1.00 52.81 O ANISOU 2667 O HOH D 201 7463 6447 6154 1516 -671 813 O HETATM 2668 O HOH C 201 19.112 27.259 15.776 1.00 68.77 O ANISOU 2668 O HOH C 201 10032 8364 7732 -2186 -354 732 O CONECT 2297 2299 CONECT 2299 2297 2300 CONECT 2300 2299 2301 2308 CONECT 2301 2300 2302 2303 CONECT 2302 2301 CONECT 2303 2301 2304 CONECT 2304 2303 2305 2306 2307 CONECT 2305 2304 CONECT 2306 2304 CONECT 2307 2304 CONECT 2308 2300 2309 2310 CONECT 2309 2308 CONECT 2310 2308 CONECT 2462 2464 CONECT 2464 2462 2465 CONECT 2465 2464 2466 2473 CONECT 2466 2465 2467 2468 CONECT 2467 2466 CONECT 2468 2466 2469 CONECT 2469 2468 2470 2471 2472 CONECT 2470 2469 CONECT 2471 2469 CONECT 2472 2469 CONECT 2473 2465 2474 2475 CONECT 2474 2473 CONECT 2475 2473 MASTER 332 0 2 16 0 0 0 6 2653 4 26 28 END
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Related entries of code: 6dcn
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Protein Sequence Similarity
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PDBbind
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Complexes with the same small molecule ligand
PDB Code
Check Database
Ligand Name
No complexes with the same small molecule ligand are found!
Entry Information
PDB ID
6dcn
Complex Type
Protein-Protein
PDBbind Subset
general set
Protein Name
BCL-xl protein, BCL2L1
Ligand Name
Beclin 1 BH3 domain T108pThr, BECN1 pThr
EC.Number
E.C.-.-.-.-
Resolution
2.44(Å)
Affinity (Kd/Ki/IC50)
Kd=1.4uM
Release Year
2018
Protein/NA Sequence
Check fasta file
Primary Reference
(2019) Autophagy Vol. 15: pp. 785-795
Links to External Databases
RCSB PDB
The mother database
PDBsum
Enhanced annotations on PDB entries
Pubchem
Comprehensive collection of chemical and biological data
UniProtKB AC
UniProt accession number (AC):
Q07817
Q14457
Entrez Gene ID
NCBI Entrez Gene ID:
598
8678
ASD
Information of known allosteric effects of PDB entries
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