HEADER MEMBRANE PROTEIN 07-JUL-23 8TF5 TITLE CRYSTAL STRUCTURE OF ORPHAN G PROTEIN-COUPLED RECEPTOR 6, PSEUDOAPO TITLE 2 FORM COMPND MOL_ID: 1; COMPND 2 MOLECULE: G-PROTEIN COUPLED RECEPTOR 6,SOLUBLE CYTOCHROME B562 COMPND 3 CHIMERA,SOLUBLE CYTOCHROME B562,G-PROTEIN COUPLED RECEPTOR 6; COMPND 4 CHAIN: A; COMPND 5 SYNONYM: CYTOCHROME B-562; COMPND 6 ENGINEERED: YES; COMPND 7 MUTATION: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS, ESCHERICHIA COLI; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606, 562; SOURCE 5 GENE: GPR6, CYBC; SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM; SOURCE 8 EXPRESSION_SYSTEM_TAXID: 7108 KEYWDS ORPHAN GPCR, GPR6, PSEUDOAPO FORM, BRIL, LCP, MEMBRANE PROTEIN, KEYWDS 2 PARKINSON'S DISEASE, ACTIVE-LIKE CONFORMATION EXPDTA X-RAY DIFFRACTION AUTHOR M.BAREKATAIN,L.JOHANSSON,J.H.LAM,A.V.SADYBEKOV,G.W.HAN,P.POPOV, AUTHOR 2 J.RUSSO,J.BLIESATH,N.BRICE,M.BERESFORD,L.CARLSON,K.S.SAIKATENDU, AUTHOR 3 H.SUN,S.MURPHY,H.MONENSCHEIN,H.H.SCHIFFER,C.LUTOMSKI,C.V.ROBINSON, AUTHOR 4 Z.LIU,T.HUA,V.KATRITCH,V.CHEREZOV REVDAT 2 18-DEC-24 8TF5 1 JRNL REVDAT 1 04-DEC-24 8TF5 0 JRNL AUTH M.BAREKATAIN,L.C.JOHANSSON,J.H.LAM,H.CHANG,A.V.SADYBEKOV, JRNL AUTH 2 G.W.HAN,J.RUSSO,J.BLIESATH,N.L.BRICE,M.B.L.CARLTON, JRNL AUTH 3 K.S.SAIKATENDU,H.SUN,S.T.MURPHY,H.MONENSCHEIN,H.H.SCHIFFER, JRNL AUTH 4 P.POPOV,C.A.LUTOMSKI,C.V.ROBINSON,Z.J.LIU,T.HUA,V.KATRITCH, JRNL AUTH 5 V.CHEREZOV JRNL TITL STRUCTURAL INSIGHTS INTO THE HIGH BASAL ACTIVITY AND INVERSE JRNL TITL 2 AGONISM OF THE ORPHAN RECEPTOR GPR6 IMPLICATED IN JRNL TITL 3 PARKINSON'S DISEASE. JRNL REF SCI.SIGNAL. V. 17 O8741 2024 JRNL REFN ESSN 1937-9145 JRNL PMID 39626010 JRNL DOI 10.1126/SCISIGNAL.ADO8741 REMARK 2 REMARK 2 RESOLUTION. 2.10 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX (1.20.1_4487: ???) 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 : ML REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.44 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350 REMARK 3 COMPLETENESS FOR RANGE (%) : 96.0 REMARK 3 NUMBER OF REFLECTIONS : 30995 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.186 REMARK 3 R VALUE (WORKING SET) : 0.185 REMARK 3 FREE R VALUE : 0.214 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.410 REMARK 3 FREE R VALUE TEST SET COUNT : 1677 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 29.4400 - 4.8000 0.99 2687 157 0.1961 0.2176 REMARK 3 2 4.8000 - 3.8100 1.00 2586 145 0.1587 0.1772 REMARK 3 3 3.8100 - 3.3300 1.00 2558 150 0.1732 0.2310 REMARK 3 4 3.3300 - 3.0300 0.99 2541 132 0.1864 0.2485 REMARK 3 5 3.0300 - 2.8100 1.00 2519 152 0.1701 0.1871 REMARK 3 6 2.8100 - 2.6500 1.00 2503 168 0.1638 0.1706 REMARK 3 7 2.6500 - 2.5100 0.99 2485 143 0.1782 0.2183 REMARK 3 8 2.5100 - 2.4000 0.99 2454 158 0.2000 0.2493 REMARK 3 9 2.4000 - 2.3100 0.98 2463 138 0.2107 0.2865 REMARK 3 10 2.3100 - 2.2300 0.95 2416 128 0.2293 0.2465 REMARK 3 11 2.2300 - 2.1600 0.88 2220 105 0.2577 0.2544 REMARK 3 12 2.1600 - 2.1000 0.75 1886 101 0.2898 0.2802 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL REMARK 3 SOLVENT RADIUS : 1.11 REMARK 3 SHRINKAGE RADIUS : 0.90 REMARK 3 K_SOL : NULL REMARK 3 B_SOL : NULL REMARK 3 REMARK 3 ERROR ESTIMATES. REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.220 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 21.440 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 : 0.003 3294 REMARK 3 ANGLE : 0.695 4398 REMARK 3 CHIRALITY : 0.038 504 REMARK 3 PLANARITY : 0.004 527 REMARK 3 DIHEDRAL : 13.722 1321 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 2 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: ( CHAIN A AND RESID 70:223 ) REMARK 3 ORIGIN FOR THE GROUP (A): 29.455 17.968 46.658 REMARK 3 T TENSOR REMARK 3 T11: 0.2364 T22: 0.1863 REMARK 3 T33: 0.2796 T12: 0.0081 REMARK 3 T13: 0.0036 T23: -0.0066 REMARK 3 L TENSOR REMARK 3 L11: 1.6428 L22: 1.3469 REMARK 3 L33: 0.2843 L12: 0.1541 REMARK 3 L13: 0.0145 L23: -0.2911 REMARK 3 S TENSOR REMARK 3 S11: -0.0201 S12: 0.0035 S13: -0.0209 REMARK 3 S21: 0.0596 S22: -0.0578 S23: -0.0447 REMARK 3 S31: 0.0446 S32: -0.0194 S33: -0.0001 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: ( CHAIN 'A' AND (RESID 224 THROUGH 256 OR RESID 1001 REMARK 3 THROUGH 1106 OR RESID 900 OR RESID 270 THROUGH 347 )) REMARK 3 ORIGIN FOR THE GROUP (A): 14.175 16.846 21.635 REMARK 3 T TENSOR REMARK 3 T11: 0.5243 T22: 0.5137 REMARK 3 T33: 0.4067 T12: 0.0190 REMARK 3 T13: -0.0332 T23: -0.0319 REMARK 3 L TENSOR REMARK 3 L11: 0.5176 L22: 0.0373 REMARK 3 L33: 0.6995 L12: -0.0526 REMARK 3 L13: 0.0998 L23: -0.4571 REMARK 3 S TENSOR REMARK 3 S11: 0.0143 S12: 0.2998 S13: -0.0498 REMARK 3 S21: -0.1949 S22: -0.0211 S23: 0.0610 REMARK 3 S31: 0.2014 S32: -0.2202 S33: 0.0001 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 8TF5 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-JUL-23. REMARK 100 THE DEPOSITION ID IS D_1000275785. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 27-FEB-20 REMARK 200 TEMPERATURE (KELVIN) : 123 REMARK 200 PH : NULL REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : APS REMARK 200 BEAMLINE : 23-ID-B REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.0332 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 16M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000 REMARK 200 DATA SCALING SOFTWARE : HKL-2000 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 31292 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100 REMARK 200 RESOLUTION RANGE LOW (A) : 30.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 96.8 REMARK 200 DATA REDUNDANCY : 6.900 REMARK 200 R MERGE (I) : 0.19100 REMARK 200 R SYM (I) : NULL REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.2000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.18 REMARK 200 COMPLETENESS FOR SHELL (%) : NULL REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : 0.63800 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.200 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: NULL REMARK 200 REMARK 200 REMARK: ORTHORHOMBIC CRYSTALS REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 56.49 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.83 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: NACH3COO, PEG 400, NACL, PPG P40, REMARK 280 LIPIDIC CUBIC PHASE, TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 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 -X+1/2,Y+1/2,-Z REMARK 290 4555 X+1/2,-Y+1/2,-Z REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 28.51650 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 48.43350 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 28.51650 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 48.43350 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 300 REMARK: THE AUTHOR STATES THAT THE BIOLOGICAL UNIT OF THIS PROTEIN REMARK 300 IS UNKNOWN. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 MET A 32 REMARK 465 LYS A 33 REMARK 465 THR A 34 REMARK 465 ILE A 35 REMARK 465 ILE A 36 REMARK 465 ALA A 37 REMARK 465 LEU A 38 REMARK 465 SER A 39 REMARK 465 TYR A 40 REMARK 465 ILE A 41 REMARK 465 PHE A 42 REMARK 465 CYS A 43 REMARK 465 LEU A 44 REMARK 465 VAL A 45 REMARK 465 PHE A 46 REMARK 465 ALA A 47 REMARK 465 GLY A 48 REMARK 465 GLY A 49 REMARK 465 ALA A 50 REMARK 465 ASN A 51 REMARK 465 GLY A 52 REMARK 465 SER A 53 REMARK 465 LEU A 54 REMARK 465 GLU A 55 REMARK 465 LEU A 56 REMARK 465 SER A 57 REMARK 465 SER A 58 REMARK 465 GLN A 59 REMARK 465 LEU A 60 REMARK 465 SER A 61 REMARK 465 ALA A 62 REMARK 465 GLY A 63 REMARK 465 PRO A 64 REMARK 465 PRO A 65 REMARK 465 GLY A 66 REMARK 465 LEU A 67 REMARK 465 LEU A 68 REMARK 465 LEU A 69 REMARK 465 ASP A 1050 REMARK 465 LYS A 1051 REMARK 465 SER A 1052 REMARK 465 PRO A 1053 REMARK 465 ASP A 1054 REMARK 465 SER A 1055 REMARK 465 PRO A 1056 REMARK 465 GLU A 1057 REMARK 465 PHE A 348 REMARK 465 GLN A 349 REMARK 465 SER A 350 REMARK 465 LYS A 351 REMARK 465 VAL A 352 REMARK 465 PRO A 353 REMARK 465 PHE A 354 REMARK 465 ARG A 355 REMARK 465 SER A 356 REMARK 465 ARG A 357 REMARK 465 SER A 358 REMARK 465 PRO A 359 REMARK 465 SER A 360 REMARK 465 GLU A 361 REMARK 465 VAL A 362 REMARK 465 GLU A 363 REMARK 465 PHE A 364 REMARK 465 HIS A 365 REMARK 465 HIS A 366 REMARK 465 HIS A 367 REMARK 465 HIS A 368 REMARK 465 HIS A 369 REMARK 465 HIS A 370 REMARK 465 HIS A 371 REMARK 465 HIS A 372 REMARK 465 HIS A 373 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 A1042 CG CD CE NZ REMARK 470 LYS A1047 CG CD CE NZ REMARK 470 LEU A1048 CG CD1 CD2 REMARK 470 GLU A1049 CG CD OE1 OE2 REMARK 470 ARG A 279 NE CZ NH1 NH2 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 PRO A 221 33.73 -98.50 REMARK 500 LEU A1048 -172.66 177.81 REMARK 500 LYS A1083 66.17 -101.22 REMARK 500 REMARK 500 REMARK: NULL REMARK 610 REMARK 610 MISSING HETEROATOM REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 610 I=INSERTION CODE): REMARK 610 M RES C SSEQI REMARK 610 OLC A 1201 REMARK 610 P15 A 1205 REMARK 610 OLA A 1213 REMARK 610 OLA A 1215 REMARK 610 OLA A 1216 REMARK 610 OLA A 1219 DBREF 8TF5 A 48 256 UNP P46095 GPR6_HUMAN 48 256 DBREF 8TF5 A 1001 1106 UNP P0ABE7 C562_ECOLX 23 128 DBREF 8TF5 A 270 362 UNP P46095 GPR6_HUMAN 270 362 SEQADV 8TF5 MET A 32 UNP P46095 INITIATING METHIONINE SEQADV 8TF5 LYS A 33 UNP P46095 EXPRESSION TAG SEQADV 8TF5 THR A 34 UNP P46095 EXPRESSION TAG SEQADV 8TF5 ILE A 35 UNP P46095 EXPRESSION TAG SEQADV 8TF5 ILE A 36 UNP P46095 EXPRESSION TAG SEQADV 8TF5 ALA A 37 UNP P46095 EXPRESSION TAG SEQADV 8TF5 LEU A 38 UNP P46095 EXPRESSION TAG SEQADV 8TF5 SER A 39 UNP P46095 EXPRESSION TAG SEQADV 8TF5 TYR A 40 UNP P46095 EXPRESSION TAG SEQADV 8TF5 ILE A 41 UNP P46095 EXPRESSION TAG SEQADV 8TF5 PHE A 42 UNP P46095 EXPRESSION TAG SEQADV 8TF5 CYS A 43 UNP P46095 EXPRESSION TAG SEQADV 8TF5 LEU A 44 UNP P46095 EXPRESSION TAG SEQADV 8TF5 VAL A 45 UNP P46095 EXPRESSION TAG SEQADV 8TF5 PHE A 46 UNP P46095 EXPRESSION TAG SEQADV 8TF5 ALA A 47 UNP P46095 EXPRESSION TAG SEQADV 8TF5 LEU A 123 UNP P46095 CYS 123 ENGINEERED MUTATION SEQADV 8TF5 PRO A 173 UNP P46095 ALA 173 ENGINEERED MUTATION SEQADV 8TF5 TRP A 1007 UNP P0ABE7 MET 29 ENGINEERED MUTATION SEQADV 8TF5 ILE A 1102 UNP P0ABE7 HIS 124 ENGINEERED MUTATION SEQADV 8TF5 LEU A 1106 UNP P0ABE7 ARG 128 ENGINEERED MUTATION SEQADV 8TF5 ALA A 900 UNP P0ABE7 LINKER SEQADV 8TF5 ARG A 279 UNP P46095 GLY 279 ENGINEERED MUTATION SEQADV 8TF5 CYS A 291 UNP P46095 SER 291 ENGINEERED MUTATION SEQADV 8TF5 LEU A 320 UNP P46095 TYR 320 ENGINEERED MUTATION SEQADV 8TF5 ASP A 345 UNP P46095 CYS 345 ENGINEERED MUTATION SEQADV 8TF5 GLU A 363 UNP P46095 EXPRESSION TAG SEQADV 8TF5 PHE A 364 UNP P46095 EXPRESSION TAG SEQADV 8TF5 HIS A 365 UNP P46095 EXPRESSION TAG SEQADV 8TF5 HIS A 366 UNP P46095 EXPRESSION TAG SEQADV 8TF5 HIS A 367 UNP P46095 EXPRESSION TAG SEQADV 8TF5 HIS A 368 UNP P46095 EXPRESSION TAG SEQADV 8TF5 HIS A 369 UNP P46095 EXPRESSION TAG SEQADV 8TF5 HIS A 370 UNP P46095 EXPRESSION TAG SEQADV 8TF5 HIS A 371 UNP P46095 EXPRESSION TAG SEQADV 8TF5 HIS A 372 UNP P46095 EXPRESSION TAG SEQADV 8TF5 HIS A 373 UNP P46095 EXPRESSION TAG SEQRES 1 A 436 MET LYS THR ILE ILE ALA LEU SER TYR ILE PHE CYS LEU SEQRES 2 A 436 VAL PHE ALA GLY GLY ALA ASN GLY SER LEU GLU LEU SER SEQRES 3 A 436 SER GLN LEU SER ALA GLY PRO PRO GLY LEU LEU LEU PRO SEQRES 4 A 436 ALA VAL ASN PRO TRP ASP VAL LEU LEU CYS VAL SER GLY SEQRES 5 A 436 THR VAL ILE ALA GLY GLU ASN ALA LEU VAL VAL ALA LEU SEQRES 6 A 436 ILE ALA SER THR PRO ALA LEU ARG THR PRO MET PHE VAL SEQRES 7 A 436 LEU VAL GLY SER LEU ALA THR ALA ASP LEU LEU ALA GLY SEQRES 8 A 436 LEU GLY LEU ILE LEU HIS PHE VAL PHE GLN TYR LEU VAL SEQRES 9 A 436 PRO SER GLU THR VAL SER LEU LEU THR VAL GLY PHE LEU SEQRES 10 A 436 VAL ALA SER PHE ALA ALA SER VAL SER SER LEU LEU ALA SEQRES 11 A 436 ILE THR VAL ASP ARG TYR LEU SER LEU TYR ASN PRO LEU SEQRES 12 A 436 THR TYR TYR SER ARG ARG THR LEU LEU GLY VAL HIS LEU SEQRES 13 A 436 LEU LEU ALA ALA THR TRP THR VAL SER LEU GLY LEU GLY SEQRES 14 A 436 LEU LEU PRO VAL LEU GLY TRP ASN CYS LEU ALA GLU ARG SEQRES 15 A 436 ALA ALA CYS SER VAL VAL ARG PRO LEU ALA ARG SER HIS SEQRES 16 A 436 VAL ALA LEU LEU SER ALA ALA PHE PHE MET VAL PHE GLY SEQRES 17 A 436 ILE MET LEU HIS LEU TYR VAL ARG ILE YCM GLN VAL VAL SEQRES 18 A 436 TRP ARG HIS ALA ALA ASP LEU GLU ASP ASN TRP GLU THR SEQRES 19 A 436 LEU ASN ASP ASN LEU LYS VAL ILE GLU LYS ALA ASP ASN SEQRES 20 A 436 ALA ALA GLN VAL LYS ASP ALA LEU THR LYS MET ARG ALA SEQRES 21 A 436 ALA ALA LEU ASP ALA GLN LYS ALA THR PRO PRO LYS LEU SEQRES 22 A 436 GLU ASP LYS SER PRO ASP SER PRO GLU MET LYS ASP PHE SEQRES 23 A 436 ARG HIS GLY PHE ASP ILE LEU VAL GLY GLN ILE ASP ASP SEQRES 24 A 436 ALA LEU LYS LEU ALA ASN GLU GLY LYS VAL LYS GLU ALA SEQRES 25 A 436 GLN ALA ALA ALA GLU GLN LEU LYS THR THR ARG ASN ALA SEQRES 26 A 436 TYR ILE GLN LYS TYR LEU ALA HIS LEU ALA ALA THR ARG SEQRES 27 A 436 LYS GLY VAL ARG THR LEU ALA VAL VAL LEU GLY THR PHE SEQRES 28 A 436 GLY ALA CYS TRP LEU PRO PHE ALA ILE TYR CYS VAL VAL SEQRES 29 A 436 GLY SER HIS GLU ASP PRO ALA VAL TYR THR TYR ALA THR SEQRES 30 A 436 LEU LEU PRO ALA THR LEU ASN SER MET ILE ASN PRO ILE SEQRES 31 A 436 ILE TYR ALA PHE ARG ASN GLN GLU ILE GLN ARG ALA LEU SEQRES 32 A 436 TRP LEU LEU LEU ASP GLY CYS PHE GLN SER LYS VAL PRO SEQRES 33 A 436 PHE ARG SER ARG SER PRO SER GLU VAL GLU PHE HIS HIS SEQRES 34 A 436 HIS HIS HIS HIS HIS HIS HIS MODRES 8TF5 YCM A 249 CYS MODIFIED RESIDUE HET YCM A 249 10 HET OLC A1201 16 HET OLC A1202 25 HET P15 A1203 20 HET OLA A1204 20 HET P15 A1205 14 HET OLA A1206 20 HET OLA A1207 20 HET OLA A1208 20 HET OLA A1209 20 HET OLA A1210 20 HET OLC A1211 25 HET OLC A1212 25 HET OLA A1213 13 HET OLC A1214 25 HET OLA A1215 14 HET OLA A1216 9 HET OLA A1217 20 HET OLA A1218 20 HET OLA A1219 13 HET CLR A1220 28 HETNAM YCM S-(2-AMINO-2-OXOETHYL)-L-CYSTEINE HETNAM OLC (2R)-2,3-DIHYDROXYPROPYL (9Z)-OCTADEC-9-ENOATE HETNAM P15 2,5,8,11,14,17-HEXAOXANONADECAN-19-OL HETNAM OLA OLEIC ACID HETNAM CLR CHOLESTEROL HETSYN YCM CYSTEINE-S-ACETAMIDE HETSYN OLC 1-OLEOYL-R-GLYCEROL FORMUL 1 YCM C5 H10 N2 O3 S FORMUL 2 OLC 5(C21 H40 O4) FORMUL 4 P15 2(C13 H28 O7) FORMUL 5 OLA 12(C18 H34 O2) FORMUL 21 CLR C27 H46 O FORMUL 22 HOH *74(H2 O) HELIX 1 AA1 ASN A 73 SER A 99 1 27 HELIX 2 AA2 THR A 105 LEU A 134 1 30 HELIX 3 AA3 SER A 137 ASN A 172 1 36 HELIX 4 AA4 SER A 178 GLY A 206 1 29 HELIX 5 AA5 GLU A 212 CYS A 216 5 5 HELIX 6 AA6 ALA A 223 ALA A 1020 1 54 HELIX 7 AA7 ASN A 1022 THR A 1044 1 23 HELIX 8 AA8 ASP A 1060 GLU A 1081 1 22 HELIX 9 AA9 LYS A 1083 ALA A 1090 1 8 HELIX 10 AB1 ALA A 1090 TYR A 1101 1 12 HELIX 11 AB2 TYR A 1101 GLY A 302 1 40 HELIX 12 AB3 ALA A 308 ALA A 330 1 23 HELIX 13 AB4 ASN A 333 ASP A 345 1 13 SSBOND 1 CYS A 209 CYS A 216 1555 1555 2.05 LINK C ILE A 248 N YCM A 249 1555 1555 1.33 LINK C YCM A 249 N GLN A 250 1555 1555 1.33 CISPEP 1 ARG A 220 PRO A 221 0 -2.92 CISPEP 2 ARG A 220 PRO A 221 0 -2.48 CRYST1 57.033 96.867 97.563 90.00 90.00 90.00 P 21 21 2 4 ORIGX1 1.000000 0.000000 0.000000 0.00000 ORIGX2 0.000000 1.000000 0.000000 0.00000 ORIGX3 0.000000 0.000000 1.000000 0.00000 SCALE1 0.017534 0.000000 0.000000 0.00000 SCALE2 0.000000 0.010323 0.000000 0.00000 SCALE3 0.000000 0.000000 0.010250 0.00000 ATOM 1 N PRO A 70 22.822 -2.903 71.131 1.00 77.27 N ANISOU 1 N PRO A 70 9870 9671 9819 -483 555 2378 N ATOM 2 CA PRO A 70 22.492 -2.151 69.916 1.00 78.12 C ANISOU 2 CA PRO A 70 9971 9715 9997 -447 573 2156 C ATOM 3 C PRO A 70 22.752 -0.652 70.065 1.00 82.44 C ANISOU 3 C PRO A 70 10618 10376 10331 -434 554 2002 C ATOM 4 O PRO A 70 21.809 0.132 70.189 1.00 87.82 O ANISOU 4 O PRO A 70 11334 11122 10910 -431 643 1901 O ATOM 5 CB PRO A 70 21.001 -2.436 69.731 1.00 86.56 C ANISOU 5 CB PRO A 70 10990 10754 11147 -453 701 2141 C ATOM 6 CG PRO A 70 20.494 -2.602 71.121 1.00101.64 C ANISOU 6 CG PRO A 70 12935 12790 12893 -488 771 2293 C ATOM 7 CD PRO A 70 21.613 -3.264 71.895 1.00 94.46 C ANISOU 7 CD PRO A 70 12038 11908 11946 -510 676 2478 C ATOM 8 N ALA A 71 24.028 -0.265 70.061 1.00 70.83 N ANISOU 8 N ALA A 71 9185 8921 8808 -427 440 1986 N ATOM 9 CA ALA A 71 24.402 1.140 70.145 1.00 86.30 C ANISOU 9 CA ALA A 71 11231 10970 10590 -415 406 1838 C ATOM 10 C ALA A 71 24.575 1.785 68.779 1.00 71.26 C ANISOU 10 C ALA A 71 9303 8974 8799 -376 384 1654 C ATOM 11 O ALA A 71 24.559 3.019 68.685 1.00 66.55 O ANISOU 11 O ALA A 71 8765 8436 8086 -363 384 1511 O ATOM 12 CB ALA A 71 25.701 1.296 70.944 1.00 82.27 C ANISOU 12 CB ALA A 71 10774 10533 9952 -433 287 1922 C ATOM 13 N VAL A 72 24.740 0.991 67.725 1.00 49.76 N ANISOU 13 N VAL A 72 6496 6111 6298 -358 367 1655 N ATOM 14 CA VAL A 72 24.823 1.531 66.373 1.00 52.51 C ANISOU 14 CA VAL A 72 6822 6379 6750 -323 354 1487 C ATOM 15 C VAL A 72 23.417 1.851 65.886 1.00 34.81 C ANISOU 15 C VAL A 72 4564 4129 4534 -316 457 1384 C ATOM 16 O VAL A 72 22.512 1.012 65.951 1.00 37.85 O ANISOU 16 O VAL A 72 4898 4475 5010 -330 526 1452 O ATOM 17 CB VAL A 72 25.533 0.546 65.430 1.00 51.31 C ANISOU 17 CB VAL A 72 6591 6086 6816 -306 303 1518 C ATOM 18 CG1 VAL A 72 25.480 1.044 63.993 1.00 44.63 C ANISOU 18 CG1 VAL A 72 5724 5167 6067 -273 304 1346 C ATOM 19 CG2 VAL A 72 26.973 0.366 65.850 1.00 59.07 C ANISOU 19 CG2 VAL A 72 7584 7075 7787 -308 197 1610 C ATOM 20 N ASN A 73 23.234 3.063 65.407 1.00 40.01 N ANISOU 20 N ASN A 73 5259 4819 5125 -296 464 1228 N ATOM 21 CA ASN A 73 21.946 3.486 64.877 1.00 36.05 C ANISOU 21 CA ASN A 73 4736 4305 4655 -287 551 1125 C ATOM 22 C ASN A 73 21.755 2.934 63.467 1.00 36.70 C ANISOU 22 C ASN A 73 4744 4260 4941 -270 542 1065 C ATOM 23 O ASN A 73 22.619 3.137 62.608 1.00 35.55 O ANISOU 23 O ASN A 73 4594 4065 4847 -249 473 1000 O ATOM 24 CB ASN A 73 21.870 5.006 64.859 1.00 36.93 C ANISOU 24 CB ASN A 73 4908 4488 4634 -271 555 984 C ATOM 25 CG ASN A 73 20.497 5.516 64.484 1.00 40.41 C ANISOU 25 CG ASN A 73 5326 4928 5100 -263 648 891 C ATOM 26 OD1 ASN A 73 20.041 5.326 63.361 1.00 47.73 O ANISOU 26 OD1 ASN A 73 6195 5771 6171 -249 653 831 O ATOM 27 ND2 ASN A 73 19.834 6.175 65.424 1.00 51.69 N ANISOU 27 ND2 ASN A 73 6799 6451 6389 -271 721 877 N ATOM 28 N PRO A 74 20.645 2.239 63.190 1.00 36.13 N ANISOU 28 N PRO A 74 4611 4133 4983 -281 609 1084 N ATOM 29 CA PRO A 74 20.448 1.668 61.844 1.00 36.10 C ANISOU 29 CA PRO A 74 4539 4009 5167 -270 593 1019 C ATOM 30 C PRO A 74 20.588 2.676 60.720 1.00 37.88 C ANISOU 30 C PRO A 74 4780 4227 5388 -242 560 859 C ATOM 31 O PRO A 74 21.099 2.346 59.642 1.00 34.28 O ANISOU 31 O PRO A 74 4295 3692 5039 -228 512 806 O ATOM 32 CB PRO A 74 19.015 1.121 61.903 1.00 43.01 C ANISOU 32 CB PRO A 74 5357 4856 6128 -290 677 1047 C ATOM 33 CG PRO A 74 18.718 0.934 63.337 1.00 46.24 C ANISOU 33 CG PRO A 74 5790 5348 6431 -313 735 1178 C ATOM 34 CD PRO A 74 19.515 1.951 64.089 1.00 34.56 C ANISOU 34 CD PRO A 74 4401 3981 4749 -305 704 1163 C ATOM 35 N TRP A 75 20.111 3.900 60.941 1.00 33.04 N ANISOU 35 N TRP A 75 4208 3692 4654 -234 590 782 N ATOM 36 CA TRP A 75 20.183 4.919 59.905 1.00 31.87 C ANISOU 36 CA TRP A 75 4069 3538 4503 -209 560 644 C ATOM 37 C TRP A 75 21.620 5.253 59.545 1.00 33.73 C ANISOU 37 C TRP A 75 4337 3769 4710 -190 476 619 C ATOM 38 O TRP A 75 21.915 5.546 58.382 1.00 35.96 O ANISOU 38 O TRP A 75 4605 4009 5051 -171 440 533 O ATOM 39 CB TRP A 75 19.446 6.172 60.366 1.00 37.44 C ANISOU 39 CB TRP A 75 4808 4324 5093 -203 611 579 C ATOM 40 CG TRP A 75 17.987 5.944 60.571 1.00 34.82 C ANISOU 40 CG TRP A 75 4432 3989 4807 -217 700 591 C ATOM 41 CD1 TRP A 75 17.355 5.693 61.750 1.00 38.37 C ANISOU 41 CD1 TRP A 75 4890 4493 5196 -236 778 673 C ATOM 42 CD2 TRP A 75 16.973 5.942 59.562 1.00 35.99 C ANISOU 42 CD2 TRP A 75 4518 4079 5077 -214 719 524 C ATOM 43 NE1 TRP A 75 16.009 5.537 61.540 1.00 40.52 N ANISOU 43 NE1 TRP A 75 5102 4739 5556 -244 851 662 N ATOM 44 CE2 TRP A 75 15.748 5.686 60.204 1.00 37.61 C ANISOU 44 CE2 TRP A 75 4689 4299 5303 -231 810 571 C ATOM 45 CE3 TRP A 75 16.983 6.138 58.177 1.00 39.70 C ANISOU 45 CE3 TRP A 75 4958 4491 5634 -201 666 432 C ATOM 46 CZ2 TRP A 75 14.541 5.618 59.510 1.00 44.08 C ANISOU 46 CZ2 TRP A 75 5437 5069 6242 -236 844 530 C ATOM 47 CZ3 TRP A 75 15.786 6.070 57.490 1.00 51.39 C ANISOU 47 CZ3 TRP A 75 6377 5931 7219 -208 693 391 C ATOM 48 CH2 TRP A 75 14.581 5.812 58.157 1.00 45.02 C ANISOU 48 CH2 TRP A 75 5530 5132 6445 -225 778 440 C ATOM 49 N ASP A 76 22.529 5.230 60.526 1.00 33.51 N ANISOU 49 N ASP A 76 4352 3790 4592 -197 443 698 N ATOM 50 CA ASP A 76 23.931 5.491 60.218 1.00 35.59 C ANISOU 50 CA ASP A 76 4635 4042 4845 -181 361 687 C ATOM 51 C ASP A 76 24.489 4.416 59.296 1.00 31.78 C ANISOU 51 C ASP A 76 4097 3456 4523 -172 330 707 C ATOM 52 O ASP A 76 25.277 4.712 58.391 1.00 29.60 O ANISOU 52 O ASP A 76 3815 3145 4286 -150 286 643 O ATOM 53 CB ASP A 76 24.748 5.579 61.505 1.00 33.85 C ANISOU 53 CB ASP A 76 4465 3893 4505 -196 323 779 C ATOM 54 CG ASP A 76 24.443 6.831 62.302 1.00 39.10 C ANISOU 54 CG ASP A 76 5195 4661 5000 -201 341 725 C ATOM 55 OD1 ASP A 76 24.244 7.892 61.677 1.00 44.89 O ANISOU 55 OD1 ASP A 76 5938 5399 5718 -182 344 606 O ATOM 56 OD2 ASP A 76 24.400 6.757 63.549 1.00 47.05 O ANISOU 56 OD2 ASP A 76 6244 5744 5890 -224 354 802 O ATOM 57 N VAL A 77 24.077 3.164 59.497 1.00 31.53 N ANISOU 57 N VAL A 77 4021 3369 4591 -189 358 792 N ATOM 58 CA VAL A 77 24.500 2.104 58.591 1.00 32.28 C ANISOU 58 CA VAL A 77 4058 3353 4853 -181 338 795 C ATOM 59 C VAL A 77 23.916 2.330 57.202 1.00 32.43 C ANISOU 59 C VAL A 77 4053 3326 4943 -168 353 661 C ATOM 60 O VAL A 77 24.593 2.119 56.190 1.00 33.70 O ANISOU 60 O VAL A 77 4196 3428 5182 -149 323 603 O ATOM 61 CB VAL A 77 24.106 0.729 59.154 1.00 35.05 C ANISOU 61 CB VAL A 77 4360 3648 5308 -205 367 919 C ATOM 62 CG1 VAL A 77 24.495 -0.367 58.175 1.00 34.96 C ANISOU 62 CG1 VAL A 77 4287 3509 5487 -196 351 903 C ATOM 63 CG2 VAL A 77 24.770 0.502 60.506 1.00 43.32 C ANISOU 63 CG2 VAL A 77 5434 4749 6278 -220 342 1066 C ATOM 64 N LEU A 78 22.656 2.767 57.126 1.00 40.43 N ANISOU 64 N LEU A 78 5064 4369 5928 -178 400 610 N ATOM 65 CA ALEU A 78 22.046 3.022 55.825 0.50 38.69 C ANISOU 65 CA ALEU A 78 4821 4114 5767 -169 403 490 C ATOM 66 CA BLEU A 78 22.042 3.024 55.828 0.50 38.69 C ANISOU 66 CA BLEU A 78 4821 4114 5766 -169 403 490 C ATOM 67 C LEU A 78 22.780 4.129 55.080 1.00 40.81 C ANISOU 67 C LEU A 78 5125 4416 5967 -142 362 399 C ATOM 68 O LEU A 78 22.985 4.036 53.864 1.00 34.23 O ANISOU 68 O LEU A 78 4274 3538 5195 -130 341 320 O ATOM 69 CB ALEU A 78 20.571 3.382 55.990 0.50 46.20 C ANISOU 69 CB ALEU A 78 5757 5094 6702 -185 457 467 C ATOM 70 CB BLEU A 78 20.573 3.393 56.017 0.50 46.19 C ANISOU 70 CB BLEU A 78 5757 5095 6699 -185 457 468 C ATOM 71 CG ALEU A 78 19.599 2.215 56.172 0.50 41.65 C ANISOU 71 CG ALEU A 78 5122 4458 6247 -212 499 525 C ATOM 72 CG BLEU A 78 19.578 2.933 54.953 0.50 50.56 C ANISOU 72 CG BLEU A 78 6256 5584 7372 -195 467 400 C ATOM 73 CD1ALEU A 78 18.197 2.743 56.409 0.50 45.54 C ANISOU 73 CD1ALEU A 78 5598 4989 6717 -225 556 505 C ATOM 74 CD1BLEU A 78 19.619 1.427 54.772 0.50 51.43 C ANISOU 74 CD1BLEU A 78 6315 5595 7632 -212 466 448 C ATOM 75 CD2ALEU A 78 19.622 1.285 54.965 0.50 51.51 C ANISOU 75 CD2ALEU A 78 6322 5602 7647 -215 471 469 C ATOM 76 CD2BLEU A 78 18.194 3.372 55.370 0.50 61.14 C ANISOU 76 CD2BLEU A 78 7576 6960 8692 -210 522 400 C ATOM 77 N LEU A 79 23.179 5.188 55.789 1.00 34.70 N ANISOU 77 N LEU A 79 4399 3720 5065 -135 350 406 N ATOM 78 CA LEU A 79 23.940 6.255 55.146 1.00 35.07 C ANISOU 78 CA LEU A 79 4474 3794 5059 -110 309 333 C ATOM 79 C LEU A 79 25.300 5.759 54.680 1.00 39.77 C ANISOU 79 C LEU A 79 5060 4340 5709 -95 264 350 C ATOM 80 O LEU A 79 25.789 6.176 53.626 1.00 34.06 O ANISOU 80 O LEU A 79 4334 3604 5003 -75 243 279 O ATOM 81 CB LEU A 79 24.122 7.430 56.101 1.00 31.80 C ANISOU 81 CB LEU A 79 4110 3463 4510 -109 303 338 C ATOM 82 CG LEU A 79 22.877 8.241 56.447 1.00 37.61 C ANISOU 82 CG LEU A 79 4856 4248 5186 -115 353 296 C ATOM 83 CD1 LEU A 79 23.181 9.194 57.590 1.00 32.89 C ANISOU 83 CD1 LEU A 79 4313 3728 4455 -117 350 305 C ATOM 84 CD2 LEU A 79 22.397 9.000 55.225 1.00 38.09 C ANISOU 84 CD2 LEU A 79 4897 4297 5280 -100 348 196 C ATOM 85 N CYS A 80 25.929 4.876 55.457 1.00 30.30 N ANISOU 85 N CYS A 80 3853 3117 4543 -103 252 450 N ATOM 86 CA CYS A 80 27.218 4.335 55.049 1.00 34.63 C ANISOU 86 CA CYS A 80 4382 3610 5167 -86 215 473 C ATOM 87 C CYS A 80 27.070 3.488 53.794 1.00 32.42 C ANISOU 87 C CYS A 80 4058 3244 5018 -77 234 411 C ATOM 88 O CYS A 80 27.879 3.589 52.866 1.00 32.08 O ANISOU 88 O CYS A 80 4007 3173 5011 -54 219 356 O ATOM 89 CB CYS A 80 27.820 3.519 56.191 1.00 40.56 C ANISOU 89 CB CYS A 80 5125 4349 5938 -99 195 607 C ATOM 90 SG CYS A 80 29.490 2.924 55.868 1.00 42.49 S ANISOU 90 SG CYS A 80 5335 4523 6286 -76 145 653 S ATOM 91 N VAL A 81 26.032 2.652 53.753 1.00 34.96 N ANISOU 91 N VAL A 81 4350 3524 5410 -97 270 415 N ATOM 92 CA VAL A 81 25.724 1.880 52.554 1.00 37.69 C ANISOU 92 CA VAL A 81 4658 3791 5873 -95 285 337 C ATOM 93 C VAL A 81 25.456 2.813 51.381 1.00 30.44 C ANISOU 93 C VAL A 81 3759 2908 4900 -82 280 214 C ATOM 94 O VAL A 81 25.977 2.623 50.275 1.00 32.41 O ANISOU 94 O VAL A 81 3999 3121 5193 -66 274 141 O ATOM 95 CB VAL A 81 24.523 0.955 52.823 1.00 30.91 C ANISOU 95 CB VAL A 81 3762 2887 5097 -124 318 365 C ATOM 96 CG1 VAL A 81 24.018 0.335 51.535 1.00 38.93 C ANISOU 96 CG1 VAL A 81 4744 3830 6216 -128 325 261 C ATOM 97 CG2 VAL A 81 24.898 -0.121 53.827 1.00 36.37 C ANISOU 97 CG2 VAL A 81 4424 3528 5867 -136 322 497 C ATOM 98 N SER A 82 24.616 3.825 51.601 1.00 36.38 N ANISOU 98 N SER A 82 4535 3733 5555 -90 285 191 N ATOM 99 CA SER A 82 24.322 4.787 50.546 1.00 30.87 C ANISOU 99 CA SER A 82 3851 3072 4805 -80 274 92 C ATOM 100 C SER A 82 25.596 5.457 50.051 1.00 34.30 C ANISOU 100 C SER A 82 4308 3528 5197 -52 247 69 C ATOM 101 O SER A 82 25.822 5.576 48.840 1.00 32.82 O ANISOU 101 O SER A 82 4118 3332 5022 -39 241 -6 O ATOM 102 CB SER A 82 23.324 5.826 51.058 1.00 37.24 C ANISOU 102 CB SER A 82 4674 3948 5528 -89 286 89 C ATOM 103 OG SER A 82 23.025 6.787 50.062 1.00 46.60 O ANISOU 103 OG SER A 82 5866 5166 6674 -80 270 7 O ATOM 104 N GLY A 83 26.450 5.893 50.978 1.00 29.75 N ANISOU 104 N GLY A 83 3753 2981 4571 -43 230 136 N ATOM 105 CA GLY A 83 27.692 6.533 50.579 1.00 28.32 C ANISOU 105 CA GLY A 83 3583 2813 4363 -18 203 125 C ATOM 106 C GLY A 83 28.590 5.620 49.768 1.00 27.63 C ANISOU 106 C GLY A 83 3468 2657 4372 -1 208 110 C ATOM 107 O GLY A 83 29.266 6.064 48.838 1.00 30.27 O ANISOU 107 O GLY A 83 3804 2998 4700 20 205 60 O ATOM 108 N THR A 84 28.619 4.332 50.115 1.00 30.67 N ANISOU 108 N THR A 84 3825 2975 4855 -10 222 154 N ATOM 109 CA THR A 84 29.433 3.381 49.365 1.00 32.90 C ANISOU 109 CA THR A 84 4074 3179 5249 8 236 132 C ATOM 110 C THR A 84 28.973 3.296 47.915 1.00 29.70 C ANISOU 110 C THR A 84 3668 2762 4856 12 260 11 C ATOM 111 O THR A 84 29.785 3.376 46.986 1.00 29.52 O ANISOU 111 O THR A 84 3641 2728 4845 36 271 -42 O ATOM 112 CB THR A 84 29.370 2.006 50.032 1.00 35.95 C ANISOU 112 CB THR A 84 4423 3484 5753 -5 247 204 C ATOM 113 OG1 THR A 84 29.917 2.094 51.352 1.00 35.38 O ANISOU 113 OG1 THR A 84 4354 3432 5656 -10 217 326 O ATOM 114 CG2 THR A 84 30.156 0.976 49.229 1.00 30.25 C ANISOU 114 CG2 THR A 84 3660 2667 5167 15 269 169 C ATOM 115 N VAL A 85 27.668 3.117 47.704 1.00 32.61 N ANISOU 115 N VAL A 85 4037 3134 5220 -13 267 -33 N ATOM 116 CA VAL A 85 27.132 3.065 46.346 1.00 30.91 C ANISOU 116 CA VAL A 85 3824 2917 5003 -16 276 -148 C ATOM 117 C VAL A 85 27.435 4.365 45.611 1.00 30.43 C ANISOU 117 C VAL A 85 3795 2937 4832 0 263 -191 C ATOM 118 O VAL A 85 27.884 4.356 44.460 1.00 30.59 O ANISOU 118 O VAL A 85 3819 2958 4844 14 275 -264 O ATOM 119 CB VAL A 85 25.622 2.770 46.381 1.00 29.57 C ANISOU 119 CB VAL A 85 3643 2742 4849 -50 273 -172 C ATOM 120 CG1 VAL A 85 25.024 2.811 44.980 1.00 37.70 C ANISOU 120 CG1 VAL A 85 4679 3783 5863 -59 266 -290 C ATOM 121 CG2 VAL A 85 25.371 1.418 47.019 1.00 37.93 C ANISOU 121 CG2 VAL A 85 4663 3712 6036 -67 290 -124 C ATOM 122 N ILE A 86 27.204 5.502 46.272 1.00 34.74 N ANISOU 122 N ILE A 86 4360 3550 5291 -1 242 -146 N ATOM 123 CA ILE A 86 27.479 6.795 45.649 1.00 26.88 C ANISOU 123 CA ILE A 86 3387 2623 4204 13 227 -174 C ATOM 124 C ILE A 86 28.947 6.897 45.262 1.00 28.36 C ANISOU 124 C ILE A 86 3572 2801 4401 43 235 -166 C ATOM 125 O ILE A 86 29.285 7.293 44.140 1.00 26.97 O ANISOU 125 O ILE A 86 3404 2652 4193 56 244 -220 O ATOM 126 CB ILE A 86 27.079 7.945 46.588 1.00 24.70 C ANISOU 126 CB ILE A 86 3126 2403 3855 8 206 -126 C ATOM 127 CG1 ILE A 86 25.564 7.992 46.768 1.00 30.06 C ANISOU 127 CG1 ILE A 86 3800 3096 4526 -17 208 -143 C ATOM 128 CG2 ILE A 86 27.598 9.274 46.045 1.00 33.80 C ANISOU 128 CG2 ILE A 86 4293 3611 4938 26 189 -140 C ATOM 129 CD1 ILE A 86 25.141 8.804 47.968 1.00 36.08 C ANISOU 129 CD1 ILE A 86 4574 3897 5237 -23 206 -93 C ATOM 130 N ALA A 87 29.843 6.561 46.192 1.00 27.56 N ANISOU 130 N ALA A 87 3460 2667 4346 52 232 -92 N ATOM 131 CA ALA A 87 31.268 6.680 45.908 1.00 26.16 C ANISOU 131 CA ALA A 87 3270 2475 4195 81 238 -73 C ATOM 132 C ALA A 87 31.673 5.778 44.750 1.00 31.39 C ANISOU 132 C ALA A 87 3914 3088 4924 96 282 -143 C ATOM 133 O ALA A 87 32.429 6.195 43.864 1.00 31.89 O ANISOU 133 O ALA A 87 3977 3171 4969 118 302 -175 O ATOM 134 CB ALA A 87 32.084 6.350 47.158 1.00 32.61 C ANISOU 134 CB ALA A 87 4070 3258 5061 83 216 26 C ATOM 135 N GLY A 88 31.178 4.540 44.734 1.00 31.07 N ANISOU 135 N GLY A 88 3858 2983 4965 84 301 -169 N ATOM 136 CA GLY A 88 31.562 3.621 43.675 1.00 31.16 C ANISOU 136 CA GLY A 88 3853 2939 5048 98 346 -250 C ATOM 137 C GLY A 88 31.085 4.077 42.310 1.00 37.35 C ANISOU 137 C GLY A 88 4666 3779 5745 95 359 -356 C ATOM 138 O GLY A 88 31.842 4.065 41.336 1.00 34.35 O ANISOU 138 O GLY A 88 4288 3404 5360 117 398 -410 O ATOM 139 N GLU A 89 29.816 4.481 42.220 1.00 34.48 N ANISOU 139 N GLU A 89 4324 3462 5313 66 328 -382 N ATOM 140 CA GLU A 89 29.277 4.972 40.956 1.00 29.77 C ANISOU 140 CA GLU A 89 3755 2930 4627 58 325 -469 C ATOM 141 C GLU A 89 30.074 6.159 40.446 1.00 34.36 C ANISOU 141 C GLU A 89 4351 3583 5121 81 330 -450 C ATOM 142 O GLU A 89 30.497 6.193 39.286 1.00 33.54 O ANISOU 142 O GLU A 89 4260 3507 4977 93 361 -513 O ATOM 143 CB GLU A 89 27.825 5.395 41.133 1.00 37.41 C ANISOU 143 CB GLU A 89 4731 3936 5546 25 281 -472 C ATOM 144 CG GLU A 89 26.791 4.342 40.911 1.00 38.89 C ANISOU 144 CG GLU A 89 4908 4074 5794 -5 275 -535 C ATOM 145 CD GLU A 89 25.405 4.921 41.084 1.00 43.53 C ANISOU 145 CD GLU A 89 5495 4705 6338 -35 231 -526 C ATOM 146 OE1 GLU A 89 25.027 5.218 42.233 1.00 43.76 O ANISOU 146 OE1 GLU A 89 5513 4732 6382 -41 223 -448 O ATOM 147 OE2 GLU A 89 24.716 5.125 40.067 1.00 47.00 O ANISOU 147 OE2 GLU A 89 5947 5186 6726 -53 206 -596 O ATOM 148 N ASN A 90 30.263 7.160 41.302 1.00 27.25 N ANISOU 148 N ASN A 90 3449 2714 4189 86 301 -364 N ATOM 149 CA ASN A 90 30.842 8.414 40.851 1.00 34.49 C ANISOU 149 CA ASN A 90 4374 3698 5031 103 297 -340 C ATOM 150 C ASN A 90 32.355 8.338 40.721 1.00 31.12 C ANISOU 150 C ASN A 90 3929 3248 4649 135 335 -313 C ATOM 151 O ASN A 90 32.932 9.081 39.919 1.00 33.35 O ANISOU 151 O ASN A 90 4214 3578 4879 151 352 -315 O ATOM 152 CB ASN A 90 30.421 9.530 41.797 1.00 29.09 C ANISOU 152 CB ASN A 90 3694 3050 4309 94 250 -273 C ATOM 153 CG ASN A 90 28.971 9.909 41.614 1.00 29.61 C ANISOU 153 CG ASN A 90 3771 3154 4324 67 221 -302 C ATOM 154 OD1 ASN A 90 28.623 10.600 40.657 1.00 32.33 O ANISOU 154 OD1 ASN A 90 4126 3555 4605 64 210 -330 O ATOM 155 ND2 ASN A 90 28.111 9.439 42.514 1.00 28.09 N ANISOU 155 ND2 ASN A 90 3575 2932 4166 47 208 -290 N ATOM 156 N ALA A 91 33.012 7.450 41.472 1.00 34.58 N ANISOU 156 N ALA A 91 4341 3610 5187 146 349 -279 N ATOM 157 CA ALA A 91 34.435 7.222 41.240 1.00 36.76 C ANISOU 157 CA ALA A 91 4588 3852 5528 178 390 -258 C ATOM 158 C ALA A 91 34.669 6.691 39.835 1.00 38.27 C ANISOU 158 C ALA A 91 4785 4045 5712 192 456 -354 C ATOM 159 O ALA A 91 35.657 7.046 39.182 1.00 35.70 O ANISOU 159 O ALA A 91 4446 3737 5381 218 500 -352 O ATOM 160 CB ALA A 91 34.999 6.250 42.274 1.00 33.74 C ANISOU 160 CB ALA A 91 4170 3381 5268 184 388 -202 C ATOM 161 N LEU A 92 33.768 5.833 39.353 1.00 35.92 N ANISOU 161 N LEU A 92 4506 3729 5415 173 466 -442 N ATOM 162 CA LEU A 92 33.904 5.301 38.004 1.00 33.18 C ANISOU 162 CA LEU A 92 4173 3390 5046 182 526 -551 C ATOM 163 C LEU A 92 33.765 6.409 36.968 1.00 36.79 C ANISOU 163 C LEU A 92 4663 3956 5360 180 526 -572 C ATOM 164 O LEU A 92 34.553 6.489 36.020 1.00 32.87 O ANISOU 164 O LEU A 92 4169 3488 4833 203 588 -607 O ATOM 165 CB LEU A 92 32.865 4.202 37.775 1.00 35.12 C ANISOU 165 CB LEU A 92 4431 3591 5323 155 520 -644 C ATOM 166 CG LEU A 92 32.806 3.590 36.374 1.00 35.97 C ANISOU 166 CG LEU A 92 4564 3709 5394 155 571 -781 C ATOM 167 CD1 LEU A 92 34.149 3.001 35.993 1.00 39.78 C ANISOU 167 CD1 LEU A 92 5020 4138 5957 196 659 -808 C ATOM 168 CD2 LEU A 92 31.714 2.531 36.299 1.00 37.33 C ANISOU 168 CD2 LEU A 92 4743 3828 5614 122 548 -868 C ATOM 169 N VAL A 93 32.764 7.277 37.138 1.00 30.02 N ANISOU 169 N VAL A 93 3826 3160 4418 154 462 -545 N ATOM 170 CA VAL A 93 32.597 8.408 36.231 1.00 30.64 C ANISOU 170 CA VAL A 93 3929 3341 4372 150 452 -542 C ATOM 171 C VAL A 93 33.847 9.278 36.238 1.00 38.43 C ANISOU 171 C VAL A 93 4893 4349 5360 181 481 -464 C ATOM 172 O VAL A 93 34.367 9.660 35.183 1.00 32.57 O ANISOU 172 O VAL A 93 4159 3663 4551 194 525 -480 O ATOM 173 CB VAL A 93 31.346 9.221 36.613 1.00 33.48 C ANISOU 173 CB VAL A 93 4300 3744 4675 120 374 -509 C ATOM 174 CG1 VAL A 93 31.224 10.448 35.725 1.00 37.95 C ANISOU 174 CG1 VAL A 93 4881 4409 5129 117 358 -487 C ATOM 175 CG2 VAL A 93 30.098 8.356 36.517 1.00 30.37 C ANISOU 175 CG2 VAL A 93 3920 3329 4289 87 346 -584 C ATOM 176 N VAL A 94 34.347 9.606 37.432 1.00 30.30 N ANISOU 176 N VAL A 94 3833 3275 4404 190 454 -376 N ATOM 177 CA VAL A 94 35.538 10.446 37.522 1.00 38.83 C ANISOU 177 CA VAL A 94 4884 4367 5504 216 471 -299 C ATOM 178 C VAL A 94 36.703 9.788 36.794 1.00 38.23 C ANISOU 178 C VAL A 94 4786 4264 5475 247 558 -328 C ATOM 179 O VAL A 94 37.436 10.443 36.042 1.00 31.20 O ANISOU 179 O VAL A 94 3885 3420 4549 265 600 -306 O ATOM 180 CB VAL A 94 35.881 10.740 38.996 1.00 39.40 C ANISOU 180 CB VAL A 94 4929 4390 5651 216 419 -212 C ATOM 181 CG1 VAL A 94 37.261 11.360 39.102 1.00 43.75 C ANISOU 181 CG1 VAL A 94 5439 4931 6251 241 436 -138 C ATOM 182 CG2 VAL A 94 34.842 11.668 39.618 1.00 37.76 C ANISOU 182 CG2 VAL A 94 4742 4221 5385 189 347 -183 C ATOM 183 N ALA A 95 36.883 8.480 36.988 1.00 32.30 N ANISOU 183 N ALA A 95 4024 3436 4814 255 592 -378 N ATOM 184 CA ALA A 95 37.983 7.779 36.333 1.00 31.29 C ANISOU 184 CA ALA A 95 3870 3270 4751 289 685 -415 C ATOM 185 C ALA A 95 37.822 7.779 34.817 1.00 36.37 C ANISOU 185 C ALA A 95 4550 3986 5282 291 749 -509 C ATOM 186 O ALA A 95 38.809 7.907 34.083 1.00 44.94 O ANISOU 186 O ALA A 95 5618 5091 6368 319 829 -511 O ATOM 187 CB ALA A 95 38.074 6.346 36.856 1.00 37.50 C ANISOU 187 CB ALA A 95 4632 3947 5668 295 704 -453 C ATOM 188 N LEU A 96 36.591 7.621 34.328 1.00 40.06 N ANISOU 188 N LEU A 96 5069 4499 5654 259 716 -586 N ATOM 189 CA LEU A 96 36.370 7.570 32.886 1.00 37.89 C ANISOU 189 CA LEU A 96 4837 4303 5256 254 766 -681 C ATOM 190 C LEU A 96 36.704 8.906 32.236 1.00 35.64 C ANISOU 190 C LEU A 96 4557 4123 4860 259 773 -611 C ATOM 191 O LEU A 96 37.409 8.959 31.221 1.00 37.77 O ANISOU 191 O LEU A 96 4834 4442 5076 279 856 -640 O ATOM 192 CB LEU A 96 34.919 7.178 32.593 1.00 31.95 C ANISOU 192 CB LEU A 96 4131 3576 4431 212 707 -766 C ATOM 193 CG LEU A 96 34.517 5.746 32.961 1.00 38.36 C ANISOU 193 CG LEU A 96 4940 4287 5349 203 710 -854 C ATOM 194 CD1 LEU A 96 33.031 5.506 32.726 1.00 37.45 C ANISOU 194 CD1 LEU A 96 4863 4198 5170 158 639 -922 C ATOM 195 CD2 LEU A 96 35.334 4.743 32.180 1.00 34.71 C ANISOU 195 CD2 LEU A 96 4475 3782 4930 230 814 -958 C ATOM 196 N ILE A 97 36.204 10.000 32.810 1.00 35.61 N ANISOU 196 N ILE A 97 4549 4153 4826 242 690 -519 N ATOM 197 CA ILE A 97 36.445 11.317 32.232 1.00 45.09 C ANISOU 197 CA ILE A 97 5749 5445 5938 244 687 -443 C ATOM 198 C ILE A 97 37.922 11.675 32.319 1.00 48.86 C ANISOU 198 C ILE A 97 6176 5899 6491 281 753 -369 C ATOM 199 O ILE A 97 38.496 12.236 31.378 1.00 61.03 O ANISOU 199 O ILE A 97 7715 7509 7965 294 811 -344 O ATOM 200 CB ILE A 97 35.557 12.365 32.928 1.00 44.91 C ANISOU 200 CB ILE A 97 5724 5443 5896 219 584 -367 C ATOM 201 CG1 ILE A 97 34.083 12.092 32.599 1.00 40.21 C ANISOU 201 CG1 ILE A 97 5173 4885 5220 182 526 -437 C ATOM 202 CG2 ILE A 97 35.978 13.772 32.519 1.00 59.67 C ANISOU 202 CG2 ILE A 97 7576 7381 7717 225 580 -269 C ATOM 203 CD1 ILE A 97 33.089 12.998 33.302 1.00 43.93 C ANISOU 203 CD1 ILE A 97 5638 5366 5687 158 432 -375 C ATOM 204 N ALA A 98 38.569 11.327 33.433 1.00 52.08 N ANISOU 204 N ALA A 98 6539 6210 7040 297 745 -327 N ATOM 205 CA ALA A 98 39.962 11.709 33.638 1.00 44.37 C ANISOU 205 CA ALA A 98 5503 5202 6154 329 791 -245 C ATOM 206 C ALA A 98 40.890 11.015 32.648 1.00 51.43 C ANISOU 206 C ALA A 98 6384 6095 7061 362 916 -300 C ATOM 207 O ALA A 98 41.843 11.626 32.150 1.00 50.41 O ANISOU 207 O ALA A 98 6220 5996 6937 384 977 -241 O ATOM 208 CB ALA A 98 40.382 11.390 35.072 1.00 39.53 C ANISOU 208 CB ALA A 98 4846 4487 5686 335 742 -191 C ATOM 209 N SER A 99 40.643 9.741 32.361 1.00 59.93 N ANISOU 209 N SER A 99 7484 7133 8153 365 962 -415 N ATOM 210 CA SER A 99 41.522 8.957 31.506 1.00 48.51 C ANISOU 210 CA SER A 99 6024 5671 6737 399 1089 -485 C ATOM 211 C SER A 99 41.108 8.987 30.040 1.00 48.24 C ANISOU 211 C SER A 99 6052 5747 6529 390 1151 -578 C ATOM 212 O SER A 99 41.623 8.190 29.251 1.00 50.56 O ANISOU 212 O SER A 99 6352 6035 6825 413 1262 -672 O ATOM 213 CB SER A 99 41.573 7.508 31.997 1.00 43.00 C ANISOU 213 CB SER A 99 5311 4857 6171 409 1111 -565 C ATOM 214 OG SER A 99 40.283 6.923 31.981 1.00 58.08 O ANISOU 214 OG SER A 99 7278 6771 8020 375 1055 -657 O ATOM 215 N THR A 100 40.203 9.884 29.657 1.00 50.80 N ANISOU 215 N THR A 100 6422 6173 6705 357 1083 -553 N ATOM 216 CA THR A 100 39.692 9.953 28.288 1.00 59.53 C ANISOU 216 CA THR A 100 7594 7398 7628 340 1120 -631 C ATOM 217 C THR A 100 39.884 11.371 27.764 1.00 59.28 C ANISOU 217 C THR A 100 7556 7472 7495 336 1113 -514 C ATOM 218 O THR A 100 39.078 12.265 28.075 1.00 58.30 O ANISOU 218 O THR A 100 7441 7386 7324 308 1009 -444 O ATOM 219 CB THR A 100 38.222 9.549 28.227 1.00 60.20 C ANISOU 219 CB THR A 100 7739 7504 7631 297 1030 -718 C ATOM 220 OG1 THR A 100 38.044 8.286 28.881 1.00 49.64 O ANISOU 220 OG1 THR A 100 6394 6051 6416 299 1027 -804 O ATOM 221 CG2 THR A 100 37.757 9.436 26.781 1.00 51.79 C ANISOU 221 CG2 THR A 100 6743 6557 6376 277 1066 -815 C ATOM 222 N PRO A 101 40.930 11.619 26.969 1.00 62.68 N ANISOU 222 N PRO A 101 7968 7950 7899 365 1227 -488 N ATOM 223 CA PRO A 101 41.164 12.989 26.482 1.00 70.45 C ANISOU 223 CA PRO A 101 8937 9030 8802 361 1223 -359 C ATOM 224 C PRO A 101 39.992 13.580 25.711 1.00 63.63 C ANISOU 224 C PRO A 101 8138 8289 7749 320 1153 -362 C ATOM 225 O PRO A 101 39.830 14.807 25.689 1.00 67.31 O ANISOU 225 O PRO A 101 8586 8809 8182 307 1098 -238 O ATOM 226 CB PRO A 101 42.404 12.833 25.590 1.00 85.13 C ANISOU 226 CB PRO A 101 10773 10922 10649 399 1381 -363 C ATOM 227 CG PRO A 101 43.093 11.609 26.101 1.00 60.70 C ANISOU 227 CG PRO A 101 7646 7706 7712 432 1449 -446 C ATOM 228 CD PRO A 101 42.001 10.692 26.560 1.00 66.83 C ANISOU 228 CD PRO A 101 8470 8431 8490 406 1368 -561 C ATOM 229 N ALA A 102 39.166 12.748 25.074 1.00 53.59 N ANISOU 229 N ALA A 102 6938 7062 6363 297 1149 -498 N ATOM 230 CA ALA A 102 38.039 13.263 24.305 1.00 60.36 C ANISOU 230 CA ALA A 102 7854 8039 7041 254 1073 -499 C ATOM 231 C ALA A 102 36.993 13.950 25.177 1.00 80.98 C ANISOU 231 C ALA A 102 10451 10621 9696 224 925 -427 C ATOM 232 O ALA A 102 36.208 14.752 24.660 1.00 72.28 O ANISOU 232 O ALA A 102 9371 9612 8478 194 853 -372 O ATOM 233 CB ALA A 102 37.378 12.130 23.518 1.00 58.99 C ANISOU 233 CB ALA A 102 7758 7906 6752 232 1089 -674 C ATOM 234 N LEU A 103 36.961 13.659 26.474 1.00 59.99 N ANISOU 234 N LEU A 103 7754 7839 7200 233 879 -422 N ATOM 235 CA LEU A 103 35.923 14.186 27.361 1.00 51.68 C ANISOU 235 CA LEU A 103 6691 6753 6191 206 751 -373 C ATOM 236 C LEU A 103 36.429 15.428 28.094 1.00 47.17 C ANISOU 236 C LEU A 103 6058 6154 5710 219 720 -224 C ATOM 237 O LEU A 103 36.557 15.461 29.319 1.00 54.62 O ANISOU 237 O LEU A 103 6965 7001 6786 227 681 -194 O ATOM 238 CB LEU A 103 35.470 13.102 28.337 1.00 47.00 C ANISOU 238 CB LEU A 103 6100 6051 5705 201 718 -460 C ATOM 239 CG LEU A 103 35.079 11.769 27.687 1.00 54.64 C ANISOU 239 CG LEU A 103 7120 7021 6619 190 753 -617 C ATOM 240 CD1 LEU A 103 34.669 10.730 28.719 1.00 51.88 C ANISOU 240 CD1 LEU A 103 6760 6552 6400 185 721 -683 C ATOM 241 CD2 LEU A 103 33.961 11.968 26.687 1.00 70.20 C ANISOU 241 CD2 LEU A 103 9146 9102 8423 148 695 -660 C ATOM 242 N ARG A 104 36.709 16.470 27.305 1.00 40.37 N ANISOU 242 N ARG A 104 5187 5381 4770 219 736 -130 N ATOM 243 CA ARG A 104 37.258 17.719 27.820 1.00 53.99 C ANISOU 243 CA ARG A 104 6849 7083 6580 231 713 12 C ATOM 244 C ARG A 104 36.458 18.937 27.365 1.00 51.11 C ANISOU 244 C ARG A 104 6484 6797 6139 204 636 104 C ATOM 245 O ARG A 104 36.920 20.070 27.545 1.00 48.27 O ANISOU 245 O ARG A 104 6071 6430 5839 212 624 227 O ATOM 246 CB ARG A 104 38.726 17.873 27.398 1.00 56.69 C ANISOU 246 CB ARG A 104 7152 7432 6957 265 825 67 C ATOM 247 CG ARG A 104 39.653 16.787 27.942 1.00 55.91 C ANISOU 247 CG ARG A 104 7033 7238 6971 296 900 -2 C ATOM 248 CD ARG A 104 39.849 16.900 29.445 1.00 64.18 C ANISOU 248 CD ARG A 104 8033 8167 8187 302 832 36 C ATOM 249 NE ARG A 104 39.778 15.596 30.094 1.00 76.68 N ANISOU 249 NE ARG A 104 9631 9667 9837 308 839 -66 N ATOM 250 CZ ARG A 104 40.781 14.731 30.155 1.00 72.28 C ANISOU 250 CZ ARG A 104 9047 9051 9364 339 926 -102 C ATOM 251 NH1 ARG A 104 41.965 15.002 29.628 1.00 83.61 N ANISOU 251 NH1 ARG A 104 10439 10500 10829 367 1019 -49 N ATOM 252 NH2 ARG A 104 40.591 13.561 30.756 1.00 69.93 N ANISOU 252 NH2 ARG A 104 8761 8675 9134 341 921 -189 N ATOM 253 N THR A 105 35.278 18.737 26.785 1.00 42.13 N ANISOU 253 N THR A 105 5396 5727 4883 172 581 53 N ATOM 254 CA THR A 105 34.416 19.849 26.431 1.00 43.94 C ANISOU 254 CA THR A 105 5617 6020 5059 146 495 145 C ATOM 255 C THR A 105 33.784 20.448 27.686 1.00 41.19 C ANISOU 255 C THR A 105 5228 5580 4842 140 401 183 C ATOM 256 O THR A 105 33.778 19.824 28.750 1.00 40.12 O ANISOU 256 O THR A 105 5089 5350 4803 148 393 119 O ATOM 257 CB THR A 105 33.319 19.389 25.477 1.00 40.35 C ANISOU 257 CB THR A 105 5224 5662 4446 111 453 75 C ATOM 258 OG1 THR A 105 32.468 18.453 26.152 1.00 36.34 O ANISOU 258 OG1 THR A 105 4740 5087 3979 97 403 -40 O ATOM 259 CG2 THR A 105 33.920 18.725 24.244 1.00 41.61 C ANISOU 259 CG2 THR A 105 5434 5916 4458 115 551 15 C ATOM 260 N PRO A 106 33.245 21.666 27.586 1.00 38.86 N ANISOU 260 N PRO A 106 4900 5311 4554 127 332 289 N ATOM 261 CA PRO A 106 32.530 22.239 28.738 1.00 39.46 C ANISOU 261 CA PRO A 106 4941 5302 4750 121 248 311 C ATOM 262 C PRO A 106 31.521 21.284 29.350 1.00 36.30 C ANISOU 262 C PRO A 106 4575 4861 4356 105 206 197 C ATOM 263 O PRO A 106 31.476 21.130 30.576 1.00 34.26 O ANISOU 263 O PRO A 106 4300 4510 4206 113 189 169 O ATOM 264 CB PRO A 106 31.859 23.480 28.136 1.00 43.09 C ANISOU 264 CB PRO A 106 5371 5820 5182 103 183 423 C ATOM 265 CG PRO A 106 32.761 23.884 27.026 1.00 41.51 C ANISOU 265 CG PRO A 106 5166 5705 4903 111 246 506 C ATOM 266 CD PRO A 106 33.322 22.609 26.455 1.00 51.31 C ANISOU 266 CD PRO A 106 6464 6989 6041 118 333 402 C ATOM 267 N MET A 107 30.706 20.633 28.519 1.00 35.43 N ANISOU 267 N MET A 107 4511 4822 4130 80 186 132 N ATOM 268 CA MET A 107 29.723 19.682 29.024 1.00 41.90 C ANISOU 268 CA MET A 107 5357 5600 4964 61 146 27 C ATOM 269 C MET A 107 30.369 18.648 29.942 1.00 33.07 C ANISOU 269 C MET A 107 4247 4392 3925 82 202 -54 C ATOM 270 O MET A 107 29.853 18.354 31.026 1.00 34.68 O ANISOU 270 O MET A 107 4441 4519 4217 79 169 -86 O ATOM 271 CB MET A 107 29.023 18.994 27.850 1.00 48.95 C ANISOU 271 CB MET A 107 6300 6583 5714 31 127 -43 C ATOM 272 CG MET A 107 27.861 18.101 28.253 1.00 58.43 C ANISOU 272 CG MET A 107 7520 7746 6936 5 72 -142 C ATOM 273 SD MET A 107 27.569 16.763 27.079 1.00 83.33 S ANISOU 273 SD MET A 107 10743 10969 9947 -22 86 -280 S ATOM 274 CE MET A 107 27.410 17.660 25.536 1.00 62.68 C ANISOU 274 CE MET A 107 8147 8510 7159 -45 52 -200 C ATOM 275 N PHE A 108 31.499 18.075 29.525 1.00 32.61 N ANISOU 275 N PHE A 108 4205 4344 3843 103 289 -83 N ATOM 276 CA PHE A 108 32.103 17.014 30.328 1.00 37.68 C ANISOU 276 CA PHE A 108 4850 4897 4568 122 339 -155 C ATOM 277 C PHE A 108 32.898 17.559 31.507 1.00 35.20 C ANISOU 277 C PHE A 108 4488 4502 4384 146 343 -85 C ATOM 278 O PHE A 108 33.028 16.877 32.531 1.00 32.64 O ANISOU 278 O PHE A 108 4159 4095 4147 153 345 -123 O ATOM 279 CB PHE A 108 32.978 16.124 29.448 1.00 40.54 C ANISOU 279 CB PHE A 108 5242 5291 4872 137 434 -223 C ATOM 280 CG PHE A 108 32.187 15.269 28.513 1.00 42.89 C ANISOU 280 CG PHE A 108 5595 5647 5055 110 427 -331 C ATOM 281 CD1 PHE A 108 31.366 14.268 29.005 1.00 53.41 C ANISOU 281 CD1 PHE A 108 6944 6921 6427 92 391 -427 C ATOM 282 CD2 PHE A 108 32.237 15.481 27.148 1.00 40.57 C ANISOU 282 CD2 PHE A 108 5335 5468 4611 100 453 -334 C ATOM 283 CE1 PHE A 108 30.620 13.486 28.151 1.00 56.45 C ANISOU 283 CE1 PHE A 108 7378 7354 6718 63 376 -533 C ATOM 284 CE2 PHE A 108 31.493 14.702 26.289 1.00 46.95 C ANISOU 284 CE2 PHE A 108 6198 6335 5306 71 436 -443 C ATOM 285 CZ PHE A 108 30.683 13.702 26.791 1.00 47.82 C ANISOU 285 CZ PHE A 108 6323 6378 5469 52 394 -546 C ATOM 286 N VAL A 109 33.430 18.775 31.397 1.00 28.51 N ANISOU 286 N VAL A 109 3605 3675 3554 156 340 21 N ATOM 287 CA VAL A 109 34.000 19.417 32.575 1.00 25.91 C ANISOU 287 CA VAL A 109 3229 3267 3347 171 321 82 C ATOM 288 C VAL A 109 32.928 19.576 33.641 1.00 28.45 C ANISOU 288 C VAL A 109 3552 3541 3719 154 244 65 C ATOM 289 O VAL A 109 33.196 19.448 34.842 1.00 29.33 O ANISOU 289 O VAL A 109 3650 3577 3918 161 232 60 O ATOM 290 CB VAL A 109 34.636 20.768 32.196 1.00 34.79 C ANISOU 290 CB VAL A 109 4310 4419 4490 180 322 198 C ATOM 291 CG1 VAL A 109 35.097 21.502 33.439 1.00 40.50 C ANISOU 291 CG1 VAL A 109 4989 5059 5342 189 285 250 C ATOM 292 CG2 VAL A 109 35.810 20.549 31.260 1.00 41.68 C ANISOU 292 CG2 VAL A 109 5177 5334 5325 200 414 220 C ATOM 293 N LEU A 110 31.692 19.846 33.219 1.00 28.76 N ANISOU 293 N LEU A 110 3604 3624 3701 130 193 56 N ATOM 294 CA LEU A 110 30.606 20.002 34.179 1.00 29.81 C ANISOU 294 CA LEU A 110 3731 3712 3884 115 131 39 C ATOM 295 C LEU A 110 30.174 18.658 34.747 1.00 27.85 C ANISOU 295 C LEU A 110 3513 3423 3646 107 140 -54 C ATOM 296 O LEU A 110 29.920 18.545 35.950 1.00 29.96 O ANISOU 296 O LEU A 110 3773 3628 3983 107 122 -65 O ATOM 297 CB LEU A 110 29.427 20.713 33.522 1.00 32.35 C ANISOU 297 CB LEU A 110 4044 4088 4159 94 73 68 C ATOM 298 CG LEU A 110 29.712 22.170 33.155 1.00 33.45 C ANISOU 298 CG LEU A 110 4141 4250 4317 100 52 176 C ATOM 299 CD1 LEU A 110 28.686 22.702 32.173 1.00 40.08 C ANISOU 299 CD1 LEU A 110 4974 5161 5094 78 0 215 C ATOM 300 CD2 LEU A 110 29.734 23.011 34.415 1.00 31.44 C ANISOU 300 CD2 LEU A 110 3848 3916 4180 109 25 207 C ATOM 301 N VAL A 111 30.091 17.625 33.908 1.00 26.92 N ANISOU 301 N VAL A 111 3429 3338 3461 100 170 -123 N ATOM 302 CA VAL A 111 29.744 16.303 34.422 1.00 30.92 C ANISOU 302 CA VAL A 111 3957 3794 3996 92 181 -208 C ATOM 303 C VAL A 111 30.808 15.825 35.400 1.00 26.72 C ANISOU 303 C VAL A 111 3414 3189 3550 116 222 -202 C ATOM 304 O VAL A 111 30.497 15.226 36.436 1.00 35.43 O ANISOU 304 O VAL A 111 4517 4231 4715 111 210 -224 O ATOM 305 CB VAL A 111 29.545 15.314 33.261 1.00 33.92 C ANISOU 305 CB VAL A 111 4374 4219 4294 79 206 -293 C ATOM 306 CG1 VAL A 111 29.365 13.898 33.783 1.00 32.93 C ANISOU 306 CG1 VAL A 111 4264 4025 4224 74 225 -379 C ATOM 307 CG2 VAL A 111 28.341 15.725 32.445 1.00 38.38 C ANISOU 307 CG2 VAL A 111 4949 4854 4779 49 144 -296 C ATOM 308 N GLY A 112 32.076 16.103 35.100 1.00 29.57 N ANISOU 308 N GLY A 112 3760 3554 3919 140 269 -163 N ATOM 309 CA GLY A 112 33.144 15.700 35.999 1.00 29.37 C ANISOU 309 CA GLY A 112 3716 3459 3984 162 299 -146 C ATOM 310 C GLY A 112 33.081 16.408 37.337 1.00 29.37 C ANISOU 310 C GLY A 112 3695 3414 4051 160 248 -92 C ATOM 311 O GLY A 112 33.401 15.820 38.374 1.00 28.34 O ANISOU 311 O GLY A 112 3559 3222 3985 164 246 -95 O ATOM 312 N SER A 113 32.662 17.674 37.333 1.00 32.12 N ANISOU 312 N SER A 113 4029 3792 4385 153 205 -43 N ATOM 313 CA SER A 113 32.470 18.398 38.583 1.00 26.53 C ANISOU 313 CA SER A 113 3306 3043 3732 149 157 -9 C ATOM 314 C SER A 113 31.343 17.780 39.401 1.00 33.28 C ANISOU 314 C SER A 113 4181 3873 4589 130 133 -58 C ATOM 315 O SER A 113 31.495 17.548 40.605 1.00 30.33 O ANISOU 315 O SER A 113 3810 3455 4260 130 121 -55 O ATOM 316 CB SER A 113 32.189 19.872 38.288 1.00 31.18 C ANISOU 316 CB SER A 113 3870 3660 4316 146 122 46 C ATOM 317 OG SER A 113 31.831 20.576 39.463 1.00 28.12 O ANISOU 317 OG SER A 113 3472 3234 3979 140 78 57 O ATOM 318 N LEU A 114 30.203 17.499 38.763 1.00 24.89 N ANISOU 318 N LEU A 114 3133 2844 3479 114 124 -98 N ATOM 319 CA LEU A 114 29.099 16.866 39.478 1.00 27.38 C ANISOU 319 CA LEU A 114 3461 3134 3808 95 107 -139 C ATOM 320 C LEU A 114 29.528 15.527 40.066 1.00 29.87 C ANISOU 320 C LEU A 114 3790 3401 4159 97 137 -170 C ATOM 321 O LEU A 114 29.254 15.231 41.236 1.00 27.91 O ANISOU 321 O LEU A 114 3544 3114 3946 91 129 -166 O ATOM 322 CB LEU A 114 27.903 16.680 38.543 1.00 27.75 C ANISOU 322 CB LEU A 114 3514 3222 3806 74 89 -177 C ATOM 323 CG LEU A 114 26.659 16.017 39.147 1.00 30.69 C ANISOU 323 CG LEU A 114 3890 3569 4203 53 72 -217 C ATOM 324 CD1 LEU A 114 26.051 16.879 40.246 1.00 29.39 C ANISOU 324 CD1 LEU A 114 3706 3384 4077 51 50 -185 C ATOM 325 CD2 LEU A 114 25.625 15.729 38.076 1.00 39.09 C ANISOU 325 CD2 LEU A 114 4955 4672 5224 30 47 -256 C ATOM 326 N ALA A 115 30.201 14.702 39.260 1.00 26.82 N ANISOU 326 N ALA A 115 3412 3016 3764 107 177 -200 N ATOM 327 CA ALA A 115 30.622 13.384 39.721 1.00 29.00 C ANISOU 327 CA ALA A 115 3692 3235 4092 111 208 -228 C ATOM 328 C ALA A 115 31.631 13.484 40.857 1.00 31.54 C ANISOU 328 C ALA A 115 3998 3512 4475 126 207 -170 C ATOM 329 O ALA A 115 31.606 12.671 41.787 1.00 30.27 O ANISOU 329 O ALA A 115 3836 3301 4362 121 206 -166 O ATOM 330 CB ALA A 115 31.212 12.590 38.556 1.00 25.41 C ANISOU 330 CB ALA A 115 3245 2787 3623 122 258 -279 C ATOM 331 N THR A 116 32.540 14.461 40.793 1.00 29.19 N ANISOU 331 N THR A 116 3683 3229 4178 142 202 -120 N ATOM 332 CA THR A 116 33.509 14.629 41.871 1.00 24.61 C ANISOU 332 CA THR A 116 3086 2609 3657 151 187 -64 C ATOM 333 C THR A 116 32.812 15.022 43.163 1.00 31.07 C ANISOU 333 C THR A 116 3916 3418 4471 134 140 -48 C ATOM 334 O THR A 116 33.124 14.489 44.234 1.00 27.66 O ANISOU 334 O THR A 116 3485 2951 4075 130 127 -25 O ATOM 335 CB THR A 116 34.552 15.681 41.491 1.00 31.77 C ANISOU 335 CB THR A 116 3965 3531 4574 168 186 -14 C ATOM 336 OG1 THR A 116 35.276 15.247 40.334 1.00 32.58 O ANISOU 336 OG1 THR A 116 4056 3644 4678 187 244 -27 O ATOM 337 CG2 THR A 116 35.528 15.921 42.639 1.00 31.03 C ANISOU 337 CG2 THR A 116 3851 3395 4544 173 154 42 C ATOM 338 N ALA A 117 31.865 15.956 43.075 1.00 28.32 N ANISOU 338 N ALA A 117 3574 3105 4081 122 116 -58 N ATOM 339 CA ALA A 117 31.122 16.388 44.251 1.00 28.55 C ANISOU 339 CA ALA A 117 3614 3129 4103 108 85 -55 C ATOM 340 C ALA A 117 30.345 15.230 44.865 1.00 29.12 C ANISOU 340 C ALA A 117 3703 3181 4179 92 98 -78 C ATOM 341 O ALA A 117 30.355 15.040 46.087 1.00 31.28 O ANISOU 341 O ALA A 117 3988 3438 4459 84 86 -56 O ATOM 342 CB ALA A 117 30.181 17.529 43.869 1.00 26.19 C ANISOU 342 CB ALA A 117 3310 2864 3777 102 67 -66 C ATOM 343 N ASP A 118 29.661 14.443 44.032 1.00 26.43 N ANISOU 343 N ASP A 118 3365 2845 3834 86 121 -119 N ATOM 344 CA ASP A 118 28.929 13.293 44.553 1.00 25.56 C ANISOU 344 CA ASP A 118 3262 2706 3745 70 134 -137 C ATOM 345 C ASP A 118 29.882 12.243 45.111 1.00 29.93 C ANISOU 345 C ASP A 118 3812 3211 4349 77 149 -109 C ATOM 346 O ASP A 118 29.616 11.660 46.168 1.00 28.41 O ANISOU 346 O ASP A 118 3624 2995 4176 65 147 -83 O ATOM 347 CB ASP A 118 28.034 12.701 43.467 1.00 28.29 C ANISOU 347 CB ASP A 118 3606 3059 4083 58 147 -194 C ATOM 348 CG ASP A 118 26.849 13.602 43.130 1.00 48.05 C ANISOU 348 CG ASP A 118 6104 5602 6550 46 124 -209 C ATOM 349 OD1 ASP A 118 26.429 14.393 44.007 1.00 42.07 O ANISOU 349 OD1 ASP A 118 5343 4851 5789 43 110 -184 O ATOM 350 OD2 ASP A 118 26.333 13.521 41.992 1.00 45.56 O ANISOU 350 OD2 ASP A 118 5786 5312 6212 38 117 -247 O ATOM 351 N LEU A 119 31.004 11.997 44.430 1.00 31.00 N ANISOU 351 N LEU A 119 3936 3332 4511 97 166 -107 N ATOM 352 CA LEU A 119 32.032 11.132 45.002 1.00 26.58 C ANISOU 352 CA LEU A 119 3361 2720 4017 107 175 -69 C ATOM 353 C LEU A 119 32.446 11.619 46.384 1.00 30.48 C ANISOU 353 C LEU A 119 3859 3215 4509 102 134 -2 C ATOM 354 O LEU A 119 32.487 10.842 47.343 1.00 28.67 O ANISOU 354 O LEU A 119 3630 2955 4311 92 127 37 O ATOM 355 CB LEU A 119 33.248 11.067 44.081 1.00 32.05 C ANISOU 355 CB LEU A 119 4033 3401 4742 133 204 -72 C ATOM 356 CG LEU A 119 34.476 10.366 44.669 1.00 34.81 C ANISOU 356 CG LEU A 119 4354 3693 5178 148 208 -18 C ATOM 357 CD1 LEU A 119 34.163 8.935 45.090 1.00 31.48 C ANISOU 357 CD1 LEU A 119 3925 3212 4822 140 224 -22 C ATOM 358 CD2 LEU A 119 35.593 10.393 43.655 1.00 37.71 C ANISOU 358 CD2 LEU A 119 4694 4052 5580 176 250 -27 C ATOM 359 N LEU A 120 32.754 12.912 46.505 1.00 27.38 N ANISOU 359 N LEU A 120 3470 2856 4079 105 105 14 N ATOM 360 CA LEU A 120 33.175 13.441 47.796 1.00 28.48 C ANISOU 360 CA LEU A 120 3617 2999 4207 97 60 63 C ATOM 361 C LEU A 120 32.076 13.285 48.837 1.00 28.73 C ANISOU 361 C LEU A 120 3677 3046 4195 74 53 61 C ATOM 362 O LEU A 120 32.352 12.955 49.995 1.00 29.57 O ANISOU 362 O LEU A 120 3794 3146 4296 62 30 107 O ATOM 363 CB LEU A 120 33.583 14.904 47.656 1.00 22.24 C ANISOU 363 CB LEU A 120 2821 2234 3393 103 30 66 C ATOM 364 CG LEU A 120 34.885 15.124 46.888 1.00 28.37 C ANISOU 364 CG LEU A 120 3563 2995 4221 124 34 91 C ATOM 365 CD1 LEU A 120 35.091 16.602 46.624 1.00 31.08 C ANISOU 365 CD1 LEU A 120 3897 3362 4551 127 8 94 C ATOM 366 CD2 LEU A 120 36.062 14.546 47.658 1.00 33.41 C ANISOU 366 CD2 LEU A 120 4182 3595 4919 127 8 150 C ATOM 367 N ALA A 121 30.821 13.505 48.444 1.00 28.57 N ANISOU 367 N ALA A 121 3666 3047 4142 66 75 13 N ATOM 368 CA ALA A 121 29.722 13.353 49.391 1.00 28.11 C ANISOU 368 CA ALA A 121 3628 3003 4050 46 82 11 C ATOM 369 C ALA A 121 29.565 11.900 49.827 1.00 33.53 C ANISOU 369 C ALA A 121 4310 3655 4774 35 102 41 C ATOM 370 O ALA A 121 29.286 11.623 51.001 1.00 30.06 O ANISOU 370 O ALA A 121 3887 3223 4311 19 99 80 O ATOM 371 CB ALA A 121 28.425 13.872 48.774 1.00 24.99 C ANISOU 371 CB ALA A 121 3230 2631 3635 41 100 -42 C ATOM 372 N GLY A 122 29.728 10.960 48.895 1.00 28.79 N ANISOU 372 N GLY A 122 3689 3017 4234 42 125 23 N ATOM 373 CA GLY A 122 29.667 9.553 49.263 1.00 26.70 C ANISOU 373 CA GLY A 122 3411 2704 4029 34 143 53 C ATOM 374 C GLY A 122 30.731 9.173 50.275 1.00 25.96 C ANISOU 374 C GLY A 122 3315 2591 3959 35 117 135 C ATOM 375 O GLY A 122 30.430 8.621 51.335 1.00 30.35 O ANISOU 375 O GLY A 122 3878 3143 4512 17 114 190 O ATOM 376 N LEU A 123 31.997 9.461 49.956 1.00 30.32 N ANISOU 376 N LEU A 123 3852 3130 4536 55 97 150 N ATOM 377 CA LEU A 123 33.079 9.217 50.903 1.00 32.80 C ANISOU 377 CA LEU A 123 4158 3428 4878 55 59 234 C ATOM 378 C LEU A 123 32.796 9.885 52.240 1.00 30.78 C ANISOU 378 C LEU A 123 3938 3225 4533 33 19 272 C ATOM 379 O LEU A 123 33.092 9.324 53.300 1.00 31.58 O ANISOU 379 O LEU A 123 4042 3321 4635 18 -8 348 O ATOM 380 CB LEU A 123 34.402 9.730 50.335 1.00 34.79 C ANISOU 380 CB LEU A 123 4384 3667 5167 79 41 240 C ATOM 381 CG LEU A 123 34.845 9.142 48.998 1.00 33.15 C ANISOU 381 CG LEU A 123 4143 3414 5038 104 90 198 C ATOM 382 CD1 LEU A 123 36.072 9.876 48.480 1.00 34.24 C ANISOU 382 CD1 LEU A 123 4256 3553 5199 126 79 209 C ATOM 383 CD2 LEU A 123 35.121 7.661 49.157 1.00 36.93 C ANISOU 383 CD2 LEU A 123 4591 3821 5620 107 110 233 C ATOM 384 N GLY A 124 32.226 11.090 52.204 1.00 30.41 N ANISOU 384 N GLY A 124 3918 3228 4407 29 15 220 N ATOM 385 CA GLY A 124 31.935 11.799 53.436 1.00 33.19 C ANISOU 385 CA GLY A 124 4309 3632 4670 9 -14 236 C ATOM 386 C GLY A 124 30.946 11.069 54.325 1.00 29.56 C ANISOU 386 C GLY A 124 3868 3187 4176 -13 14 265 C ATOM 387 O GLY A 124 31.080 11.080 55.549 1.00 31.35 O ANISOU 387 O GLY A 124 4123 3447 4340 -32 -13 316 O ATOM 388 N LEU A 125 29.929 10.437 53.728 1.00 25.26 N ANISOU 388 N LEU A 125 3308 2621 3667 -13 66 235 N ATOM 389 CA LEU A 125 28.992 9.653 54.530 1.00 22.33 C ANISOU 389 CA LEU A 125 2945 2257 3283 -35 99 273 C ATOM 390 C LEU A 125 29.696 8.480 55.198 1.00 27.66 C ANISOU 390 C LEU A 125 3606 2899 4005 -44 80 372 C ATOM 391 O LEU A 125 29.421 8.160 56.360 1.00 32.32 O ANISOU 391 O LEU A 125 4216 3519 4545 -65 80 439 O ATOM 392 CB LEU A 125 27.837 9.161 53.664 1.00 27.79 C ANISOU 392 CB LEU A 125 3612 2920 4027 -36 150 222 C ATOM 393 CG LEU A 125 26.949 10.273 53.112 1.00 32.62 C ANISOU 393 CG LEU A 125 4232 3566 4596 -31 166 141 C ATOM 394 CD1 LEU A 125 25.973 9.713 52.097 1.00 27.27 C ANISOU 394 CD1 LEU A 125 3523 2856 3982 -34 199 94 C ATOM 395 CD2 LEU A 125 26.224 10.964 54.259 1.00 32.02 C ANISOU 395 CD2 LEU A 125 4187 3546 4435 -46 183 146 C ATOM 396 N ILE A 126 30.616 7.835 54.479 1.00 24.93 N ANISOU 396 N ILE A 126 3224 2491 3758 -26 67 386 N ATOM 397 CA ILE A 126 31.411 6.758 55.063 1.00 31.84 C ANISOU 397 CA ILE A 126 4074 3323 4702 -30 44 486 C ATOM 398 C ILE A 126 32.297 7.303 56.176 1.00 31.74 C ANISOU 398 C ILE A 126 4086 3358 4617 -41 -23 556 C ATOM 399 O ILE A 126 32.384 6.729 57.268 1.00 30.94 O ANISOU 399 O ILE A 126 3991 3270 4494 -62 -45 653 O ATOM 400 CB ILE A 126 32.252 6.066 53.974 1.00 34.79 C ANISOU 400 CB ILE A 126 4397 3615 5207 -4 51 471 C ATOM 401 CG1 ILE A 126 31.348 5.511 52.866 1.00 37.76 C ANISOU 401 CG1 ILE A 126 4755 3950 5643 1 110 389 C ATOM 402 CG2 ILE A 126 33.117 4.976 54.591 1.00 40.20 C ANISOU 402 CG2 ILE A 126 5046 4245 5985 -6 25 581 C ATOM 403 CD1 ILE A 126 32.110 5.003 51.649 1.00 36.73 C ANISOU 403 CD1 ILE A 126 4586 3751 5618 28 129 342 C ATOM 404 N LEU A 127 32.978 8.417 55.910 1.00 28.55 N ANISOU 404 N LEU A 127 3694 2979 4175 -29 -59 513 N ATOM 405 CA LEU A 127 33.854 9.003 56.918 1.00 37.03 C ANISOU 405 CA LEU A 127 4791 4096 5184 -42 -134 567 C ATOM 406 C LEU A 127 33.076 9.391 58.167 1.00 32.28 C ANISOU 406 C LEU A 127 4248 3573 4445 -73 -138 580 C ATOM 407 O LEU A 127 33.551 9.196 59.292 1.00 36.58 O ANISOU 407 O LEU A 127 4812 4152 4935 -95 -191 664 O ATOM 408 CB LEU A 127 34.570 10.222 56.340 1.00 37.66 C ANISOU 408 CB LEU A 127 4869 4183 5257 -26 -166 506 C ATOM 409 CG LEU A 127 35.695 9.937 55.344 1.00 43.94 C ANISOU 409 CG LEU A 127 5607 4912 6177 2 -173 516 C ATOM 410 CD1 LEU A 127 36.165 11.224 54.683 1.00 55.10 C ANISOU 410 CD1 LEU A 127 7018 6338 7579 16 -190 452 C ATOM 411 CD2 LEU A 127 36.853 9.241 56.038 1.00 53.73 C ANISOU 411 CD2 LEU A 127 6816 6121 7480 -4 -234 626 C ATOM 412 N HIS A 128 31.879 9.947 57.988 1.00 38.03 N ANISOU 412 N HIS A 128 5002 4334 5113 -74 -82 500 N ATOM 413 CA HIS A 128 31.054 10.300 59.136 1.00 33.20 C ANISOU 413 CA HIS A 128 4444 3797 4374 -99 -66 503 C ATOM 414 C HIS A 128 30.785 9.083 60.011 1.00 33.43 C ANISOU 414 C HIS A 128 4472 3832 4397 -122 -52 612 C ATOM 415 O HIS A 128 30.837 9.171 61.242 1.00 32.06 O ANISOU 415 O HIS A 128 4342 3725 4113 -147 -78 667 O ATOM 416 CB HIS A 128 29.745 10.926 58.657 1.00 33.85 C ANISOU 416 CB HIS A 128 4536 3895 4431 -93 5 405 C ATOM 417 CG HIS A 128 28.890 11.454 59.764 1.00 40.86 C ANISOU 417 CG HIS A 128 5475 4858 5192 -113 36 389 C ATOM 418 ND1 HIS A 128 27.823 10.750 60.281 1.00 47.11 N ANISOU 418 ND1 HIS A 128 6270 5667 5961 -128 102 425 N ATOM 419 CD2 HIS A 128 28.949 12.613 60.460 1.00 44.58 C ANISOU 419 CD2 HIS A 128 5996 5389 5555 -121 15 336 C ATOM 420 CE1 HIS A 128 27.262 11.454 61.247 1.00 47.46 C ANISOU 420 CE1 HIS A 128 6365 5786 5882 -143 128 397 C ATOM 421 NE2 HIS A 128 27.925 12.589 61.375 1.00 48.99 N ANISOU 421 NE2 HIS A 128 6590 6005 6021 -139 75 336 N ATOM 422 N PHE A 129 30.493 7.935 59.395 1.00 31.88 N ANISOU 422 N PHE A 129 4228 3568 4319 -114 -12 645 N ATOM 423 CA PHE A 129 30.302 6.717 60.175 1.00 32.59 C ANISOU 423 CA PHE A 129 4304 3648 4431 -134 -2 763 C ATOM 424 C PHE A 129 31.584 6.318 60.895 1.00 31.89 C ANISOU 424 C PHE A 129 4210 3560 4348 -144 -84 876 C ATOM 425 O PHE A 129 31.553 5.946 62.074 1.00 35.42 O ANISOU 425 O PHE A 129 4682 4058 4720 -172 -104 978 O ATOM 426 CB PHE A 129 29.829 5.581 59.269 1.00 38.27 C ANISOU 426 CB PHE A 129 4963 4276 5300 -123 50 765 C ATOM 427 CG PHE A 129 29.468 4.330 60.014 1.00 36.08 C ANISOU 427 CG PHE A 129 4664 3979 5066 -145 70 886 C ATOM 428 CD1 PHE A 129 30.449 3.435 60.414 1.00 35.07 C ANISOU 428 CD1 PHE A 129 4503 3807 5014 -149 20 1006 C ATOM 429 CD2 PHE A 129 28.147 4.051 60.318 1.00 33.98 C ANISOU 429 CD2 PHE A 129 4402 3732 4777 -163 140 890 C ATOM 430 CE1 PHE A 129 30.119 2.288 61.106 1.00 34.84 C ANISOU 430 CE1 PHE A 129 4447 3756 5034 -170 37 1131 C ATOM 431 CE2 PHE A 129 27.809 2.901 61.012 1.00 34.96 C ANISOU 431 CE2 PHE A 129 4500 3836 4948 -185 162 1013 C ATOM 432 CZ PHE A 129 28.796 2.020 61.406 1.00 48.02 C ANISOU 432 CZ PHE A 129 6124 5448 6676 -189 109 1136 C ATOM 433 N VAL A 130 32.720 6.393 60.198 1.00 35.77 N ANISOU 433 N VAL A 130 4665 3995 4930 -122 -133 867 N ATOM 434 CA VAL A 130 33.992 5.953 60.768 1.00 33.34 C ANISOU 434 CA VAL A 130 4335 3672 4662 -128 -216 980 C ATOM 435 C VAL A 130 34.311 6.732 62.037 1.00 35.43 C ANISOU 435 C VAL A 130 4662 4038 4763 -159 -287 1017 C ATOM 436 O VAL A 130 34.673 6.155 63.068 1.00 34.33 O ANISOU 436 O VAL A 130 4527 3927 4588 -184 -338 1142 O ATOM 437 CB VAL A 130 35.119 6.101 59.729 1.00 42.66 C ANISOU 437 CB VAL A 130 5463 4779 5965 -96 -245 945 C ATOM 438 CG1 VAL A 130 36.489 6.004 60.395 1.00 39.11 C ANISOU 438 CG1 VAL A 130 4992 4326 5541 -104 -345 1051 C ATOM 439 CG2 VAL A 130 34.977 5.049 58.650 1.00 37.11 C ANISOU 439 CG2 VAL A 130 4698 3974 5427 -70 -183 931 C ATOM 440 N PHE A 131 34.206 8.054 61.975 1.00 36.96 N ANISOU 440 N PHE A 131 4901 4284 4857 -157 -296 909 N ATOM 441 CA PHE A 131 34.591 8.894 63.099 1.00 33.57 C ANISOU 441 CA PHE A 131 4533 3945 4276 -186 -370 918 C ATOM 442 C PHE A 131 33.463 9.084 64.093 1.00 42.61 C ANISOU 442 C PHE A 131 5747 5184 5259 -214 -321 908 C ATOM 443 O PHE A 131 33.625 9.832 65.062 1.00 43.56 O ANISOU 443 O PHE A 131 5930 5390 5230 -240 -370 894 O ATOM 444 CB PHE A 131 35.098 10.237 62.589 1.00 33.92 C ANISOU 444 CB PHE A 131 4588 3992 4309 -173 -406 806 C ATOM 445 CG PHE A 131 36.426 10.135 61.918 1.00 34.42 C ANISOU 445 CG PHE A 131 4588 3982 4507 -154 -469 839 C ATOM 446 CD1 PHE A 131 37.580 10.008 62.671 1.00 45.70 C ANISOU 446 CD1 PHE A 131 6007 5422 5935 -174 -577 935 C ATOM 447 CD2 PHE A 131 36.526 10.125 60.540 1.00 37.50 C ANISOU 447 CD2 PHE A 131 4925 4296 5028 -117 -419 780 C ATOM 448 CE1 PHE A 131 38.811 9.898 62.062 1.00 51.13 C ANISOU 448 CE1 PHE A 131 6627 6038 6764 -155 -629 971 C ATOM 449 CE2 PHE A 131 37.755 10.017 59.925 1.00 46.01 C ANISOU 449 CE2 PHE A 131 5942 5309 6232 -97 -464 812 C ATOM 450 CZ PHE A 131 38.899 9.901 60.688 1.00 45.23 C ANISOU 450 CZ PHE A 131 5825 5213 6146 -115 -566 908 C ATOM 451 N GLN A 132 32.334 8.421 63.876 1.00 41.44 N ANISOU 451 N GLN A 132 5587 5021 5139 -209 -225 911 N ATOM 452 CA GLN A 132 31.311 8.293 64.900 1.00 38.35 C ANISOU 452 CA GLN A 132 5247 4712 4614 -236 -170 940 C ATOM 453 C GLN A 132 31.476 7.009 65.707 1.00 38.79 C ANISOU 453 C GLN A 132 5286 4774 4679 -261 -188 1110 C ATOM 454 O GLN A 132 31.357 7.034 66.936 1.00 39.77 O ANISOU 454 O GLN A 132 5466 4994 4650 -294 -204 1176 O ATOM 455 CB GLN A 132 29.929 8.337 64.248 1.00 41.09 C ANISOU 455 CB GLN A 132 5580 5037 4994 -220 -56 855 C ATOM 456 CG GLN A 132 28.774 8.291 65.215 1.00 51.75 C ANISOU 456 CG GLN A 132 6975 6468 6219 -244 21 873 C ATOM 457 CD GLN A 132 27.470 8.671 64.550 1.00 66.58 C ANISOU 457 CD GLN A 132 8839 8328 8129 -226 123 767 C ATOM 458 OE1 GLN A 132 27.411 8.855 63.332 1.00 68.79 O ANISOU 458 OE1 GLN A 132 9077 8535 8527 -199 131 690 O ATOM 459 NE2 GLN A 132 26.415 8.798 65.346 1.00 82.50 N ANISOU 459 NE2 GLN A 132 10891 10415 10042 -242 203 765 N ATOM 460 N TYR A 133 31.788 5.891 65.045 1.00 32.41 N ANISOU 460 N TYR A 133 4402 3865 4047 -245 -187 1184 N ATOM 461 CA TYR A 133 31.782 4.581 65.687 1.00 33.98 C ANISOU 461 CA TYR A 133 4571 4050 4292 -266 -190 1349 C ATOM 462 C TYR A 133 33.143 3.905 65.782 1.00 38.99 C ANISOU 462 C TYR A 133 5156 4630 5030 -266 -290 1471 C ATOM 463 O TYR A 133 33.342 3.096 66.689 1.00 37.98 O ANISOU 463 O TYR A 133 5020 4524 4886 -292 -324 1628 O ATOM 464 CB TYR A 133 30.831 3.636 64.942 1.00 36.31 C ANISOU 464 CB TYR A 133 4807 4258 4731 -251 -94 1349 C ATOM 465 CG TYR A 133 29.376 4.016 65.051 1.00 34.65 C ANISOU 465 CG TYR A 133 4630 4099 4435 -258 8 1274 C ATOM 466 CD1 TYR A 133 28.664 3.771 66.215 1.00 33.45 C ANISOU 466 CD1 TYR A 133 4516 4032 4160 -290 48 1361 C ATOM 467 CD2 TYR A 133 28.710 4.610 63.987 1.00 34.97 C ANISOU 467 CD2 TYR A 133 4662 4104 4521 -233 64 1125 C ATOM 468 CE1 TYR A 133 27.330 4.114 66.319 1.00 37.80 C ANISOU 468 CE1 TYR A 133 5090 4627 4647 -294 150 1296 C ATOM 469 CE2 TYR A 133 27.378 4.954 64.081 1.00 40.77 C ANISOU 469 CE2 TYR A 133 5417 4879 5196 -238 155 1063 C ATOM 470 CZ TYR A 133 26.691 4.703 65.247 1.00 38.69 C ANISOU 470 CZ TYR A 133 5185 4693 4822 -268 201 1147 C ATOM 471 OH TYR A 133 25.362 5.044 65.341 1.00 39.34 O ANISOU 471 OH TYR A 133 5278 4811 4857 -271 300 1087 O ATOM 472 N LEU A 134 34.077 4.186 64.877 1.00 40.42 N ANISOU 472 N LEU A 134 5296 4739 5324 -237 -334 1414 N ATOM 473 CA LEU A 134 35.360 3.488 64.870 1.00 41.95 C ANISOU 473 CA LEU A 134 5426 4864 5649 -231 -419 1529 C ATOM 474 C LEU A 134 36.471 4.296 65.511 1.00 39.41 C ANISOU 474 C LEU A 134 5135 4605 5236 -248 -537 1552 C ATOM 475 O LEU A 134 37.363 3.725 66.143 1.00 41.67 O ANISOU 475 O LEU A 134 5391 4884 5559 -264 -627 1695 O ATOM 476 CB LEU A 134 35.771 3.138 63.437 1.00 36.95 C ANISOU 476 CB LEU A 134 4715 4101 5222 -187 -386 1462 C ATOM 477 CG LEU A 134 34.770 2.285 62.661 1.00 40.07 C ANISOU 477 CG LEU A 134 5073 4419 5732 -171 -280 1426 C ATOM 478 CD1 LEU A 134 35.335 1.929 61.299 1.00 41.43 C ANISOU 478 CD1 LEU A 134 5176 4472 6094 -130 -257 1359 C ATOM 479 CD2 LEU A 134 34.419 1.029 63.450 1.00 40.82 C ANISOU 479 CD2 LEU A 134 5140 4495 5875 -195 -271 1583 C ATOM 480 N VAL A 135 36.434 5.611 65.335 1.00 38.84 N ANISOU 480 N VAL A 135 5116 4586 5057 -245 -545 1415 N ATOM 481 CA VAL A 135 37.366 6.539 65.961 1.00 39.10 C ANISOU 481 CA VAL A 135 5185 4682 4989 -266 -657 1412 C ATOM 482 C VAL A 135 36.515 7.642 66.575 1.00 49.39 C ANISOU 482 C VAL A 135 6587 6099 6081 -288 -630 1304 C ATOM 483 O VAL A 135 36.446 8.748 66.018 1.00 44.98 O ANISOU 483 O VAL A 135 6048 5541 5502 -272 -616 1162 O ATOM 484 CB VAL A 135 38.367 7.110 64.946 1.00 51.79 C ANISOU 484 CB VAL A 135 6740 6212 6725 -234 -695 1342 C ATOM 485 CG1 VAL A 135 39.333 8.060 65.638 1.00 60.63 C ANISOU 485 CG1 VAL A 135 7891 7391 7754 -260 -821 1342 C ATOM 486 CG2 VAL A 135 39.108 5.990 64.226 1.00 59.02 C ANISOU 486 CG2 VAL A 135 7554 7007 7864 -205 -695 1430 C ATOM 487 N PRO A 136 35.823 7.382 67.687 1.00 47.19 N ANISOU 487 N PRO A 136 6368 5915 5648 -322 -613 1365 N ATOM 488 CA PRO A 136 34.958 8.415 68.272 1.00 48.88 C ANISOU 488 CA PRO A 136 6674 6234 5663 -340 -569 1251 C ATOM 489 C PRO A 136 35.701 9.720 68.490 1.00 58.46 C ANISOU 489 C PRO A 136 7930 7489 6791 -351 -660 1154 C ATOM 490 O PRO A 136 36.648 9.780 69.281 1.00 54.86 O ANISOU 490 O PRO A 136 7493 7079 6273 -382 -781 1229 O ATOM 491 CB PRO A 136 34.512 7.791 69.600 1.00 59.35 C ANISOU 491 CB PRO A 136 8051 7662 6837 -381 -566 1375 C ATOM 492 CG PRO A 136 34.647 6.321 69.394 1.00 48.10 C ANISOU 492 CG PRO A 136 6548 6160 5569 -375 -557 1535 C ATOM 493 CD PRO A 136 35.817 6.139 68.478 1.00 51.14 C ANISOU 493 CD PRO A 136 6851 6430 6150 -347 -629 1546 C ATOM 494 N SER A 137 35.290 10.768 67.784 1.00 51.97 N ANISOU 494 N SER A 137 7121 6648 5977 -327 -609 992 N ATOM 495 CA SER A 137 35.975 12.054 67.867 1.00 61.30 C ANISOU 495 CA SER A 137 8332 7849 7108 -334 -690 891 C ATOM 496 C SER A 137 34.962 13.147 67.567 1.00 70.91 C ANISOU 496 C SER A 137 9591 9086 8265 -319 -599 722 C ATOM 497 O SER A 137 34.463 13.243 66.441 1.00 57.55 O ANISOU 497 O SER A 137 7855 7322 6691 -282 -520 657 O ATOM 498 CB SER A 137 37.150 12.114 66.894 1.00 53.07 C ANISOU 498 CB SER A 137 7209 6705 6248 -309 -758 903 C ATOM 499 OG SER A 137 37.830 13.353 66.992 1.00 66.74 O ANISOU 499 OG SER A 137 8962 8451 7946 -320 -840 814 O ATOM 500 N GLU A 138 34.654 13.964 68.575 1.00 49.87 N ANISOU 500 N GLU A 138 7012 6518 5418 -349 -612 650 N ATOM 501 CA GLU A 138 33.781 15.108 68.341 1.00 69.51 C ANISOU 501 CA GLU A 138 9533 9015 7861 -334 -533 484 C ATOM 502 C GLU A 138 34.416 16.076 67.352 1.00 63.13 C ANISOU 502 C GLU A 138 8681 8125 7181 -309 -576 391 C ATOM 503 O GLU A 138 33.748 16.571 66.436 1.00 49.77 O ANISOU 503 O GLU A 138 6961 6381 5570 -276 -495 301 O ATOM 504 CB GLU A 138 33.469 15.806 69.667 1.00 64.99 C ANISOU 504 CB GLU A 138 9063 8561 7071 -372 -543 418 C ATOM 505 CG GLU A 138 32.730 14.929 70.676 1.00 87.09 C ANISOU 505 CG GLU A 138 11911 11455 9724 -398 -482 509 C ATOM 506 CD GLU A 138 31.319 14.576 70.235 1.00104.04 C ANISOU 506 CD GLU A 138 14038 13584 11910 -370 -322 486 C ATOM 507 OE1 GLU A 138 30.873 15.079 69.180 1.00 94.68 O ANISOU 507 OE1 GLU A 138 12806 12318 10848 -332 -264 390 O ATOM 508 OE2 GLU A 138 30.654 13.792 70.948 1.00104.29 O ANISOU 508 OE2 GLU A 138 14095 13681 11848 -387 -258 571 O ATOM 509 N THR A 139 35.717 16.337 67.503 1.00 47.64 N ANISOU 509 N THR A 139 6706 6149 5247 -326 -707 423 N ATOM 510 CA THR A 139 36.387 17.286 66.621 1.00 56.88 C ANISOU 510 CA THR A 139 7829 7242 6541 -306 -750 346 C ATOM 511 C THR A 139 36.309 16.832 65.167 1.00 59.48 C ANISOU 511 C THR A 139 8073 7474 7054 -259 -684 369 C ATOM 512 O THR A 139 35.917 17.604 64.285 1.00 49.38 O ANISOU 512 O THR A 139 6771 6149 5844 -232 -631 274 O ATOM 513 CB THR A 139 37.845 17.473 67.049 1.00 52.22 C ANISOU 513 CB THR A 139 7225 6648 5966 -334 -905 400 C ATOM 514 OG1 THR A 139 38.576 16.257 66.839 1.00 72.50 O ANISOU 514 OG1 THR A 139 9733 9180 8632 -330 -945 555 O ATOM 515 CG2 THR A 139 37.929 17.870 68.518 1.00 61.96 C ANISOU 515 CG2 THR A 139 8553 7991 7000 -386 -982 376 C ATOM 516 N VAL A 140 36.676 15.576 64.894 1.00 49.84 N ANISOU 516 N VAL A 140 6803 6219 5915 -251 -686 496 N ATOM 517 CA VAL A 140 36.652 15.094 63.518 1.00 60.37 C ANISOU 517 CA VAL A 140 8060 7463 7415 -209 -624 509 C ATOM 518 C VAL A 140 35.225 14.930 63.005 1.00 49.10 C ANISOU 518 C VAL A 140 6641 6034 5981 -189 -495 450 C ATOM 519 O VAL A 140 35.005 14.952 61.789 1.00 43.96 O ANISOU 519 O VAL A 140 5941 5321 5442 -156 -440 413 O ATOM 520 CB VAL A 140 37.441 13.775 63.391 1.00 57.42 C ANISOU 520 CB VAL A 140 7629 7044 7144 -206 -658 651 C ATOM 521 CG1 VAL A 140 37.493 13.318 61.934 1.00 60.40 C ANISOU 521 CG1 VAL A 140 7931 7328 7690 -162 -592 646 C ATOM 522 CG2 VAL A 140 38.854 13.947 63.927 1.00 55.62 C ANISOU 522 CG2 VAL A 140 7384 6816 6935 -228 -794 718 C ATOM 523 N SER A 141 34.239 14.778 63.893 1.00 50.13 N ANISOU 523 N SER A 141 6830 6235 5980 -208 -445 442 N ATOM 524 CA SER A 141 32.852 14.753 63.438 1.00 46.86 C ANISOU 524 CA SER A 141 6418 5819 5568 -190 -325 380 C ATOM 525 C SER A 141 32.401 16.133 62.975 1.00 42.03 C ANISOU 525 C SER A 141 5815 5199 4954 -174 -297 242 C ATOM 526 O SER A 141 31.615 16.250 62.029 1.00 43.69 O ANISOU 526 O SER A 141 5993 5370 5237 -148 -223 192 O ATOM 527 CB SER A 141 31.933 14.239 64.546 1.00 46.01 C ANISOU 527 CB SER A 141 6364 5790 5328 -215 -271 415 C ATOM 528 OG SER A 141 31.980 12.824 64.629 1.00 57.60 O ANISOU 528 OG SER A 141 7802 7241 6844 -220 -262 545 O ATOM 529 N LEU A 142 32.864 17.191 63.645 1.00 40.52 N ANISOU 529 N LEU A 142 5667 5044 4684 -193 -360 180 N ATOM 530 CA LEU A 142 32.626 18.536 63.135 1.00 32.56 C ANISOU 530 CA LEU A 142 4654 4009 3708 -176 -347 56 C ATOM 531 C LEU A 142 33.213 18.686 61.738 1.00 36.92 C ANISOU 531 C LEU A 142 5131 4476 4419 -146 -363 64 C ATOM 532 O LEU A 142 32.572 19.249 60.841 1.00 33.21 O ANISOU 532 O LEU A 142 4634 3970 4015 -121 -306 -1 O ATOM 533 CB LEU A 142 33.220 19.576 64.088 1.00 39.96 C ANISOU 533 CB LEU A 142 5644 4987 4553 -204 -428 -9 C ATOM 534 CG LEU A 142 33.239 21.033 63.609 1.00 38.79 C ANISOU 534 CG LEU A 142 5482 4795 4462 -191 -438 -129 C ATOM 535 CD1 LEU A 142 31.834 21.545 63.360 1.00 37.53 C ANISOU 535 CD1 LEU A 142 5328 4634 4297 -170 -324 -221 C ATOM 536 CD2 LEU A 142 33.956 21.932 64.611 1.00 37.69 C ANISOU 536 CD2 LEU A 142 5393 4688 4237 -224 -533 -191 C ATOM 537 N LEU A 143 34.422 18.158 61.529 1.00 34.06 N ANISOU 537 N LEU A 143 4734 4083 4123 -148 -438 149 N ATOM 538 CA LEU A 143 35.046 18.222 60.212 1.00 28.45 C ANISOU 538 CA LEU A 143 3952 3298 3558 -119 -443 162 C ATOM 539 C LEU A 143 34.248 17.436 59.181 1.00 31.28 C ANISOU 539 C LEU A 143 4276 3625 3984 -91 -350 175 C ATOM 540 O LEU A 143 34.090 17.881 58.039 1.00 33.17 O ANISOU 540 O LEU A 143 4477 3824 4302 -66 -316 134 O ATOM 541 CB LEU A 143 36.476 17.688 60.284 1.00 37.91 C ANISOU 541 CB LEU A 143 5115 4470 4820 -126 -531 258 C ATOM 542 CG LEU A 143 37.405 18.346 61.301 1.00 44.93 C ANISOU 542 CG LEU A 143 6031 5387 5653 -159 -645 259 C ATOM 543 CD1 LEU A 143 38.737 17.624 61.334 1.00 43.26 C ANISOU 543 CD1 LEU A 143 5772 5144 5522 -164 -728 373 C ATOM 544 CD2 LEU A 143 37.594 19.805 60.957 1.00 37.92 C ANISOU 544 CD2 LEU A 143 5135 4474 4798 -155 -670 163 C ATOM 545 N THR A 144 33.739 16.261 59.563 1.00 29.33 N ANISOU 545 N THR A 144 4041 3397 3707 -99 -311 234 N ATOM 546 CA THR A 144 33.015 15.432 58.604 1.00 35.32 C ANISOU 546 CA THR A 144 4764 4120 4537 -77 -232 243 C ATOM 547 C THR A 144 31.706 16.090 58.181 1.00 31.69 C ANISOU 547 C THR A 144 4313 3670 4058 -67 -158 153 C ATOM 548 O THR A 144 31.334 16.039 57.003 1.00 30.57 O ANISOU 548 O THR A 144 4132 3490 3992 -45 -118 127 O ATOM 549 CB THR A 144 32.750 14.042 59.188 1.00 34.25 C ANISOU 549 CB THR A 144 4634 3994 4387 -91 -211 330 C ATOM 550 OG1 THR A 144 32.014 14.161 60.411 1.00 46.77 O ANISOU 550 OG1 THR A 144 6277 5650 5845 -117 -194 327 O ATOM 551 CG2 THR A 144 34.061 13.299 59.441 1.00 34.83 C ANISOU 551 CG2 THR A 144 4680 4041 4512 -96 -284 431 C ATOM 552 N VAL A 145 30.988 16.711 59.121 1.00 30.85 N ANISOU 552 N VAL A 145 4255 3616 3850 -83 -140 104 N ATOM 553 CA VAL A 145 29.751 17.393 58.749 1.00 32.10 C ANISOU 553 CA VAL A 145 4412 3777 4007 -71 -70 21 C ATOM 554 C VAL A 145 30.055 18.608 57.880 1.00 27.47 C ANISOU 554 C VAL A 145 3798 3156 3485 -52 -94 -43 C ATOM 555 O VAL A 145 29.358 18.872 56.893 1.00 29.25 O ANISOU 555 O VAL A 145 3989 3354 3772 -32 -50 -77 O ATOM 556 CB VAL A 145 28.944 17.781 60.000 1.00 36.10 C ANISOU 556 CB VAL A 145 4975 4346 4395 -90 -33 -20 C ATOM 557 CG1 VAL A 145 27.724 18.602 59.606 1.00 33.70 C ANISOU 557 CG1 VAL A 145 4659 4034 4112 -73 39 -108 C ATOM 558 CG2 VAL A 145 28.522 16.536 60.764 1.00 40.03 C ANISOU 558 CG2 VAL A 145 5494 4881 4836 -108 3 58 C ATOM 559 N GLY A 146 31.084 19.375 58.235 1.00 27.11 N ANISOU 559 N GLY A 146 3763 3108 3429 -59 -167 -54 N ATOM 560 CA GLY A 146 31.503 20.463 57.367 1.00 34.45 C ANISOU 560 CA GLY A 146 4656 3996 4438 -42 -194 -96 C ATOM 561 C GLY A 146 31.913 19.964 55.997 1.00 36.04 C ANISOU 561 C GLY A 146 4801 4154 4739 -20 -187 -49 C ATOM 562 O GLY A 146 31.619 20.595 54.978 1.00 27.21 O ANISOU 562 O GLY A 146 3647 3009 3681 -1 -166 -79 O ATOM 563 N PHE A 147 32.600 18.820 55.958 1.00 31.29 N ANISOU 563 N PHE A 147 4189 3544 4156 -22 -203 26 N ATOM 564 CA PHE A 147 32.942 18.181 54.693 1.00 26.42 C ANISOU 564 CA PHE A 147 3523 2888 3626 0 -182 62 C ATOM 565 C PHE A 147 31.694 17.870 53.875 1.00 26.97 C ANISOU 565 C PHE A 147 3584 2958 3708 12 -109 29 C ATOM 566 O PHE A 147 31.664 18.106 52.661 1.00 26.70 O ANISOU 566 O PHE A 147 3514 2902 3727 30 -91 15 O ATOM 567 CB PHE A 147 33.741 16.908 54.988 1.00 33.64 C ANISOU 567 CB PHE A 147 4430 3789 4562 -5 -202 142 C ATOM 568 CG PHE A 147 34.282 16.223 53.773 1.00 36.71 C ANISOU 568 CG PHE A 147 4770 4134 5045 18 -180 172 C ATOM 569 CD1 PHE A 147 35.535 16.550 53.283 1.00 36.71 C ANISOU 569 CD1 PHE A 147 4732 4104 5113 30 -217 200 C ATOM 570 CD2 PHE A 147 33.553 15.232 53.136 1.00 34.51 C ANISOU 570 CD2 PHE A 147 4481 3841 4789 26 -118 169 C ATOM 571 CE1 PHE A 147 36.044 15.915 52.167 1.00 52.18 C ANISOU 571 CE1 PHE A 147 6646 6025 7153 53 -183 221 C ATOM 572 CE2 PHE A 147 34.057 14.594 52.015 1.00 41.01 C ANISOU 572 CE2 PHE A 147 5265 4626 5692 47 -93 181 C ATOM 573 CZ PHE A 147 35.305 14.935 51.532 1.00 40.22 C ANISOU 573 CZ PHE A 147 5129 4500 5650 62 -120 206 C ATOM 574 N LEU A 148 30.644 17.359 54.525 1.00 29.06 N ANISOU 574 N LEU A 148 3875 3247 3920 -1 -68 20 N ATOM 575 CA LEU A 148 29.442 16.967 53.794 1.00 26.80 C ANISOU 575 CA LEU A 148 3572 2955 3655 6 -6 -5 C ATOM 576 C LEU A 148 28.668 18.182 53.307 1.00 26.96 C ANISOU 576 C LEU A 148 3580 2979 3682 16 11 -69 C ATOM 577 O LEU A 148 28.093 18.159 52.213 1.00 28.46 O ANISOU 577 O LEU A 148 3740 3156 3916 27 35 -85 O ATOM 578 CB LEU A 148 28.565 16.083 54.678 1.00 27.74 C ANISOU 578 CB LEU A 148 3714 3096 3729 -11 35 14 C ATOM 579 CG LEU A 148 29.100 14.657 54.820 1.00 30.94 C ANISOU 579 CG LEU A 148 4113 3482 4162 -18 30 88 C ATOM 580 CD1 LEU A 148 28.425 13.920 55.956 1.00 25.43 C ANISOU 580 CD1 LEU A 148 3441 2811 3411 -40 60 126 C ATOM 581 CD2 LEU A 148 28.912 13.907 53.515 1.00 33.21 C ANISOU 581 CD2 LEU A 148 4360 3726 4531 -4 57 82 C ATOM 582 N VAL A 149 28.629 19.246 54.109 1.00 27.33 N ANISOU 582 N VAL A 149 3650 3043 3691 10 -5 -107 N ATOM 583 CA VAL A 149 27.989 20.485 53.673 1.00 28.32 C ANISOU 583 CA VAL A 149 3755 3159 3845 22 7 -165 C ATOM 584 C VAL A 149 28.626 20.982 52.379 1.00 24.61 C ANISOU 584 C VAL A 149 3243 2660 3446 39 -22 -151 C ATOM 585 O VAL A 149 27.934 21.317 51.408 1.00 26.86 O ANISOU 585 O VAL A 149 3495 2937 3772 50 -2 -164 O ATOM 586 CB VAL A 149 28.070 21.537 54.796 1.00 29.34 C ANISOU 586 CB VAL A 149 3917 3301 3929 13 -11 -216 C ATOM 587 CG1 VAL A 149 27.686 22.918 54.291 1.00 29.47 C ANISOU 587 CG1 VAL A 149 3903 3290 4006 27 -10 -270 C ATOM 588 CG2 VAL A 149 27.175 21.128 55.965 1.00 26.08 C ANISOU 588 CG2 VAL A 149 3545 2927 3436 -2 40 -237 C ATOM 589 N ALA A 150 29.958 21.024 52.342 1.00 28.40 N ANISOU 589 N ALA A 150 3721 3128 3942 39 -71 -117 N ATOM 590 CA ALA A 150 30.653 21.488 51.145 1.00 29.94 C ANISOU 590 CA ALA A 150 3873 3299 4202 55 -91 -94 C ATOM 591 C ALA A 150 30.420 20.557 49.961 1.00 31.03 C ANISOU 591 C ALA A 150 3991 3439 4360 66 -56 -70 C ATOM 592 O ALA A 150 30.251 21.017 48.826 1.00 29.74 O ANISOU 592 O ALA A 150 3796 3274 4228 77 -48 -69 O ATOM 593 CB ALA A 150 32.148 21.616 51.427 1.00 28.35 C ANISOU 593 CB ALA A 150 3667 3082 4023 53 -146 -57 C ATOM 594 N SER A 151 30.433 19.243 50.198 1.00 29.96 N ANISOU 594 N SER A 151 3872 3308 4206 60 -37 -49 N ATOM 595 CA SER A 151 30.254 18.298 49.099 1.00 29.93 C ANISOU 595 CA SER A 151 3850 3299 4224 67 -5 -40 C ATOM 596 C SER A 151 28.853 18.387 48.505 1.00 30.78 C ANISOU 596 C SER A 151 3950 3420 4325 65 26 -77 C ATOM 597 O SER A 151 28.693 18.386 47.279 1.00 25.48 O ANISOU 597 O SER A 151 3257 2754 3669 73 34 -82 O ATOM 598 CB SER A 151 30.530 16.873 49.577 1.00 37.32 C ANISOU 598 CB SER A 151 4799 4222 5160 60 7 -12 C ATOM 599 OG SER A 151 31.847 16.752 50.076 1.00 37.98 O ANISOU 599 OG SER A 151 4881 4290 5261 62 -28 32 O ATOM 600 N PHE A 152 27.822 18.448 49.350 1.00 26.98 N ANISOU 600 N PHE A 152 3483 2948 3819 53 43 -101 N ATOM 601 CA PHE A 152 26.470 18.543 48.814 1.00 30.22 C ANISOU 601 CA PHE A 152 3876 3366 4240 50 69 -130 C ATOM 602 C PHE A 152 26.208 19.919 48.218 1.00 33.87 C ANISOU 602 C PHE A 152 4311 3831 4726 61 52 -144 C ATOM 603 O PHE A 152 25.503 20.028 47.210 1.00 30.36 O ANISOU 603 O PHE A 152 3840 3393 4302 62 54 -149 O ATOM 604 CB PHE A 152 25.452 18.194 49.898 1.00 26.76 C ANISOU 604 CB PHE A 152 3453 2934 3780 36 103 -144 C ATOM 605 CG PHE A 152 25.310 16.710 50.124 1.00 33.98 C ANISOU 605 CG PHE A 152 4377 3841 4693 24 126 -122 C ATOM 606 CD1 PHE A 152 24.912 15.875 49.090 1.00 39.43 C ANISOU 606 CD1 PHE A 152 5045 4518 5417 21 134 -127 C ATOM 607 CD2 PHE A 152 25.578 16.150 51.361 1.00 35.01 C ANISOU 607 CD2 PHE A 152 4537 3976 4788 13 135 -94 C ATOM 608 CE1 PHE A 152 24.782 14.511 49.286 1.00 36.12 C ANISOU 608 CE1 PHE A 152 4629 4080 5017 9 154 -109 C ATOM 609 CE2 PHE A 152 25.447 14.785 51.563 1.00 35.18 C ANISOU 609 CE2 PHE A 152 4559 3983 4825 1 155 -61 C ATOM 610 CZ PHE A 152 25.051 13.968 50.523 1.00 49.23 C ANISOU 610 CZ PHE A 152 6312 5738 6657 0 166 -71 C ATOM 611 N ALA A 153 26.781 20.976 48.800 1.00 20.57 N ANISOU 611 N ALA A 153 2631 2138 3045 66 29 -148 N ATOM 612 CA ALA A 153 26.706 22.279 48.151 1.00 29.80 C ANISOU 612 CA ALA A 153 3765 3298 4258 77 9 -151 C ATOM 613 C ALA A 153 27.313 22.218 46.755 1.00 29.10 C ANISOU 613 C ALA A 153 3653 3217 4186 86 -7 -112 C ATOM 614 O ALA A 153 26.731 22.732 45.794 1.00 26.46 O ANISOU 614 O ALA A 153 3287 2892 3875 90 -12 -103 O ATOM 615 CB ALA A 153 27.408 23.341 48.997 1.00 27.22 C ANISOU 615 CB ALA A 153 3446 2952 3944 79 -19 -164 C ATOM 616 N ALA A 154 28.473 21.568 46.622 1.00 25.86 N ANISOU 616 N ALA A 154 3255 2806 3763 89 -13 -86 N ATOM 617 CA ALA A 154 29.134 21.487 45.326 1.00 27.72 C ANISOU 617 CA ALA A 154 3470 3054 4008 99 -14 -52 C ATOM 618 C ALA A 154 28.329 20.654 44.339 1.00 34.88 C ANISOU 618 C ALA A 154 4377 3987 4889 94 8 -66 C ATOM 619 O ALA A 154 28.352 20.930 43.135 1.00 27.24 O ANISOU 619 O ALA A 154 3390 3043 3915 99 6 -48 O ATOM 620 CB ALA A 154 30.538 20.903 45.493 1.00 26.53 C ANISOU 620 CB ALA A 154 3327 2890 3862 104 -16 -25 C ATOM 621 N SER A 155 27.625 19.630 44.826 1.00 28.08 N ANISOU 621 N SER A 155 3536 3122 4012 82 28 -95 N ATOM 622 CA SER A 155 26.808 18.799 43.949 1.00 32.76 C ANISOU 622 CA SER A 155 4127 3732 4589 73 42 -117 C ATOM 623 C SER A 155 25.599 19.570 43.434 1.00 26.39 C ANISOU 623 C SER A 155 3294 2943 3791 67 26 -123 C ATOM 624 O SER A 155 25.291 19.541 42.236 1.00 25.60 O ANISOU 624 O SER A 155 3181 2871 3673 63 13 -121 O ATOM 625 CB SER A 155 26.358 17.546 44.698 1.00 29.82 C ANISOU 625 CB SER A 155 3774 3340 4217 60 65 -139 C ATOM 626 OG SER A 155 25.534 16.741 43.881 1.00 40.03 O ANISOU 626 OG SER A 155 5062 4641 5508 47 72 -168 O ATOM 627 N VAL A 156 24.892 20.254 44.333 1.00 24.80 N ANISOU 627 N VAL A 156 3082 2725 3614 65 25 -131 N ATOM 628 CA VAL A 156 23.715 21.012 43.925 1.00 37.41 C ANISOU 628 CA VAL A 156 4643 4329 5242 62 12 -132 C ATOM 629 C VAL A 156 24.112 22.162 43.011 1.00 29.07 C ANISOU 629 C VAL A 156 3558 3285 4201 73 -20 -93 C ATOM 630 O VAL A 156 23.420 22.463 42.031 1.00 25.86 O ANISOU 630 O VAL A 156 3122 2901 3801 67 -43 -75 O ATOM 631 CB VAL A 156 22.949 21.510 45.162 1.00 30.09 C ANISOU 631 CB VAL A 156 3710 3377 4348 62 32 -156 C ATOM 632 CG1 VAL A 156 21.869 22.492 44.749 1.00 37.61 C ANISOU 632 CG1 VAL A 156 4612 4324 5356 64 18 -150 C ATOM 633 CG2 VAL A 156 22.340 20.339 45.898 1.00 34.00 C ANISOU 633 CG2 VAL A 156 4223 3866 4828 48 67 -180 C ATOM 634 N SER A 157 25.223 22.832 43.316 1.00 24.09 N ANISOU 634 N SER A 157 2931 2640 3581 86 -26 -72 N ATOM 635 CA SER A 157 25.658 23.922 42.453 1.00 27.70 C ANISOU 635 CA SER A 157 3355 3105 4064 95 -53 -23 C ATOM 636 C SER A 157 26.192 23.398 41.123 1.00 30.17 C ANISOU 636 C SER A 157 3674 3464 4325 94 -54 8 C ATOM 637 O SER A 157 26.077 24.084 40.100 1.00 29.03 O ANISOU 637 O SER A 157 3500 3347 4182 95 -76 54 O ATOM 638 CB SER A 157 26.701 24.774 43.175 1.00 26.14 C ANISOU 638 CB SER A 157 3155 2873 3905 106 -61 -11 C ATOM 639 OG SER A 157 27.841 24.015 43.536 1.00 29.21 O ANISOU 639 OG SER A 157 3576 3261 4263 108 -49 -13 O ATOM 640 N SER A 158 26.741 22.178 41.104 1.00 30.27 N ANISOU 640 N SER A 158 3722 3486 4292 92 -28 -18 N ATOM 641 CA SER A 158 27.160 21.585 39.836 1.00 28.13 C ANISOU 641 CA SER A 158 3462 3261 3967 91 -18 -8 C ATOM 642 C SER A 158 25.962 21.260 38.954 1.00 24.10 C ANISOU 642 C SER A 158 2949 2789 3421 73 -37 -25 C ATOM 643 O SER A 158 26.046 21.367 37.726 1.00 26.44 O ANISOU 643 O SER A 158 3242 3136 3668 69 -47 -1 O ATOM 644 CB SER A 158 27.979 20.317 40.074 1.00 32.04 C ANISOU 644 CB SER A 158 3990 3743 4440 94 18 -40 C ATOM 645 OG SER A 158 29.295 20.610 40.496 1.00 28.84 O ANISOU 645 OG SER A 158 3581 3314 4063 110 29 -8 O ATOM 646 N LEU A 159 24.846 20.844 39.561 1.00 28.31 N ANISOU 646 N LEU A 159 3480 3301 3975 59 -43 -63 N ATOM 647 CA LEU A 159 23.633 20.610 38.786 1.00 32.14 C ANISOU 647 CA LEU A 159 3952 3816 4444 39 -72 -76 C ATOM 648 C LEU A 159 23.127 21.905 38.178 1.00 32.47 C ANISOU 648 C LEU A 159 3949 3879 4508 40 -114 -17 C ATOM 649 O LEU A 159 22.656 21.927 37.035 1.00 27.11 O ANISOU 649 O LEU A 159 3261 3251 3787 25 -149 2 O ATOM 650 CB LEU A 159 22.553 19.991 39.669 1.00 30.90 C ANISOU 650 CB LEU A 159 3790 3624 4327 26 -65 -118 C ATOM 651 CG LEU A 159 22.749 18.528 40.055 1.00 34.68 C ANISOU 651 CG LEU A 159 4304 4083 4790 17 -33 -169 C ATOM 652 CD1 LEU A 159 21.674 18.130 41.052 1.00 44.58 C ANISOU 652 CD1 LEU A 159 5544 5300 6095 5 -21 -192 C ATOM 653 CD2 LEU A 159 22.717 17.630 38.828 1.00 41.89 C ANISOU 653 CD2 LEU A 159 5234 5031 5650 1 -45 -202 C ATOM 654 N LEU A 160 23.200 22.995 38.939 1.00 27.70 N ANISOU 654 N LEU A 160 3317 3236 3972 55 -115 11 N ATOM 655 CA LEU A 160 22.866 24.302 38.392 1.00 31.45 C ANISOU 655 CA LEU A 160 3741 3717 4490 59 -152 76 C ATOM 656 C LEU A 160 23.728 24.615 37.178 1.00 27.75 C ANISOU 656 C LEU A 160 3275 3303 3967 61 -165 136 C ATOM 657 O LEU A 160 23.216 24.994 36.118 1.00 27.20 O ANISOU 657 O LEU A 160 3180 3279 3873 50 -205 186 O ATOM 658 CB LEU A 160 23.040 25.365 39.471 1.00 30.58 C ANISOU 658 CB LEU A 160 3604 3545 4469 77 -142 83 C ATOM 659 CG LEU A 160 22.865 26.810 39.020 1.00 43.34 C ANISOU 659 CG LEU A 160 5161 5148 6159 85 -177 153 C ATOM 660 CD1 LEU A 160 21.476 27.006 38.435 1.00 40.05 C ANISOU 660 CD1 LEU A 160 4699 4744 5774 73 -215 177 C ATOM 661 CD2 LEU A 160 23.115 27.735 40.198 1.00 39.94 C ANISOU 661 CD2 LEU A 160 4711 4645 5818 102 -162 134 C ATOM 662 N ALA A 161 25.046 24.444 37.310 1.00 31.36 N ANISOU 662 N ALA A 161 3759 3757 4399 75 -130 138 N ATOM 663 CA ALA A 161 25.948 24.766 36.210 1.00 25.76 C ANISOU 663 CA ALA A 161 3048 3098 3641 79 -127 200 C ATOM 664 C ALA A 161 25.652 23.911 34.985 1.00 29.04 C ANISOU 664 C ALA A 161 3493 3591 3949 62 -132 185 C ATOM 665 O ALA A 161 25.684 24.406 33.854 1.00 30.21 O ANISOU 665 O ALA A 161 3629 3802 4048 55 -152 249 O ATOM 666 CB ALA A 161 27.399 24.581 36.652 1.00 26.41 C ANISOU 666 CB ALA A 161 3149 3156 3730 97 -83 197 C ATOM 667 N ILE A 162 25.376 22.621 35.189 1.00 32.95 N ANISOU 667 N ILE A 162 4029 4085 4406 51 -113 102 N ATOM 668 CA ILE A 162 24.999 21.756 34.074 1.00 31.98 C ANISOU 668 CA ILE A 162 3938 4030 4185 30 -123 67 C ATOM 669 C ILE A 162 23.751 22.291 33.388 1.00 34.00 C ANISOU 669 C ILE A 162 4163 4325 4431 8 -192 104 C ATOM 670 O ILE A 162 23.676 22.362 32.155 1.00 35.66 O ANISOU 670 O ILE A 162 4382 4615 4553 -8 -218 134 O ATOM 671 CB ILE A 162 24.799 20.310 34.565 1.00 38.04 C ANISOU 671 CB ILE A 162 4743 4767 4945 22 -97 -32 C ATOM 672 CG1 ILE A 162 26.159 19.659 34.801 1.00 28.66 C ANISOU 672 CG1 ILE A 162 3585 3559 3746 42 -31 -58 C ATOM 673 CG2 ILE A 162 23.979 19.502 33.562 1.00 39.91 C ANISOU 673 CG2 ILE A 162 5001 5057 5106 -8 -128 -82 C ATOM 674 CD1 ILE A 162 26.088 18.363 35.557 1.00 39.43 C ANISOU 674 CD1 ILE A 162 4974 4871 5138 39 -4 -136 C ATOM 675 N THR A 163 22.748 22.671 34.178 1.00 28.80 N ANISOU 675 N THR A 163 3466 3615 3862 4 -222 104 N ATOM 676 CA THR A 163 21.505 23.164 33.598 1.00 29.92 C ANISOU 676 CA THR A 163 3565 3783 4019 -17 -291 144 C ATOM 677 C THR A 163 21.732 24.462 32.836 1.00 34.07 C ANISOU 677 C THR A 163 4053 4346 4547 -11 -325 255 C ATOM 678 O THR A 163 21.151 24.671 31.764 1.00 32.19 O ANISOU 678 O THR A 163 3801 4175 4257 -33 -383 304 O ATOM 679 CB THR A 163 20.462 23.361 34.696 1.00 29.27 C ANISOU 679 CB THR A 163 3442 3627 4052 -15 -300 124 C ATOM 680 OG1 THR A 163 20.445 22.211 35.550 1.00 35.85 O ANISOU 680 OG1 THR A 163 4310 4421 4889 -17 -256 36 O ATOM 681 CG2 THR A 163 19.090 23.557 34.086 1.00 36.19 C ANISOU 681 CG2 THR A 163 4272 4526 4951 -41 -372 152 C ATOM 682 N VAL A 164 22.561 25.356 33.379 1.00 27.12 N ANISOU 682 N VAL A 164 3150 3422 3731 16 -294 301 N ATOM 683 CA VAL A 164 22.907 26.580 32.659 1.00 29.92 C ANISOU 683 CA VAL A 164 3463 3804 4101 22 -320 415 C ATOM 684 C VAL A 164 23.505 26.234 31.301 1.00 30.72 C ANISOU 684 C VAL A 164 3602 4009 4061 9 -318 450 C ATOM 685 O VAL A 164 23.115 26.787 30.267 1.00 29.33 O ANISOU 685 O VAL A 164 3402 3899 3843 -7 -369 535 O ATOM 686 CB VAL A 164 23.873 27.439 33.497 1.00 35.51 C ANISOU 686 CB VAL A 164 4148 4441 4904 50 -283 443 C ATOM 687 CG1 VAL A 164 24.499 28.539 32.647 1.00 32.43 C ANISOU 687 CG1 VAL A 164 3718 4081 4522 56 -297 565 C ATOM 688 CG2 VAL A 164 23.152 28.045 34.691 1.00 31.26 C ANISOU 688 CG2 VAL A 164 3566 3811 4502 60 -292 419 C ATOM 689 N ASP A 165 24.468 25.311 31.293 1.00 31.41 N ANISOU 689 N ASP A 165 3747 4113 4073 16 -255 386 N ATOM 690 CA ASP A 165 25.114 24.888 30.055 1.00 31.79 C ANISOU 690 CA ASP A 165 3838 4260 3981 8 -233 399 C ATOM 691 C ASP A 165 24.103 24.342 29.050 1.00 36.36 C ANISOU 691 C ASP A 165 4441 4923 4453 -28 -291 377 C ATOM 692 O ASP A 165 24.147 24.684 27.862 1.00 34.50 O ANISOU 692 O ASP A 165 4210 4782 4116 -43 -316 446 O ATOM 693 CB ASP A 165 26.176 23.844 30.396 1.00 30.39 C ANISOU 693 CB ASP A 165 3712 4065 3769 23 -152 313 C ATOM 694 CG ASP A 165 26.955 23.377 29.191 1.00 43.92 C ANISOU 694 CG ASP A 165 5470 5873 5346 20 -107 313 C ATOM 695 OD1 ASP A 165 27.843 24.127 28.719 1.00 30.86 O ANISOU 695 OD1 ASP A 165 3797 4250 3680 34 -76 403 O ATOM 696 OD2 ASP A 165 26.689 22.242 28.737 1.00 38.34 O ANISOU 696 OD2 ASP A 165 4814 5205 4548 4 -99 219 O ATOM 697 N ARG A 166 23.179 23.489 29.504 1.00 32.15 N ANISOU 697 N ARG A 166 3920 4356 3938 -44 -316 284 N ATOM 698 CA ARG A 166 22.187 22.939 28.585 1.00 34.71 C ANISOU 698 CA ARG A 166 4264 4754 4172 -82 -383 256 C ATOM 699 C ARG A 166 21.308 24.041 28.013 1.00 35.20 C ANISOU 699 C ARG A 166 4267 4852 4256 -99 -472 372 C ATOM 700 O ARG A 166 20.993 24.038 26.818 1.00 35.29 O ANISOU 700 O ARG A 166 4294 4965 4150 -128 -527 408 O ATOM 701 CB ARG A 166 21.353 21.870 29.295 1.00 36.72 C ANISOU 701 CB ARG A 166 4529 4949 4474 -96 -393 143 C ATOM 702 CG ARG A 166 22.197 20.653 29.667 1.00 58.22 C ANISOU 702 CG ARG A 166 7311 7645 7166 -85 -313 34 C ATOM 703 CD ARG A 166 21.540 19.716 30.669 1.00 50.77 C ANISOU 703 CD ARG A 166 6367 6619 6306 -91 -307 -56 C ATOM 704 NE ARG A 166 20.560 18.839 30.041 1.00 73.49 N ANISOU 704 NE ARG A 166 9260 9528 9134 -130 -364 -125 N ATOM 705 CZ ARG A 166 19.299 18.698 30.431 1.00 71.06 C ANISOU 705 CZ ARG A 166 8914 9183 8904 -153 -420 -137 C ATOM 706 NH1 ARG A 166 18.824 19.333 31.491 1.00 83.65 N ANISOU 706 NH1 ARG A 166 10453 10705 10625 -137 -417 -93 N ATOM 707 NH2 ARG A 166 18.496 17.894 29.743 1.00 84.70 N ANISOU 707 NH2 ARG A 166 10655 10943 10583 -193 -478 -200 N ATOM 708 N TYR A 167 20.920 25.008 28.846 1.00 33.49 N ANISOU 708 N TYR A 167 3981 4555 4190 -82 -489 432 N ATOM 709 CA TYR A 167 20.182 26.163 28.346 1.00 32.21 C ANISOU 709 CA TYR A 167 3749 4411 4078 -92 -568 556 C ATOM 710 C TYR A 167 20.965 26.888 27.256 1.00 31.66 C ANISOU 710 C TYR A 167 3682 4430 3918 -92 -571 672 C ATOM 711 O TYR A 167 20.428 27.172 26.180 1.00 32.94 O ANISOU 711 O TYR A 167 3832 4680 4003 -120 -645 750 O ATOM 712 CB TYR A 167 19.855 27.108 29.504 1.00 31.83 C ANISOU 712 CB TYR A 167 3628 4248 4220 -65 -562 590 C ATOM 713 CG TYR A 167 19.374 28.476 29.079 1.00 32.17 C ANISOU 713 CG TYR A 167 3587 4287 4348 -65 -627 731 C ATOM 714 CD1 TYR A 167 18.048 28.698 28.751 1.00 39.49 C ANISOU 714 CD1 TYR A 167 4459 5221 5325 -88 -714 773 C ATOM 715 CD2 TYR A 167 20.249 29.549 29.018 1.00 41.26 C ANISOU 715 CD2 TYR A 167 4707 5422 5547 -42 -603 828 C ATOM 716 CE1 TYR A 167 17.609 29.947 28.368 1.00 49.02 C ANISOU 716 CE1 TYR A 167 5581 6417 6627 -86 -776 911 C ATOM 717 CE2 TYR A 167 19.818 30.803 28.631 1.00 44.35 C ANISOU 717 CE2 TYR A 167 5015 5802 6034 -41 -662 964 C ATOM 718 CZ TYR A 167 18.498 30.997 28.308 1.00 47.58 C ANISOU 718 CZ TYR A 167 5370 6217 6493 -63 -748 1007 C ATOM 719 OH TYR A 167 18.065 32.246 27.924 1.00 66.14 O ANISOU 719 OH TYR A 167 7629 8547 8954 -61 -810 1152 O ATOM 720 N LEU A 168 22.239 27.198 27.511 1.00 33.15 N ANISOU 720 N LEU A 168 3882 4598 4115 -63 -492 692 N ATOM 721 CA LEU A 168 22.995 28.002 26.554 1.00 37.89 C ANISOU 721 CA LEU A 168 4472 5273 4653 -61 -486 819 C ATOM 722 C LEU A 168 23.197 27.265 25.235 1.00 36.53 C ANISOU 722 C LEU A 168 4370 5241 4270 -88 -487 805 C ATOM 723 O LEU A 168 23.135 27.878 24.164 1.00 37.78 O ANISOU 723 O LEU A 168 4515 5494 4347 -106 -529 924 O ATOM 724 CB LEU A 168 24.339 28.411 27.151 1.00 34.49 C ANISOU 724 CB LEU A 168 4034 4783 4288 -25 -400 835 C ATOM 725 CG LEU A 168 24.261 29.468 28.255 1.00 45.28 C ANISOU 725 CG LEU A 168 5326 6025 5855 -1 -408 876 C ATOM 726 CD1 LEU A 168 25.596 29.600 28.949 1.00 46.73 C ANISOU 726 CD1 LEU A 168 5515 6148 6093 29 -328 860 C ATOM 727 CD2 LEU A 168 23.822 30.820 27.710 1.00 50.28 C ANISOU 727 CD2 LEU A 168 5879 6663 6564 -6 -473 1033 C ATOM 728 N SER A 169 23.428 25.952 25.285 1.00 37.15 N ANISOU 728 N SER A 169 4522 5336 4257 -93 -440 663 N ATOM 729 CA SER A 169 23.609 25.206 24.045 1.00 38.27 C ANISOU 729 CA SER A 169 4736 5609 4197 -119 -435 627 C ATOM 730 C SER A 169 22.327 25.160 23.222 1.00 38.52 C ANISOU 730 C SER A 169 4766 5720 4151 -165 -552 649 C ATOM 731 O SER A 169 22.388 25.091 21.989 1.00 44.51 O ANISOU 731 O SER A 169 5565 6610 4736 -192 -576 685 O ATOM 732 CB SER A 169 24.098 23.790 24.351 1.00 38.05 C ANISOU 732 CB SER A 169 4780 5561 4117 -112 -359 460 C ATOM 733 OG SER A 169 23.103 23.026 25.004 1.00 45.27 O ANISOU 733 OG SER A 169 5697 6412 5094 -128 -404 355 O ATOM 734 N LEU A 170 21.162 25.200 23.875 1.00 38.58 N ANISOU 734 N LEU A 170 4726 5653 4280 -175 -626 631 N ATOM 735 CA LEU A 170 19.901 25.180 23.143 1.00 35.54 C ANISOU 735 CA LEU A 170 4327 5333 3845 -221 -747 659 C ATOM 736 C LEU A 170 19.529 26.551 22.598 1.00 36.50 C ANISOU 736 C LEU A 170 4374 5492 4003 -227 -825 846 C ATOM 737 O LEU A 170 18.944 26.642 21.513 1.00 38.26 O ANISOU 737 O LEU A 170 4603 5825 4109 -268 -916 908 O ATOM 738 CB LEU A 170 18.770 24.670 24.036 1.00 40.04 C ANISOU 738 CB LEU A 170 4863 5806 4546 -230 -793 573 C ATOM 739 CG LEU A 170 18.779 23.177 24.366 1.00 41.80 C ANISOU 739 CG LEU A 170 5153 6004 4724 -239 -751 395 C ATOM 740 CD1 LEU A 170 17.632 22.842 25.304 1.00 49.03 C ANISOU 740 CD1 LEU A 170 6019 6818 5791 -246 -793 340 C ATOM 741 CD2 LEU A 170 18.698 22.329 23.101 1.00 52.33 C ANISOU 741 CD2 LEU A 170 6562 7464 5856 -282 -790 330 C ATOM 742 N TYR A 171 19.848 27.621 23.320 1.00 38.83 N ANISOU 742 N TYR A 171 4598 5695 4461 -191 -795 938 N ATOM 743 CA TYR A 171 19.468 28.953 22.871 1.00 41.97 C ANISOU 743 CA TYR A 171 4912 6107 4927 -196 -868 1120 C ATOM 744 C TYR A 171 20.490 29.586 21.939 1.00 49.41 C ANISOU 744 C TYR A 171 5868 7146 5759 -192 -835 1247 C ATOM 745 O TYR A 171 20.162 30.570 21.268 1.00 45.91 O ANISOU 745 O TYR A 171 5366 6748 5330 -206 -907 1413 O ATOM 746 CB TYR A 171 19.218 29.857 24.082 1.00 43.72 C ANISOU 746 CB TYR A 171 5041 6175 5396 -160 -858 1156 C ATOM 747 CG TYR A 171 17.792 29.746 24.565 1.00 49.11 C ANISOU 747 CG TYR A 171 5669 6793 6197 -174 -936 1122 C ATOM 748 CD1 TYR A 171 17.404 28.717 25.413 1.00 56.23 C ANISOU 748 CD1 TYR A 171 6603 7633 7127 -173 -905 964 C ATOM 749 CD2 TYR A 171 16.821 30.642 24.138 1.00 51.11 C ANISOU 749 CD2 TYR A 171 5833 7048 6537 -190 -1040 1257 C ATOM 750 CE1 TYR A 171 16.096 28.599 25.845 1.00 53.29 C ANISOU 750 CE1 TYR A 171 6175 7203 6868 -187 -968 938 C ATOM 751 CE2 TYR A 171 15.511 30.532 24.563 1.00 59.53 C ANISOU 751 CE2 TYR A 171 6841 8053 7724 -202 -1108 1230 C ATOM 752 CZ TYR A 171 15.155 29.509 25.418 1.00 59.59 C ANISOU 752 CZ TYR A 171 6882 8002 7758 -200 -1068 1068 C ATOM 753 OH TYR A 171 13.853 29.385 25.845 1.00 52.87 O ANISOU 753 OH TYR A 171 5967 7089 7033 -212 -1127 1045 O ATOM 754 N ASN A 172 21.698 29.033 21.857 1.00 48.95 N ANISOU 754 N ASN A 172 5881 7121 5597 -176 -727 1180 N ATOM 755 CA ASN A 172 22.765 29.566 21.011 1.00 46.61 C ANISOU 755 CA ASN A 172 5597 6914 5197 -170 -674 1295 C ATOM 756 C ASN A 172 23.388 28.426 20.217 1.00 45.15 C ANISOU 756 C ASN A 172 5523 6851 4782 -184 -610 1190 C ATOM 757 O ASN A 172 24.510 27.991 20.501 1.00 50.51 O ANISOU 757 O ASN A 172 6240 7509 5442 -156 -495 1120 O ATOM 758 CB ASN A 172 23.813 30.287 21.858 1.00 38.45 C ANISOU 758 CB ASN A 172 4516 5771 4320 -124 -585 1337 C ATOM 759 CG ASN A 172 23.203 31.343 22.756 1.00 48.61 C ANISOU 759 CG ASN A 172 5700 6924 5845 -107 -638 1408 C ATOM 760 OD1 ASN A 172 22.822 32.418 22.297 1.00 53.38 O ANISOU 760 OD1 ASN A 172 6231 7539 6511 -116 -705 1569 O ATOM 761 ND2 ASN A 172 23.104 31.038 24.047 1.00 49.66 N ANISOU 761 ND2 ASN A 172 5825 6928 6114 -84 -607 1288 N ATOM 762 N PRO A 173 22.684 27.927 19.197 1.00 45.16 N ANISOU 762 N PRO A 173 5573 6979 4606 -230 -686 1173 N ATOM 763 CA PRO A 173 23.192 26.764 18.450 1.00 62.11 C ANISOU 763 CA PRO A 173 7830 9237 6532 -246 -626 1045 C ATOM 764 C PRO A 173 24.535 26.996 17.783 1.00 57.38 C ANISOU 764 C PRO A 173 7263 8723 5814 -227 -512 1109 C ATOM 765 O PRO A 173 25.186 26.019 17.390 1.00 57.77 O ANISOU 765 O PRO A 173 7398 8834 5717 -226 -425 984 O ATOM 766 CB PRO A 173 22.095 26.506 17.404 1.00 58.14 C ANISOU 766 CB PRO A 173 7358 8862 5869 -304 -754 1055 C ATOM 767 CG PRO A 173 20.890 27.231 17.896 1.00 63.58 C ANISOU 767 CG PRO A 173 7951 9471 6734 -315 -878 1143 C ATOM 768 CD PRO A 173 21.389 28.400 18.681 1.00 53.22 C ANISOU 768 CD PRO A 173 6548 8045 5626 -270 -834 1268 C ATOM 769 N LEU A 174 24.963 28.246 17.612 1.00 38.08 N ANISOU 769 N LEU A 174 4751 6284 3433 -213 -506 1299 N ATOM 770 CA LEU A 174 26.272 28.541 17.044 1.00 56.90 C ANISOU 770 CA LEU A 174 7151 8737 5730 -193 -390 1376 C ATOM 771 C LEU A 174 27.217 29.144 18.076 1.00 46.77 C ANISOU 771 C LEU A 174 5800 7311 4660 -143 -305 1416 C ATOM 772 O LEU A 174 28.260 28.556 18.369 1.00 48.53 O ANISOU 772 O LEU A 174 6057 7505 4876 -114 -185 1325 O ATOM 773 CB LEU A 174 26.121 29.474 15.836 1.00 53.14 C ANISOU 773 CB LEU A 174 6654 8404 5131 -222 -446 1581 C ATOM 774 CG LEU A 174 27.372 29.635 14.970 1.00 56.01 C ANISOU 774 CG LEU A 174 7051 8884 5346 -212 -324 1660 C ATOM 775 CD1 LEU A 174 26.978 29.998 13.553 1.00 57.35 C ANISOU 775 CD1 LEU A 174 7250 9249 5293 -258 -389 1798 C ATOM 776 CD2 LEU A 174 28.311 30.684 15.541 1.00 50.79 C ANISOU 776 CD2 LEU A 174 6297 8119 4881 -171 -253 1799 C ATOM 777 N THR A 175 26.871 30.298 18.654 1.00 46.28 N ANISOU 777 N THR A 175 5638 7150 4796 -133 -367 1545 N ATOM 778 CA THR A 175 27.783 30.993 19.554 1.00 51.18 C ANISOU 778 CA THR A 175 6192 7641 5615 -91 -298 1593 C ATOM 779 C THR A 175 28.052 30.229 20.847 1.00 45.83 C ANISOU 779 C THR A 175 5530 6828 5053 -62 -247 1416 C ATOM 780 O THR A 175 28.957 30.615 21.594 1.00 43.65 O ANISOU 780 O THR A 175 5214 6454 4918 -29 -181 1431 O ATOM 781 CB THR A 175 27.236 32.387 19.875 1.00 60.92 C ANISOU 781 CB THR A 175 7314 8792 7041 -90 -385 1756 C ATOM 782 OG1 THR A 175 25.985 32.273 20.562 1.00 57.67 O ANISOU 782 OG1 THR A 175 6880 8301 6730 -99 -481 1685 O ATOM 783 CG2 THR A 175 27.039 33.186 18.590 1.00 55.98 C ANISOU 783 CG2 THR A 175 6662 8298 6308 -118 -437 1957 C ATOM 784 N TYR A 176 27.298 29.168 21.138 1.00 39.93 N ANISOU 784 N TYR A 176 4840 6074 4257 -76 -278 1256 N ATOM 785 CA TYR A 176 27.676 28.298 22.247 1.00 44.17 C ANISOU 785 CA TYR A 176 5404 6504 4876 -50 -217 1094 C ATOM 786 C TYR A 176 29.083 27.747 22.047 1.00 44.43 C ANISOU 786 C TYR A 176 5479 6563 4839 -27 -87 1050 C ATOM 787 O TYR A 176 29.841 27.588 23.011 1.00 38.17 O ANISOU 787 O TYR A 176 4669 5664 4168 5 -25 997 O ATOM 788 CB TYR A 176 26.668 27.157 22.390 1.00 41.10 C ANISOU 788 CB TYR A 176 5071 6120 4425 -74 -266 939 C ATOM 789 CG TYR A 176 27.083 26.110 23.394 1.00 36.52 C ANISOU 789 CG TYR A 176 4526 5446 3903 -51 -199 776 C ATOM 790 CD1 TYR A 176 26.897 26.312 24.755 1.00 41.46 C ANISOU 790 CD1 TYR A 176 5107 5932 4714 -31 -209 745 C ATOM 791 CD2 TYR A 176 27.667 24.923 22.982 1.00 34.95 C ANISOU 791 CD2 TYR A 176 4404 5299 3575 -51 -122 656 C ATOM 792 CE1 TYR A 176 27.283 25.357 25.675 1.00 36.44 C ANISOU 792 CE1 TYR A 176 4502 5217 4127 -13 -152 612 C ATOM 793 CE2 TYR A 176 28.055 23.964 23.890 1.00 35.68 C ANISOU 793 CE2 TYR A 176 4521 5301 3735 -30 -64 521 C ATOM 794 CZ TYR A 176 27.863 24.184 25.235 1.00 39.88 C ANISOU 794 CZ TYR A 176 5008 5701 4445 -12 -82 507 C ATOM 795 OH TYR A 176 28.253 23.224 26.138 1.00 34.82 O ANISOU 795 OH TYR A 176 4390 4976 3863 6 -29 387 O ATOM 796 N TYR A 177 29.452 27.463 20.799 1.00 40.03 N ANISOU 796 N TYR A 177 4973 6149 4086 -41 -44 1074 N ATOM 797 CA TYR A 177 30.777 26.943 20.464 1.00 46.71 C ANISOU 797 CA TYR A 177 5857 7033 4860 -18 90 1038 C ATOM 798 C TYR A 177 31.714 28.127 20.270 1.00 44.54 C ANISOU 798 C TYR A 177 5511 6756 4656 1 138 1217 C ATOM 799 O TYR A 177 31.926 28.608 19.157 1.00 41.76 O ANISOU 799 O TYR A 177 5161 6528 4176 -13 156 1338 O ATOM 800 CB TYR A 177 30.699 26.056 19.229 1.00 45.68 C ANISOU 800 CB TYR A 177 5818 7057 4481 -43 122 965 C ATOM 801 CG TYR A 177 29.783 24.876 19.437 1.00 51.38 C ANISOU 801 CG TYR A 177 6603 7767 5152 -64 71 784 C ATOM 802 CD1 TYR A 177 30.202 23.768 20.160 1.00 46.38 C ANISOU 802 CD1 TYR A 177 6001 7047 4573 -42 139 619 C ATOM 803 CD2 TYR A 177 28.490 24.881 18.937 1.00 55.19 C ANISOU 803 CD2 TYR A 177 7103 8316 5549 -108 -52 787 C ATOM 804 CE1 TYR A 177 29.364 22.692 20.364 1.00 54.85 C ANISOU 804 CE1 TYR A 177 7124 8100 5618 -62 92 462 C ATOM 805 CE2 TYR A 177 27.645 23.810 19.135 1.00 45.34 C ANISOU 805 CE2 TYR A 177 5905 7050 4271 -130 -103 625 C ATOM 806 CZ TYR A 177 28.085 22.719 19.849 1.00 50.57 C ANISOU 806 CZ TYR A 177 6599 7623 4991 -107 -28 463 C ATOM 807 OH TYR A 177 27.244 21.649 20.049 1.00 62.37 O ANISOU 807 OH TYR A 177 8135 9091 6469 -130 -77 309 O ATOM 808 N SER A 178 32.291 28.593 21.375 1.00 37.10 N ANISOU 808 N SER A 178 4504 5673 3920 31 158 1235 N ATOM 809 CA SER A 178 33.137 29.778 21.376 1.00 45.57 C ANISOU 809 CA SER A 178 5495 6714 5107 48 190 1401 C ATOM 810 C SER A 178 34.044 29.712 22.595 1.00 45.60 C ANISOU 810 C SER A 178 5460 6572 5294 82 241 1346 C ATOM 811 O SER A 178 33.837 28.906 23.504 1.00 42.00 O ANISOU 811 O SER A 178 5035 6038 4886 90 233 1199 O ATOM 812 CB SER A 178 32.301 31.061 21.393 1.00 46.46 C ANISOU 812 CB SER A 178 5533 6800 5319 31 78 1548 C ATOM 813 OG SER A 178 31.613 31.198 22.628 1.00 53.28 O ANISOU 813 OG SER A 178 6366 7526 6352 37 5 1478 O ATOM 814 N ARG A 179 35.054 30.584 22.607 1.00 45.47 N ANISOU 814 N ARG A 179 5373 6520 5383 99 290 1473 N ATOM 815 CA AARG A 179 35.955 30.635 23.753 0.50 43.25 C ANISOU 815 CA AARG A 179 5047 6102 5284 127 325 1436 C ATOM 816 CA BARG A 179 35.958 30.649 23.751 0.50 43.26 C ANISOU 816 CA BARG A 179 5048 6103 5287 127 325 1437 C ATOM 817 C ARG A 179 35.218 31.092 25.006 1.00 40.80 C ANISOU 817 C ARG A 179 4702 5660 5142 125 224 1396 C ATOM 818 O ARG A 179 35.497 30.606 26.109 1.00 44.47 O ANISOU 818 O ARG A 179 5173 6025 5698 140 230 1287 O ATOM 819 CB AARG A 179 37.141 31.558 23.454 0.50 49.39 C ANISOU 819 CB AARG A 179 5747 6867 6153 141 387 1591 C ATOM 820 CB BARG A 179 37.114 31.604 23.448 0.50 49.38 C ANISOU 820 CB BARG A 179 5744 6866 6154 140 384 1596 C ATOM 821 CG AARG A 179 38.316 30.857 22.770 0.50 60.54 C ANISOU 821 CG AARG A 179 7184 8352 7465 158 525 1581 C ATOM 822 CG BARG A 179 37.940 31.209 22.233 0.50 62.38 C ANISOU 822 CG BARG A 179 7417 8643 7641 145 503 1644 C ATOM 823 CD AARG A 179 39.540 31.765 22.621 0.50 70.31 C ANISOU 823 CD AARG A 179 8330 9558 8826 173 589 1736 C ATOM 824 CD BARG A 179 38.986 32.258 21.883 0.50 71.93 C ANISOU 824 CD BARG A 179 8537 9843 8951 154 558 1826 C ATOM 825 NE AARG A 179 39.417 32.705 21.510 0.50 72.68 N ANISOU 825 NE AARG A 179 8597 9958 9060 156 590 1919 N ATOM 826 NE BARG A 179 39.868 32.558 23.005 0.50 69.42 N ANISOU 826 NE BARG A 179 8148 9372 8855 176 567 1818 N ATOM 827 CZ AARG A 179 39.981 32.557 20.317 0.50 53.08 C ANISOU 827 CZ AARG A 179 6133 7610 6424 156 694 1995 C ATOM 828 CZ BARG A 179 40.919 31.827 23.354 0.50 68.47 C ANISOU 828 CZ BARG A 179 8031 9214 8770 201 656 1744 C ATOM 829 NH1AARG A 179 40.729 31.505 20.025 0.50 56.05 N ANISOU 829 NH1AARG A 179 6560 8036 6700 175 814 1895 N ATOM 830 NH1BARG A 179 41.243 30.724 22.699 0.50 64.05 N ANISOU 830 NH1BARG A 179 7539 8748 8048 211 757 1661 N ATOM 831 NH2AARG A 179 39.793 33.493 19.392 0.50 50.70 N ANISOU 831 NH2AARG A 179 5797 7397 6072 137 680 2177 N ATOM 832 NH2BARG A 179 41.662 32.212 24.387 0.50 61.70 N ANISOU 832 NH2BARG A 179 7103 8218 8122 215 642 1751 N ATOM 833 N ARG A 180 34.266 32.012 24.853 1.00 42.64 N ANISOU 833 N ARG A 180 4897 5892 5414 107 134 1484 N ATOM 834 CA ARG A 180 33.530 32.534 25.998 1.00 41.70 C ANISOU 834 CA ARG A 180 4739 5648 5457 108 48 1448 C ATOM 835 C ARG A 180 32.843 31.420 26.779 1.00 51.95 C ANISOU 835 C ARG A 180 6103 6916 6719 107 28 1269 C ATOM 836 O ARG A 180 32.775 31.468 28.013 1.00 44.57 O ANISOU 836 O ARG A 180 5153 5867 5914 117 4 1196 O ATOM 837 CB ARG A 180 32.509 33.563 25.518 1.00 38.11 C ANISOU 837 CB ARG A 180 4235 5212 5034 88 -41 1569 C ATOM 838 CG ARG A 180 31.873 34.377 26.630 1.00 65.72 C ANISOU 838 CG ARG A 180 7670 8569 8730 93 -116 1557 C ATOM 839 CD ARG A 180 30.596 35.061 26.161 1.00 81.08 C ANISOU 839 CD ARG A 180 9579 10538 10691 74 -207 1641 C ATOM 840 NE ARG A 180 29.920 35.746 27.257 1.00 98.29 N ANISOU 840 NE ARG A 180 11704 12581 13062 82 -268 1608 N ATOM 841 CZ ARG A 180 28.700 36.259 27.186 1.00104.82 C ANISOU 841 CZ ARG A 180 12492 13392 13944 71 -347 1646 C ATOM 842 NH1 ARG A 180 27.980 36.183 26.078 1.00117.33 N ANISOU 842 NH1 ARG A 180 14085 15088 15407 48 -391 1726 N ATOM 843 NH2 ARG A 180 28.186 36.861 28.255 1.00111.33 N ANISOU 843 NH2 ARG A 180 13266 14085 14951 82 -384 1600 N ATOM 844 N THR A 181 32.319 30.408 26.083 1.00 39.21 N ANISOU 844 N THR A 181 4564 5403 4929 92 37 1197 N ATOM 845 CA THR A 181 31.625 29.338 26.791 1.00 40.72 C ANISOU 845 CA THR A 181 4812 5563 5098 89 17 1036 C ATOM 846 C THR A 181 32.585 28.560 27.678 1.00 36.86 C ANISOU 846 C THR A 181 4344 5002 4659 112 85 934 C ATOM 847 O THR A 181 32.239 28.197 28.807 1.00 33.74 O ANISOU 847 O THR A 181 3956 4520 4342 117 59 840 O ATOM 848 CB THR A 181 30.929 28.397 25.808 1.00 37.23 C ANISOU 848 CB THR A 181 4442 5240 4464 65 10 976 C ATOM 849 OG1 THR A 181 29.904 29.107 25.106 1.00 36.25 O ANISOU 849 OG1 THR A 181 4294 5175 4303 40 -74 1070 O ATOM 850 CG2 THR A 181 30.309 27.218 26.557 1.00 35.94 C ANISOU 850 CG2 THR A 181 4330 5032 4292 62 -2 810 C ATOM 851 N LEU A 182 33.796 28.292 27.191 1.00 38.34 N ANISOU 851 N LEU A 182 4537 5225 4805 127 174 957 N ATOM 852 CA LEU A 182 34.750 27.562 28.019 1.00 42.42 C ANISOU 852 CA LEU A 182 5063 5669 5385 150 234 873 C ATOM 853 C LEU A 182 35.226 28.419 29.186 1.00 31.96 C ANISOU 853 C LEU A 182 3673 4222 4248 162 203 912 C ATOM 854 O LEU A 182 35.324 27.939 30.321 1.00 32.12 O ANISOU 854 O LEU A 182 3704 4159 4341 170 192 823 O ATOM 855 CB LEU A 182 35.935 27.091 27.179 1.00 45.57 C ANISOU 855 CB LEU A 182 5474 6132 5707 165 343 892 C ATOM 856 CG LEU A 182 36.947 26.245 27.959 1.00 48.42 C ANISOU 856 CG LEU A 182 5839 6419 6141 190 406 810 C ATOM 857 CD1 LEU A 182 36.309 24.968 28.502 1.00 48.29 C ANISOU 857 CD1 LEU A 182 5886 6379 6084 186 393 656 C ATOM 858 CD2 LEU A 182 38.152 25.918 27.095 1.00 68.70 C ANISOU 858 CD2 LEU A 182 8403 9044 8656 209 523 842 C ATOM 859 N LEU A 183 35.533 29.691 28.930 1.00 31.38 N ANISOU 859 N LEU A 183 3532 4136 4257 162 186 1046 N ATOM 860 CA LEU A 183 35.833 30.599 30.030 1.00 36.52 C ANISOU 860 CA LEU A 183 4119 4666 5091 168 141 1073 C ATOM 861 C LEU A 183 34.701 30.606 31.048 1.00 34.08 C ANISOU 861 C LEU A 183 3826 4291 4830 159 64 985 C ATOM 862 O LEU A 183 34.942 30.585 32.261 1.00 30.58 O ANISOU 862 O LEU A 183 3376 3755 4487 166 46 921 O ATOM 863 CB LEU A 183 36.073 32.008 29.491 1.00 33.44 C ANISOU 863 CB LEU A 183 3650 4271 4785 164 123 1233 C ATOM 864 CG LEU A 183 36.244 33.109 30.535 1.00 40.64 C ANISOU 864 CG LEU A 183 4491 5052 5897 166 65 1261 C ATOM 865 CD1 LEU A 183 37.410 32.796 31.464 1.00 45.87 C ANISOU 865 CD1 LEU A 183 5143 5635 6649 180 94 1208 C ATOM 866 CD2 LEU A 183 36.441 34.437 29.827 1.00 37.34 C ANISOU 866 CD2 LEU A 183 3991 4634 5563 161 51 1429 C ATOM 867 N GLY A 184 33.456 30.614 30.568 1.00 34.76 N ANISOU 867 N GLY A 184 3932 4430 4844 144 20 983 N ATOM 868 CA GLY A 184 32.320 30.719 31.468 1.00 28.41 C ANISOU 868 CA GLY A 184 3132 3565 4099 137 -46 912 C ATOM 869 C GLY A 184 32.202 29.542 32.416 1.00 36.07 C ANISOU 869 C GLY A 184 4160 4503 5042 140 -31 769 C ATOM 870 O GLY A 184 31.844 29.711 33.584 1.00 34.73 O ANISOU 870 O GLY A 184 3984 4252 4961 142 -63 710 O ATOM 871 N VAL A 185 32.479 28.331 31.927 1.00 29.90 N ANISOU 871 N VAL A 185 3435 3784 4140 140 21 711 N ATOM 872 CA AVAL A 185 32.429 27.158 32.793 0.50 30.37 C ANISOU 872 CA AVAL A 185 3544 3809 4185 144 37 587 C ATOM 873 CA BVAL A 185 32.423 27.162 32.800 0.50 30.41 C ANISOU 873 CA BVAL A 185 3550 3813 4191 143 37 587 C ATOM 874 C VAL A 185 33.541 27.218 33.833 1.00 32.06 C ANISOU 874 C VAL A 185 3740 3941 4502 160 57 576 C ATOM 875 O VAL A 185 33.337 26.879 35.005 1.00 35.75 O ANISOU 875 O VAL A 185 4223 4345 5016 160 37 503 O ATOM 876 CB AVAL A 185 32.508 25.875 31.944 0.50 33.09 C ANISOU 876 CB AVAL A 185 3948 4233 4392 141 89 528 C ATOM 877 CB BVAL A 185 32.468 25.858 31.977 0.50 33.06 C ANISOU 877 CB BVAL A 185 3946 4228 4389 140 87 525 C ATOM 878 CG1AVAL A 185 32.683 24.646 32.826 0.50 37.74 C ANISOU 878 CG1AVAL A 185 4578 4774 4989 147 115 416 C ATOM 879 CG1BVAL A 185 33.682 25.809 31.065 0.50 38.40 C ANISOU 879 CG1BVAL A 185 4616 4955 5019 153 160 581 C ATOM 880 CG2AVAL A 185 31.264 25.743 31.077 0.50 30.56 C ANISOU 880 CG2AVAL A 185 3652 3989 3970 117 49 522 C ATOM 881 CG2BVAL A 185 32.467 24.646 32.898 0.50 37.82 C ANISOU 881 CG2BVAL A 185 4590 4781 4999 144 105 409 C ATOM 882 N HIS A 186 34.733 27.656 33.424 1.00 31.97 N ANISOU 882 N HIS A 186 3692 3931 4525 172 95 653 N ATOM 883 CA HIS A 186 35.846 27.766 34.360 1.00 35.80 C ANISOU 883 CA HIS A 186 4149 4336 5117 184 104 652 C ATOM 884 C HIS A 186 35.522 28.735 35.487 1.00 31.36 C ANISOU 884 C HIS A 186 3554 3688 4673 178 34 649 C ATOM 885 O HIS A 186 35.760 28.446 36.665 1.00 28.91 O ANISOU 885 O HIS A 186 3256 3315 4412 178 15 586 O ATOM 886 CB HIS A 186 37.101 28.220 33.619 1.00 40.43 C ANISOU 886 CB HIS A 186 4687 4939 5735 196 155 752 C ATOM 887 CG HIS A 186 37.641 27.196 32.676 1.00 34.54 C ANISOU 887 CG HIS A 186 3973 4267 4883 207 240 738 C ATOM 888 ND1 HIS A 186 38.501 27.509 31.645 1.00 38.13 N ANISOU 888 ND1 HIS A 186 4395 4773 5321 216 305 829 N ATOM 889 CD2 HIS A 186 37.444 25.859 32.610 1.00 33.90 C ANISOU 889 CD2 HIS A 186 3952 4214 4713 210 277 639 C ATOM 890 CE1 HIS A 186 38.813 26.407 30.987 1.00 43.99 C ANISOU 890 CE1 HIS A 186 5180 5574 5961 226 383 778 C ATOM 891 NE2 HIS A 186 38.185 25.391 31.553 1.00 38.29 N ANISOU 891 NE2 HIS A 186 4514 4836 5200 222 364 660 N ATOM 892 N LEU A 187 35.001 29.908 35.136 1.00 28.49 N ANISOU 892 N LEU A 187 3147 3320 4357 171 -4 720 N ATOM 893 CA LEU A 187 34.696 30.908 36.146 1.00 32.55 C ANISOU 893 CA LEU A 187 3625 3746 4995 167 -63 710 C ATOM 894 C LEU A 187 33.523 30.469 37.008 1.00 37.39 C ANISOU 894 C LEU A 187 4283 4342 5582 160 -93 605 C ATOM 895 O LEU A 187 33.541 30.663 38.229 1.00 33.13 O ANISOU 895 O LEU A 187 3747 3733 5108 159 -120 544 O ATOM 896 CB LEU A 187 34.406 32.247 35.475 1.00 30.68 C ANISOU 896 CB LEU A 187 3324 3503 4832 164 -92 817 C ATOM 897 CG LEU A 187 35.534 32.835 34.622 1.00 34.81 C ANISOU 897 CG LEU A 187 3791 4040 5396 169 -62 941 C ATOM 898 CD1 LEU A 187 35.087 34.159 34.017 1.00 31.93 C ANISOU 898 CD1 LEU A 187 3358 3663 5112 163 -97 1054 C ATOM 899 CD2 LEU A 187 36.819 33.019 35.425 1.00 41.16 C ANISOU 899 CD2 LEU A 187 4564 4766 6307 174 -59 937 C ATOM 900 N LEU A 188 32.504 29.860 36.396 1.00 30.15 N ANISOU 900 N LEU A 188 3401 3490 4566 154 -87 582 N ATOM 901 CA LEU A 188 31.331 29.442 37.157 1.00 23.32 C ANISOU 901 CA LEU A 188 2568 2607 3684 147 -109 492 C ATOM 902 C LEU A 188 31.676 28.334 38.146 1.00 33.01 C ANISOU 902 C LEU A 188 3848 3815 4880 148 -87 400 C ATOM 903 O LEU A 188 31.199 28.343 39.286 1.00 29.33 O ANISOU 903 O LEU A 188 3396 3302 4448 145 -106 335 O ATOM 904 CB LEU A 188 30.223 28.989 36.206 1.00 29.04 C ANISOU 904 CB LEU A 188 3312 3406 4318 136 -113 495 C ATOM 905 CG LEU A 188 28.918 28.546 36.870 1.00 42.36 C ANISOU 905 CG LEU A 188 5022 5077 5997 128 -133 413 C ATOM 906 CD1 LEU A 188 28.396 29.624 37.807 1.00 35.92 C ANISOU 906 CD1 LEU A 188 4164 4182 5300 131 -165 405 C ATOM 907 CD2 LEU A 188 27.881 28.203 35.811 1.00 38.99 C ANISOU 907 CD2 LEU A 188 4601 4722 5492 113 -151 429 C ATOM 908 N LEU A 189 32.500 27.369 37.732 1.00 26.97 N ANISOU 908 N LEU A 189 3110 3085 4052 153 -44 396 N ATOM 909 CA LEU A 189 32.872 26.290 38.642 1.00 30.97 C ANISOU 909 CA LEU A 189 3658 3568 4542 155 -27 324 C ATOM 910 C LEU A 189 33.812 26.779 39.735 1.00 32.34 C ANISOU 910 C LEU A 189 3812 3674 4804 158 -49 327 C ATOM 911 O LEU A 189 33.696 26.359 40.890 1.00 30.21 O ANISOU 911 O LEU A 189 3570 3370 4539 153 -64 267 O ATOM 912 CB LEU A 189 33.521 25.144 37.876 1.00 24.73 C ANISOU 912 CB LEU A 189 2894 2824 3680 162 28 318 C ATOM 913 CG LEU A 189 32.592 24.272 37.039 1.00 32.46 C ANISOU 913 CG LEU A 189 3911 3866 4558 153 46 276 C ATOM 914 CD1 LEU A 189 33.385 23.106 36.466 1.00 35.88 C ANISOU 914 CD1 LEU A 189 4369 4326 4937 163 107 251 C ATOM 915 CD2 LEU A 189 31.404 23.786 37.864 1.00 32.01 C ANISOU 915 CD2 LEU A 189 3882 3787 4494 140 19 204 C ATOM 916 N ALA A 190 34.768 27.643 39.394 1.00 30.23 N ANISOU 916 N ALA A 190 3495 3387 4604 165 -53 400 N ATOM 917 CA ALA A 190 35.602 28.235 40.434 1.00 30.03 C ANISOU 917 CA ALA A 190 3445 3291 4673 163 -89 402 C ATOM 918 C ALA A 190 34.743 28.941 41.476 1.00 28.06 C ANISOU 918 C ALA A 190 3202 2997 4464 152 -138 346 C ATOM 919 O ALA A 190 35.009 28.850 42.680 1.00 29.45 O ANISOU 919 O ALA A 190 3397 3132 4660 145 -166 294 O ATOM 920 CB ALA A 190 36.611 29.203 39.815 1.00 31.77 C ANISOU 920 CB ALA A 190 3599 3492 4979 168 -89 496 C ATOM 921 N ALA A 191 33.682 29.620 41.036 1.00 27.98 N ANISOU 921 N ALA A 191 3175 2994 4461 151 -147 356 N ATOM 922 CA ALA A 191 32.831 30.339 41.978 1.00 28.59 C ANISOU 922 CA ALA A 191 3250 3023 4588 145 -181 299 C ATOM 923 C ALA A 191 31.955 29.389 42.784 1.00 32.17 C ANISOU 923 C ALA A 191 3763 3493 4965 139 -167 210 C ATOM 924 O ALA A 191 31.811 29.557 44.000 1.00 32.81 O ANISOU 924 O ALA A 191 3865 3537 5064 133 -185 145 O ATOM 925 CB ALA A 191 31.958 31.354 41.243 1.00 28.72 C ANISOU 925 CB ALA A 191 3220 3035 4658 147 -193 345 C ATOM 926 N THR A 192 31.350 28.391 42.137 1.00 26.07 N ANISOU 926 N THR A 192 3020 2779 4108 139 -136 205 N ATOM 927 CA THR A 192 30.475 27.496 42.885 1.00 36.95 C ANISOU 927 CA THR A 192 4445 4168 5427 133 -122 130 C ATOM 928 C THR A 192 31.269 26.662 43.877 1.00 25.10 C ANISOU 928 C THR A 192 2985 2656 3898 129 -118 95 C ATOM 929 O THR A 192 30.816 26.430 45.002 1.00 24.70 O ANISOU 929 O THR A 192 2965 2589 3829 121 -121 37 O ATOM 930 CB THR A 192 29.687 26.577 41.953 1.00 34.11 C ANISOU 930 CB THR A 192 4102 3865 4993 130 -97 130 C ATOM 931 OG1 THR A 192 30.588 25.798 41.159 1.00 32.73 O ANISOU 931 OG1 THR A 192 3939 3725 4771 134 -72 160 O ATOM 932 CG2 THR A 192 28.776 27.382 41.066 1.00 32.50 C ANISOU 932 CG2 THR A 192 3858 3676 4813 129 -113 169 C ATOM 933 N TRP A 193 32.454 26.197 43.483 1.00 26.90 N ANISOU 933 N TRP A 193 3209 2891 4121 134 -109 134 N ATOM 934 CA TRP A 193 33.250 25.410 44.414 1.00 21.56 C ANISOU 934 CA TRP A 193 2561 2198 3431 130 -114 114 C ATOM 935 C TRP A 193 33.824 26.281 45.524 1.00 30.25 C ANISOU 935 C TRP A 193 3654 3252 4588 122 -162 102 C ATOM 936 O TRP A 193 33.914 25.837 46.672 1.00 27.67 O ANISOU 936 O TRP A 193 3363 2916 4234 112 -179 63 O ATOM 937 CB TRP A 193 34.360 24.671 43.676 1.00 24.25 C ANISOU 937 CB TRP A 193 2891 2553 3770 141 -87 160 C ATOM 938 CG TRP A 193 33.906 23.389 43.036 1.00 26.03 C ANISOU 938 CG TRP A 193 3145 2817 3928 144 -41 139 C ATOM 939 CD1 TRP A 193 33.403 23.235 41.775 1.00 28.83 C ANISOU 939 CD1 TRP A 193 3496 3216 4242 148 -10 148 C ATOM 940 CD2 TRP A 193 33.921 22.082 43.623 1.00 27.40 C ANISOU 940 CD2 TRP A 193 3353 2987 4071 141 -25 106 C ATOM 941 NE1 TRP A 193 33.101 21.915 41.545 1.00 25.97 N ANISOU 941 NE1 TRP A 193 3166 2873 3828 147 24 109 N ATOM 942 CE2 TRP A 193 33.406 21.188 42.665 1.00 32.25 C ANISOU 942 CE2 TRP A 193 3981 3634 4637 144 18 87 C ATOM 943 CE3 TRP A 193 34.316 21.582 44.868 1.00 29.82 C ANISOU 943 CE3 TRP A 193 3680 3265 4387 133 -46 95 C ATOM 944 CZ2 TRP A 193 33.287 19.823 42.908 1.00 29.31 C ANISOU 944 CZ2 TRP A 193 3636 3256 4244 141 43 54 C ATOM 945 CZ3 TRP A 193 34.192 20.226 45.108 1.00 23.67 C ANISOU 945 CZ3 TRP A 193 2926 2486 3583 131 -21 77 C ATOM 946 CH2 TRP A 193 33.684 19.363 44.133 1.00 25.97 C ANISOU 946 CH2 TRP A 193 3225 2799 3843 136 24 55 C ATOM 947 N THR A 194 34.192 27.528 45.214 1.00 25.41 N ANISOU 947 N THR A 194 2994 2608 4053 125 -188 135 N ATOM 948 CA THR A 194 34.670 28.427 46.262 1.00 33.21 C ANISOU 948 CA THR A 194 3973 3545 5101 114 -241 109 C ATOM 949 C THR A 194 33.579 28.686 47.292 1.00 30.51 C ANISOU 949 C THR A 194 3668 3194 4729 104 -247 25 C ATOM 950 O THR A 194 33.840 28.692 48.501 1.00 27.32 O ANISOU 950 O THR A 194 3296 2775 4308 90 -278 -25 O ATOM 951 CB THR A 194 35.151 29.748 45.659 1.00 31.20 C ANISOU 951 CB THR A 194 3653 3248 4953 118 -265 161 C ATOM 952 OG1 THR A 194 36.242 29.502 44.767 1.00 33.52 O ANISOU 952 OG1 THR A 194 3911 3552 5274 126 -250 243 O ATOM 953 CG2 THR A 194 35.615 30.701 46.753 1.00 37.13 C ANISOU 953 CG2 THR A 194 4394 3937 5776 103 -325 120 C ATOM 954 N VAL A 195 32.346 28.896 46.829 1.00 27.08 N ANISOU 954 N VAL A 195 3228 2774 4288 111 -217 10 N ATOM 955 CA VAL A 195 31.244 29.165 47.742 1.00 28.91 C ANISOU 955 CA VAL A 195 3485 2995 4502 106 -208 -69 C ATOM 956 C VAL A 195 30.871 27.907 48.511 1.00 30.46 C ANISOU 956 C VAL A 195 3743 3232 4598 98 -182 -108 C ATOM 957 O VAL A 195 30.606 27.955 49.718 1.00 27.63 O ANISOU 957 O VAL A 195 3422 2870 4206 87 -186 -171 O ATOM 958 CB VAL A 195 30.046 29.729 46.961 1.00 32.49 C ANISOU 958 CB VAL A 195 3902 3447 4995 117 -185 -61 C ATOM 959 CG1 VAL A 195 28.798 29.745 47.834 1.00 35.83 C ANISOU 959 CG1 VAL A 195 4349 3867 5397 115 -158 -139 C ATOM 960 CG2 VAL A 195 30.376 31.120 46.431 1.00 30.67 C ANISOU 960 CG2 VAL A 195 3608 3166 4881 124 -216 -21 C ATOM 961 N SER A 196 30.851 26.763 47.826 1.00 26.29 N ANISOU 961 N SER A 196 3225 2743 4020 101 -154 -71 N ATOM 962 CA SER A 196 30.539 25.499 48.483 1.00 25.78 C ANISOU 962 CA SER A 196 3210 2709 3877 93 -130 -95 C ATOM 963 C SER A 196 31.502 25.225 49.630 1.00 28.78 C ANISOU 963 C SER A 196 3622 3081 4231 80 -163 -103 C ATOM 964 O SER A 196 31.082 24.934 50.757 1.00 30.97 O ANISOU 964 O SER A 196 3942 3372 4453 68 -158 -145 O ATOM 965 CB SER A 196 30.582 24.367 47.455 1.00 27.90 C ANISOU 965 CB SER A 196 3476 3006 4119 99 -101 -56 C ATOM 966 OG SER A 196 29.534 24.507 46.509 1.00 28.14 O ANISOU 966 OG SER A 196 3485 3053 4154 104 -78 -56 O ATOM 967 N LEU A 197 32.804 25.319 49.363 1.00 30.43 N ANISOU 967 N LEU A 197 3810 3274 4480 82 -198 -56 N ATOM 968 CA LEU A 197 33.792 25.099 50.413 1.00 33.04 C ANISOU 968 CA LEU A 197 4163 3596 4796 67 -244 -53 C ATOM 969 C LEU A 197 33.597 26.080 51.561 1.00 27.87 C ANISOU 969 C LEU A 197 3531 2926 4134 51 -282 -118 C ATOM 970 O LEU A 197 33.622 25.697 52.736 1.00 26.00 O ANISOU 970 O LEU A 197 3341 2709 3829 34 -300 -147 O ATOM 971 CB LEU A 197 35.203 25.218 49.839 1.00 26.93 C ANISOU 971 CB LEU A 197 3344 2796 4091 73 -276 11 C ATOM 972 CG LEU A 197 35.843 23.898 49.406 1.00 33.73 C ANISOU 972 CG LEU A 197 4202 3670 4943 81 -253 64 C ATOM 973 CD1 LEU A 197 35.049 23.288 48.262 1.00 44.59 C ANISOU 973 CD1 LEU A 197 5575 5072 6297 97 -186 66 C ATOM 974 CD2 LEU A 197 37.306 24.092 49.031 1.00 44.14 C ANISOU 974 CD2 LEU A 197 5472 4959 6342 87 -283 125 C ATOM 975 N GLY A 198 33.414 27.359 51.238 1.00 33.07 N ANISOU 975 N GLY A 198 4154 3550 4863 57 -293 -141 N ATOM 976 CA GLY A 198 33.161 28.340 52.280 1.00 31.23 C ANISOU 976 CA GLY A 198 3940 3293 4631 44 -321 -219 C ATOM 977 C GLY A 198 31.977 27.975 53.155 1.00 36.47 C ANISOU 977 C GLY A 198 4659 3993 5206 38 -276 -287 C ATOM 978 O GLY A 198 32.022 28.143 54.376 1.00 27.39 O ANISOU 978 O GLY A 198 3555 2853 3998 20 -297 -347 O ATOM 979 N LEU A 199 30.904 27.463 52.547 1.00 29.45 N ANISOU 979 N LEU A 199 3763 3125 4301 52 -213 -278 N ATOM 980 CA LEU A 199 29.716 27.115 53.322 1.00 33.62 C ANISOU 980 CA LEU A 199 4332 3684 4759 48 -160 -334 C ATOM 981 C LEU A 199 29.997 25.986 54.305 1.00 32.20 C ANISOU 981 C LEU A 199 4211 3550 4473 30 -162 -325 C ATOM 982 O LEU A 199 29.437 25.963 55.406 1.00 28.02 O ANISOU 982 O LEU A 199 3728 3048 3870 17 -138 -380 O ATOM 983 CB LEU A 199 28.576 26.718 52.392 1.00 25.92 C ANISOU 983 CB LEU A 199 3328 2718 3803 64 -102 -313 C ATOM 984 CG LEU A 199 27.929 27.865 51.627 1.00 32.85 C ANISOU 984 CG LEU A 199 4149 3555 4776 80 -93 -326 C ATOM 985 CD1 LEU A 199 26.946 27.296 50.627 1.00 31.70 C ANISOU 985 CD1 LEU A 199 3976 3428 4641 90 -53 -290 C ATOM 986 CD2 LEU A 199 27.256 28.826 52.588 1.00 32.47 C ANISOU 986 CD2 LEU A 199 4110 3483 4746 80 -74 -415 C ATOM 987 N GLY A 200 30.834 25.022 53.916 1.00 31.98 N ANISOU 987 N GLY A 200 4180 3533 4438 28 -184 -252 N ATOM 988 CA GLY A 200 31.219 23.970 54.838 1.00 25.89 C ANISOU 988 CA GLY A 200 3455 2798 3585 10 -196 -226 C ATOM 989 C GLY A 200 32.315 24.367 55.799 1.00 34.74 C ANISOU 989 C GLY A 200 4601 3919 4679 -11 -273 -233 C ATOM 990 O GLY A 200 32.466 23.729 56.845 1.00 32.61 O ANISOU 990 O GLY A 200 4380 3689 4323 -32 -289 -224 O ATOM 991 N LEU A 201 33.073 25.416 55.471 1.00 28.31 N ANISOU 991 N LEU A 201 3753 3062 3942 -9 -324 -244 N ATOM 992 CA LEU A 201 34.158 25.866 56.332 1.00 28.39 C ANISOU 992 CA LEU A 201 3779 3065 3943 -33 -410 -254 C ATOM 993 C LEU A 201 33.650 26.700 57.496 1.00 32.80 C ANISOU 993 C LEU A 201 4388 3639 4436 -52 -420 -357 C ATOM 994 O LEU A 201 34.278 26.720 58.559 1.00 30.36 O ANISOU 994 O LEU A 201 4122 3354 4061 -80 -484 -375 O ATOM 995 CB LEU A 201 35.157 26.690 55.523 1.00 35.10 C ANISOU 995 CB LEU A 201 4564 3856 4915 -25 -460 -225 C ATOM 996 CG LEU A 201 36.608 26.683 55.986 1.00 67.70 C ANISOU 996 CG LEU A 201 8683 7970 9070 -46 -555 -184 C ATOM 997 CD1 LEU A 201 37.214 25.323 55.701 1.00 65.76 C ANISOU 997 CD1 LEU A 201 8426 7742 8816 -41 -551 -89 C ATOM 998 CD2 LEU A 201 37.374 27.798 55.291 1.00 62.15 C ANISOU 998 CD2 LEU A 201 7913 7202 8498 -41 -596 -174 C ATOM 999 N LEU A 202 32.539 27.406 57.308 1.00 34.69 N ANISOU 999 N LEU A 202 4622 3864 4695 -37 -358 -426 N ATOM 1000 CA LEU A 202 32.031 28.274 58.368 1.00 40.24 C ANISOU 1000 CA LEU A 202 5369 4573 5348 -50 -354 -538 C ATOM 1001 C LEU A 202 31.777 27.515 59.661 1.00 30.11 C ANISOU 1001 C LEU A 202 4166 3366 3908 -74 -342 -559 C ATOM 1002 O LEU A 202 32.219 27.985 60.724 1.00 31.66 O ANISOU 1002 O LEU A 202 4412 3582 4036 -102 -396 -622 O ATOM 1003 CB LEU A 202 30.769 28.986 57.873 1.00 33.94 C ANISOU 1003 CB LEU A 202 4540 3744 4611 -25 -274 -596 C ATOM 1004 CG LEU A 202 31.046 30.084 56.842 1.00 39.36 C ANISOU 1004 CG LEU A 202 5152 4352 5452 -7 -299 -590 C ATOM 1005 CD1 LEU A 202 29.755 30.522 56.166 1.00 35.12 C ANISOU 1005 CD1 LEU A 202 4573 3789 4982 20 -222 -612 C ATOM 1006 CD2 LEU A 202 31.750 31.274 57.482 1.00 40.08 C ANISOU 1006 CD2 LEU A 202 5245 4396 5587 -25 -369 -667 C ATOM 1007 N PRO A 203 31.090 26.370 59.661 1.00 32.01 N ANISOU 1007 N PRO A 203 4425 3654 4084 -69 -278 -508 N ATOM 1008 CA PRO A 203 30.919 25.640 60.928 1.00 36.79 C ANISOU 1008 CA PRO A 203 5105 4336 4538 -95 -269 -510 C ATOM 1009 C PRO A 203 32.227 25.151 61.521 1.00 30.81 C ANISOU 1009 C PRO A 203 4372 3604 3728 -124 -371 -449 C ATOM 1010 O PRO A 203 32.366 25.128 62.749 1.00 36.53 O ANISOU 1010 O PRO A 203 5164 4388 4327 -155 -401 -480 O ATOM 1011 CB PRO A 203 29.994 24.475 60.546 1.00 34.37 C ANISOU 1011 CB PRO A 203 4789 4055 4216 -81 -183 -447 C ATOM 1012 CG PRO A 203 30.054 24.383 59.059 1.00 33.27 C ANISOU 1012 CG PRO A 203 4576 3858 4208 -53 -175 -397 C ATOM 1013 CD PRO A 203 30.311 25.768 58.566 1.00 35.48 C ANISOU 1013 CD PRO A 203 4819 4081 4583 -42 -206 -456 C ATOM 1014 N VAL A 204 33.195 24.764 60.688 1.00 31.86 N ANISOU 1014 N VAL A 204 4452 3698 3955 -116 -424 -361 N ATOM 1015 CA VAL A 204 34.484 24.321 61.210 1.00 34.14 C ANISOU 1015 CA VAL A 204 4752 4002 4220 -142 -526 -294 C ATOM 1016 C VAL A 204 35.206 25.468 61.902 1.00 33.38 C ANISOU 1016 C VAL A 204 4675 3894 4114 -169 -618 -369 C ATOM 1017 O VAL A 204 35.903 25.266 62.904 1.00 29.27 O ANISOU 1017 O VAL A 204 4198 3417 3507 -204 -701 -355 O ATOM 1018 CB VAL A 204 35.337 23.722 60.078 1.00 33.34 C ANISOU 1018 CB VAL A 204 4578 3850 4241 -123 -548 -191 C ATOM 1019 CG1 VAL A 204 36.720 23.344 60.591 1.00 39.82 C ANISOU 1019 CG1 VAL A 204 5393 4673 5063 -148 -656 -118 C ATOM 1020 CG2 VAL A 204 34.632 22.517 59.478 1.00 29.71 C ANISOU 1020 CG2 VAL A 204 4105 3401 3784 -102 -463 -130 C ATOM 1021 N LEU A 205 35.051 26.687 61.386 1.00 29.81 N ANISOU 1021 N LEU A 205 4190 3383 3754 -155 -611 -448 N ATOM 1022 CA LEU A 205 35.720 27.835 61.983 1.00 32.43 C ANISOU 1022 CA LEU A 205 4532 3689 4099 -180 -700 -530 C ATOM 1023 C LEU A 205 35.007 28.339 63.227 1.00 32.86 C ANISOU 1023 C LEU A 205 4671 3796 4017 -203 -681 -654 C ATOM 1024 O LEU A 205 35.598 29.110 63.991 1.00 45.10 O ANISOU 1024 O LEU A 205 6252 5345 5541 -234 -766 -730 O ATOM 1025 CB LEU A 205 35.839 28.963 60.956 1.00 29.40 C ANISOU 1025 CB LEU A 205 4074 3213 3883 -157 -698 -560 C ATOM 1026 CG LEU A 205 36.749 28.673 59.755 1.00 38.99 C ANISOU 1026 CG LEU A 205 5204 4376 5233 -139 -726 -445 C ATOM 1027 CD1 LEU A 205 36.687 29.809 58.743 1.00 53.27 C ANISOU 1027 CD1 LEU A 205 6942 6103 7195 -116 -710 -468 C ATOM 1028 CD2 LEU A 205 38.192 28.433 60.193 1.00 43.91 C ANISOU 1028 CD2 LEU A 205 5818 4997 5869 -169 -844 -385 C ATOM 1029 N GLY A 206 33.759 27.929 63.446 1.00 43.44 N ANISOU 1029 N GLY A 206 6047 5183 5273 -189 -571 -681 N ATOM 1030 CA GLY A 206 33.095 28.207 64.704 1.00 36.87 C ANISOU 1030 CA GLY A 206 5301 4418 4289 -210 -538 -788 C ATOM 1031 C GLY A 206 31.632 28.585 64.598 1.00 38.49 C ANISOU 1031 C GLY A 206 5509 4618 4496 -182 -405 -872 C ATOM 1032 O GLY A 206 30.982 28.774 65.628 1.00 40.58 O ANISOU 1032 O GLY A 206 5845 4942 4632 -196 -355 -963 O ATOM 1033 N TRP A 207 31.087 28.695 63.384 1.00 38.75 N ANISOU 1033 N TRP A 207 5467 4587 4669 -143 -343 -842 N ATOM 1034 CA TRP A 207 29.663 28.998 63.226 1.00 41.46 C ANISOU 1034 CA TRP A 207 5799 4921 5032 -115 -220 -906 C ATOM 1035 C TRP A 207 28.900 27.684 63.357 1.00 34.81 C ANISOU 1035 C TRP A 207 4979 4147 4100 -112 -140 -828 C ATOM 1036 O TRP A 207 28.433 27.086 62.384 1.00 30.77 O ANISOU 1036 O TRP A 207 4413 3613 3665 -87 -94 -752 O ATOM 1037 CB TRP A 207 29.378 29.690 61.902 1.00 40.18 C ANISOU 1037 CB TRP A 207 5546 4665 5056 -80 -199 -900 C ATOM 1038 CG TRP A 207 27.955 30.183 61.790 1.00 38.13 C ANISOU 1038 CG TRP A 207 5266 4385 4838 -53 -86 -973 C ATOM 1039 CD1 TRP A 207 27.011 30.197 62.776 1.00 50.66 C ANISOU 1039 CD1 TRP A 207 6906 6020 6322 -56 1 -1058 C ATOM 1040 CD2 TRP A 207 27.320 30.727 60.624 1.00 38.22 C ANISOU 1040 CD2 TRP A 207 5192 4321 5007 -18 -46 -961 C ATOM 1041 NE1 TRP A 207 25.830 30.712 62.296 1.00 41.53 N ANISOU 1041 NE1 TRP A 207 5698 4817 5266 -23 94 -1101 N ATOM 1042 CE2 TRP A 207 25.994 31.045 60.978 1.00 37.43 C ANISOU 1042 CE2 TRP A 207 5093 4222 4907 -1 60 -1039 C ATOM 1043 CE3 TRP A 207 27.744 30.970 59.315 1.00 39.73 C ANISOU 1043 CE3 TRP A 207 5306 4450 5339 -1 -89 -884 C ATOM 1044 CZ2 TRP A 207 25.092 31.599 60.073 1.00 40.26 C ANISOU 1044 CZ2 TRP A 207 5372 4515 5410 32 114 -1040 C ATOM 1045 CZ3 TRP A 207 26.848 31.520 58.420 1.00 41.66 C ANISOU 1045 CZ3 TRP A 207 5480 4640 5710 29 -37 -884 C ATOM 1046 CH2 TRP A 207 25.537 31.828 58.802 1.00 41.96 C ANISOU 1046 CH2 TRP A 207 5516 4675 5754 45 59 -959 C ATOM 1047 N ASN A 208 28.776 27.236 64.599 1.00 34.22 N ANISOU 1047 N ASN A 208 4985 4160 3858 -139 -126 -849 N ATOM 1048 CA ASN A 208 28.158 25.963 64.922 1.00 35.34 C ANISOU 1048 CA ASN A 208 5152 4371 3903 -143 -58 -766 C ATOM 1049 C ASN A 208 27.483 26.117 66.275 1.00 38.68 C ANISOU 1049 C ASN A 208 5658 4877 4162 -162 9 -851 C ATOM 1050 O ASN A 208 27.460 27.209 66.852 1.00 37.69 O ANISOU 1050 O ASN A 208 5567 4748 4007 -168 7 -984 O ATOM 1051 CB ASN A 208 29.197 24.838 64.929 1.00 38.32 C ANISOU 1051 CB ASN A 208 5536 4778 4245 -164 -144 -632 C ATOM 1052 CG ASN A 208 30.309 25.087 65.925 1.00 38.61 C ANISOU 1052 CG ASN A 208 5634 4860 4178 -204 -256 -649 C ATOM 1053 OD1 ASN A 208 30.078 25.108 67.128 1.00 37.42 O ANISOU 1053 OD1 ASN A 208 5561 4789 3866 -231 -242 -697 O ATOM 1054 ND2 ASN A 208 31.524 25.266 65.428 1.00 38.83 N ANISOU 1054 ND2 ASN A 208 5624 4837 4293 -209 -368 -607 N ATOM 1055 N CYS A 209 26.946 25.017 66.797 1.00 37.33 N ANISOU 1055 N CYS A 209 5519 4781 3883 -172 72 -777 N ATOM 1056 CA CYS A 209 26.190 25.048 68.041 1.00 47.25 C ANISOU 1056 CA CYS A 209 6851 6126 4974 -188 158 -843 C ATOM 1057 C CYS A 209 26.888 24.309 69.179 1.00 50.27 C ANISOU 1057 C CYS A 209 7318 6616 5168 -233 95 -777 C ATOM 1058 O CYS A 209 26.257 24.025 70.202 1.00 48.58 O ANISOU 1058 O CYS A 209 7168 6494 4795 -249 173 -793 O ATOM 1059 CB CYS A 209 24.793 24.470 67.814 1.00 39.17 C ANISOU 1059 CB CYS A 209 5794 5110 3980 -163 302 -812 C ATOM 1060 SG CYS A 209 24.706 22.671 67.632 1.00 46.47 S ANISOU 1060 SG CYS A 209 6700 6072 4886 -173 315 -620 S ATOM 1061 N LEU A 210 28.181 24.007 69.034 1.00 46.16 N ANISOU 1061 N LEU A 210 6793 6085 4661 -253 -43 -699 N ATOM 1062 CA LEU A 210 28.885 23.265 70.076 1.00 56.67 C ANISOU 1062 CA LEU A 210 8194 7514 5824 -298 -117 -618 C ATOM 1063 C LEU A 210 28.827 23.986 71.418 1.00 50.30 C ANISOU 1063 C LEU A 210 7491 6800 4823 -331 -118 -740 C ATOM 1064 O LEU A 210 28.705 23.346 72.469 1.00 59.34 O ANISOU 1064 O LEU A 210 8708 8058 5782 -363 -103 -690 O ATOM 1065 CB LEU A 210 30.336 23.033 69.662 1.00 48.67 C ANISOU 1065 CB LEU A 210 7148 6460 4885 -312 -273 -531 C ATOM 1066 CG LEU A 210 30.507 22.071 68.490 1.00 50.41 C ANISOU 1066 CG LEU A 210 7281 6610 5265 -285 -272 -395 C ATOM 1067 CD1 LEU A 210 31.933 22.101 67.972 1.00 58.94 C ANISOU 1067 CD1 LEU A 210 8317 7632 6444 -292 -412 -337 C ATOM 1068 CD2 LEU A 210 30.106 20.664 68.910 1.00 48.76 C ANISOU 1068 CD2 LEU A 210 7085 6463 4978 -296 -224 -261 C ATOM 1069 N ALA A 211 28.906 25.317 71.405 1.00 45.61 N ANISOU 1069 N ALA A 211 6904 6159 4266 -326 -135 -901 N ATOM 1070 CA ALA A 211 28.869 26.069 72.655 1.00 72.34 C ANISOU 1070 CA ALA A 211 10390 9626 7470 -358 -137 -1041 C ATOM 1071 C ALA A 211 27.441 26.252 73.155 1.00 70.10 C ANISOU 1071 C ALA A 211 10141 9390 7105 -340 42 -1133 C ATOM 1072 O ALA A 211 27.160 26.047 74.341 1.00 82.86 O ANISOU 1072 O ALA A 211 11851 11128 8506 -370 85 -1160 O ATOM 1073 CB ALA A 211 29.545 27.428 72.468 1.00 71.99 C ANISOU 1073 CB ALA A 211 10336 9502 7514 -361 -228 -1184 C ATOM 1074 N GLU A 212 26.529 26.634 72.266 1.00 68.42 N ANISOU 1074 N GLU A 212 9850 9086 7061 -291 149 -1176 N ATOM 1075 CA GLU A 212 25.140 26.929 72.612 1.00 68.28 C ANISOU 1075 CA GLU A 212 9843 9089 7010 -267 324 -1270 C ATOM 1076 C GLU A 212 24.263 25.835 72.010 1.00 71.41 C ANISOU 1076 C GLU A 212 10175 9479 7478 -241 425 -1129 C ATOM 1077 O GLU A 212 23.933 25.875 70.821 1.00 65.63 O ANISOU 1077 O GLU A 212 9346 8644 6945 -204 443 -1097 O ATOM 1078 CB GLU A 212 24.749 28.315 72.103 1.00 74.66 C ANISOU 1078 CB GLU A 212 10604 9788 7975 -233 363 -1434 C ATOM 1079 CG GLU A 212 23.371 28.791 72.539 1.00 89.76 C ANISOU 1079 CG GLU A 212 12525 11714 9866 -206 543 -1555 C ATOM 1080 CD GLU A 212 23.003 30.135 71.935 1.00102.00 C ANISOU 1080 CD GLU A 212 14011 13138 11607 -169 574 -1701 C ATOM 1081 OE1 GLU A 212 23.897 30.800 71.370 1.00 97.96 O ANISOU 1081 OE1 GLU A 212 13467 12543 11212 -171 450 -1727 O ATOM 1082 OE2 GLU A 212 21.818 30.523 72.022 1.00103.79 O ANISOU 1082 OE2 GLU A 212 14212 13345 11879 -137 725 -1784 O ATOM 1083 N ARG A 213 23.888 24.854 72.836 1.00 64.28 N ANISOU 1083 N ARG A 213 9325 8688 6410 -263 486 -1043 N ATOM 1084 CA ARG A 213 23.083 23.740 72.350 1.00 74.49 C ANISOU 1084 CA ARG A 213 10557 9975 7770 -245 575 -904 C ATOM 1085 C ARG A 213 21.655 24.160 72.023 1.00 71.47 C ANISOU 1085 C ARG A 213 10119 9546 7488 -204 740 -981 C ATOM 1086 O ARG A 213 20.984 23.481 71.237 1.00 51.44 O ANISOU 1086 O ARG A 213 7503 6961 5082 -181 796 -888 O ATOM 1087 CB ARG A 213 23.070 22.609 73.382 1.00 71.60 C ANISOU 1087 CB ARG A 213 10258 9739 7207 -282 598 -783 C ATOM 1088 CG ARG A 213 22.684 21.250 72.804 1.00 95.27 C ANISOU 1088 CG ARG A 213 13188 12717 10294 -274 632 -602 C ATOM 1089 CD ARG A 213 22.396 20.237 73.901 1.00102.46 C ANISOU 1089 CD ARG A 213 14158 13754 11018 -307 690 -489 C ATOM 1090 NE ARG A 213 21.285 20.668 74.743 1.00118.28 N ANISOU 1090 NE ARG A 213 16206 15831 12903 -303 852 -584 N ATOM 1091 CZ ARG A 213 20.005 20.506 74.437 1.00103.70 C ANISOU 1091 CZ ARG A 213 14299 13954 11151 -273 1005 -585 C ATOM 1092 NH1 ARG A 213 19.630 19.897 73.323 1.00111.30 N ANISOU 1092 NH1 ARG A 213 15155 14816 12316 -248 1013 -496 N ATOM 1093 NH2 ARG A 213 19.076 20.973 75.267 1.00 79.31 N ANISOU 1093 NH2 ARG A 213 11252 10934 7950 -269 1155 -681 N ATOM 1094 N ALA A 214 21.173 25.260 72.606 1.00 51.00 N ANISOU 1094 N ALA A 214 7565 6965 4849 -195 817 -1153 N ATOM 1095 CA ALA A 214 19.853 25.767 72.253 1.00 66.05 C ANISOU 1095 CA ALA A 214 9405 8812 6878 -152 968 -1231 C ATOM 1096 C ALA A 214 19.796 26.264 70.814 1.00 67.62 C ANISOU 1096 C ALA A 214 9493 8866 7334 -114 925 -1235 C ATOM 1097 O ALA A 214 18.699 26.413 70.266 1.00 60.17 O ANISOU 1097 O ALA A 214 8471 7863 6529 -79 1032 -1248 O ATOM 1098 CB ALA A 214 19.449 26.896 73.204 1.00 52.03 C ANISOU 1098 CB ALA A 214 7695 7071 5005 -149 1057 -1426 C ATOM 1099 N ALA A 215 20.947 26.522 70.196 1.00 62.20 N ANISOU 1099 N ALA A 215 8796 8125 6714 -122 772 -1217 N ATOM 1100 CA ALA A 215 21.015 27.023 68.833 1.00 51.53 C ANISOU 1100 CA ALA A 215 7345 6647 5588 -90 722 -1212 C ATOM 1101 C ALA A 215 21.228 25.913 67.815 1.00 42.81 C ANISOU 1101 C ALA A 215 6178 5514 4573 -88 669 -1044 C ATOM 1102 O ALA A 215 21.405 26.206 66.630 1.00 42.21 O ANISOU 1102 O ALA A 215 6026 5346 4665 -66 616 -1023 O ATOM 1103 CB ALA A 215 22.133 28.061 68.714 1.00 48.08 C ANISOU 1103 CB ALA A 215 6923 6158 5185 -99 596 -1298 C ATOM 1104 N CYS A 216 21.208 24.652 68.244 1.00 37.78 N ANISOU 1104 N CYS A 216 5572 4955 3829 -110 684 -926 N ATOM 1105 CA CYS A 216 21.471 23.547 67.333 1.00 36.78 C ANISOU 1105 CA CYS A 216 5391 4798 3788 -109 632 -776 C ATOM 1106 C CYS A 216 20.316 23.342 66.362 1.00 40.33 C ANISOU 1106 C CYS A 216 5746 5181 4397 -77 716 -750 C ATOM 1107 O CYS A 216 19.141 23.465 66.720 1.00 43.17 O ANISOU 1107 O CYS A 216 6091 5554 4758 -65 842 -791 O ATOM 1108 CB CYS A 216 21.716 22.251 68.109 1.00 58.17 C ANISOU 1108 CB CYS A 216 8151 7599 6354 -142 629 -654 C ATOM 1109 SG CYS A 216 23.285 22.178 69.023 1.00 63.70 S ANISOU 1109 SG CYS A 216 8945 8372 6885 -186 486 -631 S ATOM 1110 N SER A 217 20.667 23.017 65.127 1.00 41.46 N ANISOU 1110 N SER A 217 5824 5255 4676 -66 645 -680 N ATOM 1111 CA SER A 217 19.693 22.596 64.135 1.00 32.25 C ANISOU 1111 CA SER A 217 4570 4033 3650 -44 699 -633 C ATOM 1112 C SER A 217 19.408 21.107 64.303 1.00 43.00 C ANISOU 1112 C SER A 217 5931 5434 4974 -62 730 -510 C ATOM 1113 O SER A 217 19.888 20.454 65.235 1.00 35.72 O ANISOU 1113 O SER A 217 5073 4584 3915 -90 720 -458 O ATOM 1114 CB SER A 217 20.209 22.902 62.735 1.00 38.98 C ANISOU 1114 CB SER A 217 5361 4803 4648 -27 609 -616 C ATOM 1115 OG SER A 217 21.244 22.002 62.381 1.00 34.93 O ANISOU 1115 OG SER A 217 4858 4295 4117 -43 518 -520 O ATOM 1116 N VAL A 218 18.616 20.555 63.381 1.00 35.61 N ANISOU 1116 N VAL A 218 4917 4448 4166 -49 762 -459 N ATOM 1117 CA VAL A 218 18.322 19.129 63.394 1.00 37.53 C ANISOU 1117 CA VAL A 218 5144 4708 4407 -67 786 -343 C ATOM 1118 C VAL A 218 19.497 18.288 62.926 1.00 36.06 C ANISOU 1118 C VAL A 218 4968 4510 4224 -80 677 -257 C ATOM 1119 O VAL A 218 19.468 17.065 63.081 1.00 40.11 O ANISOU 1119 O VAL A 218 5476 5036 4727 -98 685 -157 O ATOM 1120 CB VAL A 218 17.089 18.826 62.518 1.00 36.87 C ANISOU 1120 CB VAL A 218 4971 4568 4471 -51 847 -325 C ATOM 1121 CG1 VAL A 218 15.878 19.579 63.039 1.00 36.22 C ANISOU 1121 CG1 VAL A 218 4868 4494 4400 -36 966 -401 C ATOM 1122 CG2 VAL A 218 17.371 19.176 61.058 1.00 31.72 C ANISOU 1122 CG2 VAL A 218 4261 3840 3952 -34 763 -339 C ATOM 1123 N VAL A 219 20.517 18.908 62.341 1.00 29.90 N ANISOU 1123 N VAL A 219 4193 3697 3471 -72 580 -289 N ATOM 1124 CA VAL A 219 21.740 18.227 61.929 1.00 39.88 C ANISOU 1124 CA VAL A 219 5464 4947 4742 -82 480 -215 C ATOM 1125 C VAL A 219 22.850 18.745 62.837 1.00 37.35 C ANISOU 1125 C VAL A 219 5214 4673 4303 -98 414 -237 C ATOM 1126 O VAL A 219 23.354 19.854 62.635 1.00 36.19 O ANISOU 1126 O VAL A 219 5074 4506 4172 -88 367 -315 O ATOM 1127 CB VAL A 219 22.065 18.475 60.450 1.00 42.77 C ANISOU 1127 CB VAL A 219 5771 5239 5241 -61 421 -225 C ATOM 1128 CG1 VAL A 219 23.431 17.909 60.097 1.00 47.35 C ANISOU 1128 CG1 VAL A 219 6359 5804 5826 -68 326 -161 C ATOM 1129 CG2 VAL A 219 20.987 17.878 59.549 1.00 43.55 C ANISOU 1129 CG2 VAL A 219 5803 5297 5447 -52 471 -201 C ATOM 1130 N ARG A 220 23.242 17.955 63.851 1.00 38.81 N ANISOU 1130 N ARG A 220 5450 4921 4373 -125 405 -165 N ATOM 1131 CA AARG A 220 24.293 18.396 64.756 0.50 40.28 C ANISOU 1131 CA AARG A 220 5706 5160 4439 -146 330 -181 C ATOM 1132 CA BARG A 220 24.291 18.406 64.751 0.50 40.28 C ANISOU 1132 CA BARG A 220 5706 5160 4440 -146 330 -182 C ATOM 1133 C ARG A 220 25.655 18.303 64.069 1.00 37.89 C ANISOU 1133 C ARG A 220 5383 4810 4203 -145 209 -140 C ATOM 1134 O ARG A 220 25.880 17.416 63.240 1.00 39.31 O ANISOU 1134 O ARG A 220 5514 4943 4480 -137 190 -61 O ATOM 1135 CB AARG A 220 24.323 17.548 66.023 0.50 51.00 C ANISOU 1135 CB AARG A 220 7122 6606 5650 -178 347 -100 C ATOM 1136 CB BARG A 220 24.303 17.576 66.031 0.50 51.00 C ANISOU 1136 CB BARG A 220 7122 6606 5649 -178 349 -103 C ATOM 1137 CG AARG A 220 22.982 17.305 66.684 0.50 59.71 C ANISOU 1137 CG AARG A 220 8236 7759 6693 -182 480 -104 C ATOM 1138 CG BARG A 220 22.941 17.352 66.670 0.50 59.72 C ANISOU 1138 CG BARG A 220 8236 7759 6695 -180 483 -109 C ATOM 1139 CD AARG A 220 22.398 18.558 67.306 0.50 63.02 C ANISOU 1139 CD AARG A 220 8696 8215 7032 -175 545 -243 C ATOM 1140 CD BARG A 220 22.256 18.653 67.053 0.50 62.63 C ANISOU 1140 CD BARG A 220 8631 8147 7020 -168 553 -255 C ATOM 1141 NE AARG A 220 21.356 18.203 68.260 0.50 69.00 N ANISOU 1141 NE AARG A 220 9482 9046 7687 -186 669 -228 N ATOM 1142 NE BARG A 220 21.142 18.408 67.963 0.50 69.39 N ANISOU 1142 NE BARG A 220 9511 9071 7782 -175 683 -254 N ATOM 1143 CZ AARG A 220 20.151 17.765 67.921 0.50 62.28 C ANISOU 1143 CZ AARG A 220 8572 8169 6921 -171 778 -203 C ATOM 1144 CZ BARG A 220 21.262 18.277 69.278 0.50 63.98 C ANISOU 1144 CZ BARG A 220 8908 8492 6911 -204 705 -240 C ATOM 1145 NH1AARG A 220 19.784 17.667 66.653 0.50 47.08 N ANISOU 1145 NH1AARG A 220 6563 6150 5177 -146 774 -200 N ATOM 1146 NH1BARG A 220 22.434 18.396 69.882 0.50 67.60 N ANISOU 1146 NH1BARG A 220 9433 8999 7251 -231 597 -230 N ATOM 1147 NH2AARG A 220 19.297 17.410 68.875 0.50 57.39 N ANISOU 1147 NH2AARG A 220 7980 7625 6203 -184 893 -178 N ATOM 1148 NH2BARG A 220 20.180 18.017 70.005 0.50 67.06 N ANISOU 1148 NH2BARG A 220 9311 8942 7228 -209 839 -232 N ATOM 1149 N PRO A 221 26.594 19.209 64.403 1.00 36.11 N ANISOU 1149 N PRO A 221 5193 4594 3933 -153 128 -195 N ATOM 1150 CA PRO A 221 26.519 20.356 65.313 1.00 37.04 C ANISOU 1150 CA PRO A 221 5370 4756 3946 -164 132 -307 C ATOM 1151 C PRO A 221 26.280 21.673 64.575 1.00 40.40 C ANISOU 1151 C PRO A 221 5760 5116 4475 -137 140 -424 C ATOM 1152 O PRO A 221 26.782 22.715 64.989 1.00 37.79 O ANISOU 1152 O PRO A 221 5461 4787 4111 -144 92 -512 O ATOM 1153 CB PRO A 221 27.895 20.348 65.983 1.00 47.83 C ANISOU 1153 CB PRO A 221 6783 6158 5231 -194 9 -273 C ATOM 1154 CG PRO A 221 28.819 19.695 64.963 1.00 45.07 C ANISOU 1154 CG PRO A 221 6371 5742 5011 -184 -66 -177 C ATOM 1155 CD PRO A 221 27.965 19.039 63.895 1.00 39.44 C ANISOU 1155 CD PRO A 221 5593 4977 4416 -155 14 -140 C ATOM 1156 N LEU A 222 25.527 21.624 63.481 1.00 32.00 N ANISOU 1156 N LEU A 222 4626 3991 3539 -107 195 -421 N ATOM 1157 CA LEU A 222 25.269 22.832 62.712 1.00 37.71 C ANISOU 1157 CA LEU A 222 5306 4649 4372 -82 200 -511 C ATOM 1158 C LEU A 222 24.300 23.745 63.451 1.00 33.23 C ANISOU 1158 C LEU A 222 4764 4101 3760 -76 285 -627 C ATOM 1159 O LEU A 222 23.311 23.289 64.031 1.00 36.41 O ANISOU 1159 O LEU A 222 5184 4549 4103 -78 382 -625 O ATOM 1160 CB LEU A 222 24.704 22.481 61.337 1.00 35.58 C ANISOU 1160 CB LEU A 222 4957 4319 4242 -56 229 -467 C ATOM 1161 CG LEU A 222 25.613 21.611 60.474 1.00 37.93 C ANISOU 1161 CG LEU A 222 5226 4591 4597 -56 159 -369 C ATOM 1162 CD1 LEU A 222 24.965 21.365 59.134 1.00 31.08 C ANISOU 1162 CD1 LEU A 222 4287 3672 3849 -33 190 -346 C ATOM 1163 CD2 LEU A 222 26.983 22.257 60.304 1.00 36.53 C ANISOU 1163 CD2 LEU A 222 5052 4389 4440 -60 56 -376 C ATOM 1164 N ALA A 223 24.588 25.044 63.411 1.00 34.56 N ANISOU 1164 N ALA A 223 4931 4230 3971 -68 253 -728 N ATOM 1165 CA ALA A 223 23.712 26.045 64.000 1.00 30.44 C ANISOU 1165 CA ALA A 223 4423 3707 3437 -57 335 -854 C ATOM 1166 C ALA A 223 22.504 26.295 63.106 1.00 35.20 C ANISOU 1166 C ALA A 223 4944 4249 4181 -23 419 -864 C ATOM 1167 O ALA A 223 22.611 26.288 61.876 1.00 32.75 O ANISOU 1167 O ALA A 223 4565 3878 4000 -6 380 -811 O ATOM 1168 CB ALA A 223 24.474 27.351 64.218 1.00 35.90 C ANISOU 1168 CB ALA A 223 5131 4361 4150 -61 264 -960 C ATOM 1169 N ARG A 224 21.350 26.529 63.739 1.00 31.04 N ANISOU 1169 N ARG A 224 3813 3480 4501 394 148 -10 N ATOM 1170 CA AARG A 224 20.123 26.749 62.980 0.50 39.15 C ANISOU 1170 CA AARG A 224 4836 4533 5505 455 118 -30 C ATOM 1171 CA BARG A 224 20.121 26.750 62.985 0.50 39.15 C ANISOU 1171 CA BARG A 224 4836 4534 5505 455 118 -30 C ATOM 1172 C ARG A 224 20.269 27.907 62.003 1.00 33.99 C ANISOU 1172 C ARG A 224 4275 3810 4831 491 89 -31 C ATOM 1173 O ARG A 224 19.711 27.869 60.899 1.00 31.88 O ANISOU 1173 O ARG A 224 4015 3546 4551 512 73 -30 O ATOM 1174 CB AARG A 224 18.949 27.009 63.924 0.50 40.20 C ANISOU 1174 CB AARG A 224 4918 4737 5617 520 103 -60 C ATOM 1175 CB BARG A 224 18.963 27.007 63.952 0.50 40.22 C ANISOU 1175 CB BARG A 224 4920 4740 5620 520 104 -60 C ATOM 1176 CG AARG A 224 18.296 25.748 64.454 0.50 42.44 C ANISOU 1176 CG AARG A 224 5096 5113 5917 499 119 -55 C ATOM 1177 CG BARG A 224 17.604 26.839 63.308 0.50 45.29 C ANISOU 1177 CG BARG A 224 5526 5440 6242 570 80 -70 C ATOM 1178 CD AARG A 224 16.921 26.031 65.037 0.50 48.67 C ANISOU 1178 CD AARG A 224 5832 5983 6676 575 97 -77 C ATOM 1179 CD BARG A 224 16.471 26.720 64.311 0.50 54.48 C ANISOU 1179 CD BARG A 224 6613 6698 7389 622 73 -86 C ATOM 1180 NE AARG A 224 16.958 27.113 66.012 0.50 50.14 N ANISOU 1180 NE AARG A 224 6052 6159 6839 630 90 -101 N ATOM 1181 NE BARG A 224 15.229 26.351 63.641 0.50 56.13 N ANISOU 1181 NE BARG A 224 6775 6972 7579 654 53 -83 N ATOM 1182 CZ AARG A 224 17.400 26.984 67.255 0.50 50.16 C ANISOU 1182 CZ AARG A 224 6024 6184 6851 611 109 -105 C ATOM 1183 CZ BARG A 224 14.075 26.130 64.256 0.50 58.80 C ANISOU 1183 CZ BARG A 224 7037 7406 7898 700 43 -87 C ATOM 1184 NH1AARG A 224 17.862 25.829 67.708 0.50 44.61 N ANISOU 1184 NH1AARG A 224 5252 5515 6182 539 139 -81 N ATOM 1185 NH1BARG A 224 13.959 26.236 65.569 0.50 54.00 N ANISOU 1185 NH1BARG A 224 6388 6844 7286 725 52 -96 N ATOM 1186 NH2AARG A 224 17.383 28.041 68.062 0.50 46.70 N ANISOU 1186 NH2AARG A 224 5626 5732 6385 666 98 -132 N ATOM 1187 NH2BARG A 224 13.010 25.794 63.534 0.50 46.91 N ANISOU 1187 NH2BARG A 224 5491 5957 6374 720 22 -77 N ATOM 1188 N SER A 225 21.004 28.952 62.390 1.00 34.32 N ANISOU 1188 N SER A 225 4385 3788 4866 496 80 -30 N ATOM 1189 CA SER A 225 21.146 30.110 61.511 1.00 34.08 C ANISOU 1189 CA SER A 225 4443 3687 4818 530 48 -27 C ATOM 1190 C SER A 225 22.000 29.786 60.291 1.00 34.58 C ANISOU 1190 C SER A 225 4537 3708 4894 479 56 11 C ATOM 1191 O SER A 225 21.749 30.306 59.197 1.00 37.47 O ANISOU 1191 O SER A 225 4945 4048 5246 508 33 17 O ATOM 1192 CB SER A 225 21.752 31.280 62.283 1.00 31.91 C ANISOU 1192 CB SER A 225 4238 3352 4536 542 33 -35 C ATOM 1193 OG SER A 225 23.017 30.926 62.815 1.00 42.08 O ANISOU 1193 OG SER A 225 5529 4615 5844 464 58 -7 O ATOM 1194 N HIS A 226 23.012 28.937 60.460 1.00 33.04 N ANISOU 1194 N HIS A 226 4321 3509 4722 405 90 40 N ATOM 1195 CA HIS A 226 23.809 28.492 59.323 1.00 32.57 C ANISOU 1195 CA HIS A 226 4284 3420 4671 360 103 78 C ATOM 1196 C HIS A 226 22.996 27.590 58.401 1.00 36.14 C ANISOU 1196 C HIS A 226 4693 3919 5121 369 106 68 C ATOM 1197 O HIS A 226 23.072 27.713 57.172 1.00 29.50 O ANISOU 1197 O HIS A 226 3885 3055 4269 375 95 82 O ATOM 1198 CB HIS A 226 25.051 27.765 59.828 1.00 31.23 C ANISOU 1198 CB HIS A 226 4097 3243 4525 285 143 114 C ATOM 1199 CG HIS A 226 25.870 27.139 58.743 1.00 31.49 C ANISOU 1199 CG HIS A 226 4144 3257 4564 244 164 155 C ATOM 1200 ND1 HIS A 226 26.039 25.776 58.631 1.00 33.75 N ANISOU 1200 ND1 HIS A 226 4377 3579 4869 205 203 165 N ATOM 1201 CD2 HIS A 226 26.569 27.690 57.724 1.00 28.28 C ANISOU 1201 CD2 HIS A 226 3799 2802 4146 238 152 189 C ATOM 1202 CE1 HIS A 226 26.804 25.514 57.587 1.00 31.27 C ANISOU 1202 CE1 HIS A 226 4093 3237 4550 182 215 200 C ATOM 1203 NE2 HIS A 226 27.140 26.659 57.019 1.00 29.19 N ANISOU 1203 NE2 HIS A 226 3895 2926 4268 201 184 217 N ATOM 1204 N VAL A 227 22.215 26.675 58.979 1.00 38.62 N ANISOU 1204 N VAL A 227 4931 4299 5444 369 120 46 N ATOM 1205 CA VAL A 227 21.380 25.784 58.183 1.00 29.67 C ANISOU 1205 CA VAL A 227 3755 3211 4306 371 118 36 C ATOM 1206 C VAL A 227 20.306 26.566 57.442 1.00 35.67 C ANISOU 1206 C VAL A 227 4534 3982 5035 437 78 17 C ATOM 1207 O VAL A 227 19.941 26.220 56.311 1.00 31.85 O ANISOU 1207 O VAL A 227 4052 3509 4540 437 69 19 O ATOM 1208 CB VAL A 227 20.773 24.701 59.093 1.00 38.09 C ANISOU 1208 CB VAL A 227 4734 4347 5391 353 135 23 C ATOM 1209 CG1 VAL A 227 19.691 23.924 58.364 1.00 44.38 C ANISOU 1209 CG1 VAL A 227 5488 5196 6180 359 122 9 C ATOM 1210 CG2 VAL A 227 21.870 23.773 59.590 1.00 34.96 C ANISOU 1210 CG2 VAL A 227 4316 3938 5027 283 179 48 C ATOM 1211 N ALA A 228 19.790 27.631 58.055 1.00 32.46 N ANISOU 1211 N ALA A 228 4146 3575 4614 495 55 0 N ATOM 1212 CA ALA A 228 18.835 28.492 57.368 1.00 35.56 C ANISOU 1212 CA ALA A 228 4562 3974 4976 565 20 -12 C ATOM 1213 C ALA A 228 19.443 29.083 56.105 1.00 31.34 C ANISOU 1213 C ALA A 228 4096 3377 4433 561 7 11 C ATOM 1214 O ALA A 228 18.784 29.159 55.062 1.00 33.34 O ANISOU 1214 O ALA A 228 4351 3650 4667 588 -12 12 O ATOM 1215 CB ALA A 228 18.375 29.605 58.308 1.00 36.22 C ANISOU 1215 CB ALA A 228 4665 4052 5043 631 1 -34 C ATOM 1216 N LEU A 229 20.696 29.532 56.194 1.00 37.57 N ANISOU 1216 N LEU A 229 4941 4098 5235 528 14 34 N ATOM 1217 CA LEU A 229 21.407 30.024 55.021 1.00 39.55 C ANISOU 1217 CA LEU A 229 5252 4295 5480 518 3 66 C ATOM 1218 C LEU A 229 21.538 28.938 53.962 1.00 35.11 C ANISOU 1218 C LEU A 229 4664 3758 4917 479 20 79 C ATOM 1219 O LEU A 229 21.329 29.193 52.771 1.00 32.04 O ANISOU 1219 O LEU A 229 4297 3366 4510 498 3 89 O ATOM 1220 CB LEU A 229 22.784 30.532 55.441 1.00 41.18 C ANISOU 1220 CB LEU A 229 5512 4434 5701 478 10 96 C ATOM 1221 CG LEU A 229 23.757 30.883 54.320 1.00 41.69 C ANISOU 1221 CG LEU A 229 5630 4449 5762 453 4 142 C ATOM 1222 CD1 LEU A 229 23.189 32.010 53.485 1.00 44.48 C ANISOU 1222 CD1 LEU A 229 6028 4778 6096 512 -37 143 C ATOM 1223 CD2 LEU A 229 25.113 31.250 54.901 1.00 38.15 C ANISOU 1223 CD2 LEU A 229 5222 3947 5328 404 12 178 C ATOM 1224 N LEU A 230 21.898 27.721 54.378 1.00 32.92 N ANISOU 1224 N LEU A 230 4342 3507 4660 427 55 79 N ATOM 1225 CA LEU A 230 22.011 26.620 53.430 1.00 27.16 C ANISOU 1225 CA LEU A 230 3593 2798 3930 391 72 86 C ATOM 1226 C LEU A 230 20.695 26.378 52.706 1.00 38.28 C ANISOU 1226 C LEU A 230 4971 4258 5315 424 48 60 C ATOM 1227 O LEU A 230 20.678 26.180 51.485 1.00 28.95 O ANISOU 1227 O LEU A 230 3806 3078 4115 421 41 68 O ATOM 1228 CB LEU A 230 22.455 25.350 54.151 1.00 26.61 C ANISOU 1228 CB LEU A 230 3476 2747 3887 336 112 87 C ATOM 1229 CG LEU A 230 23.865 25.359 54.743 1.00 30.67 C ANISOU 1229 CG LEU A 230 4013 3218 4422 293 143 122 C ATOM 1230 CD1 LEU A 230 24.200 23.998 55.356 1.00 32.56 C ANISOU 1230 CD1 LEU A 230 4199 3483 4688 241 185 125 C ATOM 1231 CD2 LEU A 230 24.890 25.736 53.692 1.00 32.10 C ANISOU 1231 CD2 LEU A 230 4254 3353 4591 281 144 162 C ATOM 1232 N SER A 231 19.581 26.384 53.446 1.00 32.04 N ANISOU 1232 N SER A 231 4133 3518 4521 456 35 33 N ATOM 1233 CA SER A 231 18.282 26.151 52.828 1.00 34.49 C ANISOU 1233 CA SER A 231 4408 3888 4807 484 11 16 C ATOM 1234 C SER A 231 17.905 27.302 51.913 1.00 32.28 C ANISOU 1234 C SER A 231 4172 3594 4498 539 -20 24 C ATOM 1235 O SER A 231 17.323 27.086 50.846 1.00 32.57 O ANISOU 1235 O SER A 231 4202 3662 4512 545 -36 23 O ATOM 1236 CB SER A 231 17.207 25.954 53.897 1.00 36.27 C ANISOU 1236 CB SER A 231 4570 4178 5034 509 5 -5 C ATOM 1237 OG SER A 231 17.297 24.668 54.484 1.00 51.90 O ANISOU 1237 OG SER A 231 6494 6187 7038 454 29 -9 O ATOM 1238 N ALA A 232 18.217 28.534 52.321 1.00 32.97 N ANISOU 1238 N ALA A 232 4305 3635 4586 579 -32 31 N ATOM 1239 CA ALA A 232 17.968 29.676 51.451 1.00 38.99 C ANISOU 1239 CA ALA A 232 5115 4375 5326 630 -61 44 C ATOM 1240 C ALA A 232 18.735 29.537 50.147 1.00 31.59 C ANISOU 1240 C ALA A 232 4212 3408 4382 598 -59 70 C ATOM 1241 O ALA A 232 18.200 29.819 49.069 1.00 35.82 O ANISOU 1241 O ALA A 232 4752 3963 4893 625 -80 78 O ATOM 1242 CB ALA A 232 18.353 30.974 52.160 1.00 34.70 C ANISOU 1242 CB ALA A 232 4626 3771 4789 669 -73 48 C ATOM 1243 N ALA A 233 19.992 29.093 50.224 1.00 35.93 N ANISOU 1243 N ALA A 233 4783 3916 4952 543 -34 89 N ATOM 1244 CA ALA A 233 20.782 28.915 49.012 1.00 31.53 C ANISOU 1244 CA ALA A 233 4257 3338 4386 516 -29 118 C ATOM 1245 C ALA A 233 20.195 27.817 48.143 1.00 34.87 C ANISOU 1245 C ALA A 233 4641 3816 4791 498 -24 101 C ATOM 1246 O ALA A 233 20.148 27.946 46.914 1.00 33.47 O ANISOU 1246 O ALA A 233 4482 3647 4589 507 -37 114 O ATOM 1247 CB ALA A 233 22.233 28.594 49.365 1.00 37.99 C ANISOU 1247 CB ALA A 233 5099 4111 5227 463 1 146 C ATOM 1248 N PHE A 234 19.740 26.728 48.765 1.00 31.13 N ANISOU 1248 N PHE A 234 4117 3381 4328 470 -7 74 N ATOM 1249 CA PHE A 234 19.119 25.659 47.996 1.00 28.25 C ANISOU 1249 CA PHE A 234 3721 3067 3948 448 -8 56 C ATOM 1250 C PHE A 234 17.867 26.153 47.278 1.00 36.80 C ANISOU 1250 C PHE A 234 4788 4199 4996 492 -45 47 C ATOM 1251 O PHE A 234 17.682 25.892 46.084 1.00 28.96 O ANISOU 1251 O PHE A 234 3802 3226 3977 486 -55 48 O ATOM 1252 CB PHE A 234 18.776 24.474 48.891 1.00 28.03 C ANISOU 1252 CB PHE A 234 3639 3071 3942 410 10 32 C ATOM 1253 CG PHE A 234 17.980 23.438 48.185 1.00 36.79 C ANISOU 1253 CG PHE A 234 4716 4230 5033 386 1 11 C ATOM 1254 CD1 PHE A 234 18.607 22.449 47.449 1.00 36.17 C ANISOU 1254 CD1 PHE A 234 4656 4136 4953 341 21 9 C ATOM 1255 CD2 PHE A 234 16.600 23.486 48.207 1.00 36.03 C ANISOU 1255 CD2 PHE A 234 4575 4198 4917 409 -29 -4 C ATOM 1256 CE1 PHE A 234 17.867 21.510 46.769 1.00 38.34 C ANISOU 1256 CE1 PHE A 234 4908 4450 5207 315 7 -14 C ATOM 1257 CE2 PHE A 234 15.857 22.554 47.530 1.00 46.59 C ANISOU 1257 CE2 PHE A 234 5885 5583 6235 380 -44 -20 C ATOM 1258 CZ PHE A 234 16.488 21.566 46.809 1.00 37.41 C ANISOU 1258 CZ PHE A 234 4745 4397 5072 331 -27 -28 C ATOM 1259 N PHE A 235 16.983 26.858 47.994 1.00 29.14 N ANISOU 1259 N PHE A 235 3796 3253 4024 540 -63 39 N ATOM 1260 CA PHE A 235 15.739 27.309 47.375 1.00 34.64 C ANISOU 1260 CA PHE A 235 4470 4005 4686 586 -95 37 C ATOM 1261 C PHE A 235 16.011 28.248 46.210 1.00 32.07 C ANISOU 1261 C PHE A 235 4192 3653 4339 616 -112 62 C ATOM 1262 O PHE A 235 15.326 28.191 45.182 1.00 30.06 O ANISOU 1262 O PHE A 235 3924 3445 4053 626 -131 65 O ATOM 1263 CB PHE A 235 14.841 27.993 48.408 1.00 29.68 C ANISOU 1263 CB PHE A 235 3815 3405 4058 642 -108 30 C ATOM 1264 CG PHE A 235 14.204 27.041 49.369 1.00 38.20 C ANISOU 1264 CG PHE A 235 4828 4538 5146 619 -100 10 C ATOM 1265 CD1 PHE A 235 13.355 26.049 48.915 1.00 43.89 C ANISOU 1265 CD1 PHE A 235 5498 5328 5850 590 -111 2 C ATOM 1266 CD2 PHE A 235 14.454 27.134 50.724 1.00 33.80 C ANISOU 1266 CD2 PHE A 235 4260 3966 4615 625 -85 1 C ATOM 1267 CE1 PHE A 235 12.772 25.162 49.797 1.00 33.67 C ANISOU 1267 CE1 PHE A 235 4140 4085 4567 565 -107 -10 C ATOM 1268 CE2 PHE A 235 13.872 26.254 51.610 1.00 35.22 C ANISOU 1268 CE2 PHE A 235 4374 4202 4805 605 -78 -12 C ATOM 1269 CZ PHE A 235 13.030 25.267 51.144 1.00 36.25 C ANISOU 1269 CZ PHE A 235 4452 4400 4921 574 -90 -15 C ATOM 1270 N MET A 236 16.991 29.137 46.358 1.00 34.74 N ANISOU 1270 N MET A 236 4584 3922 4694 629 -108 84 N ATOM 1271 CA MET A 236 17.329 30.037 45.263 1.00 36.51 C ANISOU 1271 CA MET A 236 4852 4120 4901 654 -125 115 C ATOM 1272 C MET A 236 17.887 29.260 44.078 1.00 35.52 C ANISOU 1272 C MET A 236 4733 4004 4760 611 -116 124 C ATOM 1273 O MET A 236 17.484 29.483 42.930 1.00 34.01 O ANISOU 1273 O MET A 236 4541 3844 4538 628 -134 136 O ATOM 1274 CB MET A 236 18.328 31.091 45.741 1.00 38.99 C ANISOU 1274 CB MET A 236 5222 4354 5238 667 -126 141 C ATOM 1275 CG MET A 236 17.691 32.215 46.544 1.00 57.56 C ANISOU 1275 CG MET A 236 7585 6689 7594 730 -146 135 C ATOM 1276 SD MET A 236 18.865 33.494 47.038 1.00 79.02 S ANISOU 1276 SD MET A 236 10380 9305 10337 738 -155 164 S ATOM 1277 CE MET A 236 19.696 32.697 48.409 1.00 74.76 C ANISOU 1277 CE MET A 236 9832 8743 9829 680 -122 146 C ATOM 1278 N VAL A 237 18.808 28.331 44.338 1.00 29.35 N ANISOU 1278 N VAL A 237 3956 3199 3996 556 -86 120 N ATOM 1279 CA VAL A 237 19.359 27.523 43.255 1.00 29.81 C ANISOU 1279 CA VAL A 237 4025 3267 4036 521 -73 125 C ATOM 1280 C VAL A 237 18.252 26.744 42.564 1.00 33.52 C ANISOU 1280 C VAL A 237 4456 3806 4476 513 -87 96 C ATOM 1281 O VAL A 237 18.201 26.665 41.331 1.00 29.85 O ANISOU 1281 O VAL A 237 4000 3364 3977 514 -97 103 O ATOM 1282 CB VAL A 237 20.458 26.584 43.783 1.00 33.87 C ANISOU 1282 CB VAL A 237 4547 3747 4575 469 -34 125 C ATOM 1283 CG1 VAL A 237 20.778 25.511 42.756 1.00 39.08 C ANISOU 1283 CG1 VAL A 237 5211 4425 5212 436 -19 118 C ATOM 1284 CG2 VAL A 237 21.706 27.369 44.107 1.00 38.82 C ANISOU 1284 CG2 VAL A 237 5217 4312 5222 469 -24 167 C ATOM 1285 N PHE A 238 17.347 26.160 43.347 1.00 34.98 N ANISOU 1285 N PHE A 238 4596 4028 4669 504 -89 66 N ATOM 1286 CA PHE A 238 16.277 25.362 42.766 1.00 33.39 C ANISOU 1286 CA PHE A 238 4355 3893 4438 487 -105 41 C ATOM 1287 C PHE A 238 15.351 26.228 41.928 1.00 30.72 C ANISOU 1287 C PHE A 238 4007 3601 4062 534 -139 55 C ATOM 1288 O PHE A 238 14.934 25.826 40.836 1.00 30.70 O ANISOU 1288 O PHE A 238 3999 3643 4024 520 -154 50 O ATOM 1289 CB PHE A 238 15.509 24.649 43.879 1.00 34.80 C ANISOU 1289 CB PHE A 238 4483 4105 4636 468 -104 16 C ATOM 1290 CG PHE A 238 14.523 23.636 43.385 1.00 44.05 C ANISOU 1290 CG PHE A 238 5614 5341 5781 434 -122 -6 C ATOM 1291 CD1 PHE A 238 14.946 22.541 42.656 1.00 49.97 C ANISOU 1291 CD1 PHE A 238 6382 6083 6522 382 -112 -24 C ATOM 1292 CD2 PHE A 238 13.177 23.765 43.667 1.00 46.86 C ANISOU 1292 CD2 PHE A 238 5917 5767 6119 455 -149 -8 C ATOM 1293 CE1 PHE A 238 14.044 21.600 42.204 1.00 49.64 C ANISOU 1293 CE1 PHE A 238 6310 6095 6455 344 -133 -46 C ATOM 1294 CE2 PHE A 238 12.268 22.825 43.219 1.00 60.87 C ANISOU 1294 CE2 PHE A 238 7654 7604 7869 415 -170 -23 C ATOM 1295 CZ PHE A 238 12.703 21.741 42.487 1.00 43.65 C ANISOU 1295 CZ PHE A 238 5496 5408 5680 357 -164 -44 C ATOM 1296 N GLY A 239 15.028 27.425 42.420 1.00 36.10 N ANISOU 1296 N GLY A 239 4691 4275 4751 591 -152 74 N ATOM 1297 CA GLY A 239 14.207 28.337 41.639 1.00 31.36 C ANISOU 1297 CA GLY A 239 4083 3714 4118 642 -181 94 C ATOM 1298 C GLY A 239 14.834 28.693 40.304 1.00 31.16 C ANISOU 1298 C GLY A 239 4094 3675 4071 643 -186 119 C ATOM 1299 O GLY A 239 14.138 28.813 39.294 1.00 31.58 O ANISOU 1299 O GLY A 239 4129 3784 4085 656 -207 127 O ATOM 1300 N ILE A 240 16.156 28.875 40.277 1.00 32.08 N ANISOU 1300 N ILE A 240 4257 3724 4208 629 -168 135 N ATOM 1301 CA ILE A 240 16.823 29.175 39.013 1.00 36.39 C ANISOU 1301 CA ILE A 240 4833 4262 4732 630 -172 165 C ATOM 1302 C ILE A 240 16.752 27.976 38.074 1.00 34.94 C ANISOU 1302 C ILE A 240 4637 4124 4515 586 -167 142 C ATOM 1303 O ILE A 240 16.506 28.129 36.871 1.00 31.42 O ANISOU 1303 O ILE A 240 4189 3719 4031 596 -183 154 O ATOM 1304 CB ILE A 240 18.278 29.614 39.258 1.00 34.55 C ANISOU 1304 CB ILE A 240 4649 3953 4527 622 -155 195 C ATOM 1305 CG1 ILE A 240 18.307 30.942 40.016 1.00 36.62 C ANISOU 1305 CG1 ILE A 240 4932 4166 4816 667 -169 219 C ATOM 1306 CG2 ILE A 240 19.038 29.741 37.929 1.00 38.17 C ANISOU 1306 CG2 ILE A 240 5131 4413 4958 619 -157 229 C ATOM 1307 CD1 ILE A 240 19.666 31.276 40.593 1.00 41.02 C ANISOU 1307 CD1 ILE A 240 5534 4647 5405 648 -154 246 C ATOM 1308 N MET A 241 16.964 26.767 38.602 1.00 31.87 N ANISOU 1308 N MET A 241 4242 3728 4140 537 -145 108 N ATOM 1309 CA MET A 241 16.855 25.578 37.764 1.00 36.19 C ANISOU 1309 CA MET A 241 4784 4310 4655 495 -141 79 C ATOM 1310 C MET A 241 15.468 25.475 37.144 1.00 32.45 C ANISOU 1310 C MET A 241 4270 3916 4142 499 -174 65 C ATOM 1311 O MET A 241 15.329 25.120 35.969 1.00 31.74 O ANISOU 1311 O MET A 241 4185 3865 4010 486 -185 59 O ATOM 1312 CB MET A 241 17.169 24.323 38.578 1.00 32.38 C ANISOU 1312 CB MET A 241 4299 3805 4200 445 -114 46 C ATOM 1313 CG MET A 241 18.592 24.259 39.102 1.00 42.56 C ANISOU 1313 CG MET A 241 5624 5024 5523 434 -78 63 C ATOM 1314 SD MET A 241 18.904 22.789 40.114 1.00 50.69 S ANISOU 1314 SD MET A 241 6644 6029 6587 377 -44 28 S ATOM 1315 CE MET A 241 19.347 21.614 38.845 1.00 64.30 C ANISOU 1315 CE MET A 241 8399 7760 8273 345 -31 7 C ATOM 1316 N LEU A 242 14.428 25.799 37.917 1.00 32.43 N ANISOU 1316 N LEU A 242 4229 3945 4149 519 -190 63 N ATOM 1317 CA LEU A 242 13.070 25.756 37.385 1.00 36.92 C ANISOU 1317 CA LEU A 242 4752 4597 4677 524 -221 59 C ATOM 1318 C LEU A 242 12.882 26.759 36.256 1.00 32.42 C ANISOU 1318 C LEU A 242 4188 4058 4073 568 -241 93 C ATOM 1319 O LEU A 242 12.183 26.478 35.275 1.00 32.86 O ANISOU 1319 O LEU A 242 4222 4181 4083 555 -262 91 O ATOM 1320 CB LEU A 242 12.062 26.026 38.500 1.00 33.80 C ANISOU 1320 CB LEU A 242 4311 4232 4298 548 -232 60 C ATOM 1321 CG LEU A 242 11.939 24.918 39.541 1.00 35.79 C ANISOU 1321 CG LEU A 242 4541 4482 4578 501 -220 28 C ATOM 1322 CD1 LEU A 242 11.229 25.459 40.774 1.00 41.00 C ANISOU 1322 CD1 LEU A 242 5162 5159 5258 541 -225 37 C ATOM 1323 CD2 LEU A 242 11.193 23.726 38.950 1.00 40.25 C ANISOU 1323 CD2 LEU A 242 5077 5106 5109 443 -239 4 C ATOM 1324 N HIS A 243 13.475 27.946 36.386 1.00 33.32 N ANISOU 1324 N HIS A 243 4329 4124 4208 617 -236 128 N ATOM 1325 CA HIS A 243 13.389 28.930 35.313 1.00 35.55 C ANISOU 1325 CA HIS A 243 4616 4430 4462 658 -254 168 C ATOM 1326 C HIS A 243 14.070 28.411 34.053 1.00 32.78 C ANISOU 1326 C HIS A 243 4287 4089 4079 627 -250 167 C ATOM 1327 O HIS A 243 13.498 28.445 32.957 1.00 33.23 O ANISOU 1327 O HIS A 243 4324 4212 4089 630 -270 176 O ATOM 1328 CB HIS A 243 14.017 30.248 35.770 1.00 36.59 C ANISOU 1328 CB HIS A 243 4780 4494 4628 710 -251 205 C ATOM 1329 CG HIS A 243 14.105 31.284 34.693 1.00 42.66 C ANISOU 1329 CG HIS A 243 5557 5275 5376 750 -269 252 C ATOM 1330 ND1 HIS A 243 13.059 31.567 33.841 1.00 61.73 N ANISOU 1330 ND1 HIS A 243 7935 7770 7751 774 -291 268 N ATOM 1331 CD2 HIS A 243 15.115 32.112 34.335 1.00 59.81 C ANISOU 1331 CD2 HIS A 243 7770 7394 7563 769 -268 293 C ATOM 1332 CE1 HIS A 243 13.422 32.521 33.003 1.00 54.75 C ANISOU 1332 CE1 HIS A 243 7065 6879 6858 808 -302 314 C ATOM 1333 NE2 HIS A 243 14.665 32.870 33.282 1.00 59.55 N ANISOU 1333 NE2 HIS A 243 7721 7406 7500 805 -290 331 N ATOM 1334 N LEU A 244 15.299 27.915 34.199 1.00 32.38 N ANISOU 1334 N LEU A 244 4276 3979 4048 599 -224 159 N ATOM 1335 CA LEU A 244 16.004 27.337 33.064 1.00 32.47 C ANISOU 1335 CA LEU A 244 4311 4001 4026 575 -216 156 C ATOM 1336 C LEU A 244 15.244 26.148 32.495 1.00 32.77 C ANISOU 1336 C LEU A 244 4329 4099 4022 531 -226 111 C ATOM 1337 O LEU A 244 15.187 25.959 31.274 1.00 33.14 O ANISOU 1337 O LEU A 244 4378 4193 4021 525 -237 111 O ATOM 1338 CB LEU A 244 17.408 26.917 33.493 1.00 31.99 C ANISOU 1338 CB LEU A 244 4292 3868 3995 554 -183 157 C ATOM 1339 CG LEU A 244 18.337 28.048 33.930 1.00 36.36 C ANISOU 1339 CG LEU A 244 4873 4360 4584 587 -176 207 C ATOM 1340 CD1 LEU A 244 19.586 27.484 34.575 1.00 38.09 C ANISOU 1340 CD1 LEU A 244 5124 4517 4833 558 -141 207 C ATOM 1341 CD2 LEU A 244 18.710 28.915 32.748 1.00 39.16 C ANISOU 1341 CD2 LEU A 244 5236 4733 4910 619 -192 257 C ATOM 1342 N TYR A 245 14.650 25.335 33.367 1.00 32.65 N ANISOU 1342 N TYR A 245 4295 4087 4025 497 -224 73 N ATOM 1343 CA TYR A 245 13.928 24.157 32.904 1.00 36.40 C ANISOU 1343 CA TYR A 245 4754 4613 4464 446 -238 30 C ATOM 1344 C TYR A 245 12.786 24.548 31.974 1.00 33.57 C ANISOU 1344 C TYR A 245 4358 4343 4053 458 -274 43 C ATOM 1345 O TYR A 245 12.606 23.953 30.905 1.00 33.96 O ANISOU 1345 O TYR A 245 4413 4437 4053 429 -286 24 O ATOM 1346 CB TYR A 245 13.413 23.371 34.107 1.00 36.14 C ANISOU 1346 CB TYR A 245 4698 4571 4464 411 -235 0 C ATOM 1347 CG TYR A 245 12.378 22.336 33.761 1.00 40.70 C ANISOU 1347 CG TYR A 245 5249 5209 5006 359 -261 -35 C ATOM 1348 CD1 TYR A 245 11.031 22.666 33.712 1.00 33.60 C ANISOU 1348 CD1 TYR A 245 4296 4389 4081 366 -295 -21 C ATOM 1349 CD2 TYR A 245 12.746 21.027 33.488 1.00 50.43 C ANISOU 1349 CD2 TYR A 245 6512 6421 6229 302 -252 -79 C ATOM 1350 CE1 TYR A 245 10.082 21.723 33.391 1.00 42.68 C ANISOU 1350 CE1 TYR A 245 5421 5599 5197 311 -323 -47 C ATOM 1351 CE2 TYR A 245 11.806 20.077 33.173 1.00 61.17 C ANISOU 1351 CE2 TYR A 245 7853 7832 7558 247 -281 -110 C ATOM 1352 CZ TYR A 245 10.476 20.429 33.130 1.00 54.59 C ANISOU 1352 CZ TYR A 245 6964 7080 6699 248 -318 -93 C ATOM 1353 OH TYR A 245 9.535 19.482 32.812 1.00 60.57 O ANISOU 1353 OH TYR A 245 7701 7891 7422 187 -352 -118 O ATOM 1354 N VAL A 246 12.007 25.559 32.361 1.00 33.68 N ANISOU 1354 N VAL A 246 4335 4387 4076 502 -290 77 N ATOM 1355 CA VAL A 246 10.867 25.964 31.547 1.00 34.27 C ANISOU 1355 CA VAL A 246 4367 4552 4102 517 -321 97 C ATOM 1356 C VAL A 246 11.339 26.519 30.209 1.00 36.53 C ANISOU 1356 C VAL A 246 4670 4858 4351 539 -326 124 C ATOM 1357 O VAL A 246 10.717 26.284 29.167 1.00 39.61 O ANISOU 1357 O VAL A 246 5040 5324 4687 522 -347 122 O ATOM 1358 CB VAL A 246 10.004 26.988 32.307 1.00 34.35 C ANISOU 1358 CB VAL A 246 4337 4584 4130 571 -332 132 C ATOM 1359 CG1 VAL A 246 8.900 27.509 31.406 1.00 48.31 C ANISOU 1359 CG1 VAL A 246 6059 6449 5846 593 -361 164 C ATOM 1360 CG2 VAL A 246 9.414 26.362 33.566 1.00 39.04 C ANISOU 1360 CG2 VAL A 246 4905 5179 4751 548 -331 107 C ATOM 1361 N ARG A 247 12.433 27.276 30.217 1.00 34.24 N ANISOU 1361 N ARG A 247 4415 4504 4089 576 -307 153 N ATOM 1362 CA ARG A 247 12.971 27.800 28.967 1.00 38.44 C ANISOU 1362 CA ARG A 247 4960 5056 4588 597 -311 185 C ATOM 1363 C ARG A 247 13.443 26.668 28.061 1.00 34.62 C ANISOU 1363 C ARG A 247 4501 4590 4062 550 -305 147 C ATOM 1364 O ARG A 247 13.161 26.663 26.856 1.00 39.28 O ANISOU 1364 O ARG A 247 5080 5248 4598 548 -321 154 O ATOM 1365 CB ARG A 247 14.110 28.771 29.270 1.00 38.50 C ANISOU 1365 CB ARG A 247 5002 4989 4639 639 -294 227 C ATOM 1366 CG ARG A 247 13.705 29.912 30.199 1.00 46.26 C ANISOU 1366 CG ARG A 247 5971 5941 5663 688 -301 260 C ATOM 1367 CD ARG A 247 13.938 31.254 29.549 1.00 60.15 C ANISOU 1367 CD ARG A 247 7732 7700 7421 742 -314 322 C ATOM 1368 NE ARG A 247 13.113 31.416 28.359 1.00 67.49 N ANISOU 1368 NE ARG A 247 8623 8724 8298 752 -336 340 N ATOM 1369 CZ ARG A 247 13.423 32.190 27.328 1.00 89.81 C ANISOU 1369 CZ ARG A 247 11446 11574 11105 781 -346 390 C ATOM 1370 NH1 ARG A 247 14.548 32.888 27.300 1.00 71.12 N ANISOU 1370 NH1 ARG A 247 9113 9143 8766 802 -340 430 N ATOM 1371 NH2 ARG A 247 12.588 32.257 26.295 1.00 85.78 N ANISOU 1371 NH2 ARG A 247 10893 11157 10542 786 -365 404 N ATOM 1372 N ILE A 248 14.156 25.698 28.624 1.00 35.35 N ANISOU 1372 N ILE A 248 4630 4624 4177 514 -280 107 N ATOM 1373 CA ILE A 248 14.618 24.538 27.869 1.00 34.40 C ANISOU 1373 CA ILE A 248 4542 4510 4018 473 -272 65 C ATOM 1374 C ILE A 248 13.422 23.802 27.289 1.00 39.65 C ANISOU 1374 C ILE A 248 5180 5252 4632 431 -302 28 C ATOM 1375 O ILE A 248 13.390 23.487 26.100 1.00 35.40 O ANISOU 1375 O ILE A 248 4651 4765 4036 419 -313 17 O ATOM 1376 CB ILE A 248 15.460 23.599 28.748 1.00 33.92 C ANISOU 1376 CB ILE A 248 4521 4371 3997 443 -239 30 C ATOM 1377 CG1 ILE A 248 16.819 24.228 29.047 1.00 33.47 C ANISOU 1377 CG1 ILE A 248 4494 4247 3975 478 -208 71 C ATOM 1378 CG2 ILE A 248 15.642 22.249 28.070 1.00 36.44 C ANISOU 1378 CG2 ILE A 248 4872 4698 4274 397 -233 -24 C ATOM 1379 CD1 ILE A 248 17.529 23.595 30.210 1.00 36.07 C ANISOU 1379 CD1 ILE A 248 4848 4500 4355 456 -176 52 C HETATM 1380 N YCM A 249 12.444 23.520 28.142 1.00 39.47 N ANISOU 1380 N YCM A 249 5126 5243 4629 406 -316 12 N HETATM 1381 CA YCM A 249 11.241 22.855 27.717 1.00 35.48 C ANISOU 1381 CA YCM A 249 4589 4813 4077 360 -350 -14 C HETATM 1382 CB YCM A 249 10.282 22.688 28.897 1.00 57.72 C ANISOU 1382 CB YCM A 249 7365 7640 6927 343 -362 -17 C HETATM 1383 SG YCM A 249 8.602 22.293 28.494 1.00 94.03 S ANISOU 1383 SG YCM A 249 11905 12350 11471 298 -410 -20 S HETATM 1384 CD YCM A 249 8.504 20.526 28.476 1.00 78.87 C ANISOU 1384 CD YCM A 249 10016 10416 9535 204 -422 -90 C HETATM 1385 CE YCM A 249 8.777 19.868 29.811 1.00 88.63 C ANISOU 1385 CE YCM A 249 11261 11582 10833 181 -404 -112 C HETATM 1386 OZ1 YCM A 249 9.819 20.121 30.447 1.00 80.72 O ANISOU 1386 OZ1 YCM A 249 10289 10500 9882 214 -366 -110 O HETATM 1387 NZ2 YCM A 249 7.868 18.977 30.316 1.00 76.87 N ANISOU 1387 NZ2 YCM A 249 9743 10121 9343 120 -431 -132 N HETATM 1388 C YCM A 249 10.558 23.575 26.558 1.00 42.47 C ANISOU 1388 C YCM A 249 5440 5791 4906 382 -377 20 C HETATM 1389 O YCM A 249 10.080 22.984 25.588 1.00 45.35 O ANISOU 1389 O YCM A 249 5802 6218 5211 344 -400 -3 O ATOM 1390 N GLN A 250 10.534 24.902 26.662 1.00 40.07 N ANISOU 1390 N GLN A 250 5111 5493 4622 445 -375 77 N ATOM 1391 CA GLN A 250 9.982 25.765 25.616 1.00 41.00 C ANISOU 1391 CA GLN A 250 5192 5692 4694 478 -397 122 C ATOM 1392 C GLN A 250 10.661 25.566 24.252 1.00 47.97 C ANISOU 1392 C GLN A 250 6102 6599 5525 472 -396 116 C ATOM 1393 O GLN A 250 9.983 25.409 23.237 1.00 50.87 O ANISOU 1393 O GLN A 250 6443 7054 5830 453 -420 116 O ATOM 1394 CB GLN A 250 10.093 27.236 26.043 1.00 44.81 C ANISOU 1394 CB GLN A 250 5657 6152 5217 552 -390 184 C ATOM 1395 CG GLN A 250 9.464 28.234 25.072 1.00 63.79 C ANISOU 1395 CG GLN A 250 8018 8638 7582 592 -410 239 C ATOM 1396 CD GLN A 250 9.158 29.571 25.725 1.00 86.46 C ANISOU 1396 CD GLN A 250 10866 11491 10495 661 -409 295 C ATOM 1397 OE1 GLN A 250 10.042 30.218 26.289 1.00 93.81 O ANISOU 1397 OE1 GLN A 250 11830 12337 11476 697 -391 313 O ATOM 1398 NE2 GLN A 250 7.897 29.987 25.659 1.00 79.09 N ANISOU 1398 NE2 GLN A 250 9876 10637 9537 680 -429 323 N ATOM 1399 N VAL A 251 11.996 25.577 24.227 1.00 49.81 N ANISOU 1399 N VAL A 251 6383 6762 5781 490 -367 116 N ATOM 1400 CA VAL A 251 12.711 25.436 22.960 1.00 38.58 C ANISOU 1400 CA VAL A 251 4985 5367 4309 494 -363 116 C ATOM 1401 C VAL A 251 12.481 24.056 22.359 1.00 54.41 C ANISOU 1401 C VAL A 251 7014 7401 6258 433 -372 49 C ATOM 1402 O VAL A 251 12.279 23.918 21.147 1.00 54.20 O ANISOU 1402 O VAL A 251 6981 7447 6165 425 -389 44 O ATOM 1403 CB VAL A 251 14.214 25.710 23.151 1.00 55.31 C ANISOU 1403 CB VAL A 251 7148 7405 6462 527 -330 137 C ATOM 1404 CG1 VAL A 251 14.991 25.347 21.885 1.00 58.91 C ANISOU 1404 CG1 VAL A 251 7631 7892 6861 530 -323 132 C ATOM 1405 CG2 VAL A 251 14.443 27.151 23.491 1.00 65.00 C ANISOU 1405 CG2 VAL A 251 8355 8610 7733 584 -329 208 C ATOM 1406 N VAL A 252 12.536 23.010 23.186 1.00 41.35 N ANISOU 1406 N VAL A 252 5391 5691 4631 389 -362 -5 N ATOM 1407 CA VAL A 252 12.359 21.656 22.670 1.00 42.07 C ANISOU 1407 CA VAL A 252 5515 5796 4674 328 -372 -73 C ATOM 1408 C VAL A 252 10.959 21.488 22.095 1.00 61.70 C ANISOU 1408 C VAL A 252 7958 8380 7106 288 -417 -81 C ATOM 1409 O VAL A 252 10.776 20.871 21.039 1.00 55.73 O ANISOU 1409 O VAL A 252 7218 7675 6282 255 -435 -115 O ATOM 1410 CB VAL A 252 12.649 20.621 23.771 1.00 46.28 C ANISOU 1410 CB VAL A 252 6085 6244 5254 289 -354 -121 C ATOM 1411 CG1 VAL A 252 12.241 19.230 23.317 1.00 58.33 C ANISOU 1411 CG1 VAL A 252 7644 7784 6735 220 -373 -191 C ATOM 1412 CG2 VAL A 252 14.124 20.649 24.147 1.00 48.14 C ANISOU 1412 CG2 VAL A 252 6368 6394 5530 324 -308 -113 C ATOM 1413 N TRP A 253 9.951 22.050 22.770 1.00 46.41 N ANISOU 1413 N TRP A 253 5963 6475 5194 291 -435 -48 N ATOM 1414 CA TRP A 253 8.583 21.957 22.269 1.00 58.43 C ANISOU 1414 CA TRP A 253 7436 8101 6664 253 -477 -43 C ATOM 1415 C TRP A 253 8.424 22.702 20.950 1.00 57.58 C ANISOU 1415 C TRP A 253 7301 8081 6497 283 -491 -5 C ATOM 1416 O TRP A 253 7.794 22.193 20.017 1.00 63.59 O ANISOU 1416 O TRP A 253 8053 8921 7188 238 -521 -26 O ATOM 1417 CB TRP A 253 7.604 22.506 23.305 1.00 64.55 C ANISOU 1417 CB TRP A 253 8152 8896 7478 265 -489 -5 C ATOM 1418 CG TRP A 253 6.882 21.441 24.066 1.00 84.21 C ANISOU 1418 CG TRP A 253 10636 11382 9976 196 -508 -44 C ATOM 1419 CD1 TRP A 253 7.270 20.858 25.238 1.00 82.42 C ANISOU 1419 CD1 TRP A 253 10434 11071 9809 180 -489 -72 C ATOM 1420 CD2 TRP A 253 5.638 20.831 23.707 1.00 74.53 C ANISOU 1420 CD2 TRP A 253 9375 10245 8698 131 -552 -53 C ATOM 1421 NE1 TRP A 253 6.343 19.921 25.630 1.00 85.00 N ANISOU 1421 NE1 TRP A 253 10742 11427 10126 110 -520 -98 N ATOM 1422 CE2 TRP A 253 5.332 19.885 24.706 1.00 87.75 C ANISOU 1422 CE2 TRP A 253 11054 11881 10405 77 -560 -86 C ATOM 1423 CE3 TRP A 253 4.754 20.992 22.637 1.00 72.54 C ANISOU 1423 CE3 TRP A 253 9084 10106 8373 110 -587 -33 C ATOM 1424 CZ2 TRP A 253 4.179 19.105 24.665 1.00 80.92 C ANISOU 1424 CZ2 TRP A 253 10159 11084 9503 1 -605 -97 C ATOM 1425 CZ3 TRP A 253 3.611 20.217 22.599 1.00 86.77 C ANISOU 1425 CZ3 TRP A 253 10856 11977 10136 34 -630 -45 C ATOM 1426 CH2 TRP A 253 3.334 19.285 23.605 1.00 80.02 C ANISOU 1426 CH2 TRP A 253 10009 11079 9315 -21 -640 -76 C ATOM 1427 N ARG A 254 8.978 23.913 20.859 1.00 61.85 N ANISOU 1427 N ARG A 254 7827 8611 7062 355 -472 53 N ATOM 1428 CA ARG A 254 8.855 24.703 19.639 1.00 56.14 C ANISOU 1428 CA ARG A 254 7071 7972 6288 388 -484 99 C ATOM 1429 C ARG A 254 9.390 23.937 18.435 1.00 70.05 C ANISOU 1429 C ARG A 254 8872 9760 7982 360 -486 56 C ATOM 1430 O ARG A 254 8.695 23.775 17.425 1.00 61.99 O ANISOU 1430 O ARG A 254 7826 8837 6891 333 -514 53 O ATOM 1431 CB ARG A 254 9.604 26.027 19.802 1.00 68.80 C ANISOU 1431 CB ARG A 254 8666 9536 7938 467 -461 165 C ATOM 1432 CG ARG A 254 9.342 27.051 18.698 1.00 91.41 C ANISOU 1432 CG ARG A 254 11482 12488 10762 509 -475 228 C ATOM 1433 CD ARG A 254 10.528 27.996 18.491 1.00 94.65 C ANISOU 1433 CD ARG A 254 11908 12850 11203 572 -452 279 C ATOM 1434 NE ARG A 254 11.349 28.155 19.687 1.00 97.90 N ANISOU 1434 NE ARG A 254 12361 13146 11692 592 -426 277 N ATOM 1435 CZ ARG A 254 11.003 28.869 20.751 1.00 98.33 C ANISOU 1435 CZ ARG A 254 12399 13157 11806 621 -423 306 C ATOM 1436 NH1 ARG A 254 9.836 29.489 20.821 1.00103.60 N ANISOU 1436 NH1 ARG A 254 13012 13885 12467 638 -443 340 N ATOM 1437 NH2 ARG A 254 11.848 28.958 21.774 1.00 87.45 N ANISOU 1437 NH2 ARG A 254 11061 11675 10491 634 -400 301 N ATOM 1438 N HIS A 255 10.631 23.453 18.531 1.00 54.30 N ANISOU 1438 N HIS A 255 6942 7685 6006 369 -456 23 N ATOM 1439 CA HIS A 255 11.251 22.764 17.405 1.00 60.27 C ANISOU 1439 CA HIS A 255 7741 8463 6696 356 -453 -16 C ATOM 1440 C HIS A 255 10.457 21.527 17.007 1.00 62.32 C ANISOU 1440 C HIS A 255 8019 8762 6897 278 -483 -87 C ATOM 1441 O HIS A 255 10.252 21.269 15.816 1.00 61.07 O ANISOU 1441 O HIS A 255 7862 8680 6661 261 -502 -104 O ATOM 1442 CB HIS A 255 12.690 22.391 17.756 1.00 60.12 C ANISOU 1442 CB HIS A 255 7786 8344 6711 381 -412 -36 C ATOM 1443 CG HIS A 255 13.578 23.574 17.982 1.00 75.56 C ANISOU 1443 CG HIS A 255 9729 10267 8714 451 -387 36 C ATOM 1444 ND1 HIS A 255 13.185 24.863 17.690 1.00 79.99 N ANISOU 1444 ND1 HIS A 255 10231 10883 9280 493 -401 110 N ATOM 1445 CD2 HIS A 255 14.837 23.666 18.471 1.00 64.20 C ANISOU 1445 CD2 HIS A 255 8328 8745 7319 484 -351 50 C ATOM 1446 CE1 HIS A 255 14.165 25.698 17.988 1.00 74.26 C ANISOU 1446 CE1 HIS A 255 9510 10103 8600 545 -378 163 C ATOM 1447 NE2 HIS A 255 15.179 24.997 18.463 1.00 62.28 N ANISOU 1447 NE2 HIS A 255 8051 8506 7106 539 -348 130 N ATOM 1448 N ALA A 256 10.001 20.746 17.989 1.00 48.44 N ANISOU 1448 N ALA A 256 6276 6954 5174 228 -489 -128 N ATOM 1449 CA ALA A 256 9.192 19.574 17.671 1.00 64.66 C ANISOU 1449 CA ALA A 256 8349 9041 7177 145 -524 -191 C ATOM 1450 C ALA A 256 7.896 19.977 16.977 1.00 70.89 C ANISOU 1450 C ALA A 256 9071 9956 7908 119 -568 -159 C ATOM 1451 O ALA A 256 7.443 19.298 16.046 1.00 61.05 O ANISOU 1451 O ALA A 256 7839 8772 6587 66 -599 -198 O ATOM 1452 CB ALA A 256 8.898 18.778 18.942 1.00 54.11 C ANISOU 1452 CB ALA A 256 7030 7633 5898 97 -526 -225 C ATOM 1453 N ALA A1001 7.293 21.089 17.406 1.00 57.89 N ANISOU 1453 N ALA A1001 7352 8349 6293 157 -571 -87 N ATOM 1454 CA ALA A1001 6.049 21.544 16.794 1.00 60.00 C ANISOU 1454 CA ALA A1001 7548 8742 6509 139 -609 -45 C ATOM 1455 C ALA A1001 6.277 22.035 15.371 1.00 60.71 C ANISOU 1455 C ALA A1001 7624 8913 6530 166 -612 -23 C ATOM 1456 O ALA A1001 5.428 21.831 14.496 1.00 68.40 O ANISOU 1456 O ALA A1001 8567 9991 7430 122 -648 -23 O ATOM 1457 CB ALA A1001 5.422 22.650 17.640 1.00 58.27 C ANISOU 1457 CB ALA A1001 7260 8539 6343 186 -605 29 C ATOM 1458 N ASP A1002 7.410 22.694 15.122 1.00 61.59 N ANISOU 1458 N ASP A1002 7754 8984 6663 236 -578 2 N ATOM 1459 CA ASP A1002 7.695 23.180 13.776 1.00 64.27 C ANISOU 1459 CA ASP A1002 8076 9403 6940 266 -581 29 C ATOM 1460 C ASP A1002 8.039 22.029 12.841 1.00 64.33 C ANISOU 1460 C ASP A1002 8144 9426 6872 220 -591 -48 C ATOM 1461 O ASP A1002 7.642 22.032 11.670 1.00 55.06 O ANISOU 1461 O ASP A1002 6947 8356 5618 204 -614 -46 O ATOM 1462 CB ASP A1002 8.832 24.199 13.819 1.00 53.20 C ANISOU 1462 CB ASP A1002 6675 7953 5584 352 -545 83 C ATOM 1463 CG ASP A1002 8.433 25.486 14.511 1.00 64.33 C ANISOU 1463 CG ASP A1002 8026 9361 7057 403 -541 165 C ATOM 1464 OD1 ASP A1002 7.242 25.629 14.862 1.00 65.29 O ANISOU 1464 OD1 ASP A1002 8097 9532 7177 380 -563 183 O ATOM 1465 OD2 ASP A1002 9.311 26.354 14.704 1.00 67.96 O ANISOU 1465 OD2 ASP A1002 8489 9770 7564 467 -516 212 O ATOM 1466 N LEU A1003 8.777 21.037 13.340 1.00 52.40 N ANISOU 1466 N LEU A1003 6711 7814 5383 199 -572 -117 N ATOM 1467 CA LEU A1003 9.077 19.859 12.535 1.00 57.30 C ANISOU 1467 CA LEU A1003 7400 8436 5933 156 -581 -198 C ATOM 1468 C LEU A1003 7.798 19.145 12.118 1.00 57.98 C ANISOU 1468 C LEU A1003 7474 8600 5956 68 -632 -236 C ATOM 1469 O LEU A1003 7.606 18.825 10.939 1.00 60.37 O ANISOU 1469 O LEU A1003 7785 8982 6171 44 -655 -262 O ATOM 1470 CB LEU A1003 9.993 18.919 13.321 1.00 51.86 C ANISOU 1470 CB LEU A1003 6795 7617 5290 150 -551 -260 C ATOM 1471 CG LEU A1003 10.315 17.576 12.669 1.00 61.77 C ANISOU 1471 CG LEU A1003 8136 8852 6481 107 -557 -353 C ATOM 1472 CD1 LEU A1003 10.942 17.780 11.297 1.00 55.20 C ANISOU 1472 CD1 LEU A1003 7317 8087 5571 151 -549 -352 C ATOM 1473 CD2 LEU A1003 11.229 16.765 13.576 1.00 63.87 C ANISOU 1473 CD2 LEU A1003 8478 8985 6804 111 -522 -400 C ATOM 1474 N GLU A1004 6.903 18.894 13.077 1.00 56.62 N ANISOU 1474 N GLU A1004 7279 8411 5824 18 -653 -235 N ATOM 1475 CA GLU A1004 5.658 18.199 12.771 1.00 63.19 C ANISOU 1475 CA GLU A1004 8095 9316 6597 -74 -706 -262 C ATOM 1476 C GLU A1004 4.771 19.022 11.845 1.00 67.24 C ANISOU 1476 C GLU A1004 8525 9976 7048 -72 -734 -200 C ATOM 1477 O GLU A1004 4.067 18.455 11.002 1.00 65.45 O ANISOU 1477 O GLU A1004 8298 9832 6739 -139 -775 -230 O ATOM 1478 CB GLU A1004 4.922 17.863 14.071 1.00 61.50 C ANISOU 1478 CB GLU A1004 7863 9060 6445 -119 -720 -259 C ATOM 1479 CG GLU A1004 3.864 16.770 13.948 1.00 80.73 C ANISOU 1479 CG GLU A1004 10309 11535 8830 -230 -775 -305 C ATOM 1480 CD GLU A1004 3.349 16.303 15.301 1.00 96.80 C ANISOU 1480 CD GLU A1004 12335 13512 10931 -272 -785 -307 C ATOM 1481 OE1 GLU A1004 3.671 16.956 16.317 1.00 70.15 O ANISOU 1481 OE1 GLU A1004 8934 10082 7636 -213 -751 -265 O ATOM 1482 OE2 GLU A1004 2.628 15.282 15.350 1.00 75.66 O ANISOU 1482 OE2 GLU A1004 9677 10845 8225 -367 -830 -348 O ATOM 1483 N ASP A1005 4.794 20.351 11.975 1.00 63.05 N ANISOU 1483 N ASP A1005 7926 9478 6554 4 -713 -114 N ATOM 1484 CA ASP A1005 4.030 21.198 11.065 1.00 58.02 C ANISOU 1484 CA ASP A1005 7207 8979 5861 15 -733 -47 C ATOM 1485 C ASP A1005 4.548 21.068 9.639 1.00 60.20 C ANISOU 1485 C ASP A1005 7504 9315 6053 22 -736 -71 C ATOM 1486 O ASP A1005 3.813 20.670 8.729 1.00 68.88 O ANISOU 1486 O ASP A1005 8588 10517 7067 -37 -774 -88 O ATOM 1487 CB ASP A1005 4.089 22.659 11.516 1.00 51.62 C ANISOU 1487 CB ASP A1005 6328 8173 5112 103 -706 48 C ATOM 1488 CG ASP A1005 3.272 22.920 12.767 1.00 87.64 C ANISOU 1488 CG ASP A1005 10849 12714 9736 98 -711 83 C ATOM 1489 OD1 ASP A1005 2.303 22.172 13.016 1.00 99.41 O ANISOU 1489 OD1 ASP A1005 12329 14240 11201 21 -746 60 O ATOM 1490 OD2 ASP A1005 3.597 23.881 13.499 1.00 97.86 O ANISOU 1490 OD2 ASP A1005 12121 13958 11103 171 -682 136 O ATOM 1491 N ASN A1006 5.823 21.405 9.426 1.00 59.48 N ANISOU 1491 N ASN A1006 7449 9168 5984 94 -696 -70 N ATOM 1492 CA ASN A1006 6.372 21.398 8.074 1.00 62.25 C ANISOU 1492 CA ASN A1006 7812 9585 6256 114 -695 -82 C ATOM 1493 C ASN A1006 6.317 20.011 7.451 1.00 57.98 C ANISOU 1493 C ASN A1006 7346 9047 5635 40 -720 -184 C ATOM 1494 O ASN A1006 6.164 19.887 6.230 1.00 51.20 O ANISOU 1494 O ASN A1006 6481 8288 4686 25 -740 -197 O ATOM 1495 CB ASN A1006 7.810 21.914 8.091 1.00 62.80 C ANISOU 1495 CB ASN A1006 7910 9584 6366 203 -648 -62 C ATOM 1496 CG ASN A1006 7.898 23.375 8.473 1.00 67.15 C ANISOU 1496 CG ASN A1006 8389 10142 6984 276 -629 42 C ATOM 1497 OD1 ASN A1006 8.629 23.744 9.390 1.00 83.62 O ANISOU 1497 OD1 ASN A1006 10494 12125 9151 322 -598 62 O ATOM 1498 ND2 ASN A1006 7.152 24.218 7.767 1.00 68.94 N ANISOU 1498 ND2 ASN A1006 8532 10488 7174 287 -648 111 N ATOM 1499 N TRP A1007 6.457 18.962 8.262 1.00 48.40 N ANISOU 1499 N TRP A1007 6207 7728 4455 -6 -720 -256 N ATOM 1500 CA TRP A1007 6.340 17.607 7.735 1.00 58.63 C ANISOU 1500 CA TRP A1007 7581 9016 5679 -81 -748 -355 C ATOM 1501 C TRP A1007 4.923 17.332 7.249 1.00 63.55 C ANISOU 1501 C TRP A1007 8162 9751 6234 -172 -807 -356 C ATOM 1502 O TRP A1007 4.730 16.694 6.207 1.00 60.20 O ANISOU 1502 O TRP A1007 7770 9388 5715 -219 -837 -410 O ATOM 1503 CB TRP A1007 6.754 16.600 8.807 1.00 53.72 C ANISOU 1503 CB TRP A1007 7043 8251 5119 -110 -736 -423 C ATOM 1504 CG TRP A1007 6.718 15.169 8.361 1.00 64.09 C ANISOU 1504 CG TRP A1007 8450 9533 6368 -183 -763 -528 C ATOM 1505 CD1 TRP A1007 5.679 14.292 8.498 1.00 64.61 C ANISOU 1505 CD1 TRP A1007 8531 9611 6406 -289 -815 -572 C ATOM 1506 CD2 TRP A1007 7.773 14.443 7.719 1.00 55.14 C ANISOU 1506 CD2 TRP A1007 7411 8349 5189 -157 -740 -602 C ATOM 1507 NE1 TRP A1007 6.021 13.067 7.978 1.00 56.14 N ANISOU 1507 NE1 TRP A1007 7563 8492 5277 -332 -828 -672 N ATOM 1508 CE2 TRP A1007 7.301 13.133 7.493 1.00 52.82 C ANISOU 1508 CE2 TRP A1007 7194 8032 4843 -248 -781 -695 C ATOM 1509 CE3 TRP A1007 9.070 14.772 7.312 1.00 68.05 C ANISOU 1509 CE3 TRP A1007 9075 9959 6821 -63 -690 -596 C ATOM 1510 CZ2 TRP A1007 8.080 12.154 6.878 1.00 59.06 C ANISOU 1510 CZ2 TRP A1007 8092 8769 5578 -243 -771 -786 C ATOM 1511 CZ3 TRP A1007 9.842 13.799 6.701 1.00 55.31 C ANISOU 1511 CZ3 TRP A1007 7562 8302 5151 -55 -678 -681 C ATOM 1512 CH2 TRP A1007 9.345 12.506 6.491 1.00 61.79 C ANISOU 1512 CH2 TRP A1007 8463 9096 5920 -142 -717 -778 C ATOM 1513 N GLU A1008 3.918 17.822 7.981 1.00 58.83 N ANISOU 1513 N GLU A1008 7488 9186 5677 -196 -825 -295 N ATOM 1514 CA GLU A1008 2.532 17.619 7.571 1.00 66.18 C ANISOU 1514 CA GLU A1008 8368 10234 6544 -282 -882 -281 C ATOM 1515 C GLU A1008 2.207 18.415 6.314 1.00 64.52 C ANISOU 1515 C GLU A1008 8087 10171 6256 -260 -892 -226 C ATOM 1516 O GLU A1008 1.543 17.904 5.405 1.00 60.08 O ANISOU 1516 O GLU A1008 7524 9704 5600 -332 -936 -254 O ATOM 1517 CB GLU A1008 1.586 18.012 8.705 1.00 74.21 C ANISOU 1517 CB GLU A1008 9315 11255 7625 -300 -893 -218 C ATOM 1518 CG GLU A1008 0.214 17.361 8.618 1.00 95.54 C ANISOU 1518 CG GLU A1008 11989 14040 10271 -412 -955 -223 C ATOM 1519 CD GLU A1008 0.244 15.887 8.983 1.00113.72 C ANISOU 1519 CD GLU A1008 14386 16252 12570 -502 -983 -320 C ATOM 1520 OE1 GLU A1008 1.223 15.452 9.629 1.00100.15 O ANISOU 1520 OE1 GLU A1008 12742 14397 10913 -471 -949 -372 O ATOM 1521 OE2 GLU A1008 -0.711 15.166 8.623 1.00113.12 O ANISOU 1521 OE2 GLU A1008 14310 16242 12429 -606 -1041 -342 O ATOM 1522 N THR A1009 2.651 19.673 6.248 1.00 62.96 N ANISOU 1522 N THR A1009 7828 9996 6095 -163 -855 -146 N ATOM 1523 CA THR A1009 2.423 20.467 5.045 1.00 78.45 C ANISOU 1523 CA THR A1009 9720 12098 7989 -136 -861 -88 C ATOM 1524 C THR A1009 3.160 19.866 3.856 1.00 62.61 C ANISOU 1524 C THR A1009 7777 10113 5898 -138 -863 -157 C ATOM 1525 O THR A1009 2.659 19.889 2.726 1.00 64.60 O ANISOU 1525 O THR A1009 7994 10494 6057 -169 -891 -150 O ATOM 1526 CB THR A1009 2.867 21.912 5.271 1.00 67.10 C ANISOU 1526 CB THR A1009 8215 10662 6617 -29 -820 10 C ATOM 1527 OG1 THR A1009 4.286 21.953 5.463 1.00 87.78 O ANISOU 1527 OG1 THR A1009 10898 13171 9283 41 -777 -15 O ATOM 1528 CG2 THR A1009 2.171 22.508 6.489 1.00 67.56 C ANISOU 1528 CG2 THR A1009 8220 10692 6759 -18 -817 73 C ATOM 1529 N LEU A1010 4.353 19.321 4.098 1.00 58.57 N ANISOU 1529 N LEU A1010 7358 9482 5415 -103 -831 -222 N ATOM 1530 CA LEU A1010 5.077 18.599 3.059 1.00 55.61 C ANISOU 1530 CA LEU A1010 7056 9116 4957 -103 -830 -298 C ATOM 1531 C LEU A1010 4.220 17.487 2.466 1.00 55.26 C ANISOU 1531 C LEU A1010 7052 9124 4819 -213 -885 -376 C ATOM 1532 O LEU A1010 4.141 17.331 1.243 1.00 53.14 O ANISOU 1532 O LEU A1010 6784 8956 4450 -228 -905 -398 O ATOM 1533 CB LEU A1010 6.370 18.034 3.644 1.00 65.91 C ANISOU 1533 CB LEU A1010 8459 10270 6315 -57 -788 -358 C ATOM 1534 CG LEU A1010 7.307 17.289 2.697 1.00 58.67 C ANISOU 1534 CG LEU A1010 7628 9344 5321 -37 -776 -437 C ATOM 1535 CD1 LEU A1010 7.901 18.254 1.687 1.00 68.18 C ANISOU 1535 CD1 LEU A1010 8776 10646 6484 47 -754 -373 C ATOM 1536 CD2 LEU A1010 8.397 16.590 3.496 1.00 72.20 C ANISOU 1536 CD2 LEU A1010 9440 10900 7094 -5 -737 -495 C ATOM 1537 N ASN A1011 3.568 16.698 3.325 1.00 50.98 N ANISOU 1537 N ASN A1011 6544 8519 4309 -294 -913 -416 N ATOM 1538 CA ASN A1011 2.724 15.614 2.830 1.00 57.77 C ANISOU 1538 CA ASN A1011 7446 9421 5084 -409 -972 -487 C ATOM 1539 C ASN A1011 1.472 16.154 2.151 1.00 61.17 C ANISOU 1539 C ASN A1011 7774 10020 5447 -461 -1015 -420 C ATOM 1540 O ASN A1011 1.056 15.637 1.109 1.00 62.17 O ANISOU 1540 O ASN A1011 7918 10234 5468 -524 -1056 -463 O ATOM 1541 CB ASN A1011 2.341 14.673 3.971 1.00 61.93 C ANISOU 1541 CB ASN A1011 8028 9837 5667 -484 -993 -535 C ATOM 1542 CG ASN A1011 3.546 14.030 4.629 1.00 85.63 C ANISOU 1542 CG ASN A1011 11133 12672 8729 -441 -951 -604 C ATOM 1543 OD1 ASN A1011 4.574 13.807 3.988 1.00 87.87 O ANISOU 1543 OD1 ASN A1011 11481 12926 8978 -387 -922 -653 O ATOM 1544 ND2 ASN A1011 3.425 13.724 5.917 1.00 86.53 N ANISOU 1544 ND2 ASN A1011 11261 12685 8933 -462 -946 -605 N ATOM 1545 N ASP A1012 0.857 17.193 2.722 1.00 53.38 N ANISOU 1545 N ASP A1012 6682 9083 4518 -433 -1007 -315 N ATOM 1546 CA ASP A1012 -0.343 17.765 2.120 1.00 60.44 C ANISOU 1546 CA ASP A1012 7471 10142 5351 -474 -1044 -239 C ATOM 1547 C ASP A1012 -0.097 18.163 0.670 1.00 61.85 C ANISOU 1547 C ASP A1012 7622 10442 5437 -445 -1043 -229 C ATOM 1548 O ASP A1012 -0.848 17.772 -0.231 1.00 57.99 O ANISOU 1548 O ASP A1012 7119 10069 4847 -524 -1090 -245 O ATOM 1549 CB ASP A1012 -0.816 18.975 2.927 1.00 52.07 C ANISOU 1549 CB ASP A1012 6304 9107 4372 -417 -1021 -122 C ATOM 1550 CG ASP A1012 -1.328 18.595 4.303 1.00 71.35 C ANISOU 1550 CG ASP A1012 8755 11464 6890 -457 -1031 -123 C ATOM 1551 OD1 ASP A1012 -1.714 17.422 4.491 1.00 83.66 O ANISOU 1551 OD1 ASP A1012 10376 12989 8423 -556 -1071 -195 O ATOM 1552 OD2 ASP A1012 -1.350 19.470 5.194 1.00 66.38 O ANISOU 1552 OD2 ASP A1012 8071 10804 6346 -391 -1000 -50 O ATOM 1553 N ASN A1013 0.952 18.952 0.428 1.00 52.87 N ANISOU 1553 N ASN A1013 6474 9284 4330 -335 -993 -197 N ATOM 1554 CA ASN A1013 1.218 19.424 -0.926 1.00 60.50 C ANISOU 1554 CA ASN A1013 7402 10372 5213 -298 -989 -175 C ATOM 1555 C ASN A1013 1.600 18.280 -1.851 1.00 58.80 C ANISOU 1555 C ASN A1013 7285 10161 4897 -346 -1012 -289 C ATOM 1556 O ASN A1013 1.268 18.311 -3.040 1.00 60.41 O ANISOU 1556 O ASN A1013 7457 10498 4998 -371 -1037 -288 O ATOM 1557 CB ASN A1013 2.318 20.482 -0.905 1.00 55.06 C ANISOU 1557 CB ASN A1013 6683 9650 4585 -171 -932 -113 C ATOM 1558 CG ASN A1013 1.825 21.817 -0.390 1.00 54.53 C ANISOU 1558 CG ASN A1013 6504 9625 4590 -120 -916 12 C ATOM 1559 OD1 ASN A1013 1.353 22.655 -1.158 1.00 61.61 O ANISOU 1559 OD1 ASN A1013 7306 10658 5445 -101 -922 92 O ATOM 1560 ND2 ASN A1013 1.927 22.020 0.917 1.00 59.41 N ANISOU 1560 ND2 ASN A1013 7133 10125 5314 -95 -894 30 N ATOM 1561 N LEU A1014 2.286 17.263 -1.329 1.00 57.73 N ANISOU 1561 N LEU A1014 7268 9880 4787 -357 -1003 -388 N ATOM 1562 CA LEU A1014 2.612 16.103 -2.149 1.00 63.79 C ANISOU 1562 CA LEU A1014 8142 10638 5459 -403 -1026 -504 C ATOM 1563 C LEU A1014 1.349 15.440 -2.688 1.00 72.37 C ANISOU 1563 C LEU A1014 9222 11821 6452 -532 -1096 -536 C ATOM 1564 O LEU A1014 1.328 14.969 -3.831 1.00 60.75 O ANISOU 1564 O LEU A1014 7785 10429 4869 -564 -1122 -592 O ATOM 1565 CB LEU A1014 3.446 15.118 -1.333 1.00 58.49 C ANISOU 1565 CB LEU A1014 7597 9785 4842 -397 -1005 -598 C ATOM 1566 CG LEU A1014 4.021 13.909 -2.065 1.00 80.59 C ANISOU 1566 CG LEU A1014 10523 12542 7554 -420 -1017 -724 C ATOM 1567 CD1 LEU A1014 4.873 14.348 -3.241 1.00 78.64 C ANISOU 1567 CD1 LEU A1014 10269 12376 7237 -332 -987 -719 C ATOM 1568 CD2 LEU A1014 4.835 13.069 -1.098 1.00 70.46 C ANISOU 1568 CD2 LEU A1014 9352 11074 6344 -404 -988 -797 C ATOM 1569 N LYS A1015 0.278 15.405 -1.888 1.00 66.79 N ANISOU 1569 N LYS A1015 8472 11119 5786 -607 -1128 -498 N ATOM 1570 CA LYS A1015 -0.988 14.878 -2.387 1.00 68.34 C ANISOU 1570 CA LYS A1015 8648 11422 5894 -733 -1198 -509 C ATOM 1571 C LYS A1015 -1.627 15.822 -3.393 1.00 62.60 C ANISOU 1571 C LYS A1015 7801 10889 5096 -726 -1210 -418 C ATOM 1572 O LYS A1015 -2.286 15.372 -4.335 1.00 73.60 O ANISOU 1572 O LYS A1015 9193 12393 6378 -811 -1260 -446 O ATOM 1573 CB LYS A1015 -1.962 14.627 -1.240 1.00 76.37 C ANISOU 1573 CB LYS A1015 9641 12402 6973 -811 -1229 -479 C ATOM 1574 CG LYS A1015 -1.591 13.468 -0.346 1.00 77.68 C ANISOU 1574 CG LYS A1015 9927 12396 7191 -854 -1236 -574 C ATOM 1575 CD LYS A1015 -2.693 13.185 0.667 1.00104.87 C ANISOU 1575 CD LYS A1015 13335 15829 10680 -944 -1277 -538 C ATOM 1576 CE LYS A1015 -2.922 14.372 1.595 1.00106.43 C ANISOU 1576 CE LYS A1015 13421 16041 10975 -869 -1238 -419 C ATOM 1577 NZ LYS A1015 -3.934 14.081 2.647 1.00111.00 N ANISOU 1577 NZ LYS A1015 13967 16609 11601 -947 -1274 -383 N ATOM 1578 N VAL A1016 -1.478 17.134 -3.192 1.00 56.80 N ANISOU 1578 N VAL A1016 6962 10196 4422 -630 -1166 -307 N ATOM 1579 CA VAL A1016 -1.977 18.085 -4.180 1.00 66.06 C ANISOU 1579 CA VAL A1016 8019 11550 5532 -611 -1170 -217 C ATOM 1580 C VAL A1016 -1.364 17.791 -5.543 1.00 60.29 C ANISOU 1580 C VAL A1016 7328 10886 4694 -597 -1173 -277 C ATOM 1581 O VAL A1016 -2.058 17.799 -6.567 1.00 64.17 O ANISOU 1581 O VAL A1016 7770 11531 5080 -654 -1210 -262 O ATOM 1582 CB VAL A1016 -1.690 19.528 -3.725 1.00 58.41 C ANISOU 1582 CB VAL A1016 6949 10587 4655 -494 -1116 -96 C ATOM 1583 CG1 VAL A1016 -2.022 20.508 -4.835 1.00 59.14 C ANISOU 1583 CG1 VAL A1016 6928 10858 4683 -462 -1115 -5 C ATOM 1584 CG2 VAL A1016 -2.482 19.850 -2.465 1.00 58.24 C ANISOU 1584 CG2 VAL A1016 6878 10526 4723 -512 -1119 -32 C ATOM 1585 N ILE A1017 -0.060 17.502 -5.574 1.00 57.65 N ANISOU 1585 N ILE A1017 7083 10442 4380 -523 -1134 -345 N ATOM 1586 CA AILE A1017 0.600 17.195 -6.840 0.50 61.61 C ANISOU 1586 CA AILE A1017 7627 11004 4777 -498 -1133 -406 C ATOM 1587 CA BILE A1017 0.608 17.188 -6.836 0.50 61.60 C ANISOU 1587 CA BILE A1017 7627 11001 4776 -498 -1132 -406 C ATOM 1588 C ILE A1017 -0.031 15.966 -7.481 1.00 65.72 C ANISOU 1588 C ILE A1017 8225 11561 5183 -622 -1196 -509 C ATOM 1589 O ILE A1017 -0.408 15.983 -8.659 1.00 66.29 O ANISOU 1589 O ILE A1017 8264 11781 5143 -655 -1224 -511 O ATOM 1590 CB AILE A1017 2.112 17.002 -6.627 0.50 59.45 C ANISOU 1590 CB AILE A1017 7444 10595 4548 -397 -1079 -461 C ATOM 1591 CB BILE A1017 2.115 16.965 -6.611 0.50 59.45 C ANISOU 1591 CB BILE A1017 7448 10591 4548 -399 -1079 -464 C ATOM 1592 CG1AILE A1017 2.742 18.294 -6.101 0.50 56.65 C ANISOU 1592 CG1AILE A1017 7008 10217 4298 -279 -1022 -351 C ATOM 1593 CG1BILE A1017 2.764 18.188 -5.959 0.50 56.59 C ANISOU 1593 CG1BILE A1017 7013 10188 4299 -283 -1022 -360 C ATOM 1594 CG2AILE A1017 2.769 16.566 -7.934 0.50 60.74 C ANISOU 1594 CG2AILE A1017 7660 10822 4594 -372 -1080 -531 C ATOM 1595 CG2BILE A1017 2.798 16.636 -7.935 0.50 60.68 C ANISOU 1595 CG2BILE A1017 7648 10818 4591 -366 -1077 -525 C ATOM 1596 CD1AILE A1017 4.175 18.137 -5.634 0.50 57.83 C ANISOU 1596 CD1AILE A1017 7240 10222 4510 -186 -969 -390 C ATOM 1597 CD1BILE A1017 2.765 19.422 -6.822 0.50 71.07 C ANISOU 1597 CD1BILE A1017 8724 12173 6106 -218 -1006 -251 C ATOM 1598 N GLU A1018 -0.153 14.880 -6.716 1.00 70.79 N ANISOU 1598 N GLU A1018 8972 12071 5853 -693 -1220 -597 N ATOM 1599 CA GLU A1018 -0.670 13.638 -7.277 1.00 76.89 C ANISOU 1599 CA GLU A1018 9836 12856 6521 -813 -1282 -704 C ATOM 1600 C GLU A1018 -2.093 13.800 -7.790 1.00 75.27 C ANISOU 1600 C GLU A1018 9540 12819 6241 -922 -1344 -648 C ATOM 1601 O GLU A1018 -2.472 13.163 -8.779 1.00 76.54 O ANISOU 1601 O GLU A1018 9738 13062 6280 -1001 -1392 -711 O ATOM 1602 CB GLU A1018 -0.592 12.530 -6.226 1.00 74.58 C ANISOU 1602 CB GLU A1018 9662 12384 6289 -870 -1297 -792 C ATOM 1603 CG GLU A1018 0.835 12.208 -5.818 1.00 88.72 C ANISOU 1603 CG GLU A1018 11556 14014 8140 -769 -1239 -858 C ATOM 1604 CD GLU A1018 0.918 11.303 -4.604 1.00116.19 C ANISOU 1604 CD GLU A1018 15131 17315 11702 -813 -1244 -920 C ATOM 1605 OE1 GLU A1018 -0.143 10.930 -4.059 1.00110.10 O ANISOU 1605 OE1 GLU A1018 14344 16545 10945 -922 -1295 -909 O ATOM 1606 OE2 GLU A1018 2.051 10.969 -4.196 1.00 92.05 O ANISOU 1606 OE2 GLU A1018 12159 14120 8695 -737 -1197 -973 O ATOM 1607 N LYS A1019 -2.884 14.659 -7.153 1.00 77.01 N ANISOU 1607 N LYS A1019 9640 13094 6526 -926 -1341 -528 N ATOM 1608 CA ALYS A1019 -4.278 14.861 -7.516 0.50 83.88 C ANISOU 1608 CA ALYS A1019 10413 14126 7333 -1027 -1396 -459 C ATOM 1609 CA BLYS A1019 -4.278 14.857 -7.522 0.50 83.88 C ANISOU 1609 CA BLYS A1019 10413 14126 7332 -1028 -1396 -459 C ATOM 1610 C LYS A1019 -4.494 16.125 -8.341 1.00 81.19 C ANISOU 1610 C LYS A1019 9930 13963 6956 -965 -1373 -343 C ATOM 1611 O LYS A1019 -5.644 16.474 -8.633 1.00 72.69 O ANISOU 1611 O LYS A1019 8753 13033 5831 -1034 -1410 -263 O ATOM 1612 CB ALYS A1019 -5.138 14.909 -6.251 0.50 83.25 C ANISOU 1612 CB ALYS A1019 10290 14000 7339 -1079 -1412 -398 C ATOM 1613 CB BLYS A1019 -5.149 14.893 -6.263 0.50 83.25 C ANISOU 1613 CB BLYS A1019 10291 14002 7338 -1081 -1413 -399 C ATOM 1614 CG ALYS A1019 -5.045 13.645 -5.405 0.50 82.99 C ANISOU 1614 CG ALYS A1019 10387 13802 7343 -1152 -1440 -502 C ATOM 1615 CG BLYS A1019 -4.915 13.725 -5.308 0.50 83.01 C ANISOU 1615 CG BLYS A1019 10390 13790 7361 -1135 -1430 -499 C ATOM 1616 CD ALYS A1019 -5.919 13.703 -4.159 0.50 76.56 C ANISOU 1616 CD ALYS A1019 9522 12956 6612 -1202 -1457 -435 C ATOM 1617 CD BLYS A1019 -5.138 12.374 -5.980 0.50 79.12 C ANISOU 1617 CD BLYS A1019 10013 13288 6761 -1256 -1496 -622 C ATOM 1618 CE ALYS A1019 -5.564 14.883 -3.271 0.50 74.85 C ANISOU 1618 CE ALYS A1019 9221 12701 6516 -1077 -1390 -336 C ATOM 1619 CE BLYS A1019 -4.714 11.227 -5.076 0.50 82.69 C ANISOU 1619 CE BLYS A1019 10603 13544 7273 -1293 -1505 -726 C ATOM 1620 NZ ALYS A1019 -6.381 16.086 -3.593 0.50 64.68 N ANISOU 1620 NZ ALYS A1019 7779 11586 5212 -1053 -1385 -199 N ATOM 1621 NZ BLYS A1019 -3.241 11.213 -4.853 0.50 84.43 N ANISOU 1621 NZ BLYS A1019 10904 13621 7553 -1168 -1437 -786 N ATOM 1622 N ALA A1020 -3.422 16.815 -8.722 1.00 67.26 N ANISOU 1622 N ALA A1020 8152 12189 5212 -838 -1316 -326 N ATOM 1623 CA ALA A1020 -3.562 18.066 -9.454 1.00 76.72 C ANISOU 1623 CA ALA A1020 9213 13547 6389 -772 -1292 -209 C ATOM 1624 C ALA A1020 -4.319 17.851 -10.757 1.00 76.07 C ANISOU 1624 C ALA A1020 9090 13651 6162 -857 -1342 -212 C ATOM 1625 O ALA A1020 -4.165 16.825 -11.426 1.00 64.65 O ANISOU 1625 O ALA A1020 7743 12201 4619 -920 -1378 -327 O ATOM 1626 CB ALA A1020 -2.187 18.668 -9.745 1.00 75.46 C ANISOU 1626 CB ALA A1020 9063 13343 6264 -631 -1229 -205 C ATOM 1627 N ASP A1021 -5.148 18.835 -11.114 1.00 65.27 N ANISOU 1627 N ASP A1021 7576 12448 4777 -857 -1345 -84 N ATOM 1628 CA ASP A1021 -5.854 18.829 -12.386 1.00 88.78 C ANISOU 1628 CA ASP A1021 10491 15623 7619 -926 -1386 -65 C ATOM 1629 C ASP A1021 -5.424 19.949 -13.322 1.00 72.66 C ANISOU 1629 C ASP A1021 8342 13713 5552 -824 -1346 21 C ATOM 1630 O ASP A1021 -5.712 19.870 -14.519 1.00 66.52 O ANISOU 1630 O ASP A1021 7530 13092 4654 -865 -1373 17 O ATOM 1631 CB ASP A1021 -7.371 18.921 -12.159 1.00 74.91 C ANISOU 1631 CB ASP A1021 8644 13981 5839 -1035 -1433 17 C ATOM 1632 CG ASP A1021 -7.772 20.150 -11.367 1.00 97.50 C ANISOU 1632 CG ASP A1021 11378 16860 8805 -962 -1393 164 C ATOM 1633 OD1 ASP A1021 -7.688 21.269 -11.917 1.00 99.26 O ANISOU 1633 OD1 ASP A1021 11490 17195 9029 -880 -1359 267 O ATOM 1634 OD2 ASP A1021 -8.175 19.998 -10.194 1.00112.54 O ANISOU 1634 OD2 ASP A1021 13298 18669 10792 -986 -1397 178 O ATOM 1635 N ASN A1022 -4.748 20.980 -12.815 1.00 70.29 N ANISOU 1635 N ASN A1022 7991 13355 5361 -697 -1285 100 N ATOM 1636 CA ASN A1022 -4.229 22.056 -13.646 1.00 76.25 C ANISOU 1636 CA ASN A1022 8649 14219 6104 -594 -1246 185 C ATOM 1637 C ASN A1022 -2.783 22.345 -13.266 1.00 76.14 C ANISOU 1637 C ASN A1022 8693 14061 6177 -467 -1190 162 C ATOM 1638 O ASN A1022 -2.303 21.948 -12.202 1.00 65.81 O ANISOU 1638 O ASN A1022 7474 12573 4958 -449 -1173 109 O ATOM 1639 CB ASN A1022 -5.070 23.334 -13.518 1.00 74.94 C ANISOU 1639 CB ASN A1022 8322 14170 5981 -566 -1232 350 C ATOM 1640 CG ASN A1022 -5.026 23.925 -12.125 1.00 77.24 C ANISOU 1640 CG ASN A1022 8603 14325 6420 -506 -1197 409 C ATOM 1641 OD1 ASN A1022 -4.075 24.616 -11.762 1.00 84.54 O ANISOU 1641 OD1 ASN A1022 9528 15159 7435 -392 -1147 440 O ATOM 1642 ND2 ASN A1022 -6.065 23.666 -11.340 1.00102.71 N ANISOU 1642 ND2 ASN A1022 11818 17540 9670 -584 -1225 428 N ATOM 1643 N ALA A1023 -2.094 23.058 -14.159 1.00 68.69 N ANISOU 1643 N ALA A1023 7691 13204 5205 -379 -1160 211 N ATOM 1644 CA ALA A1023 -0.668 23.299 -13.977 1.00 70.22 C ANISOU 1644 CA ALA A1023 7935 13283 5462 -261 -1111 192 C ATOM 1645 C ALA A1023 -0.394 24.284 -12.848 1.00 68.67 C ANISOU 1645 C ALA A1023 7696 12979 5416 -178 -1067 286 C ATOM 1646 O ALA A1023 0.658 24.205 -12.202 1.00 59.26 O ANISOU 1646 O ALA A1023 6580 11634 4301 -110 -1033 249 O ATOM 1647 CB ALA A1023 -0.058 23.810 -15.282 1.00 73.17 C ANISOU 1647 CB ALA A1023 8248 13796 5758 -194 -1096 228 C ATOM 1648 N ALA A1024 -1.314 25.217 -12.599 1.00 69.05 N ANISOU 1648 N ALA A1024 7626 13105 5505 -182 -1068 407 N ATOM 1649 CA ALA A1024 -1.092 26.203 -11.546 1.00 66.96 C ANISOU 1649 CA ALA A1024 7321 12739 5380 -100 -1028 497 C ATOM 1650 C ALA A1024 -0.965 25.536 -10.183 1.00 71.94 C ANISOU 1650 C ALA A1024 8059 13178 6098 -123 -1025 423 C ATOM 1651 O ALA A1024 -0.151 25.955 -9.350 1.00 72.91 O ANISOU 1651 O ALA A1024 8212 13164 6328 -43 -987 438 O ATOM 1652 CB ALA A1024 -2.228 27.225 -11.539 1.00 91.31 C ANISOU 1652 CB ALA A1024 10266 15947 8482 -105 -1033 634 C ATOM 1653 N GLN A1025 -1.760 24.492 -9.935 1.00 81.63 N ANISOU 1653 N GLN A1025 9342 14395 7279 -235 -1067 345 N ATOM 1654 CA GLN A1025 -1.700 23.811 -8.646 1.00 72.79 C ANISOU 1654 CA GLN A1025 8318 13101 6239 -263 -1067 277 C ATOM 1655 C GLN A1025 -0.343 23.157 -8.428 1.00 57.47 C ANISOU 1655 C GLN A1025 6504 11008 4324 -217 -1042 174 C ATOM 1656 O GLN A1025 0.191 23.171 -7.313 1.00 56.54 O ANISOU 1656 O GLN A1025 6438 10733 4312 -175 -1014 161 O ATOM 1657 CB GLN A1025 -2.800 22.757 -8.555 1.00 68.91 C ANISOU 1657 CB GLN A1025 7862 12640 5681 -400 -1124 215 C ATOM 1658 CG GLN A1025 -4.202 23.299 -8.624 1.00 85.80 C ANISOU 1658 CG GLN A1025 9880 14925 7796 -454 -1151 319 C ATOM 1659 CD GLN A1025 -5.223 22.188 -8.721 1.00102.82 C ANISOU 1659 CD GLN A1025 12072 17127 9867 -599 -1214 256 C ATOM 1660 OE1 GLN A1025 -5.229 21.421 -9.685 1.00 89.10 O ANISOU 1660 OE1 GLN A1025 10379 15456 8018 -665 -1249 179 O ATOM 1661 NE2 GLN A1025 -6.083 22.082 -7.714 1.00110.78 N ANISOU 1661 NE2 GLN A1025 13064 18101 10928 -649 -1231 287 N ATOM 1662 N VAL A1026 0.225 22.565 -9.481 1.00 61.97 N ANISOU 1662 N VAL A1026 7125 11626 4796 -221 -1050 99 N ATOM 1663 CA VAL A1026 1.479 21.832 -9.333 1.00 57.87 C ANISOU 1663 CA VAL A1026 6731 10970 4288 -178 -1027 -4 C ATOM 1664 C VAL A1026 2.593 22.775 -8.901 1.00 62.33 C ANISOU 1664 C VAL A1026 7273 11457 4952 -52 -970 64 C ATOM 1665 O VAL A1026 3.318 22.511 -7.934 1.00 58.60 O ANISOU 1665 O VAL A1026 6879 10822 4565 -17 -943 26 O ATOM 1666 CB VAL A1026 1.829 21.101 -10.642 1.00 58.92 C ANISOU 1666 CB VAL A1026 6914 11189 4285 -198 -1046 -88 C ATOM 1667 CG1 VAL A1026 3.229 20.511 -10.563 1.00 58.63 C ANISOU 1667 CG1 VAL A1026 6994 11024 4258 -129 -1012 -176 C ATOM 1668 CG2 VAL A1026 0.800 20.016 -10.932 1.00 59.93 C ANISOU 1668 CG2 VAL A1026 7090 11362 4319 -334 -1107 -172 C ATOM 1669 N LYS A1027 2.746 23.893 -9.612 1.00 63.74 N ANISOU 1669 N LYS A1027 7343 11753 5122 17 -953 170 N ATOM 1670 CA ALYS A1027 3.786 24.853 -9.258 0.50 65.85 C ANISOU 1670 CA ALYS A1027 7584 11954 5482 132 -905 244 C ATOM 1671 CA BLYS A1027 3.787 24.850 -9.255 0.50 65.85 C ANISOU 1671 CA BLYS A1027 7584 11953 5482 132 -905 244 C ATOM 1672 C LYS A1027 3.569 25.405 -7.854 1.00 64.90 C ANISOU 1672 C LYS A1027 7451 11711 5495 150 -887 298 C ATOM 1673 O LYS A1027 4.522 25.540 -7.079 1.00 66.62 O ANISOU 1673 O LYS A1027 7721 11790 5801 212 -853 293 O ATOM 1674 CB ALYS A1027 3.818 25.985 -10.287 0.50 72.43 C ANISOU 1674 CB ALYS A1027 8293 12947 6282 191 -897 359 C ATOM 1675 CB BLYS A1027 3.832 25.982 -10.279 0.50 72.43 C ANISOU 1675 CB BLYS A1027 8294 12945 6283 192 -897 358 C ATOM 1676 CG ALYS A1027 4.893 27.034 -10.041 0.50 74.93 C ANISOU 1676 CG ALYS A1027 8574 13208 6687 307 -854 446 C ATOM 1677 CG BLYS A1027 4.412 25.568 -11.619 0.50 70.61 C ANISOU 1677 CG BLYS A1027 8076 12821 5931 207 -902 313 C ATOM 1678 CD ALYS A1027 6.294 26.464 -10.191 0.50 70.17 C ANISOU 1678 CD ALYS A1027 8066 12525 6071 361 -829 375 C ATOM 1679 CD BLYS A1027 4.571 26.752 -12.555 0.50 79.33 C ANISOU 1679 CD BLYS A1027 9052 14074 7015 275 -891 436 C ATOM 1680 CE ALYS A1027 7.345 27.497 -9.829 0.50 69.31 C ANISOU 1680 CE ALYS A1027 7925 12354 6058 467 -790 468 C ATOM 1681 CE BLYS A1027 3.233 27.360 -12.927 0.50 77.63 C ANISOU 1681 CE BLYS A1027 8718 14007 6772 223 -917 521 C ATOM 1682 NZ ALYS A1027 7.200 28.745 -10.626 0.50 67.97 N ANISOU 1682 NZ ALYS A1027 7621 12326 5880 516 -789 601 N ATOM 1683 NZ BLYS A1027 3.409 28.559 -13.785 0.50 72.96 N ANISOU 1683 NZ BLYS A1027 7997 13553 6170 294 -904 650 N ATOM 1684 N ASP A1028 2.320 25.729 -7.509 1.00 66.89 N ANISOU 1684 N ASP A1028 7636 12018 5763 96 -910 351 N ATOM 1685 CA ASP A1028 2.030 26.240 -6.173 1.00 62.92 C ANISOU 1685 CA ASP A1028 7120 11406 5379 114 -894 400 C ATOM 1686 C ASP A1028 2.439 25.236 -5.104 1.00 61.80 C ANISOU 1686 C ASP A1028 7102 11090 5289 85 -889 296 C ATOM 1687 O ASP A1028 3.090 25.591 -4.115 1.00 66.83 O ANISOU 1687 O ASP A1028 7767 11594 6031 143 -857 312 O ATOM 1688 CB ASP A1028 0.543 26.572 -6.045 1.00 72.87 C ANISOU 1688 CB ASP A1028 8293 12768 6627 54 -922 465 C ATOM 1689 CG ASP A1028 0.133 27.762 -6.891 1.00111.20 C ANISOU 1689 CG ASP A1028 13015 17781 11457 98 -918 590 C ATOM 1690 OD1 ASP A1028 1.022 28.395 -7.501 1.00110.07 O ANISOU 1690 OD1 ASP A1028 12845 17660 11316 176 -894 632 O ATOM 1691 OD2 ASP A1028 -1.080 28.065 -6.944 1.00107.09 O ANISOU 1691 OD2 ASP A1028 12412 17364 10912 53 -939 653 O ATOM 1692 N ALA A1029 2.063 23.969 -5.288 1.00 58.10 N ANISOU 1692 N ALA A1029 6708 10621 4748 -7 -923 189 N ATOM 1693 CA ALA A1029 2.350 22.960 -4.276 1.00 53.91 C ANISOU 1693 CA ALA A1029 6291 9928 4264 -43 -923 91 C ATOM 1694 C ALA A1029 3.845 22.696 -4.167 1.00 58.06 C ANISOU 1694 C ALA A1029 6905 10336 4821 30 -883 38 C ATOM 1695 O ALA A1029 4.360 22.464 -3.068 1.00 56.10 O ANISOU 1695 O ALA A1029 6718 9936 4661 50 -860 10 O ATOM 1696 CB ALA A1029 1.594 21.673 -4.596 1.00 65.51 C ANISOU 1696 CB ALA A1029 7820 11427 5643 -162 -973 -7 C ATOM 1697 N LEU A1030 4.561 22.727 -5.293 1.00 57.95 N ANISOU 1697 N LEU A1030 6893 10394 4733 73 -874 28 N ATOM 1698 CA LEU A1030 6.007 22.544 -5.242 1.00 59.46 C ANISOU 1698 CA LEU A1030 7158 10487 4948 151 -834 -9 C ATOM 1699 C LEU A1030 6.682 23.700 -4.518 1.00 52.43 C ANISOU 1699 C LEU A1030 6219 9529 4171 244 -793 90 C ATOM 1700 O LEU A1030 7.685 23.503 -3.823 1.00 55.62 O ANISOU 1700 O LEU A1030 6692 9800 4640 290 -761 63 O ATOM 1701 CB LEU A1030 6.575 22.403 -6.651 1.00 55.50 C ANISOU 1701 CB LEU A1030 6657 10096 4335 183 -835 -30 C ATOM 1702 CG LEU A1030 6.313 21.072 -7.352 1.00 59.15 C ANISOU 1702 CG LEU A1030 7205 10588 4681 107 -868 -156 C ATOM 1703 CD1 LEU A1030 6.749 21.151 -8.808 1.00 56.06 C ANISOU 1703 CD1 LEU A1030 6791 10335 4176 145 -869 -157 C ATOM 1704 CD2 LEU A1030 7.031 19.941 -6.628 1.00 54.96 C ANISOU 1704 CD2 LEU A1030 6816 9889 4179 101 -853 -268 C ATOM 1705 N THR A1031 6.154 24.914 -4.677 1.00 64.66 N ANISOU 1705 N THR A1031 7652 11168 5747 272 -795 206 N ATOM 1706 CA THR A1031 6.740 26.064 -4.000 1.00 58.74 C ANISOU 1706 CA THR A1031 6859 10352 5106 356 -760 302 C ATOM 1707 C THR A1031 6.590 25.945 -2.490 1.00 56.85 C ANISOU 1707 C THR A1031 6664 9962 4974 342 -750 286 C ATOM 1708 O THR A1031 7.519 26.268 -1.740 1.00 65.74 O ANISOU 1708 O THR A1031 7823 10971 6185 401 -718 303 O ATOM 1709 CB THR A1031 6.092 27.354 -4.499 1.00 72.95 C ANISOU 1709 CB THR A1031 8529 12280 6910 385 -767 429 C ATOM 1710 OG1 THR A1031 6.337 27.502 -5.903 1.00 69.33 O ANISOU 1710 OG1 THR A1031 8025 11963 6355 405 -774 449 O ATOM 1711 CG2 THR A1031 6.657 28.556 -3.756 1.00 62.46 C ANISOU 1711 CG2 THR A1031 7163 10871 5696 468 -736 527 C ATOM 1712 N LYS A1032 5.431 25.477 -2.024 1.00 59.90 N ANISOU 1712 N LYS A1032 7049 10354 5355 262 -779 257 N ATOM 1713 CA LYS A1032 5.240 25.289 -0.592 1.00 52.97 C ANISOU 1713 CA LYS A1032 6211 9342 4572 245 -771 238 C ATOM 1714 C LYS A1032 6.064 24.120 -0.068 1.00 57.73 C ANISOU 1714 C LYS A1032 6937 9810 5188 227 -759 128 C ATOM 1715 O LYS A1032 6.562 24.175 1.062 1.00 57.94 O ANISOU 1715 O LYS A1032 7002 9703 5308 255 -733 125 O ATOM 1716 CB LYS A1032 3.755 25.085 -0.288 1.00 58.52 C ANISOU 1716 CB LYS A1032 6873 10104 5259 163 -808 244 C ATOM 1717 CG LYS A1032 2.894 26.286 -0.656 1.00 66.73 C ANISOU 1717 CG LYS A1032 7789 11271 6296 187 -815 362 C ATOM 1718 CD LYS A1032 1.418 25.932 -0.733 1.00 80.47 C ANISOU 1718 CD LYS A1032 9482 13110 7982 98 -856 366 C ATOM 1719 CE LYS A1032 0.603 27.099 -1.279 1.00 85.34 C ANISOU 1719 CE LYS A1032 9973 13872 8582 125 -861 487 C ATOM 1720 NZ LYS A1032 -0.789 26.704 -1.637 1.00 96.03 N ANISOU 1720 NZ LYS A1032 11276 15355 9859 34 -903 494 N ATOM 1721 N MET A1033 6.232 23.062 -0.865 1.00 52.54 N ANISOU 1721 N MET A1033 6343 9182 4437 184 -775 37 N ATOM 1722 CA MET A1033 7.044 21.938 -0.410 1.00 54.95 C ANISOU 1722 CA MET A1033 6769 9357 4752 174 -760 -67 C ATOM 1723 C MET A1033 8.488 22.362 -0.189 1.00 57.59 C ANISOU 1723 C MET A1033 7131 9609 5141 271 -711 -42 C ATOM 1724 O MET A1033 9.138 21.910 0.761 1.00 67.80 O ANISOU 1724 O MET A1033 8495 10764 6500 283 -687 -83 O ATOM 1725 CB MET A1033 6.983 20.789 -1.413 1.00 60.37 C ANISOU 1725 CB MET A1033 7521 10096 5320 119 -787 -168 C ATOM 1726 CG MET A1033 5.687 20.014 -1.391 1.00 65.15 C ANISOU 1726 CG MET A1033 8135 10740 5878 4 -838 -219 C ATOM 1727 SD MET A1033 5.724 18.611 -2.527 1.00 68.98 S ANISOU 1727 SD MET A1033 8719 11266 6227 -61 -871 -348 S ATOM 1728 CE MET A1033 7.018 17.610 -1.798 1.00 62.31 C ANISOU 1728 CE MET A1033 8015 10230 5429 -26 -833 -447 C ATOM 1729 N ARG A1034 9.010 23.230 -1.057 1.00 62.64 N ANISOU 1729 N ARG A1034 7710 10336 5753 340 -698 29 N ATOM 1730 CA ARG A1034 10.386 23.685 -0.900 1.00 63.71 C ANISOU 1730 CA ARG A1034 7864 10407 5937 430 -655 66 C ATOM 1731 C ARG A1034 10.562 24.427 0.418 1.00 60.83 C ANISOU 1731 C ARG A1034 7483 9930 5699 461 -634 127 C ATOM 1732 O ARG A1034 11.525 24.188 1.155 1.00 69.27 O ANISOU 1732 O ARG A1034 8614 10878 6826 494 -602 107 O ATOM 1733 CB ARG A1034 10.785 24.579 -2.073 1.00 56.99 C ANISOU 1733 CB ARG A1034 6936 9683 5035 493 -652 147 C ATOM 1734 CG ARG A1034 12.266 24.921 -2.074 1.00 80.11 C ANISOU 1734 CG ARG A1034 9886 12559 7993 582 -612 183 C ATOM 1735 CD ARG A1034 12.647 25.845 -3.217 1.00 72.48 C ANISOU 1735 CD ARG A1034 8835 11725 6981 644 -611 274 C ATOM 1736 NE ARG A1034 14.091 26.045 -3.283 1.00 92.47 N ANISOU 1736 NE ARG A1034 11390 14215 9528 724 -577 306 N ATOM 1737 CZ ARG A1034 14.767 26.906 -2.533 1.00 90.26 C ANISOU 1737 CZ ARG A1034 11090 13857 9347 774 -555 388 C ATOM 1738 NH1 ARG A1034 14.162 27.669 -1.638 1.00100.50 N ANISOU 1738 NH1 ARG A1034 12348 15100 10737 760 -562 442 N ATOM 1739 NH2 ARG A1034 16.085 27.002 -2.685 1.00 99.11 N ANISOU 1739 NH2 ARG A1034 12234 14955 10470 841 -527 418 N ATOM 1740 N ALA A1035 9.633 25.331 0.733 1.00 60.65 N ANISOU 1740 N ALA A1035 7377 9948 5719 452 -649 203 N ATOM 1741 CA ALA A1035 9.732 26.092 1.973 1.00 62.75 C ANISOU 1741 CA ALA A1035 7628 10113 6103 484 -630 260 C ATOM 1742 C ALA A1035 9.581 25.180 3.184 1.00 66.70 C ANISOU 1742 C ALA A1035 8204 10485 6653 435 -627 181 C ATOM 1743 O ALA A1035 10.345 25.280 4.151 1.00 72.96 O ANISOU 1743 O ALA A1035 9038 11157 7529 468 -598 184 O ATOM 1744 CB ALA A1035 8.674 27.195 1.994 1.00 59.65 C ANISOU 1744 CB ALA A1035 7133 9798 5734 487 -648 353 C ATOM 1745 N ALA A1036 8.593 24.284 3.147 1.00 61.80 N ANISOU 1745 N ALA A1036 7602 9894 5985 352 -658 113 N ATOM 1746 CA ALA A1036 8.385 23.366 4.261 1.00 62.03 C ANISOU 1746 CA ALA A1036 7699 9810 6059 299 -659 41 C ATOM 1747 C ALA A1036 9.600 22.471 4.471 1.00 75.13 C ANISOU 1747 C ALA A1036 9462 11361 7725 315 -631 -35 C ATOM 1748 O ALA A1036 9.990 22.199 5.612 1.00 71.98 O ANISOU 1748 O ALA A1036 9109 10837 7404 318 -610 -56 O ATOM 1749 CB ALA A1036 7.135 22.523 4.014 1.00 60.99 C ANISOU 1749 CB ALA A1036 7568 9742 5862 202 -704 -15 C ATOM 1750 N ALA A1037 10.210 22.001 3.382 1.00 63.47 N ANISOU 1750 N ALA A1037 8020 9932 6165 330 -628 -75 N ATOM 1751 CA ALA A1037 11.387 21.150 3.514 1.00 73.48 C ANISOU 1751 CA ALA A1037 9385 11103 7430 354 -597 -143 C ATOM 1752 C ALA A1037 12.510 21.881 4.238 1.00 81.41 C ANISOU 1752 C ALA A1037 10388 12022 8523 432 -553 -80 C ATOM 1753 O ALA A1037 13.155 21.318 5.131 1.00 77.00 O ANISOU 1753 O ALA A1037 9896 11341 8018 436 -527 -120 O ATOM 1754 CB ALA A1037 11.852 20.680 2.135 1.00 76.33 C ANISOU 1754 CB ALA A1037 9774 11548 7679 371 -599 -184 C ATOM 1755 N LEU A1038 12.756 23.139 3.870 1.00 79.67 N ANISOU 1755 N LEU A1038 10090 11863 8319 493 -546 21 N ATOM 1756 CA LEU A1038 13.813 23.904 4.523 1.00 86.53 C ANISOU 1756 CA LEU A1038 10954 12654 9270 562 -511 89 C ATOM 1757 C LEU A1038 13.471 24.191 5.980 1.00 83.58 C ANISOU 1757 C LEU A1038 10579 12175 9002 545 -505 105 C ATOM 1758 O LEU A1038 14.326 24.046 6.863 1.00 84.27 O ANISOU 1758 O LEU A1038 10714 12150 9154 567 -475 99 O ATOM 1759 CB LEU A1038 14.059 25.202 3.754 1.00 78.86 C ANISOU 1759 CB LEU A1038 9897 11776 8290 623 -512 197 C ATOM 1760 CG LEU A1038 14.697 25.006 2.378 1.00 75.58 C ANISOU 1760 CG LEU A1038 9481 11459 7776 658 -509 194 C ATOM 1761 CD1 LEU A1038 14.670 26.292 1.571 1.00 97.89 C ANISOU 1761 CD1 LEU A1038 12208 14395 10590 706 -519 306 C ATOM 1762 CD2 LEU A1038 16.125 24.498 2.518 1.00 80.87 C ANISOU 1762 CD2 LEU A1038 10223 12053 8449 706 -471 171 C ATOM 1763 N ASP A1039 12.227 24.591 6.256 1.00 80.54 N ANISOU 1763 N ASP A1039 10137 11829 8634 507 -534 127 N ATOM 1764 CA ASP A1039 11.831 24.859 7.635 1.00 81.02 C ANISOU 1764 CA ASP A1039 10194 11799 8789 494 -530 141 C ATOM 1765 C ASP A1039 11.917 23.600 8.487 1.00 85.74 C ANISOU 1765 C ASP A1039 10875 12295 9408 444 -522 47 C ATOM 1766 O ASP A1039 12.357 23.651 9.642 1.00 95.37 O ANISOU 1766 O ASP A1039 12121 13405 10709 457 -499 50 O ATOM 1767 CB ASP A1039 10.417 25.436 7.675 1.00 64.85 C ANISOU 1767 CB ASP A1039 8070 9828 6741 465 -562 181 C ATOM 1768 CG ASP A1039 10.335 26.818 7.059 1.00 94.23 C ANISOU 1768 CG ASP A1039 11708 13633 10465 522 -565 287 C ATOM 1769 OD1 ASP A1039 11.359 27.536 7.070 1.00 89.78 O ANISOU 1769 OD1 ASP A1039 11143 13030 9939 586 -542 341 O ATOM 1770 OD2 ASP A1039 9.247 27.188 6.564 1.00 96.55 O ANISOU 1770 OD2 ASP A1039 11934 14031 10721 502 -592 319 O ATOM 1771 N ALA A1040 11.496 22.457 7.939 1.00 74.32 N ANISOU 1771 N ALA A1040 9470 10881 7888 384 -542 -37 N ATOM 1772 CA ALA A1040 11.635 21.203 8.670 1.00 83.52 C ANISOU 1772 CA ALA A1040 10718 11945 9070 336 -536 -127 C ATOM 1773 C ALA A1040 13.096 20.886 8.950 1.00 85.01 C ANISOU 1773 C ALA A1040 10975 12038 9287 387 -491 -144 C ATOM 1774 O ALA A1040 13.418 20.312 9.997 1.00 86.63 O ANISOU 1774 O ALA A1040 11231 12134 9552 372 -472 -180 O ATOM 1775 CB ALA A1040 10.986 20.060 7.889 1.00 67.01 C ANISOU 1775 CB ALA A1040 8666 9907 6887 265 -570 -212 C ATOM 1776 N GLN A1041 13.993 21.254 8.033 1.00 76.23 N ANISOU 1776 N GLN A1041 9860 10971 8131 447 -473 -113 N ATOM 1777 CA GLN A1041 15.418 21.034 8.256 1.00 77.98 C ANISOU 1777 CA GLN A1041 10139 11116 8376 502 -429 -115 C ATOM 1778 C GLN A1041 15.923 21.880 9.419 1.00 89.34 C ANISOU 1778 C GLN A1041 11555 12471 9921 537 -404 -46 C ATOM 1779 O GLN A1041 16.643 21.383 10.294 1.00 92.45 O ANISOU 1779 O GLN A1041 12003 12759 10364 542 -374 -71 O ATOM 1780 CB GLN A1041 16.196 21.349 6.978 1.00 76.94 C ANISOU 1780 CB GLN A1041 9995 11069 8169 561 -419 -84 C ATOM 1781 CG GLN A1041 17.677 21.024 7.050 1.00 81.13 C ANISOU 1781 CG GLN A1041 10584 11538 8704 620 -373 -84 C ATOM 1782 CD GLN A1041 18.387 21.274 5.735 1.00 80.63 C ANISOU 1782 CD GLN A1041 10506 11573 8558 680 -366 -53 C ATOM 1783 OE1 GLN A1041 18.128 22.267 5.056 1.00 91.79 O ANISOU 1783 OE1 GLN A1041 11841 13083 9952 703 -384 20 O ATOM 1784 NE2 GLN A1041 19.281 20.366 5.363 1.00 86.13 N ANISOU 1784 NE2 GLN A1041 11276 12248 9202 708 -337 -106 N ATOM 1785 N LYS A1042 15.548 23.161 9.451 1.00 87.76 N ANISOU 1785 N LYS A1042 11276 12315 9755 562 -417 42 N ATOM 1786 CA LYS A1042 16.014 24.044 10.516 1.00 82.43 C ANISOU 1786 CA LYS A1042 10582 11561 9176 596 -398 108 C ATOM 1787 C LYS A1042 15.549 23.556 11.884 1.00 93.21 C ANISOU 1787 C LYS A1042 11974 12829 10611 551 -395 65 C ATOM 1788 O LYS A1042 16.309 23.601 12.858 1.00 90.70 O ANISOU 1788 O LYS A1042 11686 12414 10362 569 -367 76 O ATOM 1789 CB LYS A1042 15.525 25.471 10.262 1.00 76.51 C ANISOU 1789 CB LYS A1042 9747 10877 8446 627 -418 203 C ATOM 1790 N ALA A1043 14.302 23.085 11.978 1.00100.67 N ANISOU 1790 N ALA A1043 12907 13805 11537 491 -426 20 N ATOM 1791 CA ALA A1043 13.778 22.613 13.255 1.00 98.37 C ANISOU 1791 CA ALA A1043 12633 13434 11308 447 -427 -17 C ATOM 1792 C ALA A1043 14.494 21.365 13.757 1.00 94.04 C ANISOU 1792 C ALA A1043 12169 12793 10771 424 -402 -92 C ATOM 1793 O ALA A1043 14.391 21.046 14.946 1.00 93.99 O ANISOU 1793 O ALA A1043 12179 12704 10829 400 -393 -111 O ATOM 1794 CB ALA A1043 12.280 22.328 13.136 1.00 95.25 C ANISOU 1794 CB ALA A1043 12203 13108 10881 384 -469 -42 C ATOM 1795 N THR A1044 15.201 20.653 12.887 1.00 87.41 N ANISOU 1795 N THR A1044 11380 11965 9866 433 -389 -134 N ATOM 1796 CA THR A1044 15.965 19.487 13.321 1.00 98.63 C ANISOU 1796 CA THR A1044 12884 13294 11296 421 -360 -201 C ATOM 1797 C THR A1044 17.271 19.944 13.964 1.00110.03 C ANISOU 1797 C THR A1044 14342 14663 12801 481 -314 -151 C ATOM 1798 O THR A1044 18.000 20.742 13.367 1.00110.99 O ANISOU 1798 O THR A1044 14441 14825 12907 539 -302 -87 O ATOM 1799 CB THR A1044 16.260 18.565 12.138 1.00108.17 C ANISOU 1799 CB THR A1044 14149 14543 12409 418 -361 -265 C ATOM 1800 OG1 THR A1044 15.029 18.068 11.596 1.00107.33 O ANISOU 1800 OG1 THR A1044 14034 14501 12244 352 -407 -316 O ATOM 1801 CG2 THR A1044 17.133 17.389 12.567 1.00106.44 C ANISOU 1801 CG2 THR A1044 14020 14225 12198 417 -326 -330 C ATOM 1802 N PRO A1045 17.599 19.473 15.168 1.00120.18 N ANISOU 1802 N PRO A1045 15661 15846 14155 465 -291 -172 N ATOM 1803 CA PRO A1045 18.847 19.897 15.793 1.00109.46 C ANISOU 1803 CA PRO A1045 14316 14422 12852 516 -248 -120 C ATOM 1804 C PRO A1045 20.032 19.542 14.915 1.00122.30 C ANISOU 1804 C PRO A1045 15986 16063 14421 564 -218 -120 C ATOM 1805 O PRO A1045 19.984 18.563 14.146 1.00129.01 O ANISOU 1805 O PRO A1045 16883 16935 15199 551 -220 -188 O ATOM 1806 CB PRO A1045 18.864 19.118 17.116 1.00108.79 C ANISOU 1806 CB PRO A1045 14268 14234 12835 477 -230 -163 C ATOM 1807 CG PRO A1045 17.927 17.978 16.911 1.00102.19 C ANISOU 1807 CG PRO A1045 13462 13406 11960 413 -257 -250 C ATOM 1808 CD PRO A1045 16.865 18.510 16.009 1.00108.77 C ANISOU 1808 CD PRO A1045 14244 14346 12740 398 -302 -239 C ATOM 1809 N PRO A1046 21.112 20.309 14.994 1.00139.35 N ANISOU 1809 N PRO A1046 18131 18212 16604 621 -191 -44 N ATOM 1810 CA PRO A1046 22.236 20.113 14.071 1.00141.88 C ANISOU 1810 CA PRO A1046 18479 18566 16863 677 -163 -27 C ATOM 1811 C PRO A1046 23.069 18.887 14.427 1.00149.77 C ANISOU 1811 C PRO A1046 19558 19491 17858 681 -121 -82 C ATOM 1812 O PRO A1046 22.886 18.244 15.461 1.00149.58 O ANISOU 1812 O PRO A1046 19564 19383 17888 641 -110 -125 O ATOM 1813 CB PRO A1046 23.045 21.404 14.234 1.00140.96 C ANISOU 1813 CB PRO A1046 18315 18456 16786 727 -153 84 C ATOM 1814 CG PRO A1046 22.771 21.827 15.639 1.00137.29 C ANISOU 1814 CG PRO A1046 17835 17910 16419 698 -154 103 C ATOM 1815 CD PRO A1046 21.340 21.445 15.906 1.00126.63 C ANISOU 1815 CD PRO A1046 16476 16563 15076 639 -187 37 C ATOM 1816 N LYS A1047 24.013 18.578 13.533 1.00146.46 N ANISOU 1816 N LYS A1047 19168 19108 17370 734 -95 -76 N ATOM 1817 CA LYS A1047 24.857 17.398 13.706 1.00148.11 C ANISOU 1817 CA LYS A1047 19456 19257 17563 750 -51 -126 C ATOM 1818 C LYS A1047 25.796 17.558 14.895 1.00147.09 C ANISOU 1818 C LYS A1047 19332 19043 17513 765 -10 -73 C ATOM 1819 O LYS A1047 25.780 16.748 15.829 1.00142.57 O ANISOU 1819 O LYS A1047 18800 18384 16987 732 10 -121 O ATOM 1820 CB LYS A1047 25.660 17.134 12.430 1.00137.15 C ANISOU 1820 CB LYS A1047 18095 17940 16077 815 -31 -122 C ATOM 1821 N LEU A1048 26.631 18.597 14.874 1.00146.89 N ANISOU 1821 N LEU A1048 19262 19044 17504 812 2 30 N ATOM 1822 CA LEU A1048 27.665 18.760 15.889 1.00135.60 C ANISOU 1822 CA LEU A1048 17838 17546 16139 829 41 88 C ATOM 1823 C LEU A1048 28.516 19.993 15.610 1.00117.58 C ANISOU 1823 C LEU A1048 15504 15313 13860 877 43 207 C ATOM 1824 O LEU A1048 28.210 20.776 14.705 1.00114.23 O ANISOU 1824 O LEU A1048 15034 14971 13398 895 10 245 O ATOM 1825 CB LEU A1048 28.550 17.513 15.948 1.00116.23 C ANISOU 1825 CB LEU A1048 15457 15048 13657 854 94 47 C ATOM 1826 N GLU A1049 29.587 20.166 16.380 1.00107.17 N ANISOU 1826 N GLU A1049 14189 13945 12586 895 78 271 N ATOM 1827 CA GLU A1049 30.462 21.326 16.242 1.00 86.54 C ANISOU 1827 CA GLU A1049 11529 11370 9983 933 76 392 C ATOM 1828 C GLU A1049 31.918 20.941 16.482 1.00 92.49 C ANISOU 1828 C GLU A1049 12310 12105 10728 974 129 446 C ATOM 1829 O GLU A1049 32.481 21.221 17.540 1.00 78.39 O ANISOU 1829 O GLU A1049 10520 10257 9008 958 147 495 O ATOM 1830 CB GLU A1049 30.048 22.429 17.215 1.00 73.99 C ANISOU 1830 CB GLU A1049 9896 9735 8483 895 47 440 C ATOM 1831 N MET A1058 23.693 14.400 14.864 1.00120.76 N ANISOU 1831 N MET A1058 16142 15621 14121 625 -48 -356 N ATOM 1832 CA MET A1058 23.785 13.760 13.556 1.00138.90 C ANISOU 1832 CA MET A1058 18489 17973 16315 649 -52 -411 C ATOM 1833 C MET A1058 23.078 14.606 12.496 1.00140.07 C ANISOU 1833 C MET A1058 18577 18237 16405 649 -97 -387 C ATOM 1834 O MET A1058 22.180 15.387 12.812 1.00135.38 O ANISOU 1834 O MET A1058 17918 17670 15852 610 -134 -356 O ATOM 1835 CB MET A1058 23.181 12.353 13.613 1.00125.97 C ANISOU 1835 CB MET A1058 16930 16277 14656 592 -64 -524 C ATOM 1836 CG MET A1058 23.302 11.561 12.317 1.00129.83 C ANISOU 1836 CG MET A1058 17486 16808 15034 616 -67 -594 C ATOM 1837 SD MET A1058 25.019 11.250 11.853 1.00148.10 S ANISOU 1837 SD MET A1058 19855 19116 17300 726 4 -568 S ATOM 1838 CE MET A1058 25.008 11.667 10.108 1.00123.10 C ANISOU 1838 CE MET A1058 16674 16091 14009 776 -19 -565 C ATOM 1839 N LYS A1059 23.496 14.453 11.239 1.00140.05 N ANISOU 1839 N LYS A1059 18597 18308 16307 698 -93 -398 N ATOM 1840 CA LYS A1059 22.899 15.150 10.102 1.00135.77 C ANISOU 1840 CA LYS A1059 18002 17886 15699 702 -132 -378 C ATOM 1841 C LYS A1059 22.636 14.176 8.958 1.00124.91 C ANISOU 1841 C LYS A1059 16691 16555 14216 697 -147 -471 C ATOM 1842 O LYS A1059 23.022 14.400 7.808 1.00124.02 O ANISOU 1842 O LYS A1059 16570 16532 14018 750 -145 -455 O ATOM 1843 CB LYS A1059 23.788 16.304 9.641 1.00138.26 C ANISOU 1843 CB LYS A1059 18256 18271 16005 778 -114 -269 C ATOM 1844 CG LYS A1059 23.435 17.644 10.269 1.00137.90 C ANISOU 1844 CG LYS A1059 18122 18236 16040 766 -134 -178 C ATOM 1845 CD LYS A1059 24.443 18.725 9.898 1.00131.27 C ANISOU 1845 CD LYS A1059 17229 17449 15197 838 -116 -66 C ATOM 1846 CE LYS A1059 24.239 19.207 8.468 1.00126.47 C ANISOU 1846 CE LYS A1059 16579 16972 14501 869 -142 -42 C ATOM 1847 NZ LYS A1059 25.215 20.262 8.073 1.00112.46 N ANISOU 1847 NZ LYS A1059 14749 15255 12724 937 -128 74 N ATOM 1848 N ASP A1060 21.971 13.063 9.269 1.00124.35 N ANISOU 1848 N ASP A1060 16685 16418 14144 631 -163 -569 N ATOM 1849 CA ASP A1060 21.490 12.124 8.262 1.00108.06 C ANISOU 1849 CA ASP A1060 14687 14389 11983 606 -190 -666 C ATOM 1850 C ASP A1060 20.002 12.304 7.997 1.00114.41 C ANISOU 1850 C ASP A1060 15448 15251 12770 521 -255 -692 C ATOM 1851 O ASP A1060 19.579 12.392 6.840 1.00107.90 O ANISOU 1851 O ASP A1060 14613 14526 11857 518 -286 -712 O ATOM 1852 CB ASP A1060 21.764 10.680 8.695 1.00112.90 C ANISOU 1852 CB ASP A1060 15412 14887 12597 588 -168 -761 C ATOM 1853 CG ASP A1060 21.192 9.665 7.722 1.00104.03 C ANISOU 1853 CG ASP A1060 14366 13785 11375 552 -201 -870 C ATOM 1854 OD1 ASP A1060 21.743 9.529 6.609 1.00115.80 O ANISOU 1854 OD1 ASP A1060 15890 15339 12771 614 -188 -888 O ATOM 1855 OD2 ASP A1060 20.187 9.009 8.068 1.00 92.89 O ANISOU 1855 OD2 ASP A1060 12984 12331 9980 460 -243 -936 O ATOM 1856 N PHE A1061 19.196 12.348 9.060 1.00 99.96 N ANISOU 1856 N PHE A1061 13591 13366 11023 450 -278 -690 N ATOM 1857 CA PHE A1061 17.813 12.783 8.919 1.00 94.11 C ANISOU 1857 CA PHE A1061 12785 12694 10278 378 -337 -684 C ATOM 1858 C PHE A1061 17.751 14.154 8.259 1.00 98.72 C ANISOU 1858 C PHE A1061 13273 13395 10842 422 -346 -593 C ATOM 1859 O PHE A1061 16.871 14.417 7.431 1.00 90.26 O ANISOU 1859 O PHE A1061 12161 12423 9710 390 -389 -596 O ATOM 1860 CB PHE A1061 17.139 12.806 10.292 1.00100.72 C ANISOU 1860 CB PHE A1061 13594 13457 11216 316 -349 -673 C ATOM 1861 CG PHE A1061 15.681 13.162 10.252 1.00 93.99 C ANISOU 1861 CG PHE A1061 12678 12674 10361 241 -408 -665 C ATOM 1862 CD1 PHE A1061 14.768 12.327 9.630 1.00 94.36 C ANISOU 1862 CD1 PHE A1061 12761 12753 10337 167 -456 -742 C ATOM 1863 CD2 PHE A1061 15.220 14.322 10.856 1.00 94.28 C ANISOU 1863 CD2 PHE A1061 12619 12740 10461 245 -416 -580 C ATOM 1864 CE1 PHE A1061 13.424 12.649 9.598 1.00 87.45 C ANISOU 1864 CE1 PHE A1061 11822 11949 9455 96 -510 -726 C ATOM 1865 CE2 PHE A1061 13.878 14.647 10.829 1.00 89.08 C ANISOU 1865 CE2 PHE A1061 11899 12150 9796 182 -467 -567 C ATOM 1866 CZ PHE A1061 12.979 13.809 10.199 1.00 84.96 C ANISOU 1866 CZ PHE A1061 11407 11669 9203 107 -514 -637 C ATOM 1867 N ARG A1062 18.697 15.034 8.601 1.00102.06 N ANISOU 1867 N ARG A1062 13657 13808 11315 494 -306 -507 N ATOM 1868 CA ARG A1062 18.746 16.357 7.987 1.00 99.73 C ANISOU 1868 CA ARG A1062 13272 13616 11006 540 -314 -413 C ATOM 1869 C ARG A1062 19.068 16.263 6.501 1.00 89.49 C ANISOU 1869 C ARG A1062 11985 12422 9595 582 -317 -427 C ATOM 1870 O ARG A1062 18.388 16.877 5.671 1.00104.73 O ANISOU 1870 O ARG A1062 13853 14463 11478 572 -351 -399 O ATOM 1871 CB ARG A1062 19.781 17.229 8.698 1.00113.12 C ANISOU 1871 CB ARG A1062 14934 15267 12778 604 -273 -320 C ATOM 1872 CG ARG A1062 19.207 18.147 9.766 1.00107.40 C ANISOU 1872 CG ARG A1062 14143 14512 12152 578 -286 -258 C ATOM 1873 CD ARG A1062 20.099 19.361 9.968 1.00108.79 C ANISOU 1873 CD ARG A1062 14267 14693 12375 645 -262 -149 C ATOM 1874 NE ARG A1062 19.426 20.433 10.689 1.00110.07 N ANISOU 1874 NE ARG A1062 14357 14851 12612 628 -283 -85 N ATOM 1875 CZ ARG A1062 19.841 21.693 10.713 1.00120.45 C ANISOU 1875 CZ ARG A1062 15613 16190 13963 674 -279 14 C ATOM 1876 NH1 ARG A1062 20.916 22.080 10.045 1.00117.39 N ANISOU 1876 NH1 ARG A1062 15219 15839 13543 737 -258 69 N ATOM 1877 NH2 ARG A1062 19.158 22.588 11.421 1.00116.55 N ANISOU 1877 NH2 ARG A1062 15064 15682 13536 658 -299 61 N ATOM 1878 N HIS A1063 20.111 15.508 6.147 1.00 93.56 N ANISOU 1878 N HIS A1063 12575 12907 10064 633 -279 -466 N ATOM 1879 CA HIS A1063 20.484 15.370 4.743 1.00 95.33 C ANISOU 1879 CA HIS A1063 12815 13232 10176 681 -279 -482 C ATOM 1880 C HIS A1063 19.371 14.734 3.918 1.00 95.10 C ANISOU 1880 C HIS A1063 12808 13262 10062 615 -329 -568 C ATOM 1881 O HIS A1063 19.370 14.865 2.689 1.00 84.43 O ANISOU 1881 O HIS A1063 11443 12022 8615 642 -342 -571 O ATOM 1882 CB HIS A1063 21.774 14.554 4.625 1.00 86.05 C ANISOU 1882 CB HIS A1063 11726 12002 8966 750 -227 -515 C ATOM 1883 CG HIS A1063 22.302 14.446 3.228 1.00 80.71 C ANISOU 1883 CG HIS A1063 11064 11431 8172 815 -220 -524 C ATOM 1884 ND1 HIS A1063 22.080 13.342 2.432 1.00 84.25 N ANISOU 1884 ND1 HIS A1063 11597 11892 8523 802 -231 -634 N ATOM 1885 CD2 HIS A1063 23.048 15.300 2.487 1.00 82.04 C ANISOU 1885 CD2 HIS A1063 11172 11697 8302 895 -203 -437 C ATOM 1886 CE1 HIS A1063 22.663 13.523 1.260 1.00 87.08 C ANISOU 1886 CE1 HIS A1063 11947 12355 8786 875 -220 -616 C ATOM 1887 NE2 HIS A1063 23.257 14.703 1.267 1.00 83.39 N ANISOU 1887 NE2 HIS A1063 11389 11944 8353 932 -203 -494 N ATOM 1888 N GLY A1064 18.426 14.047 4.563 1.00 86.35 N ANISOU 1888 N GLY A1064 11734 12090 8986 525 -358 -635 N ATOM 1889 CA GLY A1064 17.235 13.616 3.855 1.00 83.61 C ANISOU 1889 CA GLY A1064 11392 11809 8567 449 -414 -699 C ATOM 1890 C GLY A1064 16.442 14.780 3.296 1.00 82.61 C ANISOU 1890 C GLY A1064 11151 11811 8423 437 -449 -623 C ATOM 1891 O GLY A1064 15.838 14.670 2.225 1.00 71.04 O ANISOU 1891 O GLY A1064 9676 10449 6866 411 -485 -652 O ATOM 1892 N PHE A1065 16.431 15.910 4.008 1.00 76.90 N ANISOU 1892 N PHE A1065 10344 11086 7789 457 -440 -523 N ATOM 1893 CA PHE A1065 15.792 17.108 3.478 1.00 82.47 C ANISOU 1893 CA PHE A1065 10940 11912 8485 461 -467 -439 C ATOM 1894 C PHE A1065 16.638 17.757 2.390 1.00 79.20 C ANISOU 1894 C PHE A1065 10490 11594 8009 546 -447 -382 C ATOM 1895 O PHE A1065 16.097 18.422 1.499 1.00 79.68 O ANISOU 1895 O PHE A1065 10478 11780 8017 546 -475 -340 O ATOM 1896 CB PHE A1065 15.530 18.112 4.602 1.00 69.82 C ANISOU 1896 CB PHE A1065 9265 10267 6996 460 -463 -353 C ATOM 1897 CG PHE A1065 14.497 17.660 5.595 1.00 71.39 C ANISOU 1897 CG PHE A1065 9474 10402 7250 376 -489 -393 C ATOM 1898 CD1 PHE A1065 13.150 17.718 5.286 1.00 62.98 C ANISOU 1898 CD1 PHE A1065 8362 9416 6151 306 -539 -399 C ATOM 1899 CD2 PHE A1065 14.872 17.190 6.842 1.00 87.82 C ANISOU 1899 CD2 PHE A1065 11603 12350 9413 367 -464 -416 C ATOM 1900 CE1 PHE A1065 12.195 17.308 6.197 1.00 62.48 C ANISOU 1900 CE1 PHE A1065 8301 9303 6135 230 -565 -427 C ATOM 1901 CE2 PHE A1065 13.921 16.779 7.759 1.00 89.92 C ANISOU 1901 CE2 PHE A1065 11871 12565 9729 291 -489 -446 C ATOM 1902 CZ PHE A1065 12.581 16.839 7.435 1.00 81.30 C ANISOU 1902 CZ PHE A1065 10733 11556 8602 223 -540 -451 C ATOM 1903 N ASP A1066 17.961 17.579 2.447 1.00 90.85 N ANISOU 1903 N ASP A1066 12011 13020 9488 620 -400 -374 N ATOM 1904 CA ASP A1066 18.830 18.167 1.433 1.00 80.27 C ANISOU 1904 CA ASP A1066 10636 11776 8088 705 -381 -313 C ATOM 1905 C ASP A1066 18.509 17.621 0.049 1.00 86.24 C ANISOU 1905 C ASP A1066 11412 12642 8713 699 -405 -376 C ATOM 1906 O ASP A1066 18.456 18.377 -0.928 1.00 76.60 O ANISOU 1906 O ASP A1066 10117 11549 7437 731 -418 -317 O ATOM 1907 CB ASP A1066 20.296 17.906 1.782 1.00 79.87 C ANISOU 1907 CB ASP A1066 10639 11651 8058 781 -326 -299 C ATOM 1908 CG ASP A1066 20.802 18.812 2.889 1.00 91.49 C ANISOU 1908 CG ASP A1066 12065 13052 9646 805 -303 -203 C ATOM 1909 OD1 ASP A1066 20.433 20.006 2.897 1.00 83.22 O ANISOU 1909 OD1 ASP A1066 10925 12058 8638 807 -323 -113 O ATOM 1910 OD2 ASP A1066 21.568 18.332 3.751 1.00 91.16 O ANISOU 1910 OD2 ASP A1066 12081 12900 9656 822 -266 -218 O ATOM 1911 N ILE A1067 18.294 16.309 -0.058 1.00 73.76 N ANISOU 1911 N ILE A1067 9933 11013 7080 657 -413 -497 N ATOM 1912 CA ILE A1067 17.968 15.727 -1.353 1.00 86.27 C ANISOU 1912 CA ILE A1067 11547 12695 8535 646 -438 -567 C ATOM 1913 C ILE A1067 16.495 15.909 -1.700 1.00 79.28 C ANISOU 1913 C ILE A1067 10608 11891 7623 554 -498 -578 C ATOM 1914 O ILE A1067 16.133 15.821 -2.879 1.00 73.99 O ANISOU 1914 O ILE A1067 9926 11340 6848 546 -524 -603 O ATOM 1915 CB ILE A1067 18.367 14.242 -1.392 1.00 99.24 C ANISOU 1915 CB ILE A1067 13328 14251 10126 641 -424 -693 C ATOM 1916 CG1 ILE A1067 17.541 13.430 -0.399 1.00 88.67 C ANISOU 1916 CG1 ILE A1067 12048 12795 8847 542 -448 -767 C ATOM 1917 CG2 ILE A1067 19.855 14.081 -1.096 1.00 93.14 C ANISOU 1917 CG2 ILE A1067 12604 13411 9375 739 -361 -672 C ATOM 1918 CD1 ILE A1067 16.436 12.665 -1.054 1.00 87.69 C ANISOU 1918 CD1 ILE A1067 11963 12715 8640 452 -504 -861 C ATOM 1919 N LEU A1068 15.634 16.172 -0.711 1.00 69.72 N ANISOU 1919 N LEU A1068 9363 10627 6501 486 -519 -557 N ATOM 1920 CA LEU A1068 14.257 16.551 -1.016 1.00 68.42 C ANISOU 1920 CA LEU A1068 9125 10555 6314 409 -572 -541 C ATOM 1921 C LEU A1068 14.207 17.924 -1.673 1.00 71.12 C ANISOU 1921 C LEU A1068 9345 11029 6648 457 -574 -425 C ATOM 1922 O LEU A1068 13.551 18.107 -2.704 1.00 60.03 O ANISOU 1922 O LEU A1068 7894 9756 5159 434 -607 -421 O ATOM 1923 CB LEU A1068 13.404 16.545 0.251 1.00 65.91 C ANISOU 1923 CB LEU A1068 8795 10152 6095 336 -590 -536 C ATOM 1924 CG LEU A1068 12.768 15.216 0.656 1.00 79.51 C ANISOU 1924 CG LEU A1068 10610 11795 7805 243 -618 -649 C ATOM 1925 CD1 LEU A1068 12.036 15.378 1.976 1.00 89.12 C ANISOU 1925 CD1 LEU A1068 11796 12936 9127 186 -631 -622 C ATOM 1926 CD2 LEU A1068 11.821 14.715 -0.424 1.00 78.60 C ANISOU 1926 CD2 LEU A1068 10502 11787 7576 171 -672 -707 C ATOM 1927 N VAL A1069 14.887 18.907 -1.080 1.00 60.28 N ANISOU 1927 N VAL A1069 7919 9622 5362 523 -541 -327 N ATOM 1928 CA VAL A1069 14.980 20.220 -1.709 1.00 77.38 C ANISOU 1928 CA VAL A1069 9974 11903 7523 576 -542 -212 C ATOM 1929 C VAL A1069 15.550 20.089 -3.115 1.00 65.52 C ANISOU 1929 C VAL A1069 8473 10517 5905 628 -538 -222 C ATOM 1930 O VAL A1069 15.083 20.744 -4.054 1.00 68.42 O ANISOU 1930 O VAL A1069 8756 11023 6216 631 -561 -170 O ATOM 1931 CB VAL A1069 15.823 21.172 -0.843 1.00 67.52 C ANISOU 1931 CB VAL A1069 8689 10582 6383 641 -506 -115 C ATOM 1932 CG1 VAL A1069 16.047 22.490 -1.569 1.00 70.50 C ANISOU 1932 CG1 VAL A1069 8959 11074 6753 701 -507 5 C ATOM 1933 CG2 VAL A1069 15.144 21.406 0.496 1.00 63.27 C ANISOU 1933 CG2 VAL A1069 8139 9946 5954 592 -513 -101 C ATOM 1934 N GLY A1070 16.561 19.234 -3.284 1.00 68.90 N ANISOU 1934 N GLY A1070 8992 10894 6291 672 -507 -286 N ATOM 1935 CA GLY A1070 17.116 19.023 -4.611 1.00 72.88 C ANISOU 1935 CA GLY A1070 9505 11510 6678 727 -501 -302 C ATOM 1936 C GLY A1070 16.087 18.479 -5.582 1.00 74.00 C ANISOU 1936 C GLY A1070 9653 11753 6711 660 -547 -376 C ATOM 1937 O GLY A1070 15.924 18.995 -6.690 1.00 75.50 O ANISOU 1937 O GLY A1070 9773 12091 6824 681 -563 -335 O ATOM 1938 N GLN A1071 15.373 17.428 -5.173 1.00 67.02 N ANISOU 1938 N GLN A1071 8852 10794 5820 574 -571 -484 N ATOM 1939 CA GLN A1071 14.330 16.869 -6.027 1.00 66.07 C ANISOU 1939 CA GLN A1071 8743 10764 5598 496 -621 -556 C ATOM 1940 C GLN A1071 13.218 17.882 -6.273 1.00 62.75 C ANISOU 1940 C GLN A1071 8195 10461 5187 450 -658 -470 C ATOM 1941 O GLN A1071 12.687 17.973 -7.386 1.00 69.23 O ANISOU 1941 O GLN A1071 8973 11423 5909 429 -688 -472 O ATOM 1942 CB GLN A1071 13.768 15.594 -5.399 1.00 67.42 C ANISOU 1942 CB GLN A1071 9024 10817 5774 406 -644 -676 C ATOM 1943 CG GLN A1071 14.761 14.447 -5.354 1.00 75.91 C ANISOU 1943 CG GLN A1071 10236 11788 6818 447 -611 -776 C ATOM 1944 CD GLN A1071 14.195 13.207 -4.692 1.00 73.84 C ANISOU 1944 CD GLN A1071 10083 11404 6571 355 -636 -889 C ATOM 1945 OE1 GLN A1071 13.112 13.238 -4.112 1.00 87.12 O ANISOU 1945 OE1 GLN A1071 11734 13068 8298 262 -675 -885 O ATOM 1946 NE2 GLN A1071 14.928 12.106 -4.778 1.00 84.11 N ANISOU 1946 NE2 GLN A1071 11510 12618 7829 383 -614 -987 N ATOM 1947 N ILE A1072 12.845 18.650 -5.246 1.00 63.18 N ANISOU 1947 N ILE A1072 8187 10462 5357 436 -655 -392 N ATOM 1948 CA ILE A1072 11.819 19.671 -5.436 1.00 63.49 C ANISOU 1948 CA ILE A1072 8104 10610 5410 403 -685 -302 C ATOM 1949 C ILE A1072 12.306 20.728 -6.419 1.00 60.97 C ANISOU 1949 C ILE A1072 7688 10424 5052 483 -673 -203 C ATOM 1950 O ILE A1072 11.538 21.221 -7.254 1.00 66.41 O ANISOU 1950 O ILE A1072 8293 11256 5683 458 -702 -161 O ATOM 1951 CB ILE A1072 11.418 20.293 -4.086 1.00 61.18 C ANISOU 1951 CB ILE A1072 7771 10224 5249 386 -680 -239 C ATOM 1952 CG1 ILE A1072 10.712 19.251 -3.215 1.00 60.25 C ANISOU 1952 CG1 ILE A1072 7732 10002 5158 294 -702 -331 C ATOM 1953 CG2 ILE A1072 10.510 21.497 -4.309 1.00 63.13 C ANISOU 1953 CG2 ILE A1072 7887 10585 5513 376 -702 -130 C ATOM 1954 CD1 ILE A1072 10.541 19.663 -1.769 1.00 63.87 C ANISOU 1954 CD1 ILE A1072 8174 10347 5748 287 -689 -287 C ATOM 1955 N ASP A1073 13.591 21.087 -6.341 1.00 63.52 N ANISOU 1955 N ASP A1073 8019 10708 5407 578 -629 -159 N ATOM 1956 CA ASP A1073 14.148 22.042 -7.294 1.00 74.69 C ANISOU 1956 CA ASP A1073 9344 12250 6784 656 -619 -62 C ATOM 1957 C ASP A1073 14.161 21.468 -8.705 1.00 54.02 C ANISOU 1957 C ASP A1073 6742 9764 4021 660 -634 -120 C ATOM 1958 O ASP A1073 13.910 22.192 -9.676 1.00 68.27 O ANISOU 1958 O ASP A1073 8449 11720 5770 678 -649 -50 O ATOM 1959 CB ASP A1073 15.561 22.447 -6.873 1.00 73.94 C ANISOU 1959 CB ASP A1073 9262 12082 6751 751 -572 -4 C ATOM 1960 CG ASP A1073 15.576 23.276 -5.604 1.00 87.32 C ANISOU 1960 CG ASP A1073 10922 13670 8587 755 -559 75 C ATOM 1961 OD1 ASP A1073 14.628 24.063 -5.394 1.00 92.29 O ANISOU 1961 OD1 ASP A1073 11470 14335 9260 719 -583 137 O ATOM 1962 OD2 ASP A1073 16.536 23.140 -4.816 1.00102.97 O ANISOU 1962 OD2 ASP A1073 12958 15534 10633 796 -524 77 O ATOM 1963 N ASP A1074 14.457 20.172 -8.840 1.00 55.40 N ANISOU 1963 N ASP A1074 7038 9883 4130 645 -630 -247 N ATOM 1964 CA ASP A1074 14.367 19.530 -10.148 1.00 55.75 C ANISOU 1964 CA ASP A1074 7109 10045 4028 640 -649 -318 C ATOM 1965 C ASP A1074 12.952 19.630 -10.699 1.00 58.27 C ANISOU 1965 C ASP A1074 7368 10479 4293 547 -702 -324 C ATOM 1966 O ASP A1074 12.752 19.978 -11.868 1.00 58.46 O ANISOU 1966 O ASP A1074 7324 10664 4223 559 -719 -294 O ATOM 1967 CB ASP A1074 14.792 18.063 -10.055 1.00 70.77 C ANISOU 1967 CB ASP A1074 9166 11845 5878 630 -640 -463 C ATOM 1968 CG ASP A1074 16.234 17.896 -9.619 1.00 90.39 C ANISOU 1968 CG ASP A1074 11710 14231 8401 728 -585 -457 C ATOM 1969 OD1 ASP A1074 16.986 18.893 -9.646 1.00 89.04 O ANISOU 1969 OD1 ASP A1074 11460 14099 8272 809 -556 -342 O ATOM 1970 OD2 ASP A1074 16.614 16.764 -9.246 1.00 80.39 O ANISOU 1970 OD2 ASP A1074 10571 12849 7123 723 -570 -563 O ATOM 1971 N ALA A1075 11.953 19.322 -9.866 1.00 56.16 N ANISOU 1971 N ALA A1075 7120 10137 4080 452 -730 -357 N ATOM 1972 CA ALA A1075 10.571 19.385 -10.325 1.00 58.02 C ANISOU 1972 CA ALA A1075 7299 10483 4265 357 -781 -357 C ATOM 1973 C ALA A1075 10.152 20.816 -10.624 1.00 56.53 C ANISOU 1973 C ALA A1075 6954 10418 4105 382 -784 -212 C ATOM 1974 O ALA A1075 9.375 21.049 -11.556 1.00 60.22 O ANISOU 1974 O ALA A1075 7350 11039 4491 344 -817 -191 O ATOM 1975 CB ALA A1075 9.636 18.763 -9.287 1.00 56.55 C ANISOU 1975 CB ALA A1075 7163 10188 4136 254 -809 -413 C ATOM 1976 N LEU A1076 10.659 21.784 -9.858 1.00 56.87 N ANISOU 1976 N LEU A1076 6944 10400 4265 446 -752 -112 N ATOM 1977 CA LEU A1076 10.331 23.179 -10.131 1.00 61.88 C ANISOU 1977 CA LEU A1076 7436 11142 4933 478 -753 28 C ATOM 1978 C LEU A1076 10.966 23.648 -11.434 1.00 67.37 C ANISOU 1978 C LEU A1076 8070 11985 5543 549 -745 79 C ATOM 1979 O LEU A1076 10.355 24.417 -12.186 1.00 70.16 O ANISOU 1979 O LEU A1076 8311 12487 5860 543 -763 159 O ATOM 1980 CB LEU A1076 10.777 24.062 -8.967 1.00 59.60 C ANISOU 1980 CB LEU A1076 7120 10738 4789 528 -723 116 C ATOM 1981 CG LEU A1076 9.869 24.015 -7.737 1.00 62.70 C ANISOU 1981 CG LEU A1076 7523 11029 5272 460 -736 108 C ATOM 1982 CD1 LEU A1076 10.556 24.636 -6.531 1.00 79.30 C ANISOU 1982 CD1 LEU A1076 9632 12991 7509 515 -701 165 C ATOM 1983 CD2 LEU A1076 8.547 24.721 -8.016 1.00 68.56 C ANISOU 1983 CD2 LEU A1076 8155 11891 6004 411 -768 180 C ATOM 1984 N LYS A1077 12.189 23.199 -11.722 1.00 61.16 N ANISOU 1984 N LYS A1077 7350 11165 4721 620 -715 39 N ATOM 1985 CA LYS A1077 12.813 23.560 -12.990 1.00 75.29 C ANISOU 1985 CA LYS A1077 9084 13103 6420 690 -708 84 C ATOM 1986 C LYS A1077 11.962 23.083 -14.159 1.00 65.91 C ANISOU 1986 C LYS A1077 7879 12067 5095 630 -747 27 C ATOM 1987 O LYS A1077 11.687 23.843 -15.094 1.00 66.54 O ANISOU 1987 O LYS A1077 7846 12311 5125 647 -759 110 O ATOM 1988 CB LYS A1077 14.224 22.976 -13.077 1.00 67.49 C ANISOU 1988 CB LYS A1077 8184 12053 5405 773 -670 36 C ATOM 1989 CG LYS A1077 15.072 23.616 -14.166 1.00 88.34 C ANISOU 1989 CG LYS A1077 10749 14835 7983 867 -654 119 C ATOM 1990 CD LYS A1077 16.479 23.041 -14.203 1.00103.91 C ANISOU 1990 CD LYS A1077 12806 16748 9927 954 -614 80 C ATOM 1991 CE LYS A1077 16.510 21.663 -14.846 1.00116.13 C ANISOU 1991 CE LYS A1077 14470 18309 11346 938 -620 -71 C ATOM 1992 NZ LYS A1077 16.167 21.705 -16.297 1.00 97.63 N ANISOU 1992 NZ LYS A1077 12067 16161 8865 941 -645 -73 N ATOM 1993 N LEU A1078 11.530 21.820 -14.119 1.00 60.04 N ANISOU 1993 N LEU A1078 7247 11274 4291 557 -768 -111 N ATOM 1994 CA LEU A1078 10.658 21.308 -15.170 1.00 67.65 C ANISOU 1994 CA LEU A1078 8204 12374 5124 486 -811 -172 C ATOM 1995 C LEU A1078 9.376 22.123 -15.263 1.00 62.66 C ANISOU 1995 C LEU A1078 7448 11849 4510 419 -844 -84 C ATOM 1996 O LEU A1078 8.931 22.469 -16.363 1.00 68.50 O ANISOU 1996 O LEU A1078 8103 12765 5159 409 -865 -46 O ATOM 1997 CB LEU A1078 10.330 19.839 -14.913 1.00 64.21 C ANISOU 1997 CB LEU A1078 7916 11840 4640 406 -834 -332 C ATOM 1998 CG LEU A1078 11.496 18.857 -14.990 1.00 67.75 C ANISOU 1998 CG LEU A1078 8500 12198 5046 467 -804 -436 C ATOM 1999 CD1 LEU A1078 11.083 17.520 -14.398 1.00 61.40 C ANISOU 1999 CD1 LEU A1078 7839 11257 4234 380 -826 -579 C ATOM 2000 CD2 LEU A1078 11.951 18.697 -16.430 1.00 62.50 C ANISOU 2000 CD2 LEU A1078 7827 11684 4236 520 -805 -461 C ATOM 2001 N ALA A1079 8.771 22.445 -14.118 1.00 64.28 N ANISOU 2001 N ALA A1079 7637 11955 4829 376 -847 -47 N ATOM 2002 CA ALA A1079 7.502 23.163 -14.141 1.00 70.23 C ANISOU 2002 CA ALA A1079 8279 12807 5599 314 -876 35 C ATOM 2003 C ALA A1079 7.665 24.555 -14.736 1.00 61.68 C ANISOU 2003 C ALA A1079 7050 11854 4533 387 -861 184 C ATOM 2004 O ALA A1079 6.765 25.052 -15.422 1.00 66.97 O ANISOU 2004 O ALA A1079 7616 12676 5152 349 -887 246 O ATOM 2005 CB ALA A1079 6.922 23.248 -12.731 1.00 58.67 C ANISOU 2005 CB ALA A1079 6831 11205 4257 268 -878 48 C ATOM 2006 N ASN A1080 8.807 25.201 -14.487 1.00 78.00 N ANISOU 2006 N ASN A1080 9103 13864 6669 489 -821 249 N ATOM 2007 CA ASN A1080 9.021 26.550 -14.999 1.00 76.41 C ANISOU 2007 CA ASN A1080 8766 13774 6493 559 -809 397 C ATOM 2008 C ASN A1080 9.334 26.557 -16.491 1.00 76.17 C ANISOU 2008 C ASN A1080 8685 13924 6333 593 -815 407 C ATOM 2009 O ASN A1080 9.049 27.551 -17.168 1.00 86.70 O ANISOU 2009 O ASN A1080 9888 15400 7655 617 -821 522 O ATOM 2010 CB ASN A1080 10.141 27.234 -14.216 1.00 72.61 C ANISOU 2010 CB ASN A1080 8289 13171 6130 650 -769 467 C ATOM 2011 CG ASN A1080 9.752 27.520 -12.778 1.00 97.64 C ANISOU 2011 CG ASN A1080 11480 16186 9434 625 -763 487 C ATOM 2012 OD1 ASN A1080 8.605 27.864 -12.490 1.00 90.72 O ANISOU 2012 OD1 ASN A1080 10548 15337 8584 568 -784 521 O ATOM 2013 ND2 ASN A1080 10.706 27.372 -11.865 1.00 95.74 N ANISOU 2013 ND2 ASN A1080 11316 15786 9274 669 -733 467 N ATOM 2014 N GLU A1081 9.906 25.476 -17.021 1.00 65.25 N ANISOU 2014 N GLU A1081 7401 12540 4851 598 -815 290 N ATOM 2015 CA GLU A1081 10.133 25.354 -18.458 1.00 66.57 C ANISOU 2015 CA GLU A1081 7529 12884 4880 625 -824 282 C ATOM 2016 C GLU A1081 8.872 24.985 -19.233 1.00 64.12 C ANISOU 2016 C GLU A1081 7186 12714 4463 526 -869 242 C ATOM 2017 O GLU A1081 8.930 24.879 -20.463 1.00 71.72 O ANISOU 2017 O GLU A1081 8111 13836 5302 539 -881 233 O ATOM 2018 CB GLU A1081 11.217 24.308 -18.735 1.00 63.02 C ANISOU 2018 CB GLU A1081 7206 12381 4359 673 -805 168 C ATOM 2019 CG GLU A1081 12.555 24.629 -18.085 1.00 78.50 C ANISOU 2019 CG GLU A1081 9196 14223 6408 774 -759 212 C ATOM 2020 CD GLU A1081 13.545 23.482 -18.167 1.00 77.46 C ANISOU 2020 CD GLU A1081 9202 14014 6213 817 -737 91 C ATOM 2021 OE1 GLU A1081 13.236 22.468 -18.827 1.00 80.56 O ANISOU 2021 OE1 GLU A1081 9670 14453 6487 775 -758 -29 O ATOM 2022 OE2 GLU A1081 14.634 23.598 -17.568 1.00 87.24 O ANISOU 2022 OE2 GLU A1081 10478 15147 7521 893 -699 117 O ATOM 2023 N GLY A1082 7.743 24.788 -18.558 1.00 72.02 N ANISOU 2023 N GLY A1082 8197 13665 5503 429 -895 220 N ATOM 2024 CA GLY A1082 6.525 24.358 -19.208 1.00 62.35 C ANISOU 2024 CA GLY A1082 6949 12564 4177 324 -941 179 C ATOM 2025 C GLY A1082 6.280 22.867 -19.161 1.00 62.98 C ANISOU 2025 C GLY A1082 7177 12574 4180 242 -970 11 C ATOM 2026 O GLY A1082 5.312 22.399 -19.768 1.00 63.93 O ANISOU 2026 O GLY A1082 7289 12798 4201 147 -1013 -33 O ATOM 2027 N LYS A1083 7.124 22.110 -18.463 1.00 62.54 N ANISOU 2027 N LYS A1083 7255 12344 4163 272 -947 -81 N ATOM 2028 CA LYS A1083 6.989 20.656 -18.389 1.00 64.53 C ANISOU 2028 CA LYS A1083 7660 12513 4348 200 -973 -245 C ATOM 2029 C LYS A1083 6.345 20.274 -17.056 1.00 62.50 C ANISOU 2029 C LYS A1083 7460 12095 4191 121 -986 -276 C ATOM 2030 O LYS A1083 6.949 19.648 -16.182 1.00 61.95 O ANISOU 2030 O LYS A1083 7503 11850 4184 138 -966 -347 O ATOM 2031 CB LYS A1083 8.352 19.991 -18.571 1.00 65.27 C ANISOU 2031 CB LYS A1083 7866 12527 4406 289 -938 -329 C ATOM 2032 CG LYS A1083 9.066 20.368 -19.872 1.00 68.08 C ANISOU 2032 CG LYS A1083 8163 13045 4660 378 -923 -293 C ATOM 2033 CD LYS A1083 10.498 19.843 -19.895 1.00 70.56 C ANISOU 2033 CD LYS A1083 8579 13274 4958 483 -881 -354 C ATOM 2034 CE LYS A1083 11.254 20.289 -21.146 1.00 75.37 C ANISOU 2034 CE LYS A1083 9118 14050 5469 581 -863 -304 C ATOM 2035 NZ LYS A1083 11.445 21.764 -21.204 1.00 94.77 N ANISOU 2035 NZ LYS A1083 11411 16595 8001 644 -843 -127 N ATOM 2036 N VAL A1084 5.082 20.679 -16.915 1.00 62.58 N ANISOU 2036 N VAL A1084 7385 12176 4215 36 -1019 -217 N ATOM 2037 CA VAL A1084 4.371 20.462 -15.660 1.00 61.95 C ANISOU 2037 CA VAL A1084 7336 11969 4233 -36 -1033 -225 C ATOM 2038 C VAL A1084 3.950 19.006 -15.520 1.00 62.64 C ANISOU 2038 C VAL A1084 7562 11980 4259 -141 -1074 -374 C ATOM 2039 O VAL A1084 3.964 18.450 -14.418 1.00 62.07 O ANISOU 2039 O VAL A1084 7575 11743 4267 -171 -1072 -426 O ATOM 2040 CB VAL A1084 3.169 21.417 -15.561 1.00 64.05 C ANISOU 2040 CB VAL A1084 7459 12345 4532 -83 -1052 -101 C ATOM 2041 CG1 VAL A1084 2.460 21.239 -14.222 1.00 61.18 C ANISOU 2041 CG1 VAL A1084 7122 11854 4270 -148 -1064 -101 C ATOM 2042 CG2 VAL A1084 3.628 22.855 -15.743 1.00 61.24 C ANISOU 2042 CG2 VAL A1084 6974 12060 4236 24 -1013 46 C ATOM 2043 N LYS A1085 3.565 18.364 -16.625 1.00 63.91 N ANISOU 2043 N LYS A1085 7748 12258 4278 -201 -1114 -445 N ATOM 2044 CA LYS A1085 3.319 16.926 -16.590 1.00 64.69 C ANISOU 2044 CA LYS A1085 7995 12274 4310 -294 -1154 -598 C ATOM 2045 C LYS A1085 4.534 16.198 -16.030 1.00 64.25 C ANISOU 2045 C LYS A1085 8081 12034 4297 -225 -1116 -693 C ATOM 2046 O LYS A1085 4.417 15.358 -15.129 1.00 64.03 O ANISOU 2046 O LYS A1085 8159 11850 4320 -280 -1128 -771 O ATOM 2047 CB LYS A1085 2.980 16.424 -17.995 1.00 66.17 C ANISOU 2047 CB LYS A1085 8194 12618 4329 -345 -1195 -662 C ATOM 2048 CG LYS A1085 2.654 14.941 -18.099 1.00 67.18 C ANISOU 2048 CG LYS A1085 8478 12674 4373 -450 -1246 -821 C ATOM 2049 CD LYS A1085 2.736 14.485 -19.552 1.00 71.29 C ANISOU 2049 CD LYS A1085 9028 13335 4726 -460 -1272 -895 C ATOM 2050 CE LYS A1085 2.383 13.017 -19.715 1.00 81.50 C ANISOU 2050 CE LYS A1085 10482 14557 5929 -568 -1327 -1057 C ATOM 2051 NZ LYS A1085 0.923 12.813 -19.913 1.00100.70 N ANISOU 2051 NZ LYS A1085 12871 17086 8303 -726 -1400 -1048 N ATOM 2052 N GLU A1086 5.719 16.527 -16.549 1.00 64.12 N ANISOU 2052 N GLU A1086 8063 12038 4262 -101 -1069 -679 N ATOM 2053 CA GLU A1086 6.949 15.941 -16.031 1.00 63.66 C ANISOU 2053 CA GLU A1086 8127 11817 4246 -21 -1026 -752 C ATOM 2054 C GLU A1086 7.183 16.342 -14.578 1.00 62.28 C ANISOU 2054 C GLU A1086 7945 11485 4235 5 -993 -694 C ATOM 2055 O GLU A1086 7.709 15.552 -13.785 1.00 64.52 O ANISOU 2055 O GLU A1086 8348 11599 4568 11 -977 -774 O ATOM 2056 CB GLU A1086 8.134 16.366 -16.901 1.00 63.80 C ANISOU 2056 CB GLU A1086 8119 11912 4209 111 -982 -723 C ATOM 2057 CG GLU A1086 8.197 15.703 -18.280 1.00 65.24 C ANISOU 2057 CG GLU A1086 8349 12217 4222 106 -1007 -813 C ATOM 2058 CD GLU A1086 7.160 16.221 -19.267 1.00 66.04 C ANISOU 2058 CD GLU A1086 8332 12525 4235 40 -1050 -758 C ATOM 2059 OE1 GLU A1086 6.408 17.157 -18.930 1.00 65.47 O ANISOU 2059 OE1 GLU A1086 8133 12511 4233 7 -1059 -640 O ATOM 2060 OE2 GLU A1086 7.106 15.685 -20.393 1.00 67.27 O ANISOU 2060 OE2 GLU A1086 8523 12790 4248 24 -1075 -832 O ATOM 2061 N ALA A1087 6.804 17.569 -14.211 1.00 65.11 N ANISOU 2061 N ALA A1087 8165 11896 4677 22 -982 -556 N ATOM 2062 CA ALA A1087 6.977 18.010 -12.831 1.00 60.18 C ANISOU 2062 CA ALA A1087 7532 11130 4205 46 -953 -500 C ATOM 2063 C ALA A1087 6.058 17.241 -11.892 1.00 60.12 C ANISOU 2063 C ALA A1087 7587 11017 4240 -68 -989 -561 C ATOM 2064 O ALA A1087 6.465 16.865 -10.787 1.00 59.37 O ANISOU 2064 O ALA A1087 7565 10755 4238 -59 -968 -594 O ATOM 2065 CB ALA A1087 6.715 19.511 -12.721 1.00 59.50 C ANISOU 2065 CB ALA A1087 7287 11130 4191 90 -937 -340 C ATOM 2066 N GLN A1088 4.814 17.005 -12.313 1.00 60.93 N ANISOU 2066 N GLN A1088 7657 11220 4273 -179 -1045 -572 N ATOM 2067 CA GLN A1088 3.893 16.214 -11.506 1.00 61.01 C ANISOU 2067 CA GLN A1088 7726 11145 4312 -296 -1087 -629 C ATOM 2068 C GLN A1088 4.406 14.791 -11.332 1.00 61.44 C ANISOU 2068 C GLN A1088 7951 11059 4335 -324 -1095 -780 C ATOM 2069 O GLN A1088 4.459 14.268 -10.213 1.00 63.26 O ANISOU 2069 O GLN A1088 8253 11133 4652 -350 -1091 -818 O ATOM 2070 CB GLN A1088 2.507 16.209 -12.150 1.00 61.96 C ANISOU 2070 CB GLN A1088 7776 11420 4345 -410 -1149 -608 C ATOM 2071 CG GLN A1088 1.497 15.334 -11.436 1.00 62.23 C ANISOU 2071 CG GLN A1088 7867 11384 4391 -543 -1201 -664 C ATOM 2072 CD GLN A1088 0.168 15.271 -12.152 1.00 63.27 C ANISOU 2072 CD GLN A1088 7935 11680 4426 -660 -1264 -643 C ATOM 2073 OE1 GLN A1088 0.110 15.292 -13.382 1.00 68.91 O ANISOU 2073 OE1 GLN A1088 8626 12534 5022 -666 -1282 -656 O ATOM 2074 NE2 GLN A1088 -0.913 15.198 -11.383 1.00 71.65 N ANISOU 2074 NE2 GLN A1088 8963 12730 5532 -754 -1300 -607 N ATOM 2075 N ALA A1089 4.789 14.146 -12.436 1.00 62.49 N ANISOU 2075 N ALA A1089 8154 11247 4343 -318 -1106 -868 N ATOM 2076 CA ALA A1089 5.252 12.766 -12.365 1.00 71.75 C ANISOU 2076 CA ALA A1089 9497 12290 5476 -342 -1116 -1017 C ATOM 2077 C ALA A1089 6.442 12.609 -11.429 1.00 66.18 C ANISOU 2077 C ALA A1089 8864 11409 4873 -248 -1056 -1034 C ATOM 2078 O ALA A1089 6.664 11.512 -10.906 1.00 77.46 O ANISOU 2078 O ALA A1089 10426 12691 6314 -281 -1061 -1140 O ATOM 2079 CB ALA A1089 5.610 12.264 -13.765 1.00 64.33 C ANISOU 2079 CB ALA A1089 8612 11448 4383 -323 -1128 -1099 C ATOM 2080 N ALA A1090 7.209 13.679 -11.203 1.00 69.00 N ANISOU 2080 N ALA A1090 9137 11778 5303 -134 -1000 -930 N ATOM 2081 CA ALA A1090 8.335 13.624 -10.280 1.00 72.80 C ANISOU 2081 CA ALA A1090 9675 12101 5884 -46 -942 -932 C ATOM 2082 C ALA A1090 7.908 13.450 -8.828 1.00 78.50 C ANISOU 2082 C ALA A1090 10414 12680 6731 -103 -946 -925 C ATOM 2083 O ALA A1090 8.774 13.246 -7.971 1.00 77.98 O ANISOU 2083 O ALA A1090 10408 12472 6749 -46 -902 -938 O ATOM 2084 CB ALA A1090 9.183 14.891 -10.410 1.00 65.33 C ANISOU 2084 CB ALA A1090 8624 11214 4984 78 -889 -811 C ATOM 2085 N ALA A1091 6.608 13.531 -8.527 1.00 76.98 N ANISOU 2085 N ALA A1091 10168 12528 6553 -211 -995 -898 N ATOM 2086 CA ALA A1091 6.166 13.344 -7.149 1.00 87.38 C ANISOU 2086 CA ALA A1091 11499 13718 7985 -265 -1001 -890 C ATOM 2087 C ALA A1091 6.353 11.904 -6.694 1.00 83.95 C ANISOU 2087 C ALA A1091 11219 13133 7546 -319 -1015 -1021 C ATOM 2088 O ALA A1091 6.613 11.662 -5.511 1.00 88.59 O ANISOU 2088 O ALA A1091 11845 13576 8238 -315 -994 -1026 O ATOM 2089 CB ALA A1091 4.703 13.754 -6.996 1.00 79.19 C ANISOU 2089 CB ALA A1091 10362 12775 6952 -366 -1052 -825 C ATOM 2090 N GLU A1092 6.216 10.939 -7.606 1.00 67.19 N ANISOU 2090 N GLU A1092 9187 11038 5304 -370 -1052 -1128 N ATOM 2091 CA GLU A1092 6.488 9.552 -7.244 1.00 84.80 C ANISOU 2091 CA GLU A1092 11576 13117 7527 -412 -1064 -1258 C ATOM 2092 C GLU A1092 7.866 9.423 -6.607 1.00 75.32 C ANISOU 2092 C GLU A1092 10442 11776 6401 -298 -993 -1273 C ATOM 2093 O GLU A1092 8.035 8.715 -5.608 1.00 77.41 O ANISOU 2093 O GLU A1092 10786 11885 6740 -322 -986 -1320 O ATOM 2094 CB GLU A1092 6.375 8.653 -8.477 1.00 92.71 C ANISOU 2094 CB GLU A1092 12671 14175 8379 -455 -1105 -1370 C ATOM 2095 CG GLU A1092 5.141 7.760 -8.475 1.00 88.64 C ANISOU 2095 CG GLU A1092 12205 13655 7818 -615 -1186 -1437 C ATOM 2096 CD GLU A1092 5.008 6.934 -9.742 1.00134.92 C ANISOU 2096 CD GLU A1092 18159 19579 13526 -661 -1230 -1547 C ATOM 2097 OE1 GLU A1092 5.878 7.056 -10.630 1.00142.12 O ANISOU 2097 OE1 GLU A1092 19094 20542 14365 -561 -1194 -1573 O ATOM 2098 OE2 GLU A1092 4.031 6.161 -9.848 1.00136.76 O ANISOU 2098 OE2 GLU A1092 18441 19812 13708 -797 -1302 -1607 O ATOM 2099 N GLN A1093 8.860 10.121 -7.161 1.00 69.69 N ANISOU 2099 N GLN A1093 9690 11120 5669 -174 -940 -1227 N ATOM 2100 CA GLN A1093 10.202 10.079 -6.592 1.00 68.07 C ANISOU 2100 CA GLN A1093 9537 10796 5530 -62 -872 -1227 C ATOM 2101 C GLN A1093 10.276 10.850 -5.281 1.00 77.38 C ANISOU 2101 C GLN A1093 10641 11902 6858 -41 -841 -1129 C ATOM 2102 O GLN A1093 11.040 10.472 -4.385 1.00 78.70 O ANISOU 2102 O GLN A1093 10873 11926 7103 -1 -800 -1149 O ATOM 2103 CB GLN A1093 11.209 10.635 -7.599 1.00 70.58 C ANISOU 2103 CB GLN A1093 9827 11212 5780 60 -829 -1195 C ATOM 2104 CG GLN A1093 12.652 10.634 -7.115 1.00 96.58 C ANISOU 2104 CG GLN A1093 13166 14401 9128 182 -757 -1184 C ATOM 2105 CD GLN A1093 13.630 11.032 -8.206 1.00109.07 C ANISOU 2105 CD GLN A1093 14730 16088 10626 298 -720 -1160 C ATOM 2106 OE1 GLN A1093 13.239 11.285 -9.348 1.00114.27 O ANISOU 2106 OE1 GLN A1093 15342 16895 11180 290 -749 -1157 O ATOM 2107 NE2 GLN A1093 14.911 11.087 -7.858 1.00 99.50 N ANISOU 2107 NE2 GLN A1093 13548 14804 9454 408 -658 -1138 N ATOM 2108 N LEU A1094 9.501 11.929 -5.152 1.00 70.79 N ANISOU 2108 N LEU A1094 9672 11163 6062 -66 -858 -1022 N ATOM 2109 CA LEU A1094 9.445 12.651 -3.886 1.00 74.50 C ANISOU 2109 CA LEU A1094 10075 11564 6669 -53 -834 -934 C ATOM 2110 C LEU A1094 8.743 11.826 -2.817 1.00 73.99 C ANISOU 2110 C LEU A1094 10066 11382 6665 -152 -864 -986 C ATOM 2111 O LEU A1094 9.130 11.859 -1.644 1.00 71.10 O ANISOU 2111 O LEU A1094 9712 10895 6408 -130 -833 -966 O ATOM 2112 CB LEU A1094 8.734 13.990 -4.076 1.00 73.70 C ANISOU 2112 CB LEU A1094 9821 11597 6585 -51 -847 -811 C ATOM 2113 CG LEU A1094 9.451 15.013 -4.956 1.00 77.60 C ANISOU 2113 CG LEU A1094 10237 12202 7043 53 -814 -732 C ATOM 2114 CD1 LEU A1094 8.497 16.122 -5.369 1.00 88.00 C ANISOU 2114 CD1 LEU A1094 11414 13669 8351 31 -840 -629 C ATOM 2115 CD2 LEU A1094 10.653 15.586 -4.228 1.00 76.97 C ANISOU 2115 CD2 LEU A1094 10152 12031 7061 159 -751 -674 C ATOM 2116 N LYS A1095 7.702 11.085 -3.203 1.00 68.42 N ANISOU 2116 N LYS A1095 9393 10714 5891 -266 -928 -1050 N ATOM 2117 CA LYS A1095 7.033 10.211 -2.248 1.00 73.23 C ANISOU 2117 CA LYS A1095 10060 11215 6551 -367 -962 -1100 C ATOM 2118 C LYS A1095 7.938 9.057 -1.838 1.00 80.17 C ANISOU 2118 C LYS A1095 11084 11931 7446 -347 -937 -1204 C ATOM 2119 O LYS A1095 7.930 8.637 -0.675 1.00 75.03 O ANISOU 2119 O LYS A1095 10466 11153 6888 -374 -930 -1214 O ATOM 2120 CB LYS A1095 5.725 9.690 -2.841 1.00 73.66 C ANISOU 2120 CB LYS A1095 10114 11357 6518 -498 -1041 -1139 C ATOM 2121 CG LYS A1095 4.915 8.850 -1.872 1.00 91.52 C ANISOU 2121 CG LYS A1095 12420 13524 8831 -612 -1085 -1176 C ATOM 2122 CD LYS A1095 3.504 8.599 -2.376 1.00 75.91 C ANISOU 2122 CD LYS A1095 10409 11657 6777 -745 -1166 -1179 C ATOM 2123 CE LYS A1095 3.487 7.690 -3.591 1.00 91.46 C ANISOU 2123 CE LYS A1095 12478 13662 8611 -793 -1206 -1288 C ATOM 2124 NZ LYS A1095 2.094 7.328 -3.974 1.00112.20 N ANISOU 2124 NZ LYS A1095 15080 16383 11166 -938 -1290 -1294 N ATOM 2125 N THR A1096 8.727 8.532 -2.778 1.00 78.00 N ANISOU 2125 N THR A1096 10895 11660 7082 -294 -920 -1279 N ATOM 2126 CA THR A1096 9.694 7.494 -2.435 1.00 81.75 C ANISOU 2126 CA THR A1096 11509 11983 7571 -256 -886 -1371 C ATOM 2127 C THR A1096 10.701 8.012 -1.418 1.00 76.22 C ANISOU 2127 C THR A1096 10784 11189 6987 -158 -816 -1306 C ATOM 2128 O THR A1096 10.968 7.363 -0.401 1.00 74.79 O ANISOU 2128 O THR A1096 10667 10864 6883 -172 -799 -1340 O ATOM 2129 CB THR A1096 10.408 7.004 -3.696 1.00 81.23 C ANISOU 2129 CB THR A1096 11527 11957 7380 -197 -875 -1450 C ATOM 2130 OG1 THR A1096 9.494 6.249 -4.503 1.00 73.20 O ANISOU 2130 OG1 THR A1096 10564 10992 6257 -302 -945 -1534 O ATOM 2131 CG2 THR A1096 11.612 6.137 -3.338 1.00 66.52 C ANISOU 2131 CG2 THR A1096 9793 9945 5537 -123 -822 -1523 C ATOM 2132 N THR A1097 11.275 9.187 -1.683 1.00 72.82 N ANISOU 2132 N THR A1097 10259 10841 6570 -62 -774 -1211 N ATOM 2133 CA THR A1097 12.212 9.789 -0.743 1.00 69.30 C ANISOU 2133 CA THR A1097 9781 10318 6232 26 -711 -1139 C ATOM 2134 C THR A1097 11.564 9.992 0.622 1.00 73.92 C ANISOU 2134 C THR A1097 10321 10829 6938 -35 -722 -1094 C ATOM 2135 O THR A1097 12.123 9.603 1.654 1.00 71.23 O ANISOU 2135 O THR A1097 10027 10355 6680 -17 -689 -1106 O ATOM 2136 CB THR A1097 12.715 11.121 -1.300 1.00 71.85 C ANISOU 2136 CB THR A1097 9996 10758 6547 121 -680 -1032 C ATOM 2137 OG1 THR A1097 13.627 10.879 -2.377 1.00 85.28 O ANISOU 2137 OG1 THR A1097 11747 12504 8150 201 -654 -1069 O ATOM 2138 CG2 THR A1097 13.404 11.935 -0.216 1.00 71.25 C ANISOU 2138 CG2 THR A1097 9865 10612 6594 187 -629 -940 C ATOM 2139 N ARG A1098 10.382 10.609 0.643 1.00 69.20 N ANISOU 2139 N ARG A1098 9626 10322 6346 -104 -768 -1038 N ATOM 2140 CA ARG A1098 9.718 10.899 1.908 1.00 63.90 C ANISOU 2140 CA ARG A1098 8899 9596 5782 -154 -778 -987 C ATOM 2141 C ARG A1098 9.466 9.625 2.705 1.00 82.97 C ANISOU 2141 C ARG A1098 11413 11880 8231 -233 -799 -1073 C ATOM 2142 O ARG A1098 9.654 9.603 3.928 1.00 73.07 O ANISOU 2142 O ARG A1098 10158 10524 7082 -229 -775 -1051 O ATOM 2143 CB ARG A1098 8.408 11.642 1.639 1.00 69.86 C ANISOU 2143 CB ARG A1098 9542 10485 6517 -217 -828 -920 C ATOM 2144 CG ARG A1098 7.703 12.183 2.878 1.00 72.97 C ANISOU 2144 CG ARG A1098 9858 10849 7017 -251 -835 -847 C ATOM 2145 CD ARG A1098 6.872 11.126 3.605 1.00 77.29 C ANISOU 2145 CD ARG A1098 10458 11324 7586 -363 -880 -907 C ATOM 2146 NE ARG A1098 6.035 10.342 2.704 1.00 79.52 N ANISOU 2146 NE ARG A1098 10778 11673 7761 -461 -943 -974 N ATOM 2147 CZ ARG A1098 4.874 10.751 2.210 1.00 71.06 C ANISOU 2147 CZ ARG A1098 9626 10736 6639 -527 -993 -930 C ATOM 2148 NH1 ARG A1098 4.392 11.953 2.481 1.00 83.63 N ANISOU 2148 NH1 ARG A1098 11092 12410 8273 -499 -986 -819 N ATOM 2149 NH2 ARG A1098 4.178 9.933 1.426 1.00 68.28 N ANISOU 2149 NH2 ARG A1098 9321 10435 6189 -622 -1053 -998 N ATOM 2150 N ASN A1099 9.041 8.552 2.034 1.00 67.19 N ANISOU 2150 N ASN A1099 9502 9883 6145 -307 -844 -1171 N ATOM 2151 CA ASN A1099 8.763 7.308 2.745 1.00 81.31 C ANISOU 2151 CA ASN A1099 11386 11544 7963 -390 -870 -1253 C ATOM 2152 C ASN A1099 10.033 6.683 3.307 1.00 83.53 C ANISOU 2152 C ASN A1099 11765 11678 8294 -317 -810 -1299 C ATOM 2153 O ASN A1099 9.974 5.963 4.310 1.00 82.40 O ANISOU 2153 O ASN A1099 11671 11413 8222 -362 -812 -1330 O ATOM 2154 CB ASN A1099 8.058 6.314 1.822 1.00 73.29 C ANISOU 2154 CB ASN A1099 10449 10561 6836 -486 -936 -1349 C ATOM 2155 CG ASN A1099 6.690 6.795 1.379 1.00 76.55 C ANISOU 2155 CG ASN A1099 10767 11117 7202 -577 -1001 -1302 C ATOM 2156 OD1 ASN A1099 6.035 7.572 2.074 1.00 88.08 O ANISOU 2156 OD1 ASN A1099 12119 12619 8730 -597 -1008 -1210 O ATOM 2157 ND2 ASN A1099 6.249 6.329 0.217 1.00 87.09 N ANISOU 2157 ND2 ASN A1099 12143 12530 8416 -632 -1049 -1364 N ATOM 2158 N ALA A1100 11.184 6.942 2.683 1.00 69.22 N ANISOU 2158 N ALA A1100 9977 9877 6444 -206 -756 -1300 N ATOM 2159 CA ALA A1100 12.432 6.366 3.171 1.00 61.05 C ANISOU 2159 CA ALA A1100 9033 8713 5451 -130 -695 -1337 C ATOM 2160 C ALA A1100 12.824 6.931 4.529 1.00 78.62 C ANISOU 2160 C ALA A1100 11200 10863 7809 -95 -652 -1257 C ATOM 2161 O ALA A1100 13.493 6.247 5.311 1.00 82.36 O ANISOU 2161 O ALA A1100 11746 11208 8341 -76 -616 -1291 O ATOM 2162 CB ALA A1100 13.555 6.609 2.164 1.00 64.58 C ANISOU 2162 CB ALA A1100 9506 9211 5823 -13 -648 -1341 C ATOM 2163 N TYR A1101 12.427 8.169 4.827 1.00 76.15 N ANISOU 2163 N TYR A1101 10760 10629 7544 -84 -653 -1153 N ATOM 2164 CA TYR A1101 12.802 8.842 6.065 1.00 67.84 C ANISOU 2164 CA TYR A1101 9647 9516 6611 -46 -612 -1074 C ATOM 2165 C TYR A1101 11.636 8.945 7.044 1.00 71.85 C ANISOU 2165 C TYR A1101 10096 10013 7191 -137 -654 -1044 C ATOM 2166 O TYR A1101 11.704 9.716 8.007 1.00 66.23 O ANISOU 2166 O TYR A1101 9313 9280 6572 -111 -630 -967 O ATOM 2167 CB TYR A1101 13.359 10.232 5.754 1.00 72.88 C ANISOU 2167 CB TYR A1101 10191 10241 7258 49 -577 -972 C ATOM 2168 CG TYR A1101 14.732 10.212 5.118 1.00 69.43 C ANISOU 2168 CG TYR A1101 9802 9799 6779 155 -523 -979 C ATOM 2169 CD1 TYR A1101 14.895 9.929 3.767 1.00 76.81 C ANISOU 2169 CD1 TYR A1101 10777 10813 7595 178 -533 -1026 C ATOM 2170 CD2 TYR A1101 15.867 10.482 5.872 1.00 76.00 C ANISOU 2170 CD2 TYR A1101 10639 10553 7685 233 -461 -934 C ATOM 2171 CE1 TYR A1101 16.152 9.912 3.188 1.00 76.09 C ANISOU 2171 CE1 TYR A1101 10726 10726 7461 281 -482 -1027 C ATOM 2172 CE2 TYR A1101 17.123 10.468 5.303 1.00 76.76 C ANISOU 2172 CE2 TYR A1101 10774 10652 7739 331 -412 -930 C ATOM 2173 CZ TYR A1101 17.262 10.183 3.963 1.00 75.84 C ANISOU 2173 CZ TYR A1101 10694 10618 7504 358 -422 -976 C ATOM 2174 OH TYR A1101 18.518 10.172 3.405 1.00 85.80 O ANISOU 2174 OH TYR A1101 11990 11890 8721 462 -371 -967 O ATOM 2175 N ILE A1102 10.570 8.173 6.823 1.00 76.59 N ANISOU 2175 N ILE A1102 10726 10628 7747 -245 -717 -1103 N ATOM 2176 CA ILE A1102 9.394 8.276 7.680 1.00 71.34 C ANISOU 2176 CA ILE A1102 9996 9970 7140 -333 -761 -1067 C ATOM 2177 C ILE A1102 9.671 7.686 9.056 1.00 90.78 C ANISOU 2177 C ILE A1102 12495 12293 9705 -349 -739 -1080 C ATOM 2178 O ILE A1102 9.109 8.143 10.059 1.00 83.88 O ANISOU 2178 O ILE A1102 11546 11415 8909 -374 -746 -1019 O ATOM 2179 CB ILE A1102 8.191 7.592 7.006 1.00 78.44 C ANISOU 2179 CB ILE A1102 10916 10932 7956 -449 -838 -1120 C ATOM 2180 CG1 ILE A1102 6.888 8.025 7.677 1.00 90.13 C ANISOU 2180 CG1 ILE A1102 12296 12469 9478 -528 -885 -1054 C ATOM 2181 CG2 ILE A1102 8.337 6.075 7.061 1.00 85.40 C ANISOU 2181 CG2 ILE A1102 11932 11699 8818 -509 -858 -1232 C ATOM 2182 CD1 ILE A1102 5.673 7.819 6.802 1.00 99.31 C ANISOU 2182 CD1 ILE A1102 13438 13748 10547 -627 -959 -1069 C ATOM 2183 N GLN A1103 10.532 6.672 9.136 1.00 81.93 N ANISOU 2183 N GLN A1103 11487 11058 8584 -330 -711 -1156 N ATOM 2184 CA GLN A1103 10.857 6.081 10.430 1.00 79.87 C ANISOU 2184 CA GLN A1103 11260 10664 8421 -342 -687 -1166 C ATOM 2185 C GLN A1103 11.785 6.987 11.228 1.00 72.25 C ANISOU 2185 C GLN A1103 10240 9669 7542 -244 -619 -1088 C ATOM 2186 O GLN A1103 11.559 7.226 12.420 1.00 74.61 O ANISOU 2186 O GLN A1103 10489 9925 7934 -261 -612 -1042 O ATOM 2187 CB GLN A1103 11.485 4.701 10.232 1.00 80.04 C ANISOU 2187 CB GLN A1103 11423 10575 8415 -350 -677 -1270 C ATOM 2188 CG GLN A1103 10.562 3.702 9.551 1.00 91.97 C ANISOU 2188 CG GLN A1103 13001 12096 9847 -457 -750 -1354 C ATOM 2189 CD GLN A1103 9.249 3.516 10.293 1.00 91.46 C ANISOU 2189 CD GLN A1103 12884 12041 9826 -576 -814 -1333 C ATOM 2190 OE1 GLN A1103 8.177 3.527 9.691 1.00 92.49 O ANISOU 2190 OE1 GLN A1103 12985 12263 9892 -657 -880 -1337 O ATOM 2191 NE2 GLN A1103 9.330 3.343 11.607 1.00 99.45 N ANISOU 2191 NE2 GLN A1103 13879 12965 10944 -587 -795 -1305 N ATOM 2192 N LYS A1104 12.838 7.502 10.588 1.00 64.63 N ANISOU 2192 N LYS A1104 9283 8728 6544 -144 -570 -1069 N ATOM 2193 CA LYS A1104 13.719 8.444 11.270 1.00 70.82 C ANISOU 2193 CA LYS A1104 10012 9492 7404 -55 -510 -987 C ATOM 2194 C LYS A1104 12.943 9.643 11.794 1.00 69.12 C ANISOU 2194 C LYS A1104 9675 9347 7241 -68 -529 -896 C ATOM 2195 O LYS A1104 13.306 10.217 12.828 1.00 71.14 O ANISOU 2195 O LYS A1104 9887 9558 7586 -33 -496 -837 O ATOM 2196 CB LYS A1104 14.833 8.891 10.324 1.00 56.22 C ANISOU 2196 CB LYS A1104 8179 7685 5497 47 -466 -972 C ATOM 2197 CG LYS A1104 15.938 7.860 10.168 1.00 78.02 C ANISOU 2197 CG LYS A1104 11055 10354 8235 92 -423 -1040 C ATOM 2198 CD LYS A1104 16.789 8.109 8.934 1.00 93.15 C ANISOU 2198 CD LYS A1104 12994 12337 10060 179 -395 -1041 C ATOM 2199 CE LYS A1104 17.844 7.023 8.776 1.00 97.47 C ANISOU 2199 CE LYS A1104 13660 12795 10578 229 -351 -1111 C ATOM 2200 NZ LYS A1104 18.474 7.035 7.428 1.00 91.89 N ANISOU 2200 NZ LYS A1104 12990 12163 9761 302 -336 -1132 N ATOM 2201 N TYR A1105 11.866 10.025 11.104 1.00 69.57 N ANISOU 2201 N TYR A1105 9677 9514 7240 -116 -582 -884 N ATOM 2202 CA TYR A1105 11.026 11.122 11.571 1.00 66.66 C ANISOU 2202 CA TYR A1105 9195 9217 6915 -127 -602 -798 C ATOM 2203 C TYR A1105 10.218 10.716 12.799 1.00 65.44 C ANISOU 2203 C TYR A1105 9022 9009 6834 -201 -627 -798 C ATOM 2204 O TYR A1105 10.115 11.484 13.763 1.00 61.74 O ANISOU 2204 O TYR A1105 8484 8529 6444 -178 -611 -730 O ATOM 2205 CB TYR A1105 10.105 11.573 10.440 1.00 60.26 C ANISOU 2205 CB TYR A1105 8332 8545 6017 -157 -650 -783 C ATOM 2206 CG TYR A1105 8.948 12.438 10.876 1.00 59.16 C ANISOU 2206 CG TYR A1105 8084 8484 5909 -191 -682 -707 C ATOM 2207 CD1 TYR A1105 9.109 13.804 11.067 1.00 54.47 C ANISOU 2207 CD1 TYR A1105 7403 7936 5356 -119 -657 -614 C ATOM 2208 CD2 TYR A1105 7.689 11.891 11.080 1.00 58.83 C ANISOU 2208 CD2 TYR A1105 8028 8472 5853 -293 -740 -727 C ATOM 2209 CE1 TYR A1105 8.048 14.599 11.457 1.00 57.74 C ANISOU 2209 CE1 TYR A1105 7722 8421 5796 -141 -683 -545 C ATOM 2210 CE2 TYR A1105 6.623 12.677 11.470 1.00 62.32 C ANISOU 2210 CE2 TYR A1105 8368 8993 6318 -317 -767 -652 C ATOM 2211 CZ TYR A1105 6.808 14.029 11.656 1.00 56.88 C ANISOU 2211 CZ TYR A1105 7596 8346 5668 -237 -737 -563 C ATOM 2212 OH TYR A1105 5.748 14.815 12.043 1.00 66.38 O ANISOU 2212 OH TYR A1105 8702 9627 6893 -253 -761 -489 O ATOM 2213 N LEU A1106 9.631 9.518 12.781 1.00 60.81 N ANISOU 2213 N LEU A1106 8496 8388 6221 -291 -668 -871 N ATOM 2214 CA LEU A1106 8.891 9.040 13.944 1.00 66.44 C ANISOU 2214 CA LEU A1106 9192 9050 7001 -364 -694 -870 C ATOM 2215 C LEU A1106 9.825 8.776 15.118 1.00 67.80 C ANISOU 2215 C LEU A1106 9396 9096 7268 -324 -640 -870 C ATOM 2216 O LEU A1106 9.473 9.040 16.274 1.00 58.10 O ANISOU 2216 O LEU A1106 8113 7844 6120 -338 -639 -825 O ATOM 2217 CB LEU A1106 8.121 7.771 13.586 1.00 67.38 C ANISOU 2217 CB LEU A1106 9376 9157 7067 -474 -754 -949 C ATOM 2218 CG LEU A1106 7.053 7.925 12.506 1.00 78.33 C ANISOU 2218 CG LEU A1106 10730 10673 8359 -534 -816 -949 C ATOM 2219 CD1 LEU A1106 6.648 6.561 11.970 1.00 79.09 C ANISOU 2219 CD1 LEU A1106 10923 10737 8391 -631 -869 -1044 C ATOM 2220 CD2 LEU A1106 5.848 8.673 13.053 1.00 74.79 C ANISOU 2220 CD2 LEU A1106 10165 10313 7939 -575 -852 -867 C ATOM 2221 N ALA A 900 11.017 8.246 14.838 1.00 59.22 N ANISOU 2221 N ALA A 900 8396 7933 6171 -272 -595 -917 N ATOM 2222 CA ALA A 900 11.987 8.002 15.898 1.00 51.68 C ANISOU 2222 CA ALA A 900 7471 6864 5302 -229 -539 -912 C ATOM 2223 C ALA A 900 12.448 9.307 16.530 1.00 69.04 C ANISOU 2223 C ALA A 900 9586 9081 7564 -153 -498 -820 C ATOM 2224 O ALA A 900 12.633 9.384 17.751 1.00 70.30 O ANISOU 2224 O ALA A 900 9722 9177 7811 -148 -474 -791 O ATOM 2225 CB ALA A 900 13.182 7.229 15.345 1.00 56.09 C ANISOU 2225 CB ALA A 900 8136 7351 5824 -179 -497 -974 C ATOM 2226 N HIS A 270 12.646 10.345 15.714 1.00 60.17 N ANISOU 2226 N HIS A 270 8419 8045 6398 -93 -490 -774 N ATOM 2227 CA HIS A 270 13.056 11.634 16.260 1.00 56.42 C ANISOU 2227 CA HIS A 270 7869 7585 5982 -24 -456 -685 C ATOM 2228 C HIS A 270 11.964 12.225 17.141 1.00 55.56 C ANISOU 2228 C HIS A 270 7674 7508 5927 -63 -486 -635 C ATOM 2229 O HIS A 270 12.247 12.739 18.229 1.00 61.19 O ANISOU 2229 O HIS A 270 8352 8176 6722 -34 -459 -588 O ATOM 2230 CB HIS A 270 13.409 12.599 15.131 1.00 61.79 C ANISOU 2230 CB HIS A 270 8519 8356 6602 42 -448 -644 C ATOM 2231 CG HIS A 270 13.816 13.956 15.610 1.00 69.34 C ANISOU 2231 CG HIS A 270 9402 9327 7615 110 -419 -552 C ATOM 2232 ND1 HIS A 270 15.121 14.276 15.919 1.00 82.21 N ANISOU 2232 ND1 HIS A 270 11052 10900 9283 183 -365 -520 N ATOM 2233 CD2 HIS A 270 13.089 15.074 15.847 1.00 60.07 C ANISOU 2233 CD2 HIS A 270 8140 8218 6467 116 -439 -482 C ATOM 2234 CE1 HIS A 270 15.181 15.533 16.318 1.00 80.47 C ANISOU 2234 CE1 HIS A 270 10761 10704 9109 225 -356 -438 C ATOM 2235 NE2 HIS A 270 13.962 16.040 16.283 1.00 66.73 N ANISOU 2235 NE2 HIS A 270 8956 9034 7363 189 -399 -415 N ATOM 2236 N LEU A 271 10.711 12.163 16.688 1.00 63.43 N ANISOU 2236 N LEU A 271 8636 8588 6877 -128 -544 -642 N ATOM 2237 CA LEU A 271 9.611 12.633 17.522 1.00 66.38 C ANISOU 2237 CA LEU A 271 8927 8998 7295 -166 -574 -593 C ATOM 2238 C LEU A 271 9.480 11.783 18.779 1.00 66.26 C ANISOU 2238 C LEU A 271 8933 8892 7350 -215 -574 -619 C ATOM 2239 O LEU A 271 9.137 12.291 19.854 1.00 55.40 O ANISOU 2239 O LEU A 271 7497 7511 6043 -209 -569 -569 O ATOM 2240 CB LEU A 271 8.306 12.622 16.725 1.00 64.21 C ANISOU 2240 CB LEU A 271 8614 8837 6947 -231 -636 -593 C ATOM 2241 CG LEU A 271 8.203 13.606 15.555 1.00 73.37 C ANISOU 2241 CG LEU A 271 9729 10107 8040 -186 -642 -552 C ATOM 2242 CD1 LEU A 271 6.815 13.533 14.941 1.00 75.23 C ANISOU 2242 CD1 LEU A 271 9918 10456 8209 -261 -705 -546 C ATOM 2243 CD2 LEU A 271 8.529 15.036 15.978 1.00 67.37 C ANISOU 2243 CD2 LEU A 271 8898 9366 7335 -101 -607 -464 C ATOM 2244 N ALA A 272 9.751 10.481 18.664 1.00 74.92 N ANISOU 2244 N ALA A 272 10116 9919 8431 -262 -579 -696 N ATOM 2245 CA ALA A 272 9.707 9.613 19.833 1.00 55.87 C ANISOU 2245 CA ALA A 272 7726 7416 6087 -309 -577 -719 C ATOM 2246 C ALA A 272 10.833 9.931 20.809 1.00 73.99 C ANISOU 2246 C ALA A 272 10024 9625 8464 -239 -512 -691 C ATOM 2247 O ALA A 272 10.649 9.808 22.025 1.00 65.21 O ANISOU 2247 O ALA A 272 8883 8469 7426 -258 -506 -672 O ATOM 2248 CB ALA A 272 9.777 8.149 19.399 1.00 63.46 C ANISOU 2248 CB ALA A 272 8786 8316 7009 -373 -597 -809 C ATOM 2249 N ALA A 273 11.996 10.348 20.300 1.00 65.53 N ANISOU 2249 N ALA A 273 8985 8536 7378 -159 -463 -684 N ATOM 2250 CA ALA A 273 13.117 10.656 21.183 1.00 61.72 C ANISOU 2250 CA ALA A 273 8506 7976 6968 -96 -402 -653 C ATOM 2251 C ALA A 273 12.902 11.976 21.913 1.00 65.38 C ANISOU 2251 C ALA A 273 8879 8476 7485 -56 -394 -571 C ATOM 2252 O ALA A 273 13.164 12.073 23.117 1.00 54.91 O ANISOU 2252 O ALA A 273 7533 7093 6236 -48 -369 -546 O ATOM 2253 CB ALA A 273 14.421 10.699 20.388 1.00 47.65 C ANISOU 2253 CB ALA A 273 6783 6173 5149 -23 -356 -663 C ATOM 2254 N THR A 274 12.441 13.008 21.203 1.00 53.61 N ANISOU 2254 N THR A 274 7335 7079 5954 -30 -415 -529 N ATOM 2255 CA THR A 274 12.171 14.280 21.866 1.00 70.17 C ANISOU 2255 CA THR A 274 9353 9209 8100 9 -410 -453 C ATOM 2256 C THR A 274 11.085 14.117 22.925 1.00 64.04 C ANISOU 2256 C THR A 274 8526 8438 7369 -44 -440 -444 C ATOM 2257 O THR A 274 11.208 14.640 24.039 1.00 52.71 O ANISOU 2257 O THR A 274 7054 6969 6003 -18 -419 -404 O ATOM 2258 CB THR A 274 11.774 15.342 20.838 1.00 65.63 C ANISOU 2258 CB THR A 274 8730 8736 7469 43 -430 -409 C ATOM 2259 OG1 THR A 274 10.633 14.896 20.097 1.00 74.69 O ANISOU 2259 OG1 THR A 274 9866 9962 8551 -20 -483 -438 O ATOM 2260 CG2 THR A 274 12.926 15.619 19.873 1.00 59.90 C ANISOU 2260 CG2 THR A 274 8045 8011 6705 105 -398 -406 C ATOM 2261 N ARG A 275 10.023 13.376 22.598 1.00 53.95 N ANISOU 2261 N ARG A 275 7245 7204 6049 -121 -490 -478 N ATOM 2262 CA ARG A 275 8.980 13.081 23.576 1.00 57.33 C ANISOU 2262 CA ARG A 275 7625 7643 6515 -178 -522 -468 C ATOM 2263 C ARG A 275 9.576 12.454 24.832 1.00 60.66 C ANISOU 2263 C ARG A 275 8072 7961 7016 -185 -490 -483 C ATOM 2264 O ARG A 275 9.309 12.897 25.954 1.00 54.64 O ANISOU 2264 O ARG A 275 7255 7192 6313 -173 -483 -443 O ATOM 2265 CB ARG A 275 7.937 12.150 22.947 1.00 62.74 C ANISOU 2265 CB ARG A 275 8322 8378 7138 -270 -582 -510 C ATOM 2266 CG ARG A 275 6.621 12.051 23.709 1.00 82.89 C ANISOU 2266 CG ARG A 275 10804 10982 9709 -330 -627 -480 C ATOM 2267 CD ARG A 275 5.647 11.058 23.063 1.00 86.10 C ANISOU 2267 CD ARG A 275 11227 11435 10052 -431 -691 -520 C ATOM 2268 NE ARG A 275 5.458 11.296 21.633 1.00100.11 N ANISOU 2268 NE ARG A 275 13015 13285 11738 -432 -713 -531 N ATOM 2269 CZ ARG A 275 5.796 10.452 20.663 1.00 92.00 C ANISOU 2269 CZ ARG A 275 12069 12235 10652 -467 -725 -600 C ATOM 2270 NH1 ARG A 275 6.332 9.269 20.921 1.00 91.42 N ANISOU 2270 NH1 ARG A 275 12078 12059 10599 -505 -718 -666 N ATOM 2271 NH2 ARG A 275 5.580 10.801 19.398 1.00 69.20 N ANISOU 2271 NH2 ARG A 275 9181 9430 7683 -463 -744 -602 N ATOM 2272 N LYS A 276 10.391 11.414 24.653 1.00 60.78 N ANISOU 2272 N LYS A 276 8169 7895 7028 -201 -469 -542 N ATOM 2273 CA LYS A 276 11.019 10.753 25.791 1.00 55.33 C ANISOU 2273 CA LYS A 276 7504 7106 6411 -208 -436 -555 C ATOM 2274 C LYS A 276 11.946 11.707 26.533 1.00 61.06 C ANISOU 2274 C LYS A 276 8206 7797 7196 -129 -381 -504 C ATOM 2275 O LYS A 276 12.001 11.695 27.769 1.00 53.66 O ANISOU 2275 O LYS A 276 7240 6819 6329 -131 -365 -484 O ATOM 2276 CB LYS A 276 11.774 9.518 25.300 1.00 70.07 C ANISOU 2276 CB LYS A 276 9469 8897 8256 -229 -420 -625 C ATOM 2277 CG LYS A 276 12.374 8.641 26.382 1.00 74.13 C ANISOU 2277 CG LYS A 276 10016 9308 8841 -245 -387 -644 C ATOM 2278 CD LYS A 276 12.805 7.298 25.801 1.00 78.95 C ANISOU 2278 CD LYS A 276 10725 9851 9420 -280 -386 -719 C ATOM 2279 CE LYS A 276 13.742 6.551 26.733 1.00 91.01 C ANISOU 2279 CE LYS A 276 12293 11271 11015 -270 -336 -731 C ATOM 2280 NZ LYS A 276 15.076 7.205 26.810 1.00 92.16 N ANISOU 2280 NZ LYS A 276 12450 11387 11179 -179 -268 -698 N ATOM 2281 N GLY A 277 12.666 12.558 25.799 1.00 49.77 N ANISOU 2281 N GLY A 277 6786 6387 5739 -61 -356 -480 N ATOM 2282 CA GLY A 277 13.556 13.508 26.447 1.00 49.75 C ANISOU 2282 CA GLY A 277 6762 6351 5787 9 -310 -428 C ATOM 2283 C GLY A 277 12.817 14.496 27.328 1.00 56.19 C ANISOU 2283 C GLY A 277 7499 7205 6647 22 -324 -373 C ATOM 2284 O GLY A 277 13.271 14.822 28.429 1.00 49.19 O ANISOU 2284 O GLY A 277 6594 6270 5825 47 -294 -346 O ATOM 2285 N VAL A 278 11.669 14.988 26.857 1.00 51.30 N ANISOU 2285 N VAL A 278 6829 6675 5988 8 -369 -355 N ATOM 2286 CA VAL A 278 10.860 15.898 27.663 1.00 58.96 C ANISOU 2286 CA VAL A 278 7723 7687 6991 26 -383 -304 C ATOM 2287 C VAL A 278 10.433 15.216 28.955 1.00 49.24 C ANISOU 2287 C VAL A 278 6471 6423 5816 -19 -388 -314 C ATOM 2288 O VAL A 278 10.524 15.794 30.044 1.00 52.90 O ANISOU 2288 O VAL A 278 6898 6864 6336 13 -369 -280 O ATOM 2289 CB VAL A 278 9.646 16.392 26.857 1.00 54.31 C ANISOU 2289 CB VAL A 278 7085 7208 6343 14 -431 -283 C ATOM 2290 CG1 VAL A 278 8.659 17.106 27.766 1.00 65.56 C ANISOU 2290 CG1 VAL A 278 8431 8679 7798 25 -449 -234 C ATOM 2291 CG2 VAL A 278 10.096 17.309 25.730 1.00 59.29 C ANISOU 2291 CG2 VAL A 278 7721 7876 6930 70 -423 -257 C ATOM 2292 N ARG A 279 9.958 13.973 28.851 1.00 54.26 N ANISOU 2292 N ARG A 279 7129 7054 6435 -94 -415 -361 N ATOM 2293 CA ARG A 279 9.590 13.217 30.044 1.00 53.63 C ANISOU 2293 CA ARG A 279 7028 6940 6407 -142 -421 -370 C ATOM 2294 C ARG A 279 10.766 13.122 31.011 1.00 47.37 C ANISOU 2294 C ARG A 279 6261 6053 5684 -110 -366 -369 C ATOM 2295 O ARG A 279 10.621 13.384 32.210 1.00 44.43 O ANISOU 2295 O ARG A 279 5843 5670 5368 -100 -356 -340 O ATOM 2296 CB ARG A 279 9.098 11.825 29.639 1.00 58.26 C ANISOU 2296 CB ARG A 279 7651 7521 6964 -230 -458 -423 C ATOM 2297 CG ARG A 279 8.692 10.925 30.798 1.00 80.47 C ANISOU 2297 CG ARG A 279 10444 10302 9831 -289 -470 -431 C ATOM 2298 CD ARG A 279 8.138 9.597 30.299 1.00 66.86 C ANISOU 2298 CD ARG A 279 8759 8572 8073 -381 -516 -481 C ATOM 2299 N THR A 280 11.944 12.756 30.500 1.00 44.96 N ANISOU 2299 N THR A 280 6028 5684 5373 -90 -329 -397 N ATOM 2300 CA THR A 280 13.126 12.638 31.348 1.00 52.24 C ANISOU 2300 CA THR A 280 6974 6521 6354 -61 -274 -391 C ATOM 2301 C THR A 280 13.425 13.951 32.060 1.00 43.41 C ANISOU 2301 C THR A 280 5810 5408 5274 3 -250 -333 C ATOM 2302 O THR A 280 13.693 13.968 33.267 1.00 38.43 O ANISOU 2302 O THR A 280 5158 4739 4706 7 -227 -316 O ATOM 2303 CB THR A 280 14.325 12.194 30.505 1.00 41.24 C ANISOU 2303 CB THR A 280 5660 5075 4933 -38 -238 -420 C ATOM 2304 OG1 THR A 280 14.039 10.927 29.903 1.00 49.97 O ANISOU 2304 OG1 THR A 280 6818 6166 6004 -97 -260 -480 O ATOM 2305 CG2 THR A 280 15.580 12.072 31.361 1.00 45.79 C ANISOU 2305 CG2 THR A 280 6260 5569 5568 -7 -179 -406 C ATOM 2306 N LEU A 281 13.407 15.061 31.319 1.00 41.37 N ANISOU 2306 N LEU A 281 5540 5197 4981 52 -257 -302 N ATOM 2307 CA LEU A 281 13.601 16.380 31.913 1.00 47.41 C ANISOU 2307 CA LEU A 281 6267 5968 5779 112 -242 -248 C ATOM 2308 C LEU A 281 12.759 16.550 33.170 1.00 39.25 C ANISOU 2308 C LEU A 281 5172 4951 4791 100 -256 -230 C ATOM 2309 O LEU A 281 13.276 16.847 34.254 1.00 35.05 O ANISOU 2309 O LEU A 281 4630 4373 4315 122 -227 -211 O ATOM 2310 CB LEU A 281 13.235 17.462 30.896 1.00 55.05 C ANISOU 2310 CB LEU A 281 7216 7002 6697 153 -264 -217 C ATOM 2311 CG LEU A 281 14.305 17.914 29.912 1.00 59.40 C ANISOU 2311 CG LEU A 281 7811 7540 7219 197 -240 -204 C ATOM 2312 CD1 LEU A 281 13.698 18.826 28.857 1.00 66.16 C ANISOU 2312 CD1 LEU A 281 8640 8476 8022 225 -271 -177 C ATOM 2313 CD2 LEU A 281 15.406 18.622 30.665 1.00 64.20 C ANISOU 2313 CD2 LEU A 281 8428 8086 7880 244 -200 -166 C ATOM 2314 N ALA A 282 11.444 16.375 33.028 1.00 34.86 N ANISOU 2314 N ALA A 282 4573 4466 4207 66 -302 -234 N ATOM 2315 CA ALA A 282 10.533 16.630 34.135 1.00 42.01 C ANISOU 2315 CA ALA A 282 5412 5405 5145 63 -319 -209 C ATOM 2316 C ALA A 282 10.724 15.616 35.250 1.00 34.65 C ANISOU 2316 C ALA A 282 4478 4421 4265 19 -305 -230 C ATOM 2317 O ALA A 282 10.659 15.967 36.433 1.00 37.53 O ANISOU 2317 O ALA A 282 4805 4779 4678 39 -292 -206 O ATOM 2318 CB ALA A 282 9.087 16.597 33.641 1.00 40.46 C ANISOU 2318 CB ALA A 282 5167 5306 4898 32 -372 -202 C ATOM 2319 N VAL A 283 10.942 14.351 34.893 1.00 34.30 N ANISOU 2319 N VAL A 283 4476 4343 4212 -40 -307 -274 N ATOM 2320 CA VAL A 283 11.072 13.317 35.910 1.00 33.94 C ANISOU 2320 CA VAL A 283 4429 4250 4219 -87 -296 -291 C ATOM 2321 C VAL A 283 12.328 13.545 36.732 1.00 35.04 C ANISOU 2321 C VAL A 283 4588 4313 4414 -47 -239 -280 C ATOM 2322 O VAL A 283 12.316 13.413 37.962 1.00 36.20 O ANISOU 2322 O VAL A 283 4699 4444 4614 -53 -226 -266 O ATOM 2323 CB VAL A 283 11.069 11.924 35.261 1.00 36.61 C ANISOU 2323 CB VAL A 283 4818 4559 4533 -156 -312 -343 C ATOM 2324 CG1 VAL A 283 11.474 10.875 36.277 1.00 47.90 C ANISOU 2324 CG1 VAL A 283 6256 5923 6023 -196 -291 -358 C ATOM 2325 CG2 VAL A 283 9.699 11.611 34.696 1.00 52.25 C ANISOU 2325 CG2 VAL A 283 6768 6620 6465 -211 -375 -349 C ATOM 2326 N VAL A 284 13.425 13.912 36.071 1.00 33.05 N ANISOU 2326 N VAL A 284 4391 4020 4148 -7 -205 -281 N ATOM 2327 CA VAL A 284 14.681 14.113 36.779 1.00 32.42 C ANISOU 2327 CA VAL A 284 4331 3871 4115 26 -152 -264 C ATOM 2328 C VAL A 284 14.594 15.328 37.694 1.00 31.95 C ANISOU 2328 C VAL A 284 4223 3827 4088 73 -146 -219 C ATOM 2329 O VAL A 284 15.044 15.288 38.845 1.00 31.46 O ANISOU 2329 O VAL A 284 4145 3728 4079 76 -118 -206 O ATOM 2330 CB VAL A 284 15.831 14.235 35.766 1.00 36.24 C ANISOU 2330 CB VAL A 284 4881 4319 4568 58 -122 -268 C ATOM 2331 CG1 VAL A 284 17.063 14.762 36.438 1.00 41.06 C ANISOU 2331 CG1 VAL A 284 5503 4876 5221 99 -72 -234 C ATOM 2332 CG2 VAL A 284 16.100 12.884 35.115 1.00 35.32 C ANISOU 2332 CG2 VAL A 284 4822 4169 4430 16 -117 -317 C ATOM 2333 N LEU A 285 14.010 16.424 37.210 1.00 36.04 N ANISOU 2333 N LEU A 285 4718 4400 4575 112 -171 -196 N ATOM 2334 CA LEU A 285 13.885 17.602 38.059 1.00 31.76 C ANISOU 2334 CA LEU A 285 4138 3869 4061 162 -167 -157 C ATOM 2335 C LEU A 285 12.892 17.354 39.187 1.00 34.61 C ANISOU 2335 C LEU A 285 4437 4265 4450 141 -186 -154 C ATOM 2336 O LEU A 285 13.130 17.758 40.330 1.00 33.60 O ANISOU 2336 O LEU A 285 4286 4116 4365 164 -167 -136 O ATOM 2337 CB LEU A 285 13.467 18.812 37.228 1.00 33.33 C ANISOU 2337 CB LEU A 285 4329 4115 4218 211 -191 -130 C ATOM 2338 CG LEU A 285 13.429 20.148 37.975 1.00 43.81 C ANISOU 2338 CG LEU A 285 5632 5444 5572 272 -186 -91 C ATOM 2339 CD1 LEU A 285 14.693 20.379 38.803 1.00 44.40 C ANISOU 2339 CD1 LEU A 285 5735 5440 5695 288 -144 -78 C ATOM 2340 CD2 LEU A 285 13.225 21.275 36.977 1.00 44.66 C ANISOU 2340 CD2 LEU A 285 5744 5586 5639 320 -205 -63 C ATOM 2341 N GLY A 286 11.779 16.683 38.889 1.00 32.24 N ANISOU 2341 N GLY A 286 4106 4022 4122 97 -226 -170 N ATOM 2342 CA GLY A 286 10.843 16.334 39.944 1.00 36.23 C ANISOU 2342 CA GLY A 286 4547 4568 4650 73 -245 -162 C ATOM 2343 C GLY A 286 11.464 15.434 40.997 1.00 36.53 C ANISOU 2343 C GLY A 286 4586 4549 4746 38 -216 -175 C ATOM 2344 O GLY A 286 11.200 15.584 42.192 1.00 35.21 O ANISOU 2344 O GLY A 286 4369 4394 4614 47 -211 -157 O ATOM 2345 N THR A 287 12.294 14.483 40.567 1.00 32.81 N ANISOU 2345 N THR A 287 4169 4015 4280 0 -194 -205 N ATOM 2346 CA THR A 287 12.955 13.597 41.518 1.00 31.49 C ANISOU 2346 CA THR A 287 4006 3791 4168 -31 -162 -213 C ATOM 2347 C THR A 287 13.942 14.369 42.380 1.00 30.83 C ANISOU 2347 C THR A 287 3924 3665 4125 18 -116 -187 C ATOM 2348 O THR A 287 14.008 14.163 43.597 1.00 30.49 O ANISOU 2348 O THR A 287 3843 3614 4129 9 -100 -176 O ATOM 2349 CB THR A 287 13.652 12.464 40.765 1.00 36.17 C ANISOU 2349 CB THR A 287 4665 4326 4752 -72 -146 -250 C ATOM 2350 OG1 THR A 287 12.674 11.706 40.041 1.00 37.85 O ANISOU 2350 OG1 THR A 287 4878 4577 4927 -126 -194 -276 O ATOM 2351 CG2 THR A 287 14.403 11.544 41.721 1.00 40.65 C ANISOU 2351 CG2 THR A 287 5237 4830 5377 -101 -108 -254 C ATOM 2352 N PHE A 288 14.708 15.273 41.767 1.00 31.33 N ANISOU 2352 N PHE A 288 4030 3706 4170 66 -97 -175 N ATOM 2353 CA PHE A 288 15.561 16.176 42.530 1.00 37.47 C ANISOU 2353 CA PHE A 288 4810 4449 4980 112 -63 -146 C ATOM 2354 C PHE A 288 14.763 16.914 43.601 1.00 30.12 C ANISOU 2354 C PHE A 288 3816 3560 4067 138 -80 -126 C ATOM 2355 O PHE A 288 15.188 17.008 44.759 1.00 29.59 O ANISOU 2355 O PHE A 288 3729 3470 4043 143 -55 -113 O ATOM 2356 CB PHE A 288 16.233 17.163 41.574 1.00 39.84 C ANISOU 2356 CB PHE A 288 5157 4733 5248 159 -56 -129 C ATOM 2357 CG PHE A 288 17.148 18.143 42.247 1.00 32.18 C ANISOU 2357 CG PHE A 288 4196 3724 4307 200 -27 -96 C ATOM 2358 CD1 PHE A 288 18.365 17.733 42.761 1.00 39.01 C ANISOU 2358 CD1 PHE A 288 5087 4531 5206 187 18 -87 C ATOM 2359 CD2 PHE A 288 16.802 19.477 42.343 1.00 50.08 C ANISOU 2359 CD2 PHE A 288 6451 6013 6566 251 -45 -71 C ATOM 2360 CE1 PHE A 288 19.215 18.633 43.370 1.00 38.53 C ANISOU 2360 CE1 PHE A 288 5035 4436 5168 218 41 -53 C ATOM 2361 CE2 PHE A 288 17.646 20.382 42.950 1.00 43.80 C ANISOU 2361 CE2 PHE A 288 5671 5176 5796 283 -24 -42 C ATOM 2362 CZ PHE A 288 18.855 19.961 43.464 1.00 46.97 C ANISOU 2362 CZ PHE A 288 6096 5522 6229 263 18 -32 C ATOM 2363 N GLY A 289 13.599 17.450 43.229 1.00 30.41 N ANISOU 2363 N GLY A 289 3821 3665 4069 157 -121 -121 N ATOM 2364 CA GLY A 289 12.783 18.160 44.202 1.00 34.67 C ANISOU 2364 CA GLY A 289 4301 4251 4619 191 -137 -100 C ATOM 2365 C GLY A 289 12.234 17.249 45.285 1.00 30.34 C ANISOU 2365 C GLY A 289 3695 3729 4102 150 -141 -104 C ATOM 2366 O GLY A 289 12.264 17.589 46.470 1.00 30.04 O ANISOU 2366 O GLY A 289 3623 3694 4096 172 -127 -90 O ATOM 2367 N ALA A 290 11.733 16.075 44.897 1.00 34.76 N ANISOU 2367 N ALA A 290 4246 4310 4654 88 -162 -123 N ATOM 2368 CA ALA A 290 11.206 15.146 45.892 1.00 33.47 C ANISOU 2368 CA ALA A 290 4025 4172 4522 42 -170 -121 C ATOM 2369 C ALA A 290 12.290 14.689 46.862 1.00 33.68 C ANISOU 2369 C ALA A 290 4060 4133 4605 28 -123 -122 C ATOM 2370 O ALA A 290 12.004 14.451 48.041 1.00 30.68 O ANISOU 2370 O ALA A 290 3622 3777 4258 20 -120 -108 O ATOM 2371 CB ALA A 290 10.567 13.941 45.200 1.00 33.33 C ANISOU 2371 CB ALA A 290 4006 4175 4484 -29 -204 -141 C ATOM 2372 N CYS A 291 13.538 14.580 46.395 1.00 32.56 N ANISOU 2372 N CYS A 291 3984 3915 4471 28 -86 -133 N ATOM 2373 CA CYS A 291 14.630 14.125 47.251 1.00 34.15 C ANISOU 2373 CA CYS A 291 4194 4057 4723 14 -38 -128 C ATOM 2374 C CYS A 291 15.131 15.213 48.195 1.00 36.29 C ANISOU 2374 C CYS A 291 4453 4320 5017 65 -13 -104 C ATOM 2375 O CYS A 291 15.502 14.915 49.336 1.00 32.88 O ANISOU 2375 O CYS A 291 3989 3877 4627 53 12 -93 O ATOM 2376 CB CYS A 291 15.801 13.629 46.402 1.00 32.76 C ANISOU 2376 CB CYS A 291 4094 3809 4544 0 -5 -143 C ATOM 2377 SG CYS A 291 15.552 12.025 45.651 1.00 40.38 S ANISOU 2377 SG CYS A 291 5085 4757 5502 -70 -19 -178 S ATOM 2378 N TRP A 292 15.177 16.469 47.743 1.00 30.70 N ANISOU 2378 N TRP A 292 3770 3615 4279 120 -21 -94 N ATOM 2379 CA TRP A 292 15.817 17.528 48.516 1.00 30.36 C ANISOU 2379 CA TRP A 292 3732 3549 4254 166 1 -73 C ATOM 2380 C TRP A 292 14.849 18.450 49.243 1.00 29.78 C ANISOU 2380 C TRP A 292 3611 3532 4173 213 -25 -64 C ATOM 2381 O TRP A 292 15.215 19.010 50.282 1.00 28.34 O ANISOU 2381 O TRP A 292 3417 3337 4015 237 -7 -52 O ATOM 2382 CB TRP A 292 16.708 18.387 47.614 1.00 28.46 C ANISOU 2382 CB TRP A 292 3560 3261 3992 199 13 -64 C ATOM 2383 CG TRP A 292 18.087 17.848 47.446 1.00 42.31 C ANISOU 2383 CG TRP A 292 5359 4950 5765 173 56 -58 C ATOM 2384 CD1 TRP A 292 18.562 17.129 46.391 1.00 37.09 C ANISOU 2384 CD1 TRP A 292 4743 4265 5086 149 66 -69 C ATOM 2385 CD2 TRP A 292 19.179 17.987 48.362 1.00 36.34 C ANISOU 2385 CD2 TRP A 292 4610 4151 5045 170 96 -35 C ATOM 2386 NE1 TRP A 292 19.882 16.808 46.593 1.00 41.88 N ANISOU 2386 NE1 TRP A 292 5381 4817 5715 137 112 -52 N ATOM 2387 CE2 TRP A 292 20.285 17.322 47.797 1.00 36.45 C ANISOU 2387 CE2 TRP A 292 4670 4119 5062 147 131 -29 C ATOM 2388 CE3 TRP A 292 19.327 18.605 49.608 1.00 34.87 C ANISOU 2388 CE3 TRP A 292 4397 3965 4886 187 106 -20 C ATOM 2389 CZ2 TRP A 292 21.523 17.262 48.429 1.00 36.63 C ANISOU 2389 CZ2 TRP A 292 4707 4099 5114 137 175 -1 C ATOM 2390 CZ3 TRP A 292 20.561 18.543 50.235 1.00 41.68 C ANISOU 2390 CZ3 TRP A 292 5275 4782 5778 172 147 4 C ATOM 2391 CH2 TRP A 292 21.640 17.876 49.645 1.00 31.22 C ANISOU 2391 CH2 TRP A 292 3990 3415 4455 146 182 16 C ATOM 2392 N LEU A 293 13.641 18.640 48.735 1.00 33.28 N ANISOU 2392 N LEU A 293 4026 4037 4580 228 -65 -66 N ATOM 2393 CA LEU A 293 12.760 19.653 49.308 1.00 34.83 C ANISOU 2393 CA LEU A 293 4184 4287 4761 287 -87 -53 C ATOM 2394 C LEU A 293 12.278 19.269 50.703 1.00 29.18 C ANISOU 2394 C LEU A 293 3399 3614 4073 281 -84 -47 C ATOM 2395 O LEU A 293 12.274 20.128 51.592 1.00 30.41 O ANISOU 2395 O LEU A 293 3543 3776 4237 331 -77 -39 O ATOM 2396 CB LEU A 293 11.566 19.915 48.388 1.00 35.61 C ANISOU 2396 CB LEU A 293 4265 4452 4811 305 -129 -50 C ATOM 2397 CG LEU A 293 11.894 20.839 47.213 1.00 53.24 C ANISOU 2397 CG LEU A 293 6558 6658 7013 342 -134 -46 C ATOM 2398 CD1 LEU A 293 10.790 20.811 46.167 1.00 47.92 C ANISOU 2398 CD1 LEU A 293 5866 6052 6290 343 -173 -43 C ATOM 2399 CD2 LEU A 293 12.138 22.268 47.698 1.00 42.92 C ANISOU 2399 CD2 LEU A 293 5271 5328 5709 415 -127 -31 C ATOM 2400 N PRO A 294 11.861 18.020 50.948 1.00 30.60 N ANISOU 2400 N PRO A 294 3533 3826 4269 222 -92 -51 N ATOM 2401 CA PRO A 294 11.470 17.665 52.325 1.00 32.26 C ANISOU 2401 CA PRO A 294 3671 4080 4507 216 -88 -39 C ATOM 2402 C PRO A 294 12.579 17.926 53.328 1.00 31.09 C ANISOU 2402 C PRO A 294 3536 3877 4398 225 -45 -38 C ATOM 2403 O PRO A 294 12.328 18.471 54.409 1.00 28.54 O ANISOU 2403 O PRO A 294 3174 3587 4082 264 -42 -29 O ATOM 2404 CB PRO A 294 11.123 16.172 52.220 1.00 34.46 C ANISOU 2404 CB PRO A 294 3914 4378 4802 137 -100 -42 C ATOM 2405 CG PRO A 294 10.774 15.963 50.776 1.00 35.66 C ANISOU 2405 CG PRO A 294 4104 4529 4915 117 -128 -55 C ATOM 2406 CD PRO A 294 11.662 16.900 50.010 1.00 32.19 C ANISOU 2406 CD PRO A 294 3743 4026 4460 158 -107 -64 C ATOM 2407 N PHE A 295 13.813 17.568 52.975 1.00 31.19 N ANISOU 2407 N PHE A 295 3606 3812 4434 192 -12 -44 N ATOM 2408 CA PHE A 295 14.959 17.836 53.837 1.00 31.83 C ANISOU 2408 CA PHE A 295 3704 3841 4549 196 29 -37 C ATOM 2409 C PHE A 295 15.185 19.335 54.010 1.00 30.15 C ANISOU 2409 C PHE A 295 3527 3612 4319 263 28 -32 C ATOM 2410 O PHE A 295 15.318 19.831 55.135 1.00 27.57 O ANISOU 2410 O PHE A 295 3178 3292 4006 288 40 -27 O ATOM 2411 CB PHE A 295 16.194 17.158 53.241 1.00 27.50 C ANISOU 2411 CB PHE A 295 3211 3219 4019 151 64 -38 C ATOM 2412 CG PHE A 295 17.425 17.244 54.101 1.00 34.92 C ANISOU 2412 CG PHE A 295 4163 4112 4995 142 109 -22 C ATOM 2413 CD1 PHE A 295 17.408 16.805 55.411 1.00 31.53 C ANISOU 2413 CD1 PHE A 295 3673 3708 4600 124 126 -13 C ATOM 2414 CD2 PHE A 295 18.610 17.734 53.582 1.00 34.47 C ANISOU 2414 CD2 PHE A 295 4175 3990 4934 150 134 -12 C ATOM 2415 CE1 PHE A 295 18.546 16.874 56.193 1.00 34.34 C ANISOU 2415 CE1 PHE A 295 4037 4026 4985 113 167 5 C ATOM 2416 CE2 PHE A 295 19.746 17.806 54.357 1.00 49.29 C ANISOU 2416 CE2 PHE A 295 6061 5829 6840 137 174 9 C ATOM 2417 CZ PHE A 295 19.715 17.374 55.664 1.00 38.69 C ANISOU 2417 CZ PHE A 295 4658 4512 5531 117 191 17 C ATOM 2418 N ALA A 296 15.232 20.075 52.901 1.00 29.37 N ANISOU 2418 N ALA A 296 3483 3488 4187 293 13 -35 N ATOM 2419 CA ALA A 296 15.474 21.513 52.981 1.00 27.97 C ANISOU 2419 CA ALA A 296 3347 3285 3995 354 9 -29 C ATOM 2420 C ALA A 296 14.414 22.207 53.825 1.00 33.68 C ANISOU 2420 C ALA A 296 4025 4069 4704 411 -13 -30 C ATOM 2421 O ALA A 296 14.719 23.154 54.560 1.00 30.34 O ANISOU 2421 O ALA A 296 3620 3623 4284 453 -7 -29 O ATOM 2422 CB ALA A 296 15.512 22.118 51.581 1.00 28.22 C ANISOU 2422 CB ALA A 296 3435 3294 3993 376 -9 -27 C ATOM 2423 N ILE A 297 13.163 21.752 53.733 1.00 28.59 N ANISOU 2423 N ILE A 297 3320 3502 4040 414 -40 -31 N ATOM 2424 CA ILE A 297 12.094 22.367 54.513 1.00 28.90 C ANISOU 2424 CA ILE A 297 3310 3611 4060 474 -60 -27 C ATOM 2425 C ILE A 297 12.211 21.972 55.980 1.00 28.72 C ANISOU 2425 C ILE A 297 3234 3612 4067 464 -41 -26 C ATOM 2426 O ILE A 297 12.125 22.818 56.877 1.00 32.82 O ANISOU 2426 O ILE A 297 3749 4139 4581 520 -38 -28 O ATOM 2427 CB ILE A 297 10.721 21.983 53.933 1.00 29.40 C ANISOU 2427 CB ILE A 297 3320 3760 4089 478 -96 -19 C ATOM 2428 CG1 ILE A 297 10.519 22.660 52.577 1.00 30.73 C ANISOU 2428 CG1 ILE A 297 3539 3915 4221 505 -116 -17 C ATOM 2429 CG2 ILE A 297 9.611 22.378 54.889 1.00 29.72 C ANISOU 2429 CG2 ILE A 297 3294 3888 4111 535 -112 -7 C ATOM 2430 CD1 ILE A 297 9.345 22.117 51.781 1.00 30.18 C ANISOU 2430 CD1 ILE A 297 3426 3925 4117 488 -151 -7 C ATOM 2431 N TYR A 298 12.403 20.679 56.248 1.00 32.43 N ANISOU 2431 N TYR A 298 3663 4092 4567 394 -28 -23 N ATOM 2432 CA TYR A 298 12.466 20.232 57.635 1.00 28.20 C ANISOU 2432 CA TYR A 298 3066 3588 4061 381 -10 -17 C ATOM 2433 C TYR A 298 13.650 20.851 58.362 1.00 31.04 C ANISOU 2433 C TYR A 298 3468 3882 4442 391 23 -22 C ATOM 2434 O TYR A 298 13.589 21.069 59.578 1.00 30.31 O ANISOU 2434 O TYR A 298 3337 3821 4359 413 32 -20 O ATOM 2435 CB TYR A 298 12.539 18.705 57.697 1.00 33.54 C ANISOU 2435 CB TYR A 298 3696 4277 4770 299 -2 -10 C ATOM 2436 CG TYR A 298 12.685 18.185 59.104 1.00 28.09 C ANISOU 2436 CG TYR A 298 2939 3620 4115 280 19 2 C ATOM 2437 CD1 TYR A 298 11.647 18.305 60.018 1.00 32.85 C ANISOU 2437 CD1 TYR A 298 3462 4316 4705 317 -1 14 C ATOM 2438 CD2 TYR A 298 13.862 17.592 59.524 1.00 31.26 C ANISOU 2438 CD2 TYR A 298 3353 3965 4559 230 59 5 C ATOM 2439 CE1 TYR A 298 11.781 17.844 61.313 1.00 34.06 C ANISOU 2439 CE1 TYR A 298 3548 4505 4887 301 18 26 C ATOM 2440 CE2 TYR A 298 14.006 17.129 60.810 1.00 34.73 C ANISOU 2440 CE2 TYR A 298 3726 4438 5030 212 79 19 C ATOM 2441 CZ TYR A 298 12.961 17.255 61.701 1.00 33.87 C ANISOU 2441 CZ TYR A 298 3538 4423 4908 247 57 29 C ATOM 2442 OH TYR A 298 13.105 16.794 62.987 1.00 36.96 O ANISOU 2442 OH TYR A 298 3859 4855 5329 230 77 45 O ATOM 2443 N CYS A 299 14.723 21.165 57.630 1.00 27.58 N ANISOU 2443 N CYS A 299 3110 3359 4010 376 39 -25 N ATOM 2444 CA CYS A 299 15.909 21.751 58.239 1.00 27.24 C ANISOU 2444 CA CYS A 299 3110 3253 3986 377 68 -22 C ATOM 2445 C CYS A 299 15.662 23.164 58.756 1.00 28.61 C ANISOU 2445 C CYS A 299 3311 3425 4135 451 53 -31 C ATOM 2446 O CYS A 299 16.375 23.610 59.662 1.00 38.64 O ANISOU 2446 O CYS A 299 4596 4666 5418 454 71 -31 O ATOM 2447 CB CYS A 299 17.067 21.748 57.238 1.00 27.01 C ANISOU 2447 CB CYS A 299 3157 3142 3964 343 85 -15 C ATOM 2448 SG CYS A 299 17.997 20.184 57.213 1.00 37.31 S ANISOU 2448 SG CYS A 299 4445 4423 5310 256 126 -1 S ATOM 2449 N VAL A 300 14.685 23.884 58.205 1.00 31.20 N ANISOU 2449 N VAL A 300 3646 3781 4426 512 20 -38 N ATOM 2450 CA VAL A 300 14.350 25.208 58.721 1.00 33.92 C ANISOU 2450 CA VAL A 300 4017 4124 4746 591 6 -48 C ATOM 2451 C VAL A 300 13.134 25.183 59.647 1.00 41.08 C ANISOU 2451 C VAL A 300 4847 5126 5634 641 -7 -52 C ATOM 2452 O VAL A 300 12.942 26.136 60.418 1.00 42.11 O ANISOU 2452 O VAL A 300 4992 5260 5748 706 -12 -64 O ATOM 2453 CB VAL A 300 14.113 26.224 57.580 1.00 38.37 C ANISOU 2453 CB VAL A 300 4646 4654 5280 640 -19 -47 C ATOM 2454 CG1 VAL A 300 15.398 26.501 56.828 1.00 42.09 C ANISOU 2454 CG1 VAL A 300 5196 5031 5765 604 -7 -39 C ATOM 2455 CG2 VAL A 300 13.062 25.730 56.622 1.00 33.56 C ANISOU 2455 CG2 VAL A 300 3998 4106 4646 643 -42 -41 C ATOM 2456 N VAL A 301 12.317 24.133 59.598 1.00 30.66 N ANISOU 2456 N VAL A 301 3450 3885 4315 613 -15 -41 N ATOM 2457 CA VAL A 301 11.126 24.044 60.442 1.00 31.68 C ANISOU 2457 CA VAL A 301 3496 4117 4423 658 -30 -35 C ATOM 2458 C VAL A 301 11.407 23.275 61.727 1.00 38.65 C ANISOU 2458 C VAL A 301 4314 5035 5337 621 -7 -31 C ATOM 2459 O VAL A 301 10.939 23.662 62.801 1.00 36.93 O ANISOU 2459 O VAL A 301 4055 4873 5105 674 -8 -34 O ATOM 2460 CB VAL A 301 9.968 23.398 59.652 1.00 30.06 C ANISOU 2460 CB VAL A 301 3236 3988 4196 648 -58 -17 C ATOM 2461 CG1 VAL A 301 8.812 23.068 60.580 1.00 45.62 C ANISOU 2461 CG1 VAL A 301 5107 6076 6149 679 -72 0 C ATOM 2462 CG2 VAL A 301 9.505 24.314 58.535 1.00 40.09 C ANISOU 2462 CG2 VAL A 301 4560 5245 5428 702 -81 -17 C ATOM 2463 N GLY A 302 12.153 22.178 61.639 1.00 32.62 N ANISOU 2463 N GLY A 302 3537 4242 4614 534 13 -23 N ATOM 2464 CA GLY A 302 12.421 21.362 62.804 1.00 36.50 C ANISOU 2464 CA GLY A 302 3961 4769 5139 494 36 -13 C ATOM 2465 C GLY A 302 13.392 22.024 63.762 1.00 35.72 C ANISOU 2465 C GLY A 302 3895 4624 5051 507 63 -25 C ATOM 2466 O GLY A 302 13.967 23.080 63.493 1.00 39.33 O ANISOU 2466 O GLY A 302 4436 5012 5495 539 64 -40 O ATOM 2467 N SER A 303 13.576 21.379 64.914 1.00 36.49 N ANISOU 2467 N SER A 303 3924 4765 5174 478 83 -14 N ATOM 2468 CA SER A 303 14.509 21.857 65.925 1.00 40.49 C ANISOU 2468 CA SER A 303 4451 5240 5693 479 110 -22 C ATOM 2469 C SER A 303 15.217 20.670 66.560 1.00 39.97 C ANISOU 2469 C SER A 303 4328 5184 5675 398 144 1 C ATOM 2470 O SER A 303 14.836 19.511 66.368 1.00 40.64 O ANISOU 2470 O SER A 303 4351 5308 5784 352 143 21 O ATOM 2471 CB SER A 303 13.811 22.681 67.010 1.00 54.03 C ANISOU 2471 CB SER A 303 6136 7021 7374 559 98 -36 C ATOM 2472 OG SER A 303 13.232 21.839 67.993 1.00 71.68 O ANISOU 2472 OG SER A 303 8260 9356 9619 548 103 -18 O ATOM 2473 N HIS A 304 16.251 20.981 67.345 1.00 41.22 N ANISOU 2473 N HIS A 304 4508 5306 5848 382 172 0 N ATOM 2474 CA HIS A 304 17.120 19.949 67.897 1.00 44.85 C ANISOU 2474 CA HIS A 304 4924 5763 6353 305 211 27 C ATOM 2475 C HIS A 304 16.386 19.008 68.843 1.00 37.41 C ANISOU 2475 C HIS A 304 3862 4924 5428 292 212 46 C ATOM 2476 O HIS A 304 16.860 17.890 69.075 1.00 39.91 O ANISOU 2476 O HIS A 304 4131 5246 5789 224 239 74 O ATOM 2477 CB HIS A 304 18.307 20.597 68.617 1.00 48.72 C ANISOU 2477 CB HIS A 304 5458 6205 6847 293 238 25 C ATOM 2478 CG HIS A 304 17.919 21.479 69.762 1.00 51.40 C ANISOU 2478 CG HIS A 304 5781 6594 7157 354 227 4 C ATOM 2479 ND1 HIS A 304 17.786 21.009 71.052 1.00 58.27 N ANISOU 2479 ND1 HIS A 304 6560 7543 8037 345 243 16 N ATOM 2480 CD2 HIS A 304 17.642 22.804 69.814 1.00 49.50 C ANISOU 2480 CD2 HIS A 304 5603 6331 6872 426 202 -28 C ATOM 2481 CE1 HIS A 304 17.438 22.005 71.847 1.00 54.58 C ANISOU 2481 CE1 HIS A 304 6102 7104 7531 412 229 -11 C ATOM 2482 NE2 HIS A 304 17.344 23.104 71.122 1.00 64.65 N ANISOU 2482 NE2 HIS A 304 7474 8317 8775 463 204 -39 N ATOM 2483 N GLU A 305 15.241 19.423 69.386 1.00 39.98 N ANISOU 2483 N GLU A 305 4137 5333 5720 358 185 36 N ATOM 2484 CA GLU A 305 14.478 18.543 70.261 1.00 44.35 C ANISOU 2484 CA GLU A 305 4570 5995 6287 348 182 62 C ATOM 2485 C GLU A 305 13.830 17.386 69.511 1.00 52.60 C ANISOU 2485 C GLU A 305 5567 7065 7353 302 165 86 C ATOM 2486 O GLU A 305 13.515 16.367 70.134 1.00 39.73 O ANISOU 2486 O GLU A 305 3841 5504 5752 263 168 117 O ATOM 2487 CB GLU A 305 13.393 19.331 70.992 1.00 41.33 C ANISOU 2487 CB GLU A 305 4146 5703 5855 439 156 49 C ATOM 2488 CG GLU A 305 13.914 20.419 71.916 1.00 62.36 C ANISOU 2488 CG GLU A 305 6847 8352 8493 488 169 22 C ATOM 2489 CD GLU A 305 12.801 21.073 72.715 1.00 77.44 C ANISOU 2489 CD GLU A 305 8710 10362 10354 583 147 11 C ATOM 2490 OE1 GLU A 305 11.859 20.359 73.120 1.00 76.92 O ANISOU 2490 OE1 GLU A 305 8537 10404 10286 589 134 40 O ATOM 2491 OE2 GLU A 305 12.860 22.301 72.927 1.00 94.75 O ANISOU 2491 OE2 GLU A 305 10971 12524 12506 653 140 -24 O ATOM 2492 N ASP A 306 13.614 17.517 68.203 1.00 36.56 N ANISOU 2492 N ASP A 306 3601 4983 5308 303 144 73 N ATOM 2493 CA ASP A 306 12.978 16.444 67.454 1.00 41.72 C ANISOU 2493 CA ASP A 306 4217 5657 5977 256 123 92 C ATOM 2494 C ASP A 306 13.824 15.172 67.540 1.00 29.52 C ANISOU 2494 C ASP A 306 2650 4075 4490 166 155 115 C ATOM 2495 O ASP A 306 15.055 15.238 67.579 1.00 33.56 O ANISOU 2495 O ASP A 306 3214 4512 5025 138 194 111 O ATOM 2496 CB ASP A 306 12.800 16.826 65.983 1.00 35.27 C ANISOU 2496 CB ASP A 306 3485 4782 5135 267 100 73 C ATOM 2497 CG ASP A 306 11.920 18.047 65.784 1.00 43.57 C ANISOU 2497 CG ASP A 306 4559 5868 6129 357 69 55 C ATOM 2498 OD1 ASP A 306 11.203 18.445 66.729 1.00 32.56 O ANISOU 2498 OD1 ASP A 306 3104 4558 4711 413 59 61 O ATOM 2499 OD2 ASP A 306 11.938 18.602 64.662 1.00 37.49 O ANISOU 2499 OD2 ASP A 306 3867 5043 5337 375 56 38 O ATOM 2500 N PRO A 307 13.192 13.996 67.554 1.00 33.50 N ANISOU 2500 N PRO A 307 3079 4630 5020 118 140 142 N ATOM 2501 CA PRO A 307 13.964 12.753 67.453 1.00 38.63 C ANISOU 2501 CA PRO A 307 3720 5230 5725 34 168 162 C ATOM 2502 C PRO A 307 14.741 12.711 66.147 1.00 36.23 C ANISOU 2502 C PRO A 307 3525 4817 5425 8 181 140 C ATOM 2503 O PRO A 307 14.287 13.210 65.116 1.00 37.39 O ANISOU 2503 O PRO A 307 3729 4943 5535 35 151 118 O ATOM 2504 CB PRO A 307 12.893 11.656 67.504 1.00 37.85 C ANISOU 2504 CB PRO A 307 3534 5206 5643 -5 133 191 C ATOM 2505 CG PRO A 307 11.682 12.306 68.073 1.00 48.44 C ANISOU 2505 CG PRO A 307 4808 6657 6940 60 97 198 C ATOM 2506 CD PRO A 307 11.747 13.742 67.658 1.00 30.54 C ANISOU 2506 CD PRO A 307 2623 4358 4621 137 94 160 C ATOM 2507 N ALA A 308 15.923 12.092 66.199 1.00 34.70 N ANISOU 2507 N ALA A 308 3355 4556 5272 -43 226 151 N ATOM 2508 CA ALA A 308 16.834 12.133 65.061 1.00 38.03 C ANISOU 2508 CA ALA A 308 3881 4876 5694 -60 245 135 C ATOM 2509 C ALA A 308 16.281 11.416 63.839 1.00 33.59 C ANISOU 2509 C ALA A 308 3347 4289 5127 -89 216 124 C ATOM 2510 O ALA A 308 16.753 11.670 62.726 1.00 34.76 O ANISOU 2510 O ALA A 308 3583 4366 5257 -85 219 104 O ATOM 2511 CB ALA A 308 18.183 11.520 65.440 1.00 39.77 C ANISOU 2511 CB ALA A 308 4110 5043 5959 -106 302 158 C ATOM 2512 N VAL A 309 15.294 10.533 64.015 1.00 27.46 N ANISOU 2512 N VAL A 309 2497 3572 4364 -119 184 138 N ATOM 2513 CA VAL A 309 14.798 9.738 62.896 1.00 31.86 C ANISOU 2513 CA VAL A 309 3083 4105 4920 -159 154 128 C ATOM 2514 C VAL A 309 14.223 10.626 61.802 1.00 38.03 C ANISOU 2514 C VAL A 309 3926 4882 5644 -115 118 98 C ATOM 2515 O VAL A 309 14.256 10.268 60.619 1.00 34.51 O ANISOU 2515 O VAL A 309 3542 4384 5187 -138 106 80 O ATOM 2516 CB VAL A 309 13.751 8.718 63.386 1.00 35.13 C ANISOU 2516 CB VAL A 309 3399 4592 5355 -201 119 156 C ATOM 2517 CG1 VAL A 309 12.570 9.423 64.048 1.00 39.03 C ANISOU 2517 CG1 VAL A 309 3817 5198 5815 -151 80 168 C ATOM 2518 CG2 VAL A 309 13.272 7.854 62.227 1.00 41.17 C ANISOU 2518 CG2 VAL A 309 4200 5325 6117 -251 85 144 C ATOM 2519 N TYR A 310 13.675 11.783 62.168 1.00 32.97 N ANISOU 2519 N TYR A 310 3267 4294 4964 -48 100 94 N ATOM 2520 CA TYR A 310 13.042 12.630 61.166 1.00 33.23 C ANISOU 2520 CA TYR A 310 3351 4331 4944 -4 65 72 C ATOM 2521 C TYR A 310 14.084 13.321 60.302 1.00 31.99 C ANISOU 2521 C TYR A 310 3300 4081 4774 15 90 48 C ATOM 2522 O TYR A 310 13.840 13.573 59.117 1.00 32.37 O ANISOU 2522 O TYR A 310 3405 4105 4790 24 68 30 O ATOM 2523 CB TYR A 310 12.113 13.623 61.856 1.00 32.12 C ANISOU 2523 CB TYR A 310 3158 4278 4767 67 40 78 C ATOM 2524 CG TYR A 310 10.995 12.910 62.584 1.00 35.71 C ANISOU 2524 CG TYR A 310 3503 4836 5228 49 9 108 C ATOM 2525 CD1 TYR A 310 9.975 12.292 61.876 1.00 38.53 C ANISOU 2525 CD1 TYR A 310 3835 5235 5569 17 -37 118 C ATOM 2526 CD2 TYR A 310 10.976 12.824 63.970 1.00 43.09 C ANISOU 2526 CD2 TYR A 310 4357 5831 6185 58 25 131 C ATOM 2527 CE1 TYR A 310 8.956 11.625 62.522 1.00 44.38 C ANISOU 2527 CE1 TYR A 310 4473 6075 6316 -4 -69 155 C ATOM 2528 CE2 TYR A 310 9.953 12.156 64.631 1.00 39.16 C ANISOU 2528 CE2 TYR A 310 3753 5436 5692 42 -5 167 C ATOM 2529 CZ TYR A 310 8.948 11.557 63.900 1.00 45.69 C ANISOU 2529 CZ TYR A 310 4556 6302 6504 9 -53 180 C ATOM 2530 OH TYR A 310 7.925 10.888 64.534 1.00 52.59 O ANISOU 2530 OH TYR A 310 5320 7281 7381 -12 -87 223 O ATOM 2531 N THR A 311 15.255 13.600 60.871 1.00 30.66 N ANISOU 2531 N THR A 311 3157 3865 4629 18 136 52 N ATOM 2532 CA THR A 311 16.377 14.089 60.082 1.00 30.99 C ANISOU 2532 CA THR A 311 3294 3818 4663 24 162 40 C ATOM 2533 C THR A 311 16.907 12.997 59.164 1.00 37.56 C ANISOU 2533 C THR A 311 4167 4591 5514 -32 177 38 C ATOM 2534 O THR A 311 17.144 13.233 57.974 1.00 29.31 O ANISOU 2534 O THR A 311 3195 3500 4444 -24 171 21 O ATOM 2535 CB THR A 311 17.474 14.593 61.017 1.00 33.54 C ANISOU 2535 CB THR A 311 3624 4114 5005 33 205 54 C ATOM 2536 OG1 THR A 311 16.981 15.710 61.765 1.00 36.68 O ANISOU 2536 OG1 THR A 311 4000 4558 5378 92 188 48 O ATOM 2537 CG2 THR A 311 18.719 15.006 60.244 1.00 37.94 C ANISOU 2537 CG2 THR A 311 4274 4585 5557 32 233 53 C ATOM 2538 N TYR A 312 17.092 11.788 59.704 1.00 31.30 N ANISOU 2538 N TYR A 312 3327 3801 4766 -86 197 55 N ATOM 2539 CA TYR A 312 17.538 10.668 58.885 1.00 32.47 C ANISOU 2539 CA TYR A 312 3515 3891 4932 -137 211 50 C ATOM 2540 C TYR A 312 16.558 10.375 57.760 1.00 31.07 C ANISOU 2540 C TYR A 312 3358 3723 4723 -147 162 26 C ATOM 2541 O TYR A 312 16.967 10.124 56.621 1.00 30.22 O ANISOU 2541 O TYR A 312 3325 3558 4600 -157 166 7 O ATOM 2542 CB TYR A 312 17.705 9.417 59.742 1.00 35.34 C ANISOU 2542 CB TYR A 312 3816 4262 5351 -191 234 75 C ATOM 2543 CG TYR A 312 18.924 9.409 60.619 1.00 32.69 C ANISOU 2543 CG TYR A 312 3472 3900 5050 -197 293 102 C ATOM 2544 CD1 TYR A 312 20.200 9.477 60.073 1.00 33.99 C ANISOU 2544 CD1 TYR A 312 3711 3989 5214 -196 337 106 C ATOM 2545 CD2 TYR A 312 18.802 9.300 61.998 1.00 39.48 C ANISOU 2545 CD2 TYR A 312 4244 4817 5940 -204 304 129 C ATOM 2546 CE1 TYR A 312 21.320 9.455 60.881 1.00 40.01 C ANISOU 2546 CE1 TYR A 312 4463 4735 6006 -204 391 138 C ATOM 2547 CE2 TYR A 312 19.916 9.278 62.813 1.00 36.50 C ANISOU 2547 CE2 TYR A 312 3855 4422 5592 -213 358 157 C ATOM 2548 CZ TYR A 312 21.170 9.351 62.251 1.00 36.28 C ANISOU 2548 CZ TYR A 312 3903 4319 5564 -215 401 163 C ATOM 2549 OH TYR A 312 22.278 9.328 63.059 1.00 39.94 O ANISOU 2549 OH TYR A 312 4352 4771 6053 -227 454 197 O ATOM 2550 N ALA A 313 15.258 10.382 58.065 1.00 29.89 N ANISOU 2550 N ALA A 313 3142 3653 4560 -144 115 29 N ATOM 2551 CA ALA A 313 14.271 9.967 57.080 1.00 28.81 C ANISOU 2551 CA ALA A 313 3015 3535 4395 -166 65 13 C ATOM 2552 C ALA A 313 14.185 10.952 55.926 1.00 33.47 C ANISOU 2552 C ALA A 313 3676 4109 4931 -121 48 -11 C ATOM 2553 O ALA A 313 13.839 10.560 54.807 1.00 34.25 O ANISOU 2553 O ALA A 313 3815 4193 5006 -144 21 -30 O ATOM 2554 CB ALA A 313 12.901 9.804 57.738 1.00 38.58 C ANISOU 2554 CB ALA A 313 4158 4874 5629 -172 18 33 C ATOM 2555 N THR A 314 14.483 12.225 56.174 1.00 31.85 N ANISOU 2555 N THR A 314 3487 3906 4707 -59 60 -9 N ATOM 2556 CA THR A 314 14.494 13.209 55.103 1.00 32.29 C ANISOU 2556 CA THR A 314 3610 3942 4716 -15 46 -27 C ATOM 2557 C THR A 314 15.869 13.349 54.469 1.00 34.66 C ANISOU 2557 C THR A 314 3994 4153 5020 -14 87 -34 C ATOM 2558 O THR A 314 15.966 13.736 53.297 1.00 34.76 O ANISOU 2558 O THR A 314 4068 4140 4998 2 76 -49 O ATOM 2559 CB THR A 314 14.021 14.571 55.622 1.00 27.77 C ANISOU 2559 CB THR A 314 3017 3416 4118 56 33 -20 C ATOM 2560 OG1 THR A 314 14.856 15.001 56.703 1.00 30.14 O ANISOU 2560 OG1 THR A 314 3309 3696 4446 74 71 -9 O ATOM 2561 CG2 THR A 314 12.584 14.491 56.093 1.00 29.74 C ANISOU 2561 CG2 THR A 314 3183 3763 4351 65 -10 -9 C ATOM 2562 N LEU A 315 16.930 13.016 55.207 1.00 34.87 N ANISOU 2562 N LEU A 315 4021 4141 5088 -32 135 -19 N ATOM 2563 CA LEU A 315 18.276 13.101 54.656 1.00 26.86 C ANISOU 2563 CA LEU A 315 3079 3050 4075 -32 176 -16 C ATOM 2564 C LEU A 315 18.558 11.962 53.687 1.00 35.80 C ANISOU 2564 C LEU A 315 4254 4139 5209 -74 184 -30 C ATOM 2565 O LEU A 315 19.210 12.170 52.658 1.00 30.22 O ANISOU 2565 O LEU A 315 3618 3386 4477 -61 195 -38 O ATOM 2566 CB LEU A 315 19.307 13.092 55.781 1.00 37.20 C ANISOU 2566 CB LEU A 315 4370 4339 5424 -40 224 11 C ATOM 2567 CG LEU A 315 20.769 12.954 55.350 1.00 43.87 C ANISOU 2567 CG LEU A 315 5280 5113 6277 -48 273 27 C ATOM 2568 CD1 LEU A 315 21.209 14.121 54.469 1.00 42.83 C ANISOU 2568 CD1 LEU A 315 5217 4953 6104 -5 266 25 C ATOM 2569 CD2 LEU A 315 21.651 12.842 56.579 1.00 44.01 C ANISOU 2569 CD2 LEU A 315 5263 5125 6333 -63 319 59 C ATOM 2570 N LEU A 316 18.088 10.756 53.997 1.00 29.17 N ANISOU 2570 N LEU A 316 3373 3312 4398 -124 177 -33 N ATOM 2571 CA LEU A 316 18.432 9.607 53.163 1.00 34.46 C ANISOU 2571 CA LEU A 316 4091 3930 5072 -164 187 -49 C ATOM 2572 C LEU A 316 18.004 9.803 51.714 1.00 35.81 C ANISOU 2572 C LEU A 316 4322 4095 5191 -154 153 -80 C ATOM 2573 O LEU A 316 18.811 9.521 50.812 1.00 33.47 O ANISOU 2573 O LEU A 316 4097 3742 4880 -153 177 -91 O ATOM 2574 CB LEU A 316 17.830 8.332 53.762 1.00 37.61 C ANISOU 2574 CB LEU A 316 4433 4346 5511 -222 175 -46 C ATOM 2575 CG LEU A 316 18.231 7.040 53.050 1.00 61.81 C ANISOU 2575 CG LEU A 316 7550 7348 8588 -266 189 -63 C ATOM 2576 CD1 LEU A 316 19.723 6.751 53.229 1.00 43.76 C ANISOU 2576 CD1 LEU A 316 5303 4996 6329 -260 258 -45 C ATOM 2577 CD2 LEU A 316 17.384 5.890 53.554 1.00 63.23 C ANISOU 2577 CD2 LEU A 316 7672 7550 8802 -326 160 -60 C ATOM 2578 N PRO A 317 16.790 10.275 51.413 1.00 36.91 N ANISOU 2578 N PRO A 317 4434 4293 5297 -143 99 -91 N ATOM 2579 CA PRO A 317 16.439 10.508 50.001 1.00 39.11 C ANISOU 2579 CA PRO A 317 4768 4569 5522 -133 68 -117 C ATOM 2580 C PRO A 317 17.339 11.520 49.316 1.00 35.48 C ANISOU 2580 C PRO A 317 4372 4075 5034 -82 92 -114 C ATOM 2581 O PRO A 317 17.658 11.361 48.131 1.00 34.51 O ANISOU 2581 O PRO A 317 4312 3921 4879 -81 92 -133 O ATOM 2582 CB PRO A 317 14.988 11.004 50.080 1.00 43.58 C ANISOU 2582 CB PRO A 317 5277 5218 6061 -124 11 -116 C ATOM 2583 CG PRO A 317 14.478 10.480 51.379 1.00 43.39 C ANISOU 2583 CG PRO A 317 5171 5236 6080 -152 6 -95 C ATOM 2584 CD PRO A 317 15.647 10.516 52.310 1.00 40.91 C ANISOU 2584 CD PRO A 317 4856 4878 5810 -142 63 -77 C ATOM 2585 N ALA A 318 17.753 12.567 50.031 1.00 31.02 N ANISOU 2585 N ALA A 318 3791 3515 4479 -40 110 -90 N ATOM 2586 CA ALA A 318 18.662 13.543 49.444 1.00 32.97 C ANISOU 2586 CA ALA A 318 4098 3728 4703 3 130 -80 C ATOM 2587 C ALA A 318 19.954 12.879 48.985 1.00 37.36 C ANISOU 2587 C ALA A 318 4710 4218 5268 -12 177 -75 C ATOM 2588 O ALA A 318 20.504 13.233 47.935 1.00 36.66 O ANISOU 2588 O ALA A 318 4680 4104 5144 10 183 -76 O ATOM 2589 CB ALA A 318 18.952 14.656 50.449 1.00 33.30 C ANISOU 2589 CB ALA A 318 4115 3778 4760 41 142 -54 C ATOM 2590 N THR A 319 20.451 11.904 49.751 1.00 34.10 N ANISOU 2590 N THR A 319 4277 3781 4898 -48 212 -66 N ATOM 2591 CA THR A 319 21.653 11.193 49.330 1.00 36.23 C ANISOU 2591 CA THR A 319 4600 3991 5174 -58 261 -59 C ATOM 2592 C THR A 319 21.378 10.300 48.127 1.00 34.09 C ANISOU 2592 C THR A 319 4377 3700 4874 -77 245 -95 C ATOM 2593 O THR A 319 22.264 10.106 47.286 1.00 39.46 O ANISOU 2593 O THR A 319 5121 4341 5533 -63 274 -95 O ATOM 2594 CB THR A 319 22.214 10.357 50.483 1.00 31.11 C ANISOU 2594 CB THR A 319 3914 3325 4581 -90 304 -36 C ATOM 2595 OG1 THR A 319 21.388 9.205 50.698 1.00 30.82 O ANISOU 2595 OG1 THR A 319 3845 3297 4568 -136 284 -59 O ATOM 2596 CG2 THR A 319 22.268 11.177 51.746 1.00 28.73 C ANISOU 2596 CG2 THR A 319 3557 3054 4306 -77 310 -7 C ATOM 2597 N LEU A 320 20.165 9.745 48.032 1.00 33.96 N ANISOU 2597 N LEU A 320 4332 3715 4855 -110 200 -125 N ATOM 2598 CA LEU A 320 19.832 8.887 46.900 1.00 39.53 C ANISOU 2598 CA LEU A 320 5087 4402 5531 -135 179 -163 C ATOM 2599 C LEU A 320 19.938 9.640 45.584 1.00 30.04 C ANISOU 2599 C LEU A 320 3940 3204 4267 -96 164 -176 C ATOM 2600 O LEU A 320 20.199 9.033 44.540 1.00 32.63 O ANISOU 2600 O LEU A 320 4330 3503 4566 -102 167 -203 O ATOM 2601 CB LEU A 320 18.422 8.319 47.065 1.00 39.71 C ANISOU 2601 CB LEU A 320 5063 4469 5557 -181 123 -185 C ATOM 2602 CG LEU A 320 18.186 7.413 48.276 1.00 60.60 C ANISOU 2602 CG LEU A 320 7649 7115 8262 -227 130 -171 C ATOM 2603 CD1 LEU A 320 16.750 6.895 48.285 1.00 46.79 C ANISOU 2603 CD1 LEU A 320 5856 5416 6507 -274 67 -187 C ATOM 2604 CD2 LEU A 320 19.176 6.253 48.316 1.00 47.50 C ANISOU 2604 CD2 LEU A 320 6031 5381 6634 -251 178 -174 C ATOM 2605 N ASN A 321 19.730 10.956 45.611 1.00 34.18 N ANISOU 2605 N ASN A 321 4446 3767 4774 -55 147 -157 N ATOM 2606 CA ASN A 321 19.858 11.738 44.392 1.00 32.97 C ANISOU 2606 CA ASN A 321 4339 3621 4566 -17 133 -162 C ATOM 2607 C ASN A 321 21.282 11.696 43.861 1.00 37.76 C ANISOU 2607 C ASN A 321 5008 4176 5162 7 183 -146 C ATOM 2608 O ASN A 321 21.492 11.726 42.643 1.00 34.35 O ANISOU 2608 O ASN A 321 4627 3740 4684 25 178 -160 O ATOM 2609 CB ASN A 321 19.420 13.179 44.648 1.00 33.88 C ANISOU 2609 CB ASN A 321 4422 3779 4671 24 109 -139 C ATOM 2610 CG ASN A 321 19.260 13.974 43.366 1.00 38.37 C ANISOU 2610 CG ASN A 321 5027 4368 5183 58 84 -143 C ATOM 2611 OD1 ASN A 321 20.015 14.910 43.099 1.00 51.45 O ANISOU 2611 OD1 ASN A 321 6709 6011 6829 99 100 -116 O ATOM 2612 ND2 ASN A 321 18.282 13.591 42.557 1.00 34.17 N ANISOU 2612 ND2 ASN A 321 4496 3871 4616 39 43 -174 N ATOM 2613 N SER A 322 22.273 11.619 44.753 1.00 28.44 N ANISOU 2613 N SER A 322 3819 2964 4022 10 232 -113 N ATOM 2614 CA SER A 322 23.652 11.467 44.312 1.00 30.58 C ANISOU 2614 CA SER A 322 4143 3192 4283 31 282 -90 C ATOM 2615 C SER A 322 23.911 10.100 43.689 1.00 31.64 C ANISOU 2615 C SER A 322 4325 3289 4409 11 302 -120 C ATOM 2616 O SER A 322 24.924 9.934 43.005 1.00 32.99 O ANISOU 2616 O SER A 322 4548 3432 4554 37 339 -108 O ATOM 2617 CB SER A 322 24.604 11.709 45.486 1.00 36.62 C ANISOU 2617 CB SER A 322 4883 3939 5094 34 328 -41 C ATOM 2618 OG SER A 322 24.577 13.069 45.889 1.00 38.50 O ANISOU 2618 OG SER A 322 5097 4201 5330 60 312 -12 O ATOM 2619 N MET A 323 23.028 9.118 43.911 1.00 34.07 N ANISOU 2619 N MET A 323 4615 3595 4734 -35 279 -158 N ATOM 2620 CA MET A 323 23.117 7.858 43.181 1.00 39.52 C ANISOU 2620 CA MET A 323 5360 4246 5410 -55 286 -197 C ATOM 2621 C MET A 323 22.500 7.953 41.800 1.00 34.91 C ANISOU 2621 C MET A 323 4819 3682 4761 -49 243 -238 C ATOM 2622 O MET A 323 22.866 7.181 40.910 1.00 39.21 O ANISOU 2622 O MET A 323 5429 4193 5275 -46 256 -268 O ATOM 2623 CB MET A 323 22.387 6.732 43.908 1.00 44.73 C ANISOU 2623 CB MET A 323 5989 4893 6114 -114 271 -220 C ATOM 2624 CG MET A 323 22.930 6.344 45.230 1.00 40.15 C ANISOU 2624 CG MET A 323 5365 4292 5598 -129 314 -184 C ATOM 2625 SD MET A 323 21.880 5.036 45.899 1.00 48.95 S ANISOU 2625 SD MET A 323 6441 5400 6759 -202 282 -211 S ATOM 2626 CE MET A 323 22.460 5.063 47.586 1.00 50.31 C ANISOU 2626 CE MET A 323 6539 5574 7003 -208 329 -156 C ATOM 2627 N ILE A 324 21.534 8.852 41.629 1.00 37.85 N ANISOU 2627 N ILE A 324 5156 4111 5113 -46 192 -242 N ATOM 2628 CA ILE A 324 20.829 8.995 40.363 1.00 33.55 C ANISOU 2628 CA ILE A 324 4642 3597 4507 -44 147 -277 C ATOM 2629 C ILE A 324 21.607 9.891 39.417 1.00 30.97 C ANISOU 2629 C ILE A 324 4354 3279 4134 14 163 -257 C ATOM 2630 O ILE A 324 21.669 9.626 38.211 1.00 33.57 O ANISOU 2630 O ILE A 324 4736 3609 4409 24 155 -285 O ATOM 2631 CB ILE A 324 19.418 9.553 40.629 1.00 38.48 C ANISOU 2631 CB ILE A 324 5205 4287 5130 -64 87 -281 C ATOM 2632 CG1 ILE A 324 18.621 8.615 41.533 1.00 50.11 C ANISOU 2632 CG1 ILE A 324 6634 5759 6646 -124 67 -294 C ATOM 2633 CG2 ILE A 324 18.668 9.773 39.337 1.00 36.90 C ANISOU 2633 CG2 ILE A 324 5029 4128 4865 -64 40 -310 C ATOM 2634 CD1 ILE A 324 17.315 9.218 42.000 1.00 62.50 C ANISOU 2634 CD1 ILE A 324 8130 7399 8217 -137 15 -285 C ATOM 2635 N ASN A 325 22.189 10.969 39.946 1.00 31.06 N ANISOU 2635 N ASN A 325 4340 3299 4163 50 184 -207 N ATOM 2636 CA ASN A 325 22.955 11.915 39.138 1.00 36.77 C ANISOU 2636 CA ASN A 325 5093 4032 4847 102 196 -176 C ATOM 2637 C ASN A 325 23.911 11.252 38.157 1.00 37.68 C ANISOU 2637 C ASN A 325 5275 4117 4923 123 231 -185 C ATOM 2638 O ASN A 325 23.851 11.575 36.961 1.00 35.99 O ANISOU 2638 O ASN A 325 5093 3931 4652 148 212 -196 O ATOM 2639 CB ASN A 325 23.737 12.856 40.066 1.00 33.92 C ANISOU 2639 CB ASN A 325 4703 3662 4522 127 224 -117 C ATOM 2640 CG ASN A 325 22.861 13.909 40.704 1.00 34.91 C ANISOU 2640 CG ASN A 325 4774 3825 4665 130 186 -105 C ATOM 2641 OD1 ASN A 325 21.763 14.182 40.229 1.00 35.50 O ANISOU 2641 OD1 ASN A 325 4832 3941 4714 127 139 -130 O ATOM 2642 ND2 ASN A 325 23.351 14.518 41.776 1.00 35.38 N ANISOU 2642 ND2 ASN A 325 4805 3873 4766 138 206 -66 N ATOM 2643 N PRO A 326 24.800 10.345 38.568 1.00 30.80 N ANISOU 2643 N PRO A 326 4428 3196 4076 119 282 -179 N ATOM 2644 CA PRO A 326 25.739 9.769 37.591 1.00 36.29 C ANISOU 2644 CA PRO A 326 5192 3869 4728 150 318 -184 C ATOM 2645 C PRO A 326 25.050 8.996 36.485 1.00 31.37 C ANISOU 2645 C PRO A 326 4616 3248 4055 136 286 -251 C ATOM 2646 O PRO A 326 25.568 8.937 35.363 1.00 35.80 O ANISOU 2646 O PRO A 326 5229 3816 4559 173 297 -258 O ATOM 2647 CB PRO A 326 26.633 8.863 38.451 1.00 32.63 C ANISOU 2647 CB PRO A 326 4736 3351 4309 142 377 -166 C ATOM 2648 CG PRO A 326 25.862 8.611 39.699 1.00 37.75 C ANISOU 2648 CG PRO A 326 5328 3993 5021 91 360 -174 C ATOM 2649 CD PRO A 326 25.029 9.829 39.929 1.00 29.86 C ANISOU 2649 CD PRO A 326 4276 3046 4024 90 312 -163 C ATOM 2650 N ILE A 327 23.889 8.405 36.759 1.00 32.57 N ANISOU 2650 N ILE A 327 4750 3401 4225 82 245 -297 N ATOM 2651 CA ILE A 327 23.178 7.672 35.718 1.00 32.37 C ANISOU 2651 CA ILE A 327 4771 3379 4150 59 208 -361 C ATOM 2652 C ILE A 327 22.590 8.640 34.701 1.00 32.62 C ANISOU 2652 C ILE A 327 4795 3476 4122 79 163 -365 C ATOM 2653 O ILE A 327 22.697 8.432 33.488 1.00 34.47 O ANISOU 2653 O ILE A 327 5082 3722 4294 98 156 -394 O ATOM 2654 CB ILE A 327 22.097 6.776 36.350 1.00 35.63 C ANISOU 2654 CB ILE A 327 5162 3777 4599 -12 172 -401 C ATOM 2655 CG1 ILE A 327 22.753 5.733 37.256 1.00 42.93 C ANISOU 2655 CG1 ILE A 327 6099 4633 5581 -29 219 -397 C ATOM 2656 CG2 ILE A 327 21.255 6.100 35.270 1.00 43.32 C ANISOU 2656 CG2 ILE A 327 6182 4759 5519 -45 123 -466 C ATOM 2657 CD1 ILE A 327 21.795 5.037 38.188 1.00 46.25 C ANISOU 2657 CD1 ILE A 327 6476 5044 6053 -97 188 -414 C ATOM 2658 N ILE A 328 21.993 9.730 35.179 1.00 34.48 N ANISOU 2658 N ILE A 328 4966 3758 4377 79 134 -332 N ATOM 2659 CA AILE A 328 21.336 10.672 34.280 0.50 38.69 C ANISOU 2659 CA AILE A 328 5485 4356 4860 97 90 -331 C ATOM 2660 CA BILE A 328 21.337 10.675 34.281 0.50 38.69 C ANISOU 2660 CA BILE A 328 5485 4356 4860 97 90 -330 C ATOM 2661 C ILE A 328 22.365 11.455 33.474 1.00 32.41 C ANISOU 2661 C ILE A 328 4716 3573 4025 160 117 -293 C ATOM 2662 O ILE A 328 22.238 11.603 32.254 1.00 32.89 O ANISOU 2662 O ILE A 328 4805 3670 4023 179 98 -310 O ATOM 2663 CB AILE A 328 20.415 11.613 35.078 0.50 42.29 C ANISOU 2663 CB AILE A 328 5865 4854 5349 86 55 -304 C ATOM 2664 CB BILE A 328 20.430 11.625 35.081 0.50 42.28 C ANISOU 2664 CB BILE A 328 5865 4853 5348 87 56 -303 C ATOM 2665 CG1AILE A 328 19.282 10.818 35.735 0.50 34.77 C ANISOU 2665 CG1AILE A 328 4882 3905 4425 22 21 -337 C ATOM 2666 CG1BILE A 328 19.258 10.852 35.676 0.50 34.72 C ANISOU 2666 CG1BILE A 328 4875 3902 4415 24 19 -338 C ATOM 2667 CG2AILE A 328 19.869 12.717 34.179 0.50 43.55 C ANISOU 2667 CG2AILE A 328 6008 5079 5459 114 18 -290 C ATOM 2668 CG2BILE A 328 19.949 12.770 34.194 0.50 43.48 C ANISOU 2668 CG2BILE A 328 6000 5069 5452 118 20 -286 C ATOM 2669 CD1AILE A 328 18.407 10.057 34.758 0.50 39.85 C ANISOU 2669 CD1AILE A 328 5554 4571 5017 -18 -23 -392 C ATOM 2670 CD1BILE A 328 18.601 11.578 36.802 0.50 45.54 C ANISOU 2670 CD1BILE A 328 6172 5301 5831 19 2 -306 C ATOM 2671 N TYR A 329 23.392 11.976 34.141 1.00 37.70 N ANISOU 2671 N TYR A 329 5374 4219 4730 192 160 -238 N ATOM 2672 CA TYR A 329 24.292 12.914 33.489 1.00 34.73 C ANISOU 2672 CA TYR A 329 5010 3863 4321 248 178 -187 C ATOM 2673 C TYR A 329 25.563 12.286 32.942 1.00 33.57 C ANISOU 2673 C TYR A 329 4921 3690 4146 282 229 -178 C ATOM 2674 O TYR A 329 26.221 12.913 32.108 1.00 38.78 O ANISOU 2674 O TYR A 329 5595 4378 4762 328 238 -142 O ATOM 2675 CB TYR A 329 24.643 14.046 34.461 1.00 31.52 C ANISOU 2675 CB TYR A 329 4558 3457 3964 262 186 -124 C ATOM 2676 CG TYR A 329 23.436 14.901 34.781 1.00 31.02 C ANISOU 2676 CG TYR A 329 4441 3430 3913 249 135 -126 C ATOM 2677 CD1 TYR A 329 22.949 15.810 33.857 1.00 40.32 C ANISOU 2677 CD1 TYR A 329 5611 4661 5048 274 97 -117 C ATOM 2678 CD2 TYR A 329 22.766 14.775 35.987 1.00 30.72 C ANISOU 2678 CD2 TYR A 329 4361 3382 3929 214 125 -136 C ATOM 2679 CE1 TYR A 329 21.839 16.585 34.128 1.00 36.59 C ANISOU 2679 CE1 TYR A 329 5092 4225 4586 268 54 -116 C ATOM 2680 CE2 TYR A 329 21.652 15.546 36.268 1.00 35.65 C ANISOU 2680 CE2 TYR A 329 4939 4047 4562 210 80 -136 C ATOM 2681 CZ TYR A 329 21.195 16.452 35.333 1.00 37.94 C ANISOU 2681 CZ TYR A 329 5223 4384 4808 238 46 -125 C ATOM 2682 OH TYR A 329 20.087 17.225 35.600 1.00 39.42 O ANISOU 2682 OH TYR A 329 5364 4613 5000 240 5 -121 O ATOM 2683 N ALA A 330 25.919 11.070 33.353 1.00 33.72 N ANISOU 2683 N ALA A 330 4971 3656 4186 263 264 -206 N ATOM 2684 CA ALA A 330 27.145 10.443 32.867 1.00 33.86 C ANISOU 2684 CA ALA A 330 5044 3648 4174 303 319 -194 C ATOM 2685 C ALA A 330 26.882 9.143 32.117 1.00 38.79 C ANISOU 2685 C ALA A 330 5733 4248 4759 292 318 -268 C ATOM 2686 O ALA A 330 27.205 9.051 30.927 1.00 38.60 O ANISOU 2686 O ALA A 330 5755 4246 4666 331 321 -282 O ATOM 2687 CB ALA A 330 28.109 10.210 34.040 1.00 38.28 C ANISOU 2687 CB ALA A 330 5591 4163 4792 304 374 -146 C ATOM 2688 N PHE A 331 26.307 8.130 32.766 1.00 36.57 N ANISOU 2688 N PHE A 331 5457 3920 4516 241 312 -315 N ATOM 2689 CA PHE A 331 26.244 6.806 32.151 1.00 35.21 C ANISOU 2689 CA PHE A 331 5358 3708 4312 231 318 -382 C ATOM 2690 C PHE A 331 25.276 6.736 30.975 1.00 43.50 C ANISOU 2690 C PHE A 331 6435 4796 5298 214 260 -443 C ATOM 2691 O PHE A 331 25.405 5.829 30.145 1.00 39.56 O ANISOU 2691 O PHE A 331 6008 4272 4750 223 266 -496 O ATOM 2692 CB PHE A 331 25.872 5.764 33.206 1.00 37.84 C ANISOU 2692 CB PHE A 331 5687 3980 4711 174 323 -409 C ATOM 2693 CG PHE A 331 26.936 5.555 34.251 1.00 39.09 C ANISOU 2693 CG PHE A 331 5831 4096 4925 192 388 -356 C ATOM 2694 CD1 PHE A 331 28.241 5.273 33.884 1.00 47.22 C ANISOU 2694 CD1 PHE A 331 6909 5105 5928 252 451 -327 C ATOM 2695 CD2 PHE A 331 26.631 5.651 35.598 1.00 43.70 C ANISOU 2695 CD2 PHE A 331 6351 4668 5584 150 387 -330 C ATOM 2696 CE1 PHE A 331 29.218 5.084 34.840 1.00 46.78 C ANISOU 2696 CE1 PHE A 331 6836 5018 5921 267 512 -272 C ATOM 2697 CE2 PHE A 331 27.608 5.464 36.561 1.00 49.01 C ANISOU 2697 CE2 PHE A 331 7007 5308 6306 163 447 -279 C ATOM 2698 CZ PHE A 331 28.902 5.181 36.181 1.00 39.61 C ANISOU 2698 CZ PHE A 331 5863 4097 5089 220 509 -248 C ATOM 2699 N ARG A 332 24.322 7.662 30.871 1.00 37.16 N ANISOU 2699 N ARG A 332 5578 4052 4490 193 207 -436 N ATOM 2700 CA ARG A 332 23.442 7.694 29.707 1.00 47.05 C ANISOU 2700 CA ARG A 332 6849 5353 5676 179 153 -484 C ATOM 2701 C ARG A 332 24.073 8.399 28.515 1.00 44.49 C ANISOU 2701 C ARG A 332 6545 5079 5281 244 163 -461 C ATOM 2702 O ARG A 332 23.487 8.390 27.429 1.00 48.38 O ANISOU 2702 O ARG A 332 7058 5615 5709 240 125 -500 O ATOM 2703 CB ARG A 332 22.113 8.368 30.064 1.00 47.80 C ANISOU 2703 CB ARG A 332 6874 5497 5791 131 92 -481 C ATOM 2704 CG ARG A 332 21.174 7.451 30.842 1.00 60.11 C ANISOU 2704 CG ARG A 332 8422 7023 7393 56 63 -522 C ATOM 2705 CD ARG A 332 19.898 8.146 31.293 1.00 49.51 C ANISOU 2705 CD ARG A 332 7003 5738 6072 16 8 -508 C ATOM 2706 NE ARG A 332 19.225 8.845 30.204 1.00 66.73 N ANISOU 2706 NE ARG A 332 9174 7994 8187 24 -37 -514 N ATOM 2707 CZ ARG A 332 19.250 10.159 30.012 1.00 79.21 C ANISOU 2707 CZ ARG A 332 10710 9630 9758 67 -41 -464 C ATOM 2708 NH1 ARG A 332 19.886 10.972 30.842 1.00 57.43 N ANISOU 2708 NH1 ARG A 332 7915 6859 7048 104 -8 -406 N ATOM 2709 NH2 ARG A 332 18.616 10.673 28.962 1.00 73.43 N ANISOU 2709 NH2 ARG A 332 9970 8966 8963 72 -81 -471 N ATOM 2710 N ASN A 333 25.249 8.993 28.689 1.00 48.70 N ANISOU 2710 N ASN A 333 7070 5612 5823 302 212 -395 N ATOM 2711 CA ASN A 333 25.944 9.656 27.595 1.00 41.82 C ANISOU 2711 CA ASN A 333 6211 4791 4886 366 223 -362 C ATOM 2712 C ASN A 333 26.728 8.631 26.780 1.00 46.99 C ANISOU 2712 C ASN A 333 6949 5421 5483 405 262 -398 C ATOM 2713 O ASN A 333 27.470 7.818 27.340 1.00 39.14 O ANISOU 2713 O ASN A 333 5989 4366 4517 415 311 -398 O ATOM 2714 CB ASN A 333 26.872 10.733 28.155 1.00 45.06 C ANISOU 2714 CB ASN A 333 6576 5213 5329 406 255 -270 C ATOM 2715 CG ASN A 333 27.594 11.505 27.074 1.00 46.44 C ANISOU 2715 CG ASN A 333 6757 5448 5442 470 263 -222 C ATOM 2716 OD1 ASN A 333 28.659 11.099 26.611 1.00 52.21 O ANISOU 2716 OD1 ASN A 333 7529 6173 6135 520 308 -205 O ATOM 2717 ND2 ASN A 333 27.025 12.635 26.676 1.00 60.54 N ANISOU 2717 ND2 ASN A 333 8496 7293 7214 472 219 -196 N ATOM 2718 N GLN A 334 26.563 8.673 25.454 1.00 46.06 N ANISOU 2718 N GLN A 334 6863 5355 5284 431 240 -428 N ATOM 2719 CA GLN A 334 27.172 7.655 24.601 1.00 50.97 C ANISOU 2719 CA GLN A 334 7569 5955 5841 470 270 -475 C ATOM 2720 C GLN A 334 28.694 7.686 24.675 1.00 40.27 C ANISOU 2720 C GLN A 334 6231 4589 4480 545 341 -411 C ATOM 2721 O GLN A 334 29.341 6.637 24.582 1.00 42.84 O ANISOU 2721 O GLN A 334 6625 4865 4788 573 386 -440 O ATOM 2722 CB GLN A 334 26.714 7.834 23.149 1.00 57.43 C ANISOU 2722 CB GLN A 334 8410 6843 6567 486 232 -513 C ATOM 2723 CG GLN A 334 27.222 9.111 22.474 1.00 87.30 C ANISOU 2723 CG GLN A 334 12146 10710 10312 544 233 -438 C ATOM 2724 CD GLN A 334 27.036 9.102 20.967 1.00101.60 C ANISOU 2724 CD GLN A 334 13989 12591 12024 575 209 -474 C ATOM 2725 OE1 GLN A 334 26.294 8.282 20.423 1.00 88.16 O ANISOU 2725 OE1 GLN A 334 12336 10880 10281 540 178 -559 O ATOM 2726 NE2 GLN A 334 27.724 10.012 20.284 1.00 94.30 N ANISOU 2726 NE2 GLN A 334 13036 11737 11057 638 221 -406 N ATOM 2727 N GLU A 335 29.285 8.873 24.829 1.00 42.30 N ANISOU 2727 N GLU A 335 6430 4893 4750 579 353 -321 N ATOM 2728 CA GLU A 335 30.740 8.963 24.893 1.00 49.50 C ANISOU 2728 CA GLU A 335 7351 5805 5652 647 417 -248 C ATOM 2729 C GLU A 335 31.271 8.384 26.200 1.00 40.59 C ANISOU 2729 C GLU A 335 6222 4601 4598 629 464 -227 C ATOM 2730 O GLU A 335 32.350 7.779 26.225 1.00 43.82 O ANISOU 2730 O GLU A 335 6670 4986 4992 678 525 -203 O ATOM 2731 CB GLU A 335 31.177 10.419 24.721 1.00 47.26 C ANISOU 2731 CB GLU A 335 7003 5590 5364 677 408 -153 C ATOM 2732 CG GLU A 335 31.539 10.795 23.289 1.00 74.28 C ANISOU 2732 CG GLU A 335 10439 9091 8693 739 402 -137 C ATOM 2733 CD GLU A 335 31.713 12.291 23.100 1.00 84.56 C ANISOU 2733 CD GLU A 335 11672 10461 9997 755 377 -48 C ATOM 2734 OE1 GLU A 335 30.724 13.035 23.279 1.00 80.59 O ANISOU 2734 OE1 GLU A 335 11122 9973 9524 710 325 -55 O ATOM 2735 OE2 GLU A 335 32.842 12.724 22.778 1.00 80.97 O ANISOU 2735 OE2 GLU A 335 11208 10044 9512 814 410 32 O ATOM 2736 N ILE A 336 30.528 8.556 27.295 1.00 38.29 N ANISOU 2736 N ILE A 336 5887 4279 4385 562 439 -233 N ATOM 2737 CA ILE A 336 30.907 7.926 28.557 1.00 38.62 C ANISOU 2737 CA ILE A 336 5925 4251 4498 539 480 -220 C ATOM 2738 C ILE A 336 30.828 6.409 28.434 1.00 36.63 C ANISOU 2738 C ILE A 336 5747 3934 4235 531 501 -298 C ATOM 2739 O ILE A 336 31.715 5.684 28.899 1.00 37.21 O ANISOU 2739 O ILE A 336 5850 3961 4327 557 561 -278 O ATOM 2740 CB ILE A 336 30.015 8.443 29.700 1.00 39.78 C ANISOU 2740 CB ILE A 336 6005 4386 4724 470 442 -216 C ATOM 2741 CG1 ILE A 336 30.294 9.922 29.983 1.00 45.83 C ANISOU 2741 CG1 ILE A 336 6706 5201 5508 483 431 -133 C ATOM 2742 CG2 ILE A 336 30.229 7.608 30.958 1.00 37.71 C ANISOU 2742 CG2 ILE A 336 5741 4053 4533 437 479 -217 C ATOM 2743 CD1 ILE A 336 31.586 10.173 30.723 1.00 54.37 C ANISOU 2743 CD1 ILE A 336 7770 6269 6621 512 488 -47 C ATOM 2744 N GLN A 337 29.759 5.907 27.812 1.00 37.92 N ANISOU 2744 N GLN A 337 5945 4094 4369 494 451 -384 N ATOM 2745 CA GLN A 337 29.631 4.470 27.594 1.00 49.20 C ANISOU 2745 CA GLN A 337 7454 5456 5783 484 462 -463 C ATOM 2746 C GLN A 337 30.799 3.925 26.785 1.00 40.95 C ANISOU 2746 C GLN A 337 6482 4406 4671 569 521 -458 C ATOM 2747 O GLN A 337 31.320 2.847 27.090 1.00 37.96 O ANISOU 2747 O GLN A 337 6159 3960 4306 584 567 -478 O ATOM 2748 CB GLN A 337 28.307 4.170 26.894 1.00 41.49 C ANISOU 2748 CB GLN A 337 6502 4490 4771 430 391 -551 C ATOM 2749 CG GLN A 337 27.091 4.594 27.706 1.00 44.64 C ANISOU 2749 CG GLN A 337 6831 4898 5233 347 334 -555 C ATOM 2750 CD GLN A 337 25.798 4.512 26.918 1.00 42.63 C ANISOU 2750 CD GLN A 337 6587 4676 4934 297 260 -624 C ATOM 2751 OE1 GLN A 337 25.800 4.219 25.722 1.00 48.59 O ANISOU 2751 OE1 GLN A 337 7400 5451 5609 322 249 -670 O ATOM 2752 NE2 GLN A 337 24.683 4.773 27.590 1.00 43.64 N ANISOU 2752 NE2 GLN A 337 6656 4815 5111 226 210 -629 N ATOM 2753 N ARG A 338 31.227 4.654 25.750 1.00 45.58 N ANISOU 2753 N ARG A 338 7066 5067 5184 628 520 -428 N ATOM 2754 CA AARG A 338 32.361 4.209 24.947 0.50 44.41 C ANISOU 2754 CA AARG A 338 6981 4928 4965 718 577 -415 C ATOM 2755 CA BARG A 338 32.362 4.199 24.952 0.50 44.41 C ANISOU 2755 CA BARG A 338 6981 4927 4965 718 577 -416 C ATOM 2756 C ARG A 338 33.619 4.101 25.801 1.00 43.51 C ANISOU 2756 C ARG A 338 6853 4787 4891 760 652 -333 C ATOM 2757 O ARG A 338 34.343 3.101 25.744 1.00 42.50 O ANISOU 2757 O ARG A 338 6790 4613 4745 806 708 -346 O ATOM 2758 CB AARG A 338 32.572 5.177 23.781 0.50 48.07 C ANISOU 2758 CB AARG A 338 7425 5490 5349 771 558 -382 C ATOM 2759 CB BARG A 338 32.599 5.135 23.769 0.50 48.07 C ANISOU 2759 CB BARG A 338 7428 5488 5348 773 560 -383 C ATOM 2760 CG AARG A 338 33.745 4.844 22.875 0.50 52.10 C ANISOU 2760 CG AARG A 338 7990 6029 5777 872 614 -359 C ATOM 2761 CG BARG A 338 31.438 5.195 22.822 0.50 55.89 C ANISOU 2761 CG BARG A 338 8435 6513 6288 738 491 -462 C ATOM 2762 CD AARG A 338 34.099 6.027 21.988 0.50 58.77 C ANISOU 2762 CD AARG A 338 8788 6980 6561 921 600 -292 C ATOM 2763 CD BARG A 338 31.863 5.431 21.392 0.50 62.94 C ANISOU 2763 CD BARG A 338 9358 7483 7076 812 494 -461 C ATOM 2764 NE AARG A 338 35.463 5.935 21.484 0.50 62.02 N ANISOU 2764 NE AARG A 338 9223 7428 6912 1020 664 -229 N ATOM 2765 NE BARG A 338 30.679 5.574 20.557 0.50 63.31 N ANISOU 2765 NE BARG A 338 9408 7569 7078 769 424 -531 N ATOM 2766 CZ AARG A 338 36.546 6.174 22.212 0.50 61.49 C ANISOU 2766 CZ AARG A 338 9123 7360 6880 1052 719 -131 C ATOM 2767 CZ BARG A 338 29.904 6.649 20.546 0.50 68.00 C ANISOU 2767 CZ BARG A 338 9926 8221 7690 727 370 -504 C ATOM 2768 NH1AARG A 338 36.461 6.503 23.492 0.50 60.24 N ANISOU 2768 NH1AARG A 338 8911 7161 6816 993 719 -90 N ATOM 2769 NH1BARG A 338 30.201 7.723 21.261 0.50 61.66 N ANISOU 2769 NH1BARG A 338 9042 7441 6944 726 376 -412 N ATOM 2770 NH2AARG A 338 37.744 6.076 21.644 0.50 63.63 N ANISOU 2770 NH2AARG A 338 9414 7676 7085 1145 774 -71 N ATOM 2771 NH2BARG A 338 28.799 6.643 19.807 0.50 83.97 N ANISOU 2771 NH2BARG A 338 11955 10278 9671 685 309 -570 N ATOM 2772 N ALA A 339 33.897 5.133 26.597 1.00 36.82 N ANISOU 2772 N ALA A 339 5922 3970 4097 745 655 -245 N ATOM 2773 CA ALA A 339 35.041 5.071 27.497 1.00 38.41 C ANISOU 2773 CA ALA A 339 6103 4151 4340 773 722 -161 C ATOM 2774 C ALA A 339 34.933 3.873 28.433 1.00 35.85 C ANISOU 2774 C ALA A 339 5810 3735 4078 737 752 -203 C ATOM 2775 O ALA A 339 35.930 3.192 28.697 1.00 38.94 O ANISOU 2775 O ALA A 339 6231 4094 4469 784 820 -170 O ATOM 2776 CB ALA A 339 35.150 6.370 28.292 1.00 40.25 C ANISOU 2776 CB ALA A 339 6243 4423 4627 744 707 -73 C ATOM 2777 N LEU A 340 33.727 3.591 28.935 1.00 44.35 N ANISOU 2777 N LEU A 340 6876 4769 5206 656 700 -270 N ATOM 2778 CA LEU A 340 33.542 2.421 29.790 1.00 41.33 C ANISOU 2778 CA LEU A 340 6522 4300 4883 617 722 -311 C ATOM 2779 C LEU A 340 33.848 1.133 29.033 1.00 37.93 C ANISOU 2779 C LEU A 340 6196 3816 4398 662 753 -376 C ATOM 2780 O LEU A 340 34.467 0.214 29.581 1.00 41.67 O ANISOU 2780 O LEU A 340 6703 4228 4902 680 810 -368 O ATOM 2781 CB LEU A 340 32.118 2.398 30.348 1.00 37.53 C ANISOU 2781 CB LEU A 340 6007 3795 4457 521 652 -369 C ATOM 2782 CG LEU A 340 31.785 1.258 31.317 1.00 45.55 C ANISOU 2782 CG LEU A 340 7038 4725 5544 467 663 -405 C ATOM 2783 CD1 LEU A 340 32.762 1.213 32.485 1.00 37.82 C ANISOU 2783 CD1 LEU A 340 6018 3725 4627 481 730 -324 C ATOM 2784 CD2 LEU A 340 30.364 1.401 31.833 1.00 47.85 C ANISOU 2784 CD2 LEU A 340 7282 5014 5883 374 589 -449 C ATOM 2785 N TRP A 341 33.424 1.046 27.770 1.00 45.65 N ANISOU 2785 N TRP A 341 7229 4819 5297 682 717 -441 N ATOM 2786 CA ATRP A 341 33.728 -0.147 26.989 0.50 49.74 C ANISOU 2786 CA ATRP A 341 7855 5287 5755 731 746 -508 C ATOM 2787 CA BTRP A 341 33.727 -0.127 26.950 0.50 49.73 C ANISOU 2787 CA BTRP A 341 7855 5289 5752 732 745 -508 C ATOM 2788 C TRP A 341 35.231 -0.309 26.789 1.00 56.74 C ANISOU 2788 C TRP A 341 8769 6187 6602 835 832 -439 C ATOM 2789 O TRP A 341 35.754 -1.425 26.901 1.00 55.32 O ANISOU 2789 O TRP A 341 8660 5938 6422 871 884 -462 O ATOM 2790 CB ATRP A 341 33.001 -0.097 25.648 0.50 49.92 C ANISOU 2790 CB ATRP A 341 7927 5347 5694 732 688 -587 C ATOM 2791 CB BTRP A 341 33.049 0.021 25.583 0.50 49.94 C ANISOU 2791 CB BTRP A 341 7925 5360 5691 738 688 -580 C ATOM 2792 CG ATRP A 341 31.499 0.021 25.765 0.50 52.24 C ANISOU 2792 CG ATRP A 341 8195 5635 6017 630 602 -651 C ATOM 2793 CG BTRP A 341 33.527 -0.936 24.521 0.50 56.05 C ANISOU 2793 CG BTRP A 341 8812 6108 6378 811 719 -641 C ATOM 2794 CD1ATRP A 341 30.658 0.549 24.837 0.50 57.36 C ANISOU 2794 CD1ATRP A 341 8839 6345 6610 608 537 -693 C ATOM 2795 CD1BTRP A 341 33.256 -2.270 24.437 0.50 62.38 C ANISOU 2795 CD1BTRP A 341 9710 6816 7177 797 721 -730 C ATOM 2796 CD2ATRP A 341 30.668 -0.391 26.868 0.50 52.86 C ANISOU 2796 CD2ATRP A 341 8245 5653 6185 538 572 -674 C ATOM 2797 CD2BTRP A 341 34.338 -0.620 23.379 0.50 57.56 C ANISOU 2797 CD2BTRP A 341 9032 6369 6470 910 748 -618 C ATOM 2798 NE1ATRP A 341 29.359 0.492 25.281 0.50 51.43 N ANISOU 2798 NE1ATRP A 341 8059 5576 5906 509 470 -738 N ATOM 2799 NE1BTRP A 341 33.853 -2.807 23.323 0.50 55.50 N ANISOU 2799 NE1BTRP A 341 8930 5947 6209 884 752 -768 N ATOM 2800 CE2ATRP A 341 29.338 -0.081 26.525 0.50 53.46 C ANISOU 2800 CE2ATRP A 341 8300 5760 6252 465 489 -727 C ATOM 2801 CE2BTRP A 341 34.523 -1.815 22.656 0.50 46.80 C ANISOU 2801 CE2BTRP A 341 7786 4949 5045 957 770 -699 C ATOM 2802 CE3ATRP A 341 30.919 -0.992 28.106 0.50 45.37 C ANISOU 2802 CE3ATRP A 341 7282 4635 5323 510 609 -650 C ATOM 2803 CE3BTRP A 341 34.927 0.555 22.902 0.50 57.95 C ANISOU 2803 CE3BTRP A 341 9019 6522 6476 964 757 -534 C ATOM 2804 CZ2ATRP A 341 28.266 -0.350 27.376 0.50 53.82 C ANISOU 2804 CZ2ATRP A 341 8311 5770 6368 368 440 -754 C ATOM 2805 CZ2BTRP A 341 35.274 -1.871 21.483 0.50 65.55 C ANISOU 2805 CZ2BTRP A 341 10218 7376 7314 1060 803 -701 C ATOM 2806 CZ3ATRP A 341 29.857 -1.256 28.945 0.50 48.07 C ANISOU 2806 CZ3ATRP A 341 7588 4940 5736 414 560 -680 C ATOM 2807 CZ3BTRP A 341 35.673 0.497 21.735 0.50 66.41 C ANISOU 2807 CZ3BTRP A 341 10141 7648 7445 1062 787 -530 C ATOM 2808 CH2ATRP A 341 28.547 -0.937 28.578 0.50 43.95 C ANISOU 2808 CH2ATRP A 341 7046 4452 5201 345 476 -730 C ATOM 2809 CH2BTRP A 341 35.840 -0.707 21.040 0.50 53.87 C ANISOU 2809 CH2BTRP A 341 8668 6008 5793 1112 811 -613 C ATOM 2810 N LEU A 342 35.944 0.783 26.511 1.00 46.13 N ANISOU 2810 N LEU A 342 7370 4932 5227 885 849 -351 N ATOM 2811 CA LEU A 342 37.393 0.688 26.377 1.00 52.00 C ANISOU 2811 CA LEU A 342 8127 5699 5932 983 930 -270 C ATOM 2812 C LEU A 342 38.052 0.323 27.699 1.00 55.79 C ANISOU 2812 C LEU A 342 8577 6130 6493 972 989 -205 C ATOM 2813 O LEU A 342 39.107 -0.320 27.709 1.00 62.01 O ANISOU 2813 O LEU A 342 9403 6901 7258 1045 1064 -167 O ATOM 2814 CB LEU A 342 37.964 2.006 25.858 1.00 48.37 C ANISOU 2814 CB LEU A 342 7604 5348 5425 1026 926 -179 C ATOM 2815 CG LEU A 342 37.649 2.346 24.404 1.00 63.72 C ANISOU 2815 CG LEU A 342 9580 7358 7273 1065 886 -222 C ATOM 2816 CD1 LEU A 342 38.135 3.749 24.089 1.00 60.37 C ANISOU 2816 CD1 LEU A 342 9077 7039 6823 1092 875 -121 C ATOM 2817 CD2 LEU A 342 38.280 1.328 23.463 1.00 58.75 C ANISOU 2817 CD2 LEU A 342 9051 6716 6556 1158 934 -264 C ATOM 2818 N LEU A 343 37.450 0.723 28.819 1.00 51.56 N ANISOU 2818 N LEU A 343 7969 5575 6048 884 958 -190 N ATOM 2819 CA LEU A 343 38.029 0.408 30.120 1.00 50.77 C ANISOU 2819 CA LEU A 343 7832 5434 6025 867 1012 -128 C ATOM 2820 C LEU A 343 37.862 -1.069 30.452 1.00 58.13 C ANISOU 2820 C LEU A 343 8835 6265 6988 858 1039 -196 C ATOM 2821 O LEU A 343 38.804 -1.720 30.918 1.00 59.79 O ANISOU 2821 O LEU A 343 9061 6443 7212 903 1114 -149 O ATOM 2822 CB LEU A 343 37.387 1.274 31.200 1.00 53.28 C ANISOU 2822 CB LEU A 343 8054 5764 6426 779 967 -98 C ATOM 2823 CG LEU A 343 37.716 0.879 32.639 1.00 58.21 C ANISOU 2823 CG LEU A 343 8636 6342 7140 742 1010 -51 C ATOM 2824 CD1 LEU A 343 39.218 0.892 32.864 1.00 65.67 C ANISOU 2824 CD1 LEU A 343 9570 7313 8068 814 1094 55 C ATOM 2825 CD2 LEU A 343 37.012 1.809 33.605 1.00 49.64 C ANISOU 2825 CD2 LEU A 343 7459 5277 6125 661 960 -28 C ATOM 2826 N LEU A 344 36.665 -1.613 30.229 1.00 54.30 N ANISOU 2826 N LEU A 344 8390 5727 6512 797 979 -303 N ATOM 2827 CA LEU A 344 36.431 -3.020 30.535 1.00 69.06 C ANISOU 2827 CA LEU A 344 10331 7495 8415 779 996 -370 C ATOM 2828 C LEU A 344 37.267 -3.926 29.640 1.00 69.45 C ANISOU 2828 C LEU A 344 10486 7513 8388 879 1054 -394 C ATOM 2829 O LEU A 344 37.786 -4.951 30.096 1.00 81.21 O ANISOU 2829 O LEU A 344 12021 8931 9905 904 1112 -392 O ATOM 2830 CB LEU A 344 34.942 -3.339 30.394 1.00 58.07 C ANISOU 2830 CB LEU A 344 8959 6062 7041 689 909 -475 C ATOM 2831 CG LEU A 344 34.028 -2.587 31.368 1.00 53.96 C ANISOU 2831 CG LEU A 344 8337 5566 6600 592 852 -455 C ATOM 2832 CD1 LEU A 344 32.559 -2.756 31.008 1.00 51.00 C ANISOU 2832 CD1 LEU A 344 7979 5175 6224 511 763 -550 C ATOM 2833 CD2 LEU A 344 34.275 -3.038 32.803 1.00 64.55 C ANISOU 2833 CD2 LEU A 344 9631 6856 8038 555 891 -409 C ATOM 2834 N ASP A 345 37.422 -3.560 28.370 1.00 67.43 N ANISOU 2834 N ASP A 345 10271 7316 8035 940 1042 -415 N ATOM 2835 CA ASP A 345 38.146 -4.378 27.408 1.00 76.65 C ANISOU 2835 CA ASP A 345 11544 8463 9118 1041 1093 -446 C ATOM 2836 C ASP A 345 39.657 -4.165 27.459 1.00 89.69 C ANISOU 2836 C ASP A 345 13177 10165 10737 1145 1184 -333 C ATOM 2837 O ASP A 345 40.338 -4.415 26.457 1.00113.28 O ANISOU 2837 O ASP A 345 16230 13180 13632 1245 1221 -336 O ATOM 2838 CB ASP A 345 37.630 -4.098 25.994 1.00 79.72 C ANISOU 2838 CB ASP A 345 11982 8899 9409 1063 1039 -518 C ATOM 2839 CG ASP A 345 36.138 -4.346 25.857 1.00 87.12 C ANISOU 2839 CG ASP A 345 12941 9792 10367 960 948 -627 C ATOM 2840 OD1 ASP A 345 35.506 -4.751 26.857 1.00 69.92 O ANISOU 2840 OD1 ASP A 345 10740 7547 8279 874 926 -646 O ATOM 2841 OD2 ASP A 345 35.598 -4.137 24.749 1.00 89.22 O ANISOU 2841 OD2 ASP A 345 13244 10098 10559 964 898 -690 O ATOM 2842 N GLY A 346 40.191 -3.720 28.592 1.00 82.56 N ANISOU 2842 N GLY A 346 12186 9280 9905 1124 1219 -231 N ATOM 2843 CA GLY A 346 41.631 -3.507 28.697 1.00 77.04 C ANISOU 2843 CA GLY A 346 11461 8635 9176 1215 1304 -113 C ATOM 2844 C GLY A 346 42.192 -2.611 27.617 1.00102.02 C ANISOU 2844 C GLY A 346 14613 11907 12243 1289 1303 -64 C ATOM 2845 O GLY A 346 43.322 -2.821 27.157 1.00117.45 O ANISOU 2845 O GLY A 346 16596 13900 14132 1394 1372 -4 O ATOM 2846 N CYS A 347 41.424 -1.609 27.198 1.00 92.64 N ANISOU 2846 N CYS A 347 13381 10775 11043 1239 1226 -85 N ATOM 2847 CA CYS A 347 41.851 -0.690 26.148 1.00108.62 C ANISOU 2847 CA CYS A 347 15386 12906 12979 1301 1216 -38 C ATOM 2848 C CYS A 347 42.063 -1.439 24.836 1.00109.45 C ANISOU 2848 C CYS A 347 15595 13012 12977 1394 1235 -106 C ATOM 2849 O CYS A 347 41.146 -2.081 24.322 1.00 97.67 O ANISOU 2849 O CYS A 347 14176 11463 11469 1367 1191 -228 O ATOM 2850 CB CYS A 347 43.136 0.038 26.552 1.00112.77 C ANISOU 2850 CB CYS A 347 15839 13509 13501 1350 1273 113 C ATOM 2851 SG CYS A 347 43.094 0.750 28.214 1.00113.06 S ANISOU 2851 SG CYS A 347 15764 13535 13660 1249 1266 197 S TER 2852 CYS A 347 HETATM 2853 C9 OLC A1201 33.546 35.030 39.041 1.00 57.38 C HETATM 2854 C8 OLC A1201 32.125 34.667 38.782 1.00 62.49 C HETATM 2855 C24 OLC A1201 28.015 27.564 29.976 1.00 57.19 C HETATM 2856 C7 OLC A1201 32.030 33.810 37.529 1.00 61.54 C HETATM 2857 C6 OLC A1201 30.594 33.779 37.023 1.00 56.56 C HETATM 2858 C5 OLC A1201 30.531 32.965 35.736 1.00 59.49 C HETATM 2859 C4 OLC A1201 29.321 33.368 34.908 1.00 66.62 C HETATM 2860 C3 OLC A1201 29.370 32.624 33.583 1.00 63.71 C HETATM 2861 C2 OLC A1201 28.679 31.263 33.684 1.00 66.68 C HETATM 2862 C21 OLC A1201 29.232 28.730 31.888 1.00 53.51 C HETATM 2863 C1 OLC A1201 28.354 30.870 32.285 1.00 58.88 C HETATM 2864 C22 OLC A1201 29.267 28.418 30.348 1.00 49.72 C HETATM 2865 O19 OLC A1201 28.304 31.617 31.318 1.00 95.00 O HETATM 2866 O25 OLC A1201 28.491 26.257 29.844 1.00 43.27 O HETATM 2867 O23 OLC A1201 29.341 29.576 29.592 1.00 54.09 O HETATM 2868 O20 OLC A1201 28.089 29.543 32.100 1.00 63.51 O HETATM 2869 C18 OLC A1202 25.733 31.766 50.035 1.00 50.21 C HETATM 2870 C10 OLC A1202 23.450 32.449 42.258 1.00 84.43 C HETATM 2871 C9 OLC A1202 24.172 32.362 41.128 1.00 78.50 C HETATM 2872 C17 OLC A1202 25.549 31.981 48.547 1.00 60.39 C HETATM 2873 C11 OLC A1202 22.333 31.516 42.603 1.00 89.32 C HETATM 2874 C8 OLC A1202 23.956 31.321 40.073 1.00 82.55 C HETATM 2875 C24 OLC A1202 24.943 34.134 28.896 1.00106.08 C HETATM 2876 C16 OLC A1202 24.242 31.353 48.098 1.00 81.65 C HETATM 2877 C12 OLC A1202 22.575 30.904 43.968 1.00 82.28 C HETATM 2878 C7 OLC A1202 24.013 31.966 38.696 1.00 66.30 C HETATM 2879 C15 OLC A1202 23.908 31.718 46.661 1.00 73.24 C HETATM 2880 C13 OLC A1202 22.026 31.837 45.031 1.00 63.52 C HETATM 2881 C6 OLC A1202 23.950 30.884 37.629 1.00 70.94 C HETATM 2882 C14 OLC A1202 22.454 31.346 46.397 1.00 77.44 C HETATM 2883 C5 OLC A1202 23.744 31.518 36.262 1.00 70.82 C HETATM 2884 C4 OLC A1202 22.321 32.047 36.130 1.00 80.14 C HETATM 2885 C3 OLC A1202 21.880 31.891 34.687 1.00 76.19 C HETATM 2886 C2 OLC A1202 22.736 32.739 33.756 1.00 73.56 C HETATM 2887 C21 OLC A1202 23.649 33.410 30.902 1.00 96.72 C HETATM 2888 C1 OLC A1202 22.029 32.736 32.445 1.00 98.14 C HETATM 2889 C22 OLC A1202 23.741 34.492 29.810 1.00 98.97 C HETATM 2890 O19 OLC A1202 21.137 31.977 32.093 1.00 90.84 O HETATM 2891 O25 OLC A1202 24.833 35.009 27.812 1.00101.16 O HETATM 2892 O23 OLC A1202 22.557 34.568 29.095 1.00100.04 O HETATM 2893 O20 OLC A1202 22.441 33.703 31.580 1.00110.59 O HETATM 2894 C13 P15 A1203 18.486 19.077 25.809 1.00 77.86 C HETATM 2895 O6 P15 A1203 17.701 18.305 26.675 1.00 90.09 O HETATM 2896 C12 P15 A1203 17.445 17.007 26.216 1.00 94.38 C HETATM 2897 C11 P15 A1203 16.668 16.222 27.274 1.00 73.65 C HETATM 2898 O5 P15 A1203 17.550 15.711 28.237 1.00 75.93 O HETATM 2899 C10 P15 A1203 16.932 14.982 29.262 1.00 60.36 C HETATM 2900 C9 P15 A1203 17.860 14.894 30.473 1.00 64.68 C HETATM 2901 O4 P15 A1203 17.234 15.500 31.570 1.00 63.24 O HETATM 2902 C8 P15 A1203 18.082 15.818 32.639 1.00 69.15 C HETATM 2903 C7 P15 A1203 17.324 16.677 33.652 1.00 61.89 C HETATM 2904 O3 P15 A1203 17.359 18.018 33.251 1.00 75.39 O HETATM 2905 C6 P15 A1203 16.295 18.802 33.713 1.00 55.26 C HETATM 2906 C5 P15 A1203 16.397 18.955 35.225 1.00 71.68 C HETATM 2907 O2 P15 A1203 17.745 19.076 35.570 1.00 77.33 O HETATM 2908 C4 P15 A1203 17.989 19.470 36.888 1.00 59.43 C HETATM 2909 C3 P15 A1203 17.792 18.288 37.837 1.00 66.83 C HETATM 2910 O1 P15 A1203 18.997 17.589 38.002 1.00 48.63 O HETATM 2911 C2 P15 A1203 18.828 16.258 38.397 1.00 49.32 C HETATM 2912 C1 P15 A1203 19.570 15.962 39.690 1.00 53.38 C HETATM 2913 OXT P15 A1203 19.332 14.621 40.021 1.00 57.79 O HETATM 2914 C1 OLA A1204 14.520 29.672 60.873 1.00 83.14 C HETATM 2915 O1 OLA A1204 15.396 28.981 61.450 1.00 68.25 O HETATM 2916 O2 OLA A1204 13.333 29.604 61.276 1.00 84.57 O HETATM 2917 C2 OLA A1204 14.904 30.593 59.707 1.00 67.55 C HETATM 2918 C3 OLA A1204 14.373 30.098 58.360 1.00 49.88 C HETATM 2919 C4 OLA A1204 14.670 31.103 57.246 1.00 52.66 C HETATM 2920 C5 OLA A1204 14.584 30.461 55.858 1.00 56.94 C HETATM 2921 C6 OLA A1204 14.713 31.498 54.739 1.00 50.07 C HETATM 2922 C7 OLA A1204 14.686 30.832 53.362 1.00 54.30 C HETATM 2923 C8 OLA A1204 14.046 31.714 52.302 1.00 58.61 C HETATM 2924 C9 OLA A1204 15.054 32.556 51.554 1.00 66.68 C HETATM 2925 C10 OLA A1204 15.138 32.623 50.217 1.00 64.03 C HETATM 2926 C11 OLA A1204 14.244 31.871 49.257 1.00 64.57 C HETATM 2927 C12 OLA A1204 13.722 32.804 48.178 1.00 84.93 C HETATM 2928 C13 OLA A1204 12.517 32.214 47.443 1.00 72.00 C HETATM 2929 C14 OLA A1204 12.965 31.136 46.457 1.00 55.45 C HETATM 2930 C15 OLA A1204 11.776 30.444 45.793 1.00 51.70 C HETATM 2931 C16 OLA A1204 12.195 29.081 45.247 1.00 52.32 C HETATM 2932 C17 OLA A1204 11.002 28.138 45.130 1.00 52.72 C HETATM 2933 C18 OLA A1204 11.441 26.694 44.996 1.00 52.01 C HETATM 2934 C9 P15 A1205 29.660 4.238 14.698 1.00 80.81 C HETATM 2935 O4 P15 A1205 29.348 3.026 15.327 1.00111.22 O HETATM 2936 C8 P15 A1205 28.120 3.015 16.002 1.00119.16 C HETATM 2937 C7 P15 A1205 28.297 3.557 17.421 1.00114.67 C HETATM 2938 O3 P15 A1205 28.301 2.505 18.348 1.00116.86 O HETATM 2939 C6 P15 A1205 27.033 2.036 18.719 1.00110.35 C HETATM 2940 C5 P15 A1205 26.435 2.928 19.807 1.00103.98 C HETATM 2941 O2 P15 A1205 26.977 2.576 21.048 1.00102.48 O HETATM 2942 C4 P15 A1205 27.026 3.625 21.973 1.00 90.47 C HETATM 2943 C3 P15 A1205 27.447 3.084 23.338 1.00 64.23 C HETATM 2944 O1 P15 A1205 28.293 1.984 23.161 1.00 80.61 O HETATM 2945 C2 P15 A1205 29.468 2.290 22.467 1.00 91.18 C HETATM 2946 C1 P15 A1205 29.977 1.043 21.748 1.00 94.32 C HETATM 2947 OXT P15 A1205 31.351 1.178 21.504 1.00 78.32 O HETATM 2948 C1 OLA A1206 34.093 32.225 66.643 1.00 84.80 C HETATM 2949 O1 OLA A1206 33.809 31.738 67.762 1.00 88.46 O HETATM 2950 O2 OLA A1206 35.112 32.944 66.528 1.00 91.41 O HETATM 2951 C2 OLA A1206 33.206 31.944 65.430 1.00 71.23 C HETATM 2952 C3 OLA A1206 33.714 32.675 64.190 1.00 71.42 C HETATM 2953 C4 OLA A1206 32.904 32.255 62.966 1.00 61.48 C HETATM 2954 C5 OLA A1206 33.342 32.996 61.704 1.00 70.90 C HETATM 2955 C6 OLA A1206 34.701 32.489 61.227 1.00 61.99 C HETATM 2956 C7 OLA A1206 34.952 32.837 59.761 1.00 69.26 C HETATM 2957 C8 OLA A1206 35.223 34.320 59.585 1.00 70.47 C HETATM 2958 C9 OLA A1206 36.643 34.562 59.123 1.00 52.24 C HETATM 2959 C10 OLA A1206 36.977 35.143 57.962 1.00 63.07 C HETATM 2960 C11 OLA A1206 35.983 35.644 56.940 1.00 85.32 C HETATM 2961 C12 OLA A1206 35.940 34.731 55.727 1.00 83.62 C HETATM 2962 C13 OLA A1206 34.905 33.616 55.885 1.00 87.07 C HETATM 2963 C14 OLA A1206 34.983 32.629 54.720 1.00 63.71 C HETATM 2964 C15 OLA A1206 36.240 31.767 54.836 1.00 63.17 C HETATM 2965 C16 OLA A1206 36.356 30.754 53.700 1.00 63.61 C HETATM 2966 C17 OLA A1206 36.389 31.441 52.337 1.00 49.17 C HETATM 2967 C18 OLA A1206 36.578 30.434 51.220 1.00 61.28 C HETATM 2968 C1 OLA A1207 28.618 32.282 65.949 1.00 86.25 C HETATM 2969 O1 OLA A1207 27.377 32.245 65.765 1.00 87.22 O HETATM 2970 O2 OLA A1207 29.082 31.920 67.055 1.00 82.43 O HETATM 2971 C2 OLA A1207 29.554 32.762 64.838 1.00 69.19 C HETATM 2972 C3 OLA A1207 28.771 33.398 63.692 1.00 69.47 C HETATM 2973 C4 OLA A1207 29.663 33.554 62.465 1.00 74.01 C HETATM 2974 C5 OLA A1207 28.905 34.176 61.297 1.00 54.69 C HETATM 2975 C6 OLA A1207 29.781 34.179 60.047 1.00 70.47 C HETATM 2976 C7 OLA A1207 29.183 35.077 58.965 1.00 68.34 C HETATM 2977 C8 OLA A1207 30.042 35.111 57.710 1.00 74.14 C HETATM 2978 C9 OLA A1207 31.397 35.711 57.996 1.00 80.18 C HETATM 2979 C10 OLA A1207 32.226 36.073 57.016 1.00 71.99 C HETATM 2980 C11 OLA A1207 31.865 35.908 55.561 1.00 83.88 C HETATM 2981 C12 OLA A1207 32.841 36.689 54.698 1.00 87.06 C HETATM 2982 C13 OLA A1207 32.443 36.654 53.225 1.00 98.65 C HETATM 2983 C14 OLA A1207 33.555 37.226 52.348 1.00 88.06 C HETATM 2984 C15 OLA A1207 33.372 36.807 50.891 1.00 94.22 C HETATM 2985 C16 OLA A1207 32.132 37.452 50.274 1.00 91.23 C HETATM 2986 C17 OLA A1207 31.996 37.069 48.801 1.00 76.96 C HETATM 2987 C18 OLA A1207 30.888 37.856 48.126 1.00 91.34 C HETATM 2988 C1 OLA A1208 40.473 15.905 34.755 1.00 89.28 C HETATM 2989 O1 OLA A1208 39.321 16.396 34.731 1.00 82.11 O HETATM 2990 O2 OLA A1208 41.234 16.067 33.771 1.00 80.02 O HETATM 2991 C2 OLA A1208 40.936 15.117 35.980 1.00 75.14 C HETATM 2992 C3 OLA A1208 39.792 14.997 36.980 1.00 62.89 C HETATM 2993 C4 OLA A1208 40.223 14.234 38.228 1.00 65.29 C HETATM 2994 C5 OLA A1208 39.404 14.692 39.430 1.00 60.45 C HETATM 2995 C6 OLA A1208 39.754 13.892 40.679 1.00 63.21 C HETATM 2996 C7 OLA A1208 38.654 14.063 41.719 1.00 61.38 C HETATM 2997 C8 OLA A1208 38.970 13.287 42.981 1.00 53.39 C HETATM 2998 C9 OLA A1208 39.526 14.208 44.033 1.00 60.73 C HETATM 2999 C10 OLA A1208 39.616 13.835 45.309 1.00 58.96 C HETATM 3000 C11 OLA A1208 39.169 12.473 45.777 1.00 63.92 C HETATM 3001 C12 OLA A1208 40.033 12.009 46.933 1.00 66.03 C HETATM 3002 C13 OLA A1208 39.791 12.858 48.180 1.00 59.86 C HETATM 3003 C14 OLA A1208 39.198 12.019 49.309 1.00 83.54 C HETATM 3004 C15 OLA A1208 38.513 12.894 50.356 1.00 78.73 C HETATM 3005 C16 OLA A1208 38.318 12.122 51.660 1.00 70.46 C HETATM 3006 C17 OLA A1208 39.514 12.305 52.591 1.00 68.99 C HETATM 3007 C18 OLA A1208 39.884 11.002 53.273 1.00 74.84 C HETATM 3008 C1 OLA A1209 15.162 4.307 64.529 1.00 74.93 C HETATM 3009 O1 OLA A1209 16.294 4.659 64.933 1.00 73.96 O HETATM 3010 O2 OLA A1209 14.354 5.182 64.141 1.00 54.82 O HETATM 3011 C2 OLA A1209 14.771 2.828 64.506 1.00 74.94 C HETATM 3012 C3 OLA A1209 14.125 2.468 63.171 1.00 64.81 C HETATM 3013 C4 OLA A1209 15.171 1.949 62.190 1.00 56.36 C HETATM 3014 C5 OLA A1209 14.682 2.087 60.750 1.00 73.23 C HETATM 3015 C6 OLA A1209 15.391 1.096 59.831 1.00 71.62 C HETATM 3016 C7 OLA A1209 15.983 1.779 58.598 1.00 70.27 C HETATM 3017 C8 OLA A1209 14.921 2.322 57.653 1.00 85.98 C HETATM 3018 C9 OLA A1209 14.151 1.214 56.974 1.00 92.21 C HETATM 3019 C10 OLA A1209 13.543 1.383 55.794 1.00 95.08 C HETATM 3020 C11 OLA A1209 13.576 2.693 55.044 1.00 77.22 C HETATM 3021 C12 OLA A1209 14.851 2.821 54.227 1.00 80.24 C HETATM 3022 C13 OLA A1209 14.775 2.038 52.914 1.00 76.37 C HETATM 3023 C14 OLA A1209 16.143 1.482 52.511 1.00 90.87 C HETATM 3024 C15 OLA A1209 16.237 -0.035 52.688 1.00 87.53 C HETATM 3025 C16 OLA A1209 15.802 -0.480 54.085 1.00 80.29 C HETATM 3026 C17 OLA A1209 16.266 -1.905 54.381 1.00 88.35 C HETATM 3027 C18 OLA A1209 15.449 -2.513 55.505 1.00 80.27 C HETATM 3028 C1 OLA A1210 21.525 13.922 63.430 1.00 68.45 C HETATM 3029 O1 OLA A1210 21.095 13.070 64.242 1.00 78.84 O HETATM 3030 O2 OLA A1210 21.956 15.015 63.865 1.00 63.71 O HETATM 3031 C2 OLA A1210 21.523 13.633 61.925 1.00 61.82 C HETATM 3032 C3 OLA A1210 22.869 13.083 61.457 1.00 69.78 C HETATM 3033 C4 OLA A1210 23.013 13.225 59.941 1.00 56.58 C HETATM 3034 C5 OLA A1210 24.462 13.036 59.494 1.00 63.13 C HETATM 3035 C6 OLA A1210 25.107 14.356 59.069 1.00 52.49 C HETATM 3036 C7 OLA A1210 24.768 14.700 57.619 1.00 50.47 C HETATM 3037 C8 OLA A1210 25.270 16.080 57.234 1.00 42.34 C HETATM 3038 C9 OLA A1210 25.171 16.265 55.741 1.00 63.25 C HETATM 3039 C10 OLA A1210 24.646 17.350 55.170 1.00 60.83 C HETATM 3040 C11 OLA A1210 24.094 18.514 55.954 1.00 59.45 C HETATM 3041 C12 OLA A1210 23.590 19.571 54.986 1.00 52.05 C HETATM 3042 C13 OLA A1210 22.477 20.423 55.594 1.00 54.59 C HETATM 3043 C14 OLA A1210 21.664 21.092 54.487 1.00 70.40 C HETATM 3044 C15 OLA A1210 20.537 21.942 55.066 1.00 51.88 C HETATM 3045 C16 OLA A1210 19.280 21.857 54.201 1.00 61.75 C HETATM 3046 C17 OLA A1210 19.426 22.636 52.895 1.00 54.11 C HETATM 3047 C18 OLA A1210 19.607 21.699 51.715 1.00 70.34 C HETATM 3048 C18 OLC A1211 12.410 9.897 45.473 1.00 65.48 C HETATM 3049 C10 OLC A1211 9.623 12.295 54.779 1.00 84.03 C HETATM 3050 C9 OLC A1211 9.003 11.964 55.922 1.00 92.17 C HETATM 3051 C17 OLC A1211 12.224 9.397 46.897 1.00 65.80 C HETATM 3052 C11 OLC A1211 10.335 11.308 53.913 1.00 67.77 C HETATM 3053 C8 OLC A1211 8.953 10.572 56.469 1.00 81.89 C HETATM 3054 C24 OLC A1211 8.439 9.038 67.407 1.00 82.14 C HETATM 3055 C16 OLC A1211 11.643 10.506 47.781 1.00 64.84 C HETATM 3056 C12 OLC A1211 10.401 11.839 52.476 1.00 54.22 C HETATM 3057 C7 OLC A1211 8.922 10.624 58.000 1.00 64.49 C HETATM 3058 C15 OLC A1211 11.458 10.028 49.224 1.00 78.90 C HETATM 3059 C13 OLC A1211 10.814 10.700 51.547 1.00 72.71 C HETATM 3060 C6 OLC A1211 9.054 9.211 58.562 1.00 75.44 C HETATM 3061 C14 OLC A1211 10.937 11.176 50.097 1.00 85.24 C HETATM 3062 C5 OLC A1211 9.054 9.256 60.086 1.00 82.92 C HETATM 3063 C4 OLC A1211 9.018 7.843 60.663 1.00 72.09 C HETATM 3064 C3 OLC A1211 8.827 7.940 62.166 1.00 74.59 C HETATM 3065 C2 OLC A1211 8.497 6.577 62.766 1.00 92.49 C HETATM 3066 C21 OLC A1211 9.314 7.060 66.198 1.00 87.24 C HETATM 3067 C1 OLC A1211 8.124 6.833 64.185 1.00 84.88 C HETATM 3068 C22 OLC A1211 9.741 8.318 66.971 1.00 75.48 C HETATM 3069 O19 OLC A1211 7.094 6.487 64.748 1.00105.94 O HETATM 3070 O25 OLC A1211 8.739 10.394 67.293 1.00 61.93 O HETATM 3071 O23 OLC A1211 10.546 8.000 68.051 1.00 81.20 O HETATM 3072 O20 OLC A1211 9.049 7.539 64.887 1.00 93.24 O HETATM 3073 C18 OLC A1212 34.745 21.255 54.632 1.00 57.14 C HETATM 3074 C10 OLC A1212 42.247 16.670 56.806 1.00 77.35 C HETATM 3075 C9 OLC A1212 43.096 15.848 57.445 1.00 71.63 C HETATM 3076 C17 OLC A1212 35.944 21.855 55.313 1.00 52.69 C HETATM 3077 C11 OLC A1212 40.780 16.402 56.621 1.00 90.29 C HETATM 3078 C8 OLC A1212 42.705 14.546 58.054 1.00 72.97 C HETATM 3079 C24 OLC A1212 39.603 11.347 69.269 1.00 83.26 C HETATM 3080 C16 OLC A1212 36.463 20.883 56.348 1.00 58.77 C HETATM 3081 C12 OLC A1212 39.957 17.587 57.155 1.00 66.05 C HETATM 3082 C7 OLC A1212 42.646 14.663 59.569 1.00 92.10 C HETATM 3083 C15 OLC A1212 37.139 19.684 55.712 1.00 50.15 C HETATM 3084 C13 OLC A1212 38.738 17.819 56.250 1.00 46.30 C HETATM 3085 C6 OLC A1212 42.464 13.265 60.143 1.00100.08 C HETATM 3086 C14 OLC A1212 37.911 18.973 56.807 1.00 40.69 C HETATM 3087 C5 OLC A1212 42.416 13.317 61.655 1.00 85.27 C HETATM 3088 C4 OLC A1212 42.552 11.913 62.226 1.00 77.28 C HETATM 3089 C3 OLC A1212 42.521 12.016 63.731 1.00 82.46 C HETATM 3090 C2 OLC A1212 42.796 10.671 64.382 1.00 89.18 C HETATM 3091 C21 OLC A1212 40.855 10.572 67.246 1.00 95.29 C HETATM 3092 C1 OLC A1212 42.690 10.911 65.848 1.00 90.19 C HETATM 3093 C22 OLC A1212 40.981 11.384 68.550 1.00 92.06 C HETATM 3094 O19 OLC A1212 43.568 10.738 66.682 1.00108.07 O HETATM 3095 O25 OLC A1212 39.902 11.545 70.620 1.00 91.05 O HETATM 3096 O23 OLC A1212 41.991 10.873 69.348 1.00119.67 O HETATM 3097 O20 OLC A1212 41.480 11.378 66.261 1.00102.42 O HETATM 3098 C6 OLA A1213 27.616 30.037 42.912 1.00 73.09 C HETATM 3099 C7 OLA A1213 26.208 29.806 43.454 1.00 74.00 C HETATM 3100 C8 OLA A1213 26.243 29.348 44.900 1.00 57.17 C HETATM 3101 C9 OLA A1213 26.912 28.002 45.040 1.00 53.03 C HETATM 3102 C10 OLA A1213 26.475 27.049 45.869 1.00 50.84 C HETATM 3103 C11 OLA A1213 25.268 27.195 46.763 1.00 51.46 C HETATM 3104 C12 OLA A1213 24.498 25.890 46.808 1.00 41.31 C HETATM 3105 C13 OLA A1213 23.681 25.821 48.088 1.00 46.13 C HETATM 3106 C14 OLA A1213 22.527 24.843 47.927 1.00 57.37 C HETATM 3107 C15 OLA A1213 22.968 23.438 48.318 1.00 46.40 C HETATM 3108 C16 OLA A1213 23.179 23.337 49.818 1.00 41.98 C HETATM 3109 C17 OLA A1213 23.039 21.885 50.278 1.00 62.72 C HETATM 3110 C18 OLA A1213 23.731 21.671 51.615 1.00 55.71 C HETATM 3111 C18 OLC A1214 36.857 -2.546 50.558 1.00 57.99 C HETATM 3112 C10 OLC A1214 35.650 1.984 43.473 1.00 78.95 C HETATM 3113 C9 OLC A1214 35.927 2.494 42.264 1.00 75.10 C HETATM 3114 C17 OLC A1214 35.739 -1.958 49.714 1.00 56.52 C HETATM 3115 C11 OLC A1214 35.662 0.514 43.760 1.00 77.70 C HETATM 3116 C8 OLC A1214 36.275 1.646 41.088 1.00 76.48 C HETATM 3117 C24 OLC A1214 42.180 -0.799 34.677 1.00 99.89 C HETATM 3118 C16 OLC A1214 36.052 -2.121 48.230 1.00 74.73 C HETATM 3119 C12 OLC A1214 36.355 0.250 45.098 1.00 95.89 C HETATM 3120 C7 OLC A1214 36.129 2.447 39.795 1.00 65.01 C HETATM 3121 C15 OLC A1214 37.084 -1.113 47.749 1.00 80.09 C HETATM 3122 C13 OLC A1214 36.528 -1.253 45.289 1.00 77.71 C HETATM 3123 C6 OLC A1214 37.335 3.371 39.608 1.00 69.29 C HETATM 3124 C14 OLC A1214 37.577 -1.537 46.361 1.00 83.96 C HETATM 3125 C5 OLC A1214 38.531 2.598 39.051 1.00 76.67 C HETATM 3126 C4 OLC A1214 38.378 2.382 37.545 1.00 68.24 C HETATM 3127 C3 OLC A1214 39.711 1.904 36.961 1.00 81.46 C HETATM 3128 C2 OLC A1214 40.789 2.995 37.010 1.00 86.43 C HETATM 3129 C21 OLC A1214 42.595 1.610 34.113 1.00 97.09 C HETATM 3130 C1 OLC A1214 41.522 2.945 35.711 1.00100.67 C HETATM 3131 C22 OLC A1214 43.202 0.188 34.045 1.00 89.57 C HETATM 3132 O19 OLC A1214 41.605 3.844 34.886 1.00 80.91 O HETATM 3133 O25 OLC A1214 42.693 -1.072 35.947 1.00100.63 O HETATM 3134 O23 OLC A1214 43.504 -0.157 32.738 1.00 85.83 O HETATM 3135 O20 OLC A1214 42.158 1.763 35.458 1.00116.29 O HETATM 3136 C1 OLA A1215 16.427 34.046 30.299 1.00 78.41 C HETATM 3137 O1 OLA A1215 15.928 33.464 29.310 1.00 76.17 O HETATM 3138 O2 OLA A1215 16.230 35.274 30.442 1.00 92.49 O HETATM 3139 C2 OLA A1215 17.262 33.271 31.321 1.00 83.30 C HETATM 3140 C3 OLA A1215 17.562 34.153 32.530 1.00 81.46 C HETATM 3141 C4 OLA A1215 18.242 33.375 33.654 1.00 80.01 C HETATM 3142 C5 OLA A1215 18.049 34.105 34.982 1.00 90.94 C HETATM 3143 C6 OLA A1215 19.117 33.717 36.001 1.00 95.98 C HETATM 3144 C7 OLA A1215 18.981 34.548 37.276 1.00 79.55 C HETATM 3145 C8 OLA A1215 20.064 34.182 38.276 1.00 90.45 C HETATM 3146 C9 OLA A1215 20.530 35.367 39.088 1.00 75.58 C HETATM 3147 C10 OLA A1215 19.756 35.921 40.021 1.00 79.36 C HETATM 3148 C11 OLA A1215 18.375 35.389 40.310 1.00 89.84 C HETATM 3149 C12 OLA A1215 17.765 36.082 41.515 1.00 69.82 C HETATM 3150 C10 OLA A1216 36.720 33.654 39.366 1.00 66.46 C HETATM 3151 C11 OLA A1216 37.467 32.562 40.088 1.00 59.08 C HETATM 3152 C12 OLA A1216 36.756 32.177 41.376 1.00 54.26 C HETATM 3153 C13 OLA A1216 36.102 33.392 42.027 1.00 54.59 C HETATM 3154 C14 OLA A1216 36.062 33.233 43.539 1.00 48.02 C HETATM 3155 C15 OLA A1216 34.641 32.988 44.037 1.00 65.92 C HETATM 3156 C16 OLA A1216 33.869 34.301 44.143 1.00 79.28 C HETATM 3157 C17 OLA A1216 32.495 34.077 44.775 1.00 61.59 C HETATM 3158 C18 OLA A1216 31.536 35.184 44.375 1.00 76.20 C HETATM 3159 C1 OLA A1217 43.965 7.120 64.653 1.00 94.35 C HETATM 3160 O1 OLA A1217 45.105 7.434 64.240 1.00 84.48 O HETATM 3161 O2 OLA A1217 43.784 6.980 65.885 1.00 89.72 O HETATM 3162 C2 OLA A1217 42.809 6.908 63.671 1.00 82.74 C HETATM 3163 C3 OLA A1217 43.246 7.160 62.228 1.00 71.97 C HETATM 3164 C4 OLA A1217 42.086 6.945 61.255 1.00 82.24 C HETATM 3165 C5 OLA A1217 42.504 7.245 59.816 1.00 75.02 C HETATM 3166 C6 OLA A1217 41.297 7.364 58.883 1.00 78.66 C HETATM 3167 C7 OLA A1217 40.599 6.017 58.699 1.00 85.81 C HETATM 3168 C8 OLA A1217 39.588 6.046 57.563 1.00 70.38 C HETATM 3169 C9 OLA A1217 40.265 6.194 56.224 1.00 82.31 C HETATM 3170 C10 OLA A1217 39.560 6.146 55.094 1.00 92.29 C HETATM 3171 C11 OLA A1217 38.065 5.944 55.122 1.00 75.11 C HETATM 3172 C12 OLA A1217 37.491 5.784 53.722 1.00 82.48 C HETATM 3173 C13 OLA A1217 37.120 7.123 53.082 1.00 76.39 C HETATM 3174 C14 OLA A1217 38.334 7.981 52.713 1.00 89.13 C HETATM 3175 C15 OLA A1217 39.280 7.304 51.719 1.00 82.38 C HETATM 3176 C16 OLA A1217 38.583 6.972 50.400 1.00 91.12 C HETATM 3177 C17 OLA A1217 39.572 6.425 49.369 1.00 88.20 C HETATM 3178 C18 OLA A1217 40.489 7.513 48.842 1.00 85.10 C HETATM 3179 C1 OLA A1218 15.908 -2.020 64.700 1.00 86.60 C HETATM 3180 O1 OLA A1218 16.423 -1.501 65.718 1.00 89.93 O HETATM 3181 O2 OLA A1218 14.789 -2.574 64.799 1.00 97.33 O HETATM 3182 C2 OLA A1218 16.630 -1.983 63.351 1.00 57.87 C HETATM 3183 C3 OLA A1218 16.011 -3.000 62.398 1.00 64.22 C HETATM 3184 C4 OLA A1218 16.917 -3.260 61.200 1.00 61.22 C HETATM 3185 C5 OLA A1218 17.063 -2.006 60.343 1.00 77.73 C HETATM 3186 C6 OLA A1218 17.659 -2.339 58.977 1.00 81.29 C HETATM 3187 C7 OLA A1218 19.020 -1.677 58.780 1.00 66.04 C HETATM 3188 C8 OLA A1218 19.324 -1.558 57.299 1.00 59.00 C HETATM 3189 C9 OLA A1218 20.808 -1.499 57.040 1.00 64.02 C HETATM 3190 C10 OLA A1218 21.314 -1.835 55.850 1.00 53.80 C HETATM 3191 C11 OLA A1218 20.427 -2.286 54.714 1.00 74.13 C HETATM 3192 C12 OLA A1218 21.172 -2.260 53.391 1.00 56.13 C HETATM 3193 C13 OLA A1218 20.230 -2.515 52.215 1.00 73.93 C HETATM 3194 C14 OLA A1218 20.893 -3.354 51.119 1.00 68.09 C HETATM 3195 C15 OLA A1218 21.621 -2.495 50.083 1.00 75.90 C HETATM 3196 C16 OLA A1218 22.453 -3.366 49.139 1.00 64.30 C HETATM 3197 C17 OLA A1218 23.447 -2.544 48.314 1.00 52.85 C HETATM 3198 C18 OLA A1218 23.005 -2.400 46.869 1.00 52.99 C HETATM 3199 C1 OLA A1219 39.222 -3.857 33.646 1.00 82.45 C HETATM 3200 O1 OLA A1219 38.210 -4.253 33.024 1.00 78.88 O HETATM 3201 O2 OLA A1219 40.351 -3.999 33.122 1.00 90.72 O HETATM 3202 C2 OLA A1219 39.081 -3.213 35.027 1.00 74.20 C HETATM 3203 C3 OLA A1219 38.169 -1.989 34.968 1.00 72.31 C HETATM 3204 C4 OLA A1219 37.038 -2.073 35.995 1.00 75.89 C HETATM 3205 C5 OLA A1219 36.071 -0.898 35.835 1.00 91.56 C HETATM 3206 C6 OLA A1219 34.991 -0.885 36.920 1.00 63.65 C HETATM 3207 C7 OLA A1219 33.883 -1.902 36.633 1.00 73.59 C HETATM 3208 C8 OLA A1219 32.583 -1.232 36.216 1.00 71.29 C HETATM 3209 C9 OLA A1219 31.449 -2.227 36.171 1.00 68.08 C HETATM 3210 C10 OLA A1219 30.225 -1.839 35.823 1.00 63.15 C HETATM 3211 C11 OLA A1219 29.949 -0.401 35.467 1.00 65.10 C HETATM 3212 C1 CLR A1220 37.109 17.824 39.064 1.00 33.31 C HETATM 3213 C2 CLR A1220 36.938 17.746 37.550 1.00 36.00 C HETATM 3214 C3 CLR A1220 35.908 18.765 37.087 1.00 34.68 C HETATM 3215 C4 CLR A1220 36.387 20.164 37.441 1.00 35.80 C HETATM 3216 C5 CLR A1220 36.721 20.254 38.914 1.00 38.84 C HETATM 3217 C6 CLR A1220 36.250 21.309 39.597 1.00 35.25 C HETATM 3218 C7 CLR A1220 36.626 21.623 41.026 1.00 35.83 C HETATM 3219 C8 CLR A1220 37.678 20.684 41.594 1.00 32.51 C HETATM 3220 C9 CLR A1220 37.505 19.264 41.064 1.00 31.76 C HETATM 3221 C10 CLR A1220 37.598 19.194 39.537 1.00 34.08 C HETATM 3222 C11 CLR A1220 38.483 18.313 41.759 1.00 30.22 C HETATM 3223 C12 CLR A1220 38.370 18.365 43.287 1.00 33.54 C HETATM 3224 C13 CLR A1220 38.569 19.779 43.818 1.00 29.62 C HETATM 3225 C14 CLR A1220 37.550 20.657 43.108 1.00 30.66 C HETATM 3226 C15 CLR A1220 37.633 21.985 43.851 1.00 39.85 C HETATM 3227 C16 CLR A1220 37.892 21.557 45.299 1.00 39.08 C HETATM 3228 C17 CLR A1220 38.185 20.047 45.273 1.00 28.78 C HETATM 3229 C18 CLR A1220 39.999 20.270 43.565 1.00 33.02 C HETATM 3230 C19 CLR A1220 39.017 19.429 39.030 1.00 35.36 C HETATM 3231 C20 CLR A1220 39.178 19.636 46.362 1.00 31.94 C HETATM 3232 C21 CLR A1220 39.481 18.140 46.307 1.00 30.02 C HETATM 3233 C22 CLR A1220 38.704 20.011 47.774 1.00 30.26 C HETATM 3234 C23 CLR A1220 37.304 19.491 48.114 1.00 32.89 C HETATM 3235 C24 CLR A1220 36.939 19.781 49.569 1.00 31.86 C HETATM 3236 C25 CLR A1220 35.647 19.108 50.024 1.00 34.78 C HETATM 3237 C26 CLR A1220 35.360 19.439 51.485 1.00 40.03 C HETATM 3238 C27 CLR A1220 34.455 19.506 49.162 1.00 42.30 C HETATM 3239 O1 CLR A1220 35.714 18.665 35.673 1.00 38.92 O HETATM 3240 O HOH A1301 7.269 8.668 16.891 1.00 63.86 O HETATM 3241 O HOH A1302 12.149 5.341 64.969 1.00 69.06 O HETATM 3242 O HOH A1303 19.107 22.141 2.904 1.00 70.41 O HETATM 3243 O HOH A1304 12.061 30.396 23.703 1.00 67.81 O HETATM 3244 O HOH A1305 14.674 20.443 -18.911 1.00 90.28 O HETATM 3245 O HOH A1306 20.151 19.728 33.582 1.00 52.04 O HETATM 3246 O HOH A1307 17.010 13.663 39.955 1.00 38.26 O HETATM 3247 O HOH A1308 20.217 11.826 4.476 1.00 87.22 O HETATM 3248 O HOH A1309 27.382 8.307 60.875 1.00 67.29 O HETATM 3249 O HOH A1310 25.437 -1.761 68.604 1.00 61.07 O HETATM 3250 O HOH A1311 27.170 29.822 66.431 1.00 61.79 O HETATM 3251 O HOH A1312 25.654 14.986 62.552 1.00 72.64 O HETATM 3252 O HOH A1313 30.078 23.498 42.120 1.00 42.23 O HETATM 3253 O HOH A1314 36.029 14.287 70.705 1.00 73.81 O HETATM 3254 O HOH A1315 27.124 12.424 39.575 1.00 35.11 O HETATM 3255 O HOH A1316 36.810 16.679 34.131 1.00 51.52 O HETATM 3256 O HOH A1317 31.619 11.615 62.352 1.00 53.88 O HETATM 3257 O HOH A1318 15.154 15.358 63.771 1.00 30.90 O HETATM 3258 O HOH A1319 14.128 14.792 51.585 1.00 37.46 O HETATM 3259 O HOH A1320 23.240 32.918 19.737 1.00 59.16 O HETATM 3260 O HOH A1321 38.569 21.091 29.342 1.00 49.26 O HETATM 3261 O HOH A1322 17.120 22.771 62.059 1.00 40.74 O HETATM 3262 O HOH A1323 26.577 25.395 61.544 1.00 29.16 O HETATM 3263 O HOH A1324 18.231 15.226 -4.395 1.00 71.46 O HETATM 3264 O HOH A1325 34.661 8.123 24.630 1.00 52.49 O HETATM 3265 O HOH A1326 24.005 7.960 66.165 1.00 72.49 O HETATM 3266 O HOH A1327 10.523 19.149 69.234 1.00 46.68 O HETATM 3267 O HOH A1328 12.856 7.212 66.909 1.00 66.56 O HETATM 3268 O HOH A1329 10.077 26.046 63.751 1.00 49.00 O HETATM 3269 O HOH A1330 30.135 21.307 25.797 1.00 37.02 O HETATM 3270 O HOH A1331 30.392 17.682 24.593 1.00 54.29 O HETATM 3271 O HOH A1332 24.814 10.415 24.329 1.00 49.82 O HETATM 3272 O HOH A1333 -5.896 17.530 -15.888 1.00 66.73 O HETATM 3273 O HOH A1334 2.591 24.973 15.786 1.00 74.35 O HETATM 3274 O HOH A1335 25.284 20.755 30.647 1.00 47.76 O HETATM 3275 O HOH A1336 24.559 22.110 20.218 1.00 77.63 O HETATM 3276 O HOH A1337 15.456 11.202 24.333 1.00 66.95 O HETATM 3277 O HOH A1338 16.963 7.334 65.174 1.00 47.07 O HETATM 3278 O HOH A1339 36.880 17.052 31.573 1.00 42.39 O HETATM 3279 O HOH A1340 19.053 19.062 -7.785 1.00 70.04 O HETATM 3280 O HOH A1341 31.052 17.276 66.486 1.00 51.44 O HETATM 3281 O HOH A1342 13.212 28.887 66.085 1.00 68.93 O HETATM 3282 O HOH A1343 2.170 13.778 -14.554 1.00 57.70 O HETATM 3283 O HOH A1344 13.580 7.023 18.987 1.00 57.03 O HETATM 3284 O HOH A1345 14.768 24.888 -9.765 1.00 69.22 O HETATM 3285 O HOH A1346 12.741 18.571 16.698 1.00 59.28 O HETATM 3286 O HOH A1347 16.440 14.730 70.008 1.00 63.51 O HETATM 3287 O HOH A1348 28.240 13.933 24.388 1.00 66.27 O HETATM 3288 O HOH A1349 16.163 10.523 68.584 1.00 53.80 O HETATM 3289 O HOH A1350 17.164 26.556 60.554 1.00 45.99 O HETATM 3290 O HOH A1351 38.653 22.554 31.284 1.00 49.82 O HETATM 3291 O HOH A1352 27.621 14.475 63.590 1.00 57.90 O HETATM 3292 O HOH A1353 25.029 21.077 26.614 1.00 51.72 O HETATM 3293 O HOH A1354 24.008 30.991 18.107 1.00 47.25 O HETATM 3294 O HOH A1355 26.944 18.762 31.328 1.00 62.72 O HETATM 3295 O HOH A1356 18.010 15.039 67.655 1.00 75.17 O HETATM 3296 O HOH A1357 26.963 7.149 58.674 1.00 60.39 O HETATM 3297 O HOH A1358 22.165 14.813 45.948 1.00 62.27 O HETATM 3298 O HOH A1359 18.441 16.182 -6.963 1.00 63.91 O HETATM 3299 O HOH A1360 15.053 9.049 66.591 1.00 43.29 O HETATM 3300 O HOH A1361 34.096 25.442 66.945 1.00 63.37 O HETATM 3301 O HOH A1362 27.735 26.359 32.872 1.00 44.79 O HETATM 3302 O HOH A1363 5.084 14.500 -22.316 1.00 52.47 O HETATM 3303 O HOH A1364 24.768 6.007 68.192 1.00 67.78 O HETATM 3304 O HOH A1365 10.383 10.963 -10.383 1.00 74.92 O HETATM 3305 O HOH A1366 38.267 19.730 34.354 1.00 53.53 O HETATM 3306 O HOH A1367 22.512 16.348 44.233 1.00 42.68 O HETATM 3307 O HOH A1368 16.967 16.584 65.526 1.00 57.37 O HETATM 3308 O HOH A1369 10.517 15.872 70.904 1.00 58.10 O HETATM 3309 O HOH A1370 21.827 29.399 65.437 1.00 43.84 O HETATM 3310 O HOH A1371 24.636 30.560 65.586 1.00 55.29 O HETATM 3311 O HOH A1372 17.442 13.010 69.012 1.00 69.87 O HETATM 3312 O HOH A1373 27.772 13.052 36.841 1.00 44.28 O HETATM 3313 O HOH A1374 39.243 18.796 31.784 1.00 64.89 O CONECT 1060 1109 CONECT 1109 1060 CONECT 1374 1380 CONECT 1380 1374 1381 CONECT 1381 1380 1382 1388 CONECT 1382 1381 1383 CONECT 1383 1382 1384 CONECT 1384 1383 1385 CONECT 1385 1384 1386 1387 CONECT 1386 1385 CONECT 1387 1385 CONECT 1388 1381 1389 1390 CONECT 1389 1388 CONECT 1390 1388 CONECT 2853 2854 CONECT 2854 2853 2856 CONECT 2855 2864 2866 CONECT 2856 2854 2857 CONECT 2857 2856 2858 CONECT 2858 2857 2859 CONECT 2859 2858 2860 CONECT 2860 2859 2861 CONECT 2861 2860 2863 CONECT 2862 2864 2868 CONECT 2863 2861 2865 2868 CONECT 2864 2855 2862 2867 CONECT 2865 2863 CONECT 2866 2855 CONECT 2867 2864 CONECT 2868 2862 2863 CONECT 2869 2872 CONECT 2870 2871 2873 CONECT 2871 2870 2874 CONECT 2872 2869 2876 CONECT 2873 2870 2877 CONECT 2874 2871 2878 CONECT 2875 2889 2891 CONECT 2876 2872 2879 CONECT 2877 2873 2880 CONECT 2878 2874 2881 CONECT 2879 2876 2882 CONECT 2880 2877 2882 CONECT 2881 2878 2883 CONECT 2882 2879 2880 CONECT 2883 2881 2884 CONECT 2884 2883 2885 CONECT 2885 2884 2886 CONECT 2886 2885 2888 CONECT 2887 2889 2893 CONECT 2888 2886 2890 2893 CONECT 2889 2875 2887 2892 CONECT 2890 2888 CONECT 2891 2875 CONECT 2892 2889 CONECT 2893 2887 2888 CONECT 2894 2895 CONECT 2895 2894 2896 CONECT 2896 2895 2897 CONECT 2897 2896 2898 CONECT 2898 2897 2899 CONECT 2899 2898 2900 CONECT 2900 2899 2901 CONECT 2901 2900 2902 CONECT 2902 2901 2903 CONECT 2903 2902 2904 CONECT 2904 2903 2905 CONECT 2905 2904 2906 CONECT 2906 2905 2907 CONECT 2907 2906 2908 CONECT 2908 2907 2909 CONECT 2909 2908 2910 CONECT 2910 2909 2911 CONECT 2911 2910 2912 CONECT 2912 2911 2913 CONECT 2913 2912 CONECT 2914 2915 2916 2917 CONECT 2915 2914 CONECT 2916 2914 CONECT 2917 2914 2918 CONECT 2918 2917 2919 CONECT 2919 2918 2920 CONECT 2920 2919 2921 CONECT 2921 2920 2922 CONECT 2922 2921 2923 CONECT 2923 2922 2924 CONECT 2924 2923 2925 CONECT 2925 2924 2926 CONECT 2926 2925 2927 CONECT 2927 2926 2928 CONECT 2928 2927 2929 CONECT 2929 2928 2930 CONECT 2930 2929 2931 CONECT 2931 2930 2932 CONECT 2932 2931 2933 CONECT 2933 2932 CONECT 2934 2935 CONECT 2935 2934 2936 CONECT 2936 2935 2937 CONECT 2937 2936 2938 CONECT 2938 2937 2939 CONECT 2939 2938 2940 CONECT 2940 2939 2941 CONECT 2941 2940 2942 CONECT 2942 2941 2943 CONECT 2943 2942 2944 CONECT 2944 2943 2945 CONECT 2945 2944 2946 CONECT 2946 2945 2947 CONECT 2947 2946 CONECT 2948 2949 2950 2951 CONECT 2949 2948 CONECT 2950 2948 CONECT 2951 2948 2952 CONECT 2952 2951 2953 CONECT 2953 2952 2954 CONECT 2954 2953 2955 CONECT 2955 2954 2956 CONECT 2956 2955 2957 CONECT 2957 2956 2958 CONECT 2958 2957 2959 CONECT 2959 2958 2960 CONECT 2960 2959 2961 CONECT 2961 2960 2962 CONECT 2962 2961 2963 CONECT 2963 2962 2964 CONECT 2964 2963 2965 CONECT 2965 2964 2966 CONECT 2966 2965 2967 CONECT 2967 2966 CONECT 2968 2969 2970 2971 CONECT 2969 2968 CONECT 2970 2968 CONECT 2971 2968 2972 CONECT 2972 2971 2973 CONECT 2973 2972 2974 CONECT 2974 2973 2975 CONECT 2975 2974 2976 CONECT 2976 2975 2977 CONECT 2977 2976 2978 CONECT 2978 2977 2979 CONECT 2979 2978 2980 CONECT 2980 2979 2981 CONECT 2981 2980 2982 CONECT 2982 2981 2983 CONECT 2983 2982 2984 CONECT 2984 2983 2985 CONECT 2985 2984 2986 CONECT 2986 2985 2987 CONECT 2987 2986 CONECT 2988 2989 2990 2991 CONECT 2989 2988 CONECT 2990 2988 CONECT 2991 2988 2992 CONECT 2992 2991 2993 CONECT 2993 2992 2994 CONECT 2994 2993 2995 CONECT 2995 2994 2996 CONECT 2996 2995 2997 CONECT 2997 2996 2998 CONECT 2998 2997 2999 CONECT 2999 2998 3000 CONECT 3000 2999 3001 CONECT 3001 3000 3002 CONECT 3002 3001 3003 CONECT 3003 3002 3004 CONECT 3004 3003 3005 CONECT 3005 3004 3006 CONECT 3006 3005 3007 CONECT 3007 3006 CONECT 3008 3009 3010 3011 CONECT 3009 3008 CONECT 3010 3008 CONECT 3011 3008 3012 CONECT 3012 3011 3013 CONECT 3013 3012 3014 CONECT 3014 3013 3015 CONECT 3015 3014 3016 CONECT 3016 3015 3017 CONECT 3017 3016 3018 CONECT 3018 3017 3019 CONECT 3019 3018 3020 CONECT 3020 3019 3021 CONECT 3021 3020 3022 CONECT 3022 3021 3023 CONECT 3023 3022 3024 CONECT 3024 3023 3025 CONECT 3025 3024 3026 CONECT 3026 3025 3027 CONECT 3027 3026 CONECT 3028 3029 3030 3031 CONECT 3029 3028 CONECT 3030 3028 CONECT 3031 3028 3032 CONECT 3032 3031 3033 CONECT 3033 3032 3034 CONECT 3034 3033 3035 CONECT 3035 3034 3036 CONECT 3036 3035 3037 CONECT 3037 3036 3038 CONECT 3038 3037 3039 CONECT 3039 3038 3040 CONECT 3040 3039 3041 CONECT 3041 3040 3042 CONECT 3042 3041 3043 CONECT 3043 3042 3044 CONECT 3044 3043 3045 CONECT 3045 3044 3046 CONECT 3046 3045 3047 CONECT 3047 3046 CONECT 3048 3051 CONECT 3049 3050 3052 CONECT 3050 3049 3053 CONECT 3051 3048 3055 CONECT 3052 3049 3056 CONECT 3053 3050 3057 CONECT 3054 3068 3070 CONECT 3055 3051 3058 CONECT 3056 3052 3059 CONECT 3057 3053 3060 CONECT 3058 3055 3061 CONECT 3059 3056 3061 CONECT 3060 3057 3062 CONECT 3061 3058 3059 CONECT 3062 3060 3063 CONECT 3063 3062 3064 CONECT 3064 3063 3065 CONECT 3065 3064 3067 CONECT 3066 3068 3072 CONECT 3067 3065 3069 3072 CONECT 3068 3054 3066 3071 CONECT 3069 3067 CONECT 3070 3054 CONECT 3071 3068 CONECT 3072 3066 3067 CONECT 3073 3076 CONECT 3074 3075 3077 CONECT 3075 3074 3078 CONECT 3076 3073 3080 CONECT 3077 3074 3081 CONECT 3078 3075 3082 CONECT 3079 3093 3095 CONECT 3080 3076 3083 CONECT 3081 3077 3084 CONECT 3082 3078 3085 CONECT 3083 3080 3086 CONECT 3084 3081 3086 CONECT 3085 3082 3087 CONECT 3086 3083 3084 CONECT 3087 3085 3088 CONECT 3088 3087 3089 CONECT 3089 3088 3090 CONECT 3090 3089 3092 CONECT 3091 3093 3097 CONECT 3092 3090 3094 3097 CONECT 3093 3079 3091 3096 CONECT 3094 3092 CONECT 3095 3079 CONECT 3096 3093 CONECT 3097 3091 3092 CONECT 3098 3099 CONECT 3099 3098 3100 CONECT 3100 3099 3101 CONECT 3101 3100 3102 CONECT 3102 3101 3103 CONECT 3103 3102 3104 CONECT 3104 3103 3105 CONECT 3105 3104 3106 CONECT 3106 3105 3107 CONECT 3107 3106 3108 CONECT 3108 3107 3109 CONECT 3109 3108 3110 CONECT 3110 3109 CONECT 3111 3114 CONECT 3112 3113 3115 CONECT 3113 3112 3116 CONECT 3114 3111 3118 CONECT 3115 3112 3119 CONECT 3116 3113 3120 CONECT 3117 3131 3133 CONECT 3118 3114 3121 CONECT 3119 3115 3122 CONECT 3120 3116 3123 CONECT 3121 3118 3124 CONECT 3122 3119 3124 CONECT 3123 3120 3125 CONECT 3124 3121 3122 CONECT 3125 3123 3126 CONECT 3126 3125 3127 CONECT 3127 3126 3128 CONECT 3128 3127 3130 CONECT 3129 3131 3135 CONECT 3130 3128 3132 3135 CONECT 3131 3117 3129 3134 CONECT 3132 3130 CONECT 3133 3117 CONECT 3134 3131 CONECT 3135 3129 3130 CONECT 3136 3137 3138 3139 CONECT 3137 3136 CONECT 3138 3136 CONECT 3139 3136 3140 CONECT 3140 3139 3141 CONECT 3141 3140 3142 CONECT 3142 3141 3143 CONECT 3143 3142 3144 CONECT 3144 3143 3145 CONECT 3145 3144 3146 CONECT 3146 3145 3147 CONECT 3147 3146 3148 CONECT 3148 3147 3149 CONECT 3149 3148 CONECT 3150 3151 CONECT 3151 3150 3152 CONECT 3152 3151 3153 CONECT 3153 3152 3154 CONECT 3154 3153 3155 CONECT 3155 3154 3156 CONECT 3156 3155 3157 CONECT 3157 3156 3158 CONECT 3158 3157 CONECT 3159 3160 3161 3162 CONECT 3160 3159 CONECT 3161 3159 CONECT 3162 3159 3163 CONECT 3163 3162 3164 CONECT 3164 3163 3165 CONECT 3165 3164 3166 CONECT 3166 3165 3167 CONECT 3167 3166 3168 CONECT 3168 3167 3169 CONECT 3169 3168 3170 CONECT 3170 3169 3171 CONECT 3171 3170 3172 CONECT 3172 3171 3173 CONECT 3173 3172 3174 CONECT 3174 3173 3175 CONECT 3175 3174 3176 CONECT 3176 3175 3177 CONECT 3177 3176 3178 CONECT 3178 3177 CONECT 3179 3180 3181 3182 CONECT 3180 3179 CONECT 3181 3179 CONECT 3182 3179 3183 CONECT 3183 3182 3184 CONECT 3184 3183 3185 CONECT 3185 3184 3186 CONECT 3186 3185 3187 CONECT 3187 3186 3188 CONECT 3188 3187 3189 CONECT 3189 3188 3190 CONECT 3190 3189 3191 CONECT 3191 3190 3192 CONECT 3192 3191 3193 CONECT 3193 3192 3194 CONECT 3194 3193 3195 CONECT 3195 3194 3196 CONECT 3196 3195 3197 CONECT 3197 3196 3198 CONECT 3198 3197 CONECT 3199 3200 3201 3202 CONECT 3200 3199 CONECT 3201 3199 CONECT 3202 3199 3203 CONECT 3203 3202 3204 CONECT 3204 3203 3205 CONECT 3205 3204 3206 CONECT 3206 3205 3207 CONECT 3207 3206 3208 CONECT 3208 3207 3209 CONECT 3209 3208 3210 CONECT 3210 3209 3211 CONECT 3211 3210 CONECT 3212 3213 3221 CONECT 3213 3212 3214 CONECT 3214 3213 3215 3239 CONECT 3215 3214 3216 CONECT 3216 3215 3217 3221 CONECT 3217 3216 3218 CONECT 3218 3217 3219 CONECT 3219 3218 3220 3225 CONECT 3220 3219 3221 3222 CONECT 3221 3212 3216 3220 3230 CONECT 3222 3220 3223 CONECT 3223 3222 3224 CONECT 3224 3223 3225 3228 3229 CONECT 3225 3219 3224 3226 CONECT 3226 3225 3227 CONECT 3227 3226 3228 CONECT 3228 3224 3227 3231 CONECT 3229 3224 CONECT 3230 3221 CONECT 3231 3228 3232 3233 CONECT 3232 3231 CONECT 3233 3231 3234 CONECT 3234 3233 3235 CONECT 3235 3234 3236 CONECT 3236 3235 3237 3238 CONECT 3237 3236 CONECT 3238 3236 CONECT 3239 3214 MASTER 353 0 21 13 0 0 0 6 3238 1 401 34 END