HEADER SIGNALING PROTEIN 05-APR-11 3REY TITLE THERMOSTABILISED ADENOSINE A2A RECEPTOR IN COMPLEX WITH XAC COMPND MOL_ID: 1; COMPND 2 MOLECULE: ADENOSINE RECEPTOR A2A; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: RESIDUES 1-317; COMPND 5 ENGINEERED: YES; COMPND 6 MUTATION: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606; SOURCE 5 GENE: ADORA2A; SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM; SOURCE 8 EXPRESSION_SYSTEM_TAXID: 7108; SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS KEYWDS 7TM, GPCR, SIGNALING PROTEIN, G-PROTEIN, MEMBRANE PROTEIN EXPDTA X-RAY DIFFRACTION AUTHOR A.S.DORE,N.ROBERTSON,J.C.ERREY,I.NG,K.HOLLENSTEIN,B.TEHAN,E.HURRELL, AUTHOR 2 K.BENNETT,M.CONGREVE,F.MAGNANI,C.G.TATE,M.WEIR,F.H.MARSHALL REVDAT 2 20-JUN-12 3REY 1 JRNL REVDAT 1 07-SEP-11 3REY 0 JRNL AUTH A.S.DORE,N.ROBERTSON,J.C.ERREY,I.NG,K.HOLLENSTEIN,B.TEHAN, JRNL AUTH 2 E.HURRELL,K.BENNETT,M.CONGREVE,F.MAGNANI,C.G.TATE,M.WEIR, JRNL AUTH 3 F.H.MARSHALL JRNL TITL STRUCTURE OF THE ADENOSINE A(2A) RECEPTOR IN COMPLEX WITH JRNL TITL 2 ZM241385 AND THE XANTHINES XAC AND CAFFEINE JRNL REF STRUCTURE V. 19 1283 2011 JRNL REFN ISSN 0969-2126 JRNL PMID 21885291 JRNL DOI 10.1016/J.STR.2011.06.014 REMARK 2 REMARK 2 RESOLUTION. 3.31 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.4_84) REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE- REMARK 3 : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO, REMARK 3 : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL REMARK 3 : MORIARTY,REETAL PAI,RANDY READ,JANE REMARK 3 : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM REMARK 3 : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH, REMARK 3 : LAURENT STORONI,TOM TERWILLIGER,PETER REMARK 3 : ZWART REMARK 3 REMARK 3 REFINEMENT TARGET : ML REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.31 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.94 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350 REMARK 3 COMPLETENESS FOR RANGE (%) : 84.8 REMARK 3 NUMBER OF REFLECTIONS : 10404 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.300 REMARK 3 R VALUE (WORKING SET) : 0.299 REMARK 3 FREE R VALUE : 0.319 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.720 REMARK 3 FREE R VALUE TEST SET COUNT : 491 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS). REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE REMARK 3 1 19.9387 - 5.2291 0.86 2619 117 0.2837 0.2811 REMARK 3 2 5.2291 - 4.1629 0.87 2542 134 0.2482 0.3067 REMARK 3 3 4.1629 - 3.6403 0.90 2567 134 0.3455 0.3660 REMARK 3 4 3.6403 - 3.3091 0.76 2185 106 0.4329 0.4495 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL REMARK 3 SOLVENT RADIUS : 1.11 REMARK 3 SHRINKAGE RADIUS : 0.90 REMARK 3 K_SOL : 0.22 REMARK 3 B_SOL : 74.29 REMARK 3 REMARK 3 ERROR ESTIMATES. REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.450 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 42.020 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 101.20 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 156.85 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : -78.99100 REMARK 3 B22 (A**2) : 16.24410 REMARK 3 B33 (A**2) : 62.74700 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : 0.00000 REMARK 3 B23 (A**2) : -0.00000 REMARK 3 REMARK 3 TWINNING INFORMATION. REMARK 3 FRACTION: NULL REMARK 3 OPERATOR: NULL REMARK 3 REMARK 3 DEVIATIONS FROM IDEAL VALUES. REMARK 3 RMSD COUNT REMARK 3 BOND : 0.001 2343 REMARK 3 ANGLE : 0.394 3193 REMARK 3 CHIRALITY : 0.028 377 REMARK 3 PLANARITY : 0.032 392 REMARK 3 DIHEDRAL : 10.402 811 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 1 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: chain A REMARK 3 ORIGIN FOR THE GROUP (A): 31.9487 25.5491 28.2055 REMARK 3 T TENSOR REMARK 3 T11: 0.9335 T22: 1.0090 REMARK 3 T33: 1.1920 T12: 0.0060 REMARK 3 T13: -0.0567 T23: -0.1191 REMARK 3 L TENSOR REMARK 3 L11: 2.2274 L22: 3.0223 REMARK 3 L33: 0.9435 L12: 1.4046 REMARK 3 L13: -0.3168 L23: -0.6691 REMARK 3 S TENSOR REMARK 3 S11: 0.1845 S12: 0.3374 S13: 0.1892 REMARK 3 S21: -0.2261 S22: 0.0525 S23: 0.1308 REMARK 3 S31: 0.1362 S32: -0.0524 S33: 0.0000 REMARK 3 REMARK 3 NCS DETAILS REMARK 3 NUMBER OF NCS GROUPS : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: SIMULATED ANNEALING, TLS, RESTRAINED REMARK 3 REFINEMENT REMARK 4 REMARK 4 3REY COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 12-APR-11. REMARK 100 THE RCSB ID CODE IS RCSB064846. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 06-MAY-10 REMARK 200 TEMPERATURE (KELVIN) : 200 REMARK 200 PH : 8.2 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : DIAMOND REMARK 200 BEAMLINE : I24 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.9777 REMARK 200 MONOCHROMATOR : ACCEL FIXED EXIT DOUBLE CRYSTAL REMARK 200 SI (111) REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : PSI PILATUS 6M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : SCALA REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 10627 REMARK 200 RESOLUTION RANGE HIGH (A) : 3.300 REMARK 200 RESOLUTION RANGE LOW (A) : 48.690 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.500 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 89.8 REMARK 200 DATA REDUNDANCY : 5.300 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.30 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.48 REMARK 200 COMPLETENESS FOR SHELL (%) : 90.7 REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: PHASER REMARK 200 STARTING MODEL: 3PWH REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 77.62 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 5.50 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 32-42% PEG1000, 0.25M MGCL2, 0.3% NG, REMARK 280 0.1%(W/V) 1-BUTANOL, 0.05% CYMAL-6, 0.1M TRIS-HCL(PH 8.1), VAPOR REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 277K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 2 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,Y,-Z REMARK 290 4555 X,-Y,-Z REMARK 290 5555 X+1/2,Y+1/2,Z+1/2 REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2 REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2 REMARK 290 8555 X+1/2,-Y+1/2,-Z+1/2 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 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 55.93250 REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 56.53050 REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 63.40100 REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 55.93250 REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 56.53050 REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 63.40100 REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 55.93250 REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 56.53050 REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 63.40100 REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 55.93250 REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 56.53050 REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 63.40100 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 APPLY THE FOLLOWING TO CHAINS: A REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 MET A 1 REMARK 465 PRO A 2 REMARK 465 ILE A 3 REMARK 465 MET A 4 REMARK 465 GLY A 5 REMARK 465 SER A 6 REMARK 465 LYS A 150 REMARK 465 GLU A 151 REMARK 465 GLY A 152 REMARK 465 LYS A 153 REMARK 465 ASN A 154 REMARK 465 HIS A 155 REMARK 465 SER A 156 REMARK 465 GLN A 157 REMARK 465 HIS A 306 REMARK 465 VAL A 307 REMARK 465 LEU A 308 REMARK 465 ARG A 309 REMARK 465 GLN A 310 REMARK 465 GLN A 311 REMARK 465 GLU A 312 REMARK 465 PRO A 313 REMARK 465 PHE A 314 REMARK 465 LYS A 315 REMARK 465 ALA A 316 REMARK 465 ALA A 317 REMARK 465 ALA A 318 REMARK 465 ALA A 319 REMARK 465 HIS A 320 REMARK 465 HIS A 321 REMARK 465 HIS A 322 REMARK 465 HIS A 323 REMARK 465 HIS A 324 REMARK 465 HIS A 325 REMARK 465 HIS A 326 REMARK 465 HIS A 327 REMARK 465 HIS A 328 REMARK 465 HIS A 329 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 GLN A 38 33.51 -90.78 REMARK 500 LEU A 58 -51.22 -129.66 REMARK 500 ALA A 73 172.31 -56.53 REMARK 500 ALA A 165 102.14 -55.85 REMARK 500 VAL A 178 -67.57 -101.71 REMARK 500 PHE A 182 -76.06 -59.70 REMARK 500 VAL A 186 -55.15 -140.58 REMARK 500 PRO A 217 -70.24 -55.19 REMARK 500 PHE A 257 -70.23 -76.80 REMARK 500 REMARK 500 REMARK: NULL REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE XAC A 999 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 3PWH RELATED DB: PDB REMARK 900 THE SAME PROTEIN COMPLEXED WITH ZM241385 REMARK 900 RELATED ID: 3RFM RELATED DB: PDB REMARK 900 THE SAME PROTEIN COMPLEXED WITH CAFFEINE DBREF 3REY A 1 317 UNP P29274 AA2AR_HUMAN 1 317 SEQADV 3REY LEU A 54 UNP P29274 ALA 54 ENGINEERED MUTATION SEQADV 3REY ALA A 88 UNP P29274 THR 88 ENGINEERED MUTATION SEQADV 3REY ALA A 107 UNP P29274 ARG 107 ENGINEERED MUTATION SEQADV 3REY ALA A 122 UNP P29274 LYS 122 ENGINEERED MUTATION SEQADV 3REY ALA A 202 UNP P29274 LEU 202 ENGINEERED MUTATION SEQADV 3REY ALA A 235 UNP P29274 LEU 235 ENGINEERED MUTATION SEQADV 3REY ALA A 239 UNP P29274 VAL 239 ENGINEERED MUTATION SEQADV 3REY ALA A 277 UNP P29274 SER 277 ENGINEERED MUTATION SEQADV 3REY ALA A 318 UNP P29274 EXPRESSION TAG SEQADV 3REY ALA A 319 UNP P29274 EXPRESSION TAG SEQADV 3REY HIS A 320 UNP P29274 EXPRESSION TAG SEQADV 3REY HIS A 321 UNP P29274 EXPRESSION TAG SEQADV 3REY HIS A 322 UNP P29274 EXPRESSION TAG SEQADV 3REY HIS A 323 UNP P29274 EXPRESSION TAG SEQADV 3REY HIS A 324 UNP P29274 EXPRESSION TAG SEQADV 3REY HIS A 325 UNP P29274 EXPRESSION TAG SEQADV 3REY HIS A 326 UNP P29274 EXPRESSION TAG SEQADV 3REY HIS A 327 UNP P29274 EXPRESSION TAG SEQADV 3REY HIS A 328 UNP P29274 EXPRESSION TAG SEQADV 3REY HIS A 329 UNP P29274 EXPRESSION TAG SEQRES 1 A 329 MET PRO ILE MET GLY SER SER VAL TYR ILE THR VAL GLU SEQRES 2 A 329 LEU ALA ILE ALA VAL LEU ALA ILE LEU GLY ASN VAL LEU SEQRES 3 A 329 VAL CYS TRP ALA VAL TRP LEU ASN SER ASN LEU GLN ASN SEQRES 4 A 329 VAL THR ASN TYR PHE VAL VAL SER LEU ALA ALA ALA ASP SEQRES 5 A 329 ILE LEU VAL GLY VAL LEU ALA ILE PRO PHE ALA ILE THR SEQRES 6 A 329 ILE SER THR GLY PHE CYS ALA ALA CYS HIS GLY CYS LEU SEQRES 7 A 329 PHE ILE ALA CYS PHE VAL LEU VAL LEU ALA GLN SER SER SEQRES 8 A 329 ILE PHE SER LEU LEU ALA ILE ALA ILE ASP ARG TYR ILE SEQRES 9 A 329 ALA ILE ALA ILE PRO LEU ARG TYR ASN GLY LEU VAL THR SEQRES 10 A 329 GLY THR ARG ALA ALA GLY ILE ILE ALA ILE CYS TRP VAL SEQRES 11 A 329 LEU SER PHE ALA ILE GLY LEU THR PRO MET LEU GLY TRP SEQRES 12 A 329 ASN ASN CYS GLY GLN PRO LYS GLU GLY LYS ASN HIS SER SEQRES 13 A 329 GLN GLY CYS GLY GLU GLY GLN VAL ALA CYS LEU PHE GLU SEQRES 14 A 329 ASP VAL VAL PRO MET ASN TYR MET VAL TYR PHE ASN PHE SEQRES 15 A 329 PHE ALA CYS VAL LEU VAL PRO LEU LEU LEU MET LEU GLY SEQRES 16 A 329 VAL TYR LEU ARG ILE PHE ALA ALA ALA ARG ARG GLN LEU SEQRES 17 A 329 LYS GLN MET GLU SER GLN PRO LEU PRO GLY GLU ARG ALA SEQRES 18 A 329 ARG SER THR LEU GLN LYS GLU VAL HIS ALA ALA LYS SER SEQRES 19 A 329 ALA ALA ILE ILE ALA GLY LEU PHE ALA LEU CYS TRP LEU SEQRES 20 A 329 PRO LEU HIS ILE ILE ASN CYS PHE THR PHE PHE CYS PRO SEQRES 21 A 329 ASP CYS SER HIS ALA PRO LEU TRP LEU MET TYR LEU ALA SEQRES 22 A 329 ILE VAL LEU ALA HIS THR ASN SER VAL VAL ASN PRO PHE SEQRES 23 A 329 ILE TYR ALA TYR ARG ILE ARG GLU PHE ARG GLN THR PHE SEQRES 24 A 329 ARG LYS ILE ILE ARG SER HIS VAL LEU ARG GLN GLN GLU SEQRES 25 A 329 PRO PHE LYS ALA ALA ALA ALA HIS HIS HIS HIS HIS HIS SEQRES 26 A 329 HIS HIS HIS HIS HET XAC A 999 31 HETNAM XAC N-(2-AMINOETHYL)-2-[4-(2,6-DIOXO-1,3-DIPROPYL-2,3,6,7- HETNAM 2 XAC TETRAHYDRO-1H-PURIN-8-YL)PHENOXY]ACETAMIDE FORMUL 2 XAC C21 H28 N6 O4 HELIX 1 1 SER A 7 ASN A 34 1 28 HELIX 2 2 ASN A 39 LEU A 58 1 20 HELIX 3 3 LEU A 58 GLY A 69 1 12 HELIX 4 4 ALA A 73 PHE A 83 1 11 HELIX 5 5 PHE A 83 ILE A 108 1 26 HELIX 6 6 ARG A 111 VAL A 116 1 6 HELIX 7 7 THR A 117 LEU A 137 1 21 HELIX 8 8 LEU A 167 VAL A 172 1 6 HELIX 9 9 MET A 174 TYR A 179 1 6 HELIX 10 10 ASN A 181 VAL A 186 1 6 HELIX 11 11 VAL A 186 MET A 211 1 26 HELIX 12 12 GLY A 218 CYS A 259 1 42 HELIX 13 13 PRO A 266 ILE A 292 1 27 HELIX 14 14 ILE A 292 SER A 305 1 14 SHEET 1 A 2 CYS A 71 ALA A 72 0 SHEET 2 A 2 VAL A 164 ALA A 165 -1 O VAL A 164 N ALA A 72 SSBOND 1 CYS A 71 CYS A 159 1555 1555 2.03 SSBOND 2 CYS A 74 CYS A 146 1555 1555 2.04 SSBOND 3 CYS A 77 CYS A 166 1555 1555 2.03 SSBOND 4 CYS A 259 CYS A 262 1555 1555 2.03 SITE 1 AC1 9 ALA A 81 PHE A 168 MET A 177 HIS A 250 SITE 2 AC1 9 ASN A 253 LEU A 267 MET A 270 TYR A 271 SITE 3 AC1 9 ILE A 274 CRYST1 111.865 113.061 126.802 90.00 90.00 90.00 I 2 2 2 8 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 0.008939 0.000000 0.000000 0.00000 SCALE2 0.000000 0.008845 0.000000 0.00000 SCALE3 0.000000 0.000000 0.007886 0.00000 ATOM 1 N SER A 7 49.281 22.300 50.754 1.00149.77 N ANISOU 1 N SER A 7 18244 18307 20355 -2817 -3394 -166 N ATOM 2 CA SER A 7 48.061 21.518 50.583 1.00155.09 C ANISOU 2 CA SER A 7 19018 18968 20942 -2713 -3274 -235 C ATOM 3 C SER A 7 46.838 22.427 50.480 1.00151.96 C ANISOU 3 C SER A 7 18812 18612 20313 -2726 -2948 -475 C ATOM 4 O SER A 7 45.704 21.984 50.666 1.00137.20 O ANISOU 4 O SER A 7 17080 16750 18298 -2733 -2849 -539 O ATOM 5 CB SER A 7 47.894 20.526 51.737 1.00156.11 C ANISOU 5 CB SER A 7 19277 19111 20929 -2939 -3543 -66 C ATOM 6 OG SER A 7 46.819 19.634 51.497 1.00149.86 O ANISOU 6 OG SER A 7 18542 18291 20107 -2819 -3449 -107 O ATOM 7 N VAL A 8 47.079 23.700 50.182 1.00156.46 N ANISOU 7 N VAL A 8 19376 19199 20874 -2728 -2779 -598 N ATOM 8 CA VAL A 8 46.000 24.667 50.018 1.00150.23 C ANISOU 8 CA VAL A 8 18734 18426 19923 -2723 -2458 -817 C ATOM 9 C VAL A 8 45.381 24.551 48.630 1.00148.87 C ANISOU 9 C VAL A 8 18428 18215 19920 -2387 -2229 -910 C ATOM 10 O VAL A 8 44.159 24.511 48.488 1.00146.97 O ANISOU 10 O VAL A 8 18286 17974 19580 -2335 -2042 -1020 O ATOM 11 CB VAL A 8 46.491 26.110 50.234 1.00142.25 C ANISOU 11 CB VAL A 8 17768 17428 18851 -2862 -2362 -910 C ATOM 12 CG1 VAL A 8 45.380 27.101 49.920 1.00132.10 C ANISOU 12 CG1 VAL A 8 16594 16129 17469 -2812 -2008 -1128 C ATOM 13 CG2 VAL A 8 46.991 26.293 51.658 1.00143.21 C ANISOU 13 CG2 VAL A 8 18064 17595 18752 -3238 -2579 -840 C ATOM 14 N TYR A 9 46.232 24.501 47.610 1.00152.17 N ANISOU 14 N TYR A 9 18622 18601 20594 -2171 -2245 -861 N ATOM 15 CA TYR A 9 45.772 24.330 46.238 1.00151.21 C ANISOU 15 CA TYR A 9 18379 18451 20622 -1868 -2053 -935 C ATOM 16 C TYR A 9 44.967 23.045 46.103 1.00153.03 C ANISOU 16 C TYR A 9 18633 18661 20849 -1775 -2093 -909 C ATOM 17 O TYR A 9 43.979 22.993 45.370 1.00153.87 O ANISOU 17 O TYR A 9 18757 18765 20944 -1624 -1908 -1010 O ATOM 18 CB TYR A 9 46.958 24.307 45.275 1.00153.41 C ANISOU 18 CB TYR A 9 18421 18698 21170 -1683 -2087 -869 C ATOM 19 CG TYR A 9 46.590 23.952 43.851 1.00147.63 C ANISOU 19 CG TYR A 9 17576 17939 20577 -1390 -1915 -932 C ATOM 20 CD1 TYR A 9 46.188 24.930 42.954 1.00144.92 C ANISOU 20 CD1 TYR A 9 17222 17612 20229 -1272 -1668 -1051 C ATOM 21 CD2 TYR A 9 46.649 22.637 43.404 1.00141.24 C ANISOU 21 CD2 TYR A 9 16677 17084 19902 -1246 -2005 -869 C ATOM 22 CE1 TYR A 9 45.853 24.611 41.652 1.00142.07 C ANISOU 22 CE1 TYR A 9 16777 17239 19963 -1033 -1528 -1100 C ATOM 23 CE2 TYR A 9 46.317 22.309 42.103 1.00136.64 C ANISOU 23 CE2 TYR A 9 16018 16480 19420 -1005 -1847 -941 C ATOM 24 CZ TYR A 9 45.920 23.301 41.232 1.00139.81 C ANISOU 24 CZ TYR A 9 16422 16914 19784 -907 -1616 -1054 C ATOM 25 OH TYR A 9 45.588 22.982 39.936 1.00140.37 O ANISOU 25 OH TYR A 9 16434 16976 19924 -695 -1474 -1117 O ATOM 26 N ILE A 10 45.396 22.008 46.815 1.00155.06 N ANISOU 26 N ILE A 10 18887 18901 21126 -1873 -2349 -761 N ATOM 27 CA ILE A 10 44.680 20.740 46.821 1.00155.47 C ANISOU 27 CA ILE A 10 18971 18924 21178 -1814 -2411 -721 C ATOM 28 C ILE A 10 43.285 20.927 47.405 1.00155.55 C ANISOU 28 C ILE A 10 19194 18973 20934 -1940 -2278 -824 C ATOM 29 O ILE A 10 42.296 20.472 46.832 1.00153.54 O ANISOU 29 O ILE A 10 18951 18703 20684 -1805 -2154 -892 O ATOM 30 CB ILE A 10 45.426 19.673 47.641 1.00158.05 C ANISOU 30 CB ILE A 10 19263 19217 21572 -1934 -2729 -517 C ATOM 31 CG1 ILE A 10 46.860 19.514 47.130 1.00158.23 C ANISOU 31 CG1 ILE A 10 19048 19185 21887 -1816 -2859 -402 C ATOM 32 CG2 ILE A 10 44.681 18.347 47.592 1.00155.00 C ANISOU 32 CG2 ILE A 10 18903 18782 21207 -1863 -2785 -476 C ATOM 33 CD1 ILE A 10 47.674 18.498 47.902 1.00156.09 C ANISOU 33 CD1 ILE A 10 18704 18864 21739 -1923 -3187 -172 C ATOM 34 N THR A 11 43.215 21.604 48.547 1.00158.61 N ANISOU 34 N THR A 11 19751 19410 21106 -2210 -2296 -837 N ATOM 35 CA THR A 11 41.944 21.861 49.213 1.00153.46 C ANISOU 35 CA THR A 11 19307 18788 20215 -2356 -2141 -943 C ATOM 36 C THR A 11 41.008 22.672 48.322 1.00139.68 C ANISOU 36 C THR A 11 17543 17034 18496 -2187 -1826 -1117 C ATOM 37 O THR A 11 39.828 22.349 48.192 1.00131.21 O ANISOU 37 O THR A 11 16525 15953 17374 -2139 -1698 -1179 O ATOM 38 CB THR A 11 42.145 22.611 50.542 1.00157.67 C ANISOU 38 CB THR A 11 20035 19369 20505 -2689 -2179 -956 C ATOM 39 OG1 THR A 11 43.000 21.847 51.401 1.00165.54 O ANISOU 39 OG1 THR A 11 21051 20380 21465 -2870 -2505 -765 O ATOM 40 CG2 THR A 11 40.809 22.837 51.235 1.00153.93 C ANISOU 40 CG2 THR A 11 19777 18915 19795 -2841 -1981 -1079 C ATOM 41 N VAL A 12 41.544 23.724 47.710 1.00132.45 N ANISOU 41 N VAL A 12 16540 16115 17672 -2103 -1714 -1180 N ATOM 42 CA VAL A 12 40.758 24.581 46.831 1.00124.61 C ANISOU 42 CA VAL A 12 15513 15108 16726 -1946 -1435 -1317 C ATOM 43 C VAL A 12 40.217 23.798 45.639 1.00127.57 C ANISOU 43 C VAL A 12 15766 15463 17241 -1685 -1397 -1310 C ATOM 44 O VAL A 12 39.050 23.937 45.272 1.00132.77 O ANISOU 44 O VAL A 12 16452 16116 17879 -1613 -1224 -1389 O ATOM 45 CB VAL A 12 41.582 25.777 46.321 1.00118.24 C ANISOU 45 CB VAL A 12 14617 14295 16015 -1897 -1350 -1357 C ATOM 46 CG1 VAL A 12 40.765 26.607 45.342 1.00109.52 C ANISOU 46 CG1 VAL A 12 13463 13168 14981 -1725 -1082 -1467 C ATOM 47 CG2 VAL A 12 42.055 26.632 47.488 1.00123.66 C ANISOU 47 CG2 VAL A 12 15440 14993 16551 -2174 -1375 -1385 C ATOM 48 N GLU A 13 41.071 22.975 45.039 1.00129.70 N ANISOU 48 N GLU A 13 15898 15717 17663 -1551 -1557 -1216 N ATOM 49 CA GLU A 13 40.668 22.152 43.903 1.00134.24 C ANISOU 49 CA GLU A 13 16374 16269 18361 -1322 -1531 -1219 C ATOM 50 C GLU A 13 39.603 21.131 44.295 1.00134.42 C ANISOU 50 C GLU A 13 16488 16281 18303 -1362 -1573 -1208 C ATOM 51 O GLU A 13 38.749 20.771 43.485 1.00131.53 O ANISOU 51 O GLU A 13 16095 15905 17974 -1221 -1482 -1255 O ATOM 52 CB GLU A 13 41.882 21.451 43.290 1.00137.61 C ANISOU 52 CB GLU A 13 16644 16662 18979 -1191 -1677 -1131 C ATOM 53 CG GLU A 13 42.741 22.355 42.424 1.00138.89 C ANISOU 53 CG GLU A 13 16679 16830 19261 -1075 -1579 -1158 C ATOM 54 CD GLU A 13 42.022 22.804 41.168 1.00140.16 C ANISOU 54 CD GLU A 13 16808 17005 19443 -896 -1366 -1256 C ATOM 55 OE1 GLU A 13 41.155 22.050 40.680 1.00145.58 O ANISOU 55 OE1 GLU A 13 17515 17682 20115 -806 -1343 -1283 O ATOM 56 OE2 GLU A 13 42.326 23.906 40.664 1.00135.70 O ANISOU 56 OE2 GLU A 13 16197 16458 18906 -855 -1235 -1295 O ATOM 57 N LEU A 14 39.659 20.668 45.540 1.00137.20 N ANISOU 57 N LEU A 14 16952 16639 18540 -1569 -1719 -1137 N ATOM 58 CA LEU A 14 38.666 19.730 46.051 1.00141.45 C ANISOU 58 CA LEU A 14 17589 17167 18988 -1639 -1758 -1115 C ATOM 59 C LEU A 14 37.330 20.424 46.301 1.00143.09 C ANISOU 59 C LEU A 14 17908 17399 19062 -1707 -1531 -1231 C ATOM 60 O LEU A 14 36.267 19.838 46.097 1.00138.55 O ANISOU 60 O LEU A 14 17351 16811 18482 -1660 -1475 -1250 O ATOM 61 CB LEU A 14 39.167 19.058 47.332 1.00144.20 C ANISOU 61 CB LEU A 14 18030 17517 19241 -1861 -1989 -985 C ATOM 62 CG LEU A 14 39.878 17.710 47.175 1.00145.39 C ANISOU 62 CG LEU A 14 18079 17609 19553 -1785 -2233 -839 C ATOM 63 CD1 LEU A 14 40.910 17.757 46.061 1.00149.19 C ANISOU 63 CD1 LEU A 14 18364 18051 20270 -1565 -2247 -832 C ATOM 64 CD2 LEU A 14 40.515 17.279 48.489 1.00144.84 C ANISOU 64 CD2 LEU A 14 18093 17547 19393 -2029 -2482 -681 C ATOM 65 N ALA A 15 37.390 21.676 46.743 1.00143.88 N ANISOU 65 N ALA A 15 18073 17522 19073 -1820 -1393 -1307 N ATOM 66 CA ALA A 15 36.185 22.456 46.995 1.00139.01 C ANISOU 66 CA ALA A 15 17545 16905 18369 -1880 -1144 -1423 C ATOM 67 C ALA A 15 35.421 22.704 45.699 1.00141.10 C ANISOU 67 C ALA A 15 17683 17150 18779 -1644 -984 -1480 C ATOM 68 O ALA A 15 34.197 22.585 45.658 1.00147.88 O ANISOU 68 O ALA A 15 18563 17996 19630 -1630 -859 -1520 O ATOM 69 CB ALA A 15 36.534 23.774 47.669 1.00134.66 C ANISOU 69 CB ALA A 15 17083 16361 17721 -2042 -1022 -1503 C ATOM 70 N ILE A 16 36.149 23.048 44.642 1.00137.15 N ANISOU 70 N ILE A 16 17050 16650 18413 -1469 -994 -1473 N ATOM 71 CA ILE A 16 35.541 23.270 43.335 1.00135.07 C ANISOU 71 CA ILE A 16 16672 16378 18270 -1258 -874 -1505 C ATOM 72 C ILE A 16 34.954 21.976 42.783 1.00142.09 C ANISOU 72 C ILE A 16 17527 17262 19199 -1155 -971 -1465 C ATOM 73 O ILE A 16 33.913 21.986 42.129 1.00148.04 O ANISOU 73 O ILE A 16 18242 18011 19994 -1064 -872 -1491 O ATOM 74 CB ILE A 16 36.554 23.838 42.323 1.00126.28 C ANISOU 74 CB ILE A 16 15438 15273 17270 -1111 -872 -1498 C ATOM 75 CG1 ILE A 16 36.988 25.245 42.733 1.00127.23 C ANISOU 75 CG1 ILE A 16 15582 15387 17371 -1202 -749 -1547 C ATOM 76 CG2 ILE A 16 35.956 23.862 40.925 1.00120.77 C ANISOU 76 CG2 ILE A 16 14640 14579 16668 -910 -787 -1510 C ATOM 77 CD1 ILE A 16 37.912 25.911 41.735 1.00126.02 C ANISOU 77 CD1 ILE A 16 15309 15240 17334 -1066 -723 -1535 C ATOM 78 N ALA A 17 35.627 20.862 43.053 1.00142.01 N ANISOU 78 N ALA A 17 17523 17242 19191 -1176 -1172 -1393 N ATOM 79 CA ALA A 17 35.171 19.559 42.581 1.00145.06 C ANISOU 79 CA ALA A 17 17885 17604 19626 -1090 -1274 -1359 C ATOM 80 C ALA A 17 33.772 19.238 43.100 1.00148.47 C ANISOU 80 C ALA A 17 18396 18033 19982 -1179 -1210 -1375 C ATOM 81 O ALA A 17 32.937 18.702 42.372 1.00146.81 O ANISOU 81 O ALA A 17 18146 17811 19823 -1080 -1193 -1385 O ATOM 82 CB ALA A 17 36.155 18.473 42.990 1.00146.12 C ANISOU 82 CB ALA A 17 18015 17707 19798 -1121 -1495 -1268 C ATOM 83 N VAL A 18 33.525 19.569 44.363 1.00149.55 N ANISOU 83 N VAL A 18 18650 18179 19992 -1378 -1170 -1377 N ATOM 84 CA VAL A 18 32.226 19.331 44.979 1.00146.43 C ANISOU 84 CA VAL A 18 18334 17778 19524 -1485 -1079 -1396 C ATOM 85 C VAL A 18 31.151 20.220 44.363 1.00138.47 C ANISOU 85 C VAL A 18 17264 16767 18583 -1400 -853 -1472 C ATOM 86 O VAL A 18 30.103 19.738 43.938 1.00134.14 O ANISOU 86 O VAL A 18 16674 16205 18090 -1342 -822 -1467 O ATOM 87 CB VAL A 18 32.275 19.567 46.500 1.00150.06 C ANISOU 87 CB VAL A 18 18953 18252 19809 -1742 -1062 -1394 C ATOM 88 CG1 VAL A 18 30.881 19.492 47.095 1.00153.09 C ANISOU 88 CG1 VAL A 18 19412 18626 20128 -1850 -905 -1431 C ATOM 89 CG2 VAL A 18 33.198 18.557 47.164 1.00150.32 C ANISOU 89 CG2 VAL A 18 19044 18287 19785 -1844 -1320 -1279 C ATOM 90 N LEU A 19 31.422 21.521 44.314 1.00134.95 N ANISOU 90 N LEU A 19 16803 16324 18149 -1397 -705 -1531 N ATOM 91 CA LEU A 19 30.478 22.483 43.754 1.00135.27 C ANISOU 91 CA LEU A 19 16768 16344 18285 -1316 -490 -1585 C ATOM 92 C LEU A 19 30.168 22.192 42.289 1.00139.93 C ANISOU 92 C LEU A 19 17221 16942 19005 -1107 -536 -1549 C ATOM 93 O LEU A 19 29.032 22.350 41.845 1.00148.90 O ANISOU 93 O LEU A 19 18289 18061 20224 -1053 -436 -1548 O ATOM 94 CB LEU A 19 31.009 23.911 43.906 1.00135.17 C ANISOU 94 CB LEU A 19 16760 16318 18281 -1344 -341 -1647 C ATOM 95 CG LEU A 19 30.862 24.580 45.275 1.00139.44 C ANISOU 95 CG LEU A 19 17442 16835 18704 -1564 -193 -1722 C ATOM 96 CD1 LEU A 19 31.443 23.719 46.387 1.00139.01 C ANISOU 96 CD1 LEU A 19 17535 16814 18470 -1754 -363 -1687 C ATOM 97 CD2 LEU A 19 31.509 25.959 45.267 1.00142.20 C ANISOU 97 CD2 LEU A 19 17788 17160 19081 -1577 -66 -1787 C ATOM 98 N ALA A 20 31.182 21.768 41.542 1.00138.98 N ANISOU 98 N ALA A 20 17057 16844 18904 -1000 -685 -1518 N ATOM 99 CA ALA A 20 31.015 21.464 40.125 1.00141.45 C ANISOU 99 CA ALA A 20 17270 17172 19304 -824 -730 -1497 C ATOM 100 C ALA A 20 30.097 20.265 39.919 1.00142.94 C ANISOU 100 C ALA A 20 17460 17351 19500 -814 -820 -1471 C ATOM 101 O ALA A 20 29.378 20.186 38.922 1.00142.79 O ANISOU 101 O ALA A 20 17372 17341 19542 -717 -811 -1458 O ATOM 102 CB ALA A 20 32.366 21.220 39.471 1.00144.07 C ANISOU 102 CB ALA A 20 17569 17520 19652 -730 -842 -1486 C ATOM 103 N ILE A 21 30.129 19.328 40.861 1.00143.76 N ANISOU 103 N ILE A 21 17647 17435 19538 -927 -918 -1452 N ATOM 104 CA ILE A 21 29.254 18.165 40.803 1.00142.38 C ANISOU 104 CA ILE A 21 17484 17241 19375 -939 -1003 -1424 C ATOM 105 C ILE A 21 27.846 18.538 41.249 1.00141.87 C ANISOU 105 C ILE A 21 17413 17167 19325 -1016 -857 -1429 C ATOM 106 O ILE A 21 26.908 18.506 40.454 1.00145.75 O ANISOU 106 O ILE A 21 17823 17658 19898 -942 -830 -1417 O ATOM 107 CB ILE A 21 29.775 17.012 41.680 1.00141.39 C ANISOU 107 CB ILE A 21 17446 17088 19190 -1040 -1164 -1382 C ATOM 108 CG1 ILE A 21 31.136 16.531 41.175 1.00144.29 C ANISOU 108 CG1 ILE A 21 17787 17441 19597 -947 -1307 -1366 C ATOM 109 CG2 ILE A 21 28.780 15.862 41.690 1.00129.49 C ANISOU 109 CG2 ILE A 21 15952 15549 17700 -1068 -1235 -1352 C ATOM 110 CD1 ILE A 21 31.717 15.393 41.984 1.00143.52 C ANISOU 110 CD1 ILE A 21 17750 17299 19485 -1034 -1484 -1299 C ATOM 111 N LEU A 22 27.707 18.901 42.520 1.00138.37 N ANISOU 111 N LEU A 22 17055 16714 18806 -1174 -760 -1445 N ATOM 112 CA LEU A 22 26.413 19.279 43.078 1.00133.00 C ANISOU 112 CA LEU A 22 16371 16012 18152 -1260 -581 -1462 C ATOM 113 C LEU A 22 25.679 20.257 42.168 1.00134.80 C ANISOU 113 C LEU A 22 16462 16230 18527 -1139 -436 -1472 C ATOM 114 O LEU A 22 24.496 20.082 41.879 1.00131.85 O ANISOU 114 O LEU A 22 16007 15836 18253 -1120 -387 -1443 O ATOM 115 CB LEU A 22 26.587 19.897 44.467 1.00121.40 C ANISOU 115 CB LEU A 22 15026 14535 16567 -1446 -445 -1510 C ATOM 116 CG LEU A 22 27.337 19.065 45.508 1.00112.60 C ANISOU 116 CG LEU A 22 14059 13436 15288 -1604 -597 -1477 C ATOM 117 CD1 LEU A 22 27.347 19.783 46.847 1.00110.01 C ANISOU 117 CD1 LEU A 22 13871 13108 14819 -1817 -440 -1534 C ATOM 118 CD2 LEU A 22 26.720 17.683 45.643 1.00105.38 C ANISOU 118 CD2 LEU A 22 13162 12508 14369 -1639 -726 -1409 C ATOM 119 N GLY A 23 26.391 21.285 41.720 1.00133.46 N ANISOU 119 N GLY A 23 16257 16069 18383 -1064 -378 -1498 N ATOM 120 CA GLY A 23 25.810 22.309 40.873 1.00133.79 C ANISOU 120 CA GLY A 23 16167 16095 18571 -953 -249 -1486 C ATOM 121 C GLY A 23 25.179 21.767 39.606 1.00133.99 C ANISOU 121 C GLY A 23 16084 16142 18685 -829 -365 -1417 C ATOM 122 O GLY A 23 23.967 21.865 39.418 1.00125.25 O ANISOU 122 O GLY A 23 14883 15008 17697 -822 -297 -1376 O ATOM 123 N ASN A 24 26.001 21.193 38.733 1.00135.68 N ANISOU 123 N ASN A 24 16308 16401 18845 -741 -536 -1404 N ATOM 124 CA ASN A 24 25.525 20.703 37.443 1.00129.80 C ANISOU 124 CA ASN A 24 15488 15683 18146 -641 -652 -1353 C ATOM 125 C ASN A 24 24.652 19.455 37.540 1.00118.65 C ANISOU 125 C ASN A 24 14088 14260 16735 -691 -762 -1329 C ATOM 126 O ASN A 24 23.812 19.212 36.675 1.00112.41 O ANISOU 126 O ASN A 24 13220 13480 16009 -650 -823 -1278 O ATOM 127 CB ASN A 24 26.697 20.461 36.492 1.00131.28 C ANISOU 127 CB ASN A 24 15701 15914 18267 -544 -769 -1369 C ATOM 128 CG ASN A 24 27.357 21.748 36.046 1.00134.23 C ANISOU 128 CG ASN A 24 16030 16305 18667 -476 -667 -1367 C ATOM 129 OD1 ASN A 24 26.704 22.638 35.500 1.00129.31 O ANISOU 129 OD1 ASN A 24 15314 15681 18135 -433 -584 -1316 O ATOM 130 ND2 ASN A 24 28.662 21.852 36.272 1.00140.26 N ANISOU 130 ND2 ASN A 24 16846 17076 19369 -469 -680 -1410 N ATOM 131 N VAL A 25 24.855 18.664 38.587 1.00118.53 N ANISOU 131 N VAL A 25 14170 14220 16645 -794 -798 -1355 N ATOM 132 CA VAL A 25 24.004 17.505 38.826 1.00124.33 C ANISOU 132 CA VAL A 25 14920 14933 17389 -859 -887 -1328 C ATOM 133 C VAL A 25 22.600 17.972 39.188 1.00137.51 C ANISOU 133 C VAL A 25 16502 16575 19171 -915 -743 -1292 C ATOM 134 O VAL A 25 21.606 17.381 38.764 1.00144.79 O ANISOU 134 O VAL A 25 17358 17490 20168 -918 -807 -1244 O ATOM 135 CB VAL A 25 24.558 16.607 39.948 1.00126.02 C ANISOU 135 CB VAL A 25 15259 15122 17501 -970 -957 -1343 C ATOM 136 CG1 VAL A 25 23.492 15.641 40.435 1.00119.86 C ANISOU 136 CG1 VAL A 25 14490 14308 16742 -1067 -993 -1306 C ATOM 137 CG2 VAL A 25 25.787 15.854 39.462 1.00135.00 C ANISOU 137 CG2 VAL A 25 16448 16261 18585 -902 -1126 -1359 C ATOM 138 N LEU A 26 22.527 19.045 39.969 1.00139.74 N ANISOU 138 N LEU A 26 16779 16836 19479 -963 -540 -1320 N ATOM 139 CA LEU A 26 21.250 19.636 40.347 1.00134.15 C ANISOU 139 CA LEU A 26 15972 16083 18916 -1007 -354 -1296 C ATOM 140 C LEU A 26 20.524 20.149 39.109 1.00125.11 C ANISOU 140 C LEU A 26 14655 14941 17941 -888 -369 -1219 C ATOM 141 O LEU A 26 19.300 20.076 39.019 1.00120.38 O ANISOU 141 O LEU A 26 13936 14309 17492 -904 -329 -1156 O ATOM 142 CB LEU A 26 21.468 20.779 41.339 1.00130.54 C ANISOU 142 CB LEU A 26 15557 15589 18455 -1076 -113 -1364 C ATOM 143 CG LEU A 26 20.226 21.362 42.013 1.00120.76 C ANISOU 143 CG LEU A 26 14239 14279 17367 -1147 137 -1369 C ATOM 144 CD1 LEU A 26 19.498 20.288 42.803 1.00117.70 C ANISOU 144 CD1 LEU A 26 13903 13880 16936 -1276 125 -1358 C ATOM 145 CD2 LEU A 26 20.606 22.527 42.913 1.00120.39 C ANISOU 145 CD2 LEU A 26 14260 14186 17296 -1218 383 -1465 C ATOM 146 N VAL A 27 21.292 20.667 38.156 1.00127.60 N ANISOU 146 N VAL A 27 14953 15296 18235 -778 -435 -1211 N ATOM 147 CA VAL A 27 20.738 21.176 36.909 1.00121.95 C ANISOU 147 CA VAL A 27 14092 14595 17648 -677 -479 -1120 C ATOM 148 C VAL A 27 20.185 20.040 36.054 1.00118.02 C ANISOU 148 C VAL A 27 13573 14135 17135 -671 -696 -1062 C ATOM 149 O VAL A 27 19.110 20.160 35.468 1.00121.32 O ANISOU 149 O VAL A 27 13853 14546 17698 -659 -727 -964 O ATOM 150 CB VAL A 27 21.795 21.959 36.106 1.00123.84 C ANISOU 150 CB VAL A 27 14343 14875 17835 -578 -497 -1126 C ATOM 151 CG1 VAL A 27 21.253 22.347 34.739 1.00119.45 C ANISOU 151 CG1 VAL A 27 13660 14350 17377 -493 -582 -1012 C ATOM 152 CG2 VAL A 27 22.244 23.190 36.880 1.00128.27 C ANISOU 152 CG2 VAL A 27 14911 15387 18438 -589 -280 -1177 C ATOM 153 N CYS A 28 20.923 18.937 35.990 1.00120.06 N ANISOU 153 N CYS A 28 13963 14423 17232 -686 -848 -1121 N ATOM 154 CA CYS A 28 20.498 17.775 35.219 1.00126.63 C ANISOU 154 CA CYS A 28 14804 15277 18033 -695 -1048 -1094 C ATOM 155 C CYS A 28 19.240 17.144 35.809 1.00127.85 C ANISOU 155 C CYS A 28 14901 15388 18289 -790 -1047 -1049 C ATOM 156 O CYS A 28 18.481 16.474 35.108 1.00125.79 O ANISOU 156 O CYS A 28 14591 15137 18066 -808 -1191 -994 O ATOM 157 CB CYS A 28 21.620 16.737 35.148 1.00130.94 C ANISOU 157 CB CYS A 28 15501 15833 18416 -689 -1177 -1179 C ATOM 158 SG CYS A 28 23.085 17.278 34.239 1.00127.79 S ANISOU 158 SG CYS A 28 15156 15486 17913 -575 -1192 -1230 S ATOM 159 N TRP A 29 19.026 17.363 37.102 1.00132.65 N ANISOU 159 N TRP A 29 15522 15949 18931 -865 -881 -1073 N ATOM 160 CA TRP A 29 17.868 16.810 37.793 1.00145.19 C ANISOU 160 CA TRP A 29 17058 17491 20616 -967 -840 -1035 C ATOM 161 C TRP A 29 16.619 17.645 37.523 1.00134.24 C ANISOU 161 C TRP A 29 15469 16076 19462 -949 -728 -939 C ATOM 162 O TRP A 29 15.542 17.104 37.272 1.00131.41 O ANISOU 162 O TRP A 29 15006 15701 19222 -989 -801 -861 O ATOM 163 CB TRP A 29 18.138 16.732 39.297 1.00161.95 C ANISOU 163 CB TRP A 29 19291 19578 22664 -1075 -689 -1099 C ATOM 164 CG TRP A 29 17.135 15.918 40.054 1.00174.66 C ANISOU 164 CG TRP A 29 20889 21147 24326 -1196 -664 -1068 C ATOM 165 CD1 TRP A 29 16.004 15.339 39.557 1.00177.20 C ANISOU 165 CD1 TRP A 29 21093 21455 24782 -1213 -749 -988 C ATOM 166 CD2 TRP A 29 17.173 15.592 41.449 1.00183.44 C ANISOU 166 CD2 TRP A 29 22117 22232 25352 -1335 -548 -1108 C ATOM 167 NE1 TRP A 29 15.336 14.672 40.555 1.00181.89 N ANISOU 167 NE1 TRP A 29 21710 22007 25392 -1343 -681 -978 N ATOM 168 CE2 TRP A 29 16.033 14.813 41.726 1.00188.42 C ANISOU 168 CE2 TRP A 29 22687 22828 26075 -1423 -554 -1050 C ATOM 169 CE3 TRP A 29 18.061 15.883 42.489 1.00184.51 C ANISOU 169 CE3 TRP A 29 22405 22371 25329 -1409 -448 -1179 C ATOM 170 CZ2 TRP A 29 15.757 14.321 43.001 1.00195.32 C ANISOU 170 CZ2 TRP A 29 23656 23674 26884 -1579 -449 -1062 C ATOM 171 CZ3 TRP A 29 17.785 15.395 43.753 1.00189.18 C ANISOU 171 CZ3 TRP A 29 23099 22939 25841 -1575 -360 -1188 C ATOM 172 CH2 TRP A 29 16.643 14.622 43.998 1.00196.25 C ANISOU 172 CH2 TRP A 29 23938 23803 26826 -1657 -353 -1130 C ATOM 173 N ALA A 30 16.771 18.964 37.574 1.00121.34 N ANISOU 173 N ALA A 30 13766 14423 17913 -891 -554 -938 N ATOM 174 CA ALA A 30 15.658 19.877 37.341 1.00109.20 C ANISOU 174 CA ALA A 30 12016 12836 16642 -859 -428 -837 C ATOM 175 C ALA A 30 15.124 19.757 35.917 1.00119.22 C ANISOU 175 C ALA A 30 13155 14147 17996 -798 -644 -706 C ATOM 176 O ALA A 30 13.936 19.960 35.672 1.00126.97 O ANISOU 176 O ALA A 30 13944 15090 19210 -805 -634 -585 O ATOM 177 CB ALA A 30 16.076 21.309 37.633 1.00 94.84 C ANISOU 177 CB ALA A 30 10165 10974 14895 -804 -204 -871 C ATOM 178 N VAL A 31 16.007 19.430 34.979 1.00122.78 N ANISOU 178 N VAL A 31 13713 14677 18262 -748 -838 -726 N ATOM 179 CA VAL A 31 15.608 19.231 33.591 1.00129.58 C ANISOU 179 CA VAL A 31 14499 15594 19140 -719 -1061 -616 C ATOM 180 C VAL A 31 14.809 17.940 33.453 1.00135.07 C ANISOU 180 C VAL A 31 15192 16295 19833 -809 -1237 -587 C ATOM 181 O VAL A 31 14.018 17.783 32.524 1.00139.82 O ANISOU 181 O VAL A 31 15686 16924 20516 -827 -1404 -468 O ATOM 182 CB VAL A 31 16.830 19.182 32.653 1.00136.77 C ANISOU 182 CB VAL A 31 15552 16586 19827 -657 -1190 -671 C ATOM 183 CG1 VAL A 31 16.405 18.842 31.231 1.00139.11 C ANISOU 183 CG1 VAL A 31 15813 16950 20091 -664 -1428 -572 C ATOM 184 CG2 VAL A 31 17.577 20.507 32.686 1.00140.52 C ANISOU 184 CG2 VAL A 31 16013 17056 20323 -572 -1030 -681 C ATOM 185 N TRP A 32 15.015 17.021 34.390 1.00137.70 N ANISOU 185 N TRP A 32 15646 16599 20074 -878 -1208 -687 N ATOM 186 CA TRP A 32 14.327 15.737 34.365 1.00146.11 C ANISOU 186 CA TRP A 32 16723 17654 21136 -971 -1363 -670 C ATOM 187 C TRP A 32 12.953 15.841 35.020 1.00153.20 C ANISOU 187 C TRP A 32 17440 18489 22281 -1039 -1252 -575 C ATOM 188 O TRP A 32 11.961 15.345 34.485 1.00163.20 O ANISOU 188 O TRP A 32 18591 19754 23663 -1091 -1397 -474 O ATOM 189 CB TRP A 32 15.173 14.667 35.058 1.00148.00 C ANISOU 189 CB TRP A 32 17167 17881 21185 -1016 -1392 -799 C ATOM 190 CG TRP A 32 14.727 13.264 34.778 1.00152.67 C ANISOU 190 CG TRP A 32 17806 18460 21741 -1098 -1590 -797 C ATOM 191 CD1 TRP A 32 14.508 12.704 33.553 1.00150.73 C ANISOU 191 CD1 TRP A 32 17566 18252 21455 -1105 -1811 -772 C ATOM 192 CD2 TRP A 32 14.467 12.235 35.741 1.00162.87 C ANISOU 192 CD2 TRP A 32 19161 19696 23027 -1198 -1585 -825 C ATOM 193 NE1 TRP A 32 14.117 11.394 33.693 1.00156.04 N ANISOU 193 NE1 TRP A 32 18296 18883 22110 -1200 -1940 -792 N ATOM 194 CE2 TRP A 32 14.085 11.081 35.027 1.00165.20 C ANISOU 194 CE2 TRP A 32 19486 19984 23300 -1253 -1806 -816 C ATOM 195 CE3 TRP A 32 14.515 12.178 37.138 1.00170.68 C ANISOU 195 CE3 TRP A 32 20196 20639 24017 -1262 -1415 -854 C ATOM 196 CZ2 TRP A 32 13.754 9.885 35.662 1.00174.29 C ANISOU 196 CZ2 TRP A 32 20695 21074 24452 -1356 -1862 -829 C ATOM 197 CZ3 TRP A 32 14.186 10.990 37.766 1.00177.42 C ANISOU 197 CZ3 TRP A 32 21113 21444 24855 -1370 -1476 -855 C ATOM 198 CH2 TRP A 32 13.810 9.860 37.028 1.00178.51 C ANISOU 198 CH2 TRP A 32 21264 21567 24995 -1409 -1697 -839 C ATOM 199 N LEU A 33 12.900 16.493 36.177 1.00148.82 N ANISOU 199 N LEU A 33 16859 17876 21808 -1048 -987 -612 N ATOM 200 CA LEU A 33 11.646 16.669 36.902 1.00149.49 C ANISOU 200 CA LEU A 33 16773 17888 22141 -1112 -820 -541 C ATOM 201 C LEU A 33 10.696 17.604 36.160 1.00158.92 C ANISOU 201 C LEU A 33 17705 19056 23620 -1052 -806 -385 C ATOM 202 O LEU A 33 9.647 17.183 35.674 1.00167.38 O ANISOU 202 O LEU A 33 18619 20120 24857 -1094 -939 -259 O ATOM 203 CB LEU A 33 11.908 17.208 38.310 1.00134.32 C ANISOU 203 CB LEU A 33 14918 15909 20210 -1149 -511 -641 C ATOM 204 CG LEU A 33 12.727 16.326 39.253 1.00118.98 C ANISOU 204 CG LEU A 33 13215 13981 18010 -1237 -512 -763 C ATOM 205 CD1 LEU A 33 12.867 16.990 40.615 1.00113.48 C ANISOU 205 CD1 LEU A 33 12582 13235 17301 -1301 -203 -849 C ATOM 206 CD2 LEU A 33 12.093 14.951 39.389 1.00116.84 C ANISOU 206 CD2 LEU A 33 12961 13702 17730 -1340 -659 -727 C ATOM 207 N ASN A 34 11.074 18.876 36.079 1.00150.95 N ANISOU 207 N ASN A 34 16643 18028 22681 -959 -655 -382 N ATOM 208 CA ASN A 34 10.248 19.891 35.438 1.00143.45 C ANISOU 208 CA ASN A 34 15435 17035 22033 -892 -624 -219 C ATOM 209 C ASN A 34 10.289 19.792 33.915 1.00140.90 C ANISOU 209 C ASN A 34 15075 16800 21661 -854 -940 -94 C ATOM 210 O ASN A 34 11.321 20.041 33.296 1.00135.84 O ANISOU 210 O ASN A 34 14572 16229 20813 -795 -1026 -143 O ATOM 211 CB ASN A 34 10.685 21.285 35.894 1.00140.35 C ANISOU 211 CB ASN A 34 15012 16576 21737 -811 -347 -265 C ATOM 212 CG ASN A 34 9.731 22.372 35.446 1.00146.80 C ANISOU 212 CG ASN A 34 15534 17308 22934 -742 -264 -89 C ATOM 213 OD1 ASN A 34 8.800 22.121 34.683 1.00157.41 O ANISOU 213 OD1 ASN A 34 16691 18660 24458 -752 -450 87 O ATOM 214 ND2 ASN A 34 9.958 23.590 35.924 1.00145.03 N ANISOU 214 ND2 ASN A 34 15262 16995 22849 -677 11 -130 N ATOM 215 N SER A 35 9.159 19.431 33.316 1.00149.70 N ANISOU 215 N SER A 35 16006 17913 22961 -901 -1110 69 N ATOM 216 CA SER A 35 9.074 19.269 31.868 1.00153.14 C ANISOU 216 CA SER A 35 16416 18438 23333 -903 -1430 199 C ATOM 217 C SER A 35 8.953 20.607 31.145 1.00151.37 C ANISOU 217 C SER A 35 16018 18202 23294 -812 -1419 360 C ATOM 218 O SER A 35 8.857 20.653 29.919 1.00150.21 O ANISOU 218 O SER A 35 15840 18132 23100 -822 -1679 496 O ATOM 219 CB SER A 35 7.899 18.361 31.497 1.00156.88 C ANISOU 219 CB SER A 35 16761 18917 23931 -1013 -1645 326 C ATOM 220 OG SER A 35 6.680 18.873 32.006 1.00165.01 O ANISOU 220 OG SER A 35 17499 19840 25358 -1016 -1494 467 O ATOM 221 N ASN A 36 8.955 21.693 31.912 1.00149.04 N ANISOU 221 N ASN A 36 15619 17803 23206 -734 -1117 346 N ATOM 222 CA ASN A 36 8.914 23.034 31.340 1.00143.91 C ANISOU 222 CA ASN A 36 14805 17115 22758 -637 -1071 491 C ATOM 223 C ASN A 36 10.311 23.534 30.999 1.00143.65 C ANISOU 223 C ASN A 36 14982 17149 22450 -568 -1058 383 C ATOM 224 O ASN A 36 10.485 24.665 30.544 1.00144.79 O ANISOU 224 O ASN A 36 15031 17265 22719 -486 -1011 484 O ATOM 225 CB ASN A 36 8.227 24.008 32.298 1.00135.72 C ANISOU 225 CB ASN A 36 13547 15911 22111 -585 -729 521 C ATOM 226 CG ASN A 36 6.738 23.759 32.412 1.00126.05 C ANISOU 226 CG ASN A 36 12039 14606 21248 -635 -743 688 C ATOM 227 OD1 ASN A 36 6.046 23.599 31.408 1.00132.99 O ANISOU 227 OD1 ASN A 36 12758 15527 22247 -662 -1022 903 O ATOM 228 ND2 ASN A 36 6.234 23.733 33.641 1.00113.90 N ANISOU 228 ND2 ASN A 36 10436 12953 19886 -660 -439 593 N ATOM 229 N LEU A 37 11.304 22.682 31.228 1.00140.48 N ANISOU 229 N LEU A 37 14855 16827 21695 -601 -1099 187 N ATOM 230 CA LEU A 37 12.692 23.015 30.938 1.00132.84 C ANISOU 230 CA LEU A 37 14088 15924 20460 -543 -1090 73 C ATOM 231 C LEU A 37 13.268 22.038 29.923 1.00137.84 C ANISOU 231 C LEU A 37 14906 16691 20777 -586 -1376 41 C ATOM 232 O LEU A 37 14.448 22.106 29.585 1.00142.53 O ANISOU 232 O LEU A 37 15677 17349 21130 -547 -1389 -60 O ATOM 233 CB LEU A 37 13.526 22.981 32.219 1.00117.55 C ANISOU 233 CB LEU A 37 12315 13945 18405 -539 -845 -144 C ATOM 234 CG LEU A 37 13.121 23.953 33.328 1.00112.81 C ANISOU 234 CG LEU A 37 11590 13209 18064 -515 -517 -167 C ATOM 235 CD1 LEU A 37 13.840 23.622 34.628 1.00 98.22 C ANISOU 235 CD1 LEU A 37 9938 11340 16043 -564 -327 -381 C ATOM 236 CD2 LEU A 37 13.391 25.390 32.908 1.00109.57 C ANISOU 236 CD2 LEU A 37 11075 12750 17805 -416 -410 -87 C ATOM 237 N GLN A 38 12.428 21.129 29.438 1.00139.43 N ANISOU 237 N GLN A 38 15063 16928 20988 -673 -1594 122 N ATOM 238 CA GLN A 38 12.878 20.089 28.519 1.00140.62 C ANISOU 238 CA GLN A 38 15402 17188 20841 -737 -1850 68 C ATOM 239 C GLN A 38 12.758 20.510 27.059 1.00141.17 C ANISOU 239 C GLN A 38 15435 17346 20859 -750 -2072 232 C ATOM 240 O GLN A 38 12.489 19.683 26.189 1.00137.57 O ANISOU 240 O GLN A 38 15050 16966 20255 -847 -2323 263 O ATOM 241 CB GLN A 38 12.101 18.793 28.755 1.00138.88 C ANISOU 241 CB GLN A 38 15188 16957 20624 -847 -1980 48 C ATOM 242 CG GLN A 38 12.238 18.240 30.160 1.00139.84 C ANISOU 242 CG GLN A 38 15373 17002 20757 -859 -1787 -105 C ATOM 243 CD GLN A 38 11.566 16.893 30.321 1.00143.76 C ANISOU 243 CD GLN A 38 15897 17490 21237 -973 -1929 -124 C ATOM 244 OE1 GLN A 38 11.091 16.303 29.351 1.00146.30 O ANISOU 244 OE1 GLN A 38 16213 17863 21510 -1048 -2180 -49 O ATOM 245 NE2 GLN A 38 11.524 16.396 31.552 1.00143.36 N ANISOU 245 NE2 GLN A 38 15884 17371 21216 -1003 -1772 -223 N ATOM 246 N ASN A 39 12.957 21.797 26.796 1.00145.66 N ANISOU 246 N ASN A 39 15901 17901 21541 -667 -1981 339 N ATOM 247 CA ASN A 39 12.936 22.300 25.428 1.00155.33 C ANISOU 247 CA ASN A 39 17103 19214 22700 -685 -2183 512 C ATOM 248 C ASN A 39 14.248 22.016 24.704 1.00160.47 C ANISOU 248 C ASN A 39 18025 19975 22974 -683 -2239 370 C ATOM 249 O ASN A 39 15.265 21.731 25.336 1.00156.40 O ANISOU 249 O ASN A 39 17671 19446 22310 -632 -2082 158 O ATOM 250 CB ASN A 39 12.613 23.796 25.404 1.00157.80 C ANISOU 250 CB ASN A 39 17191 19456 23310 -598 -2067 703 C ATOM 251 CG ASN A 39 13.484 24.599 26.350 1.00156.49 C ANISOU 251 CG ASN A 39 17062 19209 23188 -482 -1751 560 C ATOM 252 OD1 ASN A 39 14.552 24.149 26.761 1.00156.77 O ANISOU 252 OD1 ASN A 39 17314 19275 22977 -466 -1660 340 O ATOM 253 ND2 ASN A 39 13.030 25.797 26.699 1.00158.75 N ANISOU 253 ND2 ASN A 39 17131 19381 23804 -407 -1585 688 N ATOM 254 N VAL A 40 14.219 22.091 23.377 1.00165.77 N ANISOU 254 N VAL A 40 18741 20752 23494 -749 -2462 495 N ATOM 255 CA VAL A 40 15.390 21.776 22.563 1.00163.97 C ANISOU 255 CA VAL A 40 18770 20631 22902 -765 -2510 364 C ATOM 256 C VAL A 40 16.607 22.598 22.982 1.00165.69 C ANISOU 256 C VAL A 40 19047 20822 23084 -637 -2265 257 C ATOM 257 O VAL A 40 17.746 22.148 22.855 1.00162.90 O ANISOU 257 O VAL A 40 18904 20513 22479 -620 -2209 69 O ATOM 258 CB VAL A 40 15.114 22.002 21.066 1.00164.36 C ANISOU 258 CB VAL A 40 18845 20799 22806 -868 -2763 549 C ATOM 259 CG1 VAL A 40 16.280 21.497 20.234 1.00158.37 C ANISOU 259 CG1 VAL A 40 18376 20147 21650 -906 -2791 380 C ATOM 260 CG2 VAL A 40 13.826 21.308 20.655 1.00171.64 C ANISOU 260 CG2 VAL A 40 19678 21743 23793 -1011 -3029 688 C ATOM 261 N THR A 41 16.355 23.801 23.487 1.00168.13 N ANISOU 261 N THR A 41 19164 21048 23668 -550 -2114 378 N ATOM 262 CA THR A 41 17.423 24.688 23.934 1.00160.23 C ANISOU 262 CA THR A 41 18201 20010 22669 -439 -1882 292 C ATOM 263 C THR A 41 18.231 24.064 25.066 1.00142.13 C ANISOU 263 C THR A 41 16040 17671 20291 -401 -1706 35 C ATOM 264 O THR A 41 19.458 24.024 25.013 1.00141.72 O ANISOU 264 O THR A 41 16147 17655 20045 -362 -1628 -107 O ATOM 265 CB THR A 41 16.865 26.039 24.418 1.00168.15 C ANISOU 265 CB THR A 41 18963 20900 24027 -362 -1732 453 C ATOM 266 OG1 THR A 41 16.113 26.656 23.365 1.00177.87 O ANISOU 266 OG1 THR A 41 20049 22164 25370 -396 -1913 727 O ATOM 267 CG2 THR A 41 17.998 26.964 24.841 1.00159.59 C ANISOU 267 CG2 THR A 41 17932 19775 22932 -264 -1501 357 C ATOM 268 N ASN A 42 17.534 23.576 26.086 1.00135.67 N ANISOU 268 N ASN A 42 15150 16773 19627 -419 -1647 -10 N ATOM 269 CA ASN A 42 18.191 23.026 27.266 1.00135.00 C ANISOU 269 CA ASN A 42 15176 16637 19480 -401 -1491 -222 C ATOM 270 C ASN A 42 18.775 21.631 27.056 1.00138.65 C ANISOU 270 C ASN A 42 15843 17159 19678 -452 -1612 -380 C ATOM 271 O ASN A 42 19.373 21.062 27.969 1.00138.87 O ANISOU 271 O ASN A 42 15970 17148 19647 -444 -1518 -539 O ATOM 272 CB ASN A 42 17.242 23.032 28.467 1.00138.69 C ANISOU 272 CB ASN A 42 15504 16996 20196 -417 -1364 -212 C ATOM 273 CG ASN A 42 16.888 24.435 28.922 1.00150.35 C ANISOU 273 CG ASN A 42 16799 18377 21949 -353 -1164 -114 C ATOM 274 OD1 ASN A 42 17.310 25.421 28.317 1.00154.18 O ANISOU 274 OD1 ASN A 42 17252 18876 22455 -294 -1141 -35 O ATOM 275 ND2 ASN A 42 16.111 24.531 29.995 1.00155.98 N ANISOU 275 ND2 ASN A 42 17396 18985 22883 -368 -1005 -123 N ATOM 276 N TYR A 43 18.602 21.082 25.859 1.00142.14 N ANISOU 276 N TYR A 43 16352 17688 19967 -513 -1822 -334 N ATOM 277 CA TYR A 43 19.232 19.811 25.521 1.00144.89 C ANISOU 277 CA TYR A 43 16904 18078 20069 -558 -1918 -497 C ATOM 278 C TYR A 43 20.744 19.982 25.480 1.00145.03 C ANISOU 278 C TYR A 43 17064 18116 19926 -483 -1795 -639 C ATOM 279 O TYR A 43 21.492 19.118 25.936 1.00147.07 O ANISOU 279 O TYR A 43 17448 18346 20086 -473 -1758 -806 O ATOM 280 CB TYR A 43 18.717 19.278 24.182 1.00150.62 C ANISOU 280 CB TYR A 43 17688 18893 20650 -660 -2156 -425 C ATOM 281 CG TYR A 43 17.452 18.457 24.294 1.00154.14 C ANISOU 281 CG TYR A 43 18061 19314 21191 -763 -2315 -363 C ATOM 282 CD1 TYR A 43 17.508 17.075 24.420 1.00154.54 C ANISOU 282 CD1 TYR A 43 18250 19346 21123 -829 -2393 -512 C ATOM 283 CD2 TYR A 43 16.204 19.062 24.277 1.00152.77 C ANISOU 283 CD2 TYR A 43 17669 19125 21252 -794 -2384 -149 C ATOM 284 CE1 TYR A 43 16.356 16.319 24.524 1.00155.37 C ANISOU 284 CE1 TYR A 43 18288 19425 21322 -932 -2540 -453 C ATOM 285 CE2 TYR A 43 15.046 18.315 24.380 1.00159.55 C ANISOU 285 CE2 TYR A 43 18444 19959 22217 -893 -2530 -83 C ATOM 286 CZ TYR A 43 15.128 16.944 24.504 1.00164.42 C ANISOU 286 CZ TYR A 43 19212 20565 22694 -966 -2609 -238 C ATOM 287 OH TYR A 43 13.977 16.197 24.607 1.00174.51 O ANISOU 287 OH TYR A 43 20406 21817 24085 -1073 -2756 -170 O ATOM 288 N PHE A 44 21.184 21.110 24.932 1.00140.91 N ANISOU 288 N PHE A 44 16507 17634 19397 -430 -1734 -558 N ATOM 289 CA PHE A 44 22.602 21.441 24.880 1.00128.44 C ANISOU 289 CA PHE A 44 15032 16071 17698 -358 -1604 -669 C ATOM 290 C PHE A 44 23.112 21.812 26.267 1.00130.87 C ANISOU 290 C PHE A 44 15299 16291 18135 -293 -1416 -749 C ATOM 291 O PHE A 44 24.238 21.477 26.634 1.00142.20 O ANISOU 291 O PHE A 44 16837 17714 19481 -256 -1339 -890 O ATOM 292 CB PHE A 44 22.848 22.588 23.899 1.00124.15 C ANISOU 292 CB PHE A 44 14455 15594 17122 -333 -1595 -539 C ATOM 293 CG PHE A 44 22.389 22.297 22.498 1.00135.06 C ANISOU 293 CG PHE A 44 15899 17078 18341 -424 -1790 -447 C ATOM 294 CD1 PHE A 44 21.136 22.701 22.066 1.00147.06 C ANISOU 294 CD1 PHE A 44 17282 18615 19978 -484 -1935 -236 C ATOM 295 CD2 PHE A 44 23.208 21.616 21.614 1.00139.32 C ANISOU 295 CD2 PHE A 44 16633 17691 18613 -459 -1827 -570 C ATOM 296 CE1 PHE A 44 20.710 22.433 20.778 1.00151.93 C ANISOU 296 CE1 PHE A 44 17967 19336 20423 -594 -2141 -138 C ATOM 297 CE2 PHE A 44 22.789 21.345 20.324 1.00146.47 C ANISOU 297 CE2 PHE A 44 17623 18696 19331 -570 -2002 -497 C ATOM 298 CZ PHE A 44 21.538 21.754 19.906 1.00151.28 C ANISOU 298 CZ PHE A 44 18109 19337 20035 -646 -2174 -276 C ATOM 299 N VAL A 45 22.277 22.504 27.035 1.00124.30 N ANISOU 299 N VAL A 45 14315 15393 17520 -288 -1340 -656 N ATOM 300 CA VAL A 45 22.625 22.882 28.400 1.00125.16 C ANISOU 300 CA VAL A 45 14399 15417 17738 -258 -1156 -734 C ATOM 301 C VAL A 45 22.987 21.652 29.227 1.00132.46 C ANISOU 301 C VAL A 45 15438 16314 18576 -295 -1174 -884 C ATOM 302 O VAL A 45 23.895 21.696 30.058 1.00137.93 O ANISOU 302 O VAL A 45 16192 16975 19240 -276 -1068 -985 O ATOM 303 CB VAL A 45 21.475 23.645 29.087 1.00118.99 C ANISOU 303 CB VAL A 45 13443 14557 17212 -267 -1060 -627 C ATOM 304 CG1 VAL A 45 21.791 23.879 30.557 1.00112.60 C ANISOU 304 CG1 VAL A 45 12648 13662 16472 -271 -866 -735 C ATOM 305 CG2 VAL A 45 21.215 24.963 28.374 1.00120.12 C ANISOU 305 CG2 VAL A 45 13456 14699 17485 -219 -1026 -467 C ATOM 306 N VAL A 46 22.274 20.555 28.992 1.00132.61 N ANISOU 306 N VAL A 46 15483 16343 18559 -356 -1320 -884 N ATOM 307 CA VAL A 46 22.560 19.298 29.673 1.00134.55 C ANISOU 307 CA VAL A 46 15835 16554 18733 -395 -1359 -1007 C ATOM 308 C VAL A 46 23.949 18.788 29.295 1.00132.98 C ANISOU 308 C VAL A 46 15779 16378 18370 -353 -1373 -1130 C ATOM 309 O VAL A 46 24.689 18.290 30.144 1.00133.55 O ANISOU 309 O VAL A 46 15916 16403 18423 -349 -1331 -1224 O ATOM 310 CB VAL A 46 21.511 18.221 29.340 1.00138.74 C ANISOU 310 CB VAL A 46 16366 17086 19264 -475 -1523 -979 C ATOM 311 CG1 VAL A 46 21.874 16.902 30.004 1.00140.86 C ANISOU 311 CG1 VAL A 46 16749 17304 19468 -513 -1565 -1100 C ATOM 312 CG2 VAL A 46 20.130 18.678 29.774 1.00136.45 C ANISOU 312 CG2 VAL A 46 15909 16760 19173 -516 -1499 -850 C ATOM 313 N SER A 47 24.296 18.915 28.018 1.00133.49 N ANISOU 313 N SER A 47 15886 16512 18323 -329 -1431 -1121 N ATOM 314 CA SER A 47 25.624 18.542 27.545 1.00136.63 C ANISOU 314 CA SER A 47 16401 16926 18584 -282 -1409 -1237 C ATOM 315 C SER A 47 26.682 19.388 28.242 1.00138.86 C ANISOU 315 C SER A 47 16660 17187 18914 -215 -1256 -1263 C ATOM 316 O SER A 47 27.742 18.890 28.621 1.00140.28 O ANISOU 316 O SER A 47 16904 17333 19063 -186 -1224 -1364 O ATOM 317 CB SER A 47 25.725 18.718 26.029 1.00140.08 C ANISOU 317 CB SER A 47 16892 17451 18883 -285 -1468 -1212 C ATOM 318 OG SER A 47 27.045 18.481 25.572 1.00143.18 O ANISOU 318 OG SER A 47 17385 17853 19163 -234 -1403 -1328 O ATOM 319 N LEU A 48 26.383 20.673 28.406 1.00138.09 N ANISOU 319 N LEU A 48 16460 17099 18909 -197 -1167 -1165 N ATOM 320 CA LEU A 48 27.261 21.585 29.125 1.00136.37 C ANISOU 320 CA LEU A 48 16214 16853 18747 -154 -1022 -1185 C ATOM 321 C LEU A 48 27.374 21.168 30.586 1.00134.13 C ANISOU 321 C LEU A 48 15947 16497 18517 -194 -983 -1249 C ATOM 322 O LEU A 48 28.434 21.290 31.197 1.00135.04 O ANISOU 322 O LEU A 48 16098 16591 18621 -179 -922 -1311 O ATOM 323 CB LEU A 48 26.729 23.015 29.034 1.00138.45 C ANISOU 323 CB LEU A 48 16362 17117 19127 -137 -931 -1065 C ATOM 324 CG LEU A 48 27.437 24.069 29.887 1.00143.49 C ANISOU 324 CG LEU A 48 16966 17708 19844 -113 -768 -1086 C ATOM 325 CD1 LEU A 48 28.883 24.239 29.446 1.00142.13 C ANISOU 325 CD1 LEU A 48 16854 17571 19578 -63 -735 -1144 C ATOM 326 CD2 LEU A 48 26.694 25.393 29.819 1.00152.83 C ANISOU 326 CD2 LEU A 48 18024 18862 21182 -100 -674 -967 C ATOM 327 N ALA A 49 26.271 20.676 31.139 1.00132.71 N ANISOU 327 N ALA A 49 15743 16285 18396 -256 -1024 -1223 N ATOM 328 CA ALA A 49 26.245 20.227 32.525 1.00128.62 C ANISOU 328 CA ALA A 49 15255 15706 17908 -319 -991 -1271 C ATOM 329 C ALA A 49 27.071 18.959 32.699 1.00123.58 C ANISOU 329 C ALA A 49 14722 15051 17183 -326 -1091 -1356 C ATOM 330 O ALA A 49 27.980 18.914 33.524 1.00126.82 O ANISOU 330 O ALA A 49 15174 15432 17580 -337 -1058 -1401 O ATOM 331 CB ALA A 49 24.815 19.999 32.982 1.00130.39 C ANISOU 331 CB ALA A 49 15420 15900 18224 -387 -999 -1215 C ATOM 332 N ALA A 50 26.750 17.934 31.917 1.00119.98 N ANISOU 332 N ALA A 50 14305 14604 16679 -325 -1216 -1373 N ATOM 333 CA ALA A 50 27.474 16.668 31.973 1.00122.01 C ANISOU 333 CA ALA A 50 14652 14820 16888 -323 -1304 -1455 C ATOM 334 C ALA A 50 28.973 16.887 31.805 1.00128.41 C ANISOU 334 C ALA A 50 15489 15631 17671 -251 -1255 -1511 C ATOM 335 O ALA A 50 29.780 16.315 32.538 1.00128.66 O ANISOU 335 O ALA A 50 15553 15608 17725 -256 -1276 -1547 O ATOM 336 CB ALA A 50 26.955 15.712 30.910 1.00122.30 C ANISOU 336 CB ALA A 50 14733 14865 16870 -331 -1423 -1481 C ATOM 337 N ALA A 51 29.338 17.720 30.837 1.00128.48 N ANISOU 337 N ALA A 51 15474 15699 17643 -189 -1194 -1502 N ATOM 338 CA ALA A 51 30.738 18.047 30.598 1.00119.16 C ANISOU 338 CA ALA A 51 14300 14523 16452 -120 -1127 -1547 C ATOM 339 C ALA A 51 31.361 18.672 31.840 1.00122.12 C ANISOU 339 C ALA A 51 14641 14868 16891 -141 -1063 -1529 C ATOM 340 O ALA A 51 32.435 18.264 32.278 1.00133.24 O ANISOU 340 O ALA A 51 16062 16236 18326 -125 -1078 -1565 O ATOM 341 CB ALA A 51 30.868 18.985 29.409 1.00113.59 C ANISOU 341 CB ALA A 51 13573 13894 15693 -70 -1060 -1519 C ATOM 342 N ASP A 52 30.675 19.658 32.408 1.00118.82 N ANISOU 342 N ASP A 52 14176 14463 16506 -184 -993 -1471 N ATOM 343 CA ASP A 52 31.176 20.364 33.582 1.00119.57 C ANISOU 343 CA ASP A 52 14259 14533 16638 -230 -920 -1466 C ATOM 344 C ASP A 52 31.014 19.549 34.863 1.00108.64 C ANISOU 344 C ASP A 52 12927 13097 15253 -325 -984 -1476 C ATOM 345 O ASP A 52 31.406 19.992 35.941 1.00108.43 O ANISOU 345 O ASP A 52 12917 13052 15228 -397 -943 -1475 O ATOM 346 CB ASP A 52 30.490 21.724 33.729 1.00131.37 C ANISOU 346 CB ASP A 52 15694 16040 18181 -247 -794 -1417 C ATOM 347 CG ASP A 52 30.872 22.692 32.627 1.00138.11 C ANISOU 347 CG ASP A 52 16496 16937 19041 -164 -728 -1386 C ATOM 348 OD1 ASP A 52 31.557 22.270 31.671 1.00138.36 O ANISOU 348 OD1 ASP A 52 16548 17003 19020 -101 -773 -1408 O ATOM 349 OD2 ASP A 52 30.490 23.877 32.718 1.00140.36 O ANISOU 349 OD2 ASP A 52 16722 17215 19392 -168 -619 -1340 O ATOM 350 N ILE A 53 30.428 18.363 34.744 1.00105.64 N ANISOU 350 N ILE A 53 12581 12695 14863 -341 -1089 -1483 N ATOM 351 CA ILE A 53 30.351 17.444 35.872 1.00110.73 C ANISOU 351 CA ILE A 53 13281 13287 15504 -433 -1168 -1479 C ATOM 352 C ILE A 53 31.602 16.581 35.896 1.00122.99 C ANISOU 352 C ILE A 53 14859 14797 17073 -398 -1264 -1502 C ATOM 353 O ILE A 53 32.226 16.401 36.940 1.00131.51 O ANISOU 353 O ILE A 53 15965 15845 18160 -466 -1308 -1477 O ATOM 354 CB ILE A 53 29.117 16.531 35.797 1.00108.54 C ANISOU 354 CB ILE A 53 13021 12991 15231 -475 -1238 -1465 C ATOM 355 CG1 ILE A 53 27.838 17.343 35.998 1.00105.38 C ANISOU 355 CG1 ILE A 53 12570 12613 14856 -522 -1138 -1425 C ATOM 356 CG2 ILE A 53 29.205 15.439 36.849 1.00103.09 C ANISOU 356 CG2 ILE A 53 12393 12239 14536 -564 -1335 -1453 C ATOM 357 CD1 ILE A 53 26.572 16.530 35.866 1.00 97.73 C ANISOU 357 CD1 ILE A 53 11593 11628 13913 -567 -1205 -1399 C ATOM 358 N LEU A 54 31.967 16.054 34.731 1.00123.23 N ANISOU 358 N LEU A 54 14882 14822 17116 -299 -1295 -1545 N ATOM 359 CA LEU A 54 33.171 15.245 34.600 1.00119.25 C ANISOU 359 CA LEU A 54 14380 14258 16672 -244 -1357 -1575 C ATOM 360 C LEU A 54 34.407 16.049 34.982 1.00116.71 C ANISOU 360 C LEU A 54 14010 13946 16386 -226 -1309 -1555 C ATOM 361 O LEU A 54 35.471 15.487 35.230 1.00121.19 O ANISOU 361 O LEU A 54 14555 14455 17038 -202 -1368 -1548 O ATOM 362 CB LEU A 54 33.310 14.714 33.173 1.00115.70 C ANISOU 362 CB LEU A 54 13940 13802 16218 -146 -1346 -1649 C ATOM 363 CG LEU A 54 32.222 13.744 32.715 1.00109.52 C ANISOU 363 CG LEU A 54 13213 12996 15403 -174 -1420 -1679 C ATOM 364 CD1 LEU A 54 32.420 13.365 31.255 1.00105.24 C ANISOU 364 CD1 LEU A 54 12705 12459 14822 -101 -1393 -1769 C ATOM 365 CD2 LEU A 54 32.208 12.508 33.600 1.00109.65 C ANISOU 365 CD2 LEU A 54 13260 12910 15490 -227 -1536 -1663 C ATOM 366 N VAL A 55 34.262 17.369 35.020 1.00114.07 N ANISOU 366 N VAL A 55 13652 13679 16012 -240 -1203 -1540 N ATOM 367 CA VAL A 55 35.348 18.236 35.453 1.00122.63 C ANISOU 367 CA VAL A 55 14694 14773 17125 -246 -1157 -1520 C ATOM 368 C VAL A 55 35.652 17.992 36.927 1.00135.03 C ANISOU 368 C VAL A 55 16297 16308 18700 -370 -1245 -1471 C ATOM 369 O VAL A 55 36.800 17.764 37.303 1.00143.03 O ANISOU 369 O VAL A 55 17278 17287 19778 -373 -1315 -1441 O ATOM 370 CB VAL A 55 35.017 19.723 35.231 1.00123.82 C ANISOU 370 CB VAL A 55 14819 14986 17241 -247 -1019 -1514 C ATOM 371 CG1 VAL A 55 36.045 20.606 35.921 1.00125.98 C ANISOU 371 CG1 VAL A 55 15066 15261 17541 -290 -982 -1496 C ATOM 372 CG2 VAL A 55 34.951 20.035 33.743 1.00120.10 C ANISOU 372 CG2 VAL A 55 14315 14558 16759 -135 -949 -1537 C ATOM 373 N GLY A 56 34.615 18.031 37.756 1.00136.64 N ANISOU 373 N GLY A 56 16562 16518 18835 -481 -1243 -1454 N ATOM 374 CA GLY A 56 34.773 17.786 39.178 1.00137.72 C ANISOU 374 CA GLY A 56 16760 16633 18935 -630 -1323 -1405 C ATOM 375 C GLY A 56 34.835 16.306 39.501 1.00135.53 C ANISOU 375 C GLY A 56 16510 16292 18694 -651 -1486 -1363 C ATOM 376 O GLY A 56 34.990 15.920 40.660 1.00139.50 O ANISOU 376 O GLY A 56 17069 16772 19162 -784 -1584 -1300 O ATOM 377 N VAL A 57 34.719 15.475 38.471 1.00127.40 N ANISOU 377 N VAL A 57 15449 15227 17730 -532 -1514 -1397 N ATOM 378 CA VAL A 57 34.723 14.027 38.649 1.00121.84 C ANISOU 378 CA VAL A 57 14766 14440 17089 -538 -1655 -1367 C ATOM 379 C VAL A 57 36.023 13.390 38.158 1.00117.26 C ANISOU 379 C VAL A 57 14115 13785 16654 -431 -1721 -1365 C ATOM 380 O VAL A 57 36.539 12.458 38.776 1.00110.34 O ANISOU 380 O VAL A 57 13231 12824 15867 -465 -1859 -1295 O ATOM 381 CB VAL A 57 33.526 13.369 37.929 1.00110.38 C ANISOU 381 CB VAL A 57 13343 12976 15619 -504 -1645 -1416 C ATOM 382 CG1 VAL A 57 33.641 11.854 37.977 1.00110.34 C ANISOU 382 CG1 VAL A 57 13357 12865 15704 -497 -1781 -1398 C ATOM 383 CG2 VAL A 57 32.218 13.827 38.551 1.00105.61 C ANISOU 383 CG2 VAL A 57 12787 12423 14918 -617 -1588 -1398 C ATOM 384 N LEU A 58 36.550 13.898 37.049 1.00113.49 N ANISOU 384 N LEU A 58 13578 13331 16211 -305 -1616 -1433 N ATOM 385 CA LEU A 58 37.761 13.340 36.457 1.00112.52 C ANISOU 385 CA LEU A 58 13376 13130 16244 -192 -1632 -1450 C ATOM 386 C LEU A 58 38.812 14.406 36.159 1.00115.43 C ANISOU 386 C LEU A 58 13663 13545 16648 -139 -1541 -1452 C ATOM 387 O LEU A 58 39.970 14.269 36.553 1.00115.63 O ANISOU 387 O LEU A 58 13607 13518 16809 -129 -1602 -1392 O ATOM 388 CB LEU A 58 37.428 12.561 35.183 1.00108.99 C ANISOU 388 CB LEU A 58 12948 12640 15823 -84 -1579 -1554 C ATOM 389 CG LEU A 58 36.526 11.337 35.346 1.00106.51 C ANISOU 389 CG LEU A 58 12703 12254 15512 -126 -1677 -1561 C ATOM 390 CD1 LEU A 58 36.310 10.651 34.007 1.00103.74 C ANISOU 390 CD1 LEU A 58 12382 11859 15174 -32 -1615 -1684 C ATOM 391 CD2 LEU A 58 37.114 10.367 36.359 1.00112.61 C ANISOU 391 CD2 LEU A 58 13449 12910 16427 -170 -1829 -1465 C ATOM 392 N ALA A 59 38.408 15.464 35.464 1.00113.48 N ANISOU 392 N ALA A 59 13428 13392 16297 -109 -1402 -1505 N ATOM 393 CA ALA A 59 39.336 16.521 35.072 1.00113.72 C ANISOU 393 CA ALA A 59 13384 13466 16357 -59 -1301 -1509 C ATOM 394 C ALA A 59 40.153 17.038 36.252 1.00113.44 C ANISOU 394 C ALA A 59 13306 13428 16367 -153 -1374 -1420 C ATOM 395 O ALA A 59 41.381 17.027 36.215 1.00125.53 O ANISOU 395 O ALA A 59 14740 14921 18036 -110 -1393 -1388 O ATOM 396 CB ALA A 59 38.593 17.663 34.397 1.00119.77 C ANISOU 396 CB ALA A 59 14179 14330 16997 -47 -1165 -1547 C ATOM 397 N ILE A 60 39.468 17.489 37.298 1.00106.67 N ANISOU 397 N ILE A 60 12523 12610 15397 -293 -1413 -1382 N ATOM 398 CA ILE A 60 40.142 18.000 38.488 1.00109.43 C ANISOU 398 CA ILE A 60 12868 12966 15745 -423 -1491 -1305 C ATOM 399 C ILE A 60 40.957 16.923 39.208 1.00113.78 C ANISOU 399 C ILE A 60 13379 13436 16416 -464 -1684 -1209 C ATOM 400 O ILE A 60 42.110 17.156 39.563 1.00117.62 O ANISOU 400 O ILE A 60 13783 13905 17003 -487 -1753 -1140 O ATOM 401 CB ILE A 60 39.158 18.667 39.472 1.00107.16 C ANISOU 401 CB ILE A 60 12694 12730 15292 -583 -1465 -1305 C ATOM 402 CG1 ILE A 60 38.590 19.951 38.866 1.00106.67 C ANISOU 402 CG1 ILE A 60 12635 12730 15166 -545 -1275 -1374 C ATOM 403 CG2 ILE A 60 39.846 18.967 40.793 1.00101.62 C ANISOU 403 CG2 ILE A 60 12022 12031 14559 -754 -1574 -1228 C ATOM 404 CD1 ILE A 60 37.694 20.727 39.806 1.00107.39 C ANISOU 404 CD1 ILE A 60 12822 12850 15132 -693 -1204 -1389 C ATOM 405 N PRO A 61 40.360 15.739 39.431 1.00116.20 N ANISOU 405 N PRO A 61 13735 13686 16729 -477 -1780 -1189 N ATOM 406 CA PRO A 61 41.129 14.644 40.033 1.00123.95 C ANISOU 406 CA PRO A 61 14664 14570 17860 -502 -1970 -1079 C ATOM 407 C PRO A 61 42.386 14.315 39.230 1.00126.24 C ANISOU 407 C PRO A 61 14798 14782 18385 -347 -1959 -1076 C ATOM 408 O PRO A 61 43.396 13.917 39.810 1.00122.69 O ANISOU 408 O PRO A 61 14255 14265 18097 -376 -2105 -957 O ATOM 409 CB PRO A 61 40.150 13.470 39.989 1.00120.28 C ANISOU 409 CB PRO A 61 14272 14049 17379 -496 -2019 -1094 C ATOM 410 CG PRO A 61 38.809 14.107 40.038 1.00117.94 C ANISOU 410 CG PRO A 61 14091 13845 16876 -563 -1908 -1164 C ATOM 411 CD PRO A 61 38.940 15.386 39.260 1.00114.56 C ANISOU 411 CD PRO A 61 13627 13496 16405 -489 -1734 -1246 C ATOM 412 N PHE A 62 42.319 14.482 37.912 1.00126.89 N ANISOU 412 N PHE A 62 14849 14872 18490 -193 -1785 -1197 N ATOM 413 CA PHE A 62 43.473 14.245 37.050 1.00124.60 C ANISOU 413 CA PHE A 62 14418 14510 18414 -45 -1719 -1220 C ATOM 414 C PHE A 62 44.485 15.384 37.141 1.00122.23 C ANISOU 414 C PHE A 62 14020 14262 18159 -57 -1677 -1179 C ATOM 415 O PHE A 62 45.690 15.150 37.207 1.00122.78 O ANISOU 415 O PHE A 62 13943 14258 18449 -14 -1728 -1107 O ATOM 416 CB PHE A 62 43.038 14.055 35.593 1.00122.45 C ANISOU 416 CB PHE A 62 14174 14238 18112 96 -1537 -1371 C ATOM 417 CG PHE A 62 42.356 12.743 35.325 1.00120.61 C ANISOU 417 CG PHE A 62 14005 13916 17905 129 -1578 -1421 C ATOM 418 CD1 PHE A 62 42.701 11.607 36.037 1.00122.92 C ANISOU 418 CD1 PHE A 62 14255 14078 18370 110 -1739 -1332 C ATOM 419 CD2 PHE A 62 41.382 12.643 34.346 1.00118.35 C ANISOU 419 CD2 PHE A 62 13819 13669 17479 172 -1468 -1546 C ATOM 420 CE1 PHE A 62 42.078 10.398 35.786 1.00124.82 C ANISOU 420 CE1 PHE A 62 14555 14222 18649 137 -1773 -1380 C ATOM 421 CE2 PHE A 62 40.756 11.438 34.090 1.00117.70 C ANISOU 421 CE2 PHE A 62 13801 13500 17420 188 -1510 -1598 C ATOM 422 CZ PHE A 62 41.105 10.314 34.811 1.00121.77 C ANISOU 422 CZ PHE A 62 14276 13877 18115 174 -1655 -1521 C ATOM 423 N ALA A 63 43.986 16.616 37.139 1.00120.93 N ANISOU 423 N ALA A 63 13925 14214 17807 -116 -1581 -1219 N ATOM 424 CA ALA A 63 44.844 17.795 37.192 1.00123.78 C ANISOU 424 CA ALA A 63 14209 14627 18195 -139 -1527 -1192 C ATOM 425 C ALA A 63 45.653 17.850 38.485 1.00135.36 C ANISOU 425 C ALA A 63 15625 16072 19734 -281 -1721 -1052 C ATOM 426 O ALA A 63 46.782 18.341 38.500 1.00134.19 O ANISOU 426 O ALA A 63 15350 15914 19721 -276 -1732 -996 O ATOM 427 CB ALA A 63 44.015 19.061 37.027 1.00111.78 C ANISOU 427 CB ALA A 63 12785 13216 16469 -186 -1392 -1258 C ATOM 428 N ILE A 64 45.070 17.346 39.567 1.00146.01 N ANISOU 428 N ILE A 64 17076 17416 20987 -422 -1880 -987 N ATOM 429 CA ILE A 64 45.742 17.328 40.861 1.00155.35 C ANISOU 429 CA ILE A 64 18241 18587 22197 -594 -2095 -840 C ATOM 430 C ILE A 64 46.792 16.223 40.910 1.00158.20 C ANISOU 430 C ILE A 64 18441 18827 22841 -528 -2254 -716 C ATOM 431 O ILE A 64 47.775 16.318 41.644 1.00165.84 O ANISOU 431 O ILE A 64 19316 19774 23922 -625 -2424 -574 O ATOM 432 CB ILE A 64 44.740 17.131 42.014 1.00165.99 C ANISOU 432 CB ILE A 64 19770 19974 23327 -785 -2202 -807 C ATOM 433 CG1 ILE A 64 43.667 18.222 41.977 1.00175.19 C ANISOU 433 CG1 ILE A 64 21076 21237 24254 -842 -2020 -931 C ATOM 434 CG2 ILE A 64 45.456 17.135 43.356 1.00165.81 C ANISOU 434 CG2 ILE A 64 19753 19952 23296 -995 -2437 -647 C ATOM 435 CD1 ILE A 64 42.555 18.017 42.981 1.00180.33 C ANISOU 435 CD1 ILE A 64 21901 21918 24697 -1014 -2067 -926 C ATOM 436 N THR A 65 46.580 15.178 40.118 1.00157.72 N ANISOU 436 N THR A 65 18342 18676 22908 -369 -2201 -767 N ATOM 437 CA THR A 65 47.512 14.057 40.065 1.00165.83 C ANISOU 437 CA THR A 65 19205 19556 24247 -281 -2318 -665 C ATOM 438 C THR A 65 48.679 14.350 39.128 1.00171.82 C ANISOU 438 C THR A 65 19768 20266 25249 -123 -2184 -693 C ATOM 439 O THR A 65 49.819 13.986 39.411 1.00175.80 O ANISOU 439 O THR A 65 20089 20676 26032 -106 -2304 -558 O ATOM 440 CB THR A 65 46.811 12.761 39.612 1.00167.10 C ANISOU 440 CB THR A 65 19412 19616 24462 -182 -2301 -723 C ATOM 441 OG1 THR A 65 45.774 12.426 40.542 1.00170.53 O ANISOU 441 OG1 THR A 65 20013 20087 24694 -337 -2432 -676 O ATOM 442 CG2 THR A 65 47.806 11.613 39.536 1.00169.36 C ANISOU 442 CG2 THR A 65 19515 19721 25114 -80 -2400 -621 C ATOM 443 N ILE A 66 48.387 15.014 38.014 1.00171.01 N ANISOU 443 N ILE A 66 19699 20228 25049 -15 -1936 -857 N ATOM 444 CA ILE A 66 49.406 15.325 37.018 1.00169.05 C ANISOU 444 CA ILE A 66 19286 19944 25001 132 -1766 -903 C ATOM 445 C ILE A 66 50.257 16.525 37.434 1.00166.62 C ANISOU 445 C ILE A 66 18888 19709 24713 46 -1794 -821 C ATOM 446 O ILE A 66 51.359 16.723 36.921 1.00165.02 O ANISOU 446 O ILE A 66 18503 19459 24740 137 -1714 -800 O ATOM 447 CB ILE A 66 48.778 15.592 35.633 1.00170.23 C ANISOU 447 CB ILE A 66 19521 20144 25015 260 -1496 -1097 C ATOM 448 CG1 ILE A 66 49.842 15.527 34.535 1.00169.92 C ANISOU 448 CG1 ILE A 66 19318 20034 25211 422 -1305 -1153 C ATOM 449 CG2 ILE A 66 48.059 16.933 35.620 1.00172.06 C ANISOU 449 CG2 ILE A 66 19882 20535 24959 175 -1414 -1149 C ATOM 450 CD1 ILE A 66 49.294 15.743 33.142 1.00169.86 C ANISOU 450 CD1 ILE A 66 19409 20080 25051 526 -1047 -1335 C ATOM 451 N SER A 67 49.744 17.320 38.368 1.00167.24 N ANISOU 451 N SER A 67 19094 19893 24557 -135 -1897 -782 N ATOM 452 CA SER A 67 50.473 18.482 38.864 1.00169.22 C ANISOU 452 CA SER A 67 19287 20209 24800 -250 -1938 -713 C ATOM 453 C SER A 67 51.760 18.045 39.550 1.00171.04 C ANISOU 453 C SER A 67 19322 20352 25313 -299 -2154 -525 C ATOM 454 O SER A 67 52.811 18.659 39.371 1.00172.55 O ANISOU 454 O SER A 67 19351 20539 25670 -285 -2131 -475 O ATOM 455 CB SER A 67 49.612 19.292 39.835 1.00170.92 C ANISOU 455 CB SER A 67 19700 20532 24708 -455 -2004 -720 C ATOM 456 OG SER A 67 49.375 18.572 41.032 1.00174.54 O ANISOU 456 OG SER A 67 20232 20969 25117 -609 -2246 -606 O ATOM 457 N THR A 68 51.668 16.980 40.339 1.00167.87 N ANISOU 457 N THR A 68 18928 19879 24978 -361 -2375 -407 N ATOM 458 CA THR A 68 52.831 16.441 41.032 1.00162.51 C ANISOU 458 CA THR A 68 18053 19104 24590 -413 -2618 -194 C ATOM 459 C THR A 68 53.610 15.500 40.117 1.00155.73 C ANISOU 459 C THR A 68 16967 18085 24120 -183 -2526 -188 C ATOM 460 O THR A 68 54.778 15.200 40.369 1.00165.57 O ANISOU 460 O THR A 68 17979 19233 25696 -171 -2660 -23 O ATOM 461 CB THR A 68 52.427 15.685 42.312 1.00158.87 C ANISOU 461 CB THR A 68 17694 18626 24042 -594 -2912 -42 C ATOM 462 OG1 THR A 68 51.611 14.557 41.970 1.00154.58 O ANISOU 462 OG1 THR A 68 17224 18006 23502 -486 -2867 -105 O ATOM 463 CG2 THR A 68 51.647 16.602 43.248 1.00154.82 C ANISOU 463 CG2 THR A 68 17423 18265 23138 -836 -2972 -67 C ATOM 464 N GLY A 69 52.956 15.042 39.052 1.00135.56 N ANISOU 464 N GLY A 69 14478 15498 21531 -10 -2292 -368 N ATOM 465 CA GLY A 69 53.576 14.142 38.095 1.00124.62 C ANISOU 465 CA GLY A 69 12915 13954 20482 205 -2150 -410 C ATOM 466 C GLY A 69 53.627 12.709 38.588 1.00126.24 C ANISOU 466 C GLY A 69 13056 13994 20916 227 -2335 -291 C ATOM 467 O GLY A 69 53.841 12.461 39.773 1.00127.03 O ANISOU 467 O GLY A 69 13129 14078 21059 75 -2632 -85 O ATOM 468 N PHE A 70 53.430 11.764 37.675 1.00132.56 N ANISOU 468 N PHE A 70 13841 14667 21858 405 -2162 -418 N ATOM 469 CA PHE A 70 53.475 10.344 38.011 1.00145.24 C ANISOU 469 CA PHE A 70 15379 16086 23721 450 -2303 -322 C ATOM 470 C PHE A 70 54.092 9.542 36.872 1.00145.44 C ANISOU 470 C PHE A 70 15240 15919 24102 680 -2064 -434 C ATOM 471 O PHE A 70 54.481 10.104 35.850 1.00149.45 O ANISOU 471 O PHE A 70 15698 16455 24630 791 -1791 -582 O ATOM 472 CB PHE A 70 52.072 9.817 38.324 1.00156.90 C ANISOU 472 CB PHE A 70 17111 17603 24900 372 -2371 -386 C ATOM 473 CG PHE A 70 51.097 9.982 37.192 1.00157.93 C ANISOU 473 CG PHE A 70 17425 17804 24777 461 -2093 -651 C ATOM 474 CD1 PHE A 70 50.357 11.145 37.062 1.00156.88 C ANISOU 474 CD1 PHE A 70 17464 17876 24269 379 -2004 -752 C ATOM 475 CD2 PHE A 70 50.920 8.974 36.257 1.00162.04 C ANISOU 475 CD2 PHE A 70 17946 18179 25442 618 -1925 -795 C ATOM 476 CE1 PHE A 70 49.460 11.301 36.024 1.00161.35 C ANISOU 476 CE1 PHE A 70 18186 18508 24613 450 -1778 -965 C ATOM 477 CE2 PHE A 70 50.024 9.125 35.215 1.00163.82 C ANISOU 477 CE2 PHE A 70 18349 18478 25416 674 -1696 -1027 C ATOM 478 CZ PHE A 70 49.293 10.290 35.099 1.00164.84 C ANISOU 478 CZ PHE A 70 18636 18820 25176 589 -1635 -1099 C ATOM 479 N CYS A 71 54.174 8.227 37.050 1.00145.33 N ANISOU 479 N CYS A 71 15148 15701 24368 745 -2153 -367 N ATOM 480 CA CYS A 71 54.768 7.356 36.041 1.00153.60 C ANISOU 480 CA CYS A 71 16040 16530 25791 959 -1917 -479 C ATOM 481 C CYS A 71 53.735 6.442 35.390 1.00158.49 C ANISOU 481 C CYS A 71 16856 17077 26287 1027 -1777 -683 C ATOM 482 O CYS A 71 53.068 5.660 36.067 1.00159.60 O ANISOU 482 O CYS A 71 17091 17162 26388 954 -1977 -603 O ATOM 483 CB CYS A 71 55.900 6.524 36.648 1.00158.77 C ANISOU 483 CB CYS A 71 16390 16955 26981 1008 -2099 -236 C ATOM 484 SG CYS A 71 57.296 7.498 37.260 1.00280.19 S ANISOU 484 SG CYS A 71 31484 32386 42591 943 -2253 9 S ATOM 485 N ALA A 72 53.612 6.549 34.071 1.00164.49 N ANISOU 485 N ALA A 72 17684 17838 26976 1150 -1435 -944 N ATOM 486 CA ALA A 72 52.683 5.722 33.310 1.00170.73 C ANISOU 486 CA ALA A 72 18667 18561 27641 1206 -1281 -1162 C ATOM 487 C ALA A 72 52.991 5.793 31.819 1.00172.87 C ANISOU 487 C ALA A 72 18947 18794 27943 1349 -889 -1423 C ATOM 488 O ALA A 72 53.716 6.679 31.367 1.00172.55 O ANISOU 488 O ALA A 72 18806 18833 27923 1387 -732 -1444 O ATOM 489 CB ALA A 72 51.249 6.151 33.576 1.00170.17 C ANISOU 489 CB ALA A 72 18885 18700 27072 1059 -1384 -1214 C ATOM 490 N ALA A 73 52.434 4.855 31.059 1.00173.92 N ANISOU 490 N ALA A 73 19211 18805 28066 1413 -729 -1623 N ATOM 491 CA ALA A 73 52.640 4.812 29.615 1.00176.19 C ANISOU 491 CA ALA A 73 19551 19051 28341 1523 -348 -1894 C ATOM 492 C ALA A 73 52.222 6.124 28.960 1.00177.80 C ANISOU 492 C ALA A 73 19915 19530 28110 1459 -216 -2001 C ATOM 493 O ALA A 73 51.646 6.995 29.609 1.00176.13 O ANISOU 493 O ALA A 73 19788 19525 27609 1337 -411 -1886 O ATOM 494 CB ALA A 73 51.877 3.647 29.007 1.00176.23 C ANISOU 494 CB ALA A 73 19732 18913 28315 1551 -243 -2095 C ATOM 495 N CYS A 74 52.512 6.258 27.669 1.00181.01 N ANISOU 495 N CYS A 74 20367 19931 28477 1536 127 -2220 N ATOM 496 CA CYS A 74 52.184 7.477 26.939 1.00182.85 C ANISOU 496 CA CYS A 74 20745 20411 28321 1479 268 -2313 C ATOM 497 C CYS A 74 50.674 7.615 26.752 1.00187.07 C ANISOU 497 C CYS A 74 21577 21112 28388 1361 176 -2399 C ATOM 498 O CYS A 74 50.127 8.713 26.845 1.00185.96 O ANISOU 498 O CYS A 74 21533 21196 27926 1269 104 -2348 O ATOM 499 CB CYS A 74 52.898 7.507 25.584 1.00181.73 C ANISOU 499 CB CYS A 74 20587 20213 28250 1577 665 -2521 C ATOM 500 SG CYS A 74 52.975 9.144 24.811 1.00338.39 S ANISOU 500 SG CYS A 74 40504 40330 47738 1522 836 -2556 S ATOM 501 N HIS A 75 50.007 6.495 26.491 1.00188.76 N ANISOU 501 N HIS A 75 21926 21204 28592 1362 181 -2526 N ATOM 502 CA HIS A 75 48.556 6.486 26.336 1.00180.60 C ANISOU 502 CA HIS A 75 21155 20306 27160 1247 78 -2597 C ATOM 503 C HIS A 75 47.860 6.913 27.624 1.00163.68 C ANISOU 503 C HIS A 75 19017 18284 24891 1140 -252 -2384 C ATOM 504 O HIS A 75 47.030 7.822 27.622 1.00161.98 O ANISOU 504 O HIS A 75 18931 18280 24332 1045 -316 -2363 O ATOM 505 CB HIS A 75 48.067 5.099 25.911 1.00194.76 C ANISOU 505 CB HIS A 75 23067 21913 29020 1264 129 -2762 C ATOM 506 CG HIS A 75 48.401 4.746 24.494 1.00211.74 C ANISOU 506 CG HIS A 75 25308 23985 31157 1321 475 -3027 C ATOM 507 ND1 HIS A 75 49.628 4.241 24.121 1.00220.00 N ANISOU 507 ND1 HIS A 75 26184 24819 32586 1454 713 -3102 N ATOM 508 CD2 HIS A 75 47.664 4.822 23.361 1.00217.44 C ANISOU 508 CD2 HIS A 75 26280 24811 31525 1250 627 -3234 C ATOM 509 CE1 HIS A 75 49.634 4.024 22.818 1.00224.10 C ANISOU 509 CE1 HIS A 75 26859 25316 32974 1460 1021 -3363 C ATOM 510 NE2 HIS A 75 48.454 4.368 22.333 1.00224.09 N ANISOU 510 NE2 HIS A 75 27122 25511 32512 1329 962 -3444 N ATOM 511 N GLY A 76 48.207 6.252 28.724 1.00158.12 N ANISOU 511 N GLY A 76 18170 17435 24474 1151 -455 -2220 N ATOM 512 CA GLY A 76 47.607 6.544 30.012 1.00160.09 C ANISOU 512 CA GLY A 76 18433 17781 24612 1034 -758 -2020 C ATOM 513 C GLY A 76 47.956 7.926 30.530 1.00167.25 C ANISOU 513 C GLY A 76 19268 18871 25408 977 -822 -1882 C ATOM 514 O GLY A 76 47.190 8.526 31.282 1.00171.81 O ANISOU 514 O GLY A 76 19934 19596 25750 856 -995 -1785 O ATOM 515 N CYS A 77 49.116 8.433 30.123 1.00167.84 N ANISOU 515 N CYS A 77 19182 18928 25663 1061 -667 -1881 N ATOM 516 CA CYS A 77 49.580 9.741 30.575 1.00165.83 C ANISOU 516 CA CYS A 77 18843 18826 25338 1008 -716 -1755 C ATOM 517 C CYS A 77 48.915 10.872 29.799 1.00163.43 C ANISOU 517 C CYS A 77 18700 18734 24664 965 -574 -1863 C ATOM 518 O CYS A 77 48.527 11.889 30.375 1.00162.28 O ANISOU 518 O CYS A 77 18596 18746 24318 865 -685 -1771 O ATOM 519 CB CYS A 77 51.103 9.844 30.450 1.00165.72 C ANISOU 519 CB CYS A 77 18573 18704 25690 1109 -611 -1696 C ATOM 520 SG CYS A 77 51.802 11.404 31.041 1.00156.36 S ANISOU 520 SG CYS A 77 17264 17683 24462 1034 -684 -1533 S ATOM 521 N LEU A 78 48.787 10.690 28.489 1.00160.09 N ANISOU 521 N LEU A 78 18370 18305 24151 1031 -328 -2057 N ATOM 522 CA LEU A 78 48.176 11.702 27.634 1.00155.07 C ANISOU 522 CA LEU A 78 17885 17861 23172 988 -196 -2147 C ATOM 523 C LEU A 78 46.690 11.871 27.924 1.00154.91 C ANISOU 523 C LEU A 78 18058 17967 22835 876 -352 -2138 C ATOM 524 O LEU A 78 46.176 12.988 27.924 1.00153.46 O ANISOU 524 O LEU A 78 17939 17952 22419 808 -368 -2096 O ATOM 525 CB LEU A 78 48.389 11.362 26.158 1.00152.33 C ANISOU 525 CB LEU A 78 17614 17477 22788 1061 95 -2354 C ATOM 526 CG LEU A 78 49.808 11.552 25.623 1.00153.01 C ANISOU 526 CG LEU A 78 17522 17486 23130 1165 327 -2383 C ATOM 527 CD1 LEU A 78 49.904 11.078 24.183 1.00155.02 C ANISOU 527 CD1 LEU A 78 17890 17693 23318 1216 631 -2613 C ATOM 528 CD2 LEU A 78 50.232 13.009 25.743 1.00153.68 C ANISOU 528 CD2 LEU A 78 17530 17730 23133 1132 341 -2271 C ATOM 529 N PHE A 79 46.001 10.760 28.166 1.00152.82 N ANISOU 529 N PHE A 79 17875 17607 22584 857 -459 -2173 N ATOM 530 CA PHE A 79 44.581 10.809 28.488 1.00149.72 C ANISOU 530 CA PHE A 79 17645 17314 21929 750 -608 -2158 C ATOM 531 C PHE A 79 44.346 11.656 29.732 1.00144.94 C ANISOU 531 C PHE A 79 16997 16809 21266 659 -793 -1981 C ATOM 532 O PHE A 79 43.476 12.524 29.748 1.00151.45 O ANISOU 532 O PHE A 79 17915 17784 21847 584 -815 -1963 O ATOM 533 CB PHE A 79 44.020 9.401 28.694 1.00156.55 C ANISOU 533 CB PHE A 79 18575 18034 22872 743 -707 -2204 C ATOM 534 CG PHE A 79 42.587 9.381 29.146 1.00165.30 C ANISOU 534 CG PHE A 79 19824 19232 23750 628 -870 -2169 C ATOM 535 CD1 PHE A 79 41.554 9.475 28.228 1.00161.30 C ANISOU 535 CD1 PHE A 79 19482 18820 22986 584 -810 -2283 C ATOM 536 CD2 PHE A 79 42.272 9.273 30.490 1.00168.99 C ANISOU 536 CD2 PHE A 79 20258 19691 24261 552 -1083 -2014 C ATOM 537 CE1 PHE A 79 40.234 9.460 28.642 1.00154.84 C ANISOU 537 CE1 PHE A 79 18766 18076 21991 481 -956 -2239 C ATOM 538 CE2 PHE A 79 40.955 9.256 30.911 1.00160.82 C ANISOU 538 CE2 PHE A 79 19342 18731 23031 446 -1206 -1984 C ATOM 539 CZ PHE A 79 39.935 9.349 29.986 1.00154.13 C ANISOU 539 CZ PHE A 79 18633 17969 21962 418 -1140 -2096 C ATOM 540 N ILE A 80 45.135 11.400 30.769 1.00138.32 N ANISOU 540 N ILE A 80 16016 15879 20661 659 -922 -1849 N ATOM 541 CA ILE A 80 45.024 12.137 32.023 1.00139.37 C ANISOU 541 CA ILE A 80 16121 16095 20739 549 -1098 -1688 C ATOM 542 C ILE A 80 45.435 13.598 31.843 1.00141.15 C ANISOU 542 C ILE A 80 16305 16456 20871 536 -1002 -1665 C ATOM 543 O ILE A 80 45.086 14.460 32.652 1.00139.51 O ANISOU 543 O ILE A 80 16125 16348 20536 431 -1096 -1577 O ATOM 544 CB ILE A 80 45.870 11.474 33.131 1.00139.49 C ANISOU 544 CB ILE A 80 15994 15978 21028 535 -1278 -1538 C ATOM 545 CG1 ILE A 80 45.370 10.051 33.391 1.00142.79 C ANISOU 545 CG1 ILE A 80 16461 16255 21538 536 -1388 -1542 C ATOM 546 CG2 ILE A 80 45.829 12.292 34.412 1.00136.61 C ANISOU 546 CG2 ILE A 80 15622 15709 20573 393 -1453 -1380 C ATOM 547 CD1 ILE A 80 46.050 9.361 34.550 1.00145.88 C ANISOU 547 CD1 ILE A 80 16725 16518 22184 501 -1602 -1361 C ATOM 548 N ALA A 81 46.163 13.873 30.767 1.00144.33 N ANISOU 548 N ALA A 81 16649 16854 21335 636 -800 -1750 N ATOM 549 CA ALA A 81 46.647 15.221 30.493 1.00145.45 C ANISOU 549 CA ALA A 81 16740 17109 21414 630 -693 -1726 C ATOM 550 C ALA A 81 45.734 15.977 29.531 1.00142.22 C ANISOU 550 C ALA A 81 16477 16839 20722 616 -562 -1816 C ATOM 551 O ALA A 81 45.625 17.201 29.598 1.00141.12 O ANISOU 551 O ALA A 81 16342 16812 20465 569 -535 -1767 O ATOM 552 CB ALA A 81 48.066 15.169 29.943 1.00147.14 C ANISOU 552 CB ALA A 81 16785 17241 21881 736 -545 -1740 C ATOM 553 N CYS A 82 45.078 15.243 28.639 1.00141.04 N ANISOU 553 N CYS A 82 16446 16672 20471 649 -491 -1939 N ATOM 554 CA CYS A 82 44.271 15.862 27.595 1.00147.32 C ANISOU 554 CA CYS A 82 17375 17594 21007 629 -379 -2011 C ATOM 555 C CYS A 82 42.775 15.613 27.780 1.00153.29 C ANISOU 555 C CYS A 82 18274 18401 21568 550 -506 -2014 C ATOM 556 O CYS A 82 41.973 15.929 26.900 1.00152.91 O ANISOU 556 O CYS A 82 18339 18446 21315 525 -449 -2064 O ATOM 557 CB CYS A 82 44.721 15.374 26.217 1.00148.31 C ANISOU 557 CB CYS A 82 17540 17684 21128 705 -172 -2157 C ATOM 558 SG CYS A 82 46.474 15.659 25.865 1.00192.36 S ANISOU 558 SG CYS A 82 22935 23196 26957 805 24 -2163 S ATOM 559 N PHE A 83 42.402 15.049 28.924 1.00153.39 N ANISOU 559 N PHE A 83 18276 18354 21650 501 -682 -1949 N ATOM 560 CA PHE A 83 40.995 14.803 29.216 1.00147.93 C ANISOU 560 CA PHE A 83 17701 17702 20802 420 -799 -1940 C ATOM 561 C PHE A 83 40.253 16.116 29.441 1.00145.64 C ANISOU 561 C PHE A 83 17435 17548 20353 351 -804 -1867 C ATOM 562 O PHE A 83 39.095 16.261 29.051 1.00154.07 O ANISOU 562 O PHE A 83 18593 18683 21263 308 -820 -1879 O ATOM 563 CB PHE A 83 40.836 13.893 30.436 1.00149.43 C ANISOU 563 CB PHE A 83 17874 17794 21109 374 -975 -1878 C ATOM 564 CG PHE A 83 39.405 13.576 30.769 1.00156.14 C ANISOU 564 CG PHE A 83 18832 18675 21819 288 -1082 -1868 C ATOM 565 CD1 PHE A 83 38.736 12.557 30.111 1.00156.24 C ANISOU 565 CD1 PHE A 83 18936 18639 21791 294 -1094 -1959 C ATOM 566 CD2 PHE A 83 38.727 14.299 31.737 1.00156.67 C ANISOU 566 CD2 PHE A 83 18910 18814 21803 192 -1160 -1773 C ATOM 567 CE1 PHE A 83 37.420 12.264 30.413 1.00149.64 C ANISOU 567 CE1 PHE A 83 18182 17829 20844 209 -1196 -1941 C ATOM 568 CE2 PHE A 83 37.410 14.010 32.043 1.00150.63 C ANISOU 568 CE2 PHE A 83 18227 18072 20933 114 -1238 -1761 C ATOM 569 CZ PHE A 83 36.757 12.992 31.380 1.00146.42 C ANISOU 569 CZ PHE A 83 17767 17494 20372 124 -1265 -1837 C ATOM 570 N VAL A 84 40.929 17.069 30.074 1.00135.73 N ANISOU 570 N VAL A 84 16092 16320 19158 338 -792 -1788 N ATOM 571 CA VAL A 84 40.342 18.377 30.330 1.00130.99 C ANISOU 571 CA VAL A 84 15504 15822 18444 277 -772 -1726 C ATOM 572 C VAL A 84 40.125 19.127 29.020 1.00129.32 C ANISOU 572 C VAL A 84 15325 15699 18112 316 -635 -1758 C ATOM 573 O VAL A 84 39.254 19.993 28.922 1.00125.83 O ANISOU 573 O VAL A 84 14915 15333 17562 274 -624 -1713 O ATOM 574 CB VAL A 84 41.225 19.220 31.271 1.00128.66 C ANISOU 574 CB VAL A 84 15116 15524 18243 241 -783 -1648 C ATOM 575 CG1 VAL A 84 42.586 19.476 30.636 1.00134.68 C ANISOU 575 CG1 VAL A 84 15778 16270 19123 323 -673 -1662 C ATOM 576 CG2 VAL A 84 40.534 20.530 31.623 1.00120.89 C ANISOU 576 CG2 VAL A 84 14157 14621 17157 170 -751 -1599 C ATOM 577 N LEU A 85 40.919 18.783 28.011 1.00129.12 N ANISOU 577 N LEU A 85 15290 15657 18114 392 -526 -1830 N ATOM 578 CA LEU A 85 40.800 19.402 26.697 1.00125.93 C ANISOU 578 CA LEU A 85 14934 15341 17573 414 -395 -1858 C ATOM 579 C LEU A 85 39.547 18.908 25.981 1.00126.60 C ANISOU 579 C LEU A 85 15148 15468 17485 375 -442 -1898 C ATOM 580 O LEU A 85 39.100 19.511 25.005 1.00127.91 O ANISOU 580 O LEU A 85 15372 15727 17500 357 -386 -1885 O ATOM 581 CB LEU A 85 42.043 19.115 25.852 1.00125.54 C ANISOU 581 CB LEU A 85 14847 15255 17596 492 -240 -1936 C ATOM 582 CG LEU A 85 43.377 19.575 26.446 1.00121.14 C ANISOU 582 CG LEU A 85 14139 14652 17239 531 -192 -1887 C ATOM 583 CD1 LEU A 85 44.539 19.183 25.545 1.00119.92 C ANISOU 583 CD1 LEU A 85 13935 14448 17181 614 -16 -1972 C ATOM 584 CD2 LEU A 85 43.369 21.077 26.692 1.00116.15 C ANISOU 584 CD2 LEU A 85 13463 14105 16565 491 -169 -1786 C ATOM 585 N VAL A 86 38.987 17.808 26.476 1.00128.50 N ANISOU 585 N VAL A 86 15432 15641 17753 352 -560 -1934 N ATOM 586 CA VAL A 86 37.756 17.252 25.924 1.00130.70 C ANISOU 586 CA VAL A 86 15823 15949 17886 300 -633 -1967 C ATOM 587 C VAL A 86 36.539 17.966 26.503 1.00134.03 C ANISOU 587 C VAL A 86 16237 16434 18253 230 -729 -1857 C ATOM 588 O VAL A 86 35.637 18.374 25.770 1.00132.47 O ANISOU 588 O VAL A 86 16089 16318 17925 190 -744 -1823 O ATOM 589 CB VAL A 86 37.641 15.742 26.210 1.00129.16 C ANISOU 589 CB VAL A 86 15673 15640 17761 299 -715 -2051 C ATOM 590 CG1 VAL A 86 36.315 15.202 25.696 1.00131.10 C ANISOU 590 CG1 VAL A 86 16033 15918 17862 227 -806 -2078 C ATOM 591 CG2 VAL A 86 38.805 14.992 25.585 1.00131.93 C ANISOU 591 CG2 VAL A 86 16023 15903 18200 375 -594 -2171 C ATOM 592 N LEU A 87 36.521 18.115 27.825 1.00136.17 N ANISOU 592 N LEU A 87 16444 16662 18631 207 -792 -1798 N ATOM 593 CA LEU A 87 35.421 18.786 28.508 1.00133.26 C ANISOU 593 CA LEU A 87 16061 16332 18241 140 -847 -1709 C ATOM 594 C LEU A 87 35.412 20.277 28.189 1.00134.62 C ANISOU 594 C LEU A 87 16184 16579 18385 147 -754 -1634 C ATOM 595 O LEU A 87 34.391 20.948 28.339 1.00137.11 O ANISOU 595 O LEU A 87 16484 16930 18681 105 -769 -1561 O ATOM 596 CB LEU A 87 35.521 18.574 30.020 1.00127.41 C ANISOU 596 CB LEU A 87 15286 15525 17600 96 -914 -1678 C ATOM 597 CG LEU A 87 35.589 17.123 30.500 1.00121.65 C ANISOU 597 CG LEU A 87 14591 14705 16926 84 -1020 -1723 C ATOM 598 CD1 LEU A 87 35.686 17.065 32.015 1.00117.66 C ANISOU 598 CD1 LEU A 87 14061 14153 16491 14 -1092 -1666 C ATOM 599 CD2 LEU A 87 34.386 16.334 30.008 1.00122.57 C ANISOU 599 CD2 LEU A 87 14781 14824 16966 50 -1092 -1751 C ATOM 600 N ALA A 88 36.558 20.788 27.752 1.00135.48 N ANISOU 600 N ALA A 88 16258 16702 18516 201 -651 -1648 N ATOM 601 CA ALA A 88 36.679 22.191 27.377 1.00136.26 C ANISOU 601 CA ALA A 88 16311 16863 18601 209 -555 -1575 C ATOM 602 C ALA A 88 36.199 22.412 25.947 1.00129.30 C ANISOU 602 C ALA A 88 15484 16063 17582 213 -527 -1555 C ATOM 603 O ALA A 88 35.614 23.448 25.630 1.00117.90 O ANISOU 603 O ALA A 88 14013 14670 16112 195 -506 -1457 O ATOM 604 CB ALA A 88 38.117 22.658 27.533 1.00141.32 C ANISOU 604 CB ALA A 88 16884 17482 19328 251 -461 -1587 C ATOM 605 N GLN A 89 36.451 21.429 25.088 1.00134.05 N ANISOU 605 N GLN A 89 16165 16668 18099 229 -525 -1646 N ATOM 606 CA GLN A 89 36.061 21.515 23.686 1.00142.11 C ANISOU 606 CA GLN A 89 17270 17775 18950 205 -506 -1640 C ATOM 607 C GLN A 89 34.566 21.284 23.516 1.00149.95 C ANISOU 607 C GLN A 89 18307 18802 19863 135 -646 -1583 C ATOM 608 O GLN A 89 33.915 21.943 22.707 1.00158.41 O ANISOU 608 O GLN A 89 19396 19956 20835 94 -669 -1487 O ATOM 609 CB GLN A 89 36.842 20.501 22.848 1.00150.53 C ANISOU 609 CB GLN A 89 18425 18823 19946 229 -436 -1781 C ATOM 610 CG GLN A 89 36.582 20.597 21.352 1.00158.74 C ANISOU 610 CG GLN A 89 19582 19960 20770 180 -397 -1790 C ATOM 611 CD GLN A 89 37.131 21.875 20.743 1.00165.00 C ANISOU 611 CD GLN A 89 20340 20832 21520 190 -278 -1701 C ATOM 612 OE1 GLN A 89 37.889 22.606 21.382 1.00169.84 O ANISOU 612 OE1 GLN A 89 20840 21415 22278 246 -202 -1660 O ATOM 613 NE2 GLN A 89 36.752 22.148 19.499 1.00164.74 N ANISOU 613 NE2 GLN A 89 20411 20902 21281 123 -270 -1663 N ATOM 614 N SER A 90 34.027 20.339 24.280 1.00146.59 N ANISOU 614 N SER A 90 17892 18311 19493 114 -747 -1627 N ATOM 615 CA SER A 90 32.602 20.046 24.231 1.00142.01 C ANISOU 615 CA SER A 90 17336 17753 18870 44 -883 -1572 C ATOM 616 C SER A 90 31.800 21.271 24.653 1.00135.71 C ANISOU 616 C SER A 90 16434 16981 18147 27 -892 -1419 C ATOM 617 O SER A 90 30.822 21.638 24.005 1.00137.31 O ANISOU 617 O SER A 90 16632 17243 18296 -20 -963 -1318 O ATOM 618 CB SER A 90 32.265 18.855 25.130 1.00142.53 C ANISOU 618 CB SER A 90 17418 17730 19007 25 -973 -1641 C ATOM 619 OG SER A 90 30.897 18.504 25.020 1.00143.29 O ANISOU 619 OG SER A 90 17532 17845 19068 -49 -1102 -1590 O ATOM 620 N SER A 91 32.228 21.905 25.740 1.00129.93 N ANISOU 620 N SER A 91 15618 16199 17550 60 -821 -1401 N ATOM 621 CA SER A 91 31.573 23.110 26.234 1.00126.42 C ANISOU 621 CA SER A 91 15075 15753 17205 49 -789 -1280 C ATOM 622 C SER A 91 31.591 24.220 25.186 1.00130.66 C ANISOU 622 C SER A 91 15585 16359 17700 62 -740 -1174 C ATOM 623 O SER A 91 30.757 25.123 25.215 1.00131.26 O ANISOU 623 O SER A 91 15581 16437 17857 48 -742 -1048 O ATOM 624 CB SER A 91 32.232 23.587 27.529 1.00119.44 C ANISOU 624 CB SER A 91 14137 14801 16443 63 -704 -1307 C ATOM 625 OG SER A 91 32.082 22.625 28.560 1.00112.89 O ANISOU 625 OG SER A 91 13334 13912 15648 30 -765 -1374 O ATOM 626 N ILE A 92 32.543 24.147 24.262 1.00134.46 N ANISOU 626 N ILE A 92 16130 16890 18068 87 -688 -1219 N ATOM 627 CA ILE A 92 32.629 25.114 23.173 1.00135.93 C ANISOU 627 CA ILE A 92 16311 17152 18183 85 -646 -1113 C ATOM 628 C ILE A 92 31.483 24.923 22.187 1.00138.36 C ANISOU 628 C ILE A 92 16663 17532 18374 16 -779 -1019 C ATOM 629 O ILE A 92 30.854 25.891 21.756 1.00139.05 O ANISOU 629 O ILE A 92 16687 17653 18492 -4 -806 -854 O ATOM 630 CB ILE A 92 33.974 25.012 22.426 1.00133.06 C ANISOU 630 CB ILE A 92 16014 16826 17717 117 -535 -1196 C ATOM 631 CG1 ILE A 92 35.098 25.599 23.279 1.00122.26 C ANISOU 631 CG1 ILE A 92 14566 15397 16490 176 -410 -1229 C ATOM 632 CG2 ILE A 92 33.904 25.744 21.097 1.00137.41 C ANISOU 632 CG2 ILE A 92 16604 17475 18132 84 -517 -1086 C ATOM 633 CD1 ILE A 92 34.955 27.084 23.522 1.00118.31 C ANISOU 633 CD1 ILE A 92 13967 14889 16098 182 -351 -1095 C ATOM 634 N PHE A 93 31.215 23.670 21.836 1.00141.23 N ANISOU 634 N PHE A 93 17132 17911 18618 -27 -871 -1116 N ATOM 635 CA PHE A 93 30.119 23.346 20.929 1.00151.96 C ANISOU 635 CA PHE A 93 18546 19340 19852 -117 -1025 -1037 C ATOM 636 C PHE A 93 28.763 23.617 21.576 1.00148.78 C ANISOU 636 C PHE A 93 18022 18900 19607 -142 -1135 -907 C ATOM 637 O PHE A 93 27.861 24.164 20.940 1.00152.13 O ANISOU 637 O PHE A 93 18400 19376 20026 -195 -1236 -739 O ATOM 638 CB PHE A 93 30.204 21.886 20.483 1.00160.45 C ANISOU 638 CB PHE A 93 19772 20420 20771 -166 -1085 -1198 C ATOM 639 CG PHE A 93 31.453 21.557 19.718 1.00158.37 C ANISOU 639 CG PHE A 93 19630 20183 20359 -148 -957 -1334 C ATOM 640 CD1 PHE A 93 31.642 22.044 18.435 1.00157.23 C ANISOU 640 CD1 PHE A 93 19573 20145 20023 -205 -932 -1279 C ATOM 641 CD2 PHE A 93 32.431 20.751 20.274 1.00153.39 C ANISOU 641 CD2 PHE A 93 19022 19467 19791 -81 -857 -1508 C ATOM 642 CE1 PHE A 93 32.787 21.742 17.725 1.00154.01 C ANISOU 642 CE1 PHE A 93 19278 19757 19480 -195 -781 -1415 C ATOM 643 CE2 PHE A 93 33.578 20.444 19.567 1.00154.92 C ANISOU 643 CE2 PHE A 93 19307 19669 19886 -58 -715 -1634 C ATOM 644 CZ PHE A 93 33.756 20.941 18.291 1.00155.67 C ANISOU 644 CZ PHE A 93 19494 19871 19783 -115 -663 -1598 C ATOM 645 N SER A 94 28.624 23.227 22.839 1.00141.03 N ANISOU 645 N SER A 94 16985 17828 18774 -111 -1113 -976 N ATOM 646 CA SER A 94 27.394 23.472 23.581 1.00131.10 C ANISOU 646 CA SER A 94 15605 16520 17687 -132 -1173 -872 C ATOM 647 C SER A 94 27.095 24.965 23.650 1.00130.02 C ANISOU 647 C SER A 94 15330 16370 17702 -101 -1103 -708 C ATOM 648 O SER A 94 25.981 25.396 23.360 1.00134.10 O ANISOU 648 O SER A 94 15750 16893 18308 -135 -1190 -548 O ATOM 649 CB SER A 94 27.485 22.883 24.990 1.00120.45 C ANISOU 649 CB SER A 94 14239 15077 16449 -113 -1126 -984 C ATOM 650 OG SER A 94 27.605 21.471 24.947 1.00113.48 O ANISOU 650 OG SER A 94 13467 14187 15464 -144 -1207 -1112 O ATOM 651 N LEU A 95 28.096 25.751 24.032 1.00127.72 N ANISOU 651 N LEU A 95 15019 16050 17459 -38 -950 -741 N ATOM 652 CA LEU A 95 27.936 27.198 24.127 1.00128.91 C ANISOU 652 CA LEU A 95 15045 16167 17768 -6 -861 -601 C ATOM 653 C LEU A 95 27.712 27.835 22.759 1.00126.35 C ANISOU 653 C LEU A 95 14713 15925 17367 -29 -932 -433 C ATOM 654 O LEU A 95 27.036 28.858 22.646 1.00120.12 O ANISOU 654 O LEU A 95 13798 15106 16738 -22 -931 -258 O ATOM 655 CB LEU A 95 29.149 27.832 24.812 1.00129.68 C ANISOU 655 CB LEU A 95 15141 16216 17917 49 -690 -688 C ATOM 656 CG LEU A 95 29.331 27.520 26.297 1.00127.94 C ANISOU 656 CG LEU A 95 14912 15906 17793 52 -617 -814 C ATOM 657 CD1 LEU A 95 30.608 28.155 26.822 1.00126.53 C ANISOU 657 CD1 LEU A 95 14740 15695 17642 85 -479 -885 C ATOM 658 CD2 LEU A 95 28.129 27.993 27.093 1.00130.24 C ANISOU 658 CD2 LEU A 95 15091 16116 18277 32 -590 -742 C ATOM 659 N LEU A 96 28.284 27.229 21.724 1.00128.15 N ANISOU 659 N LEU A 96 15082 16254 17357 -63 -986 -484 N ATOM 660 CA LEU A 96 28.123 27.728 20.363 1.00130.48 C ANISOU 660 CA LEU A 96 15407 16646 17522 -114 -1065 -328 C ATOM 661 C LEU A 96 26.718 27.448 19.846 1.00133.73 C ANISOU 661 C LEU A 96 15782 17095 17933 -199 -1272 -179 C ATOM 662 O LEU A 96 26.070 28.325 19.274 1.00138.38 O ANISOU 662 O LEU A 96 16278 17705 18596 -226 -1348 44 O ATOM 663 CB LEU A 96 29.159 27.100 19.430 1.00127.45 C ANISOU 663 CB LEU A 96 15204 16356 16864 -144 -1036 -452 C ATOM 664 CG LEU A 96 29.044 27.474 17.950 1.00123.56 C ANISOU 664 CG LEU A 96 14792 15986 16170 -231 -1118 -308 C ATOM 665 CD1 LEU A 96 29.157 28.980 17.758 1.00116.31 C ANISOU 665 CD1 LEU A 96 13758 15059 15376 -199 -1055 -110 C ATOM 666 CD2 LEU A 96 30.097 26.747 17.126 1.00120.80 C ANISOU 666 CD2 LEU A 96 14637 15715 15548 -266 -1045 -474 C ATOM 667 N ALA A 97 26.254 26.219 20.052 1.00131.21 N ANISOU 667 N ALA A 97 15528 16778 17548 -244 -1372 -289 N ATOM 668 CA ALA A 97 24.911 25.828 19.643 1.00133.66 C ANISOU 668 CA ALA A 97 15799 17118 17868 -336 -1581 -159 C ATOM 669 C ALA A 97 23.866 26.698 20.329 1.00134.06 C ANISOU 669 C ALA A 97 15622 17078 18236 -300 -1586 21 C ATOM 670 O ALA A 97 22.973 27.237 19.679 1.00131.17 O ANISOU 670 O ALA A 97 15157 16741 17942 -351 -1725 247 O ATOM 671 CB ALA A 97 24.668 24.360 19.953 1.00131.33 C ANISOU 671 CB ALA A 97 15602 16812 17484 -382 -1658 -330 C ATOM 672 N ILE A 98 23.987 26.834 21.646 1.00134.78 N ANISOU 672 N ILE A 98 15631 17055 18523 -220 -1431 -77 N ATOM 673 CA ILE A 98 23.077 27.672 22.418 1.00134.18 C ANISOU 673 CA ILE A 98 15346 16870 18765 -180 -1376 55 C ATOM 674 C ILE A 98 23.014 29.083 21.841 1.00142.76 C ANISOU 674 C ILE A 98 16316 17946 19980 -150 -1349 268 C ATOM 675 O ILE A 98 21.957 29.714 21.831 1.00148.50 O ANISOU 675 O ILE A 98 16861 18613 20948 -151 -1399 466 O ATOM 676 CB ILE A 98 23.491 27.743 23.901 1.00125.57 C ANISOU 676 CB ILE A 98 14230 15666 17814 -113 -1171 -109 C ATOM 677 CG1 ILE A 98 23.351 26.369 24.559 1.00114.61 C ANISOU 677 CG1 ILE A 98 12929 14272 16345 -151 -1216 -276 C ATOM 678 CG2 ILE A 98 22.648 28.766 24.643 1.00129.38 C ANISOU 678 CG2 ILE A 98 14510 16024 18625 -75 -1062 11 C ATOM 679 CD1 ILE A 98 23.718 26.357 26.026 1.00107.03 C ANISOU 679 CD1 ILE A 98 11963 13214 15489 -114 -1041 -422 C ATOM 680 N ALA A 99 24.151 29.572 21.360 1.00145.84 N ANISOU 680 N ALA A 99 16799 18383 20229 -124 -1265 235 N ATOM 681 CA ALA A 99 24.212 30.887 20.735 1.00153.83 C ANISOU 681 CA ALA A 99 17720 19389 21339 -103 -1242 441 C ATOM 682 C ALA A 99 23.409 30.899 19.438 1.00163.46 C ANISOU 682 C ALA A 99 18926 20708 22474 -197 -1480 676 C ATOM 683 O ALA A 99 22.538 31.748 19.243 1.00171.92 O ANISOU 683 O ALA A 99 19817 21725 23779 -195 -1546 920 O ATOM 684 CB ALA A 99 25.657 31.286 20.474 1.00152.93 C ANISOU 684 CB ALA A 99 17723 19315 21069 -68 -1102 345 C ATOM 685 N ILE A 100 23.707 29.949 18.557 1.00162.69 N ANISOU 685 N ILE A 100 19020 20750 22046 -289 -1610 605 N ATOM 686 CA ILE A 100 22.991 29.815 17.294 1.00164.54 C ANISOU 686 CA ILE A 100 19285 21098 22132 -417 -1860 808 C ATOM 687 C ILE A 100 21.500 29.633 17.544 1.00158.97 C ANISOU 687 C ILE A 100 18405 20342 21656 -454 -2031 965 C ATOM 688 O ILE A 100 20.669 30.302 16.932 1.00158.03 O ANISOU 688 O ILE A 100 18149 20231 21666 -502 -2189 1250 O ATOM 689 CB ILE A 100 23.505 28.612 16.481 1.00167.99 C ANISOU 689 CB ILE A 100 19984 21676 22171 -524 -1946 641 C ATOM 690 CG1 ILE A 100 25.009 28.738 16.228 1.00172.03 C ANISOU 690 CG1 ILE A 100 20654 22230 22480 -483 -1754 477 C ATOM 691 CG2 ILE A 100 22.746 28.492 15.168 1.00168.37 C ANISOU 691 CG2 ILE A 100 20087 21851 22034 -689 -2217 850 C ATOM 692 CD1 ILE A 100 25.604 27.560 15.487 1.00174.91 C ANISOU 692 CD1 ILE A 100 21272 22704 22481 -575 -1783 281 C ATOM 693 N ASP A 101 21.175 28.718 18.452 1.00155.56 N ANISOU 693 N ASP A 101 17968 19852 21284 -436 -2002 791 N ATOM 694 CA ASP A 101 19.793 28.429 18.813 1.00156.50 C ANISOU 694 CA ASP A 101 17917 19913 21633 -470 -2137 910 C ATOM 695 C ASP A 101 19.031 29.695 19.190 1.00159.35 C ANISOU 695 C ASP A 101 18000 20148 22399 -397 -2084 1147 C ATOM 696 O ASP A 101 17.991 30.000 18.607 1.00162.27 O ANISOU 696 O ASP A 101 18217 20524 22915 -458 -2280 1413 O ATOM 697 CB ASP A 101 19.754 27.436 19.975 1.00155.94 C ANISOU 697 CB ASP A 101 17876 19773 21601 -437 -2038 668 C ATOM 698 CG ASP A 101 18.356 27.217 20.506 1.00159.26 C ANISOU 698 CG ASP A 101 18099 20114 22298 -460 -2126 782 C ATOM 699 OD1 ASP A 101 17.421 27.086 19.689 1.00164.87 O ANISOU 699 OD1 ASP A 101 18742 20882 23021 -561 -2369 985 O ATOM 700 OD2 ASP A 101 18.194 27.172 21.743 1.00156.55 O ANISOU 700 OD2 ASP A 101 17670 19654 22158 -389 -1954 672 O ATOM 701 N ARG A 102 19.555 30.427 20.168 1.00159.41 N ANISOU 701 N ARG A 102 17938 20032 22598 -273 -1820 1052 N ATOM 702 CA ARG A 102 18.918 31.655 20.628 1.00164.51 C ANISOU 702 CA ARG A 102 18328 20526 23653 -193 -1714 1236 C ATOM 703 C ARG A 102 18.772 32.671 19.500 1.00170.15 C ANISOU 703 C ARG A 102 18957 21273 24420 -216 -1843 1538 C ATOM 704 O ARG A 102 17.869 33.507 19.521 1.00177.96 O ANISOU 704 O ARG A 102 19701 22151 25765 -185 -1868 1780 O ATOM 705 CB ARG A 102 19.693 32.263 21.800 1.00159.34 C ANISOU 705 CB ARG A 102 17668 19744 23130 -80 -1399 1048 C ATOM 706 CG ARG A 102 19.637 31.439 23.082 1.00160.44 C ANISOU 706 CG ARG A 102 17847 19823 23291 -64 -1265 801 C ATOM 707 CD ARG A 102 18.230 31.397 23.670 1.00167.98 C ANISOU 707 CD ARG A 102 18585 20666 24574 -67 -1272 903 C ATOM 708 NE ARG A 102 17.303 30.622 22.849 1.00169.68 N ANISOU 708 NE ARG A 102 18766 20973 24731 -162 -1557 1054 N ATOM 709 CZ ARG A 102 16.004 30.497 23.100 1.00170.54 C ANISOU 709 CZ ARG A 102 18672 21008 25117 -183 -1622 1189 C ATOM 710 NH1 ARG A 102 15.470 31.097 24.154 1.00170.29 N ANISOU 710 NH1 ARG A 102 18454 20803 25444 -110 -1397 1182 N ATOM 711 NH2 ARG A 102 15.239 29.771 22.296 1.00173.23 N ANISOU 711 NH2 ARG A 102 18996 21445 25380 -287 -1906 1326 N ATOM 712 N TYR A 103 19.661 32.594 18.516 1.00163.25 N ANISOU 712 N TYR A 103 18282 20544 23202 -274 -1919 1529 N ATOM 713 CA TYR A 103 19.579 33.468 17.353 1.00159.56 C ANISOU 713 CA TYR A 103 17771 20133 22721 -325 -2064 1823 C ATOM 714 C TYR A 103 18.437 33.038 16.439 1.00158.40 C ANISOU 714 C TYR A 103 17567 20076 22541 -463 -2399 2069 C ATOM 715 O TYR A 103 17.697 33.873 15.921 1.00160.72 O ANISOU 715 O TYR A 103 17670 20331 23064 -483 -2539 2396 O ATOM 716 CB TYR A 103 20.899 33.467 16.579 1.00157.93 C ANISOU 716 CB TYR A 103 17812 20063 22131 -363 -2024 1725 C ATOM 717 CG TYR A 103 20.853 34.277 15.303 1.00161.51 C ANISOU 717 CG TYR A 103 18258 20599 22509 -444 -2187 2031 C ATOM 718 CD1 TYR A 103 21.025 35.655 15.327 1.00164.83 C ANISOU 718 CD1 TYR A 103 18528 20912 23188 -364 -2077 2216 C ATOM 719 CD2 TYR A 103 20.638 33.665 14.075 1.00162.94 C ANISOU 719 CD2 TYR A 103 18595 20962 22353 -615 -2451 2136 C ATOM 720 CE1 TYR A 103 20.983 36.400 14.165 1.00169.60 C ANISOU 720 CE1 TYR A 103 19125 21590 23727 -447 -2236 2518 C ATOM 721 CE2 TYR A 103 20.595 34.402 12.907 1.00167.61 C ANISOU 721 CE2 TYR A 103 19196 21639 22848 -713 -2611 2431 C ATOM 722 CZ TYR A 103 20.768 35.770 12.958 1.00171.32 C ANISOU 722 CZ TYR A 103 19504 22001 23588 -625 -2507 2631 C ATOM 723 OH TYR A 103 20.726 36.510 11.799 1.00174.36 O ANISOU 723 OH TYR A 103 19899 22470 23882 -729 -2676 2947 O ATOM 724 N ILE A 104 18.301 31.730 16.249 1.00155.93 N ANISOU 724 N ILE A 104 17417 19875 21954 -563 -2534 1918 N ATOM 725 CA ILE A 104 17.253 31.181 15.398 1.00161.83 C ANISOU 725 CA ILE A 104 18140 20718 22628 -721 -2867 2121 C ATOM 726 C ILE A 104 15.867 31.565 15.905 1.00170.63 C ANISOU 726 C ILE A 104 18924 21692 24214 -685 -2946 2351 C ATOM 727 O ILE A 104 14.976 31.885 15.119 1.00175.36 O ANISOU 727 O ILE A 104 19385 22324 24921 -781 -3212 2676 O ATOM 728 CB ILE A 104 17.350 29.647 15.306 1.00163.01 C ANISOU 728 CB ILE A 104 18519 20976 22440 -825 -2958 1870 C ATOM 729 CG1 ILE A 104 18.727 29.230 14.785 1.00166.98 C ANISOU 729 CG1 ILE A 104 19338 21601 22507 -856 -2857 1635 C ATOM 730 CG2 ILE A 104 16.249 29.094 14.414 1.00167.41 C ANISOU 730 CG2 ILE A 104 19058 21633 22916 -1011 -3318 2081 C ATOM 731 CD1 ILE A 104 18.928 27.731 14.714 1.00167.65 C ANISOU 731 CD1 ILE A 104 19653 21765 22282 -946 -2909 1365 C ATOM 732 N ALA A 105 15.692 31.534 17.222 1.00170.42 N ANISOU 732 N ALA A 105 18770 21510 24472 -556 -2712 2188 N ATOM 733 CA ALA A 105 14.406 31.857 17.831 1.00167.86 C ANISOU 733 CA ALA A 105 18127 21032 24621 -511 -2724 2366 C ATOM 734 C ALA A 105 13.993 33.299 17.554 1.00168.79 C ANISOU 734 C ALA A 105 17985 21034 25114 -447 -2721 2694 C ATOM 735 O ALA A 105 12.849 33.568 17.187 1.00173.70 O ANISOU 735 O ALA A 105 18363 21612 26024 -490 -2924 3001 O ATOM 736 CB ALA A 105 14.449 31.595 19.328 1.00163.95 C ANISOU 736 CB ALA A 105 17585 20394 24315 -395 -2425 2098 C ATOM 737 N ILE A 106 14.930 34.224 17.732 1.00166.25 N ANISOU 737 N ILE A 106 17704 20654 24809 -345 -2496 2637 N ATOM 738 CA ILE A 106 14.658 35.641 17.525 1.00167.87 C ANISOU 738 CA ILE A 106 17674 20726 25385 -272 -2459 2929 C ATOM 739 C ILE A 106 14.596 35.996 16.042 1.00175.60 C ANISOU 739 C ILE A 106 18683 21843 26193 -397 -2773 3257 C ATOM 740 O ILE A 106 13.687 36.699 15.600 1.00179.67 O ANISOU 740 O ILE A 106 18942 22283 27040 -410 -2941 3619 O ATOM 741 CB ILE A 106 15.713 36.524 18.218 1.00160.27 C ANISOU 741 CB ILE A 106 16756 19647 24491 -135 -2111 2752 C ATOM 742 CG1 ILE A 106 15.679 36.302 19.731 1.00155.73 C ANISOU 742 CG1 ILE A 106 16137 18921 24113 -31 -1803 2461 C ATOM 743 CG2 ILE A 106 15.485 37.990 17.887 1.00162.16 C ANISOU 743 CG2 ILE A 106 16769 19745 25101 -69 -2084 3062 C ATOM 744 CD1 ILE A 106 16.620 37.199 20.501 1.00154.26 C ANISOU 744 CD1 ILE A 106 15983 18606 24024 84 -1468 2289 C ATOM 745 N ALA A 107 15.566 35.505 15.277 1.00176.28 N ANISOU 745 N ALA A 107 19084 22128 25767 -495 -2849 3134 N ATOM 746 CA ALA A 107 15.629 35.784 13.846 1.00183.42 C ANISOU 746 CA ALA A 107 20076 23189 26426 -642 -3131 3414 C ATOM 747 C ALA A 107 14.445 35.173 13.104 1.00192.79 C ANISOU 747 C ALA A 107 21189 24472 27591 -811 -3518 3663 C ATOM 748 O ALA A 107 13.661 35.884 12.475 1.00196.02 O ANISOU 748 O ALA A 107 21388 24852 28238 -863 -3744 4059 O ATOM 749 CB ALA A 107 16.940 35.278 13.264 1.00181.53 C ANISOU 749 CB ALA A 107 20206 23137 25632 -716 -3083 3179 C ATOM 750 N ILE A 108 14.322 33.852 13.179 1.00195.07 N ANISOU 750 N ILE A 108 21646 24868 27604 -902 -3603 3439 N ATOM 751 CA ILE A 108 13.237 33.145 12.508 1.00199.48 C ANISOU 751 CA ILE A 108 22161 25525 28106 -1083 -3974 3637 C ATOM 752 C ILE A 108 12.456 32.280 13.494 1.00201.25 C ANISOU 752 C ILE A 108 22261 25658 28548 -1041 -3930 3476 C ATOM 753 O ILE A 108 12.720 31.084 13.621 1.00204.36 O ANISOU 753 O ILE A 108 22879 26144 28624 -1109 -3933 3192 O ATOM 754 CB ILE A 108 13.765 32.254 11.368 1.00197.23 C ANISOU 754 CB ILE A 108 22245 25490 27205 -1301 -4186 3546 C ATOM 755 CG1 ILE A 108 14.805 33.008 10.537 1.00187.73 C ANISOU 755 CG1 ILE A 108 21222 24382 25723 -1331 -4137 3611 C ATOM 756 CG2 ILE A 108 12.616 31.771 10.497 1.00203.70 C ANISOU 756 CG2 ILE A 108 23010 26415 27970 -1523 -4618 3827 C ATOM 757 CD1 ILE A 108 15.399 32.187 9.413 1.00182.37 C ANISOU 757 CD1 ILE A 108 20924 23941 24426 -1549 -4292 3498 C ATOM 758 N PRO A 109 11.488 32.888 14.195 1.00196.97 N ANISOU 758 N PRO A 109 21356 24922 28563 -930 -3876 3660 N ATOM 759 CA PRO A 109 10.681 32.194 15.205 1.00194.10 C ANISOU 759 CA PRO A 109 20837 24451 28463 -883 -3799 3532 C ATOM 760 C PRO A 109 9.819 31.085 14.607 1.00198.11 C ANISOU 760 C PRO A 109 21377 25087 28809 -1082 -4157 3617 C ATOM 761 O PRO A 109 9.574 30.077 15.269 1.00196.45 O ANISOU 761 O PRO A 109 21212 24865 28565 -1091 -4102 3387 O ATOM 762 CB PRO A 109 9.790 33.308 15.768 1.00191.93 C ANISOU 762 CB PRO A 109 20144 23944 28836 -746 -3697 3797 C ATOM 763 CG PRO A 109 9.772 34.358 14.707 1.00194.98 C ANISOU 763 CG PRO A 109 20443 24357 29285 -790 -3894 4172 C ATOM 764 CD PRO A 109 11.127 34.311 14.083 1.00195.25 C ANISOU 764 CD PRO A 109 20845 24559 28781 -839 -3858 4001 C ATOM 765 N LEU A 110 9.365 31.271 13.371 1.00205.43 N ANISOU 765 N LEU A 110 22288 26135 29632 -1254 -4529 3950 N ATOM 766 CA LEU A 110 8.505 30.290 12.717 1.00211.84 C ANISOU 766 CA LEU A 110 23128 27072 30288 -1474 -4906 4063 C ATOM 767 C LEU A 110 9.252 28.996 12.407 1.00210.45 C ANISOU 767 C LEU A 110 23371 27073 29518 -1606 -4933 3710 C ATOM 768 O LEU A 110 8.815 27.910 12.788 1.00208.88 O ANISOU 768 O LEU A 110 23209 26881 29277 -1665 -4981 3543 O ATOM 769 CB LEU A 110 7.899 30.871 11.436 1.00216.05 C ANISOU 769 CB LEU A 110 23560 27701 30829 -1648 -5314 4525 C ATOM 770 CG LEU A 110 6.929 32.042 11.611 1.00214.01 C ANISOU 770 CG LEU A 110 22840 27257 31216 -1547 -5368 4944 C ATOM 771 CD1 LEU A 110 6.457 32.557 10.260 1.00216.35 C ANISOU 771 CD1 LEU A 110 23078 27670 31456 -1744 -5806 5410 C ATOM 772 CD2 LEU A 110 5.746 31.635 12.476 1.00211.71 C ANISOU 772 CD2 LEU A 110 22227 26814 31400 -1493 -5356 4977 C ATOM 773 N ARG A 111 10.379 29.119 11.715 1.00210.05 N ANISOU 773 N ARG A 111 23627 27154 29028 -1651 -4890 3598 N ATOM 774 CA ARG A 111 11.178 27.956 11.345 1.00210.62 C ANISOU 774 CA ARG A 111 24101 27380 28546 -1771 -4885 3258 C ATOM 775 C ARG A 111 11.949 27.404 12.540 1.00208.87 C ANISOU 775 C ARG A 111 23977 27062 28321 -1592 -4508 2835 C ATOM 776 O ARG A 111 12.647 26.397 12.426 1.00212.98 O ANISOU 776 O ARG A 111 24801 27670 28452 -1654 -4454 2524 O ATOM 777 CB ARG A 111 12.145 28.308 10.213 1.00212.18 C ANISOU 777 CB ARG A 111 24584 27741 28295 -1878 -4931 3280 C ATOM 778 CG ARG A 111 11.466 28.739 8.924 1.00216.56 C ANISOU 778 CG ARG A 111 25105 28423 28754 -2102 -5337 3694 C ATOM 779 CD ARG A 111 10.599 27.626 8.359 1.00221.49 C ANISOU 779 CD ARG A 111 25816 29160 29179 -2353 -5693 3730 C ATOM 780 NE ARG A 111 11.349 26.385 8.187 1.00221.46 N ANISOU 780 NE ARG A 111 26204 29263 28679 -2451 -5608 3320 N ATOM 781 CZ ARG A 111 12.090 26.100 7.121 1.00223.14 C ANISOU 781 CZ ARG A 111 26780 29654 28349 -2634 -5674 3226 C ATOM 782 NH1 ARG A 111 12.188 26.971 6.126 1.00226.94 N ANISOU 782 NH1 ARG A 111 27297 30244 28686 -2752 -5839 3523 N ATOM 783 NH2 ARG A 111 12.737 24.944 7.051 1.00220.19 N ANISOU 783 NH2 ARG A 111 26735 29342 27586 -2704 -5563 2836 N ATOM 784 N TYR A 112 11.820 28.068 13.684 1.00202.26 N ANISOU 784 N TYR A 112 22885 26040 27925 -1378 -4246 2827 N ATOM 785 CA TYR A 112 12.498 27.637 14.901 1.00191.21 C ANISOU 785 CA TYR A 112 21559 24544 26550 -1218 -3899 2460 C ATOM 786 C TYR A 112 12.036 26.251 15.335 1.00187.91 C ANISOU 786 C TYR A 112 21212 24132 26053 -1293 -3965 2261 C ATOM 787 O TYR A 112 12.851 25.368 15.596 1.00186.18 O ANISOU 787 O TYR A 112 21247 23950 25543 -1289 -3836 1935 O ATOM 788 CB TYR A 112 12.269 28.645 16.030 1.00185.00 C ANISOU 788 CB TYR A 112 20476 23553 26262 -1011 -3628 2517 C ATOM 789 CG TYR A 112 12.805 28.197 17.371 1.00178.60 C ANISOU 789 CG TYR A 112 19723 22640 25498 -873 -3298 2168 C ATOM 790 CD1 TYR A 112 11.983 27.559 18.291 1.00177.90 C ANISOU 790 CD1 TYR A 112 19496 22455 25643 -858 -3256 2097 C ATOM 791 CD2 TYR A 112 14.132 28.410 17.717 1.00175.63 C ANISOU 791 CD2 TYR A 112 19536 22265 24931 -772 -3036 1923 C ATOM 792 CE1 TYR A 112 12.467 27.148 19.518 1.00175.57 C ANISOU 792 CE1 TYR A 112 19266 22074 25368 -754 -2969 1796 C ATOM 793 CE2 TYR A 112 14.625 28.003 18.942 1.00172.43 C ANISOU 793 CE2 TYR A 112 19184 21772 24560 -666 -2764 1628 C ATOM 794 CZ TYR A 112 13.789 27.372 19.837 1.00171.25 C ANISOU 794 CZ TYR A 112 18912 21534 24621 -662 -2735 1568 C ATOM 795 OH TYR A 112 14.275 26.964 21.058 1.00164.55 O ANISOU 795 OH TYR A 112 18129 20605 23785 -577 -2477 1291 O ATOM 796 N ASN A 113 10.722 26.066 15.411 1.00185.85 N ANISOU 796 N ASN A 113 20713 23825 26078 -1361 -4165 2470 N ATOM 797 CA ASN A 113 10.154 24.788 15.818 1.00180.92 C ANISOU 797 CA ASN A 113 20124 23196 25421 -1444 -4245 2318 C ATOM 798 C ASN A 113 10.322 23.715 14.746 1.00176.86 C ANISOU 798 C ASN A 113 19915 22857 24427 -1667 -4515 2231 C ATOM 799 O ASN A 113 10.229 22.521 15.030 1.00175.61 O ANISOU 799 O ASN A 113 19886 22704 24133 -1734 -4537 2015 O ATOM 800 CB ASN A 113 8.676 24.950 16.178 1.00183.74 C ANISOU 800 CB ASN A 113 20114 23449 26251 -1458 -4379 2586 C ATOM 801 CG ASN A 113 8.456 25.930 17.314 1.00180.27 C ANISOU 801 CG ASN A 113 19379 22813 26302 -1244 -4070 2635 C ATOM 802 OD1 ASN A 113 8.641 25.595 18.484 1.00177.82 O ANISOU 802 OD1 ASN A 113 19068 22400 26096 -1133 -3792 2391 O ATOM 803 ND2 ASN A 113 8.057 27.150 16.973 1.00179.26 N ANISOU 803 ND2 ASN A 113 19004 22627 26479 -1194 -4116 2952 N ATOM 804 N GLY A 114 10.573 24.148 13.515 1.00175.98 N ANISOU 804 N GLY A 114 19927 22883 24056 -1792 -4711 2398 N ATOM 805 CA GLY A 114 10.738 23.232 12.401 1.00179.84 C ANISOU 805 CA GLY A 114 20726 23542 24061 -2030 -4960 2322 C ATOM 806 C GLY A 114 12.168 22.753 12.237 1.00182.54 C ANISOU 806 C GLY A 114 21434 23950 23973 -2005 -4740 1964 C ATOM 807 O GLY A 114 12.408 21.609 11.850 1.00185.92 O ANISOU 807 O GLY A 114 22131 24450 24061 -2143 -4810 1739 O ATOM 808 N LEU A 115 13.119 23.633 12.531 1.00178.98 N ANISOU 808 N LEU A 115 20985 23462 23559 -1830 -4468 1912 N ATOM 809 CA LEU A 115 14.535 23.301 12.419 1.00169.92 C ANISOU 809 CA LEU A 115 20143 22361 22058 -1784 -4234 1594 C ATOM 810 C LEU A 115 15.094 22.834 13.758 1.00164.75 C ANISOU 810 C LEU A 115 19476 21570 21552 -1592 -3922 1288 C ATOM 811 O LEU A 115 15.626 21.730 13.869 1.00165.04 O ANISOU 811 O LEU A 115 19734 21616 21358 -1621 -3853 995 O ATOM 812 CB LEU A 115 15.327 24.505 11.908 1.00165.97 C ANISOU 812 CB LEU A 115 19665 21907 21488 -1724 -4128 1716 C ATOM 813 CG LEU A 115 14.925 25.038 10.532 1.00168.63 C ANISOU 813 CG LEU A 115 20044 22391 21635 -1926 -4429 2031 C ATOM 814 CD1 LEU A 115 15.658 26.333 10.217 1.00164.35 C ANISOU 814 CD1 LEU A 115 19475 21864 21106 -1837 -4295 2175 C ATOM 815 CD2 LEU A 115 15.181 23.995 9.454 1.00173.52 C ANISOU 815 CD2 LEU A 115 21022 23175 21734 -2169 -4592 1879 C ATOM 816 N VAL A 116 14.969 23.683 14.773 1.00160.88 N ANISOU 816 N VAL A 116 18730 20947 21450 -1404 -3735 1364 N ATOM 817 CA VAL A 116 15.436 23.353 16.113 1.00155.97 C ANISOU 817 CA VAL A 116 18082 20197 20981 -1237 -3451 1108 C ATOM 818 C VAL A 116 14.546 22.279 16.732 1.00166.87 C ANISOU 818 C VAL A 116 19403 21519 22482 -1290 -3540 1037 C ATOM 819 O VAL A 116 13.585 22.586 17.438 1.00174.80 O ANISOU 819 O VAL A 116 20141 22423 23853 -1242 -3542 1182 O ATOM 820 CB VAL A 116 15.447 24.595 17.025 1.00143.37 C ANISOU 820 CB VAL A 116 16237 18471 19765 -1050 -3228 1213 C ATOM 821 CG1 VAL A 116 16.120 24.278 18.348 1.00130.44 C ANISOU 821 CG1 VAL A 116 14628 16724 18208 -905 -2933 933 C ATOM 822 CG2 VAL A 116 16.150 25.751 16.333 1.00141.40 C ANISOU 822 CG2 VAL A 116 16012 18274 19441 -1014 -3178 1342 C ATOM 823 N THR A 117 14.871 21.020 16.459 1.00166.52 N ANISOU 823 N THR A 117 19603 21526 22141 -1390 -3600 810 N ATOM 824 CA THR A 117 14.073 19.901 16.946 1.00167.18 C ANISOU 824 CA THR A 117 19658 21557 22304 -1462 -3701 735 C ATOM 825 C THR A 117 14.786 19.154 18.068 1.00167.32 C ANISOU 825 C THR A 117 19767 21476 22330 -1346 -3455 433 C ATOM 826 O THR A 117 16.011 19.188 18.169 1.00164.66 O ANISOU 826 O THR A 117 19591 21142 21829 -1256 -3260 242 O ATOM 827 CB THR A 117 13.749 18.907 15.814 1.00167.25 C ANISOU 827 CB THR A 117 19873 21679 21994 -1692 -3985 712 C ATOM 828 OG1 THR A 117 14.955 18.272 15.371 1.00171.56 O ANISOU 828 OG1 THR A 117 20739 22275 22169 -1710 -3876 432 O ATOM 829 CG2 THR A 117 13.101 19.628 14.642 1.00166.34 C ANISOU 829 CG2 THR A 117 19695 21679 21828 -1836 -4260 1026 C ATOM 830 N GLY A 118 14.009 18.480 18.909 1.00170.86 N ANISOU 830 N GLY A 118 20103 21836 22979 -1355 -3472 407 N ATOM 831 CA GLY A 118 14.561 17.714 20.012 1.00171.58 C ANISOU 831 CA GLY A 118 20271 21832 23090 -1268 -3272 156 C ATOM 832 C GLY A 118 15.316 16.488 19.539 1.00170.80 C ANISOU 832 C GLY A 118 20467 21766 22664 -1343 -3307 -96 C ATOM 833 O GLY A 118 15.932 15.781 20.336 1.00161.99 O ANISOU 833 O GLY A 118 19440 20571 21537 -1275 -3156 -307 O ATOM 834 N THR A 119 15.261 16.233 18.235 1.00177.14 N ANISOU 834 N THR A 119 21423 22679 23203 -1493 -3506 -68 N ATOM 835 CA THR A 119 15.966 15.103 17.644 1.00177.60 C ANISOU 835 CA THR A 119 21776 22763 22943 -1580 -3525 -316 C ATOM 836 C THR A 119 17.315 15.540 17.082 1.00183.06 C ANISOU 836 C THR A 119 22644 23510 23398 -1513 -3359 -437 C ATOM 837 O THR A 119 18.343 14.922 17.361 1.00185.64 O ANISOU 837 O THR A 119 23127 23783 23625 -1442 -3185 -684 O ATOM 838 CB THR A 119 15.141 14.440 16.526 1.00172.97 C ANISOU 838 CB THR A 119 21297 22260 22165 -1818 -3828 -255 C ATOM 839 OG1 THR A 119 13.918 13.929 17.070 1.00169.38 O ANISOU 839 OG1 THR A 119 20673 21743 21941 -1885 -3980 -155 O ATOM 840 CG2 THR A 119 15.922 13.298 15.894 1.00171.73 C ANISOU 840 CG2 THR A 119 21462 22111 21676 -1910 -3809 -541 C ATOM 841 N ARG A 120 17.305 16.608 16.289 1.00183.50 N ANISOU 841 N ARG A 120 22665 23669 23386 -1538 -3415 -250 N ATOM 842 CA ARG A 120 18.537 17.150 15.729 1.00182.33 C ANISOU 842 CA ARG A 120 22665 23583 23030 -1480 -3253 -333 C ATOM 843 C ARG A 120 19.478 17.618 16.834 1.00177.09 C ANISOU 843 C ARG A 120 21917 22823 22545 -1261 -2963 -436 C ATOM 844 O ARG A 120 20.697 17.556 16.688 1.00174.27 O ANISOU 844 O ARG A 120 21708 22469 22038 -1194 -2783 -612 O ATOM 845 CB ARG A 120 18.238 18.304 14.769 1.00185.59 C ANISOU 845 CB ARG A 120 23023 24116 23376 -1550 -3379 -66 C ATOM 846 CG ARG A 120 17.577 17.882 13.467 1.00190.91 C ANISOU 846 CG ARG A 120 23844 24916 23778 -1799 -3669 25 C ATOM 847 CD ARG A 120 17.459 19.057 12.508 1.00195.44 C ANISOU 847 CD ARG A 120 24384 25613 24261 -1869 -3784 296 C ATOM 848 NE ARG A 120 16.888 18.665 11.223 1.00200.12 N ANISOU 848 NE ARG A 120 25145 26342 24549 -2136 -4076 389 N ATOM 849 CZ ARG A 120 16.717 19.493 10.197 1.00200.08 C ANISOU 849 CZ ARG A 120 25162 26467 24391 -2260 -4236 634 C ATOM 850 NH1 ARG A 120 16.190 19.050 9.064 1.00201.74 N ANISOU 850 NH1 ARG A 120 25549 26806 24298 -2530 -4517 709 N ATOM 851 NH2 ARG A 120 17.076 20.766 10.303 1.00197.08 N ANISOU 851 NH2 ARG A 120 24635 26087 24159 -2126 -4123 811 N ATOM 852 N ALA A 121 18.903 18.087 17.937 1.00175.81 N ANISOU 852 N ALA A 121 21517 22574 22707 -1160 -2916 -326 N ATOM 853 CA ALA A 121 19.692 18.534 19.078 1.00172.12 C ANISOU 853 CA ALA A 121 20972 22015 22410 -979 -2659 -416 C ATOM 854 C ALA A 121 20.549 17.395 19.616 1.00174.04 C ANISOU 854 C ALA A 121 21371 22187 22568 -938 -2540 -693 C ATOM 855 O ALA A 121 21.769 17.518 19.717 1.00177.82 O ANISOU 855 O ALA A 121 21939 22654 22971 -845 -2362 -830 O ATOM 856 CB ALA A 121 18.787 19.078 20.170 1.00169.62 C ANISOU 856 CB ALA A 121 20398 21611 22437 -914 -2631 -271 C ATOM 857 N ALA A 122 19.901 16.285 19.956 1.00173.02 N ANISOU 857 N ALA A 122 21263 22004 22473 -1010 -2645 -760 N ATOM 858 CA ALA A 122 20.606 15.114 20.463 1.00172.79 C ANISOU 858 CA ALA A 122 21371 21889 22393 -981 -2558 -1001 C ATOM 859 C ALA A 122 21.591 14.578 19.428 1.00177.36 C ANISOU 859 C ALA A 122 22189 22510 22691 -1019 -2524 -1179 C ATOM 860 O ALA A 122 22.576 13.926 19.774 1.00180.11 O ANISOU 860 O ALA A 122 22637 22782 23014 -948 -2385 -1376 O ATOM 861 CB ALA A 122 19.616 14.033 20.868 1.00170.24 C ANISOU 861 CB ALA A 122 21029 21502 22152 -1074 -2702 -1017 C ATOM 862 N GLY A 123 21.318 14.859 18.158 1.00176.05 N ANISOU 862 N GLY A 123 22110 22460 22319 -1139 -2648 -1103 N ATOM 863 CA GLY A 123 22.183 14.425 17.076 1.00172.43 C ANISOU 863 CA GLY A 123 21893 22053 21568 -1201 -2598 -1270 C ATOM 864 C GLY A 123 23.453 15.246 16.990 1.00164.22 C ANISOU 864 C GLY A 123 20871 21037 20489 -1073 -2375 -1312 C ATOM 865 O GLY A 123 24.549 14.699 16.872 1.00162.94 O ANISOU 865 O GLY A 123 20846 20829 20235 -1024 -2212 -1523 O ATOM 866 N ILE A 124 23.305 16.566 17.050 1.00157.90 N ANISOU 866 N ILE A 124 19918 20296 19781 -1020 -2363 -1105 N ATOM 867 CA ILE A 124 24.449 17.468 16.994 1.00151.55 C ANISOU 867 CA ILE A 124 19109 19514 18960 -905 -2161 -1116 C ATOM 868 C ILE A 124 25.341 17.294 18.218 1.00147.87 C ANISOU 868 C ILE A 124 18575 18925 18682 -740 -1964 -1254 C ATOM 869 O ILE A 124 26.565 17.251 18.102 1.00153.01 O ANISOU 869 O ILE A 124 19307 19559 19269 -668 -1788 -1394 O ATOM 870 CB ILE A 124 24.005 18.939 16.894 1.00153.35 C ANISOU 870 CB ILE A 124 19168 19807 19291 -883 -2197 -850 C ATOM 871 CG1 ILE A 124 23.129 19.147 15.657 1.00165.04 C ANISOU 871 CG1 ILE A 124 20704 21413 20589 -1058 -2424 -675 C ATOM 872 CG2 ILE A 124 25.215 19.859 16.852 1.00149.89 C ANISOU 872 CG2 ILE A 124 18727 19384 18842 -771 -1985 -867 C ATOM 873 CD1 ILE A 124 22.591 20.554 15.518 1.00171.57 C ANISOU 873 CD1 ILE A 124 21347 22289 21553 -1042 -2487 -382 C ATOM 874 N ILE A 125 24.719 17.193 19.389 1.00142.01 N ANISOU 874 N ILE A 125 17684 18100 18175 -693 -1996 -1205 N ATOM 875 CA ILE A 125 25.452 17.003 20.636 1.00142.57 C ANISOU 875 CA ILE A 125 17696 18060 18416 -566 -1844 -1312 C ATOM 876 C ILE A 125 26.381 15.796 20.560 1.00146.17 C ANISOU 876 C ILE A 125 18306 18447 18783 -550 -1771 -1544 C ATOM 877 O ILE A 125 27.557 15.883 20.913 1.00152.32 O ANISOU 877 O ILE A 125 19090 19181 19604 -448 -1608 -1640 O ATOM 878 CB ILE A 125 24.498 16.833 21.832 1.00140.19 C ANISOU 878 CB ILE A 125 17250 17682 18333 -561 -1907 -1240 C ATOM 879 CG1 ILE A 125 23.720 18.126 22.079 1.00141.33 C ANISOU 879 CG1 ILE A 125 17211 17858 18629 -545 -1919 -1024 C ATOM 880 CG2 ILE A 125 25.271 16.439 23.080 1.00137.88 C ANISOU 880 CG2 ILE A 125 16938 17282 18170 -466 -1777 -1359 C ATOM 881 CD1 ILE A 125 22.802 18.062 23.277 1.00140.78 C ANISOU 881 CD1 ILE A 125 16994 17708 18786 -541 -1934 -960 C ATOM 882 N ALA A 126 25.846 14.670 20.098 1.00138.28 N ANISOU 882 N ALA A 126 17425 17432 17684 -656 -1893 -1630 N ATOM 883 CA ALA A 126 26.635 13.454 19.951 1.00134.27 C ANISOU 883 CA ALA A 126 17066 16836 17115 -649 -1822 -1856 C ATOM 884 C ALA A 126 27.828 13.695 19.034 1.00142.43 C ANISOU 884 C ALA A 126 18217 17911 17989 -617 -1658 -1966 C ATOM 885 O ALA A 126 28.952 13.304 19.348 1.00145.94 O ANISOU 885 O ALA A 126 18681 18266 18502 -519 -1499 -2107 O ATOM 886 CB ALA A 126 25.773 12.323 19.418 1.00131.36 C ANISOU 886 CB ALA A 126 16819 16450 16641 -793 -1985 -1925 C ATOM 887 N ILE A 127 27.577 14.341 17.899 1.00143.45 N ANISOU 887 N ILE A 127 18418 18173 17914 -708 -1699 -1889 N ATOM 888 CA ILE A 127 28.639 14.667 16.955 1.00140.75 C ANISOU 888 CA ILE A 127 18195 17887 17398 -698 -1533 -1977 C ATOM 889 C ILE A 127 29.675 15.576 17.606 1.00135.50 C ANISOU 889 C ILE A 127 17394 17199 16889 -538 -1352 -1939 C ATOM 890 O ILE A 127 30.878 15.377 17.444 1.00134.72 O ANISOU 890 O ILE A 127 17347 17056 16785 -467 -1164 -2082 O ATOM 891 CB ILE A 127 28.087 15.359 15.696 1.00142.04 C ANISOU 891 CB ILE A 127 18447 18213 17309 -841 -1634 -1848 C ATOM 892 CG1 ILE A 127 27.072 14.458 14.992 1.00146.09 C ANISOU 892 CG1 ILE A 127 19108 18756 17645 -1028 -1835 -1884 C ATOM 893 CG2 ILE A 127 29.221 15.727 14.751 1.00143.20 C ANISOU 893 CG2 ILE A 127 18724 18421 17266 -839 -1439 -1937 C ATOM 894 CD1 ILE A 127 26.465 15.078 13.752 1.00151.22 C ANISOU 894 CD1 ILE A 127 19854 19573 18032 -1200 -1977 -1735 C ATOM 895 N CYS A 128 29.196 16.573 18.343 1.00133.64 N ANISOU 895 N CYS A 128 16980 16987 16809 -488 -1405 -1747 N ATOM 896 CA CYS A 128 30.076 17.508 19.033 1.00138.05 C ANISOU 896 CA CYS A 128 17409 17524 17522 -356 -1253 -1701 C ATOM 897 C CYS A 128 31.015 16.781 19.988 1.00143.61 C ANISOU 897 C CYS A 128 18083 18095 18388 -251 -1142 -1851 C ATOM 898 O CYS A 128 32.207 17.079 20.042 1.00147.64 O ANISOU 898 O CYS A 128 18571 18582 18942 -165 -978 -1909 O ATOM 899 CB CYS A 128 29.260 18.558 19.790 1.00136.83 C ANISOU 899 CB CYS A 128 17076 17386 17529 -334 -1328 -1494 C ATOM 900 SG CYS A 128 28.291 19.658 18.731 1.00156.00 S ANISOU 900 SG CYS A 128 19483 19953 19838 -433 -1452 -1264 S ATOM 901 N TRP A 129 30.474 15.827 20.739 1.00142.43 N ANISOU 901 N TRP A 129 17922 17856 18338 -264 -1240 -1897 N ATOM 902 CA TRP A 129 31.279 15.043 21.670 1.00145.24 C ANISOU 902 CA TRP A 129 18249 18079 18856 -180 -1170 -2013 C ATOM 903 C TRP A 129 32.321 14.198 20.946 1.00150.49 C ANISOU 903 C TRP A 129 19035 18686 19460 -155 -1043 -2205 C ATOM 904 O TRP A 129 33.467 14.107 21.382 1.00151.36 O ANISOU 904 O TRP A 129 19091 18718 19702 -55 -914 -2268 O ATOM 905 CB TRP A 129 30.392 14.156 22.545 1.00140.52 C ANISOU 905 CB TRP A 129 17628 17399 18363 -219 -1312 -2008 C ATOM 906 CG TRP A 129 29.761 14.891 23.682 1.00139.81 C ANISOU 906 CG TRP A 129 17392 17316 18412 -207 -1364 -1856 C ATOM 907 CD1 TRP A 129 28.492 15.385 23.736 1.00140.07 C ANISOU 907 CD1 TRP A 129 17366 17408 18445 -274 -1473 -1719 C ATOM 908 CD2 TRP A 129 30.376 15.223 24.934 1.00145.87 C ANISOU 908 CD2 TRP A 129 18056 18022 19345 -132 -1297 -1829 C ATOM 909 NE1 TRP A 129 28.275 16.001 24.945 1.00141.60 N ANISOU 909 NE1 TRP A 129 17432 17573 18797 -240 -1450 -1626 N ATOM 910 CE2 TRP A 129 29.416 15.915 25.698 1.00143.25 C ANISOU 910 CE2 TRP A 129 17625 17715 19089 -164 -1348 -1695 C ATOM 911 CE3 TRP A 129 31.643 15.000 25.481 1.00150.63 C ANISOU 911 CE3 TRP A 129 18638 18549 20046 -52 -1201 -1901 C ATOM 912 CZ2 TRP A 129 29.685 16.388 26.982 1.00145.23 C ANISOU 912 CZ2 TRP A 129 17785 17922 19474 -132 -1297 -1649 C ATOM 913 CZ3 TRP A 129 31.907 15.470 26.756 1.00149.10 C ANISOU 913 CZ3 TRP A 129 18345 18321 19987 -24 -1184 -1834 C ATOM 914 CH2 TRP A 129 30.933 16.155 27.492 1.00147.90 C ANISOU 914 CH2 TRP A 129 18124 18200 19872 -71 -1227 -1719 C ATOM 915 N VAL A 130 31.917 13.579 19.841 1.00150.85 N ANISOU 915 N VAL A 130 19242 18763 19312 -255 -1077 -2296 N ATOM 916 CA VAL A 130 32.834 12.775 19.043 1.00149.93 C ANISOU 916 CA VAL A 130 19261 18584 19122 -248 -925 -2501 C ATOM 917 C VAL A 130 33.985 13.627 18.520 1.00152.92 C ANISOU 917 C VAL A 130 19623 19017 19463 -180 -723 -2512 C ATOM 918 O VAL A 130 35.143 13.211 18.555 1.00157.31 O ANISOU 918 O VAL A 130 20169 19474 20127 -92 -549 -2641 O ATOM 919 CB VAL A 130 32.117 12.099 17.860 1.00148.79 C ANISOU 919 CB VAL A 130 19321 18484 18727 -403 -996 -2599 C ATOM 920 CG1 VAL A 130 33.129 11.475 16.911 1.00144.36 C ANISOU 920 CG1 VAL A 130 18917 17871 18064 -405 -786 -2823 C ATOM 921 CG2 VAL A 130 31.134 11.055 18.365 1.00153.35 C ANISOU 921 CG2 VAL A 130 19919 18978 19370 -468 -1175 -2622 C ATOM 922 N LEU A 131 33.661 14.825 18.043 1.00151.36 N ANISOU 922 N LEU A 131 19409 18967 19134 -222 -746 -2363 N ATOM 923 CA LEU A 131 34.676 15.748 17.549 1.00151.90 C ANISOU 923 CA LEU A 131 19456 19096 19162 -170 -562 -2346 C ATOM 924 C LEU A 131 35.518 16.294 18.699 1.00158.40 C ANISOU 924 C LEU A 131 20085 19851 20249 -28 -485 -2286 C ATOM 925 O LEU A 131 36.673 16.675 18.508 1.00164.03 O ANISOU 925 O LEU A 131 20760 20553 21011 43 -304 -2326 O ATOM 926 CB LEU A 131 34.030 16.900 16.778 1.00146.86 C ANISOU 926 CB LEU A 131 18845 18626 18330 -260 -632 -2174 C ATOM 927 CG LEU A 131 33.181 16.523 15.563 1.00150.17 C ANISOU 927 CG LEU A 131 19460 19142 18456 -432 -738 -2194 C ATOM 928 CD1 LEU A 131 32.675 17.774 14.863 1.00151.41 C ANISOU 928 CD1 LEU A 131 19614 19459 18457 -512 -812 -1983 C ATOM 929 CD2 LEU A 131 33.971 15.651 14.600 1.00151.63 C ANISOU 929 CD2 LEU A 131 19842 19297 18475 -477 -561 -2430 C ATOM 930 N SER A 132 34.932 16.328 19.892 1.00157.18 N ANISOU 930 N SER A 132 19812 19650 20258 -2 -623 -2191 N ATOM 931 CA SER A 132 35.626 16.820 21.077 1.00158.04 C ANISOU 931 CA SER A 132 19757 19698 20594 100 -580 -2131 C ATOM 932 C SER A 132 36.718 15.856 21.525 1.00154.48 C ANISOU 932 C SER A 132 19277 19105 20313 183 -489 -2267 C ATOM 933 O SER A 132 37.748 16.275 22.051 1.00150.84 O ANISOU 933 O SER A 132 18702 18604 20007 265 -396 -2246 O ATOM 934 CB SER A 132 34.638 17.061 22.220 1.00162.09 C ANISOU 934 CB SER A 132 20178 20200 21209 80 -741 -2006 C ATOM 935 OG SER A 132 33.724 18.095 21.899 1.00165.94 O ANISOU 935 OG SER A 132 20646 20798 21607 24 -805 -1859 O ATOM 936 N PHE A 133 36.487 14.564 21.318 1.00155.17 N ANISOU 936 N PHE A 133 19461 19107 20390 157 -524 -2396 N ATOM 937 CA PHE A 133 37.475 13.548 21.664 1.00158.21 C ANISOU 937 CA PHE A 133 19816 19333 20966 238 -438 -2522 C ATOM 938 C PHE A 133 38.553 13.434 20.591 1.00166.37 C ANISOU 938 C PHE A 133 20905 20348 21961 277 -209 -2661 C ATOM 939 O PHE A 133 39.721 13.192 20.895 1.00168.75 O ANISOU 939 O PHE A 133 21106 20542 22469 376 -84 -2710 O ATOM 940 CB PHE A 133 36.805 12.191 21.893 1.00154.96 C ANISOU 940 CB PHE A 133 19481 18812 20587 196 -555 -2607 C ATOM 941 CG PHE A 133 36.178 12.045 23.250 1.00156.79 C ANISOU 941 CG PHE A 133 19620 19001 20953 188 -735 -2488 C ATOM 942 CD1 PHE A 133 36.920 11.578 24.323 1.00154.72 C ANISOU 942 CD1 PHE A 133 19244 18609 20933 262 -748 -2470 C ATOM 943 CD2 PHE A 133 34.847 12.372 23.455 1.00163.95 C ANISOU 943 CD2 PHE A 133 20548 19996 21749 99 -891 -2386 C ATOM 944 CE1 PHE A 133 36.349 11.441 25.574 1.00157.67 C ANISOU 944 CE1 PHE A 133 19555 18953 21400 233 -907 -2359 C ATOM 945 CE2 PHE A 133 34.269 12.238 24.704 1.00165.56 C ANISOU 945 CE2 PHE A 133 20675 20161 22069 82 -1027 -2286 C ATOM 946 CZ PHE A 133 35.021 11.772 25.765 1.00164.33 C ANISOU 946 CZ PHE A 133 20433 19887 22119 142 -1033 -2277 C ATOM 947 N ALA A 134 38.156 13.611 19.335 1.00166.21 N ANISOU 947 N ALA A 134 21043 20433 21677 189 -154 -2718 N ATOM 948 CA ALA A 134 39.099 13.566 18.224 1.00164.17 C ANISOU 948 CA ALA A 134 20866 20175 21335 200 88 -2858 C ATOM 949 C ALA A 134 40.087 14.724 18.315 1.00162.99 C ANISOU 949 C ALA A 134 20581 20080 21268 278 224 -2763 C ATOM 950 O ALA A 134 41.285 14.550 18.094 1.00165.14 O ANISOU 950 O ALA A 134 20801 20274 21671 357 432 -2858 O ATOM 951 CB ALA A 134 38.360 13.599 16.896 1.00161.99 C ANISOU 951 CB ALA A 134 20810 20025 20715 54 88 -2914 C ATOM 952 N ILE A 135 39.573 15.905 18.644 1.00159.34 N ANISOU 952 N ILE A 135 20052 19741 20748 253 111 -2576 N ATOM 953 CA ILE A 135 40.402 17.096 18.780 1.00155.97 C ANISOU 953 CA ILE A 135 19497 19367 20397 311 218 -2471 C ATOM 954 C ILE A 135 41.124 17.129 20.123 1.00147.94 C ANISOU 954 C ILE A 135 18282 18242 19688 415 191 -2416 C ATOM 955 O ILE A 135 42.345 17.258 20.179 1.00141.51 O ANISOU 955 O ILE A 135 17363 17370 19035 494 345 -2444 O ATOM 956 CB ILE A 135 39.566 18.382 18.628 1.00153.06 C ANISOU 956 CB ILE A 135 19130 19153 19874 243 114 -2288 C ATOM 957 CG1 ILE A 135 39.006 18.490 17.208 1.00151.45 C ANISOU 957 CG1 ILE A 135 19115 19072 19356 125 137 -2309 C ATOM 958 CG2 ILE A 135 40.400 19.606 18.969 1.00149.77 C ANISOU 958 CG2 ILE A 135 18566 18764 19576 305 208 -2175 C ATOM 959 CD1 ILE A 135 38.153 19.720 16.979 1.00146.45 C ANISOU 959 CD1 ILE A 135 18471 18578 18594 56 20 -2105 C ATOM 960 N GLY A 136 40.358 17.007 21.203 1.00146.14 N ANISOU 960 N GLY A 136 18004 17987 19537 402 -9 -2332 N ATOM 961 CA GLY A 136 40.906 17.063 22.546 1.00139.61 C ANISOU 961 CA GLY A 136 17014 17073 18958 464 -71 -2262 C ATOM 962 C GLY A 136 41.961 16.008 22.817 1.00136.24 C ANISOU 962 C GLY A 136 16519 16488 18756 545 2 -2364 C ATOM 963 O GLY A 136 42.804 16.177 23.698 1.00136.55 O ANISOU 963 O GLY A 136 16406 16462 19014 601 -8 -2300 O ATOM 964 N LEU A 137 41.914 14.914 22.064 1.00136.86 N ANISOU 964 N LEU A 137 16708 16497 18794 546 72 -2518 N ATOM 965 CA LEU A 137 42.889 13.840 22.226 1.00140.33 C ANISOU 965 CA LEU A 137 17078 16760 19481 632 162 -2623 C ATOM 966 C LEU A 137 43.738 13.654 20.971 1.00144.60 C ANISOU 966 C LEU A 137 17671 17276 19995 668 434 -2778 C ATOM 967 O LEU A 137 44.173 12.545 20.663 1.00139.06 O ANISOU 967 O LEU A 137 16991 16425 19419 712 542 -2927 O ATOM 968 CB LEU A 137 42.196 12.528 22.600 1.00134.64 C ANISOU 968 CB LEU A 137 16428 15923 18807 609 28 -2688 C ATOM 969 CG LEU A 137 41.446 12.518 23.933 1.00120.32 C ANISOU 969 CG LEU A 137 14558 14107 17050 572 -221 -2545 C ATOM 970 CD1 LEU A 137 40.839 11.149 24.193 1.00111.73 C ANISOU 970 CD1 LEU A 137 13541 12892 16017 548 -331 -2615 C ATOM 971 CD2 LEU A 137 42.370 12.921 25.072 1.00115.86 C ANISOU 971 CD2 LEU A 137 13802 13493 16726 629 -264 -2417 C ATOM 972 N THR A 138 43.966 14.748 20.250 1.00151.48 N ANISOU 972 N THR A 138 18563 18285 20707 644 556 -2744 N ATOM 973 CA THR A 138 44.842 14.732 19.082 1.00155.13 C ANISOU 973 CA THR A 138 19071 18740 21130 667 840 -2877 C ATOM 974 C THR A 138 46.295 14.431 19.460 1.00155.88 C ANISOU 974 C THR A 138 18965 18681 21584 794 997 -2904 C ATOM 975 O THR A 138 46.986 13.711 18.741 1.00157.41 O ANISOU 975 O THR A 138 19183 18766 21861 838 1227 -3071 O ATOM 976 CB THR A 138 44.776 16.060 18.297 1.00153.52 C ANISOU 976 CB THR A 138 18924 18725 20684 604 922 -2799 C ATOM 977 OG1 THR A 138 43.449 16.256 17.794 1.00153.30 O ANISOU 977 OG1 THR A 138 19080 18830 20339 482 783 -2771 O ATOM 978 CG2 THR A 138 45.754 16.040 17.133 1.00152.11 C ANISOU 978 CG2 THR A 138 18792 18539 20466 619 1238 -2936 C ATOM 979 N PRO A 139 46.769 14.991 20.587 1.00150.45 N ANISOU 979 N PRO A 139 18074 17976 21116 845 877 -2740 N ATOM 980 CA PRO A 139 48.116 14.659 21.060 1.00149.97 C ANISOU 980 CA PRO A 139 17795 17759 21429 957 976 -2732 C ATOM 981 C PRO A 139 48.316 13.155 21.230 1.00150.85 C ANISOU 981 C PRO A 139 17886 17661 21767 1021 990 -2850 C ATOM 982 O PRO A 139 49.439 12.668 21.101 1.00158.04 O ANISOU 982 O PRO A 139 18655 18420 22972 1118 1168 -2910 O ATOM 983 CB PRO A 139 48.186 15.356 22.420 1.00148.57 C ANISOU 983 CB PRO A 139 17456 17610 21385 953 746 -2525 C ATOM 984 CG PRO A 139 47.267 16.513 22.285 1.00145.91 C ANISOU 984 CG PRO A 139 17229 17465 20744 859 662 -2440 C ATOM 985 CD PRO A 139 46.143 16.041 21.411 1.00144.34 C ANISOU 985 CD PRO A 139 17262 17326 20256 792 665 -2553 C ATOM 986 N MET A 140 47.240 12.431 21.518 1.00150.04 N ANISOU 986 N MET A 140 17914 17539 21555 967 810 -2877 N ATOM 987 CA MET A 140 47.320 10.983 21.676 1.00150.28 C ANISOU 987 CA MET A 140 17942 17361 21795 1016 811 -2986 C ATOM 988 C MET A 140 47.448 10.295 20.323 1.00155.44 C ANISOU 988 C MET A 140 18753 17950 22357 1017 1088 -3232 C ATOM 989 O MET A 140 47.848 9.133 20.241 1.00155.17 O ANISOU 989 O MET A 140 18694 17707 22556 1082 1188 -3359 O ATOM 990 CB MET A 140 46.098 10.448 22.425 1.00142.19 C ANISOU 990 CB MET A 140 17011 16338 20677 945 530 -2932 C ATOM 991 CG MET A 140 45.958 10.986 23.838 1.00135.64 C ANISOU 991 CG MET A 140 16046 15552 19939 928 271 -2708 C ATOM 992 SD MET A 140 44.744 10.074 24.810 1.00155.94 S ANISOU 992 SD MET A 140 18696 18068 22488 858 -19 -2654 S ATOM 993 CE MET A 140 45.454 8.431 24.776 1.00152.93 C ANISOU 993 CE MET A 140 18249 17400 22457 955 60 -2769 C ATOM 994 N LEU A 141 47.109 11.020 19.262 1.00160.62 N ANISOU 994 N LEU A 141 19577 18779 22673 935 1215 -3297 N ATOM 995 CA LEU A 141 47.201 10.484 17.910 1.00170.12 C ANISOU 995 CA LEU A 141 20968 19951 23720 899 1488 -3537 C ATOM 996 C LEU A 141 48.648 10.477 17.423 1.00185.60 C ANISOU 996 C LEU A 141 22792 21800 25927 1004 1822 -3628 C ATOM 997 O LEU A 141 49.042 9.610 16.641 1.00193.76 O ANISOU 997 O LEU A 141 23908 22693 27020 1023 2080 -3849 O ATOM 998 CB LEU A 141 46.318 11.283 16.947 1.00165.59 C ANISOU 998 CB LEU A 141 20627 19612 22675 752 1484 -3548 C ATOM 999 CG LEU A 141 44.828 11.368 17.293 1.00155.40 C ANISOU 999 CG LEU A 141 19466 18442 21139 640 1171 -3453 C ATOM 1000 CD1 LEU A 141 44.091 12.279 16.318 1.00150.02 C ANISOU 1000 CD1 LEU A 141 18973 17989 20037 502 1167 -3425 C ATOM 1001 CD2 LEU A 141 44.194 9.982 17.325 1.00150.30 C ANISOU 1001 CD2 LEU A 141 18939 17652 20516 609 1096 -3596 C ATOM 1002 N GLY A 142 49.434 11.445 17.889 1.00188.99 N ANISOU 1002 N GLY A 142 23012 22285 26512 1065 1828 -3462 N ATOM 1003 CA GLY A 142 50.839 11.526 17.527 1.00188.06 C ANISOU 1003 CA GLY A 142 22723 22064 26669 1167 2131 -3514 C ATOM 1004 C GLY A 142 51.477 12.870 17.826 1.00183.09 C ANISOU 1004 C GLY A 142 21920 21563 26083 1184 2123 -3325 C ATOM 1005 O GLY A 142 52.702 12.997 17.836 1.00182.07 O ANISOU 1005 O GLY A 142 21578 21338 26261 1279 2313 -3310 O ATOM 1006 N TRP A 143 50.645 13.878 18.069 1.00182.73 N ANISOU 1006 N TRP A 143 21956 21723 25750 1091 1908 -3178 N ATOM 1007 CA TRP A 143 51.125 15.231 18.330 1.00179.72 C ANISOU 1007 CA TRP A 143 21438 21469 25377 1088 1891 -3002 C ATOM 1008 C TRP A 143 51.543 15.386 19.789 1.00171.77 C ANISOU 1008 C TRP A 143 20182 20389 24694 1150 1656 -2812 C ATOM 1009 O TRP A 143 50.910 16.119 20.548 1.00166.62 O ANISOU 1009 O TRP A 143 19531 19849 23928 1090 1409 -2657 O ATOM 1010 CB TRP A 143 50.036 16.252 17.990 1.00185.71 C ANISOU 1010 CB TRP A 143 22384 22457 25721 962 1763 -2920 C ATOM 1011 CG TRP A 143 50.537 17.658 17.846 1.00192.11 C ANISOU 1011 CG TRP A 143 23108 23399 26488 944 1831 -2785 C ATOM 1012 CD1 TRP A 143 51.308 18.349 18.734 1.00196.18 C ANISOU 1012 CD1 TRP A 143 23386 23891 27263 997 1765 -2629 C ATOM 1013 CD2 TRP A 143 50.282 18.552 16.755 1.00196.39 C ANISOU 1013 CD2 TRP A 143 23805 24112 26703 854 1964 -2784 C ATOM 1014 NE1 TRP A 143 51.559 19.614 18.259 1.00200.26 N ANISOU 1014 NE1 TRP A 143 23896 24544 27649 953 1863 -2541 N ATOM 1015 CE2 TRP A 143 50.939 19.764 17.046 1.00199.32 C ANISOU 1015 CE2 TRP A 143 24014 24546 27174 868 1985 -2626 C ATOM 1016 CE3 TRP A 143 49.566 18.444 15.559 1.00198.19 C ANISOU 1016 CE3 TRP A 143 24297 24446 26559 748 2056 -2891 C ATOM 1017 CZ2 TRP A 143 50.901 20.859 16.186 1.00199.29 C ANISOU 1017 CZ2 TRP A 143 24096 24697 26927 792 2102 -2567 C ATOM 1018 CZ3 TRP A 143 49.530 19.532 14.706 1.00199.08 C ANISOU 1018 CZ3 TRP A 143 24500 24724 26416 664 2159 -2822 C ATOM 1019 CH2 TRP A 143 50.193 20.724 15.023 1.00199.18 C ANISOU 1019 CH2 TRP A 143 24339 24788 26551 692 2185 -2658 C ATOM 1020 N ASN A 144 52.611 14.696 20.177 1.00173.81 N ANISOU 1020 N ASN A 144 20225 20454 25361 1260 1737 -2823 N ATOM 1021 CA ASN A 144 53.078 14.733 21.560 1.00172.96 C ANISOU 1021 CA ASN A 144 19880 20268 25570 1301 1498 -2633 C ATOM 1022 C ASN A 144 54.598 14.816 21.688 1.00175.80 C ANISOU 1022 C ASN A 144 19950 20503 26343 1401 1653 -2578 C ATOM 1023 O ASN A 144 55.326 14.647 20.708 1.00174.99 O ANISOU 1023 O ASN A 144 19818 20339 26331 1459 1980 -2711 O ATOM 1024 CB ASN A 144 52.547 13.522 22.332 1.00169.75 C ANISOU 1024 CB ASN A 144 19488 19721 25288 1318 1288 -2639 C ATOM 1025 CG ASN A 144 52.986 12.204 21.724 1.00171.85 C ANISOU 1025 CG ASN A 144 19745 19774 25775 1409 1503 -2822 C ATOM 1026 OD1 ASN A 144 54.141 12.043 21.329 1.00184.51 O ANISOU 1026 OD1 ASN A 144 21178 21255 27671 1503 1747 -2870 O ATOM 1027 ND2 ASN A 144 52.065 11.251 21.650 1.00162.15 N ANISOU 1027 ND2 ASN A 144 18694 18490 24427 1380 1424 -2930 N ATOM 1028 N ASN A 145 55.068 15.078 22.904 1.00170.64 N ANISOU 1028 N ASN A 145 19083 19813 25940 1408 1419 -2378 N ATOM 1029 CA ASN A 145 56.499 15.167 23.174 1.00164.97 C ANISOU 1029 CA ASN A 145 18057 18974 25649 1490 1507 -2285 C ATOM 1030 C ASN A 145 56.996 14.015 24.041 1.00177.25 C ANISOU 1030 C ASN A 145 19414 20305 27629 1568 1361 -2212 C ATOM 1031 O ASN A 145 57.825 14.209 24.932 1.00188.23 O ANISOU 1031 O ASN A 145 20551 21634 29336 1581 1206 -2024 O ATOM 1032 CB ASN A 145 56.842 16.504 23.836 1.00151.23 C ANISOU 1032 CB ASN A 145 16202 17369 23892 1419 1358 -2090 C ATOM 1033 CG ASN A 145 56.718 17.677 22.884 1.00138.29 C ANISOU 1033 CG ASN A 145 14684 15909 21950 1367 1560 -2139 C ATOM 1034 OD1 ASN A 145 56.526 17.499 21.681 1.00137.51 O ANISOU 1034 OD1 ASN A 145 14738 15837 21672 1384 1828 -2311 O ATOM 1035 ND2 ASN A 145 56.831 18.887 23.420 1.00126.21 N ANISOU 1035 ND2 ASN A 145 13094 14499 20359 1291 1429 -1986 N ATOM 1036 N CYS A 146 56.487 12.816 23.777 1.00178.43 N ANISOU 1036 N CYS A 146 19679 20328 27787 1610 1398 -2353 N ATOM 1037 CA CYS A 146 56.878 11.634 24.537 1.00183.79 C ANISOU 1037 CA CYS A 146 20183 20774 28874 1686 1264 -2284 C ATOM 1038 C CYS A 146 58.305 11.200 24.212 1.00188.64 C ANISOU 1038 C CYS A 146 20503 21177 29995 1825 1510 -2293 C ATOM 1039 O CYS A 146 58.566 10.641 23.146 1.00192.63 O ANISOU 1039 O CYS A 146 21049 21572 30569 1906 1857 -2507 O ATOM 1040 CB CYS A 146 55.908 10.479 24.273 1.00185.32 C ANISOU 1040 CB CYS A 146 20592 20881 28939 1689 1256 -2445 C ATOM 1041 SG CYS A 146 54.217 10.756 24.855 1.00228.52 S ANISOU 1041 SG CYS A 146 26357 26554 33915 1534 929 -2403 S ATOM 1042 N GLY A 147 59.225 11.461 25.135 1.00187.66 N ANISOU 1042 N GLY A 147 20081 20993 30228 1843 1334 -2061 N ATOM 1043 CA GLY A 147 60.603 11.033 24.979 1.00189.28 C ANISOU 1043 CA GLY A 147 19955 20980 30983 1977 1525 -2025 C ATOM 1044 C GLY A 147 61.478 12.021 24.232 1.00191.82 C ANISOU 1044 C GLY A 147 20159 21381 31342 1998 1813 -2052 C ATOM 1045 O GLY A 147 62.552 11.665 23.747 1.00193.50 O ANISOU 1045 O GLY A 147 20135 21417 31970 2118 2091 -2092 O ATOM 1046 N GLN A 148 61.022 13.265 24.134 1.00192.52 N ANISOU 1046 N GLN A 148 20405 21725 31017 1881 1761 -2027 N ATOM 1047 CA GLN A 148 61.797 14.304 23.465 1.00197.04 C ANISOU 1047 CA GLN A 148 20881 22391 31596 1881 2012 -2031 C ATOM 1048 C GLN A 148 62.977 14.742 24.325 1.00200.25 C ANISOU 1048 C GLN A 148 20919 22735 32433 1892 1858 -1780 C ATOM 1049 O GLN A 148 62.863 14.821 25.548 1.00200.57 O ANISOU 1049 O GLN A 148 20883 22790 32533 1821 1468 -1573 O ATOM 1050 CB GLN A 148 60.913 15.507 23.125 1.00189.45 C ANISOU 1050 CB GLN A 148 20196 21707 30077 1750 1984 -2063 C ATOM 1051 CG GLN A 148 59.828 15.210 22.102 1.00183.19 C ANISOU 1051 CG GLN A 148 19756 20996 28851 1724 2160 -2300 C ATOM 1052 CD GLN A 148 60.388 14.802 20.753 1.00183.18 C ANISOU 1052 CD GLN A 148 19771 20906 28923 1805 2623 -2521 C ATOM 1053 OE1 GLN A 148 61.548 15.072 20.441 1.00188.20 O ANISOU 1053 OE1 GLN A 148 20173 21471 29865 1870 2855 -2497 O ATOM 1054 NE2 GLN A 148 59.562 14.151 19.942 1.00180.01 N ANISOU 1054 NE2 GLN A 148 19651 20508 28236 1789 2766 -2741 N ATOM 1055 N PRO A 149 64.119 15.026 23.681 1.00201.18 N ANISOU 1055 N PRO A 149 20810 22783 32848 1969 2166 -1796 N ATOM 1056 CA PRO A 149 65.341 15.453 24.372 1.00203.93 C ANISOU 1056 CA PRO A 149 20778 23062 33645 1979 2050 -1558 C ATOM 1057 C PRO A 149 65.089 16.638 25.298 1.00197.06 C ANISOU 1057 C PRO A 149 19942 22396 32537 1817 1695 -1358 C ATOM 1058 O PRO A 149 64.839 16.424 26.484 1.00191.48 O ANISOU 1058 O PRO A 149 19202 21677 31874 1748 1301 -1187 O ATOM 1059 CB PRO A 149 66.260 15.870 23.222 1.00208.12 C ANISOU 1059 CB PRO A 149 21181 23568 34327 2052 2509 -1668 C ATOM 1060 CG PRO A 149 65.795 15.063 22.063 1.00208.06 C ANISOU 1060 CG PRO A 149 21396 23493 34163 2130 2876 -1964 C ATOM 1061 CD PRO A 149 64.308 14.944 22.222 1.00203.58 C ANISOU 1061 CD PRO A 149 21212 23070 33070 2037 2655 -2046 C ATOM 1062 N GLY A 158 64.632 7.219 36.681 1.00244.26 N ANISOU 1062 N GLY A 158 24943 26997 40869 1474 -2102 794 N ATOM 1063 CA GLY A 158 63.405 7.955 36.924 1.00239.67 C ANISOU 1063 CA GLY A 158 24771 26700 39591 1300 -2175 662 C ATOM 1064 C GLY A 158 62.195 7.048 37.033 1.00238.29 C ANISOU 1064 C GLY A 158 24875 26492 39171 1295 -2219 556 C ATOM 1065 O GLY A 158 61.849 6.587 38.121 1.00238.30 O ANISOU 1065 O GLY A 158 24930 26488 39128 1155 -2587 769 O ATOM 1066 N CYS A 159 61.550 6.792 35.899 1.00236.49 N ANISOU 1066 N CYS A 159 24831 26245 38778 1432 -1846 231 N ATOM 1067 CA CYS A 159 60.368 5.938 35.864 1.00233.75 C ANISOU 1067 CA CYS A 159 24753 25864 38197 1432 -1853 100 C ATOM 1068 C CYS A 159 60.672 4.599 35.200 1.00232.85 C ANISOU 1068 C CYS A 159 24494 25432 38547 1642 -1642 10 C ATOM 1069 O CYS A 159 59.956 3.617 35.402 1.00232.03 O ANISOU 1069 O CYS A 159 24518 25217 38426 1645 -1726 -10 O ATOM 1070 CB CYS A 159 59.219 6.641 35.136 1.00231.68 C ANISOU 1070 CB CYS A 159 24854 25834 37341 1393 -1628 -199 C ATOM 1071 SG CYS A 159 58.662 8.176 35.917 1.00206.63 S ANISOU 1071 SG CYS A 159 21889 23013 33609 1147 -1847 -125 S ATOM 1072 N GLY A 160 61.737 4.566 34.405 1.00234.11 N ANISOU 1072 N GLY A 160 24385 25435 39131 1814 -1351 -51 N ATOM 1073 CA GLY A 160 62.147 3.347 33.732 1.00238.03 C ANISOU 1073 CA GLY A 160 24719 25603 40118 2022 -1102 -154 C ATOM 1074 C GLY A 160 61.534 3.202 32.353 1.00235.97 C ANISOU 1074 C GLY A 160 24702 25345 39613 2129 -645 -562 C ATOM 1075 O GLY A 160 60.630 3.951 31.982 1.00232.60 O ANISOU 1075 O GLY A 160 24590 25177 38609 2035 -571 -745 O ATOM 1076 N GLU A 161 62.030 2.233 31.590 1.00237.54 N ANISOU 1076 N GLU A 161 24752 25245 40256 2319 -339 -703 N ATOM 1077 CA GLU A 161 61.524 1.982 30.246 1.00234.19 C ANISOU 1077 CA GLU A 161 24561 24795 39626 2409 108 -1100 C ATOM 1078 C GLU A 161 60.085 1.480 30.287 1.00222.53 C ANISOU 1078 C GLU A 161 23458 23390 37701 2318 6 -1240 C ATOM 1079 O GLU A 161 59.741 0.615 31.092 1.00219.92 O ANISOU 1079 O GLU A 161 23117 22927 37517 2288 -273 -1083 O ATOM 1080 CB GLU A 161 62.420 0.983 29.509 1.00244.98 C ANISOU 1080 CB GLU A 161 25678 25793 41612 2624 464 -1217 C ATOM 1081 CG GLU A 161 62.558 -0.367 30.199 1.00251.96 C ANISOU 1081 CG GLU A 161 26384 26350 42999 2693 262 -1042 C ATOM 1082 CD GLU A 161 63.543 -1.283 29.496 1.00259.21 C ANISOU 1082 CD GLU A 161 27013 26879 44594 2916 635 -1147 C ATOM 1083 OE1 GLU A 161 63.613 -2.476 29.858 1.00262.61 O ANISOU 1083 OE1 GLU A 161 27317 27003 45462 2995 545 -1057 O ATOM 1084 OE2 GLU A 161 64.248 -0.809 28.580 1.00260.58 O ANISOU 1084 OE2 GLU A 161 27086 27047 44877 3009 1029 -1320 O ATOM 1085 N GLY A 162 59.247 2.032 29.416 1.00216.26 N ANISOU 1085 N GLY A 162 22990 22808 36371 2265 224 -1521 N ATOM 1086 CA GLY A 162 57.841 1.677 29.382 1.00211.96 C ANISOU 1086 CA GLY A 162 22800 22359 35375 2166 135 -1659 C ATOM 1087 C GLY A 162 56.977 2.720 30.065 1.00206.17 C ANISOU 1087 C GLY A 162 22270 21966 34101 1977 -159 -1545 C ATOM 1088 O GLY A 162 55.794 2.861 29.756 1.00205.27 O ANISOU 1088 O GLY A 162 22470 22013 33509 1887 -151 -1704 O ATOM 1089 N GLN A 163 57.574 3.453 31.000 1.00202.06 N ANISOU 1089 N GLN A 163 21562 21544 33667 1910 -416 -1268 N ATOM 1090 CA GLN A 163 56.868 4.511 31.715 1.00194.76 C ANISOU 1090 CA GLN A 163 20810 20925 32265 1726 -677 -1157 C ATOM 1091 C GLN A 163 57.528 5.867 31.482 1.00184.36 C ANISOU 1091 C GLN A 163 19404 19793 30854 1705 -578 -1134 C ATOM 1092 O GLN A 163 58.753 5.988 31.520 1.00184.67 O ANISOU 1092 O GLN A 163 19142 19722 31303 1783 -530 -1016 O ATOM 1093 CB GLN A 163 56.813 4.204 33.214 1.00200.78 C ANISOU 1093 CB GLN A 163 21491 21664 33131 1608 -1124 -839 C ATOM 1094 CG GLN A 163 56.028 2.951 33.568 1.00206.85 C ANISOU 1094 CG GLN A 163 22375 22279 33937 1597 -1262 -833 C ATOM 1095 CD GLN A 163 55.980 2.697 35.063 1.00210.80 C ANISOU 1095 CD GLN A 163 22812 22776 34508 1457 -1708 -501 C ATOM 1096 OE1 GLN A 163 56.700 3.330 35.835 1.00212.95 O ANISOU 1096 OE1 GLN A 163 22914 23120 34878 1380 -1917 -264 O ATOM 1097 NE2 GLN A 163 55.130 1.765 35.478 1.00210.19 N ANISOU 1097 NE2 GLN A 163 22877 22615 34371 1408 -1858 -480 N ATOM 1098 N VAL A 164 56.707 6.885 31.242 1.00176.12 N ANISOU 1098 N VAL A 164 18609 19020 29289 1598 -550 -1239 N ATOM 1099 CA VAL A 164 57.204 8.234 31.002 1.00168.42 C ANISOU 1099 CA VAL A 164 17583 18230 28180 1564 -457 -1226 C ATOM 1100 C VAL A 164 56.803 9.170 32.136 1.00161.86 C ANISOU 1100 C VAL A 164 16824 17610 27063 1377 -788 -1034 C ATOM 1101 O VAL A 164 55.665 9.132 32.605 1.00169.33 O ANISOU 1101 O VAL A 164 18005 18665 27669 1265 -954 -1042 O ATOM 1102 CB VAL A 164 56.658 8.803 29.677 1.00164.78 C ANISOU 1102 CB VAL A 164 17346 17909 27355 1590 -116 -1507 C ATOM 1103 CG1 VAL A 164 57.105 10.246 29.492 1.00157.83 C ANISOU 1103 CG1 VAL A 164 16422 17223 26322 1541 -42 -1472 C ATOM 1104 CG2 VAL A 164 57.105 7.943 28.506 1.00170.22 C ANISOU 1104 CG2 VAL A 164 17986 18395 28295 1752 247 -1723 C ATOM 1105 N ALA A 165 57.741 10.003 32.577 1.00150.98 N ANISOU 1105 N ALA A 165 15247 16286 25834 1337 -871 -867 N ATOM 1106 CA ALA A 165 57.448 11.007 33.590 1.00144.26 C ANISOU 1106 CA ALA A 165 14473 15636 24705 1146 -1147 -711 C ATOM 1107 C ALA A 165 56.293 11.877 33.115 1.00138.50 C ANISOU 1107 C ALA A 165 14049 15130 23443 1075 -1029 -892 C ATOM 1108 O ALA A 165 56.475 12.760 32.279 1.00132.03 O ANISOU 1108 O ALA A 165 13249 14412 22503 1109 -793 -1008 O ATOM 1109 CB ALA A 165 58.675 11.857 33.866 1.00150.05 C ANISOU 1109 CB ALA A 165 14952 16391 25669 1121 -1188 -552 C ATOM 1110 N CYS A 166 55.104 11.615 33.649 1.00143.93 N ANISOU 1110 N CYS A 166 14967 15887 23833 974 -1194 -903 N ATOM 1111 CA CYS A 166 53.893 12.286 33.194 1.00136.99 C ANISOU 1111 CA CYS A 166 14366 15194 22488 916 -1091 -1065 C ATOM 1112 C CYS A 166 53.812 13.728 33.683 1.00135.12 C ANISOU 1112 C CYS A 166 14180 15155 22002 778 -1167 -997 C ATOM 1113 O CYS A 166 52.977 14.067 34.522 1.00133.29 O ANISOU 1113 O CYS A 166 14106 15032 21505 632 -1352 -943 O ATOM 1114 CB CYS A 166 52.652 11.509 33.635 1.00129.24 C ANISOU 1114 CB CYS A 166 13590 14209 21307 852 -1237 -1090 C ATOM 1115 SG CYS A 166 51.120 12.050 32.842 1.00193.43 S ANISOU 1115 SG CYS A 166 22032 22521 28941 816 -1081 -1303 S ATOM 1116 N LEU A 167 54.694 14.570 33.156 1.00138.88 N ANISOU 1116 N LEU A 167 14523 15667 22579 822 -1008 -1004 N ATOM 1117 CA LEU A 167 54.667 15.996 33.442 1.00144.32 C ANISOU 1117 CA LEU A 167 15258 16528 23051 704 -1033 -964 C ATOM 1118 C LEU A 167 54.104 16.691 32.213 1.00146.69 C ANISOU 1118 C LEU A 167 15705 16940 23090 762 -747 -1153 C ATOM 1119 O LEU A 167 54.688 16.612 31.133 1.00146.12 O ANISOU 1119 O LEU A 167 15548 16819 23150 888 -494 -1250 O ATOM 1120 CB LEU A 167 56.075 16.507 33.738 1.00153.56 C ANISOU 1120 CB LEU A 167 16164 17658 24523 696 -1073 -817 C ATOM 1121 CG LEU A 167 56.940 15.612 34.629 1.00163.54 C ANISOU 1121 CG LEU A 167 17206 18763 26169 687 -1315 -618 C ATOM 1122 CD1 LEU A 167 58.328 16.205 34.798 1.00165.06 C ANISOU 1122 CD1 LEU A 167 17123 18925 26670 677 -1341 -473 C ATOM 1123 CD2 LEU A 167 56.279 15.390 35.981 1.00165.00 C ANISOU 1123 CD2 LEU A 167 17518 18988 26185 509 -1653 -484 C ATOM 1124 N PHE A 168 52.971 17.366 32.373 1.00144.95 N ANISOU 1124 N PHE A 168 15702 16865 22507 663 -782 -1199 N ATOM 1125 CA PHE A 168 52.243 17.890 31.222 1.00143.36 C ANISOU 1125 CA PHE A 168 15658 16766 22046 708 -550 -1358 C ATOM 1126 C PHE A 168 53.105 18.665 30.233 1.00142.31 C ANISOU 1126 C PHE A 168 15420 16662 21988 780 -304 -1401 C ATOM 1127 O PHE A 168 53.156 18.325 29.053 1.00141.52 O ANISOU 1127 O PHE A 168 15348 16539 21885 885 -71 -1532 O ATOM 1128 CB PHE A 168 51.058 18.758 31.639 1.00152.79 C ANISOU 1128 CB PHE A 168 17048 18107 22899 584 -629 -1361 C ATOM 1129 CG PHE A 168 50.356 19.386 30.474 1.00159.72 C ANISOU 1129 CG PHE A 168 18062 19089 23534 621 -419 -1485 C ATOM 1130 CD1 PHE A 168 49.528 18.627 29.666 1.00156.44 C ANISOU 1130 CD1 PHE A 168 17783 18666 22989 679 -335 -1609 C ATOM 1131 CD2 PHE A 168 50.547 20.721 30.165 1.00159.39 C ANISOU 1131 CD2 PHE A 168 18013 19148 23401 589 -314 -1467 C ATOM 1132 CE1 PHE A 168 48.888 19.191 28.584 1.00147.65 C ANISOU 1132 CE1 PHE A 168 16797 17655 21646 694 -169 -1701 C ATOM 1133 CE2 PHE A 168 49.911 21.289 29.081 1.00152.19 C ANISOU 1133 CE2 PHE A 168 17221 18330 22275 616 -139 -1554 C ATOM 1134 CZ PHE A 168 49.081 20.524 28.289 1.00145.01 C ANISOU 1134 CZ PHE A 168 16449 17423 21226 664 -74 -1665 C ATOM 1135 N GLU A 169 53.763 19.716 30.711 1.00144.94 N ANISOU 1135 N GLU A 169 15647 17048 22375 709 -352 -1293 N ATOM 1136 CA GLU A 169 54.570 20.568 29.843 1.00140.83 C ANISOU 1136 CA GLU A 169 15026 16564 21921 759 -126 -1315 C ATOM 1137 C GLU A 169 55.618 19.764 29.080 1.00136.51 C ANISOU 1137 C GLU A 169 14298 15883 21687 903 60 -1359 C ATOM 1138 O GLU A 169 56.131 20.211 28.055 1.00130.61 O ANISOU 1138 O GLU A 169 13505 15158 20964 967 319 -1426 O ATOM 1139 CB GLU A 169 55.241 21.687 30.645 1.00134.64 C ANISOU 1139 CB GLU A 169 14126 15826 21207 648 -242 -1176 C ATOM 1140 CG GLU A 169 56.266 21.208 31.660 1.00140.26 C ANISOU 1140 CG GLU A 169 14619 16428 22245 614 -452 -1021 C ATOM 1141 CD GLU A 169 55.633 20.575 32.884 1.00146.24 C ANISOU 1141 CD GLU A 169 15466 17166 22935 511 -747 -946 C ATOM 1142 OE1 GLU A 169 54.447 20.857 33.158 1.00152.99 O ANISOU 1142 OE1 GLU A 169 16542 18111 23475 431 -800 -999 O ATOM 1143 OE2 GLU A 169 56.324 19.800 33.577 1.00149.40 O ANISOU 1143 OE2 GLU A 169 15706 17454 23607 505 -926 -822 O ATOM 1144 N ASP A 170 55.928 18.574 29.585 1.00137.10 N ANISOU 1144 N ASP A 170 14269 15811 22012 949 -60 -1318 N ATOM 1145 CA ASP A 170 56.910 17.704 28.950 1.00150.37 C ANISOU 1145 CA ASP A 170 15760 17329 24044 1093 120 -1360 C ATOM 1146 C ASP A 170 56.259 16.666 28.038 1.00148.35 C ANISOU 1146 C ASP A 170 15657 17009 23700 1188 295 -1551 C ATOM 1147 O ASP A 170 56.867 16.215 27.068 1.00151.12 O ANISOU 1147 O ASP A 170 15933 17265 24221 1304 568 -1665 O ATOM 1148 CB ASP A 170 57.770 17.005 30.006 1.00165.92 C ANISOU 1148 CB ASP A 170 17488 19145 26410 1094 -109 -1182 C ATOM 1149 CG ASP A 170 58.651 17.971 30.779 1.00169.09 C ANISOU 1149 CG ASP A 170 17704 19591 26951 998 -260 -996 C ATOM 1150 OD1 ASP A 170 58.625 19.181 30.472 1.00169.45 O ANISOU 1150 OD1 ASP A 170 17807 19774 26804 941 -164 -1017 O ATOM 1151 OD2 ASP A 170 59.373 17.517 31.693 1.00167.07 O ANISOU 1151 OD2 ASP A 170 17247 19228 27005 971 -485 -819 O ATOM 1152 N VAL A 171 55.021 16.291 28.350 1.00151.38 N ANISOU 1152 N VAL A 171 16259 17441 23818 1129 147 -1592 N ATOM 1153 CA VAL A 171 54.332 15.244 27.599 1.00157.69 C ANISOU 1153 CA VAL A 171 17212 18173 24529 1195 269 -1765 C ATOM 1154 C VAL A 171 53.363 15.798 26.554 1.00153.37 C ANISOU 1154 C VAL A 171 16915 17783 23574 1163 435 -1917 C ATOM 1155 O VAL A 171 52.942 15.080 25.647 1.00152.09 O ANISOU 1155 O VAL A 171 16887 17582 23319 1210 596 -2084 O ATOM 1156 CB VAL A 171 53.576 14.277 28.536 1.00158.63 C ANISOU 1156 CB VAL A 171 17402 18220 24648 1153 2 -1713 C ATOM 1157 CG1 VAL A 171 54.544 13.608 29.501 1.00163.81 C ANISOU 1157 CG1 VAL A 171 17810 18706 25723 1182 -172 -1547 C ATOM 1158 CG2 VAL A 171 52.483 15.013 29.292 1.00149.22 C ANISOU 1158 CG2 VAL A 171 16381 17196 23120 1009 -213 -1643 C ATOM 1159 N VAL A 172 53.014 17.073 26.681 1.00146.40 N ANISOU 1159 N VAL A 172 16098 17072 22457 1075 390 -1852 N ATOM 1160 CA VAL A 172 52.111 17.712 25.730 1.00141.62 C ANISOU 1160 CA VAL A 172 15707 16617 21484 1036 519 -1953 C ATOM 1161 C VAL A 172 52.737 18.967 25.127 1.00141.99 C ANISOU 1161 C VAL A 172 15696 16765 21489 1028 695 -1925 C ATOM 1162 O VAL A 172 53.140 19.876 25.853 1.00144.13 O ANISOU 1162 O VAL A 172 15857 17080 21827 977 590 -1790 O ATOM 1163 CB VAL A 172 50.766 18.073 26.381 1.00138.13 C ANISOU 1163 CB VAL A 172 15434 16287 20762 928 299 -1903 C ATOM 1164 CG1 VAL A 172 49.924 18.915 25.432 1.00128.84 C ANISOU 1164 CG1 VAL A 172 14436 15267 19249 884 414 -1962 C ATOM 1165 CG2 VAL A 172 50.021 16.811 26.799 1.00142.49 C ANISOU 1165 CG2 VAL A 172 16072 16750 21316 927 153 -1946 C ATOM 1166 N PRO A 173 52.818 19.015 23.788 1.00136.18 N ANISOU 1166 N PRO A 173 15046 16065 20632 1067 966 -2055 N ATOM 1167 CA PRO A 173 53.445 20.118 23.050 1.00133.15 C ANISOU 1167 CA PRO A 173 14616 15770 20204 1061 1170 -2036 C ATOM 1168 C PRO A 173 52.807 21.469 23.358 1.00137.20 C ANISOU 1168 C PRO A 173 15202 16439 20489 961 1050 -1923 C ATOM 1169 O PRO A 173 51.729 21.519 23.946 1.00138.38 O ANISOU 1169 O PRO A 173 15471 16638 20468 898 847 -1889 O ATOM 1170 CB PRO A 173 53.188 19.747 21.586 1.00123.76 C ANISOU 1170 CB PRO A 173 13599 14612 18811 1081 1435 -2210 C ATOM 1171 CG PRO A 173 53.003 18.274 21.595 1.00121.47 C ANISOU 1171 CG PRO A 173 13349 14181 18624 1137 1428 -2335 C ATOM 1172 CD PRO A 173 52.320 17.961 22.888 1.00127.62 C ANISOU 1172 CD PRO A 173 14120 14933 19436 1102 1098 -2233 C ATOM 1173 N MET A 174 53.473 22.550 22.962 1.00142.36 N ANISOU 1173 N MET A 174 15777 17156 21159 948 1189 -1865 N ATOM 1174 CA MET A 174 52.934 23.894 23.144 1.00148.34 C ANISOU 1174 CA MET A 174 16595 18041 21726 859 1111 -1761 C ATOM 1175 C MET A 174 52.404 24.461 21.832 1.00155.90 C ANISOU 1175 C MET A 174 17724 19121 22392 832 1291 -1808 C ATOM 1176 O MET A 174 51.473 25.266 21.827 1.00156.73 O ANISOU 1176 O MET A 174 17945 19326 22278 762 1202 -1746 O ATOM 1177 CB MET A 174 53.986 24.830 23.742 1.00152.62 C ANISOU 1177 CB MET A 174 16933 18566 22489 838 1100 -1636 C ATOM 1178 CG MET A 174 54.274 24.583 25.214 1.00155.07 C ANISOU 1178 CG MET A 174 17111 18795 23013 808 847 -1545 C ATOM 1179 SD MET A 174 52.841 24.896 26.264 1.00171.87 S ANISOU 1179 SD MET A 174 19408 20985 24908 700 572 -1500 S ATOM 1180 CE MET A 174 52.537 26.627 25.920 1.00 93.93 C ANISOU 1180 CE MET A 174 9595 11235 14861 624 651 -1434 C ATOM 1181 N ASN A 175 53.002 24.043 20.721 1.00161.72 N ANISOU 1181 N ASN A 175 18472 19842 23133 881 1548 -1912 N ATOM 1182 CA ASN A 175 52.509 24.431 19.403 1.00160.05 C ANISOU 1182 CA ASN A 175 18449 19751 22613 835 1717 -1962 C ATOM 1183 C ASN A 175 51.077 23.948 19.182 1.00160.05 C ANISOU 1183 C ASN A 175 18677 19811 22326 785 1580 -2015 C ATOM 1184 O ASN A 175 50.303 24.573 18.455 1.00159.10 O ANISOU 1184 O ASN A 175 18713 19815 21923 712 1589 -1980 O ATOM 1185 CB ASN A 175 53.427 23.901 18.297 1.00152.29 C ANISOU 1185 CB ASN A 175 17456 18726 21680 883 2037 -2093 C ATOM 1186 CG ASN A 175 53.583 22.393 18.338 1.00141.86 C ANISOU 1186 CG ASN A 175 16134 17267 20501 957 2077 -2248 C ATOM 1187 OD1 ASN A 175 53.399 21.765 19.380 1.00136.24 O ANISOU 1187 OD1 ASN A 175 15345 16461 19957 992 1865 -2226 O ATOM 1188 ND2 ASN A 175 53.933 21.803 17.200 1.00137.39 N ANISOU 1188 ND2 ASN A 175 15656 16678 19869 974 2359 -2409 N ATOM 1189 N TYR A 176 50.734 22.833 19.818 1.00158.25 N ANISOU 1189 N TYR A 176 18455 19488 22185 820 1442 -2083 N ATOM 1190 CA TYR A 176 49.382 22.295 19.756 1.00158.02 C ANISOU 1190 CA TYR A 176 18616 19499 21924 771 1288 -2127 C ATOM 1191 C TYR A 176 48.446 23.096 20.653 1.00157.11 C ANISOU 1191 C TYR A 176 18508 19448 21739 712 1046 -1984 C ATOM 1192 O TYR A 176 47.343 23.461 20.246 1.00160.46 O ANISOU 1192 O TYR A 176 19078 19972 21917 645 974 -1952 O ATOM 1193 CB TYR A 176 49.372 20.821 20.169 1.00164.24 C ANISOU 1193 CB TYR A 176 19399 20149 22854 825 1230 -2243 C ATOM 1194 CG TYR A 176 47.989 20.274 20.450 1.00174.19 C ANISOU 1194 CG TYR A 176 20815 21433 23937 772 1020 -2259 C ATOM 1195 CD1 TYR A 176 47.231 19.694 19.442 1.00180.89 C ANISOU 1195 CD1 TYR A 176 21870 22326 24533 724 1073 -2377 C ATOM 1196 CD2 TYR A 176 47.443 20.339 21.725 1.00175.63 C ANISOU 1196 CD2 TYR A 176 20940 21594 24196 754 773 -2158 C ATOM 1197 CE1 TYR A 176 45.967 19.195 19.697 1.00182.57 C ANISOU 1197 CE1 TYR A 176 22209 22558 24602 668 874 -2383 C ATOM 1198 CE2 TYR A 176 46.182 19.846 21.989 1.00178.09 C ANISOU 1198 CE2 TYR A 176 21379 21924 24362 703 596 -2168 C ATOM 1199 CZ TYR A 176 45.448 19.276 20.972 1.00184.62 C ANISOU 1199 CZ TYR A 176 22391 22791 24964 665 643 -2276 C ATOM 1200 OH TYR A 176 44.191 18.782 21.232 1.00192.02 O ANISOU 1200 OH TYR A 176 23440 23744 25774 608 460 -2277 O ATOM 1201 N MET A 177 48.895 23.370 21.874 1.00155.42 N ANISOU 1201 N MET A 177 18132 19170 21748 729 923 -1898 N ATOM 1202 CA MET A 177 48.084 24.100 22.842 1.00153.70 C ANISOU 1202 CA MET A 177 17919 18991 21487 667 720 -1784 C ATOM 1203 C MET A 177 47.816 25.529 22.387 1.00153.16 C ANISOU 1203 C MET A 177 17878 19031 21285 615 776 -1684 C ATOM 1204 O MET A 177 46.888 26.180 22.869 1.00152.33 O ANISOU 1204 O MET A 177 17817 18967 21097 561 648 -1605 O ATOM 1205 CB MET A 177 48.766 24.118 24.211 1.00153.69 C ANISOU 1205 CB MET A 177 17753 18902 21739 671 594 -1719 C ATOM 1206 CG MET A 177 49.118 22.744 24.749 1.00154.79 C ANISOU 1206 CG MET A 177 17838 18921 22054 721 519 -1782 C ATOM 1207 SD MET A 177 47.716 21.616 24.708 1.00138.69 S ANISOU 1207 SD MET A 177 15983 16876 19836 704 394 -1866 S ATOM 1208 CE MET A 177 46.486 22.576 25.586 1.00205.17 C ANISOU 1208 CE MET A 177 24472 25381 28103 604 208 -1757 C ATOM 1209 N VAL A 178 48.634 26.012 21.458 1.00150.25 N ANISOU 1209 N VAL A 178 17479 18697 20913 632 979 -1684 N ATOM 1210 CA VAL A 178 48.525 27.388 20.990 1.00145.41 C ANISOU 1210 CA VAL A 178 16876 18172 20200 583 1043 -1573 C ATOM 1211 C VAL A 178 47.821 27.498 19.637 1.00149.57 C ANISOU 1211 C VAL A 178 17578 18808 20444 543 1128 -1580 C ATOM 1212 O VAL A 178 46.715 28.031 19.548 1.00145.54 O ANISOU 1212 O VAL A 178 17156 18363 19780 488 1017 -1497 O ATOM 1213 CB VAL A 178 49.908 28.065 20.909 1.00133.82 C ANISOU 1213 CB VAL A 178 15250 16680 18916 605 1202 -1531 C ATOM 1214 CG1 VAL A 178 49.794 29.419 20.238 1.00127.31 C ANISOU 1214 CG1 VAL A 178 14453 15945 17974 553 1291 -1418 C ATOM 1215 CG2 VAL A 178 50.510 28.205 22.299 1.00131.59 C ANISOU 1215 CG2 VAL A 178 14799 16308 18892 609 1074 -1485 C ATOM 1216 N TYR A 179 48.464 26.993 18.589 1.00154.71 N ANISOU 1216 N TYR A 179 18277 19475 21032 560 1327 -1675 N ATOM 1217 CA TYR A 179 47.924 27.100 17.237 1.00160.25 C ANISOU 1217 CA TYR A 179 19162 20290 21436 494 1419 -1682 C ATOM 1218 C TYR A 179 46.637 26.301 17.057 1.00159.15 C ANISOU 1218 C TYR A 179 19193 20183 21096 451 1263 -1735 C ATOM 1219 O TYR A 179 45.594 26.855 16.712 1.00161.73 O ANISOU 1219 O TYR A 179 19618 20600 21234 379 1150 -1631 O ATOM 1220 CB TYR A 179 48.960 26.647 16.205 1.00170.94 C ANISOU 1220 CB TYR A 179 20542 21642 22764 510 1697 -1801 C ATOM 1221 CG TYR A 179 50.177 27.540 16.118 1.00178.47 C ANISOU 1221 CG TYR A 179 21341 22589 23882 533 1878 -1732 C ATOM 1222 CD1 TYR A 179 50.187 28.653 15.288 1.00182.19 C ANISOU 1222 CD1 TYR A 179 21864 23167 24192 462 1977 -1615 C ATOM 1223 CD2 TYR A 179 51.317 27.267 16.862 1.00178.97 C ANISOU 1223 CD2 TYR A 179 21196 22532 24271 618 1939 -1769 C ATOM 1224 CE1 TYR A 179 51.298 29.472 15.205 1.00181.78 C ANISOU 1224 CE1 TYR A 179 21668 23105 24297 476 2146 -1548 C ATOM 1225 CE2 TYR A 179 52.431 28.079 16.785 1.00179.96 C ANISOU 1225 CE2 TYR A 179 21166 22647 24562 631 2097 -1699 C ATOM 1226 CZ TYR A 179 52.416 29.180 15.956 1.00182.24 C ANISOU 1226 CZ TYR A 179 21516 23045 24684 560 2207 -1595 C ATOM 1227 OH TYR A 179 53.525 29.992 15.876 1.00186.43 O ANISOU 1227 OH TYR A 179 21889 23561 25386 567 2368 -1522 O ATOM 1228 N PHE A 180 46.720 24.996 17.293 1.00156.59 N ANISOU 1228 N PHE A 180 18890 19774 20835 494 1253 -1887 N ATOM 1229 CA PHE A 180 45.600 24.094 17.050 1.00153.89 C ANISOU 1229 CA PHE A 180 18712 19449 20309 448 1124 -1960 C ATOM 1230 C PHE A 180 44.487 24.253 18.083 1.00145.97 C ANISOU 1230 C PHE A 180 17681 18438 19343 434 860 -1862 C ATOM 1231 O PHE A 180 43.325 24.458 17.729 1.00146.82 O ANISOU 1231 O PHE A 180 17899 18626 19258 360 735 -1795 O ATOM 1232 CB PHE A 180 46.087 22.644 17.020 1.00158.76 C ANISOU 1232 CB PHE A 180 19352 19953 21018 501 1209 -2157 C ATOM 1233 CG PHE A 180 45.022 21.651 16.652 1.00163.14 C ANISOU 1233 CG PHE A 180 20090 20518 21379 441 1100 -2253 C ATOM 1234 CD1 PHE A 180 44.763 21.353 15.324 1.00168.35 C ANISOU 1234 CD1 PHE A 180 20956 21257 21754 352 1213 -2346 C ATOM 1235 CD2 PHE A 180 44.285 21.010 17.633 1.00165.42 C ANISOU 1235 CD2 PHE A 180 20354 20738 21761 457 884 -2252 C ATOM 1236 CE1 PHE A 180 43.784 20.437 14.983 1.00170.89 C ANISOU 1236 CE1 PHE A 180 21451 21586 21895 279 1100 -2437 C ATOM 1237 CE2 PHE A 180 43.307 20.094 17.298 1.00168.70 C ANISOU 1237 CE2 PHE A 180 20931 21157 22012 395 781 -2337 C ATOM 1238 CZ PHE A 180 43.056 19.807 15.971 1.00169.47 C ANISOU 1238 CZ PHE A 180 21228 21329 21833 305 883 -2431 C ATOM 1239 N ASN A 181 44.845 24.156 19.359 1.00139.10 N ANISOU 1239 N ASN A 181 16661 17469 18722 495 779 -1848 N ATOM 1240 CA ASN A 181 43.857 24.203 20.433 1.00130.75 C ANISOU 1240 CA ASN A 181 15582 16391 17707 476 558 -1777 C ATOM 1241 C ASN A 181 43.287 25.601 20.661 1.00133.54 C ANISOU 1241 C ASN A 181 15899 16809 18032 433 496 -1613 C ATOM 1242 O ASN A 181 42.101 25.838 20.438 1.00140.42 O ANISOU 1242 O ASN A 181 16848 17739 18766 379 388 -1545 O ATOM 1243 CB ASN A 181 44.449 23.646 21.731 1.00126.80 C ANISOU 1243 CB ASN A 181 14951 15769 17458 531 488 -1809 C ATOM 1244 CG ASN A 181 43.411 23.486 22.827 1.00120.96 C ANISOU 1244 CG ASN A 181 14218 15005 16737 497 278 -1762 C ATOM 1245 OD1 ASN A 181 42.419 24.212 22.871 1.00128.25 O ANISOU 1245 OD1 ASN A 181 15180 15991 17558 445 201 -1673 O ATOM 1246 ND2 ASN A 181 43.639 22.532 23.722 1.00114.17 N ANISOU 1246 ND2 ASN A 181 13312 14045 16021 523 191 -1814 N ATOM 1247 N PHE A 182 44.134 26.525 21.103 1.00132.07 N ANISOU 1247 N PHE A 182 15584 16601 17995 455 567 -1546 N ATOM 1248 CA PHE A 182 43.687 27.876 21.429 1.00130.97 C ANISOU 1248 CA PHE A 182 15398 16491 17873 419 527 -1402 C ATOM 1249 C PHE A 182 43.057 28.604 20.242 1.00132.07 C ANISOU 1249 C PHE A 182 15626 16735 17819 370 564 -1304 C ATOM 1250 O PHE A 182 41.838 28.741 20.167 1.00123.90 O ANISOU 1250 O PHE A 182 14651 15734 16691 329 442 -1234 O ATOM 1251 CB PHE A 182 44.839 28.704 22.005 1.00131.47 C ANISOU 1251 CB PHE A 182 15317 16508 18128 438 611 -1361 C ATOM 1252 CG PHE A 182 44.479 30.139 22.269 1.00133.32 C ANISOU 1252 CG PHE A 182 15507 16754 18394 398 601 -1226 C ATOM 1253 CD1 PHE A 182 43.356 30.458 23.016 1.00137.00 C ANISOU 1253 CD1 PHE A 182 15988 17198 18868 365 471 -1176 C ATOM 1254 CD2 PHE A 182 45.262 31.168 21.776 1.00130.75 C ANISOU 1254 CD2 PHE A 182 15121 16449 18110 393 736 -1152 C ATOM 1255 CE1 PHE A 182 43.020 31.777 23.262 1.00136.94 C ANISOU 1255 CE1 PHE A 182 15934 17175 18920 332 484 -1062 C ATOM 1256 CE2 PHE A 182 44.932 32.488 22.019 1.00131.93 C ANISOU 1256 CE2 PHE A 182 15228 16588 18311 357 733 -1030 C ATOM 1257 CZ PHE A 182 43.810 32.793 22.763 1.00134.89 C ANISOU 1257 CZ PHE A 182 15617 16928 18706 329 611 -989 C ATOM 1258 N PHE A 183 43.893 29.071 19.320 1.00141.67 N ANISOU 1258 N PHE A 183 16845 17999 18985 369 730 -1285 N ATOM 1259 CA PHE A 183 43.427 29.878 18.194 1.00144.15 C ANISOU 1259 CA PHE A 183 17240 18416 19116 307 765 -1162 C ATOM 1260 C PHE A 183 42.273 29.246 17.417 1.00138.00 C ANISOU 1260 C PHE A 183 16620 17713 18100 246 656 -1164 C ATOM 1261 O PHE A 183 41.235 29.875 17.218 1.00138.06 O ANISOU 1261 O PHE A 183 16650 17766 18040 195 539 -1019 O ATOM 1262 CB PHE A 183 44.583 30.194 17.240 1.00152.98 C ANISOU 1262 CB PHE A 183 18363 19579 20185 304 981 -1172 C ATOM 1263 CG PHE A 183 45.599 31.146 17.806 1.00156.69 C ANISOU 1263 CG PHE A 183 18671 19992 20872 338 1078 -1114 C ATOM 1264 CD1 PHE A 183 45.289 32.484 17.986 1.00160.46 C ANISOU 1264 CD1 PHE A 183 19089 20472 21408 309 1046 -948 C ATOM 1265 CD2 PHE A 183 46.868 30.707 18.145 1.00152.78 C ANISOU 1265 CD2 PHE A 183 18074 19432 20543 395 1200 -1219 C ATOM 1266 CE1 PHE A 183 46.221 33.364 18.504 1.00159.84 C ANISOU 1266 CE1 PHE A 183 18870 20335 21526 326 1131 -902 C ATOM 1267 CE2 PHE A 183 47.805 31.582 18.662 1.00151.49 C ANISOU 1267 CE2 PHE A 183 17756 19218 20583 411 1271 -1158 C ATOM 1268 CZ PHE A 183 47.481 32.912 18.842 1.00155.18 C ANISOU 1268 CZ PHE A 183 18184 19694 21085 371 1237 -1006 C ATOM 1269 N ALA A 184 42.457 28.005 16.980 1.00132.72 N ANISOU 1269 N ALA A 184 16055 17050 17324 245 693 -1324 N ATOM 1270 CA ALA A 184 41.502 27.361 16.082 1.00132.47 C ANISOU 1270 CA ALA A 184 16198 17098 17036 162 606 -1344 C ATOM 1271 C ALA A 184 40.283 26.772 16.789 1.00136.07 C ANISOU 1271 C ALA A 184 16662 17519 17519 153 388 -1343 C ATOM 1272 O ALA A 184 39.161 26.878 16.291 1.00141.77 O ANISOU 1272 O ALA A 184 17464 18312 18091 74 249 -1247 O ATOM 1273 CB ALA A 184 42.197 26.292 15.249 1.00132.44 C ANISOU 1273 CB ALA A 184 16321 17103 16897 149 762 -1533 C ATOM 1274 N CYS A 185 40.501 26.152 17.943 1.00134.22 N ANISOU 1274 N CYS A 185 16341 17176 17480 225 352 -1438 N ATOM 1275 CA CYS A 185 39.429 25.434 18.628 1.00132.66 C ANISOU 1275 CA CYS A 185 16160 16940 17307 212 167 -1458 C ATOM 1276 C CYS A 185 38.855 26.190 19.825 1.00133.14 C ANISOU 1276 C CYS A 185 16089 16949 17547 233 62 -1343 C ATOM 1277 O CYS A 185 38.024 25.657 20.559 1.00138.81 O ANISOU 1277 O CYS A 185 16801 17624 18315 225 -71 -1357 O ATOM 1278 CB CYS A 185 39.908 24.049 19.069 1.00129.17 C ANISOU 1278 CB CYS A 185 15737 16406 16936 258 183 -1643 C ATOM 1279 SG CYS A 185 40.572 23.026 17.734 1.00157.52 S ANISOU 1279 SG CYS A 185 19488 20019 20343 235 343 -1822 S ATOM 1280 N VAL A 186 39.297 27.427 20.024 1.00130.81 N ANISOU 1280 N VAL A 186 15697 16653 17352 252 137 -1238 N ATOM 1281 CA VAL A 186 38.796 28.238 21.130 1.00133.26 C ANISOU 1281 CA VAL A 186 15896 16904 17833 260 73 -1145 C ATOM 1282 C VAL A 186 38.596 29.697 20.732 1.00133.89 C ANISOU 1282 C VAL A 186 15923 17016 17935 241 115 -974 C ATOM 1283 O VAL A 186 37.507 30.245 20.889 1.00131.42 O ANISOU 1283 O VAL A 186 15578 16696 17659 215 26 -857 O ATOM 1284 CB VAL A 186 39.726 28.174 22.359 1.00145.11 C ANISOU 1284 CB VAL A 186 17300 18310 19523 306 117 -1223 C ATOM 1285 CG1 VAL A 186 39.270 29.164 23.420 1.00145.45 C ANISOU 1285 CG1 VAL A 186 17254 18296 19714 291 86 -1139 C ATOM 1286 CG2 VAL A 186 39.771 26.760 22.924 1.00147.12 C ANISOU 1286 CG2 VAL A 186 17590 18514 19795 322 45 -1358 C ATOM 1287 N LEU A 187 39.650 30.321 20.218 1.00139.54 N ANISOU 1287 N LEU A 187 16616 17754 18649 254 256 -954 N ATOM 1288 CA LEU A 187 39.588 31.727 19.838 1.00137.70 C ANISOU 1288 CA LEU A 187 16329 17538 18454 236 306 -786 C ATOM 1289 C LEU A 187 38.611 31.950 18.687 1.00138.16 C ANISOU 1289 C LEU A 187 16466 17689 18340 174 225 -645 C ATOM 1290 O LEU A 187 37.799 32.872 18.725 1.00134.49 O ANISOU 1290 O LEU A 187 15940 17206 17955 157 164 -480 O ATOM 1291 CB LEU A 187 40.977 32.252 19.468 1.00133.46 C ANISOU 1291 CB LEU A 187 15756 17010 17944 254 478 -796 C ATOM 1292 CG LEU A 187 41.078 33.759 19.215 1.00134.32 C ANISOU 1292 CG LEU A 187 15793 17112 18130 236 544 -625 C ATOM 1293 CD1 LEU A 187 40.733 34.544 20.473 1.00128.79 C ANISOU 1293 CD1 LEU A 187 14979 16298 17658 252 509 -587 C ATOM 1294 CD2 LEU A 187 42.465 34.126 18.718 1.00139.49 C ANISOU 1294 CD2 LEU A 187 16422 17788 18789 244 720 -640 C ATOM 1295 N VAL A 188 38.690 31.099 17.668 1.00141.39 N ANISOU 1295 N VAL A 188 17011 18190 18521 132 224 -707 N ATOM 1296 CA VAL A 188 37.802 31.200 16.512 1.00144.32 C ANISOU 1296 CA VAL A 188 17483 18666 18686 43 123 -574 C ATOM 1297 C VAL A 188 36.329 31.014 16.884 1.00148.78 C ANISOU 1297 C VAL A 188 18023 19212 19295 18 -79 -493 C ATOM 1298 O VAL A 188 35.487 31.829 16.504 1.00154.55 O ANISOU 1298 O VAL A 188 18712 19965 20043 -23 -173 -288 O ATOM 1299 CB VAL A 188 38.187 30.202 15.397 1.00144.70 C ANISOU 1299 CB VAL A 188 17712 18812 18456 -19 171 -695 C ATOM 1300 CG1 VAL A 188 37.079 30.109 14.356 1.00139.98 C ANISOU 1300 CG1 VAL A 188 17236 18323 17626 -140 11 -569 C ATOM 1301 CG2 VAL A 188 39.505 30.606 14.755 1.00148.88 C ANISOU 1301 CG2 VAL A 188 18265 19377 18927 -15 387 -724 C ATOM 1302 N PRO A 189 36.009 29.938 17.622 1.00142.75 N ANISOU 1302 N PRO A 189 17273 18400 18567 42 -147 -640 N ATOM 1303 CA PRO A 189 34.623 29.745 18.061 1.00133.61 C ANISOU 1303 CA PRO A 189 16074 17215 17477 19 -323 -567 C ATOM 1304 C PRO A 189 34.109 30.950 18.842 1.00126.08 C ANISOU 1304 C PRO A 189 14956 16176 16772 58 -324 -418 C ATOM 1305 O PRO A 189 33.045 31.474 18.522 1.00129.66 O ANISOU 1305 O PRO A 189 15359 16640 17265 20 -436 -238 O ATOM 1306 CB PRO A 189 34.713 28.520 18.974 1.00131.52 C ANISOU 1306 CB PRO A 189 15829 16886 17258 56 -341 -766 C ATOM 1307 CG PRO A 189 35.901 27.774 18.479 1.00135.63 C ANISOU 1307 CG PRO A 189 16452 17434 17646 67 -222 -933 C ATOM 1308 CD PRO A 189 36.878 28.821 18.033 1.00138.60 C ANISOU 1308 CD PRO A 189 16793 17835 18032 87 -68 -866 C ATOM 1309 N LEU A 190 34.862 31.385 19.848 1.00121.04 N ANISOU 1309 N LEU A 190 14234 15447 16310 124 -200 -491 N ATOM 1310 CA LEU A 190 34.471 32.531 20.663 1.00121.99 C ANISOU 1310 CA LEU A 190 14214 15466 16671 153 -165 -386 C ATOM 1311 C LEU A 190 34.352 33.811 19.839 1.00126.51 C ANISOU 1311 C LEU A 190 14736 16058 17276 136 -141 -174 C ATOM 1312 O LEU A 190 33.775 34.797 20.295 1.00130.39 O ANISOU 1312 O LEU A 190 15107 16458 17977 154 -127 -52 O ATOM 1313 CB LEU A 190 35.461 32.740 21.811 1.00124.69 C ANISOU 1313 CB LEU A 190 14506 15718 17153 199 -37 -517 C ATOM 1314 CG LEU A 190 35.522 31.641 22.873 1.00125.84 C ANISOU 1314 CG LEU A 190 14677 15819 17316 209 -72 -693 C ATOM 1315 CD1 LEU A 190 36.718 31.849 23.791 1.00133.81 C ANISOU 1315 CD1 LEU A 190 15650 16765 18425 233 35 -799 C ATOM 1316 CD2 LEU A 190 34.231 31.586 23.671 1.00119.46 C ANISOU 1316 CD2 LEU A 190 13819 14947 16622 194 -151 -662 C ATOM 1317 N LEU A 191 34.907 33.795 18.631 1.00130.91 N ANISOU 1317 N LEU A 191 15385 16724 17631 98 -124 -130 N ATOM 1318 CA LEU A 191 34.785 34.932 17.725 1.00136.04 C ANISOU 1318 CA LEU A 191 16004 17407 18277 64 -121 95 C ATOM 1319 C LEU A 191 33.533 34.790 16.868 1.00135.81 C ANISOU 1319 C LEU A 191 16003 17451 18145 -11 -314 273 C ATOM 1320 O LEU A 191 32.922 35.784 16.473 1.00136.12 O ANISOU 1320 O LEU A 191 15958 17473 18290 -32 -372 508 O ATOM 1321 CB LEU A 191 36.027 35.069 16.842 1.00139.19 C ANISOU 1321 CB LEU A 191 16492 17892 18503 40 7 71 C ATOM 1322 CG LEU A 191 37.310 35.551 17.524 1.00133.89 C ANISOU 1322 CG LEU A 191 15756 17146 17971 102 194 -33 C ATOM 1323 CD1 LEU A 191 38.472 35.544 16.543 1.00137.48 C ANISOU 1323 CD1 LEU A 191 16297 17694 18245 73 324 -58 C ATOM 1324 CD2 LEU A 191 37.121 36.935 18.128 1.00127.93 C ANISOU 1324 CD2 LEU A 191 14854 16272 17482 132 238 104 C ATOM 1325 N LEU A 192 33.159 33.547 16.583 1.00136.37 N ANISOU 1325 N LEU A 192 16190 17599 18027 -58 -423 167 N ATOM 1326 CA LEU A 192 31.906 33.265 15.896 1.00144.84 C ANISOU 1326 CA LEU A 192 17288 18738 19007 -144 -635 319 C ATOM 1327 C LEU A 192 30.742 33.509 16.846 1.00145.31 C ANISOU 1327 C LEU A 192 17180 18680 19351 -100 -721 398 C ATOM 1328 O LEU A 192 29.748 34.133 16.479 1.00147.03 O ANISOU 1328 O LEU A 192 17302 18889 19675 -133 -849 635 O ATOM 1329 CB LEU A 192 31.878 31.819 15.395 1.00148.57 C ANISOU 1329 CB LEU A 192 17939 19309 19201 -215 -714 154 C ATOM 1330 CG LEU A 192 32.892 31.442 14.315 1.00149.05 C ANISOU 1330 CG LEU A 192 18188 19488 18955 -280 -621 63 C ATOM 1331 CD1 LEU A 192 32.831 29.951 14.016 1.00148.99 C ANISOU 1331 CD1 LEU A 192 18348 19536 18723 -339 -674 -140 C ATOM 1332 CD2 LEU A 192 32.657 32.257 13.053 1.00149.82 C ANISOU 1332 CD2 LEU A 192 18335 19694 18894 -389 -694 309 C ATOM 1333 N MET A 193 30.878 33.012 18.072 1.00142.98 N ANISOU 1333 N MET A 193 16846 18292 19187 -29 -645 207 N ATOM 1334 CA MET A 193 29.858 33.189 19.098 1.00138.90 C ANISOU 1334 CA MET A 193 16183 17657 18937 9 -680 243 C ATOM 1335 C MET A 193 29.576 34.666 19.333 1.00141.20 C ANISOU 1335 C MET A 193 16308 17841 19503 52 -608 430 C ATOM 1336 O MET A 193 28.437 35.116 19.217 1.00150.40 O ANISOU 1336 O MET A 193 17350 18960 20837 40 -709 623 O ATOM 1337 CB MET A 193 30.292 32.523 20.405 1.00134.87 C ANISOU 1337 CB MET A 193 15682 17069 18495 63 -579 2 C ATOM 1338 CG MET A 193 30.537 31.029 20.281 1.00137.56 C ANISOU 1338 CG MET A 193 16169 17483 18615 32 -645 -181 C ATOM 1339 SD MET A 193 30.984 30.261 21.848 1.00150.20 S ANISOU 1339 SD MET A 193 17769 18987 20315 83 -558 -419 S ATOM 1340 CE MET A 193 29.552 30.674 22.834 1.00210.87 C ANISOU 1340 CE MET A 193 25302 26560 28261 86 -593 -325 C ATOM 1341 N LEU A 194 30.620 35.418 19.665 1.00133.10 N ANISOU 1341 N LEU A 194 15268 16762 18542 99 -433 376 N ATOM 1342 CA LEU A 194 30.488 36.855 19.857 1.00135.93 C ANISOU 1342 CA LEU A 194 15482 17004 19163 136 -343 537 C ATOM 1343 C LEU A 194 29.885 37.498 18.616 1.00141.97 C ANISOU 1343 C LEU A 194 16205 17822 19913 89 -473 828 C ATOM 1344 O LEU A 194 29.063 38.407 18.714 1.00146.88 O ANISOU 1344 O LEU A 194 16667 18335 20804 111 -491 1023 O ATOM 1345 CB LEU A 194 31.848 37.481 20.163 1.00136.63 C ANISOU 1345 CB LEU A 194 15593 17056 19266 169 -155 438 C ATOM 1346 CG LEU A 194 31.845 38.993 20.389 1.00139.30 C ANISOU 1346 CG LEU A 194 15794 17256 19879 203 -41 582 C ATOM 1347 CD1 LEU A 194 30.888 39.360 21.511 1.00140.15 C ANISOU 1347 CD1 LEU A 194 15768 17196 20288 240 7 571 C ATOM 1348 CD2 LEU A 194 33.249 39.497 20.687 1.00141.26 C ANISOU 1348 CD2 LEU A 194 16075 17479 20120 219 130 469 C ATOM 1349 N GLY A 195 30.296 37.014 17.448 1.00139.75 N ANISOU 1349 N GLY A 195 16071 17706 19323 15 -561 860 N ATOM 1350 CA GLY A 195 29.775 37.509 16.187 1.00138.21 C ANISOU 1350 CA GLY A 195 15873 17591 19048 -63 -712 1142 C ATOM 1351 C GLY A 195 28.298 37.206 16.021 1.00134.61 C ANISOU 1351 C GLY A 195 15333 17135 18677 -106 -931 1305 C ATOM 1352 O GLY A 195 27.570 37.958 15.374 1.00132.17 O ANISOU 1352 O GLY A 195 14922 16816 18480 -144 -1059 1597 O ATOM 1353 N VAL A 196 27.857 36.097 16.607 1.00133.75 N ANISOU 1353 N VAL A 196 15257 17031 18530 -104 -983 1129 N ATOM 1354 CA VAL A 196 26.451 35.713 16.562 1.00137.35 C ANISOU 1354 CA VAL A 196 15621 17479 19087 -145 -1185 1262 C ATOM 1355 C VAL A 196 25.608 36.626 17.444 1.00142.33 C ANISOU 1355 C VAL A 196 16003 17918 20157 -59 -1125 1388 C ATOM 1356 O VAL A 196 24.592 37.162 17.001 1.00142.37 O ANISOU 1356 O VAL A 196 15859 17889 20345 -85 -1270 1663 O ATOM 1357 CB VAL A 196 26.246 34.250 17.003 1.00133.22 C ANISOU 1357 CB VAL A 196 15202 17002 18413 -169 -1239 1028 C ATOM 1358 CG1 VAL A 196 24.780 33.988 17.305 1.00130.17 C ANISOU 1358 CG1 VAL A 196 14669 16560 18230 -187 -1399 1150 C ATOM 1359 CG2 VAL A 196 26.756 33.295 15.935 1.00133.17 C ANISOU 1359 CG2 VAL A 196 15431 17176 17992 -277 -1336 944 C ATOM 1360 N TYR A 197 26.034 36.801 18.691 1.00145.57 N ANISOU 1360 N TYR A 197 16369 18199 20740 34 -909 1187 N ATOM 1361 CA TYR A 197 25.326 37.671 19.623 1.00151.50 C ANISOU 1361 CA TYR A 197 16907 18751 21904 111 -796 1257 C ATOM 1362 C TYR A 197 25.250 39.100 19.093 1.00155.04 C ANISOU 1362 C TYR A 197 17218 19115 22575 135 -771 1524 C ATOM 1363 O TYR A 197 24.357 39.861 19.462 1.00159.74 O ANISOU 1363 O TYR A 197 17606 19549 23540 182 -741 1679 O ATOM 1364 CB TYR A 197 25.991 37.651 21.002 1.00151.95 C ANISOU 1364 CB TYR A 197 16989 18701 22046 177 -556 978 C ATOM 1365 CG TYR A 197 25.829 36.343 21.747 1.00148.59 C ANISOU 1365 CG TYR A 197 16649 18312 21495 160 -577 749 C ATOM 1366 CD1 TYR A 197 24.646 36.040 22.408 1.00143.99 C ANISOU 1366 CD1 TYR A 197 15948 17646 21116 164 -604 764 C ATOM 1367 CD2 TYR A 197 26.862 35.417 21.797 1.00147.05 C ANISOU 1367 CD2 TYR A 197 16643 18224 21003 140 -563 529 C ATOM 1368 CE1 TYR A 197 24.495 34.847 23.092 1.00139.90 C ANISOU 1368 CE1 TYR A 197 15512 17158 20485 141 -624 568 C ATOM 1369 CE2 TYR A 197 26.720 34.223 22.480 1.00144.59 C ANISOU 1369 CE2 TYR A 197 16406 17934 20597 124 -589 338 C ATOM 1370 CZ TYR A 197 25.535 33.944 23.126 1.00139.13 C ANISOU 1370 CZ TYR A 197 15608 17166 20089 120 -623 360 C ATOM 1371 OH TYR A 197 25.389 32.756 23.806 1.00133.00 O ANISOU 1371 OH TYR A 197 14908 16408 19218 96 -651 182 O ATOM 1372 N LEU A 198 26.193 39.457 18.227 1.00153.80 N ANISOU 1372 N LEU A 198 17173 19056 22208 101 -772 1580 N ATOM 1373 CA LEU A 198 26.187 40.768 17.589 1.00155.34 C ANISOU 1373 CA LEU A 198 17257 19187 22579 108 -770 1857 C ATOM 1374 C LEU A 198 24.966 40.922 16.692 1.00156.76 C ANISOU 1374 C LEU A 198 17317 19393 22850 48 -1025 2195 C ATOM 1375 O LEU A 198 24.362 41.991 16.629 1.00157.28 O ANISOU 1375 O LEU A 198 17181 19315 23263 86 -1029 2448 O ATOM 1376 CB LEU A 198 27.462 40.978 16.770 1.00155.23 C ANISOU 1376 CB LEU A 198 17410 19299 22273 63 -727 1846 C ATOM 1377 CG LEU A 198 28.765 41.160 17.548 1.00149.11 C ANISOU 1377 CG LEU A 198 16707 18474 21473 121 -476 1584 C ATOM 1378 CD1 LEU A 198 29.951 41.225 16.599 1.00147.22 C ANISOU 1378 CD1 LEU A 198 16625 18378 20933 65 -449 1588 C ATOM 1379 CD2 LEU A 198 28.701 42.404 18.420 1.00146.57 C ANISOU 1379 CD2 LEU A 198 16212 17923 21554 204 -292 1618 C ATOM 1380 N ARG A 199 24.610 39.845 15.998 1.00157.35 N ANISOU 1380 N ARG A 199 17514 19647 22626 -53 -1244 2203 N ATOM 1381 CA ARG A 199 23.464 39.856 15.098 1.00162.57 C ANISOU 1381 CA ARG A 199 18080 20360 23327 -141 -1530 2525 C ATOM 1382 C ARG A 199 22.158 39.687 15.869 1.00167.78 C ANISOU 1382 C ARG A 199 18521 20882 24343 -91 -1579 2573 C ATOM 1383 O ARG A 199 21.119 40.214 15.471 1.00171.25 O ANISOU 1383 O ARG A 199 18761 21259 25049 -109 -1744 2890 O ATOM 1384 CB ARG A 199 23.598 38.753 14.045 1.00163.06 C ANISOU 1384 CB ARG A 199 18378 20667 22910 -293 -1745 2499 C ATOM 1385 CG ARG A 199 24.913 38.770 13.281 1.00167.86 C ANISOU 1385 CG ARG A 199 19220 21419 23139 -352 -1666 2415 C ATOM 1386 CD ARG A 199 25.139 40.100 12.578 1.00178.36 C ANISOU 1386 CD ARG A 199 20476 22720 24572 -367 -1669 2714 C ATOM 1387 NE ARG A 199 26.331 40.073 11.735 1.00189.15 N ANISOU 1387 NE ARG A 199 22073 24242 25555 -445 -1602 2654 N ATOM 1388 CZ ARG A 199 27.559 40.358 12.161 1.00191.47 C ANISOU 1388 CZ ARG A 199 22431 24499 25821 -368 -1338 2448 C ATOM 1389 NH1 ARG A 199 27.764 40.694 13.428 1.00191.62 N ANISOU 1389 NH1 ARG A 199 22318 24337 26150 -223 -1132 2280 N ATOM 1390 NH2 ARG A 199 28.584 40.305 11.321 1.00190.71 N ANISOU 1390 NH2 ARG A 199 22531 24546 25384 -449 -1278 2410 N ATOM 1391 N ILE A 200 22.218 38.947 16.973 1.00165.28 N ANISOU 1391 N ILE A 200 18237 20518 24042 -33 -1433 2268 N ATOM 1392 CA ILE A 200 21.044 38.718 17.809 1.00163.49 C ANISOU 1392 CA ILE A 200 17818 20160 24140 12 -1436 2274 C ATOM 1393 C ILE A 200 20.466 40.026 18.337 1.00168.34 C ANISOU 1393 C ILE A 200 18156 20534 25272 114 -1294 2451 C ATOM 1394 O ILE A 200 19.365 40.422 17.962 1.00177.65 O ANISOU 1394 O ILE A 200 19119 21643 26738 106 -1447 2747 O ATOM 1395 CB ILE A 200 21.361 37.793 19.000 1.00159.16 C ANISOU 1395 CB ILE A 200 17371 19593 23510 52 -1265 1904 C ATOM 1396 CG1 ILE A 200 21.583 36.359 18.520 1.00163.43 C ANISOU 1396 CG1 ILE A 200 18136 20336 23625 -48 -1433 1756 C ATOM 1397 CG2 ILE A 200 20.233 37.828 20.018 1.00156.47 C ANISOU 1397 CG2 ILE A 200 16814 19078 23559 110 -1188 1905 C ATOM 1398 CD1 ILE A 200 21.779 35.364 19.642 1.00164.84 C ANISOU 1398 CD1 ILE A 200 18400 20493 23738 -18 -1307 1434 C ATOM 1399 N PHE A 201 21.216 40.695 19.206 1.00163.47 N ANISOU 1399 N PHE A 201 17544 19782 24787 206 -1002 2270 N ATOM 1400 CA PHE A 201 20.743 41.925 19.832 1.00167.13 C ANISOU 1400 CA PHE A 201 17765 19989 25749 304 -814 2381 C ATOM 1401 C PHE A 201 20.576 43.061 18.825 1.00173.38 C ANISOU 1401 C PHE A 201 18420 20732 26726 303 -925 2751 C ATOM 1402 O PHE A 201 19.819 44.002 19.061 1.00177.37 O ANISOU 1402 O PHE A 201 18669 21022 27701 373 -856 2946 O ATOM 1403 CB PHE A 201 21.680 42.348 20.967 1.00164.94 C ANISOU 1403 CB PHE A 201 17563 19589 25517 373 -483 2081 C ATOM 1404 CG PHE A 201 21.809 41.322 22.058 1.00166.29 C ANISOU 1404 CG PHE A 201 17853 19786 25542 369 -370 1742 C ATOM 1405 CD1 PHE A 201 20.829 41.196 23.028 1.00170.13 C ANISOU 1405 CD1 PHE A 201 18193 20124 26322 404 -259 1679 C ATOM 1406 CD2 PHE A 201 22.912 40.486 22.113 1.00165.47 C ANISOU 1406 CD2 PHE A 201 18001 19848 25022 327 -370 1496 C ATOM 1407 CE1 PHE A 201 20.945 40.253 24.032 1.00170.00 C ANISOU 1407 CE1 PHE A 201 18297 20137 26159 385 -162 1384 C ATOM 1408 CE2 PHE A 201 23.035 39.542 23.115 1.00164.52 C ANISOU 1408 CE2 PHE A 201 17984 19745 24780 317 -285 1211 C ATOM 1409 CZ PHE A 201 22.049 39.426 24.076 1.00167.75 C ANISOU 1409 CZ PHE A 201 18262 20018 25457 340 -187 1159 C ATOM 1410 N ALA A 202 21.284 42.971 17.703 1.00173.91 N ANISOU 1410 N ALA A 202 18656 20991 26432 218 -1089 2852 N ATOM 1411 CA ALA A 202 21.167 43.976 16.653 1.00176.16 C ANISOU 1411 CA ALA A 202 18839 21258 26834 190 -1226 3226 C ATOM 1412 C ALA A 202 19.824 43.857 15.944 1.00175.56 C ANISOU 1412 C ALA A 202 18579 21199 26924 130 -1532 3578 C ATOM 1413 O ALA A 202 19.208 44.862 15.589 1.00177.14 O ANISOU 1413 O ALA A 202 18549 21257 27499 158 -1598 3916 O ATOM 1414 CB ALA A 202 22.307 43.844 15.656 1.00176.22 C ANISOU 1414 CB ALA A 202 19100 21481 26373 95 -1302 3223 C ATOM 1415 N ALA A 203 19.376 42.622 15.743 1.00174.18 N ANISOU 1415 N ALA A 203 18503 21193 26486 42 -1726 3505 N ATOM 1416 CA ALA A 203 18.094 42.362 15.100 1.00177.76 C ANISOU 1416 CA ALA A 203 18792 21680 27068 -37 -2043 3820 C ATOM 1417 C ALA A 203 16.954 42.448 16.108 1.00176.60 C ANISOU 1417 C ALA A 203 18356 21312 27431 66 -1945 3827 C ATOM 1418 O ALA A 203 15.862 42.912 15.785 1.00178.58 O ANISOU 1418 O ALA A 203 18335 21460 28056 66 -2110 4169 O ATOM 1419 CB ALA A 203 18.104 40.998 14.427 1.00177.40 C ANISOU 1419 CB ALA A 203 18985 21903 26517 -192 -2293 3731 C ATOM 1420 N ALA A 204 17.220 41.998 17.330 1.00174.04 N ANISOU 1420 N ALA A 204 18088 20914 27124 147 -1672 3456 N ATOM 1421 CA ALA A 204 16.222 42.017 18.394 1.00175.64 C ANISOU 1421 CA ALA A 204 18050 20911 27775 236 -1523 3408 C ATOM 1422 C ALA A 204 15.721 43.432 18.658 1.00182.11 C ANISOU 1422 C ALA A 204 18564 21448 29182 350 -1367 3635 C ATOM 1423 O ALA A 204 14.536 43.642 18.918 1.00188.38 O ANISOU 1423 O ALA A 204 19068 22081 30428 394 -1385 3815 O ATOM 1424 CB ALA A 204 16.792 41.409 19.665 1.00171.16 C ANISOU 1424 CB ALA A 204 17637 20317 27078 287 -1232 2964 C ATOM 1425 N ARG A 205 16.629 44.400 18.592 1.00183.68 N ANISOU 1425 N ARG A 205 18819 21575 29395 399 -1204 3627 N ATOM 1426 CA ARG A 205 16.269 45.798 18.797 1.00188.02 C ANISOU 1426 CA ARG A 205 19097 21841 30500 506 -1042 3836 C ATOM 1427 C ARG A 205 15.600 46.380 17.557 1.00184.05 C ANISOU 1427 C ARG A 205 18399 21343 30188 460 -1362 4337 C ATOM 1428 O ARG A 205 14.938 47.415 17.628 1.00185.96 O ANISOU 1428 O ARG A 205 18341 21333 30980 546 -1298 4593 O ATOM 1429 CB ARG A 205 17.498 46.624 19.185 1.00198.16 C ANISOU 1429 CB ARG A 205 20517 23041 31735 562 -757 3645 C ATOM 1430 CG ARG A 205 17.832 46.590 20.671 1.00205.49 C ANISOU 1430 CG ARG A 205 21500 23820 32756 637 -374 3234 C ATOM 1431 CD ARG A 205 18.005 45.166 21.178 1.00208.98 C ANISOU 1431 CD ARG A 205 22155 24454 32793 578 -398 2916 C ATOM 1432 NE ARG A 205 18.326 45.123 22.601 1.00209.29 N ANISOU 1432 NE ARG A 205 22261 24363 32895 626 -52 2541 N ATOM 1433 CZ ARG A 205 19.562 45.130 23.089 1.00206.08 C ANISOU 1433 CZ ARG A 205 22086 24003 32211 615 120 2254 C ATOM 1434 NH1 ARG A 205 20.601 45.180 22.266 1.00203.77 N ANISOU 1434 NH1 ARG A 205 21967 23876 31581 571 0 2291 N ATOM 1435 NH2 ARG A 205 19.761 45.088 24.399 1.00204.66 N ANISOU 1435 NH2 ARG A 205 21964 23706 32093 636 411 1937 N ATOM 1436 N ARG A 206 15.780 45.713 16.421 1.00180.15 N ANISOU 1436 N ARG A 206 18080 21130 29240 315 -1705 4477 N ATOM 1437 CA ARG A 206 15.096 46.105 15.195 1.00183.10 C ANISOU 1437 CA ARG A 206 18298 21548 29723 229 -2066 4966 C ATOM 1438 C ARG A 206 13.667 45.575 15.198 1.00178.30 C ANISOU 1438 C ARG A 206 17444 20909 29394 203 -2283 5161 C ATOM 1439 O ARG A 206 12.758 46.207 14.660 1.00174.06 O ANISOU 1439 O ARG A 206 16616 20260 29258 199 -2485 5586 O ATOM 1440 CB ARG A 206 15.849 45.602 13.960 1.00188.31 C ANISOU 1440 CB ARG A 206 19266 22527 29757 56 -2340 5033 C ATOM 1441 CG ARG A 206 17.181 46.294 13.717 1.00195.86 C ANISOU 1441 CG ARG A 206 20416 23509 30493 68 -2171 4950 C ATOM 1442 CD ARG A 206 17.698 46.025 12.311 1.00203.34 C ANISOU 1442 CD ARG A 206 21603 24739 30916 -116 -2465 5132 C ATOM 1443 NE ARG A 206 17.947 44.606 12.071 1.00203.82 N ANISOU 1443 NE ARG A 206 21947 25069 30427 -238 -2587 4881 N ATOM 1444 CZ ARG A 206 19.133 44.023 12.207 1.00198.28 C ANISOU 1444 CZ ARG A 206 21550 24510 29276 -255 -2420 4518 C ATOM 1445 NH1 ARG A 206 20.186 44.735 12.584 1.00193.68 N ANISOU 1445 NH1 ARG A 206 21029 23843 28717 -165 -2136 4368 N ATOM 1446 NH2 ARG A 206 19.268 42.725 11.966 1.00197.16 N ANISOU 1446 NH2 ARG A 206 21643 24587 28683 -363 -2536 4309 N ATOM 1447 N GLN A 207 13.478 44.410 15.809 1.00175.88 N ANISOU 1447 N GLN A 207 17244 20696 28888 181 -2247 4860 N ATOM 1448 CA GLN A 207 12.148 43.833 15.959 1.00174.80 C ANISOU 1448 CA GLN A 207 16875 20520 29021 159 -2413 4996 C ATOM 1449 C GLN A 207 11.278 44.760 16.798 1.00185.05 C ANISOU 1449 C GLN A 207 17781 21470 31061 322 -2173 5111 C ATOM 1450 O GLN A 207 10.103 44.967 16.497 1.00198.04 O ANISOU 1450 O GLN A 207 19104 23012 33130 318 -2367 5462 O ATOM 1451 CB GLN A 207 12.228 42.454 16.618 1.00165.99 C ANISOU 1451 CB GLN A 207 15962 19542 27566 119 -2353 4605 C ATOM 1452 CG GLN A 207 13.067 41.440 15.855 1.00162.73 C ANISOU 1452 CG GLN A 207 15935 19449 26445 -36 -2557 4452 C ATOM 1453 CD GLN A 207 12.470 41.075 14.510 1.00167.02 C ANISOU 1453 CD GLN A 207 16478 20184 26798 -218 -3023 4809 C ATOM 1454 OE1 GLN A 207 11.326 41.416 14.212 1.00180.93 O ANISOU 1454 OE1 GLN A 207 17934 21850 28960 -234 -3230 5171 O ATOM 1455 NE2 GLN A 207 13.245 40.374 13.690 1.00155.29 N ANISOU 1455 NE2 GLN A 207 15335 18965 24702 -365 -3189 4709 N ATOM 1456 N LEU A 208 11.868 45.320 17.849 1.00183.18 N ANISOU 1456 N LEU A 208 17570 21046 30985 457 -1746 4814 N ATOM 1457 CA LEU A 208 11.156 46.237 18.731 1.00192.47 C ANISOU 1457 CA LEU A 208 18408 21869 32852 613 -1445 4860 C ATOM 1458 C LEU A 208 10.852 47.558 18.030 1.00209.07 C ANISOU 1458 C LEU A 208 20240 23786 35410 664 -1534 5300 C ATOM 1459 O LEU A 208 9.903 48.254 18.389 1.00218.57 O ANISOU 1459 O LEU A 208 21076 24703 37267 770 -1420 5496 O ATOM 1460 CB LEU A 208 11.964 46.492 20.004 1.00185.94 C ANISOU 1460 CB LEU A 208 17730 20905 32013 712 -970 4407 C ATOM 1461 CG LEU A 208 12.274 45.266 20.865 1.00185.26 C ANISOU 1461 CG LEU A 208 17893 20963 31534 671 -844 3970 C ATOM 1462 CD1 LEU A 208 13.134 45.651 22.059 1.00187.58 C ANISOU 1462 CD1 LEU A 208 18338 21123 31812 747 -404 3566 C ATOM 1463 CD2 LEU A 208 10.991 44.590 21.321 1.00187.67 C ANISOU 1463 CD2 LEU A 208 17981 21210 32116 671 -877 4003 C ATOM 1464 N LYS A 209 11.662 47.898 17.032 1.00213.41 N ANISOU 1464 N LYS A 209 20968 24491 35627 587 -1728 5459 N ATOM 1465 CA LYS A 209 11.465 49.132 16.280 1.00221.78 C ANISOU 1465 CA LYS A 209 21801 25396 37068 616 -1844 5901 C ATOM 1466 C LYS A 209 10.374 48.971 15.228 1.00230.00 C ANISOU 1466 C LYS A 209 22614 26513 38263 514 -2311 6403 C ATOM 1467 O LYS A 209 9.661 49.922 14.910 1.00231.43 O ANISOU 1467 O LYS A 209 22450 26473 39010 573 -2392 6812 O ATOM 1468 CB LYS A 209 12.771 49.585 15.624 1.00220.38 C ANISOU 1468 CB LYS A 209 21908 25356 36470 561 -1861 5887 C ATOM 1469 CG LYS A 209 12.660 50.913 14.892 1.00223.36 C ANISOU 1469 CG LYS A 209 22068 25562 37236 590 -1958 6337 C ATOM 1470 CD LYS A 209 13.986 51.325 14.273 1.00220.76 C ANISOU 1470 CD LYS A 209 22031 25376 36472 526 -1954 6306 C ATOM 1471 CE LYS A 209 13.861 52.656 13.547 1.00222.27 C ANISOU 1471 CE LYS A 209 22005 25388 37060 548 -2054 6773 C ATOM 1472 NZ LYS A 209 15.145 53.073 12.917 1.00218.62 N ANISOU 1472 NZ LYS A 209 21822 25066 36177 476 -2047 6760 N ATOM 1473 N GLN A 210 10.250 47.764 14.685 1.00235.54 N ANISOU 1473 N GLN A 210 23505 27520 38468 354 -2626 6378 N ATOM 1474 CA GLN A 210 9.190 47.469 13.728 1.00243.05 C ANISOU 1474 CA GLN A 210 24264 28568 39515 224 -3094 6828 C ATOM 1475 C GLN A 210 7.854 47.347 14.450 1.00244.74 C ANISOU 1475 C GLN A 210 24089 28561 40342 317 -3034 6907 C ATOM 1476 O GLN A 210 6.811 47.733 13.920 1.00250.86 O ANISOU 1476 O GLN A 210 24516 29232 41568 297 -3304 7370 O ATOM 1477 CB GLN A 210 9.495 46.186 12.954 1.00248.21 C ANISOU 1477 CB GLN A 210 25267 29611 39431 8 -3428 6738 C ATOM 1478 CG GLN A 210 10.755 46.256 12.108 1.00253.30 C ANISOU 1478 CG GLN A 210 26289 30489 39464 -105 -3507 6691 C ATOM 1479 CD GLN A 210 10.946 45.024 11.246 1.00256.05 C ANISOU 1479 CD GLN A 210 26963 31202 39123 -333 -3844 6636 C ATOM 1480 OE1 GLN A 210 10.033 44.213 11.092 1.00258.17 O ANISOU 1480 OE1 GLN A 210 27149 31552 39393 -430 -4100 6726 O ATOM 1481 NE2 GLN A 210 12.137 44.879 10.676 1.00254.10 N ANISOU 1481 NE2 GLN A 210 27088 31166 38293 -426 -3833 6482 N ATOM 1482 N MET A 211 7.894 46.809 15.665 1.00241.48 N ANISOU 1482 N MET A 211 23729 28074 39947 410 -2678 6463 N ATOM 1483 CA MET A 211 6.703 46.702 16.498 1.00247.56 C ANISOU 1483 CA MET A 211 24147 28617 41298 507 -2535 6476 C ATOM 1484 C MET A 211 6.376 48.060 17.106 1.00255.32 C ANISOU 1484 C MET A 211 24783 29197 43029 703 -2194 6591 C ATOM 1485 O MET A 211 5.496 48.180 17.960 1.00261.75 O ANISOU 1485 O MET A 211 25295 29760 44396 816 -1953 6553 O ATOM 1486 CB MET A 211 6.910 45.664 17.602 1.00242.63 C ANISOU 1486 CB MET A 211 23729 28058 40403 524 -2258 5956 C ATOM 1487 CG MET A 211 7.205 44.263 17.086 1.00240.55 C ANISOU 1487 CG MET A 211 23799 28160 39440 340 -2563 5812 C ATOM 1488 SD MET A 211 7.326 43.059 18.420 1.00150.15 S ANISOU 1488 SD MET A 211 12543 16753 27755 363 -2251 5252 S ATOM 1489 CE MET A 211 5.690 43.203 19.132 1.00338.42 C ANISOU 1489 CE MET A 211 35886 40311 52387 455 -2145 5434 C ATOM 1490 N GLU A 212 7.098 49.081 16.658 1.00255.60 N ANISOU 1490 N GLU A 212 24867 29165 43083 738 -2159 6726 N ATOM 1491 CA GLU A 212 6.900 50.439 17.141 1.00259.59 C ANISOU 1491 CA GLU A 212 25071 29280 44283 915 -1839 6840 C ATOM 1492 C GLU A 212 6.021 51.219 16.172 1.00259.42 C ANISOU 1492 C GLU A 212 24660 29126 44782 911 -2179 7471 C ATOM 1493 O GLU A 212 5.483 52.273 16.512 1.00262.03 O ANISOU 1493 O GLU A 212 24627 29091 45841 1063 -1968 7660 O ATOM 1494 CB GLU A 212 8.250 51.137 17.312 1.00266.42 C ANISOU 1494 CB GLU A 212 26214 30121 44891 959 -1571 6598 C ATOM 1495 CG GLU A 212 8.163 52.554 17.848 1.00276.68 C ANISOU 1495 CG GLU A 212 27244 31006 46875 1135 -1208 6668 C ATOM 1496 CD GLU A 212 9.521 53.215 17.957 1.00281.44 C ANISOU 1496 CD GLU A 212 28133 31602 47199 1155 -977 6441 C ATOM 1497 OE1 GLU A 212 10.530 52.562 17.614 1.00279.29 O ANISOU 1497 OE1 GLU A 212 28254 31650 46211 1038 -1097 6237 O ATOM 1498 OE2 GLU A 212 9.582 54.387 18.386 1.00286.42 O ANISOU 1498 OE2 GLU A 212 28589 31898 48340 1285 -669 6464 O ATOM 1499 N SER A 213 5.878 50.689 14.962 1.00257.46 N ANISOU 1499 N SER A 213 24493 29170 44159 726 -2707 7798 N ATOM 1500 CA SER A 213 5.073 51.332 13.931 1.00260.51 C ANISOU 1500 CA SER A 213 24542 29481 44959 678 -3110 8436 C ATOM 1501 C SER A 213 3.894 50.453 13.526 1.00260.09 C ANISOU 1501 C SER A 213 24288 29552 44980 558 -3511 8699 C ATOM 1502 O SER A 213 3.492 50.438 12.363 1.00262.49 O ANISOU 1502 O SER A 213 24516 30006 45212 399 -4017 9174 O ATOM 1503 CB SER A 213 5.931 51.650 12.705 1.00262.90 C ANISOU 1503 CB SER A 213 25108 30015 44767 529 -3430 8678 C ATOM 1504 OG SER A 213 7.006 52.509 13.042 1.00262.75 O ANISOU 1504 OG SER A 213 25250 29870 44713 635 -3074 8466 O ATOM 1505 N GLN A 214 3.344 49.724 14.492 1.00258.80 N ANISOU 1505 N GLN A 214 24045 29330 44956 620 -3287 8393 N ATOM 1506 CA GLN A 214 2.216 48.836 14.232 1.00263.58 C ANISOU 1506 CA GLN A 214 24455 30041 45653 509 -3629 8599 C ATOM 1507 C GLN A 214 0.902 49.443 14.716 1.00281.61 C ANISOU 1507 C GLN A 214 26153 31947 48899 662 -3515 8889 C ATOM 1508 O GLN A 214 0.830 49.979 15.822 1.00284.63 O ANISOU 1508 O GLN A 214 26375 32015 49755 864 -2998 8637 O ATOM 1509 CB GLN A 214 2.446 47.469 14.882 1.00250.54 C ANISOU 1509 CB GLN A 214 23116 28610 43469 445 -3510 8092 C ATOM 1510 CG GLN A 214 2.759 47.528 16.368 1.00242.34 C ANISOU 1510 CG GLN A 214 22121 27363 42595 630 -2893 7568 C ATOM 1511 CD GLN A 214 3.000 46.156 16.968 1.00237.89 C ANISOU 1511 CD GLN A 214 21871 27025 41493 553 -2811 7103 C ATOM 1512 OE1 GLN A 214 2.906 45.140 16.279 1.00238.71 O ANISOU 1512 OE1 GLN A 214 22149 27427 41122 369 -3203 7159 O ATOM 1513 NE2 GLN A 214 3.313 46.121 18.258 1.00234.10 N ANISOU 1513 NE2 GLN A 214 21469 26396 41081 683 -2300 6643 N ATOM 1514 N PRO A 215 -0.143 49.362 13.879 1.00291.22 N ANISOU 1514 N PRO A 215 27048 33189 50412 555 -3997 9424 N ATOM 1515 CA PRO A 215 -1.470 49.918 14.169 1.00300.05 C ANISOU 1515 CA PRO A 215 27562 33957 52487 683 -3963 9786 C ATOM 1516 C PRO A 215 -2.169 49.215 15.330 1.00308.18 C ANISOU 1516 C PRO A 215 28439 34867 53786 771 -3629 9450 C ATOM 1517 O PRO A 215 -3.264 49.622 15.718 1.00311.18 O ANISOU 1517 O PRO A 215 28315 34937 54981 893 -3519 9684 O ATOM 1518 CB PRO A 215 -2.246 49.671 12.870 1.00302.29 C ANISOU 1518 CB PRO A 215 27659 34420 52776 473 -4660 10396 C ATOM 1519 CG PRO A 215 -1.201 49.474 11.821 1.00298.76 C ANISOU 1519 CG PRO A 215 27693 34337 51485 270 -4998 10422 C ATOM 1520 CD PRO A 215 -0.071 48.795 12.522 1.00293.63 C ANISOU 1520 CD PRO A 215 27555 33863 50148 287 -4624 9744 C ATOM 1521 N LEU A 216 -1.547 48.174 15.873 1.00313.63 N ANISOU 1521 N LEU A 216 29554 35795 53818 709 -3465 8919 N ATOM 1522 CA LEU A 216 -2.140 47.420 16.973 1.00314.18 C ANISOU 1522 CA LEU A 216 29531 35784 54058 767 -3155 8583 C ATOM 1523 C LEU A 216 -1.150 47.197 18.115 1.00306.03 C ANISOU 1523 C LEU A 216 28882 34753 52643 857 -2608 7925 C ATOM 1524 O LEU A 216 0.060 47.162 17.894 1.00306.46 O ANISOU 1524 O LEU A 216 29371 35002 52068 807 -2597 7690 O ATOM 1525 CB LEU A 216 -2.699 46.085 16.467 1.00318.25 C ANISOU 1525 CB LEU A 216 30117 36610 54194 553 -3611 8666 C ATOM 1526 CG LEU A 216 -1.829 45.244 15.527 1.00317.66 C ANISOU 1526 CG LEU A 216 30554 36974 53169 321 -4022 8588 C ATOM 1527 CD1 LEU A 216 -0.630 44.655 16.254 1.00312.39 C ANISOU 1527 CD1 LEU A 216 30398 36459 51838 340 -3661 7954 C ATOM 1528 CD2 LEU A 216 -2.657 44.140 14.888 1.00318.58 C ANISOU 1528 CD2 LEU A 216 30618 37324 53102 103 -4527 8805 C ATOM 1529 N PRO A 217 -1.667 47.055 19.345 1.00290.78 N ANISOU 1529 N PRO A 217 26784 32600 51100 980 -2152 7634 N ATOM 1530 CA PRO A 217 -0.832 46.811 20.527 1.00275.68 C ANISOU 1530 CA PRO A 217 25215 30676 48853 1047 -1631 7018 C ATOM 1531 C PRO A 217 0.062 45.586 20.352 1.00255.75 C ANISOU 1531 C PRO A 217 23222 28561 45390 879 -1820 6687 C ATOM 1532 O PRO A 217 1.278 45.725 20.222 1.00252.63 O ANISOU 1532 O PRO A 217 23210 28303 44474 861 -1765 6465 O ATOM 1533 CB PRO A 217 -1.861 46.561 21.632 1.00276.27 C ANISOU 1533 CB PRO A 217 24983 30514 49474 1136 -1269 6875 C ATOM 1534 CG PRO A 217 -3.071 47.303 21.188 1.00283.45 C ANISOU 1534 CG PRO A 217 25308 31152 51238 1213 -1416 7413 C ATOM 1535 CD PRO A 217 -3.093 47.179 19.693 1.00289.28 C ANISOU 1535 CD PRO A 217 26051 32140 51724 1058 -2091 7894 C ATOM 1536 N GLY A 218 -0.541 44.401 20.349 1.00242.08 N ANISOU 1536 N GLY A 218 21499 27008 43473 759 -2034 6660 N ATOM 1537 CA GLY A 218 0.200 43.166 20.163 1.00227.10 C ANISOU 1537 CA GLY A 218 20074 25478 40736 598 -2225 6364 C ATOM 1538 C GLY A 218 1.363 43.020 21.125 1.00220.39 C ANISOU 1538 C GLY A 218 19626 24658 39455 655 -1790 5805 C ATOM 1539 O GLY A 218 2.500 42.802 20.707 1.00224.10 O ANISOU 1539 O GLY A 218 20496 25355 39299 584 -1895 5641 O ATOM 1540 N GLU A 219 1.079 43.141 22.417 1.00210.60 N ANISOU 1540 N GLU A 219 18279 23187 38551 771 -1299 5517 N ATOM 1541 CA GLU A 219 2.109 43.007 23.441 1.00204.49 C ANISOU 1541 CA GLU A 219 17870 22427 37401 810 -878 4992 C ATOM 1542 C GLU A 219 2.528 41.553 23.624 1.00201.46 C ANISOU 1542 C GLU A 219 17855 22346 36344 671 -1004 4682 C ATOM 1543 O GLU A 219 3.474 41.259 24.354 1.00199.88 O ANISOU 1543 O GLU A 219 17999 22214 35732 672 -742 4264 O ATOM 1544 CB GLU A 219 1.629 43.594 24.769 1.00200.44 C ANISOU 1544 CB GLU A 219 17139 21571 37449 952 -310 4785 C ATOM 1545 CG GLU A 219 1.346 45.086 24.716 1.00203.29 C ANISOU 1545 CG GLU A 219 17164 21591 38486 1105 -105 5026 C ATOM 1546 CD GLU A 219 2.572 45.898 24.345 1.00203.31 C ANISOU 1546 CD GLU A 219 17417 21619 38212 1135 -80 4973 C ATOM 1547 OE1 GLU A 219 2.409 47.004 23.789 1.00204.75 O ANISOU 1547 OE1 GLU A 219 17349 21611 38834 1219 -126 5302 O ATOM 1548 OE2 GLU A 219 3.699 45.428 24.606 1.00198.16 O ANISOU 1548 OE2 GLU A 219 17200 21171 36919 1073 -18 4615 O ATOM 1549 N ARG A 220 1.816 40.649 22.961 1.00199.55 N ANISOU 1549 N ARG A 220 17534 22276 36009 546 -1412 4897 N ATOM 1550 CA ARG A 220 2.157 39.233 22.998 1.00193.93 C ANISOU 1550 CA ARG A 220 17159 21848 34679 405 -1577 4642 C ATOM 1551 C ARG A 220 3.467 38.976 22.265 1.00190.58 C ANISOU 1551 C ARG A 220 17167 21691 33555 322 -1785 4522 C ATOM 1552 O ARG A 220 4.333 38.254 22.755 1.00190.09 O ANISOU 1552 O ARG A 220 17466 21770 32988 286 -1658 4139 O ATOM 1553 CB ARG A 220 1.031 38.391 22.392 1.00196.30 C ANISOU 1553 CB ARG A 220 17251 22250 35083 278 -1981 4926 C ATOM 1554 CG ARG A 220 -0.016 37.949 23.397 1.00198.46 C ANISOU 1554 CG ARG A 220 17270 22364 35773 308 -1740 4840 C ATOM 1555 CD ARG A 220 0.558 36.921 24.358 1.00191.53 C ANISOU 1555 CD ARG A 220 16746 21600 34426 265 -1504 4358 C ATOM 1556 NE ARG A 220 -0.368 36.611 25.443 1.00192.21 N ANISOU 1556 NE ARG A 220 16607 21514 34912 298 -1198 4247 N ATOM 1557 CZ ARG A 220 -0.324 37.178 26.643 1.00191.02 C ANISOU 1557 CZ ARG A 220 16405 21133 35041 418 -668 4000 C ATOM 1558 NH1 ARG A 220 0.605 38.082 26.918 1.00185.88 N ANISOU 1558 NH1 ARG A 220 15911 20396 34320 514 -400 3837 N ATOM 1559 NH2 ARG A 220 -1.208 36.837 27.571 1.00195.76 N ANISOU 1559 NH2 ARG A 220 16806 21591 35984 427 -399 3910 N ATOM 1560 N ALA A 221 3.609 39.577 21.090 1.00188.41 N ANISOU 1560 N ALA A 221 16846 21478 33262 289 -2100 4862 N ATOM 1561 CA ALA A 221 4.835 39.436 20.315 1.00187.40 C ANISOU 1561 CA ALA A 221 17108 21592 32503 209 -2281 4778 C ATOM 1562 C ALA A 221 5.988 40.175 20.987 1.00196.40 C ANISOU 1562 C ALA A 221 18442 22635 33545 331 -1877 4478 C ATOM 1563 O ALA A 221 7.151 39.807 20.823 1.00191.76 O ANISOU 1563 O ALA A 221 18230 22236 32393 282 -1885 4237 O ATOM 1564 CB ALA A 221 4.632 39.940 18.898 1.00182.19 C ANISOU 1564 CB ALA A 221 16342 21018 31866 126 -2712 5241 C ATOM 1565 N ARG A 222 5.659 41.216 21.746 1.00204.58 N ANISOU 1565 N ARG A 222 19217 23368 35147 483 -1520 4492 N ATOM 1566 CA ARG A 222 6.662 41.976 22.485 1.00202.44 C ANISOU 1566 CA ARG A 222 19108 22973 34839 590 -1114 4203 C ATOM 1567 C ARG A 222 7.136 41.205 23.712 1.00188.38 C ANISOU 1567 C ARG A 222 17580 21225 32772 587 -797 3717 C ATOM 1568 O ARG A 222 8.335 41.018 23.911 1.00183.86 O ANISOU 1568 O ARG A 222 17353 20778 31730 567 -702 3428 O ATOM 1569 CB ARG A 222 6.109 43.337 22.912 1.00213.14 C ANISOU 1569 CB ARG A 222 20102 23970 36913 743 -819 4365 C ATOM 1570 CG ARG A 222 6.693 44.516 22.151 1.00218.43 C ANISOU 1570 CG ARG A 222 20748 24575 37671 791 -883 4597 C ATOM 1571 CD ARG A 222 6.347 45.831 22.831 1.00223.63 C ANISOU 1571 CD ARG A 222 21111 24848 39009 954 -486 4640 C ATOM 1572 NE ARG A 222 6.845 46.984 22.088 1.00226.53 N ANISOU 1572 NE ARG A 222 21431 25132 39507 1000 -556 4892 N ATOM 1573 CZ ARG A 222 6.114 47.695 21.236 1.00232.19 C ANISOU 1573 CZ ARG A 222 21811 25729 40681 1027 -796 5379 C ATOM 1574 NH1 ARG A 222 4.846 47.374 21.020 1.00237.99 N ANISOU 1574 NH1 ARG A 222 22214 26413 41799 1014 -994 5666 N ATOM 1575 NH2 ARG A 222 6.649 48.731 20.603 1.00230.12 N ANISOU 1575 NH2 ARG A 222 21534 25393 40507 1062 -845 5593 N ATOM 1576 N SER A 223 6.188 40.765 24.532 1.00184.89 N ANISOU 1576 N SER A 223 16955 20666 32627 601 -637 3643 N ATOM 1577 CA SER A 223 6.509 40.012 25.739 1.00181.00 C ANISOU 1577 CA SER A 223 16683 20197 31891 582 -342 3212 C ATOM 1578 C SER A 223 7.287 38.747 25.399 1.00181.51 C ANISOU 1578 C SER A 223 17126 20581 31259 455 -598 3026 C ATOM 1579 O SER A 223 8.197 38.355 26.128 1.00187.38 O ANISOU 1579 O SER A 223 18169 21391 31635 441 -400 2667 O ATOM 1580 CB SER A 223 5.235 39.655 26.507 1.00185.37 C ANISOU 1580 CB SER A 223 16960 20597 32876 594 -183 3220 C ATOM 1581 OG SER A 223 5.537 38.923 27.681 1.00183.77 O ANISOU 1581 OG SER A 223 16982 20421 32421 559 97 2818 O ATOM 1582 N THR A 224 6.923 38.112 24.290 1.00179.38 N ANISOU 1582 N THR A 224 16840 20500 30818 355 -1040 3275 N ATOM 1583 CA THR A 224 7.619 36.915 23.833 1.00175.62 C ANISOU 1583 CA THR A 224 16712 20313 29701 230 -1295 3118 C ATOM 1584 C THR A 224 9.016 37.269 23.334 1.00167.01 C ANISOU 1584 C THR A 224 15919 19347 28190 232 -1314 3015 C ATOM 1585 O THR A 224 9.978 36.539 23.571 1.00157.32 O ANISOU 1585 O THR A 224 15020 18271 26483 188 -1278 2717 O ATOM 1586 CB THR A 224 6.844 36.203 22.707 1.00173.49 C ANISOU 1586 CB THR A 224 16355 20206 29357 101 -1767 3417 C ATOM 1587 OG1 THR A 224 5.558 35.800 23.191 1.00170.27 O ANISOU 1587 OG1 THR A 224 15666 19689 29340 91 -1755 3507 O ATOM 1588 CG2 THR A 224 7.605 34.976 22.229 1.00171.03 C ANISOU 1588 CG2 THR A 224 16423 20175 28386 -31 -1998 3225 C ATOM 1589 N LEU A 225 9.118 38.401 22.645 1.00165.61 N ANISOU 1589 N LEU A 225 15610 19093 28220 284 -1367 3276 N ATOM 1590 CA LEU A 225 10.392 38.871 22.120 1.00156.38 C ANISOU 1590 CA LEU A 225 14687 18024 26707 287 -1375 3219 C ATOM 1591 C LEU A 225 11.357 39.187 23.259 1.00156.28 C ANISOU 1591 C LEU A 225 14848 17916 26615 369 -964 2845 C ATOM 1592 O LEU A 225 12.533 38.832 23.201 1.00164.06 O ANISOU 1592 O LEU A 225 16144 19054 27137 335 -954 2621 O ATOM 1593 CB LEU A 225 10.176 40.104 21.237 1.00154.30 C ANISOU 1593 CB LEU A 225 14205 17662 26758 327 -1495 3606 C ATOM 1594 CG LEU A 225 11.309 40.570 20.319 1.00141.71 C ANISOU 1594 CG LEU A 225 12831 16205 24809 295 -1613 3664 C ATOM 1595 CD1 LEU A 225 12.421 41.237 21.110 1.00137.86 C ANISOU 1595 CD1 LEU A 225 12492 15613 24275 392 -1236 3375 C ATOM 1596 CD2 LEU A 225 11.848 39.407 19.500 1.00138.41 C ANISOU 1596 CD2 LEU A 225 12726 16100 23764 145 -1914 3588 C ATOM 1597 N GLN A 226 10.851 39.846 24.297 1.00155.76 N ANISOU 1597 N GLN A 226 14579 17593 27008 466 -624 2776 N ATOM 1598 CA GLN A 226 11.672 40.217 25.445 1.00160.65 C ANISOU 1598 CA GLN A 226 15356 18104 27581 522 -226 2428 C ATOM 1599 C GLN A 226 12.038 39.008 26.301 1.00161.57 C ANISOU 1599 C GLN A 226 15725 18345 27319 455 -144 2073 C ATOM 1600 O GLN A 226 12.968 39.066 27.103 1.00161.12 O ANISOU 1600 O GLN A 226 15883 18278 27059 461 96 1773 O ATOM 1601 CB GLN A 226 10.965 41.270 26.301 1.00170.05 C ANISOU 1601 CB GLN A 226 16265 18970 29375 628 132 2448 C ATOM 1602 CG GLN A 226 10.706 42.583 25.583 1.00184.69 C ANISOU 1602 CG GLN A 226 17865 20656 31652 711 101 2782 C ATOM 1603 CD GLN A 226 10.113 43.639 26.495 1.00200.28 C ANISOU 1603 CD GLN A 226 19581 22283 34232 822 507 2757 C ATOM 1604 OE1 GLN A 226 10.219 43.550 27.718 1.00204.53 O ANISOU 1604 OE1 GLN A 226 20208 22716 34786 829 863 2428 O ATOM 1605 NE2 GLN A 226 9.488 44.650 25.903 1.00208.04 N ANISOU 1605 NE2 GLN A 226 20248 23078 35719 901 461 3106 N ATOM 1606 N LYS A 227 11.298 37.917 26.132 1.00164.64 N ANISOU 1606 N LYS A 227 16082 18846 27626 383 -356 2122 N ATOM 1607 CA LYS A 227 11.597 36.680 26.844 1.00168.08 C ANISOU 1607 CA LYS A 227 16753 19407 27704 310 -321 1822 C ATOM 1608 C LYS A 227 12.549 35.807 26.034 1.00168.20 C ANISOU 1608 C LYS A 227 17066 19687 27156 230 -604 1755 C ATOM 1609 O LYS A 227 13.211 34.923 26.577 1.00158.04 O ANISOU 1609 O LYS A 227 16026 18503 25519 183 -558 1481 O ATOM 1610 CB LYS A 227 10.315 35.912 27.171 1.00169.53 C ANISOU 1610 CB LYS A 227 16754 19558 28103 268 -374 1885 C ATOM 1611 CG LYS A 227 9.467 36.558 28.254 1.00176.69 C ANISOU 1611 CG LYS A 227 17413 20200 29521 338 -10 1852 C ATOM 1612 CD LYS A 227 8.214 35.747 28.533 1.00185.53 C ANISOU 1612 CD LYS A 227 18347 21299 30849 289 -67 1924 C ATOM 1613 CE LYS A 227 7.346 36.417 29.585 1.00189.12 C ANISOU 1613 CE LYS A 227 18541 21478 31836 357 328 1891 C ATOM 1614 NZ LYS A 227 6.089 35.658 29.835 1.00188.19 N ANISOU 1614 NZ LYS A 227 18214 21332 31958 310 283 1980 N ATOM 1615 N GLU A 228 12.607 36.059 24.730 1.00181.20 N ANISOU 1615 N GLU A 228 18686 21436 28726 207 -891 2014 N ATOM 1616 CA GLU A 228 13.561 35.383 23.860 1.00184.50 C ANISOU 1616 CA GLU A 228 19387 22091 28624 130 -1125 1956 C ATOM 1617 C GLU A 228 14.919 36.069 23.955 1.00178.50 C ANISOU 1617 C GLU A 228 18807 21332 27681 182 -948 1806 C ATOM 1618 O GLU A 228 15.963 35.423 23.861 1.00179.95 O ANISOU 1618 O GLU A 228 19264 21667 27443 143 -978 1603 O ATOM 1619 CB GLU A 228 13.067 35.384 22.412 1.00194.36 C ANISOU 1619 CB GLU A 228 20556 23457 29835 56 -1500 2294 C ATOM 1620 CG GLU A 228 11.855 34.498 22.162 1.00202.25 C ANISOU 1620 CG GLU A 228 21424 24503 30919 -32 -1746 2434 C ATOM 1621 CD GLU A 228 12.177 33.020 22.274 1.00206.53 C ANISOU 1621 CD GLU A 228 22226 25213 31032 -128 -1848 2186 C ATOM 1622 OE1 GLU A 228 13.376 32.672 22.313 1.00210.69 O ANISOU 1622 OE1 GLU A 228 23038 25843 31172 -132 -1779 1945 O ATOM 1623 OE2 GLU A 228 11.231 32.205 22.317 1.00206.60 O ANISOU 1623 OE2 GLU A 228 22146 25242 31113 -199 -1997 2238 O ATOM 1624 N VAL A 229 14.892 37.384 24.141 1.00168.90 N ANISOU 1624 N VAL A 229 17427 19937 26811 271 -760 1913 N ATOM 1625 CA VAL A 229 16.111 38.160 24.325 1.00160.62 C ANISOU 1625 CA VAL A 229 16518 18858 25653 319 -568 1779 C ATOM 1626 C VAL A 229 16.680 37.923 25.719 1.00153.87 C ANISOU 1626 C VAL A 229 15803 17935 24724 336 -265 1420 C ATOM 1627 O VAL A 229 17.894 37.847 25.900 1.00151.50 O ANISOU 1627 O VAL A 229 15728 17712 24125 326 -191 1220 O ATOM 1628 CB VAL A 229 15.856 39.666 24.122 1.00160.45 C ANISOU 1628 CB VAL A 229 16267 18639 26057 403 -453 2008 C ATOM 1629 CG1 VAL A 229 17.058 40.479 24.575 1.00163.70 C ANISOU 1629 CG1 VAL A 229 16813 18981 26402 450 -201 1826 C ATOM 1630 CG2 VAL A 229 15.527 39.953 22.667 1.00159.28 C ANISOU 1630 CG2 VAL A 229 16022 18582 25916 369 -779 2378 C ATOM 1631 N HIS A 230 15.794 37.799 26.702 1.00153.25 N ANISOU 1631 N HIS A 230 15591 17716 24923 350 -92 1348 N ATOM 1632 CA HIS A 230 16.210 37.527 28.072 1.00150.43 C ANISOU 1632 CA HIS A 230 15372 17299 24486 337 186 1021 C ATOM 1633 C HIS A 230 16.859 36.151 28.181 1.00138.72 C ANISOU 1633 C HIS A 230 14153 16021 22534 258 46 818 C ATOM 1634 O HIS A 230 17.590 35.875 29.131 1.00137.63 O ANISOU 1634 O HIS A 230 14193 15885 22216 232 215 554 O ATOM 1635 CB HIS A 230 15.019 37.623 29.026 1.00163.74 C ANISOU 1635 CB HIS A 230 16856 18798 26561 352 399 1003 C ATOM 1636 CG HIS A 230 15.373 37.379 30.460 1.00166.84 C ANISOU 1636 CG HIS A 230 17401 19128 26863 314 693 677 C ATOM 1637 ND1 HIS A 230 15.712 38.397 31.327 1.00166.12 N ANISOU 1637 ND1 HIS A 230 17315 18854 26951 342 1031 532 N ATOM 1638 CD2 HIS A 230 15.441 36.235 31.179 1.00166.20 C ANISOU 1638 CD2 HIS A 230 17483 19142 26524 235 693 474 C ATOM 1639 CE1 HIS A 230 15.973 37.888 32.518 1.00163.12 C ANISOU 1639 CE1 HIS A 230 17104 18471 26404 269 1219 255 C ATOM 1640 NE2 HIS A 230 15.815 36.579 32.456 1.00163.92 N ANISOU 1640 NE2 HIS A 230 17299 18739 26246 208 1016 224 N ATOM 1641 N ALA A 231 16.587 35.291 27.206 1.00133.31 N ANISOU 1641 N ALA A 231 13491 15501 21660 210 -266 949 N ATOM 1642 CA ALA A 231 17.193 33.966 27.168 1.00130.51 C ANISOU 1642 CA ALA A 231 13379 15329 20882 139 -411 773 C ATOM 1643 C ALA A 231 18.459 33.981 26.320 1.00141.49 C ANISOU 1643 C ALA A 231 14965 16864 21933 135 -524 747 C ATOM 1644 O ALA A 231 19.408 33.242 26.588 1.00146.67 O ANISOU 1644 O ALA A 231 15838 17616 22273 106 -520 534 O ATOM 1645 CB ALA A 231 16.205 32.942 26.635 1.00129.30 C ANISOU 1645 CB ALA A 231 13165 15264 20700 74 -668 894 C ATOM 1646 N ALA A 232 18.469 34.829 25.296 1.00142.59 N ANISOU 1646 N ALA A 232 15016 17011 22152 161 -622 975 N ATOM 1647 CA ALA A 232 19.643 34.984 24.446 1.00137.86 C ANISOU 1647 CA ALA A 232 14585 16538 21257 153 -700 970 C ATOM 1648 C ALA A 232 20.746 35.727 25.192 1.00134.04 C ANISOU 1648 C ALA A 232 14182 15973 20774 205 -439 792 C ATOM 1649 O ALA A 232 21.932 35.486 24.968 1.00134.51 O ANISOU 1649 O ALA A 232 14429 16138 20541 193 -444 665 O ATOM 1650 CB ALA A 232 19.281 35.715 23.163 1.00138.36 C ANISOU 1650 CB ALA A 232 14531 16631 21409 148 -880 1287 C ATOM 1651 N LYS A 233 20.346 36.632 26.080 1.00132.05 N ANISOU 1651 N LYS A 233 13783 15526 20863 257 -206 782 N ATOM 1652 CA LYS A 233 21.299 37.378 26.890 1.00130.01 C ANISOU 1652 CA LYS A 233 13600 15172 20627 286 49 605 C ATOM 1653 C LYS A 233 21.877 36.494 27.987 1.00132.48 C ANISOU 1653 C LYS A 233 14094 15522 20719 240 145 308 C ATOM 1654 O LYS A 233 23.078 36.531 28.258 1.00139.03 O ANISOU 1654 O LYS A 233 15081 16394 21349 228 213 151 O ATOM 1655 CB LYS A 233 20.645 38.619 27.501 1.00129.95 C ANISOU 1655 CB LYS A 233 13389 14927 21060 342 285 673 C ATOM 1656 CG LYS A 233 21.592 39.448 28.355 1.00134.30 C ANISOU 1656 CG LYS A 233 14024 15364 21638 352 553 483 C ATOM 1657 CD LYS A 233 20.927 40.713 28.874 1.00146.28 C ANISOU 1657 CD LYS A 233 15344 16627 23609 405 802 545 C ATOM 1658 CE LYS A 233 21.904 41.545 29.694 1.00151.38 C ANISOU 1658 CE LYS A 233 16096 17161 24261 393 1061 344 C ATOM 1659 NZ LYS A 233 21.294 42.811 30.186 1.00159.11 N ANISOU 1659 NZ LYS A 233 16895 17869 25692 440 1330 385 N ATOM 1660 N SER A 234 21.018 35.701 28.619 1.00127.26 N ANISOU 1660 N SER A 234 13402 14844 20105 206 143 248 N ATOM 1661 CA SER A 234 21.469 34.762 29.636 1.00131.24 C ANISOU 1661 CA SER A 234 14078 15390 20397 148 203 -3 C ATOM 1662 C SER A 234 22.457 33.776 29.026 1.00134.15 C ANISOU 1662 C SER A 234 14639 15946 20384 121 7 -74 C ATOM 1663 O SER A 234 23.413 33.358 29.677 1.00144.59 O ANISOU 1663 O SER A 234 16122 17304 21512 91 63 -267 O ATOM 1664 CB SER A 234 20.284 34.020 30.255 1.00140.60 C ANISOU 1664 CB SER A 234 15187 16536 21698 111 207 -18 C ATOM 1665 OG SER A 234 19.438 34.913 30.958 1.00150.37 O ANISOU 1665 OG SER A 234 16252 17582 23300 134 441 11 O ATOM 1666 N ALA A 235 22.225 33.416 27.767 1.00129.79 N ANISOU 1666 N ALA A 235 14069 15508 19736 124 -221 86 N ATOM 1667 CA ALA A 235 23.133 32.536 27.040 1.00128.06 C ANISOU 1667 CA ALA A 235 14030 15456 19173 99 -385 21 C ATOM 1668 C ALA A 235 24.448 33.248 26.737 1.00108.41 C ANISOU 1668 C ALA A 235 11622 12990 16578 131 -305 -16 C ATOM 1669 O ALA A 235 25.505 32.620 26.669 1.00 96.27 O ANISOU 1669 O ALA A 235 10242 11544 14793 118 -333 -154 O ATOM 1670 CB ALA A 235 22.485 32.051 25.755 1.00136.98 C ANISOU 1670 CB ALA A 235 15132 16695 20220 70 -634 200 C ATOM 1671 N ALA A 236 24.373 34.563 26.555 1.00105.36 N ANISOU 1671 N ALA A 236 11116 12511 16406 174 -202 114 N ATOM 1672 CA ALA A 236 25.558 35.367 26.290 1.00107.51 C ANISOU 1672 CA ALA A 236 11444 12788 16617 200 -113 97 C ATOM 1673 C ALA A 236 26.439 35.458 27.529 1.00114.33 C ANISOU 1673 C ALA A 236 12396 13587 17458 189 72 -131 C ATOM 1674 O ALA A 236 27.666 35.469 27.430 1.00115.04 O ANISOU 1674 O ALA A 236 12593 13734 17382 187 94 -220 O ATOM 1675 CB ALA A 236 25.163 36.756 25.816 1.00104.24 C ANISOU 1675 CB ALA A 236 10867 12270 16469 243 -53 309 C ATOM 1676 N ILE A 237 25.807 35.524 28.696 1.00116.58 N ANISOU 1676 N ILE A 237 12634 13752 17909 170 205 -220 N ATOM 1677 CA ILE A 237 26.545 35.620 29.950 1.00117.13 C ANISOU 1677 CA ILE A 237 12800 13760 17945 129 371 -430 C ATOM 1678 C ILE A 237 27.225 34.297 30.289 1.00116.45 C ANISOU 1678 C ILE A 237 12876 13792 17578 82 264 -586 C ATOM 1679 O ILE A 237 28.314 34.278 30.862 1.00109.91 O ANISOU 1679 O ILE A 237 12152 12974 16635 50 318 -722 O ATOM 1680 CB ILE A 237 25.637 36.059 31.115 1.00112.88 C ANISOU 1680 CB ILE A 237 12185 13058 17645 101 565 -490 C ATOM 1681 CG1 ILE A 237 24.895 37.347 30.755 1.00113.38 C ANISOU 1681 CG1 ILE A 237 12062 12977 18042 160 679 -323 C ATOM 1682 CG2 ILE A 237 26.456 36.263 32.379 1.00112.69 C ANISOU 1682 CG2 ILE A 237 12285 12976 17554 29 732 -704 C ATOM 1683 CD1 ILE A 237 24.076 37.916 31.891 1.00111.20 C ANISOU 1683 CD1 ILE A 237 11705 12512 18035 138 924 -400 C ATOM 1684 N ILE A 238 26.580 33.192 29.929 1.00120.31 N ANISOU 1684 N ILE A 238 13376 14361 17974 74 104 -557 N ATOM 1685 CA ILE A 238 27.167 31.872 30.119 1.00124.01 C ANISOU 1685 CA ILE A 238 13987 14930 18202 38 -11 -686 C ATOM 1686 C ILE A 238 28.394 31.714 29.229 1.00132.26 C ANISOU 1686 C ILE A 238 15114 16079 19059 68 -89 -694 C ATOM 1687 O ILE A 238 29.449 31.260 29.677 1.00131.65 O ANISOU 1687 O ILE A 238 15138 16030 18854 50 -82 -823 O ATOM 1688 CB ILE A 238 26.168 30.756 29.780 1.00120.57 C ANISOU 1688 CB ILE A 238 13542 14550 17721 20 -170 -642 C ATOM 1689 CG1 ILE A 238 24.877 30.937 30.574 1.00135.97 C ANISOU 1689 CG1 ILE A 238 15383 16393 19885 -6 -82 -614 C ATOM 1690 CG2 ILE A 238 26.776 29.392 30.067 1.00116.73 C ANISOU 1690 CG2 ILE A 238 13200 14137 17017 -16 -272 -781 C ATOM 1691 CD1 ILE A 238 23.775 29.991 30.156 1.00149.76 C ANISOU 1691 CD1 ILE A 238 17085 18184 21633 -27 -242 -537 C ATOM 1692 N ALA A 239 28.247 32.093 27.964 1.00136.61 N ANISOU 1692 N ALA A 239 15618 16685 19602 106 -162 -545 N ATOM 1693 CA ALA A 239 29.338 32.003 27.002 1.00138.78 C ANISOU 1693 CA ALA A 239 15970 17060 19700 128 -211 -543 C ATOM 1694 C ALA A 239 30.468 32.954 27.371 1.00142.16 C ANISOU 1694 C ALA A 239 16400 17441 20175 143 -63 -590 C ATOM 1695 O ALA A 239 31.644 32.603 27.276 1.00147.81 O ANISOU 1695 O ALA A 239 17196 18210 20755 147 -60 -681 O ATOM 1696 CB ALA A 239 28.833 32.303 25.607 1.00142.28 C ANISOU 1696 CB ALA A 239 16371 17572 20117 139 -315 -356 C ATOM 1697 N GLY A 240 30.101 34.160 27.792 1.00139.96 N ANISOU 1697 N GLY A 240 16023 17049 20107 151 65 -527 N ATOM 1698 CA GLY A 240 31.074 35.171 28.160 1.00135.32 C ANISOU 1698 CA GLY A 240 15431 16398 19587 152 209 -566 C ATOM 1699 C GLY A 240 31.979 34.733 29.294 1.00129.51 C ANISOU 1699 C GLY A 240 14786 15648 18774 104 258 -756 C ATOM 1700 O GLY A 240 33.176 35.025 29.292 1.00123.81 O ANISOU 1700 O GLY A 240 14098 14943 18002 99 298 -803 O ATOM 1701 N LEU A 241 31.407 34.029 30.266 1.00133.23 N ANISOU 1701 N LEU A 241 15292 16090 19240 57 246 -851 N ATOM 1702 CA LEU A 241 32.167 33.564 31.420 1.00131.60 C ANISOU 1702 CA LEU A 241 15177 15871 18952 -11 266 -1010 C ATOM 1703 C LEU A 241 33.160 32.465 31.052 1.00134.49 C ANISOU 1703 C LEU A 241 15621 16345 19134 1 136 -1063 C ATOM 1704 O LEU A 241 34.127 32.229 31.777 1.00146.60 O ANISOU 1704 O LEU A 241 17210 17876 20615 -45 135 -1158 O ATOM 1705 CB LEU A 241 31.231 33.082 32.532 1.00132.97 C ANISOU 1705 CB LEU A 241 15376 15988 19159 -78 291 -1082 C ATOM 1706 CG LEU A 241 30.408 34.158 33.244 1.00135.44 C ANISOU 1706 CG LEU A 241 15626 16163 19671 -111 476 -1082 C ATOM 1707 CD1 LEU A 241 29.580 33.541 34.359 1.00138.92 C ANISOU 1707 CD1 LEU A 241 16111 16562 20111 -191 512 -1170 C ATOM 1708 CD2 LEU A 241 31.310 35.254 33.788 1.00128.14 C ANISOU 1708 CD2 LEU A 241 14725 15163 18799 -156 617 -1148 C ATOM 1709 N PHE A 242 32.922 31.793 29.930 1.00124.63 N ANISOU 1709 N PHE A 242 14374 15184 17797 56 26 -999 N ATOM 1710 CA PHE A 242 33.841 30.759 29.466 1.00123.47 C ANISOU 1710 CA PHE A 242 14296 15120 17498 77 -68 -1058 C ATOM 1711 C PHE A 242 35.178 31.375 29.055 1.00125.02 C ANISOU 1711 C PHE A 242 14480 15335 17686 103 -2 -1058 C ATOM 1712 O PHE A 242 36.232 30.998 29.570 1.00121.05 O ANISOU 1712 O PHE A 242 14005 14831 17158 86 -7 -1142 O ATOM 1713 CB PHE A 242 33.239 29.969 28.301 1.00120.69 C ANISOU 1713 CB PHE A 242 13965 14849 17041 112 -181 -1003 C ATOM 1714 CG PHE A 242 34.065 28.784 27.881 1.00120.74 C ANISOU 1714 CG PHE A 242 14051 14918 16907 129 -255 -1090 C ATOM 1715 CD1 PHE A 242 33.782 27.517 28.366 1.00123.59 C ANISOU 1715 CD1 PHE A 242 14468 15274 17218 106 -351 -1170 C ATOM 1716 CD2 PHE A 242 35.127 28.937 27.005 1.00116.43 C ANISOU 1716 CD2 PHE A 242 13518 14424 16297 169 -213 -1091 C ATOM 1717 CE1 PHE A 242 34.540 26.425 27.985 1.00119.68 C ANISOU 1717 CE1 PHE A 242 14035 14809 16629 129 -405 -1253 C ATOM 1718 CE2 PHE A 242 35.888 27.849 26.620 1.00118.61 C ANISOU 1718 CE2 PHE A 242 13856 14736 16475 190 -250 -1181 C ATOM 1719 CZ PHE A 242 35.594 26.591 27.109 1.00116.93 C ANISOU 1719 CZ PHE A 242 13694 14503 16232 174 -347 -1263 C ATOM 1720 N ALA A 243 35.127 32.325 28.126 1.00126.92 N ANISOU 1720 N ALA A 243 14670 15591 17963 138 55 -947 N ATOM 1721 CA ALA A 243 36.326 33.017 27.669 1.00128.10 C ANISOU 1721 CA ALA A 243 14799 15755 18118 158 134 -930 C ATOM 1722 C ALA A 243 36.995 33.758 28.820 1.00127.33 C ANISOU 1722 C ALA A 243 14677 15570 18132 109 223 -992 C ATOM 1723 O ALA A 243 38.220 33.854 28.884 1.00132.40 O ANISOU 1723 O ALA A 243 15315 16222 18769 103 252 -1031 O ATOM 1724 CB ALA A 243 35.985 33.980 26.544 1.00130.10 C ANISOU 1724 CB ALA A 243 15003 16030 18399 189 175 -777 C ATOM 1725 N LEU A 244 36.182 34.278 29.732 1.00122.45 N ANISOU 1725 N LEU A 244 14045 14863 17619 63 272 -1003 N ATOM 1726 CA LEU A 244 36.690 35.026 30.874 1.00121.04 C ANISOU 1726 CA LEU A 244 13868 14593 17528 -12 365 -1075 C ATOM 1727 C LEU A 244 37.436 34.118 31.847 1.00121.04 C ANISOU 1727 C LEU A 244 13936 14611 17444 -78 287 -1194 C ATOM 1728 O LEU A 244 38.207 34.591 32.683 1.00121.40 O ANISOU 1728 O LEU A 244 13996 14610 17521 -157 326 -1252 O ATOM 1729 CB LEU A 244 35.543 35.739 31.596 1.00125.99 C ANISOU 1729 CB LEU A 244 14475 15110 18285 -52 463 -1076 C ATOM 1730 CG LEU A 244 35.927 36.691 32.731 1.00125.11 C ANISOU 1730 CG LEU A 244 14383 14887 18266 -148 592 -1161 C ATOM 1731 CD1 LEU A 244 36.826 37.801 32.214 1.00133.47 C ANISOU 1731 CD1 LEU A 244 15390 15918 19406 -132 671 -1107 C ATOM 1732 CD2 LEU A 244 34.688 37.270 33.398 1.00111.68 C ANISOU 1732 CD2 LEU A 244 12666 13067 16702 -183 718 -1178 C ATOM 1733 N CYS A 245 37.216 32.812 31.729 1.00125.20 N ANISOU 1733 N CYS A 245 14504 15201 17867 -55 167 -1220 N ATOM 1734 CA CYS A 245 37.823 31.859 32.653 1.00131.23 C ANISOU 1734 CA CYS A 245 15324 15971 18568 -117 73 -1307 C ATOM 1735 C CYS A 245 38.834 30.928 31.987 1.00132.50 C ANISOU 1735 C CYS A 245 15475 16198 18672 -55 -14 -1313 C ATOM 1736 O CYS A 245 39.397 30.048 32.638 1.00132.69 O ANISOU 1736 O CYS A 245 15524 16221 18671 -91 -109 -1362 O ATOM 1737 CB CYS A 245 36.742 31.043 33.365 1.00132.62 C ANISOU 1737 CB CYS A 245 15558 16132 18698 -162 13 -1345 C ATOM 1738 SG CYS A 245 35.644 32.027 34.414 1.00151.39 S ANISOU 1738 SG CYS A 245 17951 18411 21159 -256 149 -1371 S ATOM 1739 N TRP A 246 39.065 31.123 30.692 1.00133.62 N ANISOU 1739 N TRP A 246 15578 16390 18802 33 26 -1258 N ATOM 1740 CA TRP A 246 40.020 30.294 29.962 1.00132.53 C ANISOU 1740 CA TRP A 246 15430 16303 18621 94 -11 -1277 C ATOM 1741 C TRP A 246 41.095 31.122 29.262 1.00122.83 C ANISOU 1741 C TRP A 246 14137 15092 17442 127 90 -1237 C ATOM 1742 O TRP A 246 42.203 30.639 29.027 1.00117.28 O ANISOU 1742 O TRP A 246 13400 14403 16759 157 90 -1265 O ATOM 1743 CB TRP A 246 39.301 29.388 28.960 1.00132.16 C ANISOU 1743 CB TRP A 246 15429 16313 18470 155 -59 -1274 C ATOM 1744 CG TRP A 246 38.548 28.262 29.604 1.00134.53 C ANISOU 1744 CG TRP A 246 15787 16597 18732 127 -173 -1325 C ATOM 1745 CD1 TRP A 246 37.299 28.316 30.150 1.00141.89 C ANISOU 1745 CD1 TRP A 246 16744 17506 19662 82 -204 -1310 C ATOM 1746 CD2 TRP A 246 38.999 26.912 29.769 1.00136.94 C ANISOU 1746 CD2 TRP A 246 16121 16895 19014 141 -263 -1394 C ATOM 1747 NE1 TRP A 246 36.943 27.084 30.643 1.00145.83 N ANISOU 1747 NE1 TRP A 246 17295 17995 20121 61 -311 -1363 N ATOM 1748 CE2 TRP A 246 37.971 26.204 30.422 1.00139.05 C ANISOU 1748 CE2 TRP A 246 16441 17141 19250 97 -355 -1412 C ATOM 1749 CE3 TRP A 246 40.172 26.233 29.427 1.00138.10 C ANISOU 1749 CE3 TRP A 246 16245 17040 19188 190 -264 -1437 C ATOM 1750 CZ2 TRP A 246 38.080 24.853 30.740 1.00135.67 C ANISOU 1750 CZ2 TRP A 246 16051 16690 18808 96 -460 -1466 C ATOM 1751 CZ3 TRP A 246 40.277 24.891 29.743 1.00136.70 C ANISOU 1751 CZ3 TRP A 246 16096 16828 19016 197 -363 -1493 C ATOM 1752 CH2 TRP A 246 39.238 24.216 30.393 1.00135.89 C ANISOU 1752 CH2 TRP A 246 16054 16705 18874 148 -465 -1504 C ATOM 1753 N LEU A 247 40.767 32.368 28.931 1.00119.21 N ANISOU 1753 N LEU A 247 13651 14621 17022 122 183 -1164 N ATOM 1754 CA LEU A 247 41.735 33.266 28.309 1.00126.09 C ANISOU 1754 CA LEU A 247 14460 15501 17947 141 287 -1113 C ATOM 1755 C LEU A 247 43.020 33.403 29.129 1.00131.13 C ANISOU 1755 C LEU A 247 15046 16099 18678 92 288 -1158 C ATOM 1756 O LEU A 247 44.116 33.287 28.583 1.00127.01 O ANISOU 1756 O LEU A 247 14469 15604 18185 128 327 -1152 O ATOM 1757 CB LEU A 247 41.125 34.645 28.039 1.00126.29 C ANISOU 1757 CB LEU A 247 14458 15491 18034 130 377 -1018 C ATOM 1758 CG LEU A 247 40.254 34.776 26.788 1.00128.37 C ANISOU 1758 CG LEU A 247 14737 15813 18226 182 385 -915 C ATOM 1759 CD1 LEU A 247 39.884 36.232 26.551 1.00127.67 C ANISOU 1759 CD1 LEU A 247 14593 15668 18246 173 477 -798 C ATOM 1760 CD2 LEU A 247 40.971 34.205 25.575 1.00131.27 C ANISOU 1760 CD2 LEU A 247 15125 16277 18476 230 400 -907 C ATOM 1761 N PRO A 248 42.891 33.652 30.444 1.00129.57 N ANISOU 1761 N PRO A 248 14867 15836 18529 -1 246 -1200 N ATOM 1762 CA PRO A 248 44.089 33.772 31.283 1.00124.68 C ANISOU 1762 CA PRO A 248 14204 15183 17987 -75 213 -1229 C ATOM 1763 C PRO A 248 45.048 32.605 31.076 1.00132.49 C ANISOU 1763 C PRO A 248 15147 16206 18987 -27 134 -1248 C ATOM 1764 O PRO A 248 46.248 32.821 30.912 1.00135.55 O ANISOU 1764 O PRO A 248 15444 16590 19467 -24 161 -1226 O ATOM 1765 CB PRO A 248 43.521 33.736 32.702 1.00116.90 C ANISOU 1765 CB PRO A 248 13292 14143 16981 -194 144 -1287 C ATOM 1766 CG PRO A 248 42.159 34.306 32.563 1.00124.66 C ANISOU 1766 CG PRO A 248 14322 15101 17943 -184 225 -1277 C ATOM 1767 CD PRO A 248 41.654 33.856 31.220 1.00127.90 C ANISOU 1767 CD PRO A 248 14717 15577 18301 -57 236 -1222 C ATOM 1768 N LEU A 249 44.521 31.385 31.078 1.00136.78 N ANISOU 1768 N LEU A 249 15742 16770 19458 10 46 -1285 N ATOM 1769 CA LEU A 249 45.356 30.202 30.908 1.00127.82 C ANISOU 1769 CA LEU A 249 14561 15642 18362 62 -20 -1307 C ATOM 1770 C LEU A 249 46.009 30.175 29.530 1.00123.25 C ANISOU 1770 C LEU A 249 13923 15103 17802 168 101 -1294 C ATOM 1771 O LEU A 249 47.189 29.855 29.403 1.00128.84 O ANISOU 1771 O LEU A 249 14536 15795 18623 197 116 -1294 O ATOM 1772 CB LEU A 249 44.544 28.926 31.135 1.00123.53 C ANISOU 1772 CB LEU A 249 14096 15100 17741 79 -128 -1352 C ATOM 1773 CG LEU A 249 45.324 27.614 31.033 1.00114.93 C ANISOU 1773 CG LEU A 249 12958 13988 16720 135 -198 -1378 C ATOM 1774 CD1 LEU A 249 46.490 27.608 32.009 1.00123.15 C ANISOU 1774 CD1 LEU A 249 13907 14982 17904 68 -288 -1344 C ATOM 1775 CD2 LEU A 249 44.409 26.423 31.279 1.00114.61 C ANISOU 1775 CD2 LEU A 249 13005 13938 16604 141 -304 -1419 C ATOM 1776 N HIS A 250 45.236 30.512 28.502 1.00125.54 N ANISOU 1776 N HIS A 250 14269 15444 17985 215 188 -1277 N ATOM 1777 CA HIS A 250 45.742 30.522 27.133 1.00130.40 C ANISOU 1777 CA HIS A 250 14864 16110 18571 291 316 -1265 C ATOM 1778 C HIS A 250 46.700 31.684 26.898 1.00130.83 C ANISOU 1778 C HIS A 250 14825 16161 18723 276 431 -1203 C ATOM 1779 O HIS A 250 47.746 31.519 26.270 1.00131.00 O ANISOU 1779 O HIS A 250 14775 16194 18806 321 525 -1208 O ATOM 1780 CB HIS A 250 44.590 30.584 26.130 1.00140.06 C ANISOU 1780 CB HIS A 250 16188 17399 19632 316 346 -1241 C ATOM 1781 CG HIS A 250 43.689 29.389 26.169 1.00144.80 C ANISOU 1781 CG HIS A 250 16876 18007 20134 330 241 -1302 C ATOM 1782 ND1 HIS A 250 43.926 28.106 26.531 1.00139.06 N ANISOU 1782 ND1 HIS A 250 16230 17316 19288 317 197 -1270 N ATOM 1783 CD2 HIS A 250 42.360 29.448 25.811 1.00146.26 C ANISOU 1783 CD2 HIS A 250 17071 18158 20342 352 165 -1384 C ATOM 1784 CE1 HIS A 250 42.746 27.419 26.381 1.00137.50 C ANISOU 1784 CE1 HIS A 250 16096 17115 19034 324 101 -1337 C ATOM 1785 NE2 HIS A 250 41.818 28.250 25.945 1.00140.82 N ANISOU 1785 NE2 HIS A 250 16479 17489 19536 347 84 -1409 N ATOM 1786 N ILE A 251 46.334 32.861 27.398 1.00129.79 N ANISOU 1786 N ILE A 251 14692 16003 18618 212 439 -1150 N ATOM 1787 CA ILE A 251 47.194 34.035 27.303 1.00131.34 C ANISOU 1787 CA ILE A 251 14802 16180 18921 181 538 -1090 C ATOM 1788 C ILE A 251 48.569 33.730 27.880 1.00127.98 C ANISOU 1788 C ILE A 251 14264 15718 18644 160 509 -1111 C ATOM 1789 O ILE A 251 49.591 34.110 27.310 1.00130.07 O ANISOU 1789 O ILE A 251 14433 15990 18997 180 614 -1075 O ATOM 1790 CB ILE A 251 46.588 35.245 28.040 1.00131.43 C ANISOU 1790 CB ILE A 251 14833 16135 18970 99 537 -1054 C ATOM 1791 CG1 ILE A 251 45.355 35.761 27.297 1.00128.09 C ANISOU 1791 CG1 ILE A 251 14476 15736 18458 130 586 -992 C ATOM 1792 CG2 ILE A 251 47.618 36.353 28.185 1.00135.64 C ANISOU 1792 CG2 ILE A 251 15273 16626 19637 46 615 -1008 C ATOM 1793 CD1 ILE A 251 44.740 36.992 27.924 1.00131.72 C ANISOU 1793 CD1 ILE A 251 14939 16114 18995 64 620 -955 C ATOM 1794 N ILE A 252 48.588 33.035 29.013 1.00127.18 N ANISOU 1794 N ILE A 252 14168 15577 18578 111 361 -1157 N ATOM 1795 CA ILE A 252 49.838 32.633 29.643 1.00125.20 C ANISOU 1795 CA ILE A 252 13799 15287 18483 81 290 -1154 C ATOM 1796 C ILE A 252 50.662 31.742 28.716 1.00131.92 C ANISOU 1796 C ILE A 252 14565 16153 19405 193 365 -1167 C ATOM 1797 O ILE A 252 51.888 31.860 28.652 1.00141.34 O ANISOU 1797 O ILE A 252 15615 17321 20767 198 406 -1133 O ATOM 1798 CB ILE A 252 49.586 31.909 30.980 1.00123.73 C ANISOU 1798 CB ILE A 252 13654 15062 18294 1 95 -1183 C ATOM 1799 CG1 ILE A 252 49.161 32.917 32.051 1.00122.30 C ANISOU 1799 CG1 ILE A 252 13538 14851 18080 -142 48 -1181 C ATOM 1800 CG2 ILE A 252 50.831 31.158 31.428 1.00123.07 C ANISOU 1800 CG2 ILE A 252 13438 14942 18382 -5 -4 -1159 C ATOM 1801 CD1 ILE A 252 48.915 32.305 33.413 1.00123.26 C ANISOU 1801 CD1 ILE A 252 13723 14944 18166 -255 -134 -1207 C ATOM 1802 N ASN A 253 49.984 30.858 27.992 1.00128.47 N ANISOU 1802 N ASN A 253 14214 15750 18850 276 393 -1220 N ATOM 1803 CA ASN A 253 50.659 29.938 27.083 1.00130.96 C ANISOU 1803 CA ASN A 253 14474 16066 19218 377 492 -1263 C ATOM 1804 C ASN A 253 51.095 30.601 25.782 1.00139.70 C ANISOU 1804 C ASN A 253 15560 17225 20296 420 707 -1242 C ATOM 1805 O ASN A 253 51.948 30.077 25.064 1.00147.68 O ANISOU 1805 O ASN A 253 16496 18226 21389 488 836 -1275 O ATOM 1806 CB ASN A 253 49.775 28.725 26.801 1.00119.89 C ANISOU 1806 CB ASN A 253 13189 14673 17690 429 444 -1342 C ATOM 1807 CG ASN A 253 49.498 27.911 28.047 1.00120.20 C ANISOU 1807 CG ASN A 253 13237 14654 17779 389 240 -1355 C ATOM 1808 OD1 ASN A 253 48.348 27.689 28.418 1.00126.90 O ANISOU 1808 OD1 ASN A 253 14205 15518 18492 356 145 -1374 O ATOM 1809 ND2 ASN A 253 50.560 27.472 28.709 1.00133.52 N ANISOU 1809 ND2 ASN A 253 14787 16272 19671 384 169 -1329 N ATOM 1810 N CYS A 254 50.506 31.753 25.484 1.00138.47 N ANISOU 1810 N CYS A 254 15466 17115 20030 377 755 -1184 N ATOM 1811 CA CYS A 254 50.912 32.534 24.323 1.00132.91 C ANISOU 1811 CA CYS A 254 14746 16462 19291 395 945 -1135 C ATOM 1812 C CYS A 254 52.198 33.300 24.622 1.00123.53 C ANISOU 1812 C CYS A 254 13392 15232 18311 363 1008 -1077 C ATOM 1813 O CYS A 254 53.030 33.501 23.737 1.00120.16 O ANISOU 1813 O CYS A 254 12896 14827 17934 396 1182 -1058 O ATOM 1814 CB CYS A 254 49.800 33.495 23.903 1.00130.91 C ANISOU 1814 CB CYS A 254 14606 16259 18874 359 956 -1067 C ATOM 1815 SG CYS A 254 48.306 32.674 23.310 1.00128.26 S ANISOU 1815 SG CYS A 254 14450 15987 18296 386 890 -1109 S ATOM 1816 N PHE A 255 52.355 33.720 25.874 1.00123.49 N ANISOU 1816 N PHE A 255 13330 15168 18422 286 867 -1050 N ATOM 1817 CA PHE A 255 53.569 34.406 26.306 1.00137.95 C ANISOU 1817 CA PHE A 255 15000 16953 20461 233 886 -992 C ATOM 1818 C PHE A 255 54.766 33.463 26.319 1.00148.32 C ANISOU 1818 C PHE A 255 16156 18229 21970 286 897 -1011 C ATOM 1819 O PHE A 255 55.845 33.805 25.834 1.00146.37 O ANISOU 1819 O PHE A 255 15768 17972 21875 301 1031 -970 O ATOM 1820 CB PHE A 255 53.378 35.020 27.695 1.00137.60 C ANISOU 1820 CB PHE A 255 14963 16856 20464 110 716 -973 C ATOM 1821 CG PHE A 255 52.687 36.352 27.680 1.00141.89 C ANISOU 1821 CG PHE A 255 15585 17397 20928 46 766 -933 C ATOM 1822 CD1 PHE A 255 51.450 36.498 27.076 1.00149.15 C ANISOU 1822 CD1 PHE A 255 16642 18357 21672 87 812 -935 C ATOM 1823 CD2 PHE A 255 53.269 37.456 28.281 1.00141.75 C ANISOU 1823 CD2 PHE A 255 15500 17326 21033 -60 760 -887 C ATOM 1824 CE1 PHE A 255 50.809 37.723 27.063 1.00148.97 C ANISOU 1824 CE1 PHE A 255 16671 18312 21621 38 860 -883 C ATOM 1825 CE2 PHE A 255 52.631 38.683 28.273 1.00143.20 C ANISOU 1825 CE2 PHE A 255 15753 17483 21175 -114 820 -855 C ATOM 1826 CZ PHE A 255 51.400 38.816 27.663 1.00146.50 C ANISOU 1826 CZ PHE A 255 16291 17931 21441 -58 874 -849 C ATOM 1827 N THR A 256 54.569 32.275 26.882 1.00150.67 N ANISOU 1827 N THR A 256 16468 18495 22285 315 761 -1065 N ATOM 1828 CA THR A 256 55.643 31.297 26.991 1.00153.23 C ANISOU 1828 CA THR A 256 16627 18757 22834 371 752 -1072 C ATOM 1829 C THR A 256 56.095 30.796 25.623 1.00157.88 C ANISOU 1829 C THR A 256 17183 19361 23442 489 997 -1125 C ATOM 1830 O THR A 256 57.289 30.615 25.382 1.00170.53 O ANISOU 1830 O THR A 256 18600 20914 25279 530 1102 -1103 O ATOM 1831 CB THR A 256 55.232 30.098 27.866 1.00150.43 C ANISOU 1831 CB THR A 256 16309 18356 22491 376 549 -1109 C ATOM 1832 OG1 THR A 256 55.005 30.541 29.211 1.00147.82 O ANISOU 1832 OG1 THR A 256 16001 18010 22156 243 330 -1057 O ATOM 1833 CG2 THR A 256 56.326 29.040 27.869 1.00150.95 C ANISOU 1833 CG2 THR A 256 16190 18339 22825 452 553 -1104 C ATOM 1834 N PHE A 257 55.137 30.579 24.727 1.00150.49 N ANISOU 1834 N PHE A 257 16427 18491 22261 532 1093 -1194 N ATOM 1835 CA PHE A 257 55.444 30.062 23.399 1.00153.04 C ANISOU 1835 CA PHE A 257 16768 18836 22543 618 1333 -1266 C ATOM 1836 C PHE A 257 56.024 31.135 22.484 1.00158.56 C ANISOU 1836 C PHE A 257 17425 19589 23230 600 1551 -1210 C ATOM 1837 O PHE A 257 57.207 31.101 22.142 1.00164.66 O ANISOU 1837 O PHE A 257 18033 20322 24209 635 1709 -1201 O ATOM 1838 CB PHE A 257 54.200 29.450 22.756 1.00153.36 C ANISOU 1838 CB PHE A 257 17032 18937 22302 641 1337 -1354 C ATOM 1839 CG PHE A 257 54.453 28.855 21.400 1.00157.05 C ANISOU 1839 CG PHE A 257 17557 19430 22686 704 1581 -1450 C ATOM 1840 CD1 PHE A 257 54.726 27.504 21.262 1.00160.69 C ANISOU 1840 CD1 PHE A 257 18001 19814 23241 780 1628 -1567 C ATOM 1841 CD2 PHE A 257 54.421 29.646 20.263 1.00159.62 C ANISOU 1841 CD2 PHE A 257 17962 19848 22838 675 1772 -1425 C ATOM 1842 CE1 PHE A 257 54.959 26.953 20.016 1.00164.58 C ANISOU 1842 CE1 PHE A 257 18565 20320 23647 824 1879 -1680 C ATOM 1843 CE2 PHE A 257 54.656 29.100 19.015 1.00164.20 C ANISOU 1843 CE2 PHE A 257 18622 20458 23309 708 2010 -1524 C ATOM 1844 CZ PHE A 257 54.924 27.752 18.892 1.00166.14 C ANISOU 1844 CZ PHE A 257 18860 20624 23641 780 2073 -1663 C ATOM 1845 N PHE A 258 55.182 32.084 22.088 1.00159.51 N ANISOU 1845 N PHE A 258 17688 19793 23127 545 1560 -1161 N ATOM 1846 CA PHE A 258 55.582 33.122 21.142 1.00160.49 C ANISOU 1846 CA PHE A 258 17802 19974 23203 518 1760 -1091 C ATOM 1847 C PHE A 258 56.796 33.921 21.615 1.00161.51 C ANISOU 1847 C PHE A 258 17718 20048 23601 482 1794 -1004 C ATOM 1848 O PHE A 258 57.569 34.428 20.801 1.00163.28 O ANISOU 1848 O PHE A 258 17869 20294 23876 483 2006 -965 O ATOM 1849 CB PHE A 258 54.413 34.064 20.843 1.00155.21 C ANISOU 1849 CB PHE A 258 17299 19380 22293 457 1712 -1019 C ATOM 1850 CG PHE A 258 53.318 33.431 20.034 1.00147.37 C ANISOU 1850 CG PHE A 258 16509 18463 21022 477 1718 -1078 C ATOM 1851 CD1 PHE A 258 52.170 32.960 20.645 1.00150.07 C ANISOU 1851 CD1 PHE A 258 16958 18801 21263 473 1519 -1111 C ATOM 1852 CD2 PHE A 258 53.441 33.304 18.661 1.00143.74 C ANISOU 1852 CD2 PHE A 258 16139 18080 20395 482 1924 -1100 C ATOM 1853 CE1 PHE A 258 51.162 32.378 19.900 1.00154.28 C ANISOU 1853 CE1 PHE A 258 17668 19401 21549 478 1508 -1157 C ATOM 1854 CE2 PHE A 258 52.437 32.722 17.910 1.00145.44 C ANISOU 1854 CE2 PHE A 258 16554 18370 20338 475 1910 -1151 C ATOM 1855 CZ PHE A 258 51.296 32.258 18.532 1.00152.69 C ANISOU 1855 CZ PHE A 258 17561 19280 21175 475 1693 -1176 C ATOM 1856 N CYS A 259 56.962 34.030 22.928 1.00164.73 N ANISOU 1856 N CYS A 259 18030 20387 24172 437 1584 -971 N ATOM 1857 CA CYS A 259 58.086 34.770 23.488 1.00174.23 C ANISOU 1857 CA CYS A 259 19033 21535 25631 380 1575 -885 C ATOM 1858 C CYS A 259 58.865 33.927 24.491 1.00178.64 C ANISOU 1858 C CYS A 259 19420 22006 26449 389 1422 -892 C ATOM 1859 O CYS A 259 58.647 34.036 25.697 1.00180.72 O ANISOU 1859 O CYS A 259 19684 22235 26749 309 1187 -865 O ATOM 1860 CB CYS A 259 57.603 36.062 24.150 1.00170.12 C ANISOU 1860 CB CYS A 259 18565 21015 25058 267 1458 -808 C ATOM 1861 SG CYS A 259 58.928 37.151 24.715 1.00366.20 S ANISOU 1861 SG CYS A 259 43178 45786 50175 167 1457 -702 S ATOM 1862 N PRO A 260 59.779 33.081 23.990 1.00173.95 N ANISOU 1862 N PRO A 260 18680 21371 26041 479 1561 -924 N ATOM 1863 CA PRO A 260 60.627 32.238 24.840 1.00172.23 C ANISOU 1863 CA PRO A 260 18262 21054 26124 499 1424 -903 C ATOM 1864 C PRO A 260 61.425 33.079 25.830 1.00171.23 C ANISOU 1864 C PRO A 260 17962 20886 26211 382 1266 -779 C ATOM 1865 O PRO A 260 61.779 32.596 26.906 1.00171.14 O ANISOU 1865 O PRO A 260 17843 20811 26373 340 1036 -733 O ATOM 1866 CB PRO A 260 61.572 31.571 23.835 1.00173.39 C ANISOU 1866 CB PRO A 260 18262 21160 26458 615 1696 -947 C ATOM 1867 CG PRO A 260 60.825 31.587 22.548 1.00170.95 C ANISOU 1867 CG PRO A 260 18168 20940 25845 660 1925 -1043 C ATOM 1868 CD PRO A 260 60.048 32.868 22.558 1.00170.49 C ANISOU 1868 CD PRO A 260 18263 20972 25544 561 1868 -980 C ATOM 1869 N ASP A 261 61.703 34.326 25.463 1.00170.52 N ANISOU 1869 N ASP A 261 17853 20833 26105 318 1380 -720 N ATOM 1870 CA ASP A 261 62.421 35.242 26.342 1.00173.21 C ANISOU 1870 CA ASP A 261 18050 21135 26628 185 1240 -611 C ATOM 1871 C ASP A 261 61.560 35.651 27.530 1.00169.77 C ANISOU 1871 C ASP A 261 17769 20703 26031 58 973 -610 C ATOM 1872 O ASP A 261 62.029 35.675 28.667 1.00169.35 O ANISOU 1872 O ASP A 261 17621 20602 26123 -52 746 -551 O ATOM 1873 CB ASP A 261 62.872 36.486 25.573 1.00177.04 C ANISOU 1873 CB ASP A 261 18490 21650 27128 148 1450 -552 C ATOM 1874 CG ASP A 261 64.028 36.204 24.633 1.00177.96 C ANISOU 1874 CG ASP A 261 18397 21744 27476 236 1706 -530 C ATOM 1875 OD1 ASP A 261 64.528 35.059 24.629 1.00176.78 O ANISOU 1875 OD1 ASP A 261 18118 21541 27508 329 1719 -562 O ATOM 1876 OD2 ASP A 261 64.438 37.130 23.903 1.00175.92 O ANISOU 1876 OD2 ASP A 261 18098 21513 27231 210 1905 -480 O ATOM 1877 N CYS A 262 60.300 35.972 27.256 1.00167.67 N ANISOU 1877 N CYS A 262 17743 20495 25470 62 1005 -673 N ATOM 1878 CA CYS A 262 59.371 36.396 28.296 1.00165.53 C ANISOU 1878 CA CYS A 262 17634 20223 25039 -52 804 -691 C ATOM 1879 C CYS A 262 59.392 35.424 29.469 1.00161.91 C ANISOU 1879 C CYS A 262 17155 19725 24638 -95 547 -700 C ATOM 1880 O CYS A 262 59.102 34.239 29.307 1.00165.03 O ANISOU 1880 O CYS A 262 17576 20122 25008 6 526 -749 O ATOM 1881 CB CYS A 262 57.955 36.515 27.729 1.00166.54 C ANISOU 1881 CB CYS A 262 17994 20408 24875 -1 881 -757 C ATOM 1882 SG CYS A 262 57.815 37.659 26.336 1.00147.24 S ANISOU 1882 SG CYS A 262 15592 18014 22337 34 1153 -715 S ATOM 1883 N SER A 263 59.744 35.935 30.646 1.00150.72 N ANISOU 1883 N SER A 263 15701 18270 23295 -258 349 -650 N ATOM 1884 CA SER A 263 59.866 35.108 31.842 1.00145.37 C ANISOU 1884 CA SER A 263 15003 17560 22671 -337 79 -629 C ATOM 1885 C SER A 263 58.712 34.119 31.959 1.00150.12 C ANISOU 1885 C SER A 263 15782 18185 23072 -267 21 -712 C ATOM 1886 O SER A 263 57.570 34.509 32.200 1.00153.95 O ANISOU 1886 O SER A 263 16473 18699 23321 -312 15 -778 O ATOM 1887 CB SER A 263 59.954 35.979 33.098 1.00137.63 C ANISOU 1887 CB SER A 263 14069 16558 21664 -562 -117 -596 C ATOM 1888 OG SER A 263 58.823 36.822 33.218 1.00146.49 O ANISOU 1888 OG SER A 263 15417 17701 22543 -621 -56 -677 O ATOM 1889 N HIS A 264 59.021 32.838 31.778 1.00148.51 N ANISOU 1889 N HIS A 264 15485 17956 22986 -156 -11 -707 N ATOM 1890 CA HIS A 264 58.012 31.789 31.849 1.00152.98 C ANISOU 1890 CA HIS A 264 16201 18533 23391 -87 -67 -781 C ATOM 1891 C HIS A 264 57.151 31.963 33.094 1.00159.67 C ANISOU 1891 C HIS A 264 17224 19393 24050 -243 -279 -795 C ATOM 1892 O HIS A 264 57.662 31.987 34.214 1.00165.00 O ANISOU 1892 O HIS A 264 17847 20039 24806 -391 -496 -723 O ATOM 1893 CB HIS A 264 58.666 30.406 31.846 1.00145.32 C ANISOU 1893 CB HIS A 264 15076 17499 22639 11 -134 -749 C ATOM 1894 CG HIS A 264 59.540 30.152 30.657 1.00131.05 C ANISOU 1894 CG HIS A 264 13093 15664 21038 162 103 -753 C ATOM 1895 ND1 HIS A 264 59.038 29.789 29.426 1.00127.72 N ANISOU 1895 ND1 HIS A 264 12761 15271 20495 306 343 -859 N ATOM 1896 CD2 HIS A 264 60.886 30.199 30.514 1.00119.35 C ANISOU 1896 CD2 HIS A 264 11350 14124 19873 181 147 -665 C ATOM 1897 CE1 HIS A 264 60.035 29.629 28.575 1.00113.66 C ANISOU 1897 CE1 HIS A 264 10800 13453 18934 404 543 -850 C ATOM 1898 NE2 HIS A 264 61.167 29.872 29.210 1.00115.67 N ANISOU 1898 NE2 HIS A 264 10827 13650 19473 340 436 -731 N ATOM 1899 N ALA A 265 55.844 32.091 32.884 1.00152.42 N ANISOU 1899 N ALA A 265 16515 18518 22881 -220 -212 -884 N ATOM 1900 CA ALA A 265 54.898 32.331 33.968 1.00142.84 C ANISOU 1900 CA ALA A 265 15483 17314 21477 -362 -354 -917 C ATOM 1901 C ALA A 265 55.194 31.486 35.203 1.00130.54 C ANISOU 1901 C ALA A 265 13907 15725 19968 -472 -620 -864 C ATOM 1902 O ALA A 265 55.403 30.277 35.100 1.00124.68 O ANISOU 1902 O ALA A 265 13093 14957 19321 -381 -690 -840 O ATOM 1903 CB ALA A 265 53.475 32.092 33.490 1.00144.76 C ANISOU 1903 CB ALA A 265 15908 17595 21501 -280 -261 -1007 C ATOM 1904 N PRO A 266 55.214 32.131 36.378 1.00123.42 N ANISOU 1904 N PRO A 266 13077 14818 19000 -681 -769 -844 N ATOM 1905 CA PRO A 266 55.464 31.465 37.660 1.00123.60 C ANISOU 1905 CA PRO A 266 13112 14824 19027 -834 -1045 -778 C ATOM 1906 C PRO A 266 54.445 30.365 37.919 1.00131.70 C ANISOU 1906 C PRO A 266 14273 15859 19908 -791 -1113 -820 C ATOM 1907 O PRO A 266 53.393 30.348 37.281 1.00146.79 O ANISOU 1907 O PRO A 266 16302 17794 21676 -682 -954 -916 O ATOM 1908 CB PRO A 266 55.280 32.592 38.680 1.00122.12 C ANISOU 1908 CB PRO A 266 13060 14644 18695 -1073 -1111 -805 C ATOM 1909 CG PRO A 266 55.524 33.845 37.913 1.00119.82 C ANISOU 1909 CG PRO A 266 12722 14348 18455 -1037 -900 -837 C ATOM 1910 CD PRO A 266 54.997 33.578 36.539 1.00118.55 C ANISOU 1910 CD PRO A 266 12544 14207 18293 -796 -674 -886 C ATOM 1911 N LEU A 267 54.751 29.461 38.843 1.00131.56 N ANISOU 1911 N LEU A 267 14234 15820 19933 -883 -1359 -734 N ATOM 1912 CA LEU A 267 53.839 28.370 39.167 1.00146.24 C ANISOU 1912 CA LEU A 267 16217 17680 21669 -857 -1441 -759 C ATOM 1913 C LEU A 267 52.674 28.844 40.031 1.00152.86 C ANISOU 1913 C LEU A 267 17305 18557 22217 -1022 -1455 -840 C ATOM 1914 O LEU A 267 51.547 28.373 39.878 1.00141.09 O ANISOU 1914 O LEU A 267 15945 17081 20582 -958 -1390 -915 O ATOM 1915 CB LEU A 267 54.584 27.229 39.862 1.00151.14 C ANISOU 1915 CB LEU A 267 16720 18253 22454 -903 -1704 -617 C ATOM 1916 CG LEU A 267 55.599 26.471 39.004 1.00159.75 C ANISOU 1916 CG LEU A 267 17554 19276 23868 -710 -1672 -544 C ATOM 1917 CD1 LEU A 267 56.272 25.372 39.812 1.00170.24 C ANISOU 1917 CD1 LEU A 267 18761 20539 25382 -768 -1954 -381 C ATOM 1918 CD2 LEU A 267 54.930 25.898 37.764 1.00151.92 C ANISOU 1918 CD2 LEU A 267 16589 18275 22857 -476 -1441 -661 C ATOM 1919 N TRP A 268 52.951 29.776 40.937 1.00162.60 N ANISOU 1919 N TRP A 268 18604 19802 23375 -1241 -1532 -831 N ATOM 1920 CA TRP A 268 51.922 30.307 41.824 1.00164.14 C ANISOU 1920 CA TRP A 268 19041 20021 23305 -1419 -1517 -924 C ATOM 1921 C TRP A 268 50.872 31.089 41.038 1.00158.85 C ANISOU 1921 C TRP A 268 18461 19356 22537 -1305 -1235 -1059 C ATOM 1922 O TRP A 268 49.744 31.272 41.498 1.00158.62 O ANISOU 1922 O TRP A 268 18614 19333 22320 -1375 -1169 -1149 O ATOM 1923 CB TRP A 268 52.544 31.192 42.906 1.00171.18 C ANISOU 1923 CB TRP A 268 19987 20913 24140 -1694 -1642 -899 C ATOM 1924 CG TRP A 268 53.188 32.429 42.367 1.00177.79 C ANISOU 1924 CG TRP A 268 20731 21732 25089 -1684 -1504 -922 C ATOM 1925 CD1 TRP A 268 54.492 32.581 42.000 1.00185.72 C ANISOU 1925 CD1 TRP A 268 21516 22720 26327 -1655 -1569 -816 C ATOM 1926 CD2 TRP A 268 52.555 33.692 42.131 1.00178.11 C ANISOU 1926 CD2 TRP A 268 20881 21758 25034 -1703 -1272 -1050 C ATOM 1927 NE1 TRP A 268 54.712 33.861 41.551 1.00189.15 N ANISOU 1927 NE1 TRP A 268 21929 23138 26802 -1663 -1394 -871 N ATOM 1928 CE2 TRP A 268 53.537 34.564 41.622 1.00185.91 C ANISOU 1928 CE2 TRP A 268 21719 22723 26194 -1690 -1213 -1013 C ATOM 1929 CE3 TRP A 268 51.252 34.171 42.302 1.00172.63 C ANISOU 1929 CE3 TRP A 268 20385 21055 24153 -1728 -1102 -1185 C ATOM 1930 CZ2 TRP A 268 53.259 35.886 41.281 1.00185.76 C ANISOU 1930 CZ2 TRP A 268 21752 22672 26159 -1703 -1000 -1102 C ATOM 1931 CZ3 TRP A 268 50.977 35.484 41.964 1.00171.80 C ANISOU 1931 CZ3 TRP A 268 20317 20909 24049 -1733 -887 -1273 C ATOM 1932 CH2 TRP A 268 51.976 36.326 41.459 1.00178.98 C ANISOU 1932 CH2 TRP A 268 21084 21794 25125 -1722 -842 -1230 C ATOM 1933 N LEU A 269 51.251 31.551 39.852 1.00152.37 N ANISOU 1933 N LEU A 269 17507 18530 21857 -1134 -1070 -1062 N ATOM 1934 CA LEU A 269 50.331 32.265 38.976 1.00142.02 C ANISOU 1934 CA LEU A 269 16256 17223 20482 -1014 -823 -1154 C ATOM 1935 C LEU A 269 49.805 31.325 37.900 1.00131.11 C ANISOU 1935 C LEU A 269 14837 15862 19117 -792 -748 -1162 C ATOM 1936 O LEU A 269 48.763 31.576 37.294 1.00125.59 O ANISOU 1936 O LEU A 269 14215 15176 18328 -704 -597 -1225 O ATOM 1937 CB LEU A 269 51.028 33.465 38.333 1.00137.40 C ANISOU 1937 CB LEU A 269 15570 16623 20015 -992 -684 -1144 C ATOM 1938 CG LEU A 269 50.186 34.304 37.370 1.00130.49 C ANISOU 1938 CG LEU A 269 14735 15745 19100 -874 -441 -1205 C ATOM 1939 CD1 LEU A 269 48.967 34.857 38.082 1.00131.31 C ANISOU 1939 CD1 LEU A 269 15024 15823 19045 -982 -379 -1296 C ATOM 1940 CD2 LEU A 269 51.014 35.427 36.767 1.00126.98 C ANISOU 1940 CD2 LEU A 269 14180 15280 18788 -863 -323 -1171 C ATOM 1941 N MET A 270 50.536 30.238 37.674 1.00124.95 N ANISOU 1941 N MET A 270 13934 15076 18464 -709 -859 -1094 N ATOM 1942 CA MET A 270 50.160 29.249 36.673 1.00131.95 C ANISOU 1942 CA MET A 270 14791 15970 19375 -513 -793 -1114 C ATOM 1943 C MET A 270 48.938 28.448 37.109 1.00137.59 C ANISOU 1943 C MET A 270 15656 16692 19930 -529 -855 -1160 C ATOM 1944 O MET A 270 48.018 28.232 36.321 1.00131.25 O ANISOU 1944 O MET A 270 14911 15909 19048 -413 -739 -1218 O ATOM 1945 CB MET A 270 51.328 28.304 36.388 1.00133.88 C ANISOU 1945 CB MET A 270 14855 16178 19835 -428 -878 -1038 C ATOM 1946 CG MET A 270 51.050 27.298 35.285 1.00139.20 C ANISOU 1946 CG MET A 270 15501 16844 20544 -231 -780 -1081 C ATOM 1947 SD MET A 270 50.859 28.069 33.667 1.00197.68 S ANISOU 1947 SD MET A 270 22899 24296 27916 -82 -494 -1147 S ATOM 1948 CE MET A 270 52.521 28.675 33.390 1.00186.51 C ANISOU 1948 CE MET A 270 21265 22854 26745 -75 -441 -1070 C ATOM 1949 N TYR A 271 48.929 28.007 38.363 1.00142.93 N ANISOU 1949 N TYR A 271 16396 17355 20555 -685 -1045 -1123 N ATOM 1950 CA TYR A 271 47.809 27.226 38.875 1.00140.65 C ANISOU 1950 CA TYR A 271 16249 17072 20120 -719 -1107 -1156 C ATOM 1951 C TYR A 271 46.564 28.087 39.043 1.00136.32 C ANISOU 1951 C TYR A 271 15854 16546 19396 -778 -966 -1247 C ATOM 1952 O TYR A 271 45.445 27.585 38.974 1.00144.49 O ANISOU 1952 O TYR A 271 16980 17588 20330 -741 -935 -1291 O ATOM 1953 CB TYR A 271 48.162 26.539 40.198 1.00154.42 C ANISOU 1953 CB TYR A 271 18028 18799 21845 -891 -1352 -1076 C ATOM 1954 CG TYR A 271 48.166 27.456 41.403 1.00168.67 C ANISOU 1954 CG TYR A 271 19950 20620 23517 -1136 -1408 -1082 C ATOM 1955 CD1 TYR A 271 46.976 27.878 41.988 1.00166.26 C ANISOU 1955 CD1 TYR A 271 19833 20331 23005 -1246 -1324 -1173 C ATOM 1956 CD2 TYR A 271 49.359 27.886 41.967 1.00180.63 C ANISOU 1956 CD2 TYR A 271 21386 22127 25117 -1269 -1540 -1002 C ATOM 1957 CE1 TYR A 271 46.977 28.713 43.092 1.00171.35 C ANISOU 1957 CE1 TYR A 271 20606 20982 23518 -1483 -1347 -1203 C ATOM 1958 CE2 TYR A 271 49.369 28.718 43.072 1.00184.30 C ANISOU 1958 CE2 TYR A 271 21981 22607 25438 -1517 -1593 -1021 C ATOM 1959 CZ TYR A 271 48.177 29.129 43.629 1.00180.72 C ANISOU 1959 CZ TYR A 271 21734 22166 24764 -1625 -1486 -1132 C ATOM 1960 OH TYR A 271 48.188 29.958 44.728 1.00181.90 O ANISOU 1960 OH TYR A 271 22032 22320 24761 -1886 -1511 -1175 O ATOM 1961 N LEU A 272 46.760 29.381 39.273 1.00126.96 N ANISOU 1961 N LEU A 272 14687 15358 18194 -870 -877 -1273 N ATOM 1962 CA LEU A 272 45.633 30.296 39.415 1.00123.74 C ANISOU 1962 CA LEU A 272 14402 14945 17668 -918 -717 -1358 C ATOM 1963 C LEU A 272 44.861 30.373 38.104 1.00124.08 C ANISOU 1963 C LEU A 272 14411 15001 17731 -722 -554 -1383 C ATOM 1964 O LEU A 272 43.637 30.488 38.100 1.00128.53 O ANISOU 1964 O LEU A 272 15061 15562 18212 -713 -467 -1431 O ATOM 1965 CB LEU A 272 46.105 31.685 39.854 1.00123.41 C ANISOU 1965 CB LEU A 272 14375 14877 17638 -1051 -644 -1384 C ATOM 1966 CG LEU A 272 45.029 32.757 40.065 1.00120.37 C ANISOU 1966 CG LEU A 272 14105 14455 17175 -1108 -455 -1477 C ATOM 1967 CD1 LEU A 272 45.489 33.800 41.074 1.00118.65 C ANISOU 1967 CD1 LEU A 272 13963 14197 16923 -1327 -444 -1523 C ATOM 1968 CD2 LEU A 272 44.634 33.418 38.749 1.00117.14 C ANISOU 1968 CD2 LEU A 272 13616 14038 16855 -925 -267 -1476 C ATOM 1969 N ALA A 273 45.587 30.307 36.993 1.00125.69 N ANISOU 1969 N ALA A 273 14487 15221 18047 -576 -513 -1344 N ATOM 1970 CA ALA A 273 44.972 30.296 35.672 1.00128.36 C ANISOU 1970 CA ALA A 273 14802 15585 18384 -408 -381 -1354 C ATOM 1971 C ALA A 273 44.344 28.936 35.401 1.00128.97 C ANISOU 1971 C ALA A 273 14914 15680 18410 -328 -456 -1366 C ATOM 1972 O ALA A 273 43.490 28.796 34.526 1.00132.95 O ANISOU 1972 O ALA A 273 15443 16209 18864 -229 -379 -1383 O ATOM 1973 CB ALA A 273 46.002 30.623 34.607 1.00129.21 C ANISOU 1973 CB ALA A 273 14782 15707 18605 -302 -303 -1315 C ATOM 1974 N ILE A 274 44.780 27.937 36.159 1.00122.63 N ANISOU 1974 N ILE A 274 14110 14858 17624 -382 -619 -1347 N ATOM 1975 CA ILE A 274 44.241 26.589 36.046 1.00118.96 C ANISOU 1975 CA ILE A 274 13681 14390 17127 -323 -704 -1357 C ATOM 1976 C ILE A 274 43.000 26.442 36.922 1.00127.77 C ANISOU 1976 C ILE A 274 14930 15506 18111 -427 -739 -1386 C ATOM 1977 O ILE A 274 41.992 25.872 36.502 1.00131.18 O ANISOU 1977 O ILE A 274 15410 15947 18484 -366 -720 -1412 O ATOM 1978 CB ILE A 274 45.288 25.535 36.449 1.00120.38 C ANISOU 1978 CB ILE A 274 13783 14532 17422 -327 -866 -1304 C ATOM 1979 CG1 ILE A 274 46.554 25.698 35.605 1.00132.63 C ANISOU 1979 CG1 ILE A 274 15182 16074 19137 -224 -806 -1277 C ATOM 1980 CG2 ILE A 274 44.724 24.136 36.294 1.00107.30 C ANISOU 1980 CG2 ILE A 274 12164 12854 15752 -263 -944 -1317 C ATOM 1981 CD1 ILE A 274 47.675 24.765 35.997 1.00126.50 C ANISOU 1981 CD1 ILE A 274 14290 15241 18534 -221 -955 -1207 C ATOM 1982 N VAL A 275 43.078 26.964 38.142 1.00130.08 N ANISOU 1982 N VAL A 275 15285 15785 18353 -598 -785 -1383 N ATOM 1983 CA VAL A 275 41.940 26.957 39.051 1.00132.81 C ANISOU 1983 CA VAL A 275 15765 16126 18571 -719 -781 -1421 C ATOM 1984 C VAL A 275 40.800 27.767 38.450 1.00143.07 C ANISOU 1984 C VAL A 275 17089 17429 19844 -658 -594 -1471 C ATOM 1985 O VAL A 275 39.633 27.396 38.564 1.00153.65 O ANISOU 1985 O VAL A 275 18491 18766 21122 -660 -568 -1495 O ATOM 1986 CB VAL A 275 42.303 27.552 40.423 1.00126.87 C ANISOU 1986 CB VAL A 275 15094 15360 17749 -937 -831 -1426 C ATOM 1987 CG1 VAL A 275 41.068 27.655 41.302 1.00129.13 C ANISOU 1987 CG1 VAL A 275 15529 15637 17897 -1065 -770 -1485 C ATOM 1988 CG2 VAL A 275 43.369 26.715 41.099 1.00122.96 C ANISOU 1988 CG2 VAL A 275 14571 14863 17284 -1019 -1054 -1344 C ATOM 1989 N LEU A 276 41.149 28.874 37.803 1.00137.39 N ANISOU 1989 N LEU A 276 16307 16707 19189 -605 -469 -1472 N ATOM 1990 CA LEU A 276 40.160 29.740 37.175 1.00132.79 C ANISOU 1990 CA LEU A 276 15723 16116 18617 -543 -301 -1491 C ATOM 1991 C LEU A 276 39.413 29.003 36.067 1.00142.72 C ANISOU 1991 C LEU A 276 16952 17407 19867 -397 -304 -1469 C ATOM 1992 O LEU A 276 38.235 29.265 35.817 1.00149.53 O ANISOU 1992 O LEU A 276 17831 18262 20720 -372 -226 -1470 O ATOM 1993 CB LEU A 276 40.831 30.995 36.613 1.00123.55 C ANISOU 1993 CB LEU A 276 14479 14932 17531 -511 -186 -1474 C ATOM 1994 CG LEU A 276 39.900 32.109 36.135 1.00121.88 C ANISOU 1994 CG LEU A 276 14259 14687 17364 -472 -13 -1473 C ATOM 1995 CD1 LEU A 276 39.019 32.593 37.274 1.00124.55 C ANISOU 1995 CD1 LEU A 276 14688 14961 17676 -604 66 -1538 C ATOM 1996 CD2 LEU A 276 40.699 33.260 35.553 1.00125.34 C ANISOU 1996 CD2 LEU A 276 14621 15108 17893 -442 83 -1440 C ATOM 1997 N ALA A 277 40.101 28.074 35.411 1.00141.81 N ANISOU 1997 N ALA A 277 16791 17323 19767 -308 -394 -1448 N ATOM 1998 CA ALA A 277 39.506 27.307 34.321 1.00137.04 C ANISOU 1998 CA ALA A 277 16180 16753 19138 -188 -404 -1443 C ATOM 1999 C ALA A 277 38.578 26.206 34.834 1.00130.32 C ANISOU 1999 C ALA A 277 15399 15892 18225 -224 -500 -1462 C ATOM 2000 O ALA A 277 37.659 25.784 34.133 1.00123.57 O ANISOU 2000 O ALA A 277 14559 15058 17336 -163 -498 -1461 O ATOM 2001 CB ALA A 277 40.591 26.721 33.430 1.00144.31 C ANISOU 2001 CB ALA A 277 17036 17692 20102 -88 -430 -1437 C ATOM 2002 N HIS A 278 38.825 25.741 36.055 1.00137.82 N ANISOU 2002 N HIS A 278 16396 16813 19158 -335 -596 -1470 N ATOM 2003 CA HIS A 278 37.980 24.721 36.667 1.00141.52 C ANISOU 2003 CA HIS A 278 16936 17268 19568 -389 -686 -1479 C ATOM 2004 C HIS A 278 36.783 25.362 37.352 1.00135.80 C ANISOU 2004 C HIS A 278 16271 16530 18795 -482 -594 -1499 C ATOM 2005 O HIS A 278 35.787 24.697 37.635 1.00141.62 O ANISOU 2005 O HIS A 278 17056 17261 19493 -511 -623 -1504 O ATOM 2006 CB HIS A 278 38.768 23.889 37.679 1.00152.34 C ANISOU 2006 CB HIS A 278 18333 18613 20938 -480 -840 -1457 C ATOM 2007 CG HIS A 278 39.903 23.119 37.078 1.00153.99 C ANISOU 2007 CG HIS A 278 18461 18808 21241 -382 -926 -1433 C ATOM 2008 ND1 HIS A 278 39.918 22.120 36.165 1.00148.01 N ANISOU 2008 ND1 HIS A 278 17637 18036 20562 -410 -978 -1395 N ATOM 2009 CD2 HIS A 278 41.220 23.356 37.408 1.00155.96 C ANISOU 2009 CD2 HIS A 278 18680 19045 21531 -261 -957 -1446 C ATOM 2010 CE1 HIS A 278 41.232 21.774 35.964 1.00150.75 C ANISOU 2010 CE1 HIS A 278 17902 18357 21018 -299 -1026 -1382 C ATOM 2011 NE2 HIS A 278 41.997 22.533 36.727 1.00151.99 N ANISOU 2011 NE2 HIS A 278 18090 18513 21148 -208 -1005 -1422 N ATOM 2012 N THR A 279 36.891 26.659 37.622 1.00132.91 N ANISOU 2012 N THR A 279 15899 16149 18451 -530 -469 -1513 N ATOM 2013 CA THR A 279 35.811 27.401 38.262 1.00140.39 C ANISOU 2013 CA THR A 279 16893 17061 19387 -614 -338 -1546 C ATOM 2014 C THR A 279 34.666 27.646 37.283 1.00143.09 C ANISOU 2014 C THR A 279 17174 17405 19789 -503 -252 -1518 C ATOM 2015 O THR A 279 33.509 27.779 37.681 1.00143.65 O ANISOU 2015 O THR A 279 17262 17443 19875 -546 -173 -1530 O ATOM 2016 CB THR A 279 36.311 28.747 38.817 1.00140.88 C ANISOU 2016 CB THR A 279 16968 17086 19474 -701 -217 -1580 C ATOM 2017 OG1 THR A 279 37.402 28.516 39.717 1.00145.37 O ANISOU 2017 OG1 THR A 279 17591 17661 19982 -823 -327 -1590 O ATOM 2018 CG2 THR A 279 35.195 29.474 39.554 1.00136.22 C ANISOU 2018 CG2 THR A 279 16432 16437 18891 -794 -51 -1634 C ATOM 2019 N ASN A 280 35.002 27.697 35.998 1.00143.09 N ANISOU 2019 N ASN A 280 17100 17442 19824 -371 -267 -1475 N ATOM 2020 CA ASN A 280 34.018 27.932 34.948 1.00141.99 C ANISOU 2020 CA ASN A 280 16902 17318 19730 -277 -221 -1423 C ATOM 2021 C ASN A 280 32.910 26.884 34.943 1.00149.81 C ANISOU 2021 C ASN A 280 17916 18318 20689 -280 -299 -1416 C ATOM 2022 O ASN A 280 31.795 27.147 34.491 1.00159.06 O ANISOU 2022 O ASN A 280 19038 19482 21915 -250 -258 -1369 O ATOM 2023 CB ASN A 280 34.703 27.969 33.582 1.00137.50 C ANISOU 2023 CB ASN A 280 16283 16804 19157 -162 -246 -1381 C ATOM 2024 CG ASN A 280 33.752 28.332 32.464 1.00139.65 C ANISOU 2024 CG ASN A 280 16502 17100 19458 -89 -217 -1304 C ATOM 2025 OD1 ASN A 280 34.025 27.823 31.270 1.00146.93 O ANISOU 2025 OD1 ASN A 280 17384 17979 20464 -107 -135 -1265 O ATOM 2026 ND2 ASN A 280 32.786 29.067 32.668 1.00134.19 N ANISOU 2026 ND2 ASN A 280 15810 16474 18704 -14 -282 -1279 N ATOM 2027 N SER A 281 33.223 25.696 35.447 1.00145.29 N ANISOU 2027 N SER A 281 17404 17753 20045 -320 -422 -1450 N ATOM 2028 CA SER A 281 32.262 24.599 35.471 1.00142.06 C ANISOU 2028 CA SER A 281 17022 17346 19607 -332 -508 -1445 C ATOM 2029 C SER A 281 31.199 24.792 36.551 1.00138.46 C ANISOU 2029 C SER A 281 16592 16845 19170 -438 -432 -1456 C ATOM 2030 O SER A 281 30.196 24.080 36.581 1.00136.77 O ANISOU 2030 O SER A 281 16380 16627 18958 -454 -474 -1441 O ATOM 2031 CB SER A 281 32.985 23.266 35.679 1.00140.23 C ANISOU 2031 CB SER A 281 16845 17119 19318 -340 -658 -1471 C ATOM 2032 OG SER A 281 33.925 23.030 34.645 1.00141.25 O ANISOU 2032 OG SER A 281 16944 17276 19448 -238 -698 -1474 O ATOM 2033 N VAL A 282 31.419 25.766 37.427 1.00137.92 N ANISOU 2033 N VAL A 282 16545 16739 19119 -519 -308 -1490 N ATOM 2034 CA VAL A 282 30.535 25.990 38.567 1.00134.43 C ANISOU 2034 CA VAL A 282 16148 16245 18682 -641 -198 -1525 C ATOM 2035 C VAL A 282 29.605 27.186 38.365 1.00135.22 C ANISOU 2035 C VAL A 282 16166 16291 18921 -613 -7 -1511 C ATOM 2036 O VAL A 282 28.543 27.265 38.982 1.00140.11 O ANISOU 2036 O VAL A 282 16783 16860 19592 -677 102 -1527 O ATOM 2037 CB VAL A 282 31.346 26.184 39.867 1.00125.48 C ANISOU 2037 CB VAL A 282 15125 15095 17455 -791 -181 -1587 C ATOM 2038 CG1 VAL A 282 30.425 26.486 41.038 1.00127.07 C ANISOU 2038 CG1 VAL A 282 15396 15243 17641 -936 -30 -1642 C ATOM 2039 CG2 VAL A 282 32.187 24.951 40.153 1.00118.60 C ANISOU 2039 CG2 VAL A 282 14317 14263 16483 -825 -385 -1572 C ATOM 2040 N VAL A 283 30.002 28.112 37.499 1.00132.24 N ANISOU 2040 N VAL A 283 15711 15913 18620 -519 42 -1475 N ATOM 2041 CA VAL A 283 29.219 29.325 37.284 1.00136.69 C ANISOU 2041 CA VAL A 283 16181 16405 19349 -485 220 -1444 C ATOM 2042 C VAL A 283 27.892 29.040 36.586 1.00138.31 C ANISOU 2042 C VAL A 283 16281 16608 19663 -417 199 -1354 C ATOM 2043 O VAL A 283 26.906 29.740 36.810 1.00141.44 O ANISOU 2043 O VAL A 283 16597 16921 20221 -423 352 -1332 O ATOM 2044 CB VAL A 283 29.999 30.377 36.471 1.00141.40 C ANISOU 2044 CB VAL A 283 16718 17002 20007 -404 260 -1404 C ATOM 2045 CG1 VAL A 283 31.268 30.777 37.202 1.00144.84 C ANISOU 2045 CG1 VAL A 283 17240 17429 20364 -485 287 -1487 C ATOM 2046 CG2 VAL A 283 30.316 29.852 35.078 1.00142.94 C ANISOU 2046 CG2 VAL A 283 16866 17286 20158 -286 104 -1318 C ATOM 2047 N ASN A 284 27.869 28.011 35.746 1.00136.86 N ANISOU 2047 N ASN A 284 16093 16504 19402 -358 14 -1303 N ATOM 2048 CA ASN A 284 26.672 27.681 34.977 1.00140.06 C ANISOU 2048 CA ASN A 284 16403 16920 19894 -307 -46 -1206 C ATOM 2049 C ASN A 284 25.436 27.412 35.840 1.00143.96 C ANISOU 2049 C ASN A 284 16868 17351 20478 -381 34 -1215 C ATOM 2050 O ASN A 284 24.387 28.012 35.619 1.00139.58 O ANISOU 2050 O ASN A 284 16185 16739 20109 -353 123 -1138 O ATOM 2051 CB ASN A 284 26.941 26.509 34.028 1.00139.64 C ANISOU 2051 CB ASN A 284 16387 16960 19709 -262 -258 -1181 C ATOM 2052 CG ASN A 284 28.014 26.826 33.004 1.00140.77 C ANISOU 2052 CG ASN A 284 16539 17163 19782 -184 -307 -1161 C ATOM 2053 OD1 ASN A 284 28.276 27.991 32.704 1.00141.01 O ANISOU 2053 OD1 ASN A 284 16513 17172 19891 -147 -207 -1119 O ATOM 2054 ND2 ASN A 284 28.641 25.789 32.463 1.00142.72 N ANISOU 2054 ND2 ASN A 284 16859 17476 19894 -162 -447 -1194 N ATOM 2055 N PRO A 285 25.553 26.511 36.828 1.00151.68 N ANISOU 2055 N PRO A 285 17958 18335 21339 -478 4 -1299 N ATOM 2056 CA PRO A 285 24.402 26.232 37.695 1.00146.86 C ANISOU 2056 CA PRO A 285 17331 17667 20801 -563 100 -1312 C ATOM 2057 C PRO A 285 23.886 27.488 38.393 1.00135.78 C ANISOU 2057 C PRO A 285 15873 16157 19561 -600 366 -1344 C ATOM 2058 O PRO A 285 22.687 27.763 38.357 1.00135.73 O ANISOU 2058 O PRO A 285 15741 16086 19745 -586 470 -1288 O ATOM 2059 CB PRO A 285 24.972 25.255 38.727 1.00156.56 C ANISOU 2059 CB PRO A 285 18720 18922 21844 -678 34 -1399 C ATOM 2060 CG PRO A 285 26.112 24.599 38.031 1.00159.86 C ANISOU 2060 CG PRO A 285 19193 19416 22130 -617 -166 -1394 C ATOM 2061 CD PRO A 285 26.708 25.656 37.153 1.00157.98 C ANISOU 2061 CD PRO A 285 18890 19188 21949 -516 -125 -1366 C ATOM 2062 N PHE A 286 24.787 28.239 39.017 1.00131.77 N ANISOU 2062 N PHE A 286 15452 15621 18993 -650 478 -1433 N ATOM 2063 CA PHE A 286 24.410 29.442 39.750 1.00133.11 C ANISOU 2063 CA PHE A 286 15599 15674 19304 -702 753 -1495 C ATOM 2064 C PHE A 286 23.925 30.555 38.824 1.00136.02 C ANISOU 2064 C PHE A 286 15786 15972 19923 -575 844 -1397 C ATOM 2065 O PHE A 286 23.167 31.431 39.240 1.00137.70 O ANISOU 2065 O PHE A 286 15918 16060 20344 -587 1079 -1413 O ATOM 2066 CB PHE A 286 25.579 29.939 40.604 1.00130.41 C ANISOU 2066 CB PHE A 286 15411 15324 18814 -806 823 -1618 C ATOM 2067 CG PHE A 286 25.905 29.044 41.764 1.00132.74 C ANISOU 2067 CG PHE A 286 15883 15661 18890 -969 773 -1705 C ATOM 2068 CD1 PHE A 286 26.752 27.959 41.606 1.00136.01 C ANISOU 2068 CD1 PHE A 286 16375 16179 19122 -972 521 -1679 C ATOM 2069 CD2 PHE A 286 25.364 29.288 43.015 1.00132.82 C ANISOU 2069 CD2 PHE A 286 15984 15601 18882 -1126 984 -1808 C ATOM 2070 CE1 PHE A 286 27.052 27.134 42.674 1.00136.64 C ANISOU 2070 CE1 PHE A 286 16609 16291 19015 -1127 455 -1730 C ATOM 2071 CE2 PHE A 286 25.660 28.468 44.086 1.00136.06 C ANISOU 2071 CE2 PHE A 286 16570 16058 19070 -1297 925 -1869 C ATOM 2072 CZ PHE A 286 26.505 27.389 43.916 1.00137.18 C ANISOU 2072 CZ PHE A 286 16777 16303 19041 -1296 647 -1818 C ATOM 2073 N ILE A 287 24.360 30.517 37.569 1.00135.79 N ANISOU 2073 N ILE A 287 15696 16017 19883 -458 666 -1290 N ATOM 2074 CA ILE A 287 23.976 31.541 36.603 1.00134.21 C ANISOU 2074 CA ILE A 287 15330 15763 19901 -345 714 -1165 C ATOM 2075 C ILE A 287 22.578 31.274 36.048 1.00131.32 C ANISOU 2075 C ILE A 287 14796 15374 19724 -294 673 -1028 C ATOM 2076 O ILE A 287 21.976 32.144 35.417 1.00131.52 O ANISOU 2076 O ILE A 287 14655 15328 19989 -216 730 -901 O ATOM 2077 CB ILE A 287 24.990 31.644 35.442 1.00136.68 C ANISOU 2077 CB ILE A 287 15651 16170 20109 -259 546 -1095 C ATOM 2078 CG1 ILE A 287 24.970 33.046 34.831 1.00136.05 C ANISOU 2078 CG1 ILE A 287 15448 16010 20235 -182 659 -1001 C ATOM 2079 CG2 ILE A 287 24.712 30.592 34.383 1.00140.51 C ANISOU 2079 CG2 ILE A 287 16113 16771 20503 -206 303 -993 C ATOM 2080 CD1 ILE A 287 25.911 33.203 33.659 1.00135.27 C ANISOU 2080 CD1 ILE A 287 15358 16006 20034 -107 514 -920 C ATOM 2081 N TYR A 288 22.066 30.069 36.286 1.00126.46 N ANISOU 2081 N TYR A 288 14218 14815 19016 -344 562 -1040 N ATOM 2082 CA TYR A 288 20.699 29.734 35.903 1.00125.30 C ANISOU 2082 CA TYR A 288 13912 14644 19053 -320 520 -916 C ATOM 2083 C TYR A 288 19.729 30.106 37.018 1.00127.88 C ANISOU 2083 C TYR A 288 14173 14835 19582 -384 784 -971 C ATOM 2084 O TYR A 288 18.689 30.717 36.773 1.00122.41 O ANISOU 2084 O TYR A 288 13281 14042 19187 -334 886 -862 O ATOM 2085 CB TYR A 288 20.566 28.244 35.580 1.00123.84 C ANISOU 2085 CB TYR A 288 13793 14574 18687 -349 277 -901 C ATOM 2086 CG TYR A 288 21.343 27.795 34.365 1.00130.12 C ANISOU 2086 CG TYR A 288 14641 15492 19305 -288 34 -847 C ATOM 2087 CD1 TYR A 288 21.202 28.444 33.146 1.00131.88 C ANISOU 2087 CD1 TYR A 288 14751 15735 19624 -204 -44 -699 C ATOM 2088 CD2 TYR A 288 22.202 26.707 34.432 1.00135.02 C ANISOU 2088 CD2 TYR A 288 15428 16203 19671 -322 -111 -940 C ATOM 2089 CE1 TYR A 288 21.906 28.033 32.032 1.00133.93 C ANISOU 2089 CE1 TYR A 288 15079 16110 19699 -166 -242 -663 C ATOM 2090 CE2 TYR A 288 22.912 26.288 33.322 1.00136.52 C ANISOU 2090 CE2 TYR A 288 15671 16492 19710 -269 -297 -910 C ATOM 2091 CZ TYR A 288 22.760 26.954 32.124 1.00137.14 C ANISOU 2091 CZ TYR A 288 15652 16597 19856 -197 -354 -780 C ATOM 2092 OH TYR A 288 23.464 26.539 31.016 1.00136.85 O ANISOU 2092 OH TYR A 288 15687 16662 19647 -161 -516 -763 O ATOM 2093 N ALA A 289 20.081 29.735 38.245 1.00130.28 N ANISOU 2093 N ALA A 289 14642 15132 19728 -502 896 -1136 N ATOM 2094 CA ALA A 289 19.245 30.018 39.406 1.00126.59 C ANISOU 2094 CA ALA A 289 14154 14543 19401 -591 1175 -1221 C ATOM 2095 C ALA A 289 19.059 31.517 39.617 1.00130.76 C ANISOU 2095 C ALA A 289 14584 14913 20186 -557 1460 -1244 C ATOM 2096 O ALA A 289 18.201 31.941 40.387 1.00138.94 O ANISOU 2096 O ALA A 289 15553 15816 21421 -606 1732 -1297 O ATOM 2097 CB ALA A 289 19.834 29.374 40.653 1.00119.10 C ANISOU 2097 CB ALA A 289 13440 13634 18179 -749 1221 -1389 C ATOM 2098 N TYR A 290 19.867 32.316 38.931 1.00134.28 N ANISOU 2098 N TYR A 290 15020 15364 20638 -476 1413 -1207 N ATOM 2099 CA TYR A 290 19.773 33.766 39.045 1.00143.34 C ANISOU 2099 CA TYR A 290 16072 16349 22041 -437 1669 -1220 C ATOM 2100 C TYR A 290 19.049 34.379 37.850 1.00147.24 C ANISOU 2100 C TYR A 290 16307 16784 22852 -288 1610 -999 C ATOM 2101 O TYR A 290 18.076 35.114 38.012 1.00149.71 O ANISOU 2101 O TYR A 290 16438 16933 23514 -252 1825 -949 O ATOM 2102 CB TYR A 290 21.163 34.389 39.195 1.00149.61 C ANISOU 2102 CB TYR A 290 17025 17163 22658 -464 1685 -1326 C ATOM 2103 CG TYR A 290 21.151 35.900 39.219 1.00161.78 C ANISOU 2103 CG TYR A 290 18474 18530 24464 -422 1933 -1336 C ATOM 2104 CD1 TYR A 290 20.998 36.595 40.412 1.00166.65 C ANISOU 2104 CD1 TYR A 290 19164 18995 25161 -529 2263 -1516 C ATOM 2105 CD2 TYR A 290 21.290 36.633 38.048 1.00167.29 C ANISOU 2105 CD2 TYR A 290 19024 19209 25331 -286 1844 -1168 C ATOM 2106 CE1 TYR A 290 20.984 37.979 40.437 1.00169.36 C ANISOU 2106 CE1 TYR A 290 19425 19156 25767 -491 2506 -1538 C ATOM 2107 CE2 TYR A 290 21.277 38.016 38.063 1.00170.03 C ANISOU 2107 CE2 TYR A 290 19279 19380 25944 -245 2069 -1167 C ATOM 2108 CZ TYR A 290 21.124 38.684 39.259 1.00168.74 C ANISOU 2108 CZ TYR A 290 19183 19053 25879 -343 2403 -1357 C ATOM 2109 OH TYR A 290 21.111 40.060 39.276 1.00165.58 O ANISOU 2109 OH TYR A 290 18694 18456 25763 -303 2641 -1367 O ATOM 2110 N ARG A 291 19.532 34.071 36.650 1.00149.70 N ANISOU 2110 N ARG A 291 16603 17228 23048 -209 1321 -861 N ATOM 2111 CA ARG A 291 18.966 34.628 35.427 1.00151.43 C ANISOU 2111 CA ARG A 291 16602 17418 23516 -89 1216 -628 C ATOM 2112 C ARG A 291 17.557 34.116 35.153 1.00155.21 C ANISOU 2112 C ARG A 291 16887 17874 24212 -70 1151 -479 C ATOM 2113 O ARG A 291 16.630 34.901 34.956 1.00162.47 O ANISOU 2113 O ARG A 291 17576 18649 25506 -8 1269 -344 O ATOM 2114 CB ARG A 291 19.872 34.324 34.234 1.00147.14 C ANISOU 2114 CB ARG A 291 16128 17041 22737 -40 926 -534 C ATOM 2115 CG ARG A 291 21.190 35.070 34.264 1.00139.95 C ANISOU 2115 CG ARG A 291 15342 16133 21701 -34 990 -622 C ATOM 2116 CD ARG A 291 20.961 36.566 34.151 1.00137.90 C ANISOU 2116 CD ARG A 291 14931 15699 21767 29 1191 -545 C ATOM 2117 NE ARG A 291 20.326 36.917 32.885 1.00138.69 N ANISOU 2117 NE ARG A 291 14830 15798 22067 125 1039 -280 N ATOM 2118 CZ ARG A 291 20.029 38.159 32.516 1.00145.99 C ANISOU 2118 CZ ARG A 291 15585 16575 23310 197 1154 -143 C ATOM 2119 NH1 ARG A 291 20.307 39.176 33.320 1.00144.84 N ANISOU 2119 NH1 ARG A 291 15450 16260 23324 188 1441 -268 N ATOM 2120 NH2 ARG A 291 19.452 38.384 31.344 1.00153.20 N ANISOU 2120 NH2 ARG A 291 16322 17506 24383 267 975 124 N ATOM 2121 N ILE A 292 17.401 32.797 35.139 1.00153.05 N ANISOU 2121 N ILE A 292 16696 17733 23723 -125 959 -498 N ATOM 2122 CA ILE A 292 16.109 32.191 34.841 1.00158.97 C ANISOU 2122 CA ILE A 292 17270 18478 24654 -123 861 -355 C ATOM 2123 C ILE A 292 15.281 31.961 36.103 1.00164.75 C ANISOU 2123 C ILE A 292 17975 19101 25524 -200 1113 -470 C ATOM 2124 O ILE A 292 15.650 31.167 36.969 1.00161.07 O ANISOU 2124 O ILE A 292 17702 18692 24805 -300 1145 -642 O ATOM 2125 CB ILE A 292 16.269 30.865 34.078 1.00155.70 C ANISOU 2125 CB ILE A 292 16949 18252 23959 -150 517 -304 C ATOM 2126 CG1 ILE A 292 17.118 31.078 32.823 1.00151.63 C ANISOU 2126 CG1 ILE A 292 16483 17848 23283 -89 296 -207 C ATOM 2127 CG2 ILE A 292 14.908 30.294 33.717 1.00158.91 C ANISOU 2127 CG2 ILE A 292 17164 18650 24567 -160 398 -142 C ATOM 2128 CD1 ILE A 292 17.281 29.838 31.975 1.00149.27 C ANISOU 2128 CD1 ILE A 292 16282 17721 22715 -120 -21 -169 C ATOM 2129 N ARG A 293 14.158 32.665 36.195 1.00174.69 N ANISOU 2129 N ARG A 293 18983 20195 27195 -157 1295 -364 N ATOM 2130 CA ARG A 293 13.267 32.561 37.345 1.00185.26 C ANISOU 2130 CA ARG A 293 20265 21408 28716 -226 1580 -464 C ATOM 2131 C ARG A 293 12.595 31.191 37.414 1.00178.48 C ANISOU 2131 C ARG A 293 19407 20650 27758 -297 1410 -431 C ATOM 2132 O ARG A 293 12.142 30.763 38.476 1.00180.74 O ANISOU 2132 O ARG A 293 19740 20888 28043 -392 1608 -557 O ATOM 2133 CB ARG A 293 12.207 33.665 37.293 1.00197.85 C ANISOU 2133 CB ARG A 293 21554 22786 30835 -143 1815 -335 C ATOM 2134 CG ARG A 293 12.775 35.077 37.355 1.00203.00 C ANISOU 2134 CG ARG A 293 22196 23298 31637 -80 2034 -380 C ATOM 2135 CD ARG A 293 11.719 36.116 37.009 1.00208.77 C ANISOU 2135 CD ARG A 293 22583 23813 32927 28 2194 -190 C ATOM 2136 NE ARG A 293 11.285 36.008 35.619 1.00211.53 N ANISOU 2136 NE ARG A 293 22725 24235 33412 117 1844 121 N ATOM 2137 CZ ARG A 293 10.371 36.792 35.056 1.00214.82 C ANISOU 2137 CZ ARG A 293 22814 24494 34312 215 1871 363 C ATOM 2138 NH1 ARG A 293 9.787 37.749 35.764 1.00218.11 N ANISOU 2138 NH1 ARG A 293 23062 24654 35156 255 2259 317 N ATOM 2139 NH2 ARG A 293 10.040 36.620 33.783 1.00214.51 N ANISOU 2139 NH2 ARG A 293 22619 24548 34337 265 1512 654 N ATOM 2140 N GLU A 294 12.535 30.507 36.276 1.00165.67 N ANISOU 2140 N GLU A 294 17743 19164 26041 -264 1049 -266 N ATOM 2141 CA GLU A 294 11.912 29.190 36.206 1.00154.42 C ANISOU 2141 CA GLU A 294 16316 17832 24525 -333 854 -223 C ATOM 2142 C GLU A 294 12.775 28.127 36.879 1.00141.57 C ANISOU 2142 C GLU A 294 14990 16324 22476 -435 797 -423 C ATOM 2143 O GLU A 294 12.261 27.169 37.455 1.00133.19 O ANISOU 2143 O GLU A 294 13963 15282 21363 -524 794 -466 O ATOM 2144 CB GLU A 294 11.637 28.804 34.751 1.00160.25 C ANISOU 2144 CB GLU A 294 16943 18678 25266 -287 480 2 C ATOM 2145 CG GLU A 294 11.040 27.414 34.570 1.00170.18 C ANISOU 2145 CG GLU A 294 18212 20033 26416 -369 249 44 C ATOM 2146 CD GLU A 294 9.646 27.284 35.159 1.00178.39 C ANISOU 2146 CD GLU A 294 19025 20955 27801 -406 400 114 C ATOM 2147 OE1 GLU A 294 9.131 26.147 35.217 1.00176.60 O ANISOU 2147 OE1 GLU A 294 18811 20789 27500 -488 255 127 O ATOM 2148 OE2 GLU A 294 9.063 28.313 35.561 1.00183.90 O ANISOU 2148 OE2 GLU A 294 19525 21488 28860 -355 674 155 O ATOM 2149 N PHE A 295 14.090 28.305 36.803 1.00145.05 N ANISOU 2149 N PHE A 295 15636 16837 22638 -423 749 -531 N ATOM 2150 CA PHE A 295 15.029 27.354 37.389 1.00144.25 C ANISOU 2150 CA PHE A 295 15807 16842 22160 -510 674 -697 C ATOM 2151 C PHE A 295 15.084 27.455 38.911 1.00139.82 C ANISOU 2151 C PHE A 295 15368 16203 21553 -620 970 -880 C ATOM 2152 O PHE A 295 14.933 26.454 39.611 1.00132.96 O ANISOU 2152 O PHE A 295 14610 15374 20535 -726 951 -950 O ATOM 2153 CB PHE A 295 16.430 27.545 36.801 1.00143.47 C ANISOU 2153 CB PHE A 295 15865 16839 21810 -461 532 -740 C ATOM 2154 CG PHE A 295 16.676 26.762 35.541 1.00143.33 C ANISOU 2154 CG PHE A 295 15864 16953 21642 -419 195 -637 C ATOM 2155 CD1 PHE A 295 17.101 25.445 35.600 1.00138.79 C ANISOU 2155 CD1 PHE A 295 15453 16479 20803 -479 12 -708 C ATOM 2156 CD2 PHE A 295 16.495 27.346 34.298 1.00143.96 C ANISOU 2156 CD2 PHE A 295 15805 17051 21842 -329 67 -469 C ATOM 2157 CE1 PHE A 295 17.334 24.723 34.443 1.00132.86 C ANISOU 2157 CE1 PHE A 295 14733 15836 19911 -449 -269 -639 C ATOM 2158 CE2 PHE A 295 16.727 26.629 33.138 1.00141.45 C ANISOU 2158 CE2 PHE A 295 15531 16860 21355 -315 -227 -390 C ATOM 2159 CZ PHE A 295 17.147 25.316 33.212 1.00135.32 C ANISOU 2159 CZ PHE A 295 14925 16175 20315 -375 -384 -488 C ATOM 2160 N ARG A 296 15.301 28.665 39.418 1.00139.50 N ANISOU 2160 N ARG A 296 15317 16050 21634 -608 1244 -957 N ATOM 2161 CA ARG A 296 15.449 28.873 40.856 1.00137.74 C ANISOU 2161 CA ARG A 296 15244 15756 21332 -736 1539 -1150 C ATOM 2162 C ARG A 296 14.266 28.326 41.649 1.00146.24 C ANISOU 2162 C ARG A 296 16256 16772 22538 -829 1702 -1164 C ATOM 2163 O ARG A 296 14.437 27.802 42.750 1.00150.05 O ANISOU 2163 O ARG A 296 16926 17272 22813 -975 1810 -1303 O ATOM 2164 CB ARG A 296 15.669 30.355 41.173 1.00131.83 C ANISOU 2164 CB ARG A 296 14464 14867 20758 -707 1832 -1224 C ATOM 2165 CG ARG A 296 14.555 31.274 40.706 1.00136.16 C ANISOU 2165 CG ARG A 296 14713 15258 21763 -598 1995 -1091 C ATOM 2166 CD ARG A 296 14.832 32.714 41.109 1.00147.64 C ANISOU 2166 CD ARG A 296 16155 16551 23391 -578 2307 -1187 C ATOM 2167 NE ARG A 296 13.697 33.588 40.832 1.00174.52 N ANISOU 2167 NE ARG A 296 19260 19768 27282 -480 2509 -1067 N ATOM 2168 CZ ARG A 296 13.656 34.881 41.141 1.00189.74 C ANISOU 2168 CZ ARG A 296 21118 21506 29468 -448 2819 -1129 C ATOM 2169 NH1 ARG A 296 12.580 35.600 40.853 1.00194.41 N ANISOU 2169 NH1 ARG A 296 21410 21915 30542 -349 2990 -996 N ATOM 2170 NH2 ARG A 296 14.691 35.455 41.739 1.00192.78 N ANISOU 2170 NH2 ARG A 296 21726 21875 29648 -518 2956 -1320 N ATOM 2171 N GLN A 297 13.068 28.447 41.086 1.00149.13 N ANISOU 2171 N GLN A 297 16351 17066 23247 -753 1713 -1006 N ATOM 2172 CA GLN A 297 11.862 27.954 41.741 1.00154.53 C ANISOU 2172 CA GLN A 297 16930 17682 24104 -830 1872 -997 C ATOM 2173 C GLN A 297 11.813 26.429 41.716 1.00149.47 C ANISOU 2173 C GLN A 297 16392 17180 23221 -909 1603 -969 C ATOM 2174 O GLN A 297 11.299 25.799 42.641 1.00145.02 O ANISOU 2174 O GLN A 297 15885 16599 22617 -1034 1736 -1036 O ATOM 2175 CB GLN A 297 10.614 28.535 41.076 1.00166.67 C ANISOU 2175 CB GLN A 297 18114 19095 26116 -720 1935 -809 C ATOM 2176 CG GLN A 297 10.559 30.054 41.086 1.00171.78 C ANISOU 2176 CG GLN A 297 18627 19574 27069 -632 2215 -817 C ATOM 2177 CD GLN A 297 9.339 30.596 40.369 1.00172.98 C ANISOU 2177 CD GLN A 297 18403 19596 27723 -516 2241 -594 C ATOM 2178 OE1 GLN A 297 8.412 29.851 40.048 1.00166.41 O ANISOU 2178 OE1 GLN A 297 17407 18790 27029 -524 2099 -451 O ATOM 2179 NE2 GLN A 297 9.332 31.899 40.113 1.00174.98 N ANISOU 2179 NE2 GLN A 297 18511 19701 28271 -412 2413 -552 N ATOM 2180 N THR A 298 12.351 25.844 40.651 1.00152.45 N ANISOU 2180 N THR A 298 16800 17686 23439 -843 1238 -875 N ATOM 2181 CA THR A 298 12.424 24.394 40.527 1.00157.59 C ANISOU 2181 CA THR A 298 17560 18456 23859 -909 968 -857 C ATOM 2182 C THR A 298 13.382 23.816 41.563 1.00165.09 C ANISOU 2182 C THR A 298 18805 19464 24456 -1033 999 -1029 C ATOM 2183 O THR A 298 13.051 22.853 42.257 1.00165.54 O ANISOU 2183 O THR A 298 18945 19541 24412 -1152 995 -1059 O ATOM 2184 CB THR A 298 12.882 23.970 39.119 1.00157.06 C ANISOU 2184 CB THR A 298 17482 18504 23691 -815 596 -743 C ATOM 2185 OG1 THR A 298 11.969 24.485 38.142 1.00156.77 O ANISOU 2185 OG1 THR A 298 17176 18424 23967 -723 533 -557 O ATOM 2186 CG2 THR A 298 12.934 22.455 39.008 1.00157.14 C ANISOU 2186 CG2 THR A 298 17608 18612 23486 -887 339 -741 C ATOM 2187 N PHE A 299 14.569 24.408 41.663 1.00168.04 N ANISOU 2187 N PHE A 299 19332 19864 24653 -1014 1018 -1125 N ATOM 2188 CA PHE A 299 15.558 23.984 42.648 1.00169.26 C ANISOU 2188 CA PHE A 299 19755 20070 24485 -1139 1033 -1269 C ATOM 2189 C PHE A 299 15.012 24.154 44.061 1.00169.50 C ANISOU 2189 C PHE A 299 19855 20020 24528 -1296 1355 -1378 C ATOM 2190 O PHE A 299 15.110 23.250 44.891 1.00171.22 O ANISOU 2190 O PHE A 299 20236 20281 24538 -1439 1329 -1428 O ATOM 2191 CB PHE A 299 16.853 24.789 42.505 1.00175.62 C ANISOU 2191 CB PHE A 299 20674 20899 25154 -1093 1025 -1342 C ATOM 2192 CG PHE A 299 17.491 24.689 41.146 1.00178.16 C ANISOU 2192 CG PHE A 299 20949 21302 25442 -950 744 -1249 C ATOM 2193 CD1 PHE A 299 17.964 23.477 40.673 1.00177.32 C ANISOU 2193 CD1 PHE A 299 20930 21300 25145 -947 453 -1218 C ATOM 2194 CD2 PHE A 299 17.639 25.815 40.353 1.00175.56 C ANISOU 2194 CD2 PHE A 299 20498 20937 25271 -827 787 -1198 C ATOM 2195 CE1 PHE A 299 18.558 23.387 39.427 1.00170.11 C ANISOU 2195 CE1 PHE A 299 19991 20457 24187 -829 226 -1153 C ATOM 2196 CE2 PHE A 299 18.232 25.731 39.108 1.00169.09 C ANISOU 2196 CE2 PHE A 299 19652 20199 24395 -715 544 -1115 C ATOM 2197 CZ PHE A 299 18.692 24.516 38.644 1.00166.30 C ANISOU 2197 CZ PHE A 299 19396 19953 23837 -719 273 -1101 C ATOM 2198 N ARG A 300 14.438 25.325 44.321 1.00167.17 N ANISOU 2198 N ARG A 300 19438 19599 24482 -1274 1668 -1413 N ATOM 2199 CA ARG A 300 13.885 25.657 45.630 1.00165.71 C ANISOU 2199 CA ARG A 300 19316 19317 24330 -1424 2035 -1540 C ATOM 2200 C ARG A 300 12.924 24.580 46.123 1.00168.22 C ANISOU 2200 C ARG A 300 19611 19644 24661 -1529 2047 -1499 C ATOM 2201 O ARG A 300 12.807 24.337 47.324 1.00170.39 O ANISOU 2201 O ARG A 300 20048 19904 24787 -1709 2249 -1611 O ATOM 2202 CB ARG A 300 13.175 27.010 45.568 1.00167.24 C ANISOU 2202 CB ARG A 300 19306 19343 24893 -1345 2363 -1552 C ATOM 2203 CG ARG A 300 12.639 27.508 46.898 1.00177.63 C ANISOU 2203 CG ARG A 300 20692 20536 26262 -1498 2802 -1714 C ATOM 2204 CD ARG A 300 12.016 28.884 46.739 1.00193.93 C ANISOU 2204 CD ARG A 300 22541 22412 28733 -1396 3126 -1726 C ATOM 2205 NE ARG A 300 11.435 29.377 47.983 1.00211.34 N ANISOU 2205 NE ARG A 300 24806 24478 31016 -1543 3589 -1898 N ATOM 2206 CZ ARG A 300 10.819 30.548 48.105 1.00221.93 C ANISOU 2206 CZ ARG A 300 25977 25619 32726 -1485 3957 -1948 C ATOM 2207 NH1 ARG A 300 10.703 31.349 47.054 1.00225.62 N ANISOU 2207 NH1 ARG A 300 26197 26005 33523 -1282 3889 -1815 N ATOM 2208 NH2 ARG A 300 10.317 30.919 49.274 1.00224.91 N ANISOU 2208 NH2 ARG A 300 26437 25871 33149 -1637 4399 -2130 N ATOM 2209 N LYS A 301 12.239 23.936 45.185 1.00168.59 N ANISOU 2209 N LYS A 301 19463 19719 24876 -1431 1825 -1336 N ATOM 2210 CA LYS A 301 11.304 22.869 45.515 1.00173.65 C ANISOU 2210 CA LYS A 301 20057 20368 25555 -1522 1801 -1276 C ATOM 2211 C LYS A 301 12.031 21.557 45.797 1.00175.95 C ANISOU 2211 C LYS A 301 20584 20785 25484 -1626 1533 -1292 C ATOM 2212 O LYS A 301 11.711 20.854 46.756 1.00178.39 O ANISOU 2212 O LYS A 301 21007 21099 25676 -1788 1623 -1330 O ATOM 2213 CB LYS A 301 10.291 22.693 44.384 1.00177.54 C ANISOU 2213 CB LYS A 301 20248 20837 26373 -1393 1647 -1089 C ATOM 2214 CG LYS A 301 9.468 21.420 44.463 1.00179.36 C ANISOU 2214 CG LYS A 301 20430 21099 26620 -1475 1518 -1003 C ATOM 2215 CD LYS A 301 9.772 20.524 43.276 1.00177.89 C ANISOU 2215 CD LYS A 301 20232 21022 26338 -1399 1082 -885 C ATOM 2216 CE LYS A 301 9.615 21.283 41.968 1.00179.04 C ANISOU 2216 CE LYS A 301 20161 21155 26710 -1229 953 -760 C ATOM 2217 NZ LYS A 301 10.354 20.631 40.852 1.00179.52 N ANISOU 2217 NZ LYS A 301 20302 21336 26571 -1163 562 -706 N ATOM 2218 N ILE A 302 13.012 21.233 44.960 1.00175.73 N ANISOU 2218 N ILE A 302 20627 20851 25293 -1536 1213 -1257 N ATOM 2219 CA ILE A 302 13.791 20.010 45.130 1.00173.61 C ANISOU 2219 CA ILE A 302 20562 20682 24721 -1610 948 -1263 C ATOM 2220 C ILE A 302 14.435 19.954 46.510 1.00173.28 C ANISOU 2220 C ILE A 302 20776 20653 24410 -1793 1091 -1386 C ATOM 2221 O ILE A 302 14.330 18.951 47.216 1.00175.49 O ANISOU 2221 O ILE A 302 21180 20962 24537 -1934 1038 -1379 O ATOM 2222 CB ILE A 302 14.900 19.889 44.066 1.00168.18 C ANISOU 2222 CB ILE A 302 19915 20075 23912 -1479 645 -1235 C ATOM 2223 CG1 ILE A 302 14.306 19.952 42.658 1.00168.92 C ANISOU 2223 CG1 ILE A 302 19784 20170 24228 -1324 485 -1109 C ATOM 2224 CG2 ILE A 302 15.683 18.600 44.259 1.00162.96 C ANISOU 2224 CG2 ILE A 302 19443 19489 22987 -1548 389 -1239 C ATOM 2225 CD1 ILE A 302 15.339 19.841 41.556 1.00161.59 C ANISOU 2225 CD1 ILE A 302 18902 19321 23176 -1205 216 -1090 C ATOM 2226 N ILE A 303 15.102 21.041 46.887 1.00170.65 N ANISOU 2226 N ILE A 303 20527 20298 24016 -1801 1264 -1492 N ATOM 2227 CA ILE A 303 15.807 21.113 48.162 1.00170.92 C ANISOU 2227 CA ILE A 303 20821 20352 23771 -1992 1385 -1611 C ATOM 2228 C ILE A 303 14.875 20.864 49.344 1.00174.79 C ANISOU 2228 C ILE A 303 21371 20794 24247 -2187 1654 -1658 C ATOM 2229 O ILE A 303 15.118 19.975 50.161 1.00175.34 O ANISOU 2229 O ILE A 303 21631 20919 24071 -2358 1577 -1658 O ATOM 2230 CB ILE A 303 16.497 22.479 48.346 1.00164.85 C ANISOU 2230 CB ILE A 303 20107 19544 22984 -1978 1570 -1727 C ATOM 2231 CG1 ILE A 303 17.433 22.765 47.170 1.00146.67 C ANISOU 2231 CG1 ILE A 303 17742 17289 20698 -1791 1321 -1677 C ATOM 2232 CG2 ILE A 303 17.256 22.521 49.664 1.00166.68 C ANISOU 2232 CG2 ILE A 303 20625 19807 22898 -2205 1663 -1847 C ATOM 2233 CD1 ILE A 303 18.109 24.116 47.243 1.00132.96 C ANISOU 2233 CD1 ILE A 303 16039 15509 18972 -1766 1486 -1776 C ATOM 2234 N ARG A 304 13.810 21.654 49.430 1.00178.76 N ANISOU 2234 N ARG A 304 21707 21189 25026 -2162 1976 -1689 N ATOM 2235 CA ARG A 304 12.855 21.529 50.524 1.00190.91 C ANISOU 2235 CA ARG A 304 23283 22667 26587 -2342 2291 -1746 C ATOM 2236 C ARG A 304 12.297 20.113 50.625 1.00193.77 C ANISOU 2236 C ARG A 304 23641 23080 26901 -2416 2114 -1633 C ATOM 2237 O ARG A 304 12.294 19.513 51.700 1.00197.30 O ANISOU 2237 O ARG A 304 24288 23558 27118 -2629 2187 -1670 O ATOM 2238 CB ARG A 304 11.718 22.540 50.361 1.00197.72 C ANISOU 2238 CB ARG A 304 23896 23385 27846 -2257 2644 -1768 C ATOM 2239 CG ARG A 304 12.160 23.987 50.493 1.00202.55 C ANISOU 2239 CG ARG A 304 24529 23912 28518 -2220 2896 -1902 C ATOM 2240 CD ARG A 304 10.987 24.940 50.350 1.00205.58 C ANISOU 2240 CD ARG A 304 24643 24126 29341 -2130 3256 -1910 C ATOM 2241 NE ARG A 304 11.372 26.320 50.629 1.00208.25 N ANISOU 2241 NE ARG A 304 25025 24358 29743 -2121 3544 -2060 N ATOM 2242 CZ ARG A 304 10.539 27.354 50.571 1.00209.54 C ANISOU 2242 CZ ARG A 304 24973 24345 30299 -2040 3894 -2093 C ATOM 2243 NH1 ARG A 304 10.976 28.576 50.842 1.00210.71 N ANISOU 2243 NH1 ARG A 304 25183 24388 30488 -2041 4146 -2239 N ATOM 2244 NH2 ARG A 304 9.268 27.167 50.241 1.00210.38 N ANISOU 2244 NH2 ARG A 304 24791 24366 30778 -1960 3991 -1974 N ATOM 2245 N SER A 305 11.831 19.582 49.500 1.00191.65 N ANISOU 2245 N SER A 305 23155 22821 26843 -2253 1876 -1491 N ATOM 2246 CA SER A 305 11.258 18.241 49.469 1.00190.29 C ANISOU 2246 CA SER A 305 22957 22683 26662 -2312 1693 -1380 C ATOM 2247 C SER A 305 12.281 17.214 48.994 1.00177.66 C ANISOU 2247 C SER A 305 21492 21185 24826 -2283 1273 -1318 C ATOM 2248 O SER A 305 13.149 16.791 49.757 1.00170.28 O ANISOU 2248 O SER A 305 20802 20305 23589 -2417 1199 -1360 O ATOM 2249 CB SER A 305 10.018 18.208 48.573 1.00195.78 C ANISOU 2249 CB SER A 305 23330 23316 27740 -2181 1688 -1260 C ATOM 2250 OG SER A 305 9.399 16.933 48.601 1.00195.16 O ANISOU 2250 OG SER A 305 23226 23261 27667 -2256 1532 -1159 O TER 2251 SER A 305 HETATM 2252 C1 XAC A 999 48.999 24.127 30.369 1.00135.88 C HETATM 2253 N1 XAC A 999 47.420 21.950 31.232 1.00138.86 N HETATM 2254 O1 XAC A 999 49.720 25.080 30.049 1.00134.02 O HETATM 2255 C2 XAC A 999 47.253 22.480 29.971 1.00138.43 C HETATM 2256 N2 XAC A 999 48.022 23.568 29.592 1.00136.32 N HETATM 2257 O2 XAC A 999 46.413 21.992 29.200 1.00138.97 O HETATM 2258 C3 XAC A 999 49.710 23.027 33.745 1.00137.42 C HETATM 2259 N3 XAC A 999 48.744 22.145 33.419 1.00137.76 N HETATM 2260 O3 XAC A 999 52.177 23.419 38.861 1.00138.97 O HETATM 2261 C4 XAC A 999 48.393 22.487 32.111 1.00138.09 C HETATM 2262 N4 XAC A 999 49.971 23.867 32.721 1.00137.07 N HETATM 2263 O4 XAC A 999 53.469 23.025 41.513 1.00139.58 O HETATM 2264 C5 XAC A 999 49.132 23.520 31.679 1.00137.35 C HETATM 2265 N5 XAC A 999 51.509 23.992 42.074 1.00136.41 N HETATM 2266 C6 XAC A 999 47.740 24.215 28.290 1.00134.91 C HETATM 2267 N6 XAC A 999 51.161 25.965 45.217 1.00131.76 N HETATM 2268 C7 XAC A 999 46.694 25.338 28.436 1.00130.45 C HETATM 2269 C8 XAC A 999 46.580 20.848 31.722 1.00139.84 C HETATM 2270 C9 XAC A 999 47.275 19.484 31.565 1.00140.76 C HETATM 2271 C10 XAC A 999 46.490 18.350 32.233 1.00142.47 C HETATM 2272 C11 XAC A 999 46.268 25.934 27.091 1.00128.15 C HETATM 2273 C12 XAC A 999 51.572 23.242 37.635 1.00136.80 C HETATM 2274 C13 XAC A 999 50.572 22.276 37.365 1.00138.29 C HETATM 2275 C14 XAC A 999 49.974 22.199 36.092 1.00137.27 C HETATM 2276 C15 XAC A 999 50.368 23.077 35.056 1.00136.45 C HETATM 2277 C16 XAC A 999 51.391 24.017 35.316 1.00135.82 C HETATM 2278 C17 XAC A 999 51.984 24.096 36.593 1.00135.27 C HETATM 2279 C18 XAC A 999 51.640 22.721 39.981 1.00141.47 C HETATM 2280 C19 XAC A 999 52.284 23.261 41.262 1.00139.22 C HETATM 2281 C20 XAC A 999 51.925 24.580 43.339 1.00134.77 C HETATM 2282 C21 XAC A 999 50.760 25.370 43.957 1.00131.01 C CONECT 484 1071 CONECT 500 1041 CONECT 520 1115 CONECT 1041 500 CONECT 1071 484 CONECT 1115 520 CONECT 1861 1882 CONECT 1882 1861 CONECT 2252 2254 2256 2264 CONECT 2253 2255 2261 2269 CONECT 2254 2252 CONECT 2255 2253 2256 2257 CONECT 2256 2252 2255 2266 CONECT 2257 2255 CONECT 2258 2259 2262 2276 CONECT 2259 2258 2261 CONECT 2260 2273 2279 CONECT 2261 2253 2259 2264 CONECT 2262 2258 2264 CONECT 2263 2280 CONECT 2264 2252 2261 2262 CONECT 2265 2280 2281 CONECT 2266 2256 2268 CONECT 2267 2282 CONECT 2268 2266 2272 CONECT 2269 2253 2270 CONECT 2270 2269 2271 CONECT 2271 2270 CONECT 2272 2268 CONECT 2273 2260 2274 2278 CONECT 2274 2273 2275 CONECT 2275 2274 2276 CONECT 2276 2258 2275 2277 CONECT 2277 2276 2278 CONECT 2278 2273 2277 CONECT 2279 2260 2280 CONECT 2280 2263 2265 2279 CONECT 2281 2265 2282 CONECT 2282 2267 2281 MASTER 309 0 1 14 2 0 3 6 2281 1 39 26 END