HEADER SIGNALING PROTEIN 06-APR-11 3RFM TITLE THERMOSTABILISED ADENOSINE A2A RECEPTOR IN COMPLEX WITH CAFFEINE 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 INVERSE AGONIST, 7TM, GPCR, SIGNALING PROTEIN, G-PROTEIN, MEMBRANE KEYWDS 2 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 3RFM 1 JRNL REVDAT 1 07-SEP-11 3RFM 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. 3.60 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) : 3.60 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.97 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350 REMARK 3 COMPLETENESS FOR RANGE (%) : 89.2 REMARK 3 NUMBER OF REFLECTIONS : 8775 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.297 REMARK 3 R VALUE (WORKING SET) : 0.297 REMARK 3 FREE R VALUE : 0.311 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.810 REMARK 3 FREE R VALUE TEST SET COUNT : 422 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 19.9717 - 5.1691 0.88 2829 139 0.2742 0.2939 REMARK 3 2 5.1691 - 4.1146 0.90 2777 138 0.2609 0.2582 REMARK 3 3 4.1146 - 3.5980 0.89 2747 145 0.4149 0.4433 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 : 71.44 REMARK 3 REMARK 3 ERROR ESTIMATES. REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.390 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 42.960 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 108.36 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 148.89 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : -81.75570 REMARK 3 B22 (A**2) : 7.26170 REMARK 3 B33 (A**2) : 74.49400 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 : 0.002 2325 REMARK 3 ANGLE : 0.389 3171 REMARK 3 CHIRALITY : 0.027 377 REMARK 3 PLANARITY : 0.002 388 REMARK 3 DIHEDRAL : 10.516 781 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): 23.5394 -31.1724 -28.8621 REMARK 3 T TENSOR REMARK 3 T11: 0.8085 T22: 0.8086 REMARK 3 T33: 0.8771 T12: -0.0604 REMARK 3 T13: -0.0970 T23: -0.0705 REMARK 3 L TENSOR REMARK 3 L11: 0.9860 L22: 2.1254 REMARK 3 L33: 1.8727 L12: -1.3229 REMARK 3 L13: 0.0883 L23: -0.1383 REMARK 3 S TENSOR REMARK 3 S11: 0.1886 S12: -0.2845 S13: 0.4812 REMARK 3 S21: 0.0605 S22: -0.0739 S23: 0.1058 REMARK 3 S31: 0.0025 S32: 0.2174 S33: 0.0000 REMARK 3 REMARK 3 NCS DETAILS REMARK 3 NUMBER OF NCS GROUPS : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 3RFM 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 RCSB064870. 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 : DECTRIS PILATUS 6M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : SCALA REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 8939 REMARK 200 RESOLUTION RANGE HIGH (A) : 3.590 REMARK 200 RESOLUTION RANGE LOW (A) : 50.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.500 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 91.9 REMARK 200 DATA REDUNDANCY : 6.700 REMARK 200 R MERGE (I) : 0.13900 REMARK 200 R SYM (I) : NULL REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 6.8000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.60 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.79 REMARK 200 COMPLETENESS FOR SHELL (%) : 93.5 REMARK 200 DATA REDUNDANCY IN SHELL : 6.80 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 (%): NULL REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): NULL 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 8.2, 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 56.16350 REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 56.66400 REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 64.65000 REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 56.16350 REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 56.66400 REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 64.65000 REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 56.16350 REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 56.66400 REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 64.65000 REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 56.16350 REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 56.66400 REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 64.65000 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 33.43 -91.75 REMARK 500 ALA A 73 173.54 -58.85 REMARK 500 LEU A 115 -61.58 -96.21 REMARK 500 VAL A 116 92.04 -67.29 REMARK 500 ALA A 165 101.06 -58.70 REMARK 500 VAL A 178 -67.24 -92.35 REMARK 500 VAL A 186 -56.76 -141.95 REMARK 500 PHE A 257 -70.41 -72.01 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 CFF A 330 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: 3REY RELATED DB: PDB REMARK 900 THE SAME PROTEIN COMPLEXED WITH XAC DBREF 3RFM A 1 317 UNP P29274 AA2AR_HUMAN 1 317 SEQADV 3RFM LEU A 54 UNP P29274 ALA 54 ENGINEERED MUTATION SEQADV 3RFM ALA A 88 UNP P29274 THR 88 ENGINEERED MUTATION SEQADV 3RFM ALA A 107 UNP P29274 ARG 107 ENGINEERED MUTATION SEQADV 3RFM ALA A 122 UNP P29274 LYS 122 ENGINEERED MUTATION SEQADV 3RFM ALA A 202 UNP P29274 LEU 202 ENGINEERED MUTATION SEQADV 3RFM ALA A 235 UNP P29274 LEU 235 ENGINEERED MUTATION SEQADV 3RFM ALA A 239 UNP P29274 VAL 239 ENGINEERED MUTATION SEQADV 3RFM ALA A 277 UNP P29274 SER 277 ENGINEERED MUTATION SEQADV 3RFM ALA A 318 UNP P29274 EXPRESSION TAG SEQADV 3RFM ALA A 319 UNP P29274 EXPRESSION TAG SEQADV 3RFM HIS A 320 UNP P29274 EXPRESSION TAG SEQADV 3RFM HIS A 321 UNP P29274 EXPRESSION TAG SEQADV 3RFM HIS A 322 UNP P29274 EXPRESSION TAG SEQADV 3RFM HIS A 323 UNP P29274 EXPRESSION TAG SEQADV 3RFM HIS A 324 UNP P29274 EXPRESSION TAG SEQADV 3RFM HIS A 325 UNP P29274 EXPRESSION TAG SEQADV 3RFM HIS A 326 UNP P29274 EXPRESSION TAG SEQADV 3RFM HIS A 327 UNP P29274 EXPRESSION TAG SEQADV 3RFM HIS A 328 UNP P29274 EXPRESSION TAG SEQADV 3RFM 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 CFF A 330 14 HETNAM CFF CAFFEINE HETSYN CFF 3,7-DIHYDRO-1,3,7-TRIMETHYL-1H-PURINE-2,6-DIONE FORMUL 2 CFF C8 H10 N4 O2 HELIX 1 1 SER A 7 ASN A 34 1 28 HELIX 2 2 SER A 35 GLN A 38 5 4 HELIX 3 3 ASN A 39 VAL A 40 5 2 HELIX 4 4 THR A 41 LEU A 58 1 18 HELIX 5 5 LEU A 58 GLY A 69 1 12 HELIX 6 6 ALA A 73 ILE A 108 1 36 HELIX 7 7 ILE A 108 VAL A 116 1 9 HELIX 8 8 THR A 117 LEU A 137 1 21 HELIX 9 9 THR A 138 GLY A 142 5 5 HELIX 10 10 LEU A 167 VAL A 172 1 6 HELIX 11 11 PRO A 173 TYR A 179 1 7 HELIX 12 12 ASN A 181 VAL A 186 1 6 HELIX 13 13 VAL A 186 MET A 211 1 26 HELIX 14 14 GLU A 212 GLN A 214 5 3 HELIX 15 15 GLY A 218 CYS A 259 1 42 HELIX 16 16 PRO A 266 ILE A 292 1 27 HELIX 17 17 ILE A 292 SER A 305 1 14 SHEET 1 A 2 PHE A 70 ALA A 72 0 SHEET 2 A 2 VAL A 164 CYS A 166 -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 2.03 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 6 PHE A 168 MET A 177 LEU A 249 ASN A 253 SITE 2 AC1 6 MET A 270 ILE A 274 CRYST1 112.327 113.328 129.300 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 0.008903 0.000000 0.000000 0.00000 SCALE2 0.000000 0.008824 0.000000 0.00000 SCALE3 0.000000 0.000000 0.007734 0.00000 ATOM 1 N SER A 7 6.159 -34.006 -51.651 1.00173.70 N ANISOU 1 N SER A 7 23082 19588 23328 2203 -4205 -175 N ATOM 2 CA SER A 7 7.411 -34.717 -51.420 1.00167.91 C ANISOU 2 CA SER A 7 22499 18893 22408 2150 -4109 -100 C ATOM 3 C SER A 7 8.576 -33.748 -51.253 1.00160.56 C ANISOU 3 C SER A 7 21632 18016 21357 2188 -3781 -8 C ATOM 4 O SER A 7 9.732 -34.120 -51.446 1.00158.67 O ANISOU 4 O SER A 7 21567 17796 20924 2246 -3704 72 O ATOM 5 CB SER A 7 7.696 -35.690 -52.566 1.00169.28 C ANISOU 5 CB SER A 7 22958 18973 22387 2373 -4378 -86 C ATOM 6 OG SER A 7 6.695 -36.690 -52.648 1.00172.73 O ANISOU 6 OG SER A 7 23336 19350 22946 2304 -4694 -177 O ATOM 7 N VAL A 8 8.265 -32.506 -50.893 1.00157.19 N ANISOU 7 N VAL A 8 21060 17609 21054 2155 -3592 -20 N ATOM 8 CA VAL A 8 9.290 -31.489 -50.680 1.00151.82 C ANISOU 8 CA VAL A 8 20419 16965 20302 2165 -3282 58 C ATOM 9 C VAL A 8 9.910 -31.630 -49.294 1.00150.82 C ANISOU 9 C VAL A 8 20132 16953 20218 1876 -3071 61 C ATOM 10 O VAL A 8 11.132 -31.650 -49.150 1.00148.50 O ANISOU 10 O VAL A 8 19927 16705 19790 1860 -2910 135 O ATOM 11 CB VAL A 8 8.720 -30.068 -50.840 1.00145.24 C ANISOU 11 CB VAL A 8 19515 16089 19579 2251 -3165 41 C ATOM 12 CG1 VAL A 8 9.794 -29.031 -50.552 1.00136.41 C ANISOU 12 CG1 VAL A 8 18429 14991 18410 2228 -2844 119 C ATOM 13 CG2 VAL A 8 8.149 -29.883 -52.238 1.00148.00 C ANISOU 13 CG2 VAL A 8 20042 16326 19865 2567 -3371 40 C ATOM 14 N TYR A 9 9.056 -31.725 -48.278 1.00151.15 N ANISOU 14 N TYR A 9 19937 17047 20447 1658 -3072 -18 N ATOM 15 CA TYR A 9 9.508 -31.947 -46.909 1.00149.91 C ANISOU 15 CA TYR A 9 19633 16999 20328 1394 -2897 -27 C ATOM 16 C TYR A 9 10.413 -33.169 -46.848 1.00154.47 C ANISOU 16 C TYR A 9 20336 17613 20741 1355 -2955 19 C ATOM 17 O TYR A 9 11.458 -33.153 -46.195 1.00156.43 O ANISOU 17 O TYR A 9 20588 17942 20906 1255 -2773 57 O ATOM 18 CB TYR A 9 8.310 -32.138 -45.979 1.00148.92 C ANISOU 18 CB TYR A 9 19258 16912 20413 1202 -2937 -109 C ATOM 19 CG TYR A 9 8.679 -32.569 -44.577 1.00144.59 C ANISOU 19 CG TYR A 9 18580 16472 19886 947 -2787 -118 C ATOM 20 CD1 TYR A 9 9.042 -31.636 -43.615 1.00142.24 C ANISOU 20 CD1 TYR A 9 18173 16242 19628 834 -2529 -131 C ATOM 21 CD2 TYR A 9 8.656 -33.909 -44.214 1.00141.93 C ANISOU 21 CD2 TYR A 9 18244 16158 19524 829 -2909 -116 C ATOM 22 CE1 TYR A 9 9.377 -32.026 -42.332 1.00142.43 C ANISOU 22 CE1 TYR A 9 18095 16366 19655 624 -2401 -145 C ATOM 23 CE2 TYR A 9 8.988 -34.309 -42.932 1.00139.75 C ANISOU 23 CE2 TYR A 9 17867 15979 19252 616 -2767 -119 C ATOM 24 CZ TYR A 9 9.348 -33.363 -41.995 1.00142.63 C ANISOU 24 CZ TYR A 9 18126 16420 19645 522 -2516 -136 C ATOM 25 OH TYR A 9 9.681 -33.753 -40.717 1.00144.26 O ANISOU 25 OH TYR A 9 18249 16725 19840 333 -2383 -145 O ATOM 26 N ILE A 10 10.002 -34.228 -47.536 1.00156.61 N ANISOU 26 N ILE A 10 20714 17823 20968 1440 -3220 10 N ATOM 27 CA ILE A 10 10.781 -35.456 -47.597 1.00156.24 C ANISOU 27 CA ILE A 10 20818 17792 20753 1435 -3307 52 C ATOM 28 C ILE A 10 12.152 -35.192 -48.207 1.00149.52 C ANISOU 28 C ILE A 10 20171 16957 19684 1605 -3183 147 C ATOM 29 O ILE A 10 13.175 -35.623 -47.676 1.00142.61 O ANISOU 29 O ILE A 10 19327 16163 18694 1526 -3068 191 O ATOM 30 CB ILE A 10 10.063 -36.532 -48.431 1.00161.19 C ANISOU 30 CB ILE A 10 21561 18318 21366 1538 -3641 19 C ATOM 31 CG1 ILE A 10 8.636 -36.741 -47.919 1.00163.62 C ANISOU 31 CG1 ILE A 10 21641 18604 21922 1373 -3769 -69 C ATOM 32 CG2 ILE A 10 10.848 -37.837 -48.407 1.00161.26 C ANISOU 32 CG2 ILE A 10 21736 18337 21200 1526 -3728 58 C ATOM 33 CD1 ILE A 10 7.834 -37.733 -48.732 1.00166.05 C ANISOU 33 CD1 ILE A 10 22034 18798 22258 1455 -4119 -115 C ATOM 34 N THR A 11 12.162 -34.476 -49.327 1.00147.83 N ANISOU 34 N THR A 11 20089 16664 19413 1848 -3201 183 N ATOM 35 CA THR A 11 13.403 -34.156 -50.022 1.00140.47 C ANISOU 35 CA THR A 11 19349 15737 18286 2033 -3070 290 C ATOM 36 C THR A 11 14.377 -33.410 -49.114 1.00132.13 C ANISOU 36 C THR A 11 18173 14783 17250 1875 -2760 330 C ATOM 37 O THR A 11 15.554 -33.762 -49.029 1.00134.91 O ANISOU 37 O THR A 11 18601 15201 17456 1882 -2659 401 O ATOM 38 CB THR A 11 13.141 -33.316 -51.288 1.00139.69 C ANISOU 38 CB THR A 11 19395 15531 18148 2315 -3102 327 C ATOM 39 OG1 THR A 11 12.335 -34.068 -52.202 1.00140.35 O ANISOU 39 OG1 THR A 11 19617 15521 18189 2489 -3417 284 O ATOM 40 CG2 THR A 11 14.452 -32.947 -51.965 1.00140.83 C ANISOU 40 CG2 THR A 11 19725 15682 18101 2499 -2927 459 C ATOM 41 N VAL A 12 13.881 -32.381 -48.434 1.00119.14 N ANISOU 41 N VAL A 12 16337 13146 15783 1738 -2618 278 N ATOM 42 CA VAL A 12 14.713 -31.582 -47.542 1.00107.31 C ANISOU 42 CA VAL A 12 14719 11727 14325 1582 -2343 294 C ATOM 43 C VAL A 12 15.232 -32.406 -46.368 1.00110.40 C ANISOU 43 C VAL A 12 15014 12240 14692 1362 -2304 267 C ATOM 44 O VAL A 12 16.387 -32.265 -45.965 1.00112.51 O ANISOU 44 O VAL A 12 15277 12586 14886 1306 -2139 312 O ATOM 45 CB VAL A 12 13.955 -30.352 -47.009 1.00 92.97 C ANISOU 45 CB VAL A 12 12733 9885 12706 1487 -2223 228 C ATOM 46 CG1 VAL A 12 14.767 -29.652 -45.930 1.00 81.16 C ANISOU 46 CG1 VAL A 12 11110 8469 11258 1297 -1972 219 C ATOM 47 CG2 VAL A 12 13.636 -29.397 -48.148 1.00 89.40 C ANISOU 47 CG2 VAL A 12 12394 9314 12259 1718 -2219 267 C ATOM 48 N GLU A 13 14.378 -33.265 -45.822 1.00114.94 N ANISOU 48 N GLU A 13 15509 12830 15333 1242 -2455 197 N ATOM 49 CA GLU A 13 14.773 -34.127 -44.713 1.00125.71 C ANISOU 49 CA GLU A 13 16801 14298 16664 1049 -2428 175 C ATOM 50 C GLU A 13 15.880 -35.093 -45.121 1.00127.84 C ANISOU 50 C GLU A 13 17252 14606 16718 1145 -2477 250 C ATOM 51 O GLU A 13 16.773 -35.399 -44.330 1.00122.27 O ANISOU 51 O GLU A 13 16513 14006 15938 1037 -2366 261 O ATOM 52 CB GLU A 13 13.569 -34.895 -44.170 1.00131.35 C ANISOU 52 CB GLU A 13 17410 14999 17500 918 -2582 103 C ATOM 53 CG GLU A 13 12.656 -34.059 -43.294 1.00139.19 C ANISOU 53 CG GLU A 13 18178 16009 18698 767 -2475 29 C ATOM 54 CD GLU A 13 13.364 -33.534 -42.060 1.00145.57 C ANISOU 54 CD GLU A 13 18874 16925 19511 603 -2238 9 C ATOM 55 OE1 GLU A 13 14.400 -34.116 -41.672 1.00147.93 O ANISOU 55 OE1 GLU A 13 19234 17300 19672 559 -2189 40 O ATOM 56 OE2 GLU A 13 12.884 -32.542 -41.472 1.00148.44 O ANISOU 56 OE2 GLU A 13 19092 17296 20011 527 -2109 -43 O ATOM 57 N LEU A 14 15.815 -35.572 -46.358 1.00130.65 N ANISOU 57 N LEU A 14 17803 14877 16963 1365 -2649 297 N ATOM 58 CA LEU A 14 16.850 -36.449 -46.889 1.00130.90 C ANISOU 58 CA LEU A 14 18032 14935 16770 1502 -2698 376 C ATOM 59 C LEU A 14 18.137 -35.671 -47.130 1.00125.06 C ANISOU 59 C LEU A 14 17325 14254 15937 1588 -2474 466 C ATOM 60 O LEU A 14 19.233 -36.170 -46.875 1.00128.59 O ANISOU 60 O LEU A 14 17815 14796 16247 1585 -2402 518 O ATOM 61 CB LEU A 14 16.383 -37.118 -48.184 1.00140.02 C ANISOU 61 CB LEU A 14 19404 15970 17825 1738 -2952 395 C ATOM 62 CG LEU A 14 15.620 -38.437 -48.039 1.00148.44 C ANISOU 62 CG LEU A 14 20513 16989 18899 1674 -3208 335 C ATOM 63 CD1 LEU A 14 14.510 -38.324 -47.007 1.00151.00 C ANISOU 63 CD1 LEU A 14 20595 17319 19460 1419 -3213 241 C ATOM 64 CD2 LEU A 14 15.065 -38.887 -49.383 1.00154.12 C ANISOU 64 CD2 LEU A 14 21443 17572 19545 1919 -3475 334 C ATOM 65 N ALA A 15 17.997 -34.444 -47.622 1.00116.38 N ANISOU 65 N ALA A 15 16201 13097 14922 1665 -2362 487 N ATOM 66 CA ALA A 15 19.147 -33.583 -47.873 1.00110.10 C ANISOU 66 CA ALA A 15 15418 12337 14077 1730 -2134 580 C ATOM 67 C ALA A 15 19.958 -33.383 -46.597 1.00116.10 C ANISOU 67 C ALA A 15 16000 13227 14884 1497 -1951 554 C ATOM 68 O ALA A 15 21.187 -33.464 -46.612 1.00121.52 O ANISOU 68 O ALA A 15 16712 13997 15465 1527 -1832 630 O ATOM 69 CB ALA A 15 18.698 -32.244 -48.433 1.00100.75 C ANISOU 69 CB ALA A 15 14219 11051 13010 1811 -2037 593 C ATOM 70 N ILE A 16 19.261 -33.127 -45.494 1.00116.69 N ANISOU 70 N ILE A 16 15893 13325 15117 1276 -1932 445 N ATOM 71 CA ILE A 16 19.911 -32.941 -44.202 1.00120.69 C ANISOU 71 CA ILE A 16 16239 13952 15667 1060 -1782 399 C ATOM 72 C ILE A 16 20.579 -34.226 -43.723 1.00129.26 C ANISOU 72 C ILE A 16 17367 15148 16598 1024 -1849 409 C ATOM 73 O ILE A 16 21.723 -34.207 -43.266 1.00131.46 O ANISOU 73 O ILE A 16 17604 15534 16810 976 -1728 435 O ATOM 74 CB ILE A 16 18.912 -32.467 -43.132 1.00118.58 C ANISOU 74 CB ILE A 16 15792 13680 15581 861 -1758 280 C ATOM 75 CG1 ILE A 16 18.409 -31.061 -43.459 1.00121.75 C ANISOU 75 CG1 ILE A 16 16142 13985 16133 888 -1657 266 C ATOM 76 CG2 ILE A 16 19.555 -32.485 -41.754 1.00116.24 C ANISOU 76 CG2 ILE A 16 15360 13512 15294 658 -1639 222 C ATOM 77 CD1 ILE A 16 17.482 -30.488 -42.412 1.00125.04 C ANISOU 77 CD1 ILE A 16 16387 14403 16721 715 -1612 154 C ATOM 78 N ALA A 17 19.860 -35.340 -43.829 1.00133.13 N ANISOU 78 N ALA A 17 17940 15607 17036 1047 -2047 386 N ATOM 79 CA ALA A 17 20.381 -36.630 -43.393 1.00136.45 C ANISOU 79 CA ALA A 17 18427 16111 17305 1022 -2126 395 C ATOM 80 C ALA A 17 21.747 -36.917 -44.008 1.00136.47 C ANISOU 80 C ALA A 17 18557 16179 17115 1185 -2074 499 C ATOM 81 O ALA A 17 22.643 -37.428 -43.336 1.00137.56 O ANISOU 81 O ALA A 17 18673 16440 17154 1127 -2021 506 O ATOM 82 CB ALA A 17 19.399 -37.742 -43.729 1.00138.35 C ANISOU 82 CB ALA A 17 18778 16266 17523 1061 -2364 373 C ATOM 83 N VAL A 18 21.902 -36.584 -45.285 1.00133.07 N ANISOU 83 N VAL A 18 18261 15672 16629 1402 -2086 583 N ATOM 84 CA VAL A 18 23.168 -36.787 -45.980 1.00128.65 C ANISOU 84 CA VAL A 18 17821 15171 15890 1585 -2017 701 C ATOM 85 C VAL A 18 24.285 -35.958 -45.353 1.00122.68 C ANISOU 85 C VAL A 18 16898 14531 15183 1476 -1779 724 C ATOM 86 O VAL A 18 25.352 -36.483 -45.025 1.00118.63 O ANISOU 86 O VAL A 18 16381 14146 14549 1482 -1728 763 O ATOM 87 CB VAL A 18 23.060 -36.424 -47.472 1.00128.38 C ANISOU 87 CB VAL A 18 17961 15022 15795 1852 -2047 794 C ATOM 88 CG1 VAL A 18 24.411 -36.588 -48.154 1.00135.34 C ANISOU 88 CG1 VAL A 18 18955 15976 16493 2048 -1940 931 C ATOM 89 CG2 VAL A 18 22.007 -37.282 -48.153 1.00124.62 C ANISOU 89 CG2 VAL A 18 17662 14427 15262 1977 -2314 760 C ATOM 90 N LEU A 19 24.034 -34.663 -45.193 1.00116.83 N ANISOU 90 N LEU A 19 16022 13743 14626 1380 -1642 698 N ATOM 91 CA LEU A 19 25.022 -33.755 -44.620 1.00111.68 C ANISOU 91 CA LEU A 19 15203 13174 14055 1260 -1426 708 C ATOM 92 C LEU A 19 25.363 -34.134 -43.184 1.00120.45 C ANISOU 92 C LEU A 19 16167 14420 15179 1045 -1412 610 C ATOM 93 O LEU A 19 26.534 -34.184 -42.807 1.00122.22 O ANISOU 93 O LEU A 19 16321 14768 15349 1015 -1316 638 O ATOM 94 CB LEU A 19 24.523 -32.309 -44.678 1.00 97.38 C ANISOU 94 CB LEU A 19 13295 11257 12447 1190 -1304 682 C ATOM 95 CG LEU A 19 24.659 -31.567 -46.010 1.00 87.80 C ANISOU 95 CG LEU A 19 12197 9932 11232 1395 -1222 805 C ATOM 96 CD1 LEU A 19 23.998 -32.332 -47.147 1.00 79.69 C ANISOU 96 CD1 LEU A 19 11394 8820 10065 1638 -1405 855 C ATOM 97 CD2 LEU A 19 24.085 -30.164 -45.896 1.00 85.62 C ANISOU 97 CD2 LEU A 19 11825 9545 11161 1304 -1108 761 C ATOM 98 N ALA A 20 24.332 -34.398 -42.388 1.00126.84 N ANISOU 98 N ALA A 20 16927 15207 16060 907 -1507 498 N ATOM 99 CA ALA A 20 24.513 -34.779 -40.992 1.00131.85 C ANISOU 99 CA ALA A 20 17444 15958 16695 719 -1497 402 C ATOM 100 C ALA A 20 25.474 -35.955 -40.867 1.00127.21 C ANISOU 100 C ALA A 20 16935 15495 15903 787 -1549 447 C ATOM 101 O ALA A 20 26.329 -35.979 -39.980 1.00122.07 O ANISOU 101 O ALA A 20 16181 14976 15223 691 -1474 412 O ATOM 102 CB ALA A 20 23.174 -35.116 -40.357 1.00137.98 C ANISOU 102 CB ALA A 20 18195 16680 17549 607 -1602 307 C ATOM 103 N ILE A 21 25.330 -36.928 -41.761 1.00128.31 N ANISOU 103 N ILE A 21 17266 15591 15895 965 -1686 520 N ATOM 104 CA ILE A 21 26.211 -38.087 -41.773 1.00131.69 C ANISOU 104 CA ILE A 21 17803 16125 16110 1067 -1744 573 C ATOM 105 C ILE A 21 27.606 -37.700 -42.247 1.00134.55 C ANISOU 105 C ILE A 21 18140 16583 16401 1179 -1606 671 C ATOM 106 O ILE A 21 28.569 -37.781 -41.488 1.00138.23 O ANISOU 106 O ILE A 21 18500 17196 16827 1109 -1529 655 O ATOM 107 CB ILE A 21 25.660 -39.209 -42.670 1.00131.84 C ANISOU 107 CB ILE A 21 18056 16049 15988 1242 -1941 621 C ATOM 108 CG1 ILE A 21 24.320 -39.714 -42.132 1.00127.89 C ANISOU 108 CG1 ILE A 21 17559 15461 15572 1111 -2082 528 C ATOM 109 CG2 ILE A 21 26.659 -40.352 -42.765 1.00132.24 C ANISOU 109 CG2 ILE A 21 18240 16203 15801 1378 -1990 684 C ATOM 110 CD1 ILE A 21 23.698 -40.810 -42.972 1.00126.56 C ANISOU 110 CD1 ILE A 21 17611 15179 15296 1257 -2300 558 C ATOM 111 N LEU A 22 27.705 -37.269 -43.501 1.00131.26 N ANISOU 111 N LEU A 22 17815 16084 15972 1358 -1571 776 N ATOM 112 CA LEU A 22 28.988 -36.902 -44.094 1.00125.89 C ANISOU 112 CA LEU A 22 17117 15484 15233 1485 -1422 897 C ATOM 113 C LEU A 22 29.803 -35.981 -43.190 1.00119.24 C ANISOU 113 C LEU A 22 16025 14747 14533 1293 -1245 856 C ATOM 114 O LEU A 22 30.995 -36.200 -42.983 1.00114.61 O ANISOU 114 O LEU A 22 15370 14307 13869 1318 -1171 902 O ATOM 115 CB LEU A 22 28.777 -36.238 -45.457 1.00121.81 C ANISOU 115 CB LEU A 22 16708 14835 14737 1671 -1372 1005 C ATOM 116 CG LEU A 22 28.067 -37.065 -46.531 1.00115.50 C ANISOU 116 CG LEU A 22 16174 13923 13787 1903 -1556 1051 C ATOM 117 CD1 LEU A 22 27.938 -36.267 -47.818 1.00112.78 C ANISOU 117 CD1 LEU A 22 15930 13458 13461 2097 -1483 1157 C ATOM 118 CD2 LEU A 22 28.806 -38.372 -46.782 1.00113.66 C ANISOU 118 CD2 LEU A 22 16100 13784 13301 2077 -1645 1115 C ATOM 119 N GLY A 23 29.152 -34.953 -42.656 1.00118.77 N ANISOU 119 N GLY A 23 15832 14613 14683 1108 -1188 764 N ATOM 120 CA GLY A 23 29.817 -33.975 -41.815 1.00116.68 C ANISOU 120 CA GLY A 23 15342 14416 14573 919 -1038 708 C ATOM 121 C GLY A 23 30.421 -34.563 -40.555 1.00117.89 C ANISOU 121 C GLY A 23 15390 14737 14666 792 -1070 615 C ATOM 122 O GLY A 23 31.639 -34.555 -40.382 1.00120.71 O ANISOU 122 O GLY A 23 15648 15226 14989 797 -992 652 O ATOM 123 N ASN A 24 29.569 -35.072 -39.671 1.00121.17 N ANISOU 123 N ASN A 24 15822 15148 15069 686 -1182 499 N ATOM 124 CA ASN A 24 30.025 -35.628 -38.401 1.00125.28 C ANISOU 124 CA ASN A 24 16264 15816 15521 574 -1214 403 C ATOM 125 C ASN A 24 30.939 -36.840 -38.563 1.00126.14 C ANISOU 125 C ASN A 24 16465 16060 15401 722 -1275 475 C ATOM 126 O ASN A 24 31.843 -37.054 -37.758 1.00127.36 O ANISOU 126 O ASN A 24 16521 16369 15499 673 -1255 432 O ATOM 127 CB ASN A 24 28.835 -35.974 -37.505 1.00127.40 C ANISOU 127 CB ASN A 24 16556 16038 15814 453 -1306 287 C ATOM 128 CG ASN A 24 28.144 -34.743 -36.955 1.00133.56 C ANISOU 128 CG ASN A 24 17203 16734 16809 286 -1229 187 C ATOM 129 OD1 ASN A 24 28.776 -33.889 -36.332 1.00130.31 O ANISOU 129 OD1 ASN A 24 16639 16376 16496 172 -1132 125 O ATOM 130 ND2 ASN A 24 26.838 -34.647 -37.178 1.00140.40 N ANISOU 130 ND2 ASN A 24 18126 17468 17753 274 -1280 168 N ATOM 131 N VAL A 25 30.698 -37.633 -39.602 1.00124.96 N ANISOU 131 N VAL A 25 16514 15850 15113 916 -1360 578 N ATOM 132 CA VAL A 25 31.566 -38.766 -39.907 1.00125.17 C ANISOU 132 CA VAL A 25 16658 15991 14909 1093 -1415 659 C ATOM 133 C VAL A 25 32.949 -38.263 -40.300 1.00126.72 C ANISOU 133 C VAL A 25 16737 16306 15105 1168 -1271 750 C ATOM 134 O VAL A 25 33.967 -38.841 -39.919 1.00127.60 O ANISOU 134 O VAL A 25 16811 16584 15089 1218 -1268 764 O ATOM 135 CB VAL A 25 30.995 -39.636 -41.042 1.00127.71 C ANISOU 135 CB VAL A 25 17237 16200 15087 1302 -1542 748 C ATOM 136 CG1 VAL A 25 32.053 -40.596 -41.563 1.00123.80 C ANISOU 136 CG1 VAL A 25 16867 15818 14354 1525 -1566 854 C ATOM 137 CG2 VAL A 25 29.767 -40.394 -40.561 1.00135.59 C ANISOU 137 CG2 VAL A 25 18343 17104 16071 1224 -1702 662 C ATOM 138 N LEU A 26 32.975 -37.175 -41.063 1.00124.53 N ANISOU 138 N LEU A 26 16398 15942 14977 1178 -1148 817 N ATOM 139 CA LEU A 26 34.227 -36.545 -41.460 1.00115.55 C ANISOU 139 CA LEU A 26 15122 14896 13887 1224 -985 916 C ATOM 140 C LEU A 26 34.979 -36.050 -40.231 1.00118.41 C ANISOU 140 C LEU A 26 15232 15394 14363 1016 -923 808 C ATOM 141 O LEU A 26 36.208 -36.089 -40.185 1.00125.64 O ANISOU 141 O LEU A 26 16026 16463 15249 1054 -849 862 O ATOM 142 CB LEU A 26 33.957 -35.384 -42.417 1.00108.42 C ANISOU 142 CB LEU A 26 14206 13843 13147 1247 -855 1000 C ATOM 143 CG LEU A 26 35.181 -34.685 -43.005 1.00110.79 C ANISOU 143 CG LEU A 26 14375 14206 13515 1304 -660 1135 C ATOM 144 CD1 LEU A 26 36.027 -35.668 -43.799 1.00122.38 C ANISOU 144 CD1 LEU A 26 15964 15785 14748 1572 -660 1284 C ATOM 145 CD2 LEU A 26 34.762 -33.512 -43.876 1.00105.34 C ANISOU 145 CD2 LEU A 26 13695 13338 12990 1316 -531 1212 C ATOM 146 N VAL A 27 34.231 -35.586 -39.235 1.00120.24 N ANISOU 146 N VAL A 27 15387 15573 14724 805 -960 654 N ATOM 147 CA VAL A 27 34.819 -35.101 -37.992 1.00126.63 C ANISOU 147 CA VAL A 27 15982 16496 15637 610 -929 526 C ATOM 148 C VAL A 27 35.469 -36.235 -37.204 1.00128.66 C ANISOU 148 C VAL A 27 16248 16941 15695 654 -1025 480 C ATOM 149 O VAL A 27 36.592 -36.102 -36.719 1.00125.02 O ANISOU 149 O VAL A 27 15621 16636 15246 618 -985 458 O ATOM 150 CB VAL A 27 33.770 -34.402 -37.106 1.00128.99 C ANISOU 150 CB VAL A 27 16233 16688 16091 406 -951 370 C ATOM 151 CG1 VAL A 27 34.365 -34.046 -35.751 1.00128.99 C ANISOU 151 CG1 VAL A 27 16046 16808 16155 231 -950 221 C ATOM 152 CG2 VAL A 27 33.229 -33.162 -37.801 1.00130.62 C ANISOU 152 CG2 VAL A 27 16412 16715 16503 359 -847 406 C ATOM 153 N CYS A 28 34.757 -37.351 -37.081 1.00135.29 N ANISOU 153 N CYS A 28 17284 17761 16360 732 -1156 466 N ATOM 154 CA CYS A 28 35.267 -38.507 -36.352 1.00140.71 C ANISOU 154 CA CYS A 28 18022 18605 16838 791 -1251 429 C ATOM 155 C CYS A 28 36.508 -39.084 -37.027 1.00140.42 C ANISOU 155 C CYS A 28 17995 18709 16647 992 -1225 557 C ATOM 156 O CYS A 28 37.442 -39.528 -36.359 1.00138.32 O ANISOU 156 O CYS A 28 17650 18625 16281 1013 -1245 523 O ATOM 157 CB CYS A 28 34.186 -39.582 -36.225 1.00144.65 C ANISOU 157 CB CYS A 28 18748 19019 17195 836 -1387 409 C ATOM 158 SG CYS A 28 32.728 -39.069 -35.290 1.00125.20 S ANISOU 158 SG CYS A 28 16258 16419 14891 613 -1412 263 S ATOM 159 N TRP A 29 36.508 -39.073 -38.355 1.00143.82 N ANISOU 159 N TRP A 29 18531 19062 17054 1156 -1179 706 N ATOM 160 CA TRP A 29 37.635 -39.574 -39.130 1.00149.69 C ANISOU 160 CA TRP A 29 19298 19929 17648 1376 -1133 850 C ATOM 161 C TRP A 29 38.843 -38.658 -38.964 1.00150.77 C ANISOU 161 C TRP A 29 19150 20198 17938 1300 -985 870 C ATOM 162 O TRP A 29 39.973 -39.120 -38.805 1.00152.69 O ANISOU 162 O TRP A 29 19309 20632 18076 1394 -970 907 O ATOM 163 CB TRP A 29 37.252 -39.679 -40.606 1.00154.66 C ANISOU 163 CB TRP A 29 20123 20423 18219 1579 -1112 1003 C ATOM 164 CG TRP A 29 38.282 -40.356 -41.457 1.00163.99 C ANISOU 164 CG TRP A 29 21383 21722 19205 1849 -1074 1160 C ATOM 165 CD1 TRP A 29 39.480 -40.868 -41.048 1.00170.36 C ANISOU 165 CD1 TRP A 29 22091 22744 19894 1923 -1055 1180 C ATOM 166 CD2 TRP A 29 38.203 -40.601 -42.866 1.00169.09 C ANISOU 166 CD2 TRP A 29 22230 22279 19736 2103 -1051 1319 C ATOM 167 NE1 TRP A 29 40.152 -41.413 -42.115 1.00174.50 N ANISOU 167 NE1 TRP A 29 22736 23324 20241 2206 -1010 1348 N ATOM 168 CE2 TRP A 29 39.389 -41.261 -43.243 1.00174.41 C ANISOU 168 CE2 TRP A 29 22919 23125 20222 2325 -1006 1436 C ATOM 169 CE3 TRP A 29 37.243 -40.324 -43.844 1.00169.34 C ANISOU 169 CE3 TRP A 29 22436 22107 19798 2179 -1069 1371 C ATOM 170 CZ2 TRP A 29 39.641 -41.649 -44.558 1.00176.45 C ANISOU 170 CZ2 TRP A 29 23372 23354 20315 2625 -969 1607 C ATOM 171 CZ3 TRP A 29 37.495 -40.709 -45.148 1.00173.54 C ANISOU 171 CZ3 TRP A 29 23165 22607 20165 2476 -1046 1533 C ATOM 172 CH2 TRP A 29 38.684 -41.364 -45.494 1.00177.06 C ANISOU 172 CH2 TRP A 29 23633 23223 20417 2698 -992 1651 C ATOM 173 N ALA A 30 38.593 -37.354 -39.001 1.00148.52 N ANISOU 173 N ALA A 30 18714 19807 17911 1128 -879 843 N ATOM 174 CA ALA A 30 39.651 -36.360 -38.859 1.00145.00 C ANISOU 174 CA ALA A 30 17987 19449 17658 1019 -738 858 C ATOM 175 C ALA A 30 40.344 -36.474 -37.504 1.00137.47 C ANISOU 175 C ALA A 30 16846 18673 16712 883 -802 707 C ATOM 176 O ALA A 30 41.548 -36.244 -37.390 1.00135.65 O ANISOU 176 O ALA A 30 16404 18598 16537 877 -735 736 O ATOM 177 CB ALA A 30 39.090 -34.960 -39.052 1.00148.81 C ANISOU 177 CB ALA A 30 18378 19750 18414 845 -632 837 C ATOM 178 N VAL A 31 39.576 -36.828 -36.479 1.00136.90 N ANISOU 178 N VAL A 31 16850 18580 16586 781 -933 548 N ATOM 179 CA VAL A 31 40.121 -36.997 -35.137 1.00139.81 C ANISOU 179 CA VAL A 31 17081 19109 16929 675 -1011 392 C ATOM 180 C VAL A 31 40.926 -38.287 -35.033 1.00141.84 C ANISOU 180 C VAL A 31 17408 19564 16921 872 -1088 437 C ATOM 181 O VAL A 31 41.974 -38.326 -34.391 1.00146.96 O ANISOU 181 O VAL A 31 17877 20401 17560 858 -1103 383 O ATOM 182 CB VAL A 31 39.009 -37.014 -34.071 1.00145.59 C ANISOU 182 CB VAL A 31 17897 19754 17664 530 -1111 222 C ATOM 183 CG1 VAL A 31 39.583 -37.371 -32.707 1.00145.09 C ANISOU 183 CG1 VAL A 31 17743 19867 17517 474 -1204 70 C ATOM 184 CG2 VAL A 31 38.298 -35.669 -34.023 1.00151.24 C ANISOU 184 CG2 VAL A 31 18525 20295 18645 334 -1037 158 C ATOM 185 N TRP A 32 40.427 -39.340 -35.671 1.00139.95 N ANISOU 185 N TRP A 32 17432 19276 16467 1062 -1146 531 N ATOM 186 CA TRP A 32 41.080 -40.642 -35.622 1.00143.66 C ANISOU 186 CA TRP A 32 18016 19907 16660 1272 -1226 578 C ATOM 187 C TRP A 32 42.339 -40.665 -36.482 1.00148.45 C ANISOU 187 C TRP A 32 18514 20655 17234 1445 -1125 733 C ATOM 188 O TRP A 32 43.169 -41.565 -36.359 1.00154.03 O ANISOU 188 O TRP A 32 19245 21541 17740 1616 -1170 767 O ATOM 189 CB TRP A 32 40.113 -41.741 -36.066 1.00143.57 C ANISOU 189 CB TRP A 32 18335 19772 16443 1413 -1328 628 C ATOM 190 CG TRP A 32 40.671 -43.123 -35.921 1.00142.65 C ANISOU 190 CG TRP A 32 18374 19794 16031 1623 -1423 662 C ATOM 191 CD1 TRP A 32 41.032 -43.743 -34.760 1.00138.49 C ANISOU 191 CD1 TRP A 32 17837 19410 15374 1609 -1510 553 C ATOM 192 CD2 TRP A 32 40.917 -44.063 -36.973 1.00144.41 C ANISOU 192 CD2 TRP A 32 18811 20020 16038 1895 -1445 813 C ATOM 193 NE1 TRP A 32 41.495 -45.009 -35.024 1.00138.59 N ANISOU 193 NE1 TRP A 32 18039 19513 15107 1851 -1580 630 N ATOM 194 CE2 TRP A 32 41.434 -45.231 -36.375 1.00145.37 C ANISOU 194 CE2 TRP A 32 19040 20286 15908 2029 -1545 788 C ATOM 195 CE3 TRP A 32 40.755 -44.032 -38.361 1.00146.11 C ANISOU 195 CE3 TRP A 32 19154 20127 16235 2055 -1393 966 C ATOM 196 CZ2 TRP A 32 41.789 -46.355 -37.117 1.00152.51 C ANISOU 196 CZ2 TRP A 32 20172 21224 16549 2311 -1594 909 C ATOM 197 CZ3 TRP A 32 41.106 -45.150 -39.096 1.00151.43 C ANISOU 197 CZ3 TRP A 32 20056 20837 16643 2340 -1446 1082 C ATOM 198 CH2 TRP A 32 41.618 -46.296 -38.472 1.00155.00 C ANISOU 198 CH2 TRP A 32 20610 21429 16853 2462 -1546 1052 C ATOM 199 N LEU A 33 42.474 -39.668 -37.350 1.00149.25 N ANISOU 199 N LEU A 33 18499 20675 17534 1411 -978 834 N ATOM 200 CA LEU A 33 43.643 -39.560 -38.216 1.00153.10 C ANISOU 200 CA LEU A 33 18863 21287 18023 1566 -846 1001 C ATOM 201 C LEU A 33 44.706 -38.652 -37.601 1.00152.42 C ANISOU 201 C LEU A 33 18409 21343 18160 1396 -765 945 C ATOM 202 O LEU A 33 45.852 -39.061 -37.410 1.00155.59 O ANISOU 202 O LEU A 33 18668 21965 18486 1494 -761 974 O ATOM 203 CB LEU A 33 43.236 -39.042 -39.597 1.00157.75 C ANISOU 203 CB LEU A 33 19550 21703 18685 1655 -716 1167 C ATOM 204 CG LEU A 33 44.368 -38.750 -40.585 1.00169.42 C ANISOU 204 CG LEU A 33 20895 23280 20197 1811 -534 1365 C ATOM 205 CD1 LEU A 33 45.323 -39.931 -40.693 1.00175.12 C ANISOU 205 CD1 LEU A 33 21665 24222 20652 2069 -572 1444 C ATOM 206 CD2 LEU A 33 43.804 -38.381 -41.950 1.00169.73 C ANISOU 206 CD2 LEU A 33 21105 23129 20255 1939 -423 1527 C ATOM 207 N ASN A 34 44.318 -37.419 -37.291 1.00145.67 N ANISOU 207 N ASN A 34 17403 20360 17585 1143 -710 860 N ATOM 208 CA ASN A 34 45.232 -36.454 -36.694 1.00137.77 C ANISOU 208 CA ASN A 34 16057 19457 16832 948 -649 788 C ATOM 209 C ASN A 34 45.246 -36.564 -35.172 1.00137.47 C ANISOU 209 C ASN A 34 15934 19513 16784 794 -810 555 C ATOM 210 O ASN A 34 44.245 -36.288 -34.510 1.00137.37 O ANISOU 210 O ASN A 34 16016 19367 16814 648 -886 412 O ATOM 211 CB ASN A 34 44.862 -35.034 -37.125 1.00133.20 C ANISOU 211 CB ASN A 34 15369 18679 16562 758 -509 812 C ATOM 212 CG ASN A 34 45.915 -34.013 -36.740 1.00133.54 C ANISOU 212 CG ASN A 34 15052 18803 16886 567 -426 775 C ATOM 213 OD1 ASN A 34 46.807 -34.295 -35.941 1.00136.80 O ANISOU 213 OD1 ASN A 34 15280 19420 17280 541 -506 685 O ATOM 214 ND2 ASN A 34 45.817 -32.818 -37.311 1.00133.85 N ANISOU 214 ND2 ASN A 34 14989 18677 17190 435 -271 843 N ATOM 215 N SER A 35 46.387 -36.970 -34.624 1.00141.14 N ANISOU 215 N SER A 35 16223 20216 17187 844 -860 518 N ATOM 216 CA SER A 35 46.523 -37.163 -33.184 1.00141.62 C ANISOU 216 CA SER A 35 16214 20392 17203 741 -1023 300 C ATOM 217 C SER A 35 46.544 -35.837 -32.427 1.00135.39 C ANISOU 217 C SER A 35 15189 19534 16720 449 -1022 137 C ATOM 218 O SER A 35 46.411 -35.810 -31.204 1.00130.48 O ANISOU 218 O SER A 35 14542 18954 16079 342 -1158 -66 O ATOM 219 CB SER A 35 47.785 -37.970 -32.869 1.00150.41 C ANISOU 219 CB SER A 35 17203 21789 18157 901 -1084 309 C ATOM 220 OG SER A 35 48.945 -37.305 -33.341 1.00159.82 O ANISOU 220 OG SER A 35 18079 23089 19555 870 -964 401 O ATOM 221 N ASN A 36 46.711 -34.740 -33.158 1.00135.99 N ANISOU 221 N ASN A 36 15107 19495 17069 330 -869 227 N ATOM 222 CA ASN A 36 46.716 -33.412 -32.556 1.00140.14 C ANISOU 222 CA ASN A 36 15423 19920 17905 50 -860 84 C ATOM 223 C ASN A 36 45.313 -32.962 -32.167 1.00144.76 C ANISOU 223 C ASN A 36 16201 20277 18523 -77 -898 -32 C ATOM 224 O ASN A 36 45.137 -31.904 -31.565 1.00153.10 O ANISOU 224 O ASN A 36 17139 21230 19804 -298 -910 -174 O ATOM 225 CB ASN A 36 47.349 -32.394 -33.506 1.00143.94 C ANISOU 225 CB ASN A 36 15685 20334 18671 -34 -667 235 C ATOM 226 CG ASN A 36 48.825 -32.657 -33.745 1.00147.21 C ANISOU 226 CG ASN A 36 15836 20985 19111 51 -620 333 C ATOM 227 OD1 ASN A 36 49.573 -32.950 -32.813 1.00148.31 O ANISOU 227 OD1 ASN A 36 15810 21320 19218 28 -756 196 O ATOM 228 ND2 ASN A 36 49.252 -32.546 -34.999 1.00145.98 N ANISOU 228 ND2 ASN A 36 15637 20816 19011 162 -426 575 N ATOM 229 N LEU A 37 44.319 -33.772 -32.519 1.00137.90 N ANISOU 229 N LEU A 37 15630 19331 17435 68 -920 28 N ATOM 230 CA LEU A 37 42.928 -33.472 -32.205 1.00123.12 C ANISOU 230 CA LEU A 37 13944 17258 15579 -26 -952 -64 C ATOM 231 C LEU A 37 42.365 -34.483 -31.213 1.00121.35 C ANISOU 231 C LEU A 37 13901 17102 15103 36 -1109 -190 C ATOM 232 O LEU A 37 41.188 -34.428 -30.861 1.00125.21 O ANISOU 232 O LEU A 37 14552 17450 15573 -21 -1142 -263 O ATOM 233 CB LEU A 37 42.081 -33.470 -33.481 1.00108.93 C ANISOU 233 CB LEU A 37 12339 15279 13772 71 -844 111 C ATOM 234 CG LEU A 37 42.388 -32.385 -34.515 1.00 97.93 C ANISOU 234 CG LEU A 37 10819 13766 12623 15 -666 248 C ATOM 235 CD1 LEU A 37 41.695 -32.683 -35.836 1.00 84.48 C ANISOU 235 CD1 LEU A 37 9339 11929 10830 189 -582 436 C ATOM 236 CD2 LEU A 37 41.989 -31.014 -33.989 1.00 93.59 C ANISOU 236 CD2 LEU A 37 10152 13055 12350 -238 -637 114 C ATOM 237 N GLN A 38 43.210 -35.406 -30.765 1.00121.96 N ANISOU 237 N GLN A 38 13951 17398 14991 160 -1197 -208 N ATOM 238 CA GLN A 38 42.773 -36.472 -29.869 1.00121.90 C ANISOU 238 CA GLN A 38 14132 17462 14721 247 -1333 -304 C ATOM 239 C GLN A 38 42.934 -36.107 -28.396 1.00124.32 C ANISOU 239 C GLN A 38 14334 17842 15060 113 -1443 -534 C ATOM 240 O GLN A 38 43.215 -36.967 -27.561 1.00123.59 O ANISOU 240 O GLN A 38 14305 17900 14752 209 -1557 -615 O ATOM 241 CB GLN A 38 43.525 -37.769 -30.174 1.00120.73 C ANISOU 241 CB GLN A 38 14060 17501 14310 488 -1376 -197 C ATOM 242 CG GLN A 38 43.279 -38.307 -31.573 1.00121.93 C ANISOU 242 CG GLN A 38 14376 17577 14373 660 -1292 20 C ATOM 243 CD GLN A 38 43.970 -39.631 -31.818 1.00130.67 C ANISOU 243 CD GLN A 38 15592 18860 15197 915 -1344 115 C ATOM 244 OE1 GLN A 38 44.674 -40.145 -30.950 1.00140.09 O ANISOU 244 OE1 GLN A 38 16725 20241 16263 964 -1438 24 O ATOM 245 NE2 GLN A 38 43.772 -40.192 -33.005 1.00130.18 N ANISOU 245 NE2 GLN A 38 15704 18734 15025 1092 -1291 295 N ATOM 246 N ASN A 39 42.757 -34.828 -28.082 1.00126.05 N ANISOU 246 N ASN A 39 14407 17947 15537 -96 -1412 -641 N ATOM 247 CA ASN A 39 42.801 -34.374 -26.698 1.00132.12 C ANISOU 247 CA ASN A 39 15101 18756 16343 -222 -1522 -873 C ATOM 248 C ASN A 39 41.548 -34.792 -25.931 1.00139.81 C ANISOU 248 C ASN A 39 16320 19640 17161 -212 -1573 -962 C ATOM 249 O ASN A 39 40.523 -35.115 -26.533 1.00142.42 O ANISOU 249 O ASN A 39 16839 19833 17442 -169 -1510 -854 O ATOM 250 CB ASN A 39 42.997 -32.856 -26.632 1.00132.51 C ANISOU 250 CB ASN A 39 14934 18691 16721 -446 -1476 -960 C ATOM 251 CG ASN A 39 42.046 -32.104 -27.543 1.00131.04 C ANISOU 251 CG ASN A 39 14822 18261 16706 -526 -1336 -856 C ATOM 252 OD1 ASN A 39 40.937 -32.561 -27.815 1.00135.36 O ANISOU 252 OD1 ASN A 39 15595 18701 17136 -457 -1310 -796 O ATOM 253 ND2 ASN A 39 42.477 -30.940 -28.016 1.00128.73 N ANISOU 253 ND2 ASN A 39 14337 17876 16698 -672 -1248 -835 N ATOM 254 N VAL A 40 41.637 -34.790 -24.605 1.00143.41 N ANISOU 254 N VAL A 40 16770 20177 17541 -244 -1687 -1156 N ATOM 255 CA VAL A 40 40.522 -35.208 -23.760 1.00143.62 C ANISOU 255 CA VAL A 40 17020 20138 17410 -223 -1722 -1238 C ATOM 256 C VAL A 40 39.243 -34.446 -24.094 1.00136.46 C ANISOU 256 C VAL A 40 16191 18994 16663 -342 -1624 -1220 C ATOM 257 O VAL A 40 38.142 -34.990 -24.010 1.00121.43 O ANISOU 257 O VAL A 40 14489 17004 14644 -297 -1601 -1182 O ATOM 258 CB VAL A 40 40.844 -35.018 -22.266 1.00145.06 C ANISOU 258 CB VAL A 40 17165 20425 17526 -253 -1847 -1467 C ATOM 259 CG1 VAL A 40 39.686 -35.507 -21.409 1.00140.32 C ANISOU 259 CG1 VAL A 40 16806 19761 16747 -210 -1857 -1528 C ATOM 260 CG2 VAL A 40 42.128 -35.749 -21.903 1.00147.59 C ANISOU 260 CG2 VAL A 40 17398 20991 17687 -124 -1959 -1498 C ATOM 261 N THR A 41 39.400 -33.183 -24.478 1.00143.24 N ANISOU 261 N THR A 41 16884 19745 17796 -494 -1565 -1243 N ATOM 262 CA THR A 41 38.264 -32.328 -24.800 1.00140.93 C ANISOU 262 CA THR A 41 16648 19227 17670 -603 -1473 -1234 C ATOM 263 C THR A 41 37.419 -32.901 -25.932 1.00129.89 C ANISOU 263 C THR A 41 15406 17723 16221 -514 -1388 -1038 C ATOM 264 O THR A 41 36.192 -32.940 -25.844 1.00130.05 O ANISOU 264 O THR A 41 15573 17617 16224 -523 -1359 -1037 O ATOM 265 CB THR A 41 38.724 -30.914 -25.202 1.00150.73 C ANISOU 265 CB THR A 41 17687 20365 19216 -766 -1414 -1262 C ATOM 266 OG1 THR A 41 39.519 -30.348 -24.152 1.00158.92 O ANISOU 266 OG1 THR A 41 18573 21488 20320 -860 -1517 -1459 O ATOM 267 CG2 THR A 41 37.524 -30.016 -25.471 1.00148.23 C ANISOU 267 CG2 THR A 41 17448 19816 19057 -862 -1324 -1263 C ATOM 268 N ASN A 42 38.083 -33.344 -26.995 1.00125.30 N ANISOU 268 N ASN A 42 14792 17198 15619 -419 -1351 -874 N ATOM 269 CA ASN A 42 37.386 -33.821 -28.185 1.00129.40 C ANISOU 269 CA ASN A 42 15458 17610 16097 -322 -1284 -690 C ATOM 270 C ASN A 42 36.751 -35.200 -28.032 1.00132.56 C ANISOU 270 C ASN A 42 16082 18046 16239 -183 -1347 -644 C ATOM 271 O ASN A 42 36.083 -35.684 -28.946 1.00130.34 O ANISOU 271 O ASN A 42 15943 17667 15913 -100 -1319 -509 O ATOM 272 CB ASN A 42 38.310 -33.787 -29.404 1.00135.29 C ANISOU 272 CB ASN A 42 16110 18395 16901 -248 -1214 -525 C ATOM 273 CG ASN A 42 38.569 -32.376 -29.896 1.00143.08 C ANISOU 273 CG ASN A 42 16922 19266 18177 -390 -1109 -516 C ATOM 274 OD1 ASN A 42 38.052 -31.406 -29.340 1.00144.40 O ANISOU 274 OD1 ASN A 42 17047 19316 18503 -544 -1099 -641 O ATOM 275 ND2 ASN A 42 39.369 -32.255 -30.947 1.00148.26 N ANISOU 275 ND2 ASN A 42 17486 19948 18900 -331 -1021 -362 N ATOM 276 N TYR A 43 36.955 -35.830 -26.880 1.00137.76 N ANISOU 276 N TYR A 43 16780 18833 16728 -154 -1436 -756 N ATOM 277 CA TYR A 43 36.283 -37.090 -26.587 1.00138.39 C ANISOU 277 CA TYR A 43 17080 18926 16576 -43 -1487 -721 C ATOM 278 C TYR A 43 34.777 -36.865 -26.530 1.00132.46 C ANISOU 278 C TYR A 43 16444 17989 15895 -118 -1445 -728 C ATOM 279 O TYR A 43 33.992 -37.713 -26.956 1.00129.86 O ANISOU 279 O TYR A 43 16284 17588 15468 -46 -1453 -630 O ATOM 280 CB TYR A 43 36.784 -37.683 -25.269 1.00142.43 C ANISOU 280 CB TYR A 43 17614 19604 16898 2 -1577 -849 C ATOM 281 CG TYR A 43 38.069 -38.468 -25.400 1.00146.61 C ANISOU 281 CG TYR A 43 18109 20330 17266 146 -1639 -803 C ATOM 282 CD1 TYR A 43 38.055 -39.856 -25.466 1.00148.55 C ANISOU 282 CD1 TYR A 43 18547 20638 17255 313 -1688 -718 C ATOM 283 CD2 TYR A 43 39.295 -37.823 -25.462 1.00150.49 C ANISOU 283 CD2 TYR A 43 18370 20941 17867 115 -1649 -844 C ATOM 284 CE1 TYR A 43 39.226 -40.578 -25.587 1.00152.82 C ANISOU 284 CE1 TYR A 43 19064 21364 17636 465 -1743 -675 C ATOM 285 CE2 TYR A 43 40.474 -38.537 -25.584 1.00154.99 C ANISOU 285 CE2 TYR A 43 18890 21706 18294 258 -1702 -799 C ATOM 286 CZ TYR A 43 40.434 -39.914 -25.646 1.00157.20 C ANISOU 286 CZ TYR A 43 19374 22052 18301 441 -1749 -715 C ATOM 287 OH TYR A 43 41.605 -40.628 -25.767 1.00162.08 O ANISOU 287 OH TYR A 43 19949 22869 18764 603 -1800 -670 O ATOM 288 N PHE A 44 34.382 -35.708 -26.008 1.00125.28 N ANISOU 288 N PHE A 44 15437 16999 15164 -261 -1405 -846 N ATOM 289 CA PHE A 44 32.976 -35.339 -25.936 1.00117.65 C ANISOU 289 CA PHE A 44 14548 15865 14288 -332 -1354 -859 C ATOM 290 C PHE A 44 32.455 -34.920 -27.305 1.00118.69 C ANISOU 290 C PHE A 44 14683 15842 14571 -336 -1290 -727 C ATOM 291 O PHE A 44 31.306 -35.191 -27.653 1.00125.61 O ANISOU 291 O PHE A 44 15671 16599 15456 -325 -1275 -668 O ATOM 292 CB PHE A 44 32.770 -34.211 -24.924 1.00119.06 C ANISOU 292 CB PHE A 44 14633 16011 14593 -461 -1333 -1033 C ATOM 293 CG PHE A 44 33.205 -34.562 -23.532 1.00128.46 C ANISOU 293 CG PHE A 44 15839 17344 15625 -440 -1403 -1176 C ATOM 294 CD1 PHE A 44 34.438 -34.154 -23.054 1.00135.78 C ANISOU 294 CD1 PHE A 44 16627 18397 16564 -462 -1464 -1284 C ATOM 295 CD2 PHE A 44 32.384 -35.309 -22.704 1.00134.67 C ANISOU 295 CD2 PHE A 44 16778 18138 16251 -393 -1408 -1200 C ATOM 296 CE1 PHE A 44 34.843 -34.479 -21.773 1.00140.80 C ANISOU 296 CE1 PHE A 44 17289 19168 17041 -423 -1545 -1425 C ATOM 297 CE2 PHE A 44 32.782 -35.639 -21.423 1.00139.05 C ANISOU 297 CE2 PHE A 44 17370 18823 16640 -351 -1466 -1326 C ATOM 298 CZ PHE A 44 34.013 -35.223 -20.957 1.00141.43 C ANISOU 298 CZ PHE A 44 17544 19253 16940 -357 -1543 -1445 C ATOM 299 N VAL A 45 33.307 -34.256 -28.080 1.00116.11 N ANISOU 299 N VAL A 45 14231 15518 14367 -348 -1252 -678 N ATOM 300 CA VAL A 45 32.944 -33.848 -29.431 1.00113.92 C ANISOU 300 CA VAL A 45 13969 15101 14215 -325 -1184 -544 C ATOM 301 C VAL A 45 32.600 -35.069 -30.277 1.00116.51 C ANISOU 301 C VAL A 45 14468 15420 14380 -171 -1227 -397 C ATOM 302 O VAL A 45 31.736 -35.010 -31.150 1.00115.01 O ANISOU 302 O VAL A 45 14362 15087 14247 -139 -1207 -311 O ATOM 303 CB VAL A 45 34.075 -33.053 -30.110 1.00108.21 C ANISOU 303 CB VAL A 45 13086 14400 13629 -345 -1121 -494 C ATOM 304 CG1 VAL A 45 33.688 -32.690 -31.537 1.00 95.59 C ANISOU 304 CG1 VAL A 45 11533 12655 12132 -290 -1042 -341 C ATOM 305 CG2 VAL A 45 34.397 -31.804 -29.307 1.00111.63 C ANISOU 305 CG2 VAL A 45 13353 14815 14247 -513 -1093 -647 C ATOM 306 N VAL A 46 33.283 -36.177 -30.008 1.00121.42 N ANISOU 306 N VAL A 46 15149 16191 14795 -68 -1296 -375 N ATOM 307 CA VAL A 46 33.000 -37.431 -30.694 1.00125.34 C ANISOU 307 CA VAL A 46 15831 16677 15115 83 -1355 -250 C ATOM 308 C VAL A 46 31.610 -37.928 -30.321 1.00132.20 C ANISOU 308 C VAL A 46 16839 17435 15955 50 -1393 -274 C ATOM 309 O VAL A 46 30.870 -38.431 -31.167 1.00136.11 O ANISOU 309 O VAL A 46 17465 17819 16432 117 -1424 -177 O ATOM 310 CB VAL A 46 34.036 -38.516 -30.350 1.00126.67 C ANISOU 310 CB VAL A 46 16042 17030 15056 206 -1422 -234 C ATOM 311 CG1 VAL A 46 33.649 -39.840 -30.991 1.00126.97 C ANISOU 311 CG1 VAL A 46 16304 17033 14906 359 -1493 -117 C ATOM 312 CG2 VAL A 46 35.422 -38.087 -30.798 1.00127.52 C ANISOU 312 CG2 VAL A 46 15993 17259 15201 249 -1381 -194 C ATOM 313 N SER A 47 31.261 -37.784 -29.046 1.00135.50 N ANISOU 313 N SER A 47 17228 17885 16372 -49 -1391 -403 N ATOM 314 CA SER A 47 29.933 -38.146 -28.568 1.00137.61 C ANISOU 314 CA SER A 47 17594 18054 16636 -97 -1400 -425 C ATOM 315 C SER A 47 28.877 -37.284 -29.250 1.00129.94 C ANISOU 315 C SER A 47 16590 16909 15873 -164 -1350 -402 C ATOM 316 O SER A 47 27.794 -37.760 -29.591 1.00122.04 O ANISOU 316 O SER A 47 15685 15798 14884 -154 -1376 -349 O ATOM 317 CB SER A 47 29.845 -37.983 -27.049 1.00143.10 C ANISOU 317 CB SER A 47 18254 18825 17294 -176 -1382 -568 C ATOM 318 OG SER A 47 28.537 -38.262 -26.579 1.00143.66 O ANISOU 318 OG SER A 47 18403 18801 17380 -223 -1363 -576 O ATOM 319 N LEU A 48 29.203 -36.010 -29.445 1.00130.95 N ANISOU 319 N LEU A 48 16578 17007 16170 -231 -1281 -445 N ATOM 320 CA LEU A 48 28.323 -35.087 -30.149 1.00131.87 C ANISOU 320 CA LEU A 48 16664 16961 16481 -277 -1228 -422 C ATOM 321 C LEU A 48 28.143 -35.527 -31.596 1.00131.69 C ANISOU 321 C LEU A 48 16738 16855 16443 -158 -1263 -273 C ATOM 322 O LEU A 48 27.032 -35.522 -32.124 1.00137.22 O ANISOU 322 O LEU A 48 17498 17424 17214 -150 -1279 -235 O ATOM 323 CB LEU A 48 28.893 -33.667 -30.106 1.00134.26 C ANISOU 323 CB LEU A 48 16813 17245 16955 -364 -1147 -489 C ATOM 324 CG LEU A 48 28.163 -32.619 -30.951 1.00137.24 C ANISOU 324 CG LEU A 48 17165 17450 17529 -391 -1081 -453 C ATOM 325 CD1 LEU A 48 26.719 -32.466 -30.494 1.00137.40 C ANISOU 325 CD1 LEU A 48 17219 17373 17613 -442 -1076 -508 C ATOM 326 CD2 LEU A 48 28.891 -31.284 -30.899 1.00139.00 C ANISOU 326 CD2 LEU A 48 17248 17651 17915 -479 -1000 -511 C ATOM 327 N ALA A 49 29.246 -35.908 -32.231 1.00127.56 N ANISOU 327 N ALA A 49 16230 16412 15823 -55 -1278 -191 N ATOM 328 CA ALA A 49 29.216 -36.357 -33.617 1.00125.91 C ANISOU 328 CA ALA A 49 16134 16136 15568 90 -1312 -48 C ATOM 329 C ALA A 49 28.370 -37.616 -33.769 1.00123.45 C ANISOU 329 C ALA A 49 16000 15777 15129 161 -1425 -5 C ATOM 330 O ALA A 49 27.410 -37.638 -34.537 1.00128.45 O ANISOU 330 O ALA A 49 16709 16271 15824 195 -1464 43 O ATOM 331 CB ALA A 49 30.627 -36.597 -34.128 1.00130.95 C ANISOU 331 CB ALA A 49 16753 16895 16106 201 -1294 32 C ATOM 332 N ALA A 50 28.730 -38.662 -33.031 1.00118.82 N ANISOU 332 N ALA A 50 15478 15300 14368 183 -1483 -25 N ATOM 333 CA ALA A 50 28.003 -39.927 -33.081 1.00118.60 C ANISOU 333 CA ALA A 50 15625 15221 14218 236 -1590 15 C ATOM 334 C ALA A 50 26.511 -39.713 -32.856 1.00122.29 C ANISOU 334 C ALA A 50 16086 15550 14829 128 -1597 -24 C ATOM 335 O ALA A 50 25.676 -40.288 -33.555 1.00121.61 O ANISOU 335 O ALA A 50 16111 15345 14749 174 -1683 35 O ATOM 336 CB ALA A 50 28.560 -40.899 -32.055 1.00120.02 C ANISOU 336 CB ALA A 50 15859 15535 14208 248 -1623 -21 C ATOM 337 N ALA A 51 26.183 -38.885 -31.870 1.00124.95 N ANISOU 337 N ALA A 51 16289 15903 15282 -10 -1511 -128 N ATOM 338 CA ALA A 51 24.794 -38.567 -31.570 1.00124.91 C ANISOU 338 CA ALA A 51 16251 15786 15423 -109 -1494 -167 C ATOM 339 C ALA A 51 24.132 -37.886 -32.761 1.00130.49 C ANISOU 339 C ALA A 51 16943 16351 16285 -78 -1505 -118 C ATOM 340 O ALA A 51 23.017 -38.233 -33.149 1.00139.10 O ANISOU 340 O ALA A 51 18082 17329 17439 -80 -1569 -89 O ATOM 341 CB ALA A 51 24.707 -37.681 -30.336 1.00120.94 C ANISOU 341 CB ALA A 51 15615 15336 15002 -233 -1390 -289 C ATOM 342 N ASP A 52 24.830 -36.914 -33.339 1.00128.38 N ANISOU 342 N ASP A 52 16609 16087 16084 -48 -1442 -108 N ATOM 343 CA ASP A 52 24.300 -36.160 -34.469 1.00128.50 C ANISOU 343 CA ASP A 52 16621 15969 16235 0 -1436 -59 C ATOM 344 C ASP A 52 24.404 -36.933 -35.782 1.00116.02 C ANISOU 344 C ASP A 52 15195 14334 14554 167 -1541 60 C ATOM 345 O ASP A 52 23.907 -36.486 -36.815 1.00110.56 O ANISOU 345 O ASP A 52 14537 13526 13945 241 -1560 109 O ATOM 346 CB ASP A 52 24.997 -34.802 -34.584 1.00141.21 C ANISOU 346 CB ASP A 52 18112 17584 17958 -32 -1314 -84 C ATOM 347 CG ASP A 52 24.585 -33.840 -33.483 1.00149.08 C ANISOU 347 CG ASP A 52 18977 18578 19089 -183 -1227 -209 C ATOM 348 OD1 ASP A 52 23.748 -34.223 -32.638 1.00151.89 O ANISOU 348 OD1 ASP A 52 19331 18939 19443 -251 -1247 -269 O ATOM 349 OD2 ASP A 52 25.096 -32.700 -33.464 1.00149.26 O ANISOU 349 OD2 ASP A 52 18904 18587 19219 -231 -1134 -245 O ATOM 350 N ILE A 53 25.053 -38.092 -35.736 1.00114.25 N ANISOU 350 N ILE A 53 15078 14192 14141 242 -1612 103 N ATOM 351 CA ILE A 53 25.123 -38.972 -36.897 1.00114.50 C ANISOU 351 CA ILE A 53 15286 14170 14048 414 -1729 207 C ATOM 352 C ILE A 53 23.885 -39.854 -36.950 1.00113.23 C ANISOU 352 C ILE A 53 15226 13900 13895 397 -1867 203 C ATOM 353 O ILE A 53 23.257 -39.998 -37.998 1.00114.45 O ANISOU 353 O ILE A 53 15476 13932 14078 492 -1967 251 O ATOM 354 CB ILE A 53 26.371 -39.869 -36.866 1.00114.69 C ANISOU 354 CB ILE A 53 15397 14325 13855 521 -1752 258 C ATOM 355 CG1 ILE A 53 27.632 -39.037 -37.090 1.00107.84 C ANISOU 355 CG1 ILE A 53 14423 13557 12994 561 -1627 287 C ATOM 356 CG2 ILE A 53 26.273 -40.949 -37.931 1.00117.04 C ANISOU 356 CG2 ILE A 53 15911 14553 14005 702 -1895 352 C ATOM 357 CD1 ILE A 53 28.907 -39.840 -37.043 1.00104.69 C ANISOU 357 CD1 ILE A 53 14078 13307 12392 675 -1639 338 C ATOM 358 N LEU A 54 23.540 -40.441 -35.809 1.00110.66 N ANISOU 358 N LEU A 54 14879 13617 13548 278 -1872 146 N ATOM 359 CA LEU A 54 22.343 -41.264 -35.705 1.00106.05 C ANISOU 359 CA LEU A 54 14362 12931 13003 227 -1982 143 C ATOM 360 C LEU A 54 21.098 -40.451 -36.050 1.00 97.11 C ANISOU 360 C LEU A 54 13131 11675 12091 166 -1983 115 C ATOM 361 O LEU A 54 20.024 -41.010 -36.271 1.00 91.21 O ANISOU 361 O LEU A 54 12421 10820 11413 140 -2094 122 O ATOM 362 CB LEU A 54 22.219 -41.864 -34.303 1.00107.73 C ANISOU 362 CB LEU A 54 14548 13217 13169 102 -1940 93 C ATOM 363 CG LEU A 54 23.346 -42.811 -33.886 1.00107.35 C ANISOU 363 CG LEU A 54 14613 13287 12888 172 -1956 118 C ATOM 364 CD1 LEU A 54 23.155 -43.289 -32.453 1.00105.53 C ANISOU 364 CD1 LEU A 54 14360 13122 12613 57 -1900 66 C ATOM 365 CD2 LEU A 54 23.436 -43.989 -34.843 1.00106.53 C ANISOU 365 CD2 LEU A 54 14721 13110 12645 313 -2116 202 C ATOM 366 N VAL A 55 21.248 -39.131 -36.095 1.00 96.99 N ANISOU 366 N VAL A 55 12988 11673 12191 144 -1865 82 N ATOM 367 CA VAL A 55 20.154 -38.252 -36.492 1.00104.02 C ANISOU 367 CA VAL A 55 13792 12452 13279 114 -1858 57 C ATOM 368 C VAL A 55 19.800 -38.490 -37.954 1.00112.36 C ANISOU 368 C VAL A 55 14974 13388 14331 269 -2000 125 C ATOM 369 O VAL A 55 18.681 -38.886 -38.276 1.00124.12 O ANISOU 369 O VAL A 55 16482 14774 15904 262 -2121 121 O ATOM 370 CB VAL A 55 20.511 -36.769 -36.296 1.00108.37 C ANISOU 370 CB VAL A 55 14208 13029 13938 75 -1701 12 C ATOM 371 CG1 VAL A 55 19.418 -35.879 -36.870 1.00112.95 C ANISOU 371 CG1 VAL A 55 14729 13486 14702 84 -1703 -3 C ATOM 372 CG2 VAL A 55 20.732 -36.467 -34.822 1.00105.44 C ANISOU 372 CG2 VAL A 55 13719 12764 13580 -71 -1580 -76 C ATOM 373 N GLY A 56 20.763 -38.250 -38.837 1.00109.43 N ANISOU 373 N GLY A 56 14687 13030 13861 417 -1985 189 N ATOM 374 CA GLY A 56 20.574 -38.503 -40.251 1.00109.35 C ANISOU 374 CA GLY A 56 14830 12914 13805 602 -2116 260 C ATOM 375 C GLY A 56 20.516 -39.988 -40.559 1.00109.77 C ANISOU 375 C GLY A 56 15060 12938 13708 677 -2297 296 C ATOM 376 O GLY A 56 20.234 -40.381 -41.693 1.00106.31 O ANISOU 376 O GLY A 56 14775 12399 13221 836 -2446 341 O ATOM 377 N VAL A 57 20.783 -40.819 -39.555 1.00113.02 N ANISOU 377 N VAL A 57 15471 13432 14041 575 -2292 274 N ATOM 378 CA VAL A 57 20.749 -42.265 -39.751 1.00114.90 C ANISOU 378 CA VAL A 57 15890 13632 14135 636 -2459 307 C ATOM 379 C VAL A 57 19.415 -42.881 -39.328 1.00119.64 C ANISOU 379 C VAL A 57 16463 14132 14863 499 -2570 263 C ATOM 380 O VAL A 57 18.853 -43.710 -40.045 1.00125.54 O ANISOU 380 O VAL A 57 17350 14759 15592 567 -2762 283 O ATOM 381 CB VAL A 57 21.909 -42.978 -39.024 1.00109.32 C ANISOU 381 CB VAL A 57 15240 13064 13234 641 -2402 326 C ATOM 382 CG1 VAL A 57 21.725 -44.488 -39.090 1.00108.60 C ANISOU 382 CG1 VAL A 57 15341 12913 13008 682 -2572 353 C ATOM 383 CG2 VAL A 57 23.243 -42.579 -39.635 1.00105.34 C ANISOU 383 CG2 VAL A 57 14775 12652 12596 802 -2322 388 C ATOM 384 N LEU A 58 18.910 -42.473 -38.168 1.00112.67 N ANISOU 384 N LEU A 58 15401 13296 14114 310 -2450 205 N ATOM 385 CA LEU A 58 17.681 -43.045 -37.632 1.00102.52 C ANISOU 385 CA LEU A 58 14061 11931 12961 165 -2518 177 C ATOM 386 C LEU A 58 16.651 -41.983 -37.303 1.00101.56 C ANISOU 386 C LEU A 58 13727 11785 13075 52 -2432 122 C ATOM 387 O LEU A 58 15.491 -42.089 -37.695 1.00110.04 O ANISOU 387 O LEU A 58 14758 12748 14305 21 -2544 112 O ATOM 388 CB LEU A 58 17.980 -43.853 -36.375 1.00 95.69 C ANISOU 388 CB LEU A 58 13206 11148 12004 52 -2449 173 C ATOM 389 CG LEU A 58 18.868 -45.070 -36.606 1.00 94.41 C ANISOU 389 CG LEU A 58 13266 11000 11606 161 -2547 227 C ATOM 390 CD1 LEU A 58 19.124 -45.789 -35.296 1.00 94.22 C ANISOU 390 CD1 LEU A 58 13252 11057 11492 56 -2464 222 C ATOM 391 CD2 LEU A 58 18.213 -45.990 -37.617 1.00 94.42 C ANISOU 391 CD2 LEU A 58 13426 10835 11614 231 -2777 260 C ATOM 392 N ALA A 59 17.084 -40.965 -36.570 1.00100.07 N ANISOU 392 N ALA A 59 13407 11702 12914 -4 -2241 82 N ATOM 393 CA ALA A 59 16.180 -39.925 -36.101 1.00106.90 C ANISOU 393 CA ALA A 59 14079 12557 13983 -105 -2137 26 C ATOM 394 C ALA A 59 15.368 -39.324 -37.241 1.00113.23 C ANISOU 394 C ALA A 59 14858 13241 14924 -22 -2234 27 C ATOM 395 O ALA A 59 14.140 -39.284 -37.177 1.00122.62 O ANISOU 395 O ALA A 59 15941 14362 16285 -90 -2281 4 O ATOM 396 CB ALA A 59 16.949 -38.847 -35.367 1.00109.94 C ANISOU 396 CB ALA A 59 14367 13053 14352 -140 -1943 -21 C ATOM 397 N ILE A 60 16.049 -38.863 -38.285 1.00110.94 N ANISOU 397 N ILE A 60 14664 12929 14560 135 -2261 59 N ATOM 398 CA ILE A 60 15.354 -38.291 -39.433 1.00115.19 C ANISOU 398 CA ILE A 60 15212 13355 15202 249 -2357 64 C ATOM 399 C ILE A 60 14.433 -39.307 -40.110 1.00122.00 C ANISOU 399 C ILE A 60 16153 14102 16099 285 -2593 76 C ATOM 400 O ILE A 60 13.258 -39.020 -40.330 1.00129.54 O ANISOU 400 O ILE A 60 17007 14981 17232 259 -2665 42 O ATOM 401 CB ILE A 60 16.326 -37.680 -40.463 1.00116.06 C ANISOU 401 CB ILE A 60 15437 13458 15202 431 -2330 115 C ATOM 402 CG1 ILE A 60 17.010 -36.445 -39.878 1.00120.30 C ANISOU 402 CG1 ILE A 60 15860 14076 15774 376 -2105 92 C ATOM 403 CG2 ILE A 60 15.581 -37.308 -41.737 1.00111.09 C ANISOU 403 CG2 ILE A 60 14866 12701 14644 583 -2461 128 C ATOM 404 CD1 ILE A 60 17.947 -35.745 -40.846 1.00122.41 C ANISOU 404 CD1 ILE A 60 16215 14330 15965 536 -2045 154 C ATOM 405 N PRO A 61 14.962 -40.500 -40.441 1.00115.40 N ANISOU 405 N PRO A 61 15498 13249 15099 348 -2722 120 N ATOM 406 CA PRO A 61 14.108 -41.557 -40.998 1.00114.71 C ANISOU 406 CA PRO A 61 15497 13038 15049 363 -2964 122 C ATOM 407 C PRO A 61 12.852 -41.784 -40.161 1.00110.43 C ANISOU 407 C PRO A 61 14771 12469 14721 161 -2971 79 C ATOM 408 O PRO A 61 11.753 -41.873 -40.710 1.00107.49 O ANISOU 408 O PRO A 61 14348 11990 14504 161 -3130 55 O ATOM 409 CB PRO A 61 15.008 -42.793 -40.945 1.00110.57 C ANISOU 409 CB PRO A 61 15170 12534 14307 404 -3030 168 C ATOM 410 CG PRO A 61 16.373 -42.255 -41.058 1.00104.00 C ANISOU 410 CG PRO A 61 14401 11811 13303 518 -2883 206 C ATOM 411 CD PRO A 61 16.372 -40.921 -40.368 1.00104.82 C ANISOU 411 CD PRO A 61 14296 11998 13532 420 -2664 168 C ATOM 412 N PHE A 62 13.018 -41.870 -38.846 1.00108.39 N ANISOU 412 N PHE A 62 14408 12308 14468 -1 -2798 73 N ATOM 413 CA PHE A 62 11.884 -42.057 -37.950 1.00112.17 C ANISOU 413 CA PHE A 62 14705 12775 15141 -188 -2761 50 C ATOM 414 C PHE A 62 10.931 -40.873 -38.020 1.00127.49 C ANISOU 414 C PHE A 62 16443 14705 17294 -206 -2702 4 C ATOM 415 O PHE A 62 9.714 -41.048 -38.032 1.00135.64 O ANISOU 415 O PHE A 62 17346 15670 18523 -284 -2786 -11 O ATOM 416 CB PHE A 62 12.345 -42.261 -36.504 1.00103.93 C ANISOU 416 CB PHE A 62 13610 11848 14030 -324 -2561 55 C ATOM 417 CG PHE A 62 13.018 -43.582 -36.254 1.00107.40 C ANISOU 417 CG PHE A 62 14230 12288 14288 -332 -2622 100 C ATOM 418 CD1 PHE A 62 12.439 -44.765 -36.678 1.00114.47 C ANISOU 418 CD1 PHE A 62 15220 13057 15216 -357 -2820 130 C ATOM 419 CD2 PHE A 62 14.216 -43.641 -35.566 1.00109.18 C ANISOU 419 CD2 PHE A 62 14529 12637 14315 -314 -2488 109 C ATOM 420 CE1 PHE A 62 13.054 -45.979 -36.438 1.00114.76 C ANISOU 420 CE1 PHE A 62 15441 13082 15080 -357 -2874 173 C ATOM 421 CE2 PHE A 62 14.833 -44.851 -35.322 1.00110.16 C ANISOU 421 CE2 PHE A 62 14826 12766 14262 -304 -2542 151 C ATOM 422 CZ PHE A 62 14.251 -46.022 -35.758 1.00111.11 C ANISOU 422 CZ PHE A 62 15058 12752 14407 -323 -2730 186 C ATOM 423 N ALA A 63 11.488 -39.668 -38.065 1.00132.55 N ANISOU 423 N ALA A 63 17053 15411 17901 -134 -2558 -17 N ATOM 424 CA ALA A 63 10.673 -38.461 -38.108 1.00140.81 C ANISOU 424 CA ALA A 63 17927 16447 19128 -132 -2486 -61 C ATOM 425 C ALA A 63 9.836 -38.401 -39.383 1.00148.62 C ANISOU 425 C ALA A 63 18934 17314 20221 -13 -2698 -68 C ATOM 426 O ALA A 63 8.700 -37.930 -39.366 1.00150.17 O ANISOU 426 O ALA A 63 18963 17480 20615 -47 -2715 -103 O ATOM 427 CB ALA A 63 11.544 -37.218 -37.977 1.00140.06 C ANISOU 427 CB ALA A 63 17830 16423 18965 -72 -2302 -79 C ATOM 428 N ILE A 64 10.396 -38.891 -40.484 1.00155.17 N ANISOU 428 N ILE A 64 19970 18078 20910 141 -2864 -36 N ATOM 429 CA ILE A 64 9.699 -38.877 -41.766 1.00162.45 C ANISOU 429 CA ILE A 64 20948 18880 21895 288 -3088 -48 C ATOM 430 C ILE A 64 8.594 -39.927 -41.799 1.00163.02 C ANISOU 430 C ILE A 64 20963 18868 22111 192 -3299 -67 C ATOM 431 O ILE A 64 7.587 -39.767 -42.489 1.00165.77 O ANISOU 431 O ILE A 64 21244 19132 22608 246 -3465 -103 O ATOM 432 CB ILE A 64 10.668 -39.121 -42.939 1.00170.58 C ANISOU 432 CB ILE A 64 22241 19863 22707 506 -3199 -5 C ATOM 433 CG1 ILE A 64 11.828 -38.125 -42.885 1.00179.74 C ANISOU 433 CG1 ILE A 64 23442 21107 23742 582 -2977 27 C ATOM 434 CG2 ILE A 64 9.936 -39.018 -44.270 1.00168.96 C ANISOU 434 CG2 ILE A 64 22110 19534 22553 686 -3432 -25 C ATOM 435 CD1 ILE A 64 12.908 -38.389 -43.910 1.00183.69 C ANISOU 435 CD1 ILE A 64 24189 21585 24020 791 -3037 91 C ATOM 436 N THR A 65 8.794 -41.001 -41.043 1.00161.69 N ANISOU 436 N THR A 65 20818 18717 21900 48 -3292 -41 N ATOM 437 CA THR A 65 7.829 -42.091 -40.974 1.00165.31 C ANISOU 437 CA THR A 65 21226 19084 22502 -73 -3475 -47 C ATOM 438 C THR A 65 6.661 -41.737 -40.060 1.00167.15 C ANISOU 438 C THR A 65 21163 19351 22994 -257 -3363 -68 C ATOM 439 O THR A 65 5.498 -41.925 -40.417 1.00169.06 O ANISOU 439 O THR A 65 21275 19512 23446 -297 -3525 -95 O ATOM 440 CB THR A 65 8.489 -43.383 -40.458 1.00167.63 C ANISOU 440 CB THR A 65 21669 19373 22650 -158 -3490 -1 C ATOM 441 OG1 THR A 65 9.576 -43.742 -41.320 1.00171.27 O ANISOU 441 OG1 THR A 65 22404 19808 22861 31 -3592 24 O ATOM 442 CG2 THR A 65 7.481 -44.518 -40.413 1.00170.08 C ANISOU 442 CG2 THR A 65 21933 19564 23125 -297 -3681 -1 C ATOM 443 N ILE A 66 6.982 -41.217 -38.881 1.00168.23 N ANISOU 443 N ILE A 66 21193 19612 23115 -358 -3089 -57 N ATOM 444 CA ILE A 66 5.968 -40.888 -37.886 1.00171.96 C ANISOU 444 CA ILE A 66 21399 20134 23804 -518 -2943 -65 C ATOM 445 C ILE A 66 5.121 -39.686 -38.306 1.00172.74 C ANISOU 445 C ILE A 66 21325 20234 24073 -443 -2936 -115 C ATOM 446 O ILE A 66 4.016 -39.488 -37.799 1.00176.40 O ANISOU 446 O ILE A 66 21554 20715 24757 -545 -2885 -124 O ATOM 447 CB ILE A 66 6.601 -40.611 -36.506 1.00175.09 C ANISOU 447 CB ILE A 66 21758 20664 24105 -615 -2652 -48 C ATOM 448 CG1 ILE A 66 5.519 -40.538 -35.426 1.00181.01 C ANISOU 448 CG1 ILE A 66 22257 21456 25061 -778 -2505 -39 C ATOM 449 CG2 ILE A 66 7.430 -39.336 -36.540 1.00173.71 C ANISOU 449 CG2 ILE A 66 21621 20569 23812 -497 -2501 -81 C ATOM 450 CD1 ILE A 66 6.062 -40.291 -34.038 1.00182.56 C ANISOU 450 CD1 ILE A 66 22430 21779 25156 -855 -2229 -27 C ATOM 451 N SER A 67 5.641 -38.890 -39.236 1.00169.70 N ANISOU 451 N SER A 67 21060 19832 23586 -254 -2980 -139 N ATOM 452 CA SER A 67 4.929 -37.709 -39.714 1.00169.15 C ANISOU 452 CA SER A 67 20865 19755 23650 -152 -2976 -184 C ATOM 453 C SER A 67 3.614 -38.093 -40.382 1.00169.76 C ANISOU 453 C SER A 67 20818 19741 23941 -149 -3217 -211 C ATOM 454 O SER A 67 2.604 -37.407 -40.224 1.00173.89 O ANISOU 454 O SER A 67 21124 20286 24660 -161 -3180 -243 O ATOM 455 CB SER A 67 5.798 -36.914 -40.690 1.00170.14 C ANISOU 455 CB SER A 67 21180 19857 23609 61 -2989 -189 C ATOM 456 OG SER A 67 6.015 -37.642 -41.886 1.00172.73 O ANISOU 456 OG SER A 67 21705 20083 23841 194 -3244 -177 O ATOM 457 N THR A 68 3.634 -39.191 -41.131 1.00165.39 N ANISOU 457 N THR A 68 20404 19086 23352 -126 -3473 -204 N ATOM 458 CA THR A 68 2.440 -39.677 -41.811 1.00160.50 C ANISOU 458 CA THR A 68 19679 18365 22937 -130 -3744 -240 C ATOM 459 C THR A 68 1.654 -40.628 -40.914 1.00156.68 C ANISOU 459 C THR A 68 19006 17876 22650 -378 -3740 -214 C ATOM 460 O THR A 68 0.465 -40.864 -41.133 1.00161.91 O ANISOU 460 O THR A 68 19476 18485 23558 -440 -3898 -242 O ATOM 461 CB THR A 68 2.789 -40.397 -43.126 1.00156.47 C ANISOU 461 CB THR A 68 19428 17727 22298 29 -4053 -255 C ATOM 462 OG1 THR A 68 3.605 -41.541 -42.845 1.00156.01 O ANISOU 462 OG1 THR A 68 19553 17643 22081 -48 -4072 -209 O ATOM 463 CG2 THR A 68 3.539 -39.463 -44.065 1.00152.38 C ANISOU 463 CG2 THR A 68 19102 17208 21586 290 -4043 -264 C ATOM 464 N GLY A 69 2.327 -41.171 -39.905 1.00145.97 N ANISOU 464 N GLY A 69 17701 16575 21186 -515 -3557 -158 N ATOM 465 CA GLY A 69 1.696 -42.080 -38.968 1.00138.57 C ANISOU 465 CA GLY A 69 16610 15631 20409 -747 -3509 -114 C ATOM 466 C GLY A 69 1.622 -43.501 -39.492 1.00135.70 C ANISOU 466 C GLY A 69 16382 15124 20056 -808 -3779 -101 C ATOM 467 O GLY A 69 1.447 -43.724 -40.690 1.00134.57 O ANISOU 467 O GLY A 69 16345 14869 19917 -683 -4069 -149 O ATOM 468 N PHE A 70 1.760 -44.465 -38.589 1.00137.29 N ANISOU 468 N PHE A 70 16594 15318 20252 -988 -3686 -36 N ATOM 469 CA PHE A 70 1.690 -45.873 -38.955 1.00144.57 C ANISOU 469 CA PHE A 70 17653 16089 21190 -1068 -3923 -18 C ATOM 470 C PHE A 70 1.050 -46.693 -37.840 1.00143.54 C ANISOU 470 C PHE A 70 17357 15942 21241 -1327 -3801 55 C ATOM 471 O PHE A 70 0.528 -46.140 -36.874 1.00145.60 O ANISOU 471 O PHE A 70 17374 16310 21635 -1430 -3550 88 O ATOM 472 CB PHE A 70 3.083 -46.416 -39.280 1.00152.89 C ANISOU 472 CB PHE A 70 19062 17120 21909 -946 -3967 -2 C ATOM 473 CG PHE A 70 4.056 -46.314 -38.140 1.00154.39 C ANISOU 473 CG PHE A 70 19316 17444 21902 -987 -3660 54 C ATOM 474 CD1 PHE A 70 4.827 -45.176 -37.969 1.00152.95 C ANISOU 474 CD1 PHE A 70 19152 17401 21562 -861 -3462 37 C ATOM 475 CD2 PHE A 70 4.204 -47.358 -37.242 1.00155.11 C ANISOU 475 CD2 PHE A 70 19455 17513 21966 -1148 -3575 122 C ATOM 476 CE1 PHE A 70 5.724 -45.080 -36.923 1.00152.70 C ANISOU 476 CE1 PHE A 70 19174 17491 21355 -896 -3205 75 C ATOM 477 CE2 PHE A 70 5.099 -47.268 -36.193 1.00153.38 C ANISOU 477 CE2 PHE A 70 19303 17421 21555 -1167 -3308 166 C ATOM 478 CZ PHE A 70 5.860 -46.127 -36.035 1.00153.10 C ANISOU 478 CZ PHE A 70 19274 17530 21367 -1041 -3132 136 C ATOM 479 N CYS A 71 1.095 -48.013 -37.979 1.00142.49 N ANISOU 479 N CYS A 71 17367 15666 21106 -1423 -3972 86 N ATOM 480 CA CYS A 71 0.483 -48.905 -37.001 1.00147.51 C ANISOU 480 CA CYS A 71 17870 16256 21923 -1674 -3869 168 C ATOM 481 C CYS A 71 1.491 -49.894 -36.429 1.00146.30 C ANISOU 481 C CYS A 71 17988 16074 21525 -1713 -3787 236 C ATOM 482 O CYS A 71 2.123 -50.646 -37.169 1.00144.31 O ANISOU 482 O CYS A 71 18017 15709 21106 -1626 -4010 216 O ATOM 483 CB CYS A 71 -0.689 -49.659 -37.630 1.00154.30 C ANISOU 483 CB CYS A 71 18595 16938 23094 -1802 -4164 148 C ATOM 484 SG CYS A 71 -2.010 -48.594 -38.255 1.00239.28 S ANISOU 484 SG CYS A 71 29004 27736 34176 -1764 -4278 68 S ATOM 485 N ALA A 72 1.632 -49.888 -35.107 1.00150.93 N ANISOU 485 N ALA A 72 18500 16767 22082 -1825 -3469 316 N ATOM 486 CA ALA A 72 2.553 -50.792 -34.427 1.00155.54 C ANISOU 486 CA ALA A 72 19327 17339 22432 -1857 -3363 385 C ATOM 487 C ALA A 72 2.280 -50.829 -32.926 1.00156.16 C ANISOU 487 C ALA A 72 19254 17510 22569 -2013 -3023 479 C ATOM 488 O ALA A 72 1.550 -49.989 -32.400 1.00158.68 O ANISOU 488 O ALA A 72 19295 17932 23063 -2062 -2841 485 O ATOM 489 CB ALA A 72 3.994 -50.383 -34.695 1.00156.39 C ANISOU 489 CB ALA A 72 19699 17545 22176 -1639 -3336 345 C ATOM 490 N ALA A 73 2.871 -51.804 -32.242 1.00154.53 N ANISOU 490 N ALA A 73 19244 17268 22202 -2072 -2934 555 N ATOM 491 CA ALA A 73 2.707 -51.937 -30.799 1.00156.24 C ANISOU 491 CA ALA A 73 19366 17565 22431 -2195 -2607 654 C ATOM 492 C ALA A 73 3.183 -50.678 -30.082 1.00162.70 C ANISOU 492 C ALA A 73 20108 18607 23104 -2080 -2337 622 C ATOM 493 O ALA A 73 3.740 -49.776 -30.704 1.00160.19 O ANISOU 493 O ALA A 73 19829 18369 22665 -1916 -2402 530 O ATOM 494 CB ALA A 73 3.455 -53.158 -30.289 1.00154.46 C ANISOU 494 CB ALA A 73 19425 17266 21997 -2227 -2576 729 C ATOM 495 N CYS A 74 2.964 -50.620 -28.773 1.00173.25 N ANISOU 495 N CYS A 74 21343 20033 24450 -2161 -2032 699 N ATOM 496 CA CYS A 74 3.318 -49.435 -27.998 1.00182.16 C ANISOU 496 CA CYS A 74 22393 21362 25456 -2060 -1776 663 C ATOM 497 C CYS A 74 4.831 -49.286 -27.850 1.00192.73 C ANISOU 497 C CYS A 74 24006 22798 26423 -1897 -1747 613 C ATOM 498 O CYS A 74 5.369 -48.188 -27.988 1.00198.93 O ANISOU 498 O CYS A 74 24779 23705 27100 -1764 -1708 528 O ATOM 499 CB CYS A 74 2.644 -49.464 -26.624 1.00183.70 C ANISOU 499 CB CYS A 74 22423 21623 25752 -2173 -1460 763 C ATOM 500 SG CYS A 74 2.552 -47.850 -25.804 1.00353.13 S ANISOU 500 SG CYS A 74 43695 43299 47180 -2066 -1176 708 S ATOM 501 N HIS A 75 5.512 -50.393 -27.570 1.00193.76 N ANISOU 501 N HIS A 75 24379 22871 26368 -1908 -1768 669 N ATOM 502 CA HIS A 75 6.964 -50.383 -27.418 1.00188.48 C ANISOU 502 CA HIS A 75 23966 22297 25349 -1754 -1752 628 C ATOM 503 C HIS A 75 7.663 -49.922 -28.694 1.00179.56 C ANISOU 503 C HIS A 75 22936 21166 24123 -1605 -1982 532 C ATOM 504 O HIS A 75 8.566 -49.087 -28.651 1.00178.53 O ANISOU 504 O HIS A 75 22852 21171 23812 -1470 -1920 465 O ATOM 505 CB HIS A 75 7.472 -51.768 -27.012 1.00192.91 C ANISOU 505 CB HIS A 75 24778 22776 25744 -1786 -1764 709 C ATOM 506 CG HIS A 75 7.182 -52.126 -25.587 1.00198.16 C ANISOU 506 CG HIS A 75 25413 23483 26394 -1874 -1485 804 C ATOM 507 ND1 HIS A 75 5.998 -52.717 -25.192 1.00201.37 N ANISOU 507 ND1 HIS A 75 25676 23776 27059 -2058 -1406 910 N ATOM 508 CD2 HIS A 75 7.920 -51.980 -24.464 1.00197.88 C ANISOU 508 CD2 HIS A 75 25479 23590 26118 -1794 -1265 813 C ATOM 509 CE1 HIS A 75 6.023 -52.916 -23.890 1.00202.26 C ANISOU 509 CE1 HIS A 75 25811 23959 27078 -2080 -1133 990 C ATOM 510 NE2 HIS A 75 7.178 -52.478 -23.419 1.00200.77 N ANISOU 510 NE2 HIS A 75 25778 23926 26579 -1915 -1050 927 N ATOM 511 N GLY A 76 7.241 -50.473 -29.827 1.00174.16 N ANISOU 511 N GLY A 76 22287 20322 23564 -1627 -2247 528 N ATOM 512 CA GLY A 76 7.826 -50.127 -31.108 1.00171.51 C ANISOU 512 CA GLY A 76 22063 19967 23137 -1471 -2471 451 C ATOM 513 C GLY A 76 7.467 -48.725 -31.560 1.00173.13 C ANISOU 513 C GLY A 76 22066 20250 23467 -1407 -2453 376 C ATOM 514 O GLY A 76 8.267 -48.049 -32.205 1.00172.80 O ANISOU 514 O GLY A 76 22109 20268 23280 -1249 -2507 316 O ATOM 515 N CYS A 77 6.259 -48.288 -31.218 1.00176.17 N ANISOU 515 N CYS A 77 22182 20631 24123 -1525 -2367 387 N ATOM 516 CA CYS A 77 5.783 -46.963 -31.604 1.00175.52 C ANISOU 516 CA CYS A 77 21899 20613 24176 -1465 -2344 319 C ATOM 517 C CYS A 77 6.403 -45.873 -30.733 1.00170.66 C ANISOU 517 C CYS A 77 21244 20176 23423 -1397 -2085 284 C ATOM 518 O CYS A 77 6.604 -44.744 -31.184 1.00169.34 O ANISOU 518 O CYS A 77 21026 20068 23246 -1287 -2081 215 O ATOM 519 CB CYS A 77 4.255 -46.897 -31.527 1.00177.85 C ANISOU 519 CB CYS A 77 21911 20851 24814 -1605 -2344 343 C ATOM 520 SG CYS A 77 3.534 -45.358 -32.149 1.00209.01 S ANISOU 520 SG CYS A 77 25618 24855 28943 -1514 -2358 259 S ATOM 521 N LEU A 78 6.702 -46.216 -29.484 1.00167.07 N ANISOU 521 N LEU A 78 20823 19796 22860 -1457 -1873 332 N ATOM 522 CA LEU A 78 7.327 -45.273 -28.561 1.00163.21 C ANISOU 522 CA LEU A 78 20317 19471 22226 -1392 -1641 291 C ATOM 523 C LEU A 78 8.803 -45.070 -28.884 1.00160.90 C ANISOU 523 C LEU A 78 20236 19242 21655 -1250 -1692 237 C ATOM 524 O LEU A 78 9.290 -43.941 -28.918 1.00161.04 O ANISOU 524 O LEU A 78 20219 19351 21617 -1161 -1625 165 O ATOM 525 CB LEU A 78 7.172 -45.742 -27.113 1.00161.38 C ANISOU 525 CB LEU A 78 20070 19297 21949 -1481 -1406 358 C ATOM 526 CG LEU A 78 5.812 -45.519 -26.450 1.00165.69 C ANISOU 526 CG LEU A 78 20362 19845 22750 -1596 -1244 409 C ATOM 527 CD1 LEU A 78 5.812 -46.095 -25.044 1.00169.02 C ANISOU 527 CD1 LEU A 78 20820 20318 23080 -1657 -1006 490 C ATOM 528 CD2 LEU A 78 5.467 -44.038 -26.428 1.00166.06 C ANISOU 528 CD2 LEU A 78 20225 19983 22885 -1527 -1147 330 C ATOM 529 N PHE A 79 9.510 -46.170 -29.116 1.00154.61 N ANISOU 529 N PHE A 79 19656 18395 20693 -1230 -1808 275 N ATOM 530 CA PHE A 79 10.923 -46.102 -29.461 1.00148.40 C ANISOU 530 CA PHE A 79 19065 17673 19646 -1089 -1863 238 C ATOM 531 C PHE A 79 11.151 -45.206 -30.673 1.00143.68 C ANISOU 531 C PHE A 79 18448 17063 19082 -975 -1990 177 C ATOM 532 O PHE A 79 12.058 -44.375 -30.681 1.00149.13 O ANISOU 532 O PHE A 79 19163 17855 19646 -878 -1924 126 O ATOM 533 CB PHE A 79 11.484 -47.496 -29.740 1.00152.51 C ANISOU 533 CB PHE A 79 19824 18116 20008 -1070 -2004 294 C ATOM 534 CG PHE A 79 12.882 -47.484 -30.287 1.00157.37 C ANISOU 534 CG PHE A 79 20630 18793 20371 -908 -2084 265 C ATOM 535 CD1 PHE A 79 13.971 -47.406 -29.438 1.00153.16 C ANISOU 535 CD1 PHE A 79 20178 18402 19612 -850 -1949 248 C ATOM 536 CD2 PHE A 79 13.108 -47.544 -31.653 1.00158.89 C ANISOU 536 CD2 PHE A 79 20916 18904 20550 -802 -2295 254 C ATOM 537 CE1 PHE A 79 15.258 -47.392 -29.938 1.00148.09 C ANISOU 537 CE1 PHE A 79 19685 17827 18755 -703 -2017 227 C ATOM 538 CE2 PHE A 79 14.393 -47.528 -32.158 1.00154.63 C ANISOU 538 CE2 PHE A 79 20541 18428 19782 -644 -2348 242 C ATOM 539 CZ PHE A 79 15.469 -47.453 -31.300 1.00149.31 C ANISOU 539 CZ PHE A 79 19924 17903 18904 -601 -2206 230 C ATOM 540 N ILE A 80 10.324 -45.386 -31.697 1.00132.76 N ANISOU 540 N ILE A 80 17023 15550 17871 -984 -2174 186 N ATOM 541 CA ILE A 80 10.447 -44.606 -32.922 1.00127.56 C ANISOU 541 CA ILE A 80 16366 14861 17241 -858 -2305 138 C ATOM 542 C ILE A 80 10.167 -43.126 -32.678 1.00138.37 C ANISOU 542 C ILE A 80 17546 16313 18716 -844 -2152 81 C ATOM 543 O ILE A 80 10.760 -42.258 -33.319 1.00140.60 O ANISOU 543 O ILE A 80 17860 16624 18938 -723 -2165 40 O ATOM 544 CB ILE A 80 9.512 -45.138 -34.028 1.00111.08 C ANISOU 544 CB ILE A 80 14272 12611 15321 -864 -2552 150 C ATOM 545 CG1 ILE A 80 9.990 -46.509 -34.511 1.00102.17 C ANISOU 545 CG1 ILE A 80 13385 11384 14050 -835 -2739 193 C ATOM 546 CG2 ILE A 80 9.448 -44.162 -35.194 1.00105.15 C ANISOU 546 CG2 ILE A 80 13496 11836 14620 -725 -2657 99 C ATOM 547 CD1 ILE A 80 9.199 -47.055 -35.679 1.00100.37 C ANISOU 547 CD1 ILE A 80 13190 10985 13962 -819 -3018 188 C ATOM 548 N ALA A 81 9.272 -42.844 -31.737 1.00145.80 N ANISOU 548 N ALA A 81 18298 17288 19812 -960 -1998 83 N ATOM 549 CA ALA A 81 8.877 -41.470 -31.447 1.00150.87 C ANISOU 549 CA ALA A 81 18763 17997 20564 -944 -1853 27 C ATOM 550 C ALA A 81 9.773 -40.811 -30.400 1.00149.68 C ANISOU 550 C ALA A 81 18636 17983 20254 -926 -1641 -13 C ATOM 551 O ALA A 81 9.918 -39.589 -30.378 1.00150.76 O ANISOU 551 O ALA A 81 18702 18168 20411 -871 -1552 -75 O ATOM 552 CB ALA A 81 7.422 -41.422 -31.005 1.00155.95 C ANISOU 552 CB ALA A 81 19181 18613 21459 -1056 -1792 48 C ATOM 553 N CYS A 82 10.376 -41.623 -29.538 1.00149.47 N ANISOU 553 N CYS A 82 18717 18011 20066 -967 -1570 18 N ATOM 554 CA CYS A 82 11.171 -41.102 -28.430 1.00156.12 C ANISOU 554 CA CYS A 82 19579 18984 20754 -951 -1383 -28 C ATOM 555 C CYS A 82 12.671 -41.253 -28.664 1.00158.71 C ANISOU 555 C CYS A 82 20089 19369 20845 -860 -1437 -49 C ATOM 556 O CYS A 82 13.479 -40.865 -27.820 1.00156.77 O ANISOU 556 O CYS A 82 19871 19234 20460 -838 -1315 -98 O ATOM 557 CB CYS A 82 10.776 -41.789 -27.121 1.00158.99 C ANISOU 557 CB CYS A 82 19926 19389 21093 -1043 -1234 18 C ATOM 558 SG CYS A 82 9.028 -41.622 -26.688 1.00185.41 S ANISOU 558 SG CYS A 82 23032 22691 24723 -1152 -1127 60 S ATOM 559 N PHE A 83 13.039 -41.820 -29.807 1.00159.25 N ANISOU 559 N PHE A 83 20276 19363 20867 -797 -1623 -15 N ATOM 560 CA PHE A 83 14.447 -42.009 -30.139 1.00154.60 C ANISOU 560 CA PHE A 83 19850 18831 20060 -695 -1675 -21 C ATOM 561 C PHE A 83 15.144 -40.666 -30.332 1.00147.95 C ANISOU 561 C PHE A 83 18952 18056 19207 -627 -1605 -90 C ATOM 562 O PHE A 83 16.338 -40.530 -30.066 1.00146.23 O ANISOU 562 O PHE A 83 18803 17933 18825 -576 -1565 -116 O ATOM 563 CB PHE A 83 14.596 -42.871 -31.394 1.00154.83 C ANISOU 563 CB PHE A 83 20026 18757 20046 -620 -1889 34 C ATOM 564 CG PHE A 83 16.024 -43.124 -31.790 1.00154.05 C ANISOU 564 CG PHE A 83 20093 18721 19720 -497 -1937 43 C ATOM 565 CD1 PHE A 83 16.760 -44.126 -31.179 1.00150.78 C ANISOU 565 CD1 PHE A 83 19817 18364 19108 -487 -1932 71 C ATOM 566 CD2 PHE A 83 16.630 -42.361 -32.774 1.00149.45 C ANISOU 566 CD2 PHE A 83 19525 18141 19119 -382 -1979 29 C ATOM 567 CE1 PHE A 83 18.072 -44.360 -31.540 1.00142.46 C ANISOU 567 CE1 PHE A 83 18900 17382 17847 -362 -1974 81 C ATOM 568 CE2 PHE A 83 17.942 -42.590 -33.140 1.00141.87 C ANISOU 568 CE2 PHE A 83 18697 17247 17960 -265 -2008 49 C ATOM 569 CZ PHE A 83 18.663 -43.592 -32.525 1.00139.24 C ANISOU 569 CZ PHE A 83 18487 16983 17434 -254 -2010 72 C ATOM 570 N VAL A 84 14.388 -39.676 -30.797 1.00141.86 N ANISOU 570 N VAL A 84 18053 17230 18619 -628 -1592 -119 N ATOM 571 CA VAL A 84 14.923 -38.337 -31.015 1.00136.52 C ANISOU 571 CA VAL A 84 17323 16588 17961 -574 -1520 -180 C ATOM 572 C VAL A 84 15.221 -37.648 -29.687 1.00126.16 C ANISOU 572 C VAL A 84 15938 15383 16616 -630 -1340 -254 C ATOM 573 O VAL A 84 16.104 -36.794 -29.603 1.00122.48 O ANISOU 573 O VAL A 84 15469 14970 16099 -597 -1281 -310 O ATOM 574 CB VAL A 84 13.949 -37.469 -31.840 1.00144.34 C ANISOU 574 CB VAL A 84 18209 17482 19152 -548 -1554 -190 C ATOM 575 CG1 VAL A 84 12.597 -37.374 -31.146 1.00144.25 C ANISOU 575 CG1 VAL A 84 18045 17452 19309 -641 -1483 -201 C ATOM 576 CG2 VAL A 84 14.534 -36.085 -32.079 1.00149.54 C ANISOU 576 CG2 VAL A 84 18834 18157 19828 -493 -1471 -244 C ATOM 577 N LEU A 85 14.482 -38.027 -28.650 1.00123.61 N ANISOU 577 N LEU A 85 15559 15086 16324 -711 -1254 -254 N ATOM 578 CA LEU A 85 14.679 -37.460 -27.322 1.00124.39 C ANISOU 578 CA LEU A 85 15609 15282 16372 -745 -1088 -326 C ATOM 579 C LEU A 85 15.999 -37.932 -26.725 1.00121.52 C ANISOU 579 C LEU A 85 15365 15024 15782 -718 -1080 -349 C ATOM 580 O LEU A 85 16.586 -37.258 -25.880 1.00113.94 O ANISOU 580 O LEU A 85 14388 14150 14753 -714 -984 -433 O ATOM 581 CB LEU A 85 13.520 -37.841 -26.401 1.00126.89 C ANISOU 581 CB LEU A 85 15846 15599 16767 -819 -986 -300 C ATOM 582 CG LEU A 85 12.124 -37.450 -26.885 1.00127.08 C ANISOU 582 CG LEU A 85 15722 15534 17029 -848 -990 -275 C ATOM 583 CD1 LEU A 85 11.064 -37.928 -25.907 1.00130.93 C ANISOU 583 CD1 LEU A 85 16121 16035 17590 -924 -870 -232 C ATOM 584 CD2 LEU A 85 12.028 -35.946 -27.091 1.00125.19 C ANISOU 584 CD2 LEU A 85 15393 15288 16887 -803 -932 -356 C ATOM 585 N VAL A 86 16.459 -39.096 -27.172 1.00128.19 N ANISOU 585 N VAL A 86 16335 15861 16510 -691 -1193 -278 N ATOM 586 CA VAL A 86 17.719 -39.658 -26.700 1.00129.76 C ANISOU 586 CA VAL A 86 16654 16164 16485 -646 -1203 -290 C ATOM 587 C VAL A 86 18.909 -38.908 -27.292 1.00125.76 C ANISOU 587 C VAL A 86 16151 15704 15929 -579 -1237 -335 C ATOM 588 O VAL A 86 19.843 -38.543 -26.577 1.00122.75 O ANISOU 588 O VAL A 86 15769 15431 15441 -566 -1183 -406 O ATOM 589 CB VAL A 86 17.837 -41.155 -27.049 1.00129.97 C ANISOU 589 CB VAL A 86 16829 16158 16397 -623 -1316 -195 C ATOM 590 CG1 VAL A 86 19.171 -41.707 -26.569 1.00137.29 C ANISOU 590 CG1 VAL A 86 17879 17203 17081 -555 -1326 -210 C ATOM 591 CG2 VAL A 86 16.684 -41.934 -26.440 1.00127.87 C ANISOU 591 CG2 VAL A 86 16555 15834 16197 -707 -1272 -140 C ATOM 592 N LEU A 87 18.868 -38.681 -28.602 1.00121.93 N ANISOU 592 N LEU A 87 15668 15133 15526 -533 -1328 -291 N ATOM 593 CA LEU A 87 19.931 -37.955 -29.286 1.00113.12 C ANISOU 593 CA LEU A 87 14549 14045 14386 -467 -1343 -309 C ATOM 594 C LEU A 87 19.981 -36.504 -28.824 1.00118.67 C ANISOU 594 C LEU A 87 15125 14765 15200 -513 -1228 -406 C ATOM 595 O LEU A 87 21.058 -35.935 -28.648 1.00128.31 O ANISOU 595 O LEU A 87 16326 16058 16370 -501 -1195 -457 O ATOM 596 CB LEU A 87 19.739 -38.015 -30.803 1.00100.13 C ANISOU 596 CB LEU A 87 12949 12292 12803 -390 -1453 -231 C ATOM 597 CG LEU A 87 19.739 -39.407 -31.437 1.00 96.81 C ANISOU 597 CG LEU A 87 12679 11833 12271 -325 -1594 -141 C ATOM 598 CD1 LEU A 87 19.642 -39.302 -32.950 1.00 91.75 C ANISOU 598 CD1 LEU A 87 12094 11089 11678 -221 -1703 -79 C ATOM 599 CD2 LEU A 87 20.983 -40.182 -31.035 1.00100.31 C ANISOU 599 CD2 LEU A 87 13226 12395 12494 -273 -1607 -129 C ATOM 600 N ALA A 88 18.809 -35.912 -28.628 1.00118.02 N ANISOU 600 N ALA A 88 14955 14613 15276 -564 -1170 -432 N ATOM 601 CA ALA A 88 18.718 -34.529 -28.178 1.00121.14 C ANISOU 601 CA ALA A 88 15246 15003 15779 -600 -1063 -527 C ATOM 602 C ALA A 88 19.201 -34.386 -26.739 1.00121.69 C ANISOU 602 C ALA A 88 15306 15185 15748 -640 -977 -623 C ATOM 603 O ALA A 88 19.760 -33.356 -26.362 1.00119.60 O ANISOU 603 O ALA A 88 14992 14943 15507 -657 -921 -717 O ATOM 604 CB ALA A 88 17.292 -34.020 -28.313 1.00125.52 C ANISOU 604 CB ALA A 88 15715 15462 16514 -623 -1026 -525 C ATOM 605 N GLN A 89 18.985 -35.425 -25.938 1.00125.37 N ANISOU 605 N GLN A 89 15827 15711 16098 -652 -970 -602 N ATOM 606 CA GLN A 89 19.380 -35.400 -24.534 1.00133.20 C ANISOU 606 CA GLN A 89 16833 16810 16967 -666 -892 -689 C ATOM 607 C GLN A 89 20.875 -35.652 -24.367 1.00137.24 C ANISOU 607 C GLN A 89 17404 17430 17312 -628 -948 -726 C ATOM 608 O GLN A 89 21.523 -35.045 -23.514 1.00137.31 O ANISOU 608 O GLN A 89 17390 17515 17265 -633 -909 -838 O ATOM 609 CB GLN A 89 18.580 -36.427 -23.730 1.00137.86 C ANISOU 609 CB GLN A 89 17469 17419 17490 -681 -846 -638 C ATOM 610 CG GLN A 89 18.851 -36.390 -22.234 1.00141.56 C ANISOU 610 CG GLN A 89 17971 17994 17820 -670 -751 -724 C ATOM 611 CD GLN A 89 18.444 -35.074 -21.598 1.00142.35 C ANISOU 611 CD GLN A 89 17984 18086 18016 -684 -647 -834 C ATOM 612 OE1 GLN A 89 17.785 -34.244 -22.226 1.00142.06 O ANISOU 612 OE1 GLN A 89 17857 17958 18161 -707 -630 -835 O ATOM 613 NE2 GLN A 89 18.833 -34.878 -20.344 1.00141.97 N ANISOU 613 NE2 GLN A 89 17978 18130 17836 -654 -583 -932 N ATOM 614 N SER A 90 21.416 -36.552 -25.182 1.00141.37 N ANISOU 614 N SER A 90 18002 17960 17753 -582 -1047 -636 N ATOM 615 CA SER A 90 22.843 -36.853 -25.142 1.00139.61 C ANISOU 615 CA SER A 90 17824 17848 17374 -530 -1103 -655 C ATOM 616 C SER A 90 23.657 -35.620 -25.511 1.00126.87 C ANISOU 616 C SER A 90 16111 16241 15854 -545 -1092 -723 C ATOM 617 O SER A 90 24.702 -35.352 -24.919 1.00117.24 O ANISOU 617 O SER A 90 14865 15125 14555 -541 -1097 -806 O ATOM 618 CB SER A 90 23.178 -38.010 -26.085 1.00140.47 C ANISOU 618 CB SER A 90 18038 17947 17386 -459 -1208 -534 C ATOM 619 OG SER A 90 24.557 -38.329 -26.030 1.00138.00 O ANISOU 619 OG SER A 90 17761 17757 16917 -394 -1255 -547 O ATOM 620 N SER A 91 23.166 -34.872 -26.494 1.00122.65 N ANISOU 620 N SER A 91 15521 15587 15492 -559 -1081 -687 N ATOM 621 CA SER A 91 23.813 -33.636 -26.914 1.00115.11 C ANISOU 621 CA SER A 91 14477 14606 14654 -582 -1053 -736 C ATOM 622 C SER A 91 23.881 -32.653 -25.752 1.00116.36 C ANISOU 622 C SER A 91 14564 14791 14854 -650 -983 -885 C ATOM 623 O SER A 91 24.815 -31.859 -25.653 1.00113.09 O ANISOU 623 O SER A 91 14086 14405 14479 -680 -978 -959 O ATOM 624 CB SER A 91 23.062 -33.009 -28.091 1.00105.46 C ANISOU 624 CB SER A 91 13230 13235 13604 -573 -1041 -669 C ATOM 625 OG SER A 91 23.068 -33.869 -29.217 1.00 97.18 O ANISOU 625 OG SER A 91 12261 12155 12508 -492 -1122 -541 O ATOM 626 N ILE A 92 22.885 -32.716 -24.875 1.00123.00 N ANISOU 626 N ILE A 92 15420 15623 15693 -670 -931 -929 N ATOM 627 CA ILE A 92 22.844 -31.857 -23.699 1.00130.55 C ANISOU 627 CA ILE A 92 16339 16603 16662 -709 -866 -1074 C ATOM 628 C ILE A 92 24.032 -32.127 -22.783 1.00132.61 C ANISOU 628 C ILE A 92 16620 17005 16760 -697 -909 -1166 C ATOM 629 O ILE A 92 24.731 -31.203 -22.369 1.00131.87 O ANISOU 629 O ILE A 92 16471 16928 16707 -733 -914 -1287 O ATOM 630 CB ILE A 92 21.539 -32.049 -22.906 1.00131.82 C ANISOU 630 CB ILE A 92 16522 16743 16822 -708 -788 -1081 C ATOM 631 CG1 ILE A 92 20.341 -31.581 -23.733 1.00128.96 C ANISOU 631 CG1 ILE A 92 16109 16245 16644 -720 -749 -1015 C ATOM 632 CG2 ILE A 92 21.599 -31.294 -21.588 1.00133.65 C ANISOU 632 CG2 ILE A 92 16748 17017 17017 -716 -727 -1235 C ATOM 633 CD1 ILE A 92 20.383 -30.111 -24.082 1.00125.12 C ANISOU 633 CD1 ILE A 92 15555 15667 16319 -746 -714 -1087 C ATOM 634 N PHE A 93 24.255 -33.400 -22.472 1.00134.37 N ANISOU 634 N PHE A 93 16929 17325 16802 -644 -950 -1112 N ATOM 635 CA PHE A 93 25.351 -33.792 -21.594 1.00139.61 C ANISOU 635 CA PHE A 93 17624 18134 17287 -607 -1002 -1194 C ATOM 636 C PHE A 93 26.711 -33.495 -22.219 1.00136.58 C ANISOU 636 C PHE A 93 17168 17803 16924 -612 -1076 -1206 C ATOM 637 O PHE A 93 27.643 -33.081 -21.529 1.00131.17 O ANISOU 637 O PHE A 93 16438 17206 16195 -621 -1115 -1329 O ATOM 638 CB PHE A 93 25.250 -35.276 -21.241 1.00142.69 C ANISOU 638 CB PHE A 93 18139 18601 17476 -536 -1025 -1112 C ATOM 639 CG PHE A 93 24.000 -35.638 -20.494 1.00141.52 C ANISOU 639 CG PHE A 93 18054 18415 17302 -535 -936 -1093 C ATOM 640 CD1 PHE A 93 23.871 -35.339 -19.148 1.00141.20 C ANISOU 640 CD1 PHE A 93 18043 18432 17174 -515 -877 -1208 C ATOM 641 CD2 PHE A 93 22.957 -36.284 -21.135 1.00138.20 C ANISOU 641 CD2 PHE A 93 17662 17901 16946 -549 -912 -958 C ATOM 642 CE1 PHE A 93 22.722 -35.673 -18.458 1.00139.97 C ANISOU 642 CE1 PHE A 93 17941 18247 16996 -504 -771 -1173 C ATOM 643 CE2 PHE A 93 21.806 -36.621 -20.450 1.00139.05 C ANISOU 643 CE2 PHE A 93 17804 17976 17053 -558 -818 -928 C ATOM 644 CZ PHE A 93 21.688 -36.316 -19.110 1.00141.06 C ANISOU 644 CZ PHE A 93 18084 18294 17219 -533 -735 -1028 C ATOM 645 N SER A 94 26.818 -33.712 -23.526 1.00136.82 N ANISOU 645 N SER A 94 17186 17779 17022 -599 -1097 -1078 N ATOM 646 CA SER A 94 28.058 -33.449 -24.247 1.00128.46 C ANISOU 646 CA SER A 94 16050 16764 15994 -594 -1143 -1058 C ATOM 647 C SER A 94 28.388 -31.959 -24.254 1.00132.67 C ANISOU 647 C SER A 94 16456 17233 16718 -686 -1106 -1158 C ATOM 648 O SER A 94 29.519 -31.563 -23.970 1.00133.56 O ANISOU 648 O SER A 94 16483 17426 16838 -714 -1144 -1237 O ATOM 649 CB SER A 94 27.973 -33.977 -25.681 1.00114.62 C ANISOU 649 CB SER A 94 14334 14951 14264 -538 -1159 -889 C ATOM 650 OG SER A 94 27.813 -35.385 -25.699 1.00107.37 O ANISOU 650 OG SER A 94 13544 14086 13167 -453 -1211 -803 O ATOM 651 N LEU A 95 27.394 -31.137 -24.577 1.00133.24 N ANISOU 651 N LEU A 95 16516 17157 16954 -734 -1037 -1155 N ATOM 652 CA LEU A 95 27.577 -29.691 -24.603 1.00130.49 C ANISOU 652 CA LEU A 95 16071 16717 16794 -820 -995 -1245 C ATOM 653 C LEU A 95 27.866 -29.143 -23.209 1.00127.82 C ANISOU 653 C LEU A 95 15710 16433 16424 -866 -1013 -1434 C ATOM 654 O LEU A 95 28.638 -28.198 -23.052 1.00124.24 O ANISOU 654 O LEU A 95 15167 15962 16078 -939 -1029 -1533 O ATOM 655 CB LEU A 95 26.347 -29.000 -25.200 1.00127.02 C ANISOU 655 CB LEU A 95 15645 16107 16511 -836 -919 -1201 C ATOM 656 CG LEU A 95 26.065 -29.249 -26.683 1.00123.99 C ANISOU 656 CG LEU A 95 15281 15639 16189 -785 -910 -1032 C ATOM 657 CD1 LEU A 95 24.783 -28.548 -27.111 1.00123.05 C ANISOU 657 CD1 LEU A 95 15175 15364 16215 -789 -848 -1012 C ATOM 658 CD2 LEU A 95 27.238 -28.798 -27.539 1.00125.90 C ANISOU 658 CD2 LEU A 95 15454 15876 16507 -797 -908 -981 C ATOM 659 N LEU A 96 27.242 -29.744 -22.200 1.00127.52 N ANISOU 659 N LEU A 96 15758 16454 16239 -821 -1011 -1482 N ATOM 660 CA LEU A 96 27.443 -29.326 -20.818 1.00131.00 C ANISOU 660 CA LEU A 96 16210 16952 16611 -830 -1032 -1663 C ATOM 661 C LEU A 96 28.842 -29.695 -20.336 1.00127.88 C ANISOU 661 C LEU A 96 15780 16712 16098 -816 -1138 -1738 C ATOM 662 O LEU A 96 29.483 -28.927 -19.619 1.00127.75 O ANISOU 662 O LEU A 96 15710 16717 16113 -859 -1189 -1900 O ATOM 663 CB LEU A 96 26.388 -29.956 -19.908 1.00138.16 C ANISOU 663 CB LEU A 96 17231 17886 17376 -763 -981 -1669 C ATOM 664 CG LEU A 96 26.478 -29.626 -18.417 1.00145.42 C ANISOU 664 CG LEU A 96 18199 18869 18184 -735 -993 -1847 C ATOM 665 CD1 LEU A 96 26.475 -28.122 -18.188 1.00146.65 C ANISOU 665 CD1 LEU A 96 18299 18917 18504 -804 -983 -1992 C ATOM 666 CD2 LEU A 96 25.341 -30.287 -17.650 1.00147.50 C ANISOU 666 CD2 LEU A 96 18576 19150 18318 -659 -907 -1813 C ATOM 667 N ALA A 97 29.310 -30.873 -20.736 1.00126.74 N ANISOU 667 N ALA A 97 15665 16673 15817 -748 -1179 -1625 N ATOM 668 CA ALA A 97 30.643 -31.334 -20.366 1.00125.12 C ANISOU 668 CA ALA A 97 15420 16631 15489 -712 -1281 -1679 C ATOM 669 C ALA A 97 31.718 -30.452 -20.990 1.00121.27 C ANISOU 669 C ALA A 97 14767 16130 15180 -798 -1315 -1707 C ATOM 670 O ALA A 97 32.683 -30.072 -20.329 1.00118.16 O ANISOU 670 O ALA A 97 14290 15821 14784 -827 -1398 -1846 O ATOM 671 CB ALA A 97 30.835 -32.783 -20.780 1.00124.04 C ANISOU 671 CB ALA A 97 15366 16593 15171 -608 -1308 -1535 C ATOM 672 N ILE A 98 31.545 -30.131 -22.268 1.00119.49 N ANISOU 672 N ILE A 98 14494 15794 15113 -835 -1251 -1571 N ATOM 673 CA ILE A 98 32.483 -29.264 -22.972 1.00118.00 C ANISOU 673 CA ILE A 98 14150 15570 15116 -919 -1249 -1566 C ATOM 674 C ILE A 98 32.567 -27.895 -22.305 1.00120.90 C ANISOU 674 C ILE A 98 14441 15847 15649 -1039 -1256 -1743 C ATOM 675 O ILE A 98 33.649 -27.325 -22.170 1.00120.75 O ANISOU 675 O ILE A 98 14285 15866 15730 -1115 -1312 -1826 O ATOM 676 CB ILE A 98 32.094 -29.091 -24.453 1.00115.02 C ANISOU 676 CB ILE A 98 13769 15064 14870 -918 -1158 -1383 C ATOM 677 CG1 ILE A 98 32.214 -30.425 -25.193 1.00112.11 C ANISOU 677 CG1 ILE A 98 13475 14782 14338 -792 -1174 -1215 C ATOM 678 CG2 ILE A 98 32.967 -28.040 -25.116 1.00114.50 C ANISOU 678 CG2 ILE A 98 13549 14935 15023 -1014 -1125 -1374 C ATOM 679 CD1 ILE A 98 31.926 -30.331 -26.674 1.00109.95 C ANISOU 679 CD1 ILE A 98 13216 14395 14166 -761 -1103 -1038 C ATOM 680 N ALA A 99 31.418 -27.373 -21.886 1.00129.76 N ANISOU 680 N ALA A 99 15649 16848 16805 -1055 -1202 -1802 N ATOM 681 CA ALA A 99 31.371 -26.092 -21.194 1.00139.34 C ANISOU 681 CA ALA A 99 16827 17960 18155 -1149 -1212 -1979 C ATOM 682 C ALA A 99 32.165 -26.160 -19.894 1.00145.45 C ANISOU 682 C ALA A 99 17584 18868 18812 -1144 -1337 -2172 C ATOM 683 O ALA A 99 33.000 -25.299 -19.617 1.00149.99 O ANISOU 683 O ALA A 99 18050 19422 19519 -1241 -1406 -2303 O ATOM 684 CB ALA A 99 29.931 -25.690 -20.918 1.00139.76 C ANISOU 684 CB ALA A 99 16994 17885 18222 -1128 -1128 -1999 C ATOM 685 N ILE A 100 31.893 -27.190 -19.099 1.00143.77 N ANISOU 685 N ILE A 100 17484 18786 18355 -1028 -1370 -2189 N ATOM 686 CA ILE A 100 32.605 -27.402 -17.845 1.00143.26 C ANISOU 686 CA ILE A 100 17432 18864 18136 -984 -1495 -2365 C ATOM 687 C ILE A 100 34.099 -27.553 -18.100 1.00141.07 C ANISOU 687 C ILE A 100 16998 18711 17890 -1018 -1603 -2381 C ATOM 688 O ILE A 100 34.924 -26.976 -17.392 1.00142.71 O ANISOU 688 O ILE A 100 17123 18960 18139 -1068 -1720 -2561 O ATOM 689 CB ILE A 100 32.096 -28.660 -17.115 1.00139.97 C ANISOU 689 CB ILE A 100 17177 18572 17435 -835 -1491 -2334 C ATOM 690 CG1 ILE A 100 30.610 -28.519 -16.778 1.00131.56 C ANISOU 690 CG1 ILE A 100 16244 17395 16346 -801 -1373 -2316 C ATOM 691 CG2 ILE A 100 32.913 -28.914 -15.857 1.00142.62 C ANISOU 691 CG2 ILE A 100 17537 19063 17590 -764 -1627 -2513 C ATOM 692 CD1 ILE A 100 30.009 -29.742 -16.123 1.00123.81 C ANISOU 692 CD1 ILE A 100 15418 16512 15112 -668 -1339 -2259 C ATOM 693 N ASP A 101 34.436 -28.338 -19.119 1.00136.72 N ANISOU 693 N ASP A 101 16406 18220 17321 -984 -1569 -2194 N ATOM 694 CA ASP A 101 35.825 -28.572 -19.496 1.00131.28 C ANISOU 694 CA ASP A 101 15559 17662 16661 -997 -1647 -2173 C ATOM 695 C ASP A 101 36.550 -27.267 -19.808 1.00123.36 C ANISOU 695 C ASP A 101 14364 16566 15942 -1161 -1664 -2248 C ATOM 696 O ASP A 101 37.605 -26.980 -19.241 1.00112.13 O ANISOU 696 O ASP A 101 12811 15236 14558 -1207 -1787 -2389 O ATOM 697 CB ASP A 101 35.894 -29.505 -20.705 1.00128.47 C ANISOU 697 CB ASP A 101 15211 17347 16255 -924 -1578 -1938 C ATOM 698 CG ASP A 101 37.306 -29.691 -21.214 1.00128.70 C ANISOU 698 CG ASP A 101 15064 17509 16328 -926 -1632 -1892 C ATOM 699 OD1 ASP A 101 38.207 -29.953 -20.389 1.00137.00 O ANISOU 699 OD1 ASP A 101 16050 18722 17281 -894 -1758 -2018 O ATOM 700 OD2 ASP A 101 37.512 -29.579 -22.440 1.00122.53 O ANISOU 700 OD2 ASP A 101 14208 16673 15673 -948 -1547 -1727 O ATOM 701 N ARG A 102 35.980 -26.480 -20.714 1.00128.42 N ANISOU 701 N ARG A 102 14990 17016 16788 -1248 -1543 -2153 N ATOM 702 CA ARG A 102 36.576 -25.208 -21.108 1.00132.31 C ANISOU 702 CA ARG A 102 15318 17385 17569 -1411 -1532 -2199 C ATOM 703 C ARG A 102 36.663 -24.245 -19.930 1.00133.59 C ANISOU 703 C ARG A 102 15469 17487 17801 -1500 -1636 -2454 C ATOM 704 O ARG A 102 37.409 -23.267 -19.971 1.00136.98 O ANISOU 704 O ARG A 102 15746 17843 18456 -1645 -1678 -2541 O ATOM 705 CB ARG A 102 35.791 -24.577 -22.260 1.00136.42 C ANISOU 705 CB ARG A 102 15870 17700 18265 -1459 -1373 -2046 C ATOM 706 CG ARG A 102 35.817 -25.380 -23.554 1.00140.64 C ANISOU 706 CG ARG A 102 16408 18271 18757 -1373 -1280 -1798 C ATOM 707 CD ARG A 102 37.209 -25.416 -24.174 1.00147.34 C ANISOU 707 CD ARG A 102 17062 19215 19706 -1411 -1289 -1721 C ATOM 708 NE ARG A 102 38.148 -26.223 -23.400 1.00154.53 N ANISOU 708 NE ARG A 102 17905 20354 20454 -1354 -1424 -1807 N ATOM 709 CZ ARG A 102 39.439 -26.353 -23.690 1.00160.93 C ANISOU 709 CZ ARG A 102 18525 21293 21326 -1374 -1459 -1771 C ATOM 710 NH1 ARG A 102 39.949 -25.725 -24.740 1.00163.51 N ANISOU 710 NH1 ARG A 102 18711 21537 21879 -1456 -1353 -1641 N ATOM 711 NH2 ARG A 102 40.220 -27.108 -22.929 1.00162.09 N ANISOU 711 NH2 ARG A 102 18623 21655 21310 -1303 -1592 -1860 N ATOM 712 N TYR A 103 35.897 -24.527 -18.882 1.00134.14 N ANISOU 712 N TYR A 103 15706 17583 17678 -1409 -1676 -2571 N ATOM 713 CA TYR A 103 35.950 -23.728 -17.665 1.00140.93 C ANISOU 713 CA TYR A 103 16594 18401 18552 -1452 -1789 -2824 C ATOM 714 C TYR A 103 37.099 -24.181 -16.773 1.00147.43 C ANISOU 714 C TYR A 103 17339 19424 19254 -1415 -1975 -2975 C ATOM 715 O TYR A 103 37.843 -23.360 -16.239 1.00150.64 O ANISOU 715 O TYR A 103 17637 19804 19794 -1517 -2104 -3162 O ATOM 716 CB TYR A 103 34.629 -23.815 -16.899 1.00141.26 C ANISOU 716 CB TYR A 103 16854 18390 18428 -1347 -1739 -2879 C ATOM 717 CG TYR A 103 34.656 -23.095 -15.570 1.00150.07 C ANISOU 717 CG TYR A 103 18035 19476 19507 -1348 -1859 -3143 C ATOM 718 CD1 TYR A 103 34.424 -21.728 -15.496 1.00155.78 C ANISOU 718 CD1 TYR A 103 18752 19995 20441 -1464 -1856 -3262 C ATOM 719 CD2 TYR A 103 34.922 -23.780 -14.390 1.00154.53 C ANISOU 719 CD2 TYR A 103 18686 20211 19818 -1219 -1979 -3276 C ATOM 720 CE1 TYR A 103 34.451 -21.063 -14.285 1.00162.98 C ANISOU 720 CE1 TYR A 103 19743 20870 21310 -1451 -1978 -3513 C ATOM 721 CE2 TYR A 103 34.951 -23.123 -13.174 1.00161.46 C ANISOU 721 CE2 TYR A 103 19643 21060 20644 -1197 -2099 -3525 C ATOM 722 CZ TYR A 103 34.716 -21.765 -13.127 1.00166.40 C ANISOU 722 CZ TYR A 103 20263 21480 21482 -1313 -2102 -3646 C ATOM 723 OH TYR A 103 34.743 -21.106 -11.919 1.00171.46 O ANISOU 723 OH TYR A 103 21001 22082 22061 -1278 -2233 -3902 O ATOM 724 N ILE A 104 37.236 -25.494 -16.617 1.00150.05 N ANISOU 724 N ILE A 104 17729 19949 19335 -1266 -1995 -2898 N ATOM 725 CA ILE A 104 38.290 -26.067 -15.787 1.00152.69 C ANISOU 725 CA ILE A 104 18007 20493 19516 -1194 -2170 -3027 C ATOM 726 C ILE A 104 39.673 -25.647 -16.276 1.00148.14 C ANISOU 726 C ILE A 104 17162 19969 19157 -1320 -2256 -3045 C ATOM 727 O ILE A 104 40.572 -25.382 -15.477 1.00144.29 O ANISOU 727 O ILE A 104 16571 19571 18681 -1345 -2435 -3241 O ATOM 728 CB ILE A 104 38.211 -27.606 -15.763 1.00155.56 C ANISOU 728 CB ILE A 104 18482 21042 19583 -1008 -2152 -2897 C ATOM 729 CG1 ILE A 104 36.838 -28.062 -15.262 1.00158.39 C ANISOU 729 CG1 ILE A 104 19091 21347 19744 -895 -2056 -2867 C ATOM 730 CG2 ILE A 104 39.321 -28.186 -14.898 1.00156.07 C ANISOU 730 CG2 ILE A 104 18494 21327 19478 -915 -2338 -3034 C ATOM 731 CD1 ILE A 104 36.650 -29.563 -15.268 1.00158.65 C ANISOU 731 CD1 ILE A 104 19254 21525 19502 -727 -2024 -2726 C ATOM 732 N ALA A 105 39.834 -25.586 -17.594 1.00144.07 N ANISOU 732 N ALA A 105 16530 19398 18813 -1393 -2127 -2837 N ATOM 733 CA ALA A 105 41.109 -25.219 -18.199 1.00136.53 C ANISOU 733 CA ALA A 105 15306 18490 18080 -1511 -2166 -2809 C ATOM 734 C ALA A 105 41.518 -23.796 -17.836 1.00143.26 C ANISOU 734 C ALA A 105 16022 19193 19216 -1709 -2247 -2997 C ATOM 735 O ALA A 105 42.633 -23.561 -17.370 1.00156.86 O ANISOU 735 O ALA A 105 17558 21012 21028 -1777 -2406 -3138 O ATOM 736 CB ALA A 105 41.045 -25.385 -19.710 1.00124.85 C ANISOU 736 CB ALA A 105 13768 16954 16715 -1529 -1982 -2534 C ATOM 737 N ILE A 106 40.612 -22.848 -18.050 1.00137.23 N ANISOU 737 N ILE A 106 15353 18189 18599 -1801 -2146 -3001 N ATOM 738 CA ILE A 106 40.899 -21.444 -17.779 1.00142.83 C ANISOU 738 CA ILE A 106 15964 18716 19588 -1994 -2210 -3169 C ATOM 739 C ILE A 106 40.896 -21.135 -16.283 1.00151.07 C ANISOU 739 C ILE A 106 17098 19779 20524 -1968 -2412 -3469 C ATOM 740 O ILE A 106 41.718 -20.355 -15.800 1.00154.96 O ANISOU 740 O ILE A 106 17445 20236 21196 -2101 -2569 -3658 O ATOM 741 CB ILE A 106 39.905 -20.516 -18.505 1.00139.93 C ANISOU 741 CB ILE A 106 15692 18078 19400 -2080 -2033 -3075 C ATOM 742 CG1 ILE A 106 40.049 -20.674 -20.020 1.00136.34 C ANISOU 742 CG1 ILE A 106 15136 17589 19078 -2110 -1847 -2792 C ATOM 743 CG2 ILE A 106 40.129 -19.068 -18.098 1.00144.89 C ANISOU 743 CG2 ILE A 106 16260 18498 20294 -2268 -2111 -3269 C ATOM 744 CD1 ILE A 106 39.194 -19.715 -20.818 1.00137.00 C ANISOU 744 CD1 ILE A 106 15298 17406 19352 -2191 -1678 -2694 C ATOM 745 N ALA A 107 39.973 -21.753 -15.553 1.00155.17 N ANISOU 745 N ALA A 107 17857 20351 20750 -1791 -2409 -3510 N ATOM 746 CA ALA A 107 39.875 -21.544 -14.113 1.00164.42 C ANISOU 746 CA ALA A 107 19155 21547 21769 -1722 -2584 -3781 C ATOM 747 C ALA A 107 41.093 -22.109 -13.391 1.00170.03 C ANISOU 747 C ALA A 107 19743 22488 22372 -1669 -2802 -3922 C ATOM 748 O ALA A 107 41.833 -21.375 -12.734 1.00172.52 O ANISOU 748 O ALA A 107 19955 22781 22814 -1763 -2995 -4151 O ATOM 749 CB ALA A 107 38.597 -22.166 -13.569 1.00165.19 C ANISOU 749 CB ALA A 107 19533 21660 21573 -1531 -2495 -3754 C ATOM 750 N ILE A 108 41.298 -23.416 -13.518 1.00173.34 N ANISOU 750 N ILE A 108 20177 23125 22558 -1513 -2781 -3791 N ATOM 751 CA ILE A 108 42.428 -24.077 -12.877 1.00180.49 C ANISOU 751 CA ILE A 108 20976 24270 23330 -1429 -2980 -3905 C ATOM 752 C ILE A 108 43.242 -24.869 -13.897 1.00181.24 C ANISOU 752 C ILE A 108 20877 24522 23462 -1425 -2920 -3690 C ATOM 753 O ILE A 108 43.088 -26.085 -14.013 1.00182.09 O ANISOU 753 O ILE A 108 21088 24786 23312 -1249 -2865 -3553 O ATOM 754 CB ILE A 108 41.963 -25.027 -11.758 1.00182.22 C ANISOU 754 CB ILE A 108 21447 24636 23154 -1184 -3045 -3990 C ATOM 755 CG1 ILE A 108 40.849 -24.378 -10.933 1.00179.36 C ANISOU 755 CG1 ILE A 108 21323 24106 22718 -1149 -3024 -4130 C ATOM 756 CG2 ILE A 108 43.137 -25.424 -10.875 1.00185.04 C ANISOU 756 CG2 ILE A 108 21709 25212 23386 -1097 -3296 -4180 C ATOM 757 CD1 ILE A 108 40.282 -25.275 -9.857 1.00176.88 C ANISOU 757 CD1 ILE A 108 21272 23916 22018 -903 -3046 -4187 C ATOM 758 N PRO A 109 44.116 -24.174 -14.641 1.00176.55 N ANISOU 758 N PRO A 109 20008 23882 23192 -1615 -2924 -3655 N ATOM 759 CA PRO A 109 44.925 -24.787 -15.702 1.00175.78 C ANISOU 759 CA PRO A 109 19706 23918 23162 -1617 -2844 -3437 C ATOM 760 C PRO A 109 45.794 -25.930 -15.187 1.00181.61 C ANISOU 760 C PRO A 109 20394 24953 23656 -1440 -2991 -3474 C ATOM 761 O PRO A 109 45.988 -26.920 -15.893 1.00178.05 O ANISOU 761 O PRO A 109 19931 24639 23081 -1324 -2895 -3266 O ATOM 762 CB PRO A 109 45.810 -23.629 -16.186 1.00172.12 C ANISOU 762 CB PRO A 109 18945 23348 23105 -1865 -2871 -3474 C ATOM 763 CG PRO A 109 45.729 -22.588 -15.111 1.00172.60 C ANISOU 763 CG PRO A 109 19040 23276 23266 -1971 -3047 -3770 C ATOM 764 CD PRO A 109 44.371 -22.731 -14.518 1.00172.81 C ANISOU 764 CD PRO A 109 19406 23209 23046 -1840 -2994 -3815 C ATOM 765 N LEU A 110 46.305 -25.792 -13.969 1.00191.21 N ANISOU 765 N LEU A 110 21593 26263 24794 -1407 -3228 -3741 N ATOM 766 CA LEU A 110 47.183 -26.801 -13.387 1.00197.61 C ANISOU 766 CA LEU A 110 22353 27357 25371 -1229 -3393 -3805 C ATOM 767 C LEU A 110 46.440 -28.101 -13.104 1.00197.63 C ANISOU 767 C LEU A 110 22654 27469 24969 -972 -3322 -3704 C ATOM 768 O LEU A 110 46.804 -29.162 -13.612 1.00196.44 O ANISOU 768 O LEU A 110 22484 27486 24668 -840 -3269 -3533 O ATOM 769 CB LEU A 110 47.823 -26.272 -12.102 1.00201.92 C ANISOU 769 CB LEU A 110 22836 27959 25924 -1243 -3680 -4135 C ATOM 770 CG LEU A 110 48.711 -25.038 -12.267 1.00206.25 C ANISOU 770 CG LEU A 110 23067 28415 26885 -1506 -3794 -4264 C ATOM 771 CD1 LEU A 110 49.224 -24.559 -10.919 1.00210.74 C ANISOU 771 CD1 LEU A 110 23617 29024 27430 -1499 -4105 -4613 C ATOM 772 CD2 LEU A 110 49.865 -25.335 -13.212 1.00207.82 C ANISOU 772 CD2 LEU A 110 22927 28766 27268 -1570 -3759 -4098 C ATOM 773 N ARG A 111 45.397 -28.012 -12.287 1.00197.64 N ANISOU 773 N ARG A 111 22933 27367 24796 -899 -3316 -3807 N ATOM 774 CA ARG A 111 44.610 -29.185 -11.926 1.00197.87 C ANISOU 774 CA ARG A 111 23253 27474 24455 -670 -3239 -3717 C ATOM 775 C ARG A 111 43.825 -29.722 -13.119 1.00194.40 C ANISOU 775 C ARG A 111 22894 26951 24016 -669 -2989 -3418 C ATOM 776 O ARG A 111 43.229 -30.797 -13.044 1.00198.14 O ANISOU 776 O ARG A 111 23584 27486 24216 -498 -2909 -3300 O ATOM 777 CB ARG A 111 43.656 -28.859 -10.776 1.00203.15 C ANISOU 777 CB ARG A 111 24184 28039 24963 -601 -3271 -3891 C ATOM 778 CG ARG A 111 44.352 -28.515 -9.469 1.00210.39 C ANISOU 778 CG ARG A 111 25088 29052 25797 -540 -3537 -4198 C ATOM 779 CD ARG A 111 45.190 -29.684 -8.972 1.00216.52 C ANISOU 779 CD ARG A 111 25872 30104 26292 -325 -3674 -4222 C ATOM 780 NE ARG A 111 44.406 -30.914 -8.874 1.00219.64 N ANISOU 780 NE ARG A 111 26543 30559 26351 -115 -3531 -4057 N ATOM 781 CZ ARG A 111 43.632 -31.230 -7.840 1.00223.95 C ANISOU 781 CZ ARG A 111 27381 31093 26615 53 -3526 -4140 C ATOM 782 NH1 ARG A 111 43.531 -30.404 -6.807 1.00228.61 N ANISOU 782 NH1 ARG A 111 28041 31621 27199 57 -3663 -4393 N ATOM 783 NH2 ARG A 111 42.954 -32.369 -7.838 1.00221.89 N ANISOU 783 NH2 ARG A 111 27349 30876 26081 222 -3382 -3966 N ATOM 784 N TYR A 112 43.824 -28.971 -14.217 1.00188.64 N ANISOU 784 N TYR A 112 22001 26077 23596 -856 -2871 -3297 N ATOM 785 CA TYR A 112 43.106 -29.378 -15.421 1.00182.83 C ANISOU 785 CA TYR A 112 21335 25251 22881 -856 -2649 -3024 C ATOM 786 C TYR A 112 43.533 -30.765 -15.886 1.00179.27 C ANISOU 786 C TYR A 112 20909 24994 22211 -681 -2624 -2848 C ATOM 787 O TYR A 112 42.696 -31.634 -16.124 1.00176.46 O ANISOU 787 O TYR A 112 20768 24621 21659 -562 -2514 -2702 O ATOM 788 CB TYR A 112 43.312 -28.361 -16.546 1.00181.27 C ANISOU 788 CB TYR A 112 20930 24896 23048 -1065 -2544 -2926 C ATOM 789 CG TYR A 112 42.765 -28.809 -17.884 1.00176.95 C ANISOU 789 CG TYR A 112 20435 24279 22521 -1044 -2337 -2642 C ATOM 790 CD1 TYR A 112 43.580 -29.442 -18.815 1.00176.19 C ANISOU 790 CD1 TYR A 112 20201 24311 22431 -992 -2294 -2463 C ATOM 791 CD2 TYR A 112 41.433 -28.601 -18.216 1.00172.08 C ANISOU 791 CD2 TYR A 112 20005 23468 21909 -1060 -2191 -2557 C ATOM 792 CE1 TYR A 112 43.084 -29.853 -20.039 1.00171.37 C ANISOU 792 CE1 TYR A 112 19659 23631 21823 -953 -2118 -2213 C ATOM 793 CE2 TYR A 112 40.928 -29.008 -19.439 1.00167.14 C ANISOU 793 CE2 TYR A 112 19431 22775 21298 -1031 -2025 -2312 C ATOM 794 CZ TYR A 112 41.758 -29.634 -20.345 1.00165.02 C ANISOU 794 CZ TYR A 112 19045 22630 21026 -974 -1993 -2144 C ATOM 795 OH TYR A 112 41.263 -30.044 -21.562 1.00158.21 O ANISOU 795 OH TYR A 112 18255 21696 20162 -925 -1842 -1909 O ATOM 796 N ASN A 113 44.839 -30.967 -16.011 1.00177.75 N ANISOU 796 N ASN A 113 20496 24983 22060 -665 -2731 -2865 N ATOM 797 CA ASN A 113 45.370 -32.246 -16.461 1.00172.87 C ANISOU 797 CA ASN A 113 19889 24559 21235 -486 -2718 -2705 C ATOM 798 C ASN A 113 45.246 -33.327 -15.392 1.00164.03 C ANISOU 798 C ASN A 113 18993 23592 19740 -263 -2822 -2789 C ATOM 799 O ASN A 113 45.255 -34.520 -15.697 1.00155.62 O ANISOU 799 O ASN A 113 18051 22635 18444 -90 -2779 -2640 O ATOM 800 CB ASN A 113 46.826 -32.091 -16.901 1.00178.16 C ANISOU 800 CB ASN A 113 20234 25388 22072 -529 -2794 -2697 C ATOM 801 CG ASN A 113 47.000 -31.028 -17.969 1.00179.20 C ANISOU 801 CG ASN A 113 20143 25365 22578 -747 -2671 -2596 C ATOM 802 OD1 ASN A 113 46.769 -31.276 -19.153 1.00177.66 O ANISOU 802 OD1 ASN A 113 19959 25113 22430 -736 -2497 -2360 O ATOM 803 ND2 ASN A 113 47.407 -29.833 -17.554 1.00180.88 N ANISOU 803 ND2 ASN A 113 20166 25502 23059 -939 -2765 -2776 N ATOM 804 N GLY A 114 45.127 -32.900 -14.138 1.00163.59 N ANISOU 804 N GLY A 114 19005 23534 19618 -258 -2958 -3028 N ATOM 805 CA GLY A 114 44.984 -33.824 -13.029 1.00164.50 C ANISOU 805 CA GLY A 114 19349 23779 19373 -39 -3052 -3120 C ATOM 806 C GLY A 114 43.561 -34.320 -12.866 1.00167.89 C ANISOU 806 C GLY A 114 20095 24076 19619 34 -2899 -3022 C ATOM 807 O GLY A 114 43.333 -35.451 -12.439 1.00169.33 O ANISOU 807 O GLY A 114 20490 24353 19494 229 -2893 -2970 O ATOM 808 N LEU A 115 42.601 -33.467 -13.209 1.00169.04 N ANISOU 808 N LEU A 115 20268 23999 19962 -124 -2774 -2995 N ATOM 809 CA LEU A 115 41.188 -33.815 -13.113 1.00159.05 C ANISOU 809 CA LEU A 115 19264 22596 18571 -80 -2620 -2899 C ATOM 810 C LEU A 115 40.656 -34.302 -14.457 1.00154.66 C ANISOU 810 C LEU A 115 18728 21953 18083 -112 -2445 -2631 C ATOM 811 O LEU A 115 40.211 -35.442 -14.583 1.00153.09 O ANISOU 811 O LEU A 115 18711 21788 17668 22 -2379 -2489 O ATOM 812 CB LEU A 115 40.372 -32.614 -12.631 1.00151.96 C ANISOU 812 CB LEU A 115 18401 21511 17827 -207 -2589 -3034 C ATOM 813 CG LEU A 115 40.749 -32.043 -11.263 1.00152.32 C ANISOU 813 CG LEU A 115 18466 21609 17801 -168 -2766 -3316 C ATOM 814 CD1 LEU A 115 39.976 -30.764 -10.981 1.00147.78 C ANISOU 814 CD1 LEU A 115 17913 20826 17410 -303 -2727 -3435 C ATOM 815 CD2 LEU A 115 40.515 -33.071 -10.165 1.00155.09 C ANISOU 815 CD2 LEU A 115 19067 22086 17774 68 -2804 -3362 C ATOM 816 N VAL A 116 40.706 -33.428 -15.456 1.00154.75 N ANISOU 816 N VAL A 116 18562 21842 18395 -285 -2376 -2564 N ATOM 817 CA VAL A 116 40.259 -33.768 -16.801 1.00154.03 C ANISOU 817 CA VAL A 116 18480 21660 18383 -310 -2224 -2321 C ATOM 818 C VAL A 116 41.178 -34.812 -17.425 1.00157.31 C ANISOU 818 C VAL A 116 18847 22249 18675 -185 -2253 -2185 C ATOM 819 O VAL A 116 42.188 -34.474 -18.043 1.00162.71 O ANISOU 819 O VAL A 116 19305 23001 19515 -238 -2281 -2158 O ATOM 820 CB VAL A 116 40.212 -32.524 -17.710 1.00149.00 C ANISOU 820 CB VAL A 116 17664 20858 18091 -509 -2146 -2286 C ATOM 821 CG1 VAL A 116 39.674 -32.890 -19.084 1.00142.09 C ANISOU 821 CG1 VAL A 116 16830 19885 17273 -507 -1994 -2039 C ATOM 822 CG2 VAL A 116 39.364 -31.434 -17.074 1.00146.96 C ANISOU 822 CG2 VAL A 116 17455 20427 17955 -623 -2127 -2433 C ATOM 823 N THR A 117 40.825 -36.082 -17.254 1.00152.71 N ANISOU 823 N THR A 117 18477 21733 17812 -15 -2238 -2094 N ATOM 824 CA THR A 117 41.632 -37.179 -17.775 1.00150.51 C ANISOU 824 CA THR A 117 18197 21617 17374 137 -2269 -1966 C ATOM 825 C THR A 117 40.959 -37.840 -18.972 1.00150.50 C ANISOU 825 C THR A 117 18317 21509 17357 170 -2137 -1728 C ATOM 826 O THR A 117 39.745 -37.732 -19.150 1.00150.93 O ANISOU 826 O THR A 117 18507 21386 17453 110 -2038 -1671 O ATOM 827 CB THR A 117 41.891 -38.249 -16.698 1.00147.87 C ANISOU 827 CB THR A 117 18034 21447 16704 335 -2371 -2040 C ATOM 828 OG1 THR A 117 40.658 -38.895 -16.356 1.00145.02 O ANISOU 828 OG1 THR A 117 17949 20976 16175 392 -2286 -1979 O ATOM 829 CG2 THR A 117 42.489 -37.615 -15.451 1.00150.70 C ANISOU 829 CG2 THR A 117 18300 21906 17052 325 -2521 -2293 C ATOM 830 N GLY A 118 41.753 -38.524 -19.790 1.00152.72 N ANISOU 830 N GLY A 118 18549 21902 17576 275 -2143 -1593 N ATOM 831 CA GLY A 118 41.232 -39.218 -20.952 1.00158.10 C ANISOU 831 CA GLY A 118 19359 22492 18220 335 -2044 -1375 C ATOM 832 C GLY A 118 40.329 -40.372 -20.567 1.00165.59 C ANISOU 832 C GLY A 118 20605 23397 18914 452 -2033 -1319 C ATOM 833 O GLY A 118 39.472 -40.789 -21.346 1.00165.26 O ANISOU 833 O GLY A 118 20703 23214 18873 455 -1953 -1172 O ATOM 834 N THR A 119 40.523 -40.889 -19.357 1.00172.99 N ANISOU 834 N THR A 119 21642 24451 19635 549 -2117 -1438 N ATOM 835 CA THR A 119 39.725 -42.005 -18.861 1.00174.30 C ANISOU 835 CA THR A 119 22094 24578 19552 662 -2099 -1386 C ATOM 836 C THR A 119 38.360 -41.541 -18.364 1.00172.79 C ANISOU 836 C THR A 119 22004 24207 19442 541 -2015 -1426 C ATOM 837 O THR A 119 37.328 -42.069 -18.778 1.00172.26 O ANISOU 837 O THR A 119 22098 23997 19356 532 -1932 -1300 O ATOM 838 CB THR A 119 40.447 -42.757 -17.728 1.00177.29 C ANISOU 838 CB THR A 119 22562 25150 19649 836 -2209 -1489 C ATOM 839 OG1 THR A 119 41.711 -43.239 -18.201 1.00180.01 O ANISOU 839 OG1 THR A 119 22808 25675 19911 966 -2287 -1445 O ATOM 840 CG2 THR A 119 39.605 -43.931 -17.248 1.00174.66 C ANISOU 840 CG2 THR A 119 22540 24758 19065 949 -2169 -1415 C ATOM 841 N ARG A 120 38.361 -40.552 -17.475 1.00171.71 N ANISOU 841 N ARG A 120 21768 24077 19397 453 -2040 -1605 N ATOM 842 CA ARG A 120 37.119 -40.004 -16.938 1.00169.15 C ANISOU 842 CA ARG A 120 21523 23595 19150 351 -1955 -1655 C ATOM 843 C ARG A 120 36.198 -39.531 -18.057 1.00165.25 C ANISOU 843 C ARG A 120 20993 22905 18888 216 -1843 -1528 C ATOM 844 O ARG A 120 34.974 -39.599 -17.938 1.00163.84 O ANISOU 844 O ARG A 120 20934 22587 18728 174 -1752 -1483 O ATOM 845 CB ARG A 120 37.402 -38.851 -15.972 1.00171.27 C ANISOU 845 CB ARG A 120 21670 23895 19511 278 -2014 -1875 C ATOM 846 CG ARG A 120 38.081 -39.266 -14.675 1.00175.43 C ANISOU 846 CG ARG A 120 22269 24596 19790 424 -2131 -2027 C ATOM 847 CD ARG A 120 38.228 -38.081 -13.731 1.00180.30 C ANISOU 847 CD ARG A 120 22788 25214 20502 351 -2199 -2255 C ATOM 848 NE ARG A 120 38.884 -38.448 -12.479 1.00184.50 N ANISOU 848 NE ARG A 120 23399 25915 20789 509 -2329 -2415 N ATOM 849 CZ ARG A 120 39.099 -37.607 -11.473 1.00186.56 C ANISOU 849 CZ ARG A 120 23620 26200 21063 496 -2424 -2636 C ATOM 850 NH1 ARG A 120 39.704 -38.029 -10.371 1.00188.12 N ANISOU 850 NH1 ARG A 120 23907 26556 21013 666 -2553 -2776 N ATOM 851 NH2 ARG A 120 38.709 -36.343 -11.568 1.00185.93 N ANISOU 851 NH2 ARG A 120 23426 25983 21238 325 -2397 -2722 N ATOM 852 N ALA A 121 36.795 -39.048 -19.143 1.00165.65 N ANISOU 852 N ALA A 121 20873 22950 19117 157 -1846 -1468 N ATOM 853 CA ALA A 121 36.033 -38.596 -20.300 1.00164.98 C ANISOU 853 CA ALA A 121 20757 22688 19241 53 -1749 -1344 C ATOM 854 C ALA A 121 35.159 -39.721 -20.841 1.00165.60 C ANISOU 854 C ALA A 121 21039 22680 19201 126 -1702 -1176 C ATOM 855 O ALA A 121 33.945 -39.567 -20.975 1.00165.97 O ANISOU 855 O ALA A 121 21157 22569 19335 54 -1625 -1134 O ATOM 856 CB ALA A 121 36.969 -38.081 -21.383 1.00164.79 C ANISOU 856 CB ALA A 121 20541 22693 19380 20 -1755 -1284 C ATOM 857 N ALA A 122 35.787 -40.853 -21.145 1.00164.75 N ANISOU 857 N ALA A 122 21022 22675 18899 272 -1756 -1085 N ATOM 858 CA ALA A 122 35.069 -42.016 -21.652 1.00162.47 C ANISOU 858 CA ALA A 122 20944 22303 18486 349 -1735 -932 C ATOM 859 C ALA A 122 34.014 -42.486 -20.656 1.00159.95 C ANISOU 859 C ALA A 122 20794 21916 18062 340 -1695 -960 C ATOM 860 O ALA A 122 32.938 -42.942 -21.044 1.00161.86 O ANISOU 860 O ALA A 122 21157 22012 18332 310 -1644 -856 O ATOM 861 CB ALA A 122 36.042 -43.142 -21.968 1.00162.24 C ANISOU 861 CB ALA A 122 20997 22409 18236 527 -1810 -853 C ATOM 862 N GLY A 123 34.330 -42.370 -19.369 1.00153.93 N ANISOU 862 N GLY A 123 20039 21263 17184 371 -1719 -1100 N ATOM 863 CA GLY A 123 33.408 -42.760 -18.319 1.00147.34 C ANISOU 863 CA GLY A 123 19364 20380 16237 381 -1662 -1127 C ATOM 864 C GLY A 123 32.173 -41.882 -18.288 1.00140.57 C ANISOU 864 C GLY A 123 18457 19361 15592 231 -1560 -1144 C ATOM 865 O GLY A 123 31.048 -42.376 -18.354 1.00139.57 O ANISOU 865 O GLY A 123 18446 19108 15474 203 -1483 -1048 O ATOM 866 N ILE A 124 32.386 -40.573 -18.188 1.00134.13 N ANISOU 866 N ILE A 124 17464 18544 14956 134 -1560 -1266 N ATOM 867 CA ILE A 124 31.285 -39.617 -18.166 1.00125.32 C ANISOU 867 CA ILE A 124 16291 17280 14044 5 -1465 -1294 C ATOM 868 C ILE A 124 30.386 -39.796 -19.383 1.00122.94 C ANISOU 868 C ILE A 124 16000 16820 13891 -58 -1410 -1134 C ATOM 869 O ILE A 124 29.164 -39.858 -19.257 1.00126.98 O ANISOU 869 O ILE A 124 16571 17214 14461 -107 -1325 -1087 O ATOM 870 CB ILE A 124 31.796 -38.166 -18.125 1.00123.84 C ANISOU 870 CB ILE A 124 15911 17098 14046 -90 -1489 -1437 C ATOM 871 CG1 ILE A 124 32.596 -37.920 -16.845 1.00127.43 C ANISOU 871 CG1 ILE A 124 16357 17697 14365 -32 -1565 -1620 C ATOM 872 CG2 ILE A 124 30.635 -37.190 -18.221 1.00121.56 C ANISOU 872 CG2 ILE A 124 15578 16645 13966 -209 -1390 -1452 C ATOM 873 CD1 ILE A 124 33.150 -36.518 -16.730 1.00128.86 C ANISOU 873 CD1 ILE A 124 16353 17873 14734 -133 -1610 -1777 C ATOM 874 N ILE A 125 31.000 -39.880 -20.560 1.00121.57 N ANISOU 874 N ILE A 125 15766 16648 13778 -48 -1459 -1049 N ATOM 875 CA ILE A 125 30.258 -40.081 -21.799 1.00127.24 C ANISOU 875 CA ILE A 125 16506 17221 14617 -81 -1432 -903 C ATOM 876 C ILE A 125 29.320 -41.279 -21.692 1.00133.38 C ANISOU 876 C ILE A 125 17468 17929 15281 -43 -1413 -797 C ATOM 877 O ILE A 125 28.127 -41.173 -21.977 1.00136.77 O ANISOU 877 O ILE A 125 17911 18216 15841 -117 -1355 -743 O ATOM 878 CB ILE A 125 31.203 -40.285 -22.997 1.00127.10 C ANISOU 878 CB ILE A 125 16446 17243 14603 -20 -1494 -814 C ATOM 879 CG1 ILE A 125 32.014 -39.015 -23.256 1.00129.74 C ANISOU 879 CG1 ILE A 125 16577 17614 15105 -86 -1490 -894 C ATOM 880 CG2 ILE A 125 30.415 -40.669 -24.238 1.00123.98 C ANISOU 880 CG2 ILE A 125 16120 16698 14287 -19 -1486 -664 C ATOM 881 CD1 ILE A 125 32.981 -39.136 -24.409 1.00130.87 C ANISOU 881 CD1 ILE A 125 16660 17804 15260 -20 -1524 -796 C ATOM 882 N ALA A 126 29.868 -42.417 -21.277 1.00131.18 N ANISOU 882 N ALA A 126 17328 17747 14766 73 -1463 -768 N ATOM 883 CA ALA A 126 29.077 -43.629 -21.104 1.00129.58 C ANISOU 883 CA ALA A 126 17316 17473 14446 108 -1446 -666 C ATOM 884 C ALA A 126 27.889 -43.373 -20.183 1.00127.38 C ANISOU 884 C ALA A 126 17053 17118 14229 25 -1337 -699 C ATOM 885 O ALA A 126 26.757 -43.744 -20.495 1.00123.19 O ANISOU 885 O ALA A 126 16571 16448 13789 -36 -1291 -605 O ATOM 886 CB ALA A 126 29.943 -44.755 -20.558 1.00129.67 C ANISOU 886 CB ALA A 126 17480 17614 14176 255 -1506 -655 C ATOM 887 N ILE A 127 28.155 -42.736 -19.047 1.00129.18 N ANISOU 887 N ILE A 127 17234 17439 14409 30 -1299 -835 N ATOM 888 CA ILE A 127 27.107 -42.400 -18.092 1.00130.49 C ANISOU 888 CA ILE A 127 17414 17550 14615 -22 -1182 -874 C ATOM 889 C ILE A 127 26.049 -41.509 -18.733 1.00129.62 C ANISOU 889 C ILE A 127 17176 17296 14778 -152 -1117 -852 C ATOM 890 O ILE A 127 24.849 -41.743 -18.584 1.00132.62 O ANISOU 890 O ILE A 127 17587 17572 15229 -203 -1027 -783 O ATOM 891 CB ILE A 127 27.680 -41.680 -16.858 1.00133.28 C ANISOU 891 CB ILE A 127 17736 18028 14877 21 -1173 -1047 C ATOM 892 CG1 ILE A 127 28.713 -42.562 -16.156 1.00138.80 C ANISOU 892 CG1 ILE A 127 18564 18881 15293 169 -1246 -1078 C ATOM 893 CG2 ILE A 127 26.563 -41.296 -15.898 1.00132.36 C ANISOU 893 CG2 ILE A 127 17644 17853 14794 -12 -1038 -1081 C ATOM 894 CD1 ILE A 127 29.361 -41.904 -14.957 1.00144.24 C ANISOU 894 CD1 ILE A 127 19230 19699 15875 230 -1270 -1262 C ATOM 895 N CYS A 128 26.505 -40.486 -19.449 1.00125.24 N ANISOU 895 N CYS A 128 16473 16734 14379 -201 -1160 -907 N ATOM 896 CA CYS A 128 25.607 -39.546 -20.108 1.00124.58 C ANISOU 896 CA CYS A 128 16271 16517 14547 -306 -1107 -894 C ATOM 897 C CYS A 128 24.631 -40.260 -21.033 1.00124.87 C ANISOU 897 C CYS A 128 16354 16421 14668 -336 -1105 -742 C ATOM 898 O CYS A 128 23.435 -39.971 -21.025 1.00127.56 O ANISOU 898 O CYS A 128 16655 16657 15153 -405 -1028 -715 O ATOM 899 CB CYS A 128 26.406 -38.502 -20.889 1.00125.55 C ANISOU 899 CB CYS A 128 16253 16646 14805 -339 -1159 -950 C ATOM 900 SG CYS A 128 27.432 -37.429 -19.859 1.00136.11 S ANISOU 900 SG CYS A 128 17499 18104 16114 -342 -1176 -1150 S ATOM 901 N TRP A 129 25.145 -41.193 -21.828 1.00124.63 N ANISOU 901 N TRP A 129 16408 16396 14550 -278 -1197 -646 N ATOM 902 CA TRP A 129 24.308 -41.958 -22.746 1.00131.27 C ANISOU 902 CA TRP A 129 17314 17105 15458 -296 -1229 -511 C ATOM 903 C TRP A 129 23.271 -42.794 -22.005 1.00135.76 C ANISOU 903 C TRP A 129 17975 17617 15988 -326 -1160 -454 C ATOM 904 O TRP A 129 22.101 -42.828 -22.388 1.00134.78 O ANISOU 904 O TRP A 129 17818 17367 16027 -402 -1132 -390 O ATOM 905 CB TRP A 129 25.166 -42.851 -23.644 1.00131.13 C ANISOU 905 CB TRP A 129 17399 17111 15314 -201 -1347 -430 C ATOM 906 CG TRP A 129 25.829 -42.107 -24.758 1.00134.38 C ANISOU 906 CG TRP A 129 17715 17523 15822 -181 -1399 -430 C ATOM 907 CD1 TRP A 129 27.101 -41.617 -24.774 1.00137.08 C ANISOU 907 CD1 TRP A 129 17987 17989 16107 -131 -1421 -490 C ATOM 908 CD2 TRP A 129 25.250 -41.763 -26.022 1.00139.12 C ANISOU 908 CD2 TRP A 129 18276 17991 16594 -206 -1429 -362 C ATOM 909 NE1 TRP A 129 27.352 -40.991 -25.971 1.00139.11 N ANISOU 909 NE1 TRP A 129 18166 18196 16494 -127 -1444 -450 N ATOM 910 CE2 TRP A 129 26.231 -41.067 -26.755 1.00139.16 C ANISOU 910 CE2 TRP A 129 18200 18044 16629 -162 -1451 -374 C ATOM 911 CE3 TRP A 129 23.997 -41.977 -26.605 1.00143.38 C ANISOU 911 CE3 TRP A 129 18835 18376 17266 -255 -1443 -293 C ATOM 912 CZ2 TRP A 129 26.000 -40.582 -28.040 1.00141.46 C ANISOU 912 CZ2 TRP A 129 18456 18233 17061 -152 -1475 -313 C ATOM 913 CZ3 TRP A 129 23.768 -41.496 -27.882 1.00145.56 C ANISOU 913 CZ3 TRP A 129 19071 18555 17681 -242 -1489 -247 C ATOM 914 CH2 TRP A 129 24.765 -40.806 -28.585 1.00145.62 C ANISOU 914 CH2 TRP A 129 19021 18610 17696 -184 -1499 -254 C ATOM 915 N VAL A 130 23.705 -43.471 -20.948 1.00136.51 N ANISOU 915 N VAL A 130 18186 17809 15874 -262 -1133 -473 N ATOM 916 CA VAL A 130 22.798 -44.262 -20.127 1.00135.18 C ANISOU 916 CA VAL A 130 18115 17593 15656 -284 -1041 -411 C ATOM 917 C VAL A 130 21.671 -43.385 -19.595 1.00135.60 C ANISOU 917 C VAL A 130 18044 17594 15885 -373 -907 -446 C ATOM 918 O VAL A 130 20.498 -43.752 -19.663 1.00134.05 O ANISOU 918 O VAL A 130 17837 17285 15808 -446 -845 -356 O ATOM 919 CB VAL A 130 23.533 -44.924 -18.947 1.00133.17 C ANISOU 919 CB VAL A 130 18005 17465 15129 -177 -1016 -445 C ATOM 920 CG1 VAL A 130 22.542 -45.601 -18.015 1.00131.23 C ANISOU 920 CG1 VAL A 130 17855 17164 14843 -199 -884 -374 C ATOM 921 CG2 VAL A 130 24.561 -45.921 -19.457 1.00136.05 C ANISOU 921 CG2 VAL A 130 18506 17878 15308 -74 -1143 -395 C ATOM 922 N LEU A 131 22.038 -42.221 -19.070 1.00136.14 N ANISOU 922 N LEU A 131 18014 17740 15972 -365 -867 -578 N ATOM 923 CA LEU A 131 21.060 -41.265 -18.566 1.00139.98 C ANISOU 923 CA LEU A 131 18388 18185 16612 -426 -742 -626 C ATOM 924 C LEU A 131 20.208 -40.719 -19.704 1.00145.12 C ANISOU 924 C LEU A 131 18908 18707 17525 -517 -759 -577 C ATOM 925 O LEU A 131 19.061 -40.323 -19.498 1.00150.28 O ANISOU 925 O LEU A 131 19479 19292 18327 -573 -657 -559 O ATOM 926 CB LEU A 131 21.760 -40.117 -17.838 1.00141.92 C ANISOU 926 CB LEU A 131 18577 18531 16815 -390 -725 -793 C ATOM 927 CG LEU A 131 22.600 -40.509 -16.622 1.00147.59 C ANISOU 927 CG LEU A 131 19418 19388 17272 -283 -721 -870 C ATOM 928 CD1 LEU A 131 23.353 -39.305 -16.077 1.00152.22 C ANISOU 928 CD1 LEU A 131 19933 20057 17846 -258 -747 -1051 C ATOM 929 CD2 LEU A 131 21.726 -41.135 -15.546 1.00147.46 C ANISOU 929 CD2 LEU A 131 19506 19364 17159 -251 -576 -813 C ATOM 930 N SER A 132 20.776 -40.699 -20.905 1.00146.24 N ANISOU 930 N SER A 132 19032 18820 17715 -514 -886 -554 N ATOM 931 CA SER A 132 20.063 -40.218 -22.082 1.00148.60 C ANISOU 931 CA SER A 132 19229 18996 18238 -573 -923 -507 C ATOM 932 C SER A 132 18.955 -41.184 -22.484 1.00145.28 C ANISOU 932 C SER A 132 18840 18461 17897 -621 -934 -380 C ATOM 933 O SER A 132 17.876 -40.764 -22.901 1.00145.38 O ANISOU 933 O SER A 132 18747 18378 18112 -683 -907 -353 O ATOM 934 CB SER A 132 21.028 -40.007 -23.250 1.00154.29 C ANISOU 934 CB SER A 132 19945 19718 18960 -534 -1047 -505 C ATOM 935 OG SER A 132 21.958 -38.978 -22.961 1.00159.97 O ANISOU 935 OG SER A 132 20596 20522 19663 -517 -1033 -621 O ATOM 936 N PHE A 133 19.228 -42.479 -22.360 1.00140.98 N ANISOU 936 N PHE A 133 18443 17924 17199 -590 -980 -304 N ATOM 937 CA PHE A 133 18.225 -43.496 -22.651 1.00139.20 C ANISOU 937 CA PHE A 133 18262 17578 17048 -648 -998 -184 C ATOM 938 C PHE A 133 17.184 -43.565 -21.540 1.00142.60 C ANISOU 938 C PHE A 133 18649 18000 17534 -710 -831 -161 C ATOM 939 O PHE A 133 15.994 -43.738 -21.802 1.00144.05 O ANISOU 939 O PHE A 133 18752 18076 17905 -795 -805 -89 O ATOM 940 CB PHE A 133 18.879 -44.864 -22.855 1.00135.21 C ANISOU 940 CB PHE A 133 17950 17069 16354 -590 -1099 -110 C ATOM 941 CG PHE A 133 19.497 -45.042 -24.212 1.00135.41 C ANISOU 941 CG PHE A 133 18023 17055 16372 -535 -1270 -86 C ATOM 942 CD1 PHE A 133 18.741 -45.508 -25.274 1.00131.03 C ANISOU 942 CD1 PHE A 133 17479 16352 15955 -573 -1378 -8 C ATOM 943 CD2 PHE A 133 20.832 -44.744 -24.427 1.00141.02 C ANISOU 943 CD2 PHE A 133 18767 17878 16938 -435 -1323 -142 C ATOM 944 CE1 PHE A 133 19.303 -45.674 -26.526 1.00129.84 C ANISOU 944 CE1 PHE A 133 17395 16163 15776 -496 -1532 15 C ATOM 945 CE2 PHE A 133 21.400 -44.908 -25.677 1.00141.23 C ANISOU 945 CE2 PHE A 133 18841 17872 16948 -365 -1459 -106 C ATOM 946 CZ PHE A 133 20.633 -45.374 -26.728 1.00135.54 C ANISOU 946 CZ PHE A 133 18154 17001 16344 -387 -1561 -27 C ATOM 947 N ALA A 134 17.641 -43.428 -20.300 1.00141.04 N ANISOU 947 N ALA A 134 18500 17916 17171 -658 -720 -220 N ATOM 948 CA ALA A 134 16.744 -43.425 -19.152 1.00137.82 C ANISOU 948 CA ALA A 134 18065 17515 16783 -686 -536 -198 C ATOM 949 C ALA A 134 15.727 -42.296 -19.273 1.00138.89 C ANISOU 949 C ALA A 134 18006 17608 17156 -747 -454 -231 C ATOM 950 O ALA A 134 14.525 -42.510 -19.115 1.00144.29 O ANISOU 950 O ALA A 134 18610 18221 17990 -817 -359 -148 O ATOM 951 CB ALA A 134 17.536 -43.295 -17.860 1.00132.47 C ANISOU 951 CB ALA A 134 17488 16978 15868 -586 -450 -282 C ATOM 952 N ILE A 135 16.220 -41.096 -19.560 1.00134.97 N ANISOU 952 N ILE A 135 17430 17153 16699 -718 -491 -347 N ATOM 953 CA ILE A 135 15.363 -39.926 -19.707 1.00136.55 C ANISOU 953 CA ILE A 135 17462 17312 17107 -755 -421 -391 C ATOM 954 C ILE A 135 14.605 -39.938 -21.032 1.00135.94 C ANISOU 954 C ILE A 135 17284 17112 17257 -823 -519 -320 C ATOM 955 O ILE A 135 13.380 -39.840 -21.057 1.00135.70 O ANISOU 955 O ILE A 135 17136 17018 17407 -879 -449 -267 O ATOM 956 CB ILE A 135 16.173 -38.619 -19.602 1.00137.40 C ANISOU 956 CB ILE A 135 17534 17485 17187 -706 -434 -540 C ATOM 957 CG1 ILE A 135 16.755 -38.464 -18.196 1.00136.86 C ANISOU 957 CG1 ILE A 135 17551 17534 16914 -633 -341 -632 C ATOM 958 CG2 ILE A 135 15.303 -37.424 -19.952 1.00139.70 C ANISOU 958 CG2 ILE A 135 17670 17713 17699 -736 -382 -578 C ATOM 959 CD1 ILE A 135 17.535 -37.183 -17.997 1.00136.59 C ANISOU 959 CD1 ILE A 135 17482 17552 16863 -596 -364 -792 C ATOM 960 N GLY A 136 15.344 -40.060 -22.130 1.00134.74 N ANISOU 960 N GLY A 136 17177 16930 17089 -804 -683 -320 N ATOM 961 CA GLY A 136 14.761 -40.025 -23.459 1.00130.89 C ANISOU 961 CA GLY A 136 16619 16326 16786 -838 -800 -268 C ATOM 962 C GLY A 136 13.651 -41.037 -23.675 1.00125.34 C ANISOU 962 C GLY A 136 15897 15526 16199 -912 -821 -152 C ATOM 963 O GLY A 136 12.707 -40.783 -24.426 1.00114.94 O ANISOU 963 O GLY A 136 14463 14117 15091 -953 -868 -124 O ATOM 964 N LEU A 137 13.766 -42.189 -23.022 1.00133.47 N ANISOU 964 N LEU A 137 17044 16570 17100 -928 -791 -86 N ATOM 965 CA LEU A 137 12.770 -43.246 -23.161 1.00140.33 C ANISOU 965 CA LEU A 137 17904 17332 18082 -1015 -809 31 C ATOM 966 C LEU A 137 11.953 -43.432 -21.886 1.00149.82 C ANISOU 966 C LEU A 137 19051 18563 19313 -1066 -600 78 C ATOM 967 O LEU A 137 11.502 -44.537 -21.582 1.00149.14 O ANISOU 967 O LEU A 137 19018 18417 19230 -1129 -572 183 O ATOM 968 CB LEU A 137 13.434 -44.565 -23.562 1.00134.84 C ANISOU 968 CB LEU A 137 17404 16592 17236 -998 -947 96 C ATOM 969 CG LEU A 137 14.132 -44.583 -24.923 1.00125.12 C ANISOU 969 CG LEU A 137 16244 15317 15978 -935 -1157 77 C ATOM 970 CD1 LEU A 137 14.756 -45.943 -25.188 1.00120.11 C ANISOU 970 CD1 LEU A 137 15821 14642 15175 -902 -1277 143 C ATOM 971 CD2 LEU A 137 13.156 -44.214 -26.031 1.00118.75 C ANISOU 971 CD2 LEU A 137 15305 14392 15422 -981 -1262 91 C ATOM 972 N THR A 138 11.768 -42.346 -21.141 1.00158.30 N ANISOU 972 N THR A 138 20024 19719 20402 -1034 -448 5 N ATOM 973 CA THR A 138 10.938 -42.371 -19.940 1.00162.61 C ANISOU 973 CA THR A 138 20507 20300 20976 -1057 -228 50 C ATOM 974 C THR A 138 9.474 -42.686 -20.258 1.00163.22 C ANISOU 974 C THR A 138 20414 20275 21327 -1168 -193 157 C ATOM 975 O THR A 138 8.824 -43.424 -19.516 1.00162.30 O ANISOU 975 O THR A 138 20290 20141 21234 -1223 -55 262 O ATOM 976 CB THR A 138 11.025 -41.045 -19.152 1.00162.04 C ANISOU 976 CB THR A 138 20371 20330 20865 -979 -86 -64 C ATOM 977 OG1 THR A 138 12.369 -40.841 -18.700 1.00157.88 O ANISOU 977 OG1 THR A 138 19997 19901 20089 -886 -116 -164 O ATOM 978 CG2 THR A 138 10.093 -41.079 -17.950 1.00164.54 C ANISOU 978 CG2 THR A 138 20628 20682 21207 -981 152 -5 C ATOM 979 N PRO A 139 8.945 -42.122 -21.358 1.00162.08 N ANISOU 979 N PRO A 139 20127 20062 21393 -1199 -316 134 N ATOM 980 CA PRO A 139 7.572 -42.450 -21.757 1.00165.56 C ANISOU 980 CA PRO A 139 20389 20407 22110 -1306 -320 226 C ATOM 981 C PRO A 139 7.367 -43.949 -21.969 1.00166.33 C ANISOU 981 C PRO A 139 20567 20399 22232 -1406 -403 346 C ATOM 982 O PRO A 139 6.234 -44.424 -21.910 1.00170.77 O ANISOU 982 O PRO A 139 20989 20890 23008 -1515 -354 442 O ATOM 983 CB PRO A 139 7.408 -41.702 -23.082 1.00164.22 C ANISOU 983 CB PRO A 139 20122 20180 22094 -1288 -503 162 C ATOM 984 CG PRO A 139 8.339 -40.552 -22.973 1.00160.37 C ANISOU 984 CG PRO A 139 19690 19781 21460 -1175 -479 37 C ATOM 985 CD PRO A 139 9.523 -41.064 -22.205 1.00159.47 C ANISOU 985 CD PRO A 139 19780 19744 21067 -1130 -438 21 C ATOM 986 N MET A 140 8.450 -44.680 -22.213 1.00165.37 N ANISOU 986 N MET A 140 20667 20265 21903 -1369 -526 340 N ATOM 987 CA MET A 140 8.366 -46.125 -22.394 1.00168.93 C ANISOU 987 CA MET A 140 21234 20604 22346 -1450 -613 447 C ATOM 988 C MET A 140 8.337 -46.850 -21.054 1.00169.00 C ANISOU 988 C MET A 140 21333 20649 22231 -1470 -400 534 C ATOM 989 O MET A 140 8.205 -48.072 -21.000 1.00166.59 O ANISOU 989 O MET A 140 21133 20246 21918 -1544 -428 637 O ATOM 990 CB MET A 140 9.530 -46.637 -23.245 1.00173.55 C ANISOU 990 CB MET A 140 22033 21159 22747 -1379 -833 411 C ATOM 991 CG MET A 140 9.552 -46.091 -24.660 1.00176.87 C ANISOU 991 CG MET A 140 22398 21524 23280 -1348 -1049 347 C ATOM 992 SD MET A 140 10.667 -47.010 -25.737 1.00150.42 S ANISOU 992 SD MET A 140 19305 18104 19744 -1272 -1308 347 S ATOM 993 CE MET A 140 9.940 -48.645 -25.654 1.00124.41 C ANISOU 993 CE MET A 140 16092 14646 16531 -1404 -1366 477 C ATOM 994 N LEU A 141 8.464 -46.086 -19.974 1.00172.67 N ANISOU 994 N LEU A 141 21770 21247 22590 -1395 -189 491 N ATOM 995 CA LEU A 141 8.427 -46.647 -18.630 1.00179.17 C ANISOU 995 CA LEU A 141 22685 22116 23273 -1382 35 570 C ATOM 996 C LEU A 141 6.996 -46.700 -18.104 1.00182.62 C ANISOU 996 C LEU A 141 22921 22515 23952 -1484 234 684 C ATOM 997 O LEU A 141 6.742 -47.229 -17.023 1.00183.11 O ANISOU 997 O LEU A 141 23037 22596 23940 -1485 446 782 O ATOM 998 CB LEU A 141 9.310 -45.830 -17.682 1.00181.82 C ANISOU 998 CB LEU A 141 23114 22616 23355 -1229 155 460 C ATOM 999 CG LEU A 141 10.779 -45.674 -18.085 1.00180.60 C ANISOU 999 CG LEU A 141 23128 22523 22967 -1125 -18 343 C ATOM 1000 CD1 LEU A 141 11.512 -44.755 -17.118 1.00179.81 C ANISOU 1000 CD1 LEU A 141 23078 22578 22664 -991 94 223 C ATOM 1001 CD2 LEU A 141 11.465 -47.031 -18.168 1.00180.52 C ANISOU 1001 CD2 LEU A 141 23343 22463 22782 -1120 -114 414 C ATOM 1002 N GLY A 142 6.065 -46.147 -18.877 1.00186.41 N ANISOU 1002 N GLY A 142 23164 22944 24718 -1558 168 676 N ATOM 1003 CA GLY A 142 4.660 -46.152 -18.508 1.00188.77 C ANISOU 1003 CA GLY A 142 23229 23211 25282 -1659 339 784 C ATOM 1004 C GLY A 142 3.996 -44.798 -18.674 1.00183.22 C ANISOU 1004 C GLY A 142 22292 22578 24747 -1616 390 708 C ATOM 1005 O GLY A 142 2.770 -44.692 -18.665 1.00183.17 O ANISOU 1005 O GLY A 142 22046 22544 25007 -1698 481 783 O ATOM 1006 N TRP A 143 4.813 -43.761 -18.827 1.00177.36 N ANISOU 1006 N TRP A 143 21614 21923 23851 -1488 330 559 N ATOM 1007 CA TRP A 143 4.317 -42.397 -18.972 1.00172.20 C ANISOU 1007 CA TRP A 143 20777 21329 23321 -1426 375 473 C ATOM 1008 C TRP A 143 3.944 -42.113 -20.424 1.00165.20 C ANISOU 1008 C TRP A 143 19761 20353 22653 -1475 134 433 C ATOM 1009 O TRP A 143 4.629 -41.356 -21.112 1.00162.76 O ANISOU 1009 O TRP A 143 19509 20058 22275 -1397 -8 315 O ATOM 1010 CB TRP A 143 5.384 -41.403 -18.506 1.00177.18 C ANISOU 1010 CB TRP A 143 21546 22072 23701 -1275 409 328 C ATOM 1011 CG TRP A 143 4.873 -40.016 -18.254 1.00182.81 C ANISOU 1011 CG TRP A 143 22111 22854 24495 -1192 524 248 C ATOM 1012 CD1 TRP A 143 4.275 -39.185 -19.155 1.00184.68 C ANISOU 1012 CD1 TRP A 143 22173 23054 24942 -1196 430 201 C ATOM 1013 CD2 TRP A 143 4.938 -39.291 -17.020 1.00185.93 C ANISOU 1013 CD2 TRP A 143 22541 23360 24746 -1076 748 200 C ATOM 1014 NE1 TRP A 143 3.951 -37.991 -18.556 1.00186.72 N ANISOU 1014 NE1 TRP A 143 22353 23391 25201 -1094 588 130 N ATOM 1015 CE2 TRP A 143 4.350 -38.030 -17.246 1.00187.70 C ANISOU 1015 CE2 TRP A 143 22606 23604 25109 -1019 780 125 C ATOM 1016 CE3 TRP A 143 5.431 -39.585 -15.745 1.00186.24 C ANISOU 1016 CE3 TRP A 143 22744 23480 24540 -999 917 208 C ATOM 1017 CZ2 TRP A 143 4.240 -37.067 -16.244 1.00187.36 C ANISOU 1017 CZ2 TRP A 143 22566 23652 24970 -891 974 58 C ATOM 1018 CZ3 TRP A 143 5.322 -38.628 -14.753 1.00186.52 C ANISOU 1018 CZ3 TRP A 143 22782 23609 24477 -868 1104 139 C ATOM 1019 CH2 TRP A 143 4.733 -37.383 -15.008 1.00186.61 C ANISOU 1019 CH2 TRP A 143 22636 23633 24633 -817 1130 63 C ATOM 1020 N ASN A 144 2.856 -42.720 -20.889 1.00164.88 N ANISOU 1020 N ASN A 144 19547 20218 22880 -1602 87 532 N ATOM 1021 CA ASN A 144 2.435 -42.565 -22.278 1.00164.12 C ANISOU 1021 CA ASN A 144 19337 20029 22993 -1641 -163 496 C ATOM 1022 C ASN A 144 0.918 -42.518 -22.456 1.00169.41 C ANISOU 1022 C ASN A 144 19704 20661 24004 -1734 -125 569 C ATOM 1023 O ASN A 144 0.162 -42.809 -21.528 1.00171.73 O ANISOU 1023 O ASN A 144 19872 20986 24391 -1794 99 675 O ATOM 1024 CB ASN A 144 3.036 -43.677 -23.143 1.00159.58 C ANISOU 1024 CB ASN A 144 18936 19334 22362 -1701 -413 516 C ATOM 1025 CG ASN A 144 2.680 -45.063 -22.640 1.00161.17 C ANISOU 1025 CG ASN A 144 19173 19456 22607 -1836 -356 655 C ATOM 1026 OD1 ASN A 144 1.513 -45.368 -22.398 1.00170.98 O ANISOU 1026 OD1 ASN A 144 20209 20659 24099 -1951 -264 752 O ATOM 1027 ND2 ASN A 144 3.688 -45.913 -22.484 1.00155.67 N ANISOU 1027 ND2 ASN A 144 18739 18735 21674 -1823 -406 671 N ATOM 1028 N ASN A 145 0.483 -42.146 -23.656 1.00165.30 N ANISOU 1028 N ASN A 145 19062 20076 23666 -1735 -343 515 N ATOM 1029 CA ASN A 145 -0.939 -42.075 -23.976 1.00158.66 C ANISOU 1029 CA ASN A 145 17919 19202 23165 -1815 -354 567 C ATOM 1030 C ASN A 145 -1.353 -43.106 -25.021 1.00156.95 C ANISOU 1030 C ASN A 145 17665 18829 23139 -1945 -628 607 C ATOM 1031 O ASN A 145 -2.074 -42.789 -25.966 1.00159.85 O ANISOU 1031 O ASN A 145 17862 19148 23727 -1948 -807 568 O ATOM 1032 CB ASN A 145 -1.318 -40.671 -24.453 1.00153.61 C ANISOU 1032 CB ASN A 145 17133 18621 22610 -1690 -374 465 C ATOM 1033 CG ASN A 145 -1.305 -39.650 -23.333 1.00149.59 C ANISOU 1033 CG ASN A 145 16594 18253 21991 -1579 -84 440 C ATOM 1034 OD1 ASN A 145 -1.282 -40.004 -22.154 1.00150.45 O ANISOU 1034 OD1 ASN A 145 16734 18422 22008 -1602 152 515 O ATOM 1035 ND2 ASN A 145 -1.327 -38.373 -23.697 1.00145.45 N ANISOU 1035 ND2 ASN A 145 16022 17774 21467 -1448 -101 335 N ATOM 1036 N CYS A 146 -0.894 -44.341 -24.844 1.00153.99 N ANISOU 1036 N CYS A 146 17463 18371 22674 -2042 -668 679 N ATOM 1037 CA CYS A 146 -1.223 -45.417 -25.771 1.00157.17 C ANISOU 1037 CA CYS A 146 17869 18607 23240 -2169 -936 714 C ATOM 1038 C CYS A 146 -2.640 -45.932 -25.538 1.00164.18 C ANISOU 1038 C CYS A 146 18459 19438 24483 -2344 -874 827 C ATOM 1039 O CYS A 146 -2.911 -46.596 -24.538 1.00165.98 O ANISOU 1039 O CYS A 146 18660 19666 24738 -2450 -654 953 O ATOM 1040 CB CYS A 146 -0.223 -46.568 -25.639 1.00158.99 C ANISOU 1040 CB CYS A 146 18407 18760 23243 -2204 -997 753 C ATOM 1041 SG CYS A 146 1.487 -46.135 -26.042 1.00198.11 S ANISOU 1041 SG CYS A 146 23699 23773 27802 -2010 -1104 630 S ATOM 1042 N GLY A 147 -3.540 -45.619 -26.465 1.00168.10 N ANISOU 1042 N GLY A 147 18729 19888 25255 -2368 -1066 784 N ATOM 1043 CA GLY A 147 -4.911 -46.089 -26.386 1.00169.47 C ANISOU 1043 CA GLY A 147 18584 20003 25802 -2540 -1047 881 C ATOM 1044 C GLY A 147 -5.823 -45.163 -25.605 1.00170.66 C ANISOU 1044 C GLY A 147 18433 20303 26107 -2508 -763 922 C ATOM 1045 O GLY A 147 -6.930 -45.549 -25.225 1.00172.26 O ANISOU 1045 O GLY A 147 18355 20491 26604 -2651 -654 1034 O ATOM 1046 N GLN A 148 -5.363 -43.940 -25.363 1.00171.41 N ANISOU 1046 N GLN A 148 18583 20538 26008 -2317 -641 835 N ATOM 1047 CA GLN A 148 -6.164 -42.962 -24.635 1.00179.62 C ANISOU 1047 CA GLN A 148 19368 21723 27157 -2249 -374 859 C ATOM 1048 C GLN A 148 -7.307 -42.434 -25.494 1.00191.10 C ANISOU 1048 C GLN A 148 20504 23172 28934 -2247 -533 819 C ATOM 1049 O GLN A 148 -7.114 -42.124 -26.670 1.00196.57 O ANISOU 1049 O GLN A 148 21252 23805 29630 -2176 -827 703 O ATOM 1050 CB GLN A 148 -5.292 -41.807 -24.141 1.00175.47 C ANISOU 1050 CB GLN A 148 19020 21329 26322 -2044 -217 765 C ATOM 1051 CG GLN A 148 -4.292 -42.207 -23.070 1.00178.28 C ANISOU 1051 CG GLN A 148 19644 21725 26371 -2029 -14 806 C ATOM 1052 CD GLN A 148 -4.960 -42.777 -21.833 1.00184.46 C ANISOU 1052 CD GLN A 148 20299 22548 27240 -2123 297 968 C ATOM 1053 OE1 GLN A 148 -6.119 -42.478 -21.544 1.00184.70 O ANISOU 1053 OE1 GLN A 148 20027 22629 27520 -2151 443 1038 O ATOM 1054 NE2 GLN A 148 -4.227 -43.601 -21.092 1.00189.72 N ANISOU 1054 NE2 GLN A 148 21198 23194 27694 -2161 408 1035 N ATOM 1055 N PRO A 149 -8.506 -42.332 -24.900 1.00189.92 N ANISOU 1055 N PRO A 149 20020 23089 29052 -2311 -333 919 N ATOM 1056 CA PRO A 149 -9.713 -41.858 -25.586 1.00184.71 C ANISOU 1056 CA PRO A 149 19011 22443 28727 -2310 -458 894 C ATOM 1057 C PRO A 149 -9.471 -40.547 -26.328 1.00176.64 C ANISOU 1057 C PRO A 149 18038 21482 27597 -2089 -588 734 C ATOM 1058 O PRO A 149 -9.381 -40.570 -27.556 1.00172.91 O ANISOU 1058 O PRO A 149 17611 20915 27170 -2064 -922 637 O ATOM 1059 CB PRO A 149 -10.698 -41.636 -24.437 1.00187.13 C ANISOU 1059 CB PRO A 149 19020 22875 29204 -2338 -94 1028 C ATOM 1060 CG PRO A 149 -10.261 -42.590 -23.386 1.00188.56 C ANISOU 1060 CG PRO A 149 19354 23031 29259 -2456 136 1163 C ATOM 1061 CD PRO A 149 -8.764 -42.655 -23.486 1.00189.25 C ANISOU 1061 CD PRO A 149 19873 23079 28955 -2371 44 1069 C ATOM 1062 N GLY A 158 -9.196 -49.093 -37.587 1.00248.94 N ANISOU 1062 N GLY A 158 28269 28820 37497 -2656 -4547 140 N ATOM 1063 CA GLY A 158 -7.999 -48.294 -37.771 1.00246.44 C ANISOU 1063 CA GLY A 158 28262 28606 36769 -2398 -4448 93 C ATOM 1064 C GLY A 158 -6.758 -49.141 -37.978 1.00247.45 C ANISOU 1064 C GLY A 158 28826 28620 36573 -2360 -4534 98 C ATOM 1065 O GLY A 158 -6.352 -49.398 -39.110 1.00248.13 O ANISOU 1065 O GLY A 158 29159 28590 36530 -2219 -4863 2 O ATOM 1066 N CYS A 159 -6.154 -49.578 -36.877 1.00245.48 N ANISOU 1066 N CYS A 159 28681 28408 36184 -2470 -4236 211 N ATOM 1067 CA CYS A 159 -4.945 -50.392 -36.936 1.00241.35 C ANISOU 1067 CA CYS A 159 28564 27797 35343 -2432 -4280 227 C ATOM 1068 C CYS A 159 -5.188 -51.783 -36.357 1.00235.95 C ANISOU 1068 C CYS A 159 27896 26958 34796 -2691 -4277 329 C ATOM 1069 O CYS A 159 -4.371 -52.688 -36.529 1.00235.77 O ANISOU 1069 O CYS A 159 28204 26815 34564 -2683 -4384 339 O ATOM 1070 CB CYS A 159 -3.800 -49.704 -36.188 1.00239.63 C ANISOU 1070 CB CYS A 159 28519 27754 34774 -2299 -3947 262 C ATOM 1071 SG CYS A 159 -3.360 -48.070 -36.830 1.00230.22 S ANISOU 1071 SG CYS A 159 27351 26723 33399 -2000 -3926 155 S ATOM 1072 N GLY A 160 -6.314 -51.944 -35.670 1.00231.08 N ANISOU 1072 N GLY A 160 26924 26344 34533 -2915 -4143 410 N ATOM 1073 CA GLY A 160 -6.666 -53.216 -35.067 1.00228.20 C ANISOU 1073 CA GLY A 160 26536 25825 34344 -3181 -4109 524 C ATOM 1074 C GLY A 160 -6.128 -53.359 -33.657 1.00221.68 C ANISOU 1074 C GLY A 160 25778 25101 33351 -3249 -3679 667 C ATOM 1075 O GLY A 160 -5.324 -52.543 -33.204 1.00215.35 O ANISOU 1075 O GLY A 160 25089 24479 32257 -3077 -3445 660 O ATOM 1076 N GLU A 161 -6.575 -54.398 -32.960 1.00223.52 N ANISOU 1076 N GLU A 161 25944 25212 33771 -3496 -3580 795 N ATOM 1077 CA GLU A 161 -6.131 -54.651 -31.594 1.00221.08 C ANISOU 1077 CA GLU A 161 25711 24981 33310 -3561 -3175 941 C ATOM 1078 C GLU A 161 -4.660 -55.052 -31.565 1.00211.53 C ANISOU 1078 C GLU A 161 24964 23756 31651 -3413 -3177 925 C ATOM 1079 O GLU A 161 -4.203 -55.834 -32.400 1.00210.82 O ANISOU 1079 O GLU A 161 25144 23493 31466 -3388 -3487 866 O ATOM 1080 CB GLU A 161 -6.994 -55.732 -30.938 1.00228.96 C ANISOU 1080 CB GLU A 161 26539 25825 34630 -3863 -3080 1093 C ATOM 1081 CG GLU A 161 -6.941 -57.084 -31.633 1.00236.40 C ANISOU 1081 CG GLU A 161 27694 26480 35646 -3998 -3421 1080 C ATOM 1082 CD GLU A 161 -7.870 -58.101 -30.998 1.00246.71 C ANISOU 1082 CD GLU A 161 28803 27621 37315 -4317 -3321 1236 C ATOM 1083 OE1 GLU A 161 -7.752 -59.300 -31.328 1.00250.26 O ANISOU 1083 OE1 GLU A 161 29460 27822 37804 -4447 -3537 1253 O ATOM 1084 OE2 GLU A 161 -8.714 -57.701 -30.167 1.00251.57 O ANISOU 1084 OE2 GLU A 161 29059 28350 38176 -4434 -3020 1347 O ATOM 1085 N GLY A 162 -3.924 -54.510 -30.600 1.00204.18 N ANISOU 1085 N GLY A 162 24124 23011 30445 -3304 -2837 972 N ATOM 1086 CA GLY A 162 -2.501 -54.766 -30.489 1.00195.64 C ANISOU 1086 CA GLY A 162 23447 21954 28935 -3147 -2812 954 C ATOM 1087 C GLY A 162 -1.679 -53.616 -31.039 1.00189.37 C ANISOU 1087 C GLY A 162 22754 21320 27876 -2883 -2858 825 C ATOM 1088 O GLY A 162 -0.764 -53.124 -30.378 1.00187.27 O ANISOU 1088 O GLY A 162 22627 21211 27316 -2753 -2631 830 O ATOM 1089 N GLN A 163 -2.009 -53.186 -32.254 1.00185.74 N ANISOU 1089 N GLN A 163 22229 20817 27526 -2803 -3158 709 N ATOM 1090 CA GLN A 163 -1.310 -52.077 -32.898 1.00177.91 C ANISOU 1090 CA GLN A 163 21327 19957 26315 -2554 -3215 592 C ATOM 1091 C GLN A 163 -1.990 -50.745 -32.585 1.00172.47 C ANISOU 1091 C GLN A 163 20313 19441 25777 -2517 -3028 569 C ATOM 1092 O GLN A 163 -3.220 -50.662 -32.555 1.00178.24 O ANISOU 1092 O GLN A 163 20725 20147 26851 -2649 -3039 592 O ATOM 1093 CB GLN A 163 -1.243 -52.293 -34.413 1.00178.05 C ANISOU 1093 CB GLN A 163 21487 19834 26332 -2447 -3633 480 C ATOM 1094 CG GLN A 163 -0.453 -53.525 -34.840 1.00178.28 C ANISOU 1094 CG GLN A 163 21882 19696 26162 -2432 -3838 486 C ATOM 1095 CD GLN A 163 -0.426 -53.711 -36.346 1.00180.33 C ANISOU 1095 CD GLN A 163 22291 19815 26410 -2302 -4254 372 C ATOM 1096 OE1 GLN A 163 -1.143 -53.031 -37.081 1.00184.66 O ANISOU 1096 OE1 GLN A 163 22648 20370 27143 -2251 -4412 292 O ATOM 1097 NE2 GLN A 163 0.404 -54.637 -36.814 1.00177.94 N ANISOU 1097 NE2 GLN A 163 22345 19386 25879 -2228 -4435 363 N ATOM 1098 N VAL A 164 -1.189 -49.709 -32.351 1.00159.39 N ANISOU 1098 N VAL A 164 18735 17956 23871 -2336 -2859 524 N ATOM 1099 CA VAL A 164 -1.718 -48.386 -32.036 1.00147.45 C ANISOU 1099 CA VAL A 164 16958 16605 22461 -2275 -2675 496 C ATOM 1100 C VAL A 164 -1.293 -47.363 -33.086 1.00144.25 C ANISOU 1100 C VAL A 164 16626 16245 21937 -2054 -2838 371 C ATOM 1101 O VAL A 164 -0.163 -47.397 -33.572 1.00144.45 O ANISOU 1101 O VAL A 164 16941 16263 21681 -1914 -2929 327 O ATOM 1102 CB VAL A 164 -1.247 -47.909 -30.643 1.00132.94 C ANISOU 1102 CB VAL A 164 15121 14935 20454 -2262 -2283 556 C ATOM 1103 CG1 VAL A 164 -1.780 -46.514 -30.346 1.00122.53 C ANISOU 1103 CG1 VAL A 164 13554 13772 19228 -2181 -2104 517 C ATOM 1104 CG2 VAL A 164 -1.690 -48.892 -29.569 1.00134.15 C ANISOU 1104 CG2 VAL A 164 15210 15045 20714 -2462 -2094 694 C ATOM 1105 N ALA A 165 -2.205 -46.463 -33.443 1.00142.80 N ANISOU 1105 N ALA A 165 16179 16108 21969 -2017 -2867 323 N ATOM 1106 CA ALA A 165 -1.891 -45.408 -34.396 1.00142.40 C ANISOU 1106 CA ALA A 165 16188 16099 21819 -1801 -2993 215 C ATOM 1107 C ALA A 165 -0.732 -44.577 -33.870 1.00146.35 C ANISOU 1107 C ALA A 165 16855 16738 22013 -1664 -2759 199 C ATOM 1108 O ALA A 165 -0.916 -43.717 -33.007 1.00144.39 O ANISOU 1108 O ALA A 165 16457 16624 21781 -1658 -2490 211 O ATOM 1109 CB ALA A 165 -3.107 -44.538 -34.650 1.00144.04 C ANISOU 1109 CB ALA A 165 16069 16351 22308 -1784 -3011 176 C ATOM 1110 N CYS A 166 0.460 -44.841 -34.397 1.00150.91 N ANISOU 1110 N CYS A 166 17742 17282 22315 -1551 -2867 171 N ATOM 1111 CA CYS A 166 1.668 -44.182 -33.923 1.00147.48 C ANISOU 1111 CA CYS A 166 17474 16969 21591 -1437 -2669 157 C ATOM 1112 C CYS A 166 1.721 -42.726 -34.367 1.00140.70 C ANISOU 1112 C CYS A 166 16554 16190 20716 -1272 -2629 81 C ATOM 1113 O CYS A 166 2.271 -42.403 -35.420 1.00137.26 O ANISOU 1113 O CYS A 166 16276 15715 20163 -1115 -2795 27 O ATOM 1114 CB CYS A 166 2.911 -44.928 -34.405 1.00147.86 C ANISOU 1114 CB CYS A 166 17854 16960 21365 -1359 -2801 157 C ATOM 1115 SG CYS A 166 4.455 -44.356 -33.658 1.00221.62 S ANISOU 1115 SG CYS A 166 27385 26456 30366 -1256 -2555 151 S ATOM 1116 N LEU A 167 1.141 -41.854 -33.552 1.00138.74 N ANISOU 1116 N LEU A 167 16087 16049 20580 -1300 -2399 82 N ATOM 1117 CA LEU A 167 1.173 -40.423 -33.808 1.00137.00 C ANISOU 1117 CA LEU A 167 15809 15901 20343 -1152 -2326 13 C ATOM 1118 C LEU A 167 1.840 -39.735 -32.629 1.00128.41 C ANISOU 1118 C LEU A 167 14746 14947 19097 -1144 -2021 14 C ATOM 1119 O LEU A 167 1.418 -39.898 -31.486 1.00120.32 O ANISOU 1119 O LEU A 167 13594 13987 18134 -1254 -1817 62 O ATOM 1120 CB LEU A 167 -0.241 -39.880 -34.014 1.00150.79 C ANISOU 1120 CB LEU A 167 17263 17648 22383 -1162 -2357 -4 C ATOM 1121 CG LEU A 167 -1.100 -40.646 -35.023 1.00159.63 C ANISOU 1121 CG LEU A 167 18307 18637 23709 -1200 -2666 -9 C ATOM 1122 CD1 LEU A 167 -2.457 -39.985 -35.187 1.00160.09 C ANISOU 1122 CD1 LEU A 167 18055 18719 24053 -1191 -2685 -34 C ATOM 1123 CD2 LEU A 167 -0.388 -40.758 -36.362 1.00161.25 C ANISOU 1123 CD2 LEU A 167 18765 18746 23758 -1045 -2936 -64 C ATOM 1124 N PHE A 168 2.887 -38.970 -32.915 1.00135.40 N ANISOU 1124 N PHE A 168 15800 15868 19780 -1010 -1993 -39 N ATOM 1125 CA PHE A 168 3.709 -38.368 -31.871 1.00146.73 C ANISOU 1125 CA PHE A 168 17294 17415 21041 -998 -1745 -54 C ATOM 1126 C PHE A 168 2.894 -37.701 -30.763 1.00153.04 C ANISOU 1126 C PHE A 168 17880 18305 21964 -1045 -1505 -53 C ATOM 1127 O PHE A 168 3.057 -38.020 -29.586 1.00152.45 O ANISOU 1127 O PHE A 168 17804 18300 21818 -1123 -1317 -18 O ATOM 1128 CB PHE A 168 4.693 -37.367 -32.475 1.00152.16 C ANISOU 1128 CB PHE A 168 18126 18116 21572 -847 -1756 -120 C ATOM 1129 CG PHE A 168 5.696 -36.841 -31.493 1.00154.95 C ANISOU 1129 CG PHE A 168 18564 18572 21740 -841 -1546 -147 C ATOM 1130 CD1 PHE A 168 6.779 -37.616 -31.109 1.00154.57 C ANISOU 1130 CD1 PHE A 168 18689 18553 21486 -871 -1534 -124 C ATOM 1131 CD2 PHE A 168 5.556 -35.571 -30.953 1.00157.29 C ANISOU 1131 CD2 PHE A 168 18769 18930 22064 -796 -1371 -204 C ATOM 1132 CE1 PHE A 168 7.705 -37.137 -30.206 1.00156.63 C ANISOU 1132 CE1 PHE A 168 19019 18912 21582 -861 -1363 -161 C ATOM 1133 CE2 PHE A 168 6.476 -35.082 -30.051 1.00156.77 C ANISOU 1133 CE2 PHE A 168 18783 18947 21833 -791 -1201 -244 C ATOM 1134 CZ PHE A 168 7.554 -35.869 -29.673 1.00157.84 C ANISOU 1134 CZ PHE A 168 19080 19120 21773 -825 -1202 -225 C ATOM 1135 N GLU A 169 2.018 -36.777 -31.145 1.00158.56 N ANISOU 1135 N GLU A 169 18409 19002 22834 -980 -1510 -90 N ATOM 1136 CA GLU A 169 1.238 -36.017 -30.172 1.00162.21 C ANISOU 1136 CA GLU A 169 18674 19553 23405 -990 -1282 -93 C ATOM 1137 C GLU A 169 0.206 -36.878 -29.447 1.00160.45 C ANISOU 1137 C GLU A 169 18258 19347 23360 -1134 -1203 -5 C ATOM 1138 O GLU A 169 -0.231 -36.540 -28.346 1.00156.81 O ANISOU 1138 O GLU A 169 17674 18975 22931 -1156 -964 18 O ATOM 1139 CB GLU A 169 0.548 -34.826 -30.844 1.00167.85 C ANISOU 1139 CB GLU A 169 19263 20257 24256 -865 -1320 -153 C ATOM 1140 CG GLU A 169 -0.510 -35.208 -31.869 1.00174.46 C ANISOU 1140 CG GLU A 169 19951 21015 25322 -868 -1547 -138 C ATOM 1141 CD GLU A 169 0.080 -35.814 -33.128 1.00177.40 C ANISOU 1141 CD GLU A 169 20510 21276 25617 -827 -1826 -150 C ATOM 1142 OE1 GLU A 169 1.268 -35.553 -33.417 1.00176.48 O ANISOU 1142 OE1 GLU A 169 20622 21150 25282 -749 -1834 -179 O ATOM 1143 OE2 GLU A 169 -0.647 -36.544 -33.834 1.00178.52 O ANISOU 1143 OE2 GLU A 169 20569 21341 25921 -868 -2039 -131 O ATOM 1144 N ASP A 170 -0.178 -37.991 -30.065 1.00162.70 N ANISOU 1144 N ASP A 170 18520 19538 23760 -1227 -1401 45 N ATOM 1145 CA ASP A 170 -1.219 -38.854 -29.513 1.00164.87 C ANISOU 1145 CA ASP A 170 18594 19805 24247 -1382 -1348 138 C ATOM 1146 C ASP A 170 -0.665 -39.949 -28.605 1.00159.49 C ANISOU 1146 C ASP A 170 18040 19125 23432 -1503 -1235 218 C ATOM 1147 O ASP A 170 -1.335 -40.384 -27.668 1.00162.57 O ANISOU 1147 O ASP A 170 18285 19550 23933 -1612 -1056 305 O ATOM 1148 CB ASP A 170 -2.047 -39.480 -30.638 1.00170.32 C ANISOU 1148 CB ASP A 170 19169 20376 25168 -1433 -1634 145 C ATOM 1149 CG ASP A 170 -2.818 -38.447 -31.436 1.00175.61 C ANISOU 1149 CG ASP A 170 19673 21052 26000 -1312 -1734 76 C ATOM 1150 OD1 ASP A 170 -2.825 -37.265 -31.031 1.00177.90 O ANISOU 1150 OD1 ASP A 170 19914 21435 26245 -1203 -1555 34 O ATOM 1151 OD2 ASP A 170 -3.419 -38.820 -32.466 1.00177.45 O ANISOU 1151 OD2 ASP A 170 19832 21191 26400 -1317 -1999 58 O ATOM 1152 N VAL A 171 0.555 -40.395 -28.888 1.00148.60 N ANISOU 1152 N VAL A 171 16937 17712 21814 -1472 -1333 196 N ATOM 1153 CA VAL A 171 1.168 -41.467 -28.113 1.00139.70 C ANISOU 1153 CA VAL A 171 15963 16581 20535 -1564 -1251 267 C ATOM 1154 C VAL A 171 2.087 -40.919 -27.026 1.00134.90 C ANISOU 1154 C VAL A 171 15481 16097 19677 -1495 -1012 241 C ATOM 1155 O VAL A 171 2.391 -41.609 -26.052 1.00126.13 O ANISOU 1155 O VAL A 171 14453 15019 18453 -1556 -867 304 O ATOM 1156 CB VAL A 171 1.965 -42.432 -29.011 1.00135.00 C ANISOU 1156 CB VAL A 171 15603 15875 19816 -1566 -1505 264 C ATOM 1157 CG1 VAL A 171 1.047 -43.086 -30.030 1.00137.99 C ANISOU 1157 CG1 VAL A 171 15877 16116 20438 -1638 -1762 283 C ATOM 1158 CG2 VAL A 171 3.100 -41.696 -29.703 1.00133.90 C ANISOU 1158 CG2 VAL A 171 15653 15761 19463 -1404 -1594 173 C ATOM 1159 N VAL A 172 2.523 -39.675 -27.196 1.00140.81 N ANISOU 1159 N VAL A 172 16251 16909 20341 -1364 -978 145 N ATOM 1160 CA VAL A 172 3.422 -39.040 -26.240 1.00143.07 C ANISOU 1160 CA VAL A 172 16654 17305 20402 -1293 -784 97 C ATOM 1161 C VAL A 172 2.712 -37.944 -25.451 1.00146.44 C ANISOU 1161 C VAL A 172 16908 17820 20914 -1246 -564 70 C ATOM 1162 O VAL A 172 2.161 -37.009 -26.034 1.00148.09 O ANISOU 1162 O VAL A 172 16992 18019 21258 -1180 -605 20 O ATOM 1163 CB VAL A 172 4.662 -38.444 -26.938 1.00139.89 C ANISOU 1163 CB VAL A 172 16439 16901 19812 -1181 -901 5 C ATOM 1164 CG1 VAL A 172 5.571 -37.770 -25.922 1.00138.82 C ANISOU 1164 CG1 VAL A 172 16404 16874 19467 -1120 -717 -57 C ATOM 1165 CG2 VAL A 172 5.414 -39.524 -27.699 1.00138.02 C ANISOU 1165 CG2 VAL A 172 16387 16587 19466 -1200 -1106 35 C ATOM 1166 N PRO A 173 2.721 -38.062 -24.115 1.00142.76 N ANISOU 1166 N PRO A 173 16447 17439 20355 -1263 -329 105 N ATOM 1167 CA PRO A 173 2.100 -37.086 -23.212 1.00144.93 C ANISOU 1167 CA PRO A 173 16588 17804 20673 -1200 -96 84 C ATOM 1168 C PRO A 173 2.711 -35.697 -23.366 1.00147.06 C ANISOU 1168 C PRO A 173 16926 18109 20841 -1067 -92 -49 C ATOM 1169 O PRO A 173 3.889 -35.575 -23.701 1.00142.84 O ANISOU 1169 O PRO A 173 16580 17563 20131 -1031 -194 -116 O ATOM 1170 CB PRO A 173 2.422 -37.644 -21.822 1.00138.14 C ANISOU 1170 CB PRO A 173 15824 17020 19642 -1219 118 137 C ATOM 1171 CG PRO A 173 2.645 -39.097 -22.039 1.00134.36 C ANISOU 1171 CG PRO A 173 15434 16470 19146 -1336 11 230 C ATOM 1172 CD PRO A 173 3.292 -39.204 -23.382 1.00134.93 C ANISOU 1172 CD PRO A 173 15607 16457 19203 -1331 -270 174 C ATOM 1173 N MET A 174 1.913 -34.663 -23.122 1.00153.77 N ANISOU 1173 N MET A 174 17623 18997 21805 -995 29 -81 N ATOM 1174 CA MET A 174 2.391 -33.289 -23.215 1.00155.44 C ANISOU 1174 CA MET A 174 17899 19225 21938 -871 47 -205 C ATOM 1175 C MET A 174 3.023 -32.832 -21.905 1.00155.27 C ANISOU 1175 C MET A 174 17999 19290 21705 -811 243 -264 C ATOM 1176 O MET A 174 3.997 -32.080 -21.906 1.00154.08 O ANISOU 1176 O MET A 174 17994 19141 21408 -747 215 -372 O ATOM 1177 CB MET A 174 1.252 -32.347 -23.611 1.00159.36 C ANISOU 1177 CB MET A 174 18194 19712 22644 -800 71 -222 C ATOM 1178 CG MET A 174 0.722 -32.574 -25.016 1.00160.59 C ANISOU 1178 CG MET A 174 18248 19776 22991 -824 -156 -197 C ATOM 1179 SD MET A 174 1.991 -32.351 -26.278 1.00241.72 S ANISOU 1179 SD MET A 174 28743 29961 33139 -782 -395 -273 S ATOM 1180 CE MET A 174 2.478 -30.654 -25.971 1.00 78.92 C ANISOU 1180 CE MET A 174 8202 9363 12421 -643 -274 -398 C ATOM 1181 N ASN A 175 2.464 -33.291 -20.790 1.00158.09 N ANISOU 1181 N ASN A 175 18298 19718 22051 -827 440 -191 N ATOM 1182 CA ASN A 175 2.995 -32.957 -19.474 1.00162.12 C ANISOU 1182 CA ASN A 175 18937 20314 22346 -752 626 -243 C ATOM 1183 C ASN A 175 4.436 -33.427 -19.301 1.00164.83 C ANISOU 1183 C ASN A 175 19516 20665 22447 -771 539 -293 C ATOM 1184 O ASN A 175 5.189 -32.873 -18.498 1.00167.90 O ANISOU 1184 O ASN A 175 20042 21109 22643 -692 614 -390 O ATOM 1185 CB ASN A 175 2.108 -33.537 -18.370 1.00163.60 C ANISOU 1185 CB ASN A 175 19029 20571 22562 -761 858 -128 C ATOM 1186 CG ASN A 175 1.994 -35.048 -18.443 1.00164.84 C ANISOU 1186 CG ASN A 175 19178 20697 22755 -899 822 11 C ATOM 1187 OD1 ASN A 175 2.470 -35.673 -19.390 1.00160.85 O ANISOU 1187 OD1 ASN A 175 18728 20116 22271 -983 608 19 O ATOM 1188 ND2 ASN A 175 1.361 -35.643 -17.437 1.00169.64 N ANISOU 1188 ND2 ASN A 175 19731 21357 23368 -914 1038 125 N ATOM 1189 N TYR A 176 4.812 -34.449 -20.064 1.00160.91 N ANISOU 1189 N TYR A 176 19064 20113 21963 -867 371 -232 N ATOM 1190 CA TYR A 176 6.177 -34.963 -20.038 1.00155.56 C ANISOU 1190 CA TYR A 176 18596 19445 21065 -878 271 -271 C ATOM 1191 C TYR A 176 7.134 -34.026 -20.755 1.00142.74 C ANISOU 1191 C TYR A 176 17055 17795 19386 -826 134 -395 C ATOM 1192 O TYR A 176 8.075 -33.504 -20.158 1.00144.61 O ANISOU 1192 O TYR A 176 17416 18083 19447 -770 167 -496 O ATOM 1193 CB TYR A 176 6.241 -36.354 -20.675 1.00163.53 C ANISOU 1193 CB TYR A 176 19636 20394 22103 -983 132 -163 C ATOM 1194 CG TYR A 176 7.644 -36.829 -20.977 1.00169.53 C ANISOU 1194 CG TYR A 176 20600 21155 22661 -979 -11 -203 C ATOM 1195 CD1 TYR A 176 8.391 -37.504 -20.021 1.00173.93 C ANISOU 1195 CD1 TYR A 176 21312 21778 22994 -966 60 -194 C ATOM 1196 CD2 TYR A 176 8.225 -36.596 -22.218 1.00170.45 C ANISOU 1196 CD2 TYR A 176 20753 21209 22802 -972 -212 -245 C ATOM 1197 CE1 TYR A 176 9.678 -37.937 -20.293 1.00175.36 C ANISOU 1197 CE1 TYR A 176 21665 21972 22990 -950 -73 -231 C ATOM 1198 CE2 TYR A 176 9.511 -37.024 -22.499 1.00173.62 C ANISOU 1198 CE2 TYR A 176 21326 21622 23021 -957 -330 -272 C ATOM 1199 CZ TYR A 176 10.232 -37.694 -21.533 1.00175.52 C ANISOU 1199 CZ TYR A 176 21704 21937 23050 -948 -263 -267 C ATOM 1200 OH TYR A 176 11.511 -38.122 -21.807 1.00175.18 O ANISOU 1200 OH TYR A 176 21818 21917 22826 -922 -382 -294 O ATOM 1201 N MET A 177 6.880 -33.815 -22.041 1.00129.91 N ANISOU 1201 N MET A 177 15359 16085 17917 -844 -20 -387 N ATOM 1202 CA MET A 177 7.763 -33.006 -22.875 1.00118.84 C ANISOU 1202 CA MET A 177 14034 14641 16480 -799 -147 -478 C ATOM 1203 C MET A 177 7.858 -31.559 -22.405 1.00120.96 C ANISOU 1203 C MET A 177 14298 14928 16735 -716 -42 -595 C ATOM 1204 O MET A 177 8.778 -30.838 -22.777 1.00130.46 O ANISOU 1204 O MET A 177 15587 16105 17876 -686 -109 -681 O ATOM 1205 CB MET A 177 7.305 -33.036 -24.332 1.00107.93 C ANISOU 1205 CB MET A 177 12579 13160 15270 -809 -317 -436 C ATOM 1206 CG MET A 177 7.419 -34.409 -24.996 1.00 98.26 C ANISOU 1206 CG MET A 177 11399 11892 14041 -880 -471 -341 C ATOM 1207 SD MET A 177 6.966 -34.350 -26.723 1.00286.90 S ANISOU 1207 SD MET A 177 35238 35665 38107 -857 -692 -315 S ATOM 1208 CE MET A 177 8.147 -33.148 -27.346 1.00201.38 C ANISOU 1208 CE MET A 177 24528 24815 27174 -760 -735 -413 C ATOM 1209 N VAL A 178 6.914 -31.137 -21.572 1.00113.47 N ANISOU 1209 N VAL A 178 13251 14018 15844 -678 126 -596 N ATOM 1210 CA VAL A 178 6.926 -29.773 -21.051 1.00115.42 C ANISOU 1210 CA VAL A 178 13509 14274 16071 -586 229 -711 C ATOM 1211 C VAL A 178 7.663 -29.687 -19.719 1.00127.94 C ANISOU 1211 C VAL A 178 15227 15942 17441 -550 340 -789 C ATOM 1212 O VAL A 178 8.726 -29.075 -19.628 1.00135.03 O ANISOU 1212 O VAL A 178 16245 16834 18227 -529 288 -901 O ATOM 1213 CB VAL A 178 5.510 -29.197 -20.887 1.00111.49 C ANISOU 1213 CB VAL A 178 12843 13777 15742 -528 354 -684 C ATOM 1214 CG1 VAL A 178 5.568 -27.880 -20.138 1.00106.25 C ANISOU 1214 CG1 VAL A 178 12227 13126 15017 -418 477 -807 C ATOM 1215 CG2 VAL A 178 4.855 -29.016 -22.246 1.00111.02 C ANISOU 1215 CG2 VAL A 178 12661 13631 15890 -535 222 -642 C ATOM 1216 N TYR A 179 7.096 -30.300 -18.686 1.00134.23 N ANISOU 1216 N TYR A 179 16003 16814 18184 -538 491 -728 N ATOM 1217 CA TYR A 179 7.680 -30.235 -17.349 1.00146.93 C ANISOU 1217 CA TYR A 179 17747 18505 19573 -475 605 -800 C ATOM 1218 C TYR A 179 8.979 -31.030 -17.254 1.00150.41 C ANISOU 1218 C TYR A 179 18343 18978 19828 -521 494 -818 C ATOM 1219 O TYR A 179 10.048 -30.469 -17.015 1.00151.37 O ANISOU 1219 O TYR A 179 18582 19114 19820 -490 434 -945 O ATOM 1220 CB TYR A 179 6.683 -30.731 -16.299 1.00154.77 C ANISOU 1220 CB TYR A 179 18683 19569 20554 -434 815 -707 C ATOM 1221 CG TYR A 179 5.461 -29.852 -16.150 1.00160.27 C ANISOU 1221 CG TYR A 179 19234 20262 21401 -355 956 -702 C ATOM 1222 CD1 TYR A 179 5.453 -28.784 -15.262 1.00162.81 C ANISOU 1222 CD1 TYR A 179 19623 20614 21623 -221 1077 -816 C ATOM 1223 CD2 TYR A 179 4.312 -30.097 -16.891 1.00162.69 C ANISOU 1223 CD2 TYR A 179 19335 20533 21946 -406 958 -587 C ATOM 1224 CE1 TYR A 179 4.337 -27.981 -15.120 1.00165.73 C ANISOU 1224 CE1 TYR A 179 19867 20984 22118 -129 1211 -810 C ATOM 1225 CE2 TYR A 179 3.191 -29.300 -16.756 1.00164.44 C ANISOU 1225 CE2 TYR A 179 19411 20763 22305 -320 1086 -580 C ATOM 1226 CZ TYR A 179 3.207 -28.245 -15.868 1.00165.89 C ANISOU 1226 CZ TYR A 179 19672 20983 22378 -178 1220 -688 C ATOM 1227 OH TYR A 179 2.092 -27.449 -15.732 1.00165.43 O ANISOU 1227 OH TYR A 179 19475 20935 22444 -74 1352 -679 O ATOM 1228 N PHE A 180 8.878 -32.341 -17.444 1.00150.27 N ANISOU 1228 N PHE A 180 18322 18970 19805 -594 464 -691 N ATOM 1229 CA PHE A 180 10.024 -33.234 -17.301 1.00146.99 C ANISOU 1229 CA PHE A 180 18057 18593 19200 -622 372 -691 C ATOM 1230 C PHE A 180 11.106 -32.963 -18.346 1.00145.78 C ANISOU 1230 C PHE A 180 17951 18396 19044 -654 173 -756 C ATOM 1231 O PHE A 180 12.233 -32.602 -18.005 1.00151.00 O ANISOU 1231 O PHE A 180 18720 19098 19555 -622 124 -865 O ATOM 1232 CB PHE A 180 9.573 -34.695 -17.378 1.00147.74 C ANISOU 1232 CB PHE A 180 18141 18682 19312 -695 381 -531 C ATOM 1233 CG PHE A 180 10.674 -35.686 -17.130 1.00151.16 C ANISOU 1233 CG PHE A 180 18743 19157 19532 -703 304 -521 C ATOM 1234 CD1 PHE A 180 10.953 -36.126 -15.847 1.00153.78 C ANISOU 1234 CD1 PHE A 180 19197 19575 19657 -639 429 -525 C ATOM 1235 CD2 PHE A 180 11.426 -36.181 -18.181 1.00152.78 C ANISOU 1235 CD2 PHE A 180 18995 19320 19735 -755 111 -506 C ATOM 1236 CE1 PHE A 180 11.963 -37.040 -15.617 1.00154.52 C ANISOU 1236 CE1 PHE A 180 19452 19712 19547 -630 354 -517 C ATOM 1237 CE2 PHE A 180 12.439 -37.094 -17.960 1.00153.85 C ANISOU 1237 CE2 PHE A 180 19285 19502 19669 -746 42 -496 C ATOM 1238 CZ PHE A 180 12.708 -37.526 -16.675 1.00154.11 C ANISOU 1238 CZ PHE A 180 19434 19620 19499 -685 160 -503 C ATOM 1239 N ASN A 181 10.757 -33.138 -19.616 1.00138.75 N ANISOU 1239 N ASN A 181 16977 17422 18320 -712 59 -686 N ATOM 1240 CA ASN A 181 11.725 -33.008 -20.701 1.00132.24 C ANISOU 1240 CA ASN A 181 16201 16553 17492 -732 -117 -716 C ATOM 1241 C ASN A 181 12.263 -31.590 -20.876 1.00124.93 C ANISOU 1241 C ASN A 181 15277 15601 16591 -692 -131 -846 C ATOM 1242 O ASN A 181 13.435 -31.329 -20.610 1.00130.97 O ANISOU 1242 O ASN A 181 16133 16405 17226 -680 -175 -934 O ATOM 1243 CB ASN A 181 11.126 -33.513 -22.017 1.00132.95 C ANISOU 1243 CB ASN A 181 16215 16552 17748 -779 -235 -611 C ATOM 1244 CG ASN A 181 12.142 -33.550 -23.144 1.00131.27 C ANISOU 1244 CG ASN A 181 16075 16298 17504 -780 -406 -620 C ATOM 1245 OD1 ASN A 181 13.306 -33.195 -22.961 1.00131.97 O ANISOU 1245 OD1 ASN A 181 16249 16429 17466 -757 -431 -698 O ATOM 1246 ND2 ASN A 181 11.705 -33.987 -24.319 1.00132.35 N ANISOU 1246 ND2 ASN A 181 16175 16353 17759 -798 -527 -539 N ATOM 1247 N PHE A 182 11.407 -30.679 -21.327 1.00114.11 N ANISOU 1247 N PHE A 182 13802 14160 15394 -671 -97 -858 N ATOM 1248 CA PHE A 182 11.833 -29.315 -21.626 1.00117.20 C ANISOU 1248 CA PHE A 182 14201 14496 15833 -637 -112 -968 C ATOM 1249 C PHE A 182 12.456 -28.538 -20.467 1.00120.69 C ANISOU 1249 C PHE A 182 14723 14993 16143 -598 -34 -1106 C ATOM 1250 O PHE A 182 13.639 -28.206 -20.502 1.00124.29 O ANISOU 1250 O PHE A 182 15260 15465 16501 -615 -107 -1183 O ATOM 1251 CB PHE A 182 10.669 -28.490 -22.177 1.00128.32 C ANISOU 1251 CB PHE A 182 15494 15824 17438 -599 -71 -954 C ATOM 1252 CG PHE A 182 11.018 -27.053 -22.436 1.00138.41 C ANISOU 1252 CG PHE A 182 16794 17027 18767 -558 -69 -1063 C ATOM 1253 CD1 PHE A 182 12.058 -26.722 -23.290 1.00140.47 C ANISOU 1253 CD1 PHE A 182 17116 17230 19026 -583 -180 -1087 C ATOM 1254 CD2 PHE A 182 10.306 -26.031 -21.830 1.00144.57 C ANISOU 1254 CD2 PHE A 182 17541 17789 19600 -490 50 -1134 C ATOM 1255 CE1 PHE A 182 12.384 -25.400 -23.531 1.00144.74 C ANISOU 1255 CE1 PHE A 182 17681 17685 19628 -557 -169 -1177 C ATOM 1256 CE2 PHE A 182 10.628 -24.708 -22.069 1.00148.14 C ANISOU 1256 CE2 PHE A 182 18033 18154 20102 -455 49 -1235 C ATOM 1257 CZ PHE A 182 11.667 -24.393 -22.921 1.00148.80 C ANISOU 1257 CZ PHE A 182 18173 18168 20195 -496 -60 -1254 C ATOM 1258 N PHE A 183 11.658 -28.244 -19.445 1.00124.27 N ANISOU 1258 N PHE A 183 15150 15474 16593 -540 110 -1139 N ATOM 1259 CA PHE A 183 12.114 -27.412 -18.334 1.00131.96 C ANISOU 1259 CA PHE A 183 16212 16483 17443 -481 178 -1285 C ATOM 1260 C PHE A 183 13.308 -28.039 -17.609 1.00133.04 C ANISOU 1260 C PHE A 183 16470 16711 17369 -492 126 -1339 C ATOM 1261 O PHE A 183 14.345 -27.397 -17.442 1.00137.45 O ANISOU 1261 O PHE A 183 17096 17264 17866 -495 55 -1466 O ATOM 1262 CB PHE A 183 10.976 -27.145 -17.340 1.00144.19 C ANISOU 1262 CB PHE A 183 17730 18068 18988 -393 356 -1286 C ATOM 1263 CG PHE A 183 9.965 -26.140 -17.824 1.00154.69 C ANISOU 1263 CG PHE A 183 18959 19316 20502 -348 412 -1288 C ATOM 1264 CD1 PHE A 183 10.302 -24.802 -17.949 1.00159.68 C ANISOU 1264 CD1 PHE A 183 19635 19865 21171 -311 389 -1419 C ATOM 1265 CD2 PHE A 183 8.672 -26.532 -18.137 1.00158.12 C ANISOU 1265 CD2 PHE A 183 19252 19750 21075 -340 486 -1162 C ATOM 1266 CE1 PHE A 183 9.372 -23.875 -18.389 1.00161.84 C ANISOU 1266 CE1 PHE A 183 19832 20060 21601 -252 441 -1420 C ATOM 1267 CE2 PHE A 183 7.737 -25.610 -18.576 1.00160.32 C ANISOU 1267 CE2 PHE A 183 19433 19964 21517 -281 532 -1167 C ATOM 1268 CZ PHE A 183 8.088 -24.281 -18.701 1.00161.84 C ANISOU 1268 CZ PHE A 183 19689 20077 21727 -229 512 -1296 C ATOM 1269 N ALA A 184 13.162 -29.289 -17.183 1.00131.04 N ANISOU 1269 N ALA A 184 16241 16537 17011 -497 158 -1242 N ATOM 1270 CA ALA A 184 14.187 -29.942 -16.369 1.00131.09 C ANISOU 1270 CA ALA A 184 16372 16641 16794 -479 124 -1290 C ATOM 1271 C ALA A 184 15.381 -30.448 -17.177 1.00133.55 C ANISOU 1271 C ALA A 184 16715 16959 17069 -544 -44 -1279 C ATOM 1272 O ALA A 184 16.532 -30.185 -16.827 1.00131.62 O ANISOU 1272 O ALA A 184 16541 16760 16711 -534 -121 -1391 O ATOM 1273 CB ALA A 184 13.577 -31.080 -15.559 1.00128.05 C ANISOU 1273 CB ALA A 184 16022 16330 16300 -447 239 -1183 C ATOM 1274 N CYS A 185 15.104 -31.174 -18.255 1.00136.47 N ANISOU 1274 N CYS A 185 17031 17285 17537 -602 -106 -1145 N ATOM 1275 CA CYS A 185 16.157 -31.831 -19.026 1.00136.66 C ANISOU 1275 CA CYS A 185 17096 17323 17506 -642 -251 -1109 C ATOM 1276 C CYS A 185 16.651 -31.010 -20.216 1.00127.92 C ANISOU 1276 C CYS A 185 15936 16133 16534 -676 -348 -1134 C ATOM 1277 O CYS A 185 17.411 -31.511 -21.046 1.00127.35 O ANISOU 1277 O CYS A 185 15885 16061 16441 -698 -459 -1083 O ATOM 1278 CB CYS A 185 15.689 -33.209 -19.504 1.00139.50 C ANISOU 1278 CB CYS A 185 17462 17677 17863 -671 -277 -950 C ATOM 1279 SG CYS A 185 15.274 -34.363 -18.176 1.00147.42 S ANISOU 1279 SG CYS A 185 18549 18768 18694 -638 -159 -890 S ATOM 1280 N VAL A 186 16.221 -29.754 -20.301 1.00118.15 N ANISOU 1280 N VAL A 186 14641 14821 15429 -669 -299 -1206 N ATOM 1281 CA VAL A 186 16.668 -28.877 -21.381 1.00112.06 C ANISOU 1281 CA VAL A 186 13832 13957 14789 -695 -369 -1227 C ATOM 1282 C VAL A 186 16.893 -27.441 -20.914 1.00118.08 C ANISOU 1282 C VAL A 186 14593 14671 15601 -686 -326 -1374 C ATOM 1283 O VAL A 186 17.985 -26.896 -21.070 1.00122.62 O ANISOU 1283 O VAL A 186 15185 15234 16172 -718 -390 -1451 O ATOM 1284 CB VAL A 186 15.686 -28.881 -22.572 1.00102.90 C ANISOU 1284 CB VAL A 186 12599 12697 13801 -696 -382 -1114 C ATOM 1285 CG1 VAL A 186 16.016 -27.750 -23.535 1.00100.84 C ANISOU 1285 CG1 VAL A 186 12314 12328 13672 -698 -417 -1145 C ATOM 1286 CG2 VAL A 186 15.717 -30.225 -23.286 1.00 94.39 C ANISOU 1286 CG2 VAL A 186 11540 11639 12685 -711 -470 -980 C ATOM 1287 N LEU A 187 15.861 -26.832 -20.343 1.00121.21 N ANISOU 1287 N LEU A 187 14967 15037 16051 -642 -218 -1412 N ATOM 1288 CA LEU A 187 15.953 -25.447 -19.894 1.00121.60 C ANISOU 1288 CA LEU A 187 15034 15022 16148 -621 -178 -1555 C ATOM 1289 C LEU A 187 16.960 -25.296 -18.758 1.00114.34 C ANISOU 1289 C LEU A 187 14198 14177 15071 -617 -205 -1701 C ATOM 1290 O LEU A 187 17.780 -24.380 -18.768 1.00109.66 O ANISOU 1290 O LEU A 187 13624 13529 14514 -650 -259 -1817 O ATOM 1291 CB LEU A 187 14.583 -24.919 -19.464 1.00129.38 C ANISOU 1291 CB LEU A 187 15986 15972 17202 -549 -49 -1559 C ATOM 1292 CG LEU A 187 14.521 -23.429 -19.125 1.00132.91 C ANISOU 1292 CG LEU A 187 16465 16326 17710 -510 -7 -1700 C ATOM 1293 CD1 LEU A 187 14.949 -22.588 -20.319 1.00131.89 C ANISOU 1293 CD1 LEU A 187 16314 16064 17736 -559 -76 -1700 C ATOM 1294 CD2 LEU A 187 13.126 -23.036 -18.664 1.00134.52 C ANISOU 1294 CD2 LEU A 187 16633 16516 17960 -415 130 -1689 C ATOM 1295 N VAL A 188 16.897 -26.199 -17.784 1.00116.57 N ANISOU 1295 N VAL A 188 14532 14578 15181 -574 -170 -1694 N ATOM 1296 CA VAL A 188 17.818 -26.166 -16.650 1.00123.99 C ANISOU 1296 CA VAL A 188 15564 15603 15945 -545 -208 -1834 C ATOM 1297 C VAL A 188 19.280 -26.320 -17.079 1.00128.21 C ANISOU 1297 C VAL A 188 16097 16167 16452 -616 -353 -1872 C ATOM 1298 O VAL A 188 20.129 -25.519 -16.685 1.00127.63 O ANISOU 1298 O VAL A 188 16044 16078 16370 -634 -419 -2023 O ATOM 1299 CB VAL A 188 17.466 -27.231 -15.588 1.00122.86 C ANISOU 1299 CB VAL A 188 15492 15583 15606 -470 -135 -1795 C ATOM 1300 CG1 VAL A 188 18.577 -27.337 -14.552 1.00121.45 C ANISOU 1300 CG1 VAL A 188 15417 15502 15226 -429 -207 -1935 C ATOM 1301 CG2 VAL A 188 16.136 -26.902 -14.929 1.00126.01 C ANISOU 1301 CG2 VAL A 188 15892 15965 16022 -385 28 -1782 C ATOM 1302 N PRO A 189 19.581 -27.354 -17.883 1.00125.85 N ANISOU 1302 N PRO A 189 15770 15909 16140 -652 -408 -1736 N ATOM 1303 CA PRO A 189 20.950 -27.523 -18.381 1.00118.86 C ANISOU 1303 CA PRO A 189 14868 15059 15233 -705 -534 -1753 C ATOM 1304 C PRO A 189 21.453 -26.279 -19.106 1.00114.49 C ANISOU 1304 C PRO A 189 14251 14390 14860 -774 -571 -1814 C ATOM 1305 O PRO A 189 22.540 -25.794 -18.802 1.00120.39 O ANISOU 1305 O PRO A 189 14991 15158 15595 -812 -647 -1933 O ATOM 1306 CB PRO A 189 20.821 -28.688 -19.364 1.00116.23 C ANISOU 1306 CB PRO A 189 14519 14747 14897 -715 -561 -1572 C ATOM 1307 CG PRO A 189 19.662 -29.469 -18.860 1.00118.55 C ANISOU 1307 CG PRO A 189 14849 15068 15129 -667 -470 -1492 C ATOM 1308 CD PRO A 189 18.701 -28.455 -18.315 1.00122.50 C ANISOU 1308 CD PRO A 189 15331 15501 15713 -640 -362 -1565 C ATOM 1309 N LEU A 190 20.667 -25.773 -20.051 1.00107.53 N ANISOU 1309 N LEU A 190 13324 13386 14149 -789 -520 -1734 N ATOM 1310 CA LEU A 190 21.052 -24.582 -20.803 1.00108.11 C ANISOU 1310 CA LEU A 190 13351 13328 14397 -846 -535 -1772 C ATOM 1311 C LEU A 190 21.288 -23.388 -19.883 1.00107.54 C ANISOU 1311 C LEU A 190 13308 13203 14349 -859 -528 -1960 C ATOM 1312 O LEU A 190 22.118 -22.527 -20.173 1.00108.09 O ANISOU 1312 O LEU A 190 13349 13196 14524 -931 -574 -2032 O ATOM 1313 CB LEU A 190 19.997 -24.238 -21.858 1.00116.66 C ANISOU 1313 CB LEU A 190 14402 14287 15637 -828 -474 -1659 C ATOM 1314 CG LEU A 190 19.870 -25.205 -23.037 1.00123.69 C ANISOU 1314 CG LEU A 190 15268 15190 16540 -819 -510 -1482 C ATOM 1315 CD1 LEU A 190 18.723 -24.795 -23.947 1.00133.84 C ANISOU 1315 CD1 LEU A 190 16526 16355 17973 -782 -462 -1397 C ATOM 1316 CD2 LEU A 190 21.173 -25.278 -23.817 1.00118.87 C ANISOU 1316 CD2 LEU A 190 14638 14586 15940 -864 -586 -1447 C ATOM 1317 N LEU A 191 20.554 -23.338 -18.777 1.00112.13 N ANISOU 1317 N LEU A 191 13951 13819 14836 -787 -467 -2038 N ATOM 1318 CA LEU A 191 20.728 -22.271 -17.799 1.00120.46 C ANISOU 1318 CA LEU A 191 15062 14825 15882 -774 -471 -2230 C ATOM 1319 C LEU A 191 22.016 -22.470 -17.009 1.00119.98 C ANISOU 1319 C LEU A 191 15027 14864 15696 -801 -588 -2361 C ATOM 1320 O LEU A 191 22.662 -21.503 -16.606 1.00120.48 O ANISOU 1320 O LEU A 191 15106 14863 15810 -842 -652 -2522 O ATOM 1321 CB LEU A 191 19.525 -22.193 -16.857 1.00127.74 C ANISOU 1321 CB LEU A 191 16052 15762 16721 -661 -359 -2263 C ATOM 1322 CG LEU A 191 18.213 -21.720 -17.486 1.00127.30 C ANISOU 1322 CG LEU A 191 15961 15601 16808 -623 -247 -2172 C ATOM 1323 CD1 LEU A 191 17.073 -21.792 -16.479 1.00130.32 C ANISOU 1323 CD1 LEU A 191 16392 16029 17094 -501 -124 -2189 C ATOM 1324 CD2 LEU A 191 18.356 -20.310 -18.044 1.00123.52 C ANISOU 1324 CD2 LEU A 191 15478 14947 16507 -666 -259 -2246 C ATOM 1325 N LEU A 192 22.383 -23.729 -16.790 1.00121.81 N ANISOU 1325 N LEU A 192 15266 15248 15767 -773 -624 -2295 N ATOM 1326 CA LEU A 192 23.645 -24.053 -16.138 1.00125.27 C ANISOU 1326 CA LEU A 192 15719 15801 16079 -785 -747 -2405 C ATOM 1327 C LEU A 192 24.809 -23.737 -17.068 1.00118.27 C ANISOU 1327 C LEU A 192 14724 14880 15333 -902 -841 -2394 C ATOM 1328 O LEU A 192 25.783 -23.103 -16.666 1.00113.81 O ANISOU 1328 O LEU A 192 14134 14310 14799 -957 -940 -2545 O ATOM 1329 CB LEU A 192 23.684 -25.528 -15.735 1.00128.78 C ANISOU 1329 CB LEU A 192 16210 16411 16309 -710 -750 -2318 C ATOM 1330 CG LEU A 192 22.721 -25.966 -14.632 1.00130.55 C ANISOU 1330 CG LEU A 192 16546 16693 16365 -589 -651 -2329 C ATOM 1331 CD1 LEU A 192 22.819 -27.466 -14.402 1.00131.80 C ANISOU 1331 CD1 LEU A 192 16753 16993 16332 -531 -650 -2217 C ATOM 1332 CD2 LEU A 192 22.999 -25.205 -13.346 1.00129.49 C ANISOU 1332 CD2 LEU A 192 16500 16569 16130 -524 -689 -2545 C ATOM 1333 N MET A 193 24.697 -24.185 -18.315 1.00116.25 N ANISOU 1333 N MET A 193 14405 14599 15165 -935 -810 -2214 N ATOM 1334 CA MET A 193 25.721 -23.933 -19.322 1.00115.73 C ANISOU 1334 CA MET A 193 14238 14500 15234 -1028 -867 -2166 C ATOM 1335 C MET A 193 25.955 -22.439 -19.504 1.00124.10 C ANISOU 1335 C MET A 193 15259 15396 16499 -1118 -865 -2270 C ATOM 1336 O MET A 193 27.094 -21.973 -19.480 1.00135.08 O ANISOU 1336 O MET A 193 16577 16783 17962 -1204 -947 -2354 O ATOM 1337 CB MET A 193 25.326 -24.562 -20.658 1.00106.67 C ANISOU 1337 CB MET A 193 13061 13327 14141 -1017 -817 -1952 C ATOM 1338 CG MET A 193 25.216 -26.075 -20.625 1.00101.19 C ANISOU 1338 CG MET A 193 12409 12776 13262 -944 -835 -1840 C ATOM 1339 SD MET A 193 24.906 -26.772 -22.256 1.00174.37 S ANISOU 1339 SD MET A 193 21655 22000 22596 -927 -813 -1609 S ATOM 1340 CE MET A 193 26.288 -26.095 -23.171 1.00236.45 C ANISOU 1340 CE MET A 193 29417 29827 30597 -1004 -856 -1597 C ATOM 1341 N LEU A 194 24.872 -21.692 -19.691 1.00120.67 N ANISOU 1341 N LEU A 194 14867 14820 16164 -1098 -772 -2261 N ATOM 1342 CA LEU A 194 24.966 -20.247 -19.841 1.00125.30 C ANISOU 1342 CA LEU A 194 15443 15226 16938 -1171 -759 -2358 C ATOM 1343 C LEU A 194 25.658 -19.636 -18.629 1.00120.61 C ANISOU 1343 C LEU A 194 14878 14642 16307 -1204 -855 -2586 C ATOM 1344 O LEU A 194 26.477 -18.727 -18.761 1.00117.96 O ANISOU 1344 O LEU A 194 14491 14206 16123 -1314 -911 -2676 O ATOM 1345 CB LEU A 194 23.578 -19.630 -20.025 1.00132.79 C ANISOU 1345 CB LEU A 194 16456 16044 17956 -1107 -645 -2328 C ATOM 1346 CG LEU A 194 23.545 -18.122 -20.276 1.00137.68 C ANISOU 1346 CG LEU A 194 17091 16454 18768 -1166 -618 -2411 C ATOM 1347 CD1 LEU A 194 24.388 -17.765 -21.492 1.00143.72 C ANISOU 1347 CD1 LEU A 194 17770 17128 19709 -1272 -625 -2314 C ATOM 1348 CD2 LEU A 194 22.116 -17.633 -20.447 1.00133.53 C ANISOU 1348 CD2 LEU A 194 16629 15823 18285 -1073 -505 -2372 C ATOM 1349 N GLY A 195 25.326 -20.148 -17.447 1.00118.32 N ANISOU 1349 N GLY A 195 14673 14468 15815 -1106 -874 -2677 N ATOM 1350 CA GLY A 195 25.936 -19.683 -16.215 1.00120.39 C ANISOU 1350 CA GLY A 195 14986 14754 16001 -1104 -982 -2903 C ATOM 1351 C GLY A 195 27.420 -19.990 -16.158 1.00125.08 C ANISOU 1351 C GLY A 195 15484 15449 16591 -1188 -1128 -2962 C ATOM 1352 O GLY A 195 28.201 -19.229 -15.588 1.00128.38 O ANISOU 1352 O GLY A 195 15888 15823 17068 -1254 -1243 -3147 O ATOM 1353 N VAL A 196 27.809 -21.116 -16.750 1.00124.44 N ANISOU 1353 N VAL A 196 15334 15503 16444 -1181 -1130 -2807 N ATOM 1354 CA VAL A 196 29.212 -21.508 -16.804 1.00117.14 C ANISOU 1354 CA VAL A 196 14300 14695 15513 -1245 -1256 -2835 C ATOM 1355 C VAL A 196 30.022 -20.513 -17.625 1.00114.67 C ANISOU 1355 C VAL A 196 13854 14249 15467 -1404 -1280 -2841 C ATOM 1356 O VAL A 196 31.003 -19.950 -17.142 1.00115.24 O ANISOU 1356 O VAL A 196 13858 14317 15611 -1489 -1404 -3001 O ATOM 1357 CB VAL A 196 29.390 -22.919 -17.398 1.00107.02 C ANISOU 1357 CB VAL A 196 12987 13571 14105 -1188 -1237 -2646 C ATOM 1358 CG1 VAL A 196 30.844 -23.161 -17.769 1.00108.06 C ANISOU 1358 CG1 VAL A 196 12976 13799 14283 -1261 -1343 -2642 C ATOM 1359 CG2 VAL A 196 28.901 -23.974 -16.419 1.00102.50 C ANISOU 1359 CG2 VAL A 196 12539 13146 13260 -1045 -1239 -2661 C ATOM 1360 N TYR A 197 29.602 -20.296 -18.868 1.00112.84 N ANISOU 1360 N TYR A 197 13585 13902 15385 -1442 -1163 -2665 N ATOM 1361 CA TYR A 197 30.291 -19.367 -19.756 1.00117.80 C ANISOU 1361 CA TYR A 197 14099 14389 16271 -1584 -1150 -2634 C ATOM 1362 C TYR A 197 30.351 -17.962 -19.164 1.00121.04 C ANISOU 1362 C TYR A 197 14535 14622 16832 -1674 -1192 -2831 C ATOM 1363 O TYR A 197 31.216 -17.163 -19.525 1.00121.55 O ANISOU 1363 O TYR A 197 14492 14583 17106 -1817 -1226 -2867 O ATOM 1364 CB TYR A 197 29.628 -19.340 -21.136 1.00121.16 C ANISOU 1364 CB TYR A 197 14526 14707 16801 -1570 -1006 -2414 C ATOM 1365 CG TYR A 197 29.857 -20.598 -21.944 1.00122.95 C ANISOU 1365 CG TYR A 197 14710 15079 16926 -1506 -985 -2217 C ATOM 1366 CD1 TYR A 197 31.015 -20.765 -22.692 1.00124.23 C ANISOU 1366 CD1 TYR A 197 14739 15289 17172 -1571 -1003 -2127 C ATOM 1367 CD2 TYR A 197 28.915 -21.617 -21.962 1.00126.30 C ANISOU 1367 CD2 TYR A 197 15228 15588 17174 -1379 -945 -2119 C ATOM 1368 CE1 TYR A 197 31.229 -21.912 -23.433 1.00125.47 C ANISOU 1368 CE1 TYR A 197 14876 15575 17220 -1492 -986 -1951 C ATOM 1369 CE2 TYR A 197 29.121 -22.769 -22.699 1.00127.31 C ANISOU 1369 CE2 TYR A 197 15336 15831 17205 -1318 -940 -1948 C ATOM 1370 CZ TYR A 197 30.279 -22.910 -23.434 1.00125.40 C ANISOU 1370 CZ TYR A 197 14981 15636 17029 -1365 -963 -1867 C ATOM 1371 OH TYR A 197 30.492 -24.053 -24.171 1.00122.38 O ANISOU 1371 OH TYR A 197 14599 15365 16536 -1284 -960 -1700 O ATOM 1372 N LEU A 198 29.429 -17.664 -18.254 1.00125.54 N ANISOU 1372 N LEU A 198 15250 15151 17299 -1588 -1185 -2955 N ATOM 1373 CA LEU A 198 29.450 -16.392 -17.544 1.00134.46 C ANISOU 1373 CA LEU A 198 16438 16118 18533 -1646 -1243 -3165 C ATOM 1374 C LEU A 198 30.717 -16.289 -16.706 1.00136.38 C ANISOU 1374 C LEU A 198 16608 16436 18773 -1724 -1432 -3360 C ATOM 1375 O LEU A 198 31.409 -15.272 -16.731 1.00134.19 O ANISOU 1375 O LEU A 198 16268 16016 18704 -1869 -1503 -3474 O ATOM 1376 CB LEU A 198 28.219 -16.249 -16.648 1.00137.92 C ANISOU 1376 CB LEU A 198 17056 16533 18815 -1500 -1197 -3255 C ATOM 1377 CG LEU A 198 26.869 -16.074 -17.344 1.00134.53 C ANISOU 1377 CG LEU A 198 16696 15999 18421 -1424 -1024 -3104 C ATOM 1378 CD1 LEU A 198 25.743 -16.053 -16.324 1.00135.22 C ANISOU 1378 CD1 LEU A 198 16938 16104 18336 -1268 -979 -3194 C ATOM 1379 CD2 LEU A 198 26.862 -14.806 -18.185 1.00133.61 C ANISOU 1379 CD2 LEU A 198 16562 15638 18565 -1531 -970 -3086 C ATOM 1380 N ARG A 199 31.015 -17.351 -15.965 1.00140.93 N ANISOU 1380 N ARG A 199 17195 17234 19118 -1628 -1516 -3400 N ATOM 1381 CA ARG A 199 32.202 -17.392 -15.123 1.00149.35 C ANISOU 1381 CA ARG A 199 18193 18404 20149 -1672 -1713 -3589 C ATOM 1382 C ARG A 199 33.464 -17.537 -15.967 1.00149.93 C ANISOU 1382 C ARG A 199 18044 18526 20396 -1816 -1759 -3502 C ATOM 1383 O ARG A 199 34.516 -17.001 -15.621 1.00155.36 O ANISOU 1383 O ARG A 199 18619 19198 21212 -1935 -1908 -3656 O ATOM 1384 CB ARG A 199 32.107 -18.542 -14.118 1.00153.13 C ANISOU 1384 CB ARG A 199 18765 19109 20308 -1499 -1776 -3640 C ATOM 1385 CG ARG A 199 30.809 -18.582 -13.327 1.00158.54 C ANISOU 1385 CG ARG A 199 19662 19775 20802 -1335 -1694 -3682 C ATOM 1386 CD ARG A 199 30.571 -17.288 -12.568 1.00170.49 C ANISOU 1386 CD ARG A 199 21282 21112 22386 -1349 -1754 -3907 C ATOM 1387 NE ARG A 199 29.359 -17.350 -11.753 1.00180.20 N ANISOU 1387 NE ARG A 199 22713 22340 23414 -1167 -1666 -3945 N ATOM 1388 CZ ARG A 199 28.145 -17.030 -12.191 1.00181.81 C ANISOU 1388 CZ ARG A 199 22987 22429 23663 -1123 -1490 -3831 C ATOM 1389 NH1 ARG A 199 27.972 -16.625 -13.442 1.00182.22 N ANISOU 1389 NH1 ARG A 199 22941 22351 23941 -1238 -1392 -3677 N ATOM 1390 NH2 ARG A 199 27.100 -17.117 -11.379 1.00179.69 N ANISOU 1390 NH2 ARG A 199 22885 22180 23210 -950 -1408 -3866 N ATOM 1391 N ILE A 200 33.352 -18.266 -17.074 1.00139.79 N ANISOU 1391 N ILE A 200 16695 17301 19116 -1800 -1633 -3254 N ATOM 1392 CA ILE A 200 34.487 -18.493 -17.962 1.00130.08 C ANISOU 1392 CA ILE A 200 15262 16131 18030 -1906 -1644 -3136 C ATOM 1393 C ILE A 200 35.068 -17.187 -18.491 1.00138.51 C ANISOU 1393 C ILE A 200 16209 16991 19425 -2102 -1639 -3171 C ATOM 1394 O ILE A 200 36.232 -16.873 -18.244 1.00145.63 O ANISOU 1394 O ILE A 200 16954 17922 20457 -2224 -1767 -3280 O ATOM 1395 CB ILE A 200 34.108 -19.391 -19.157 1.00113.28 C ANISOU 1395 CB ILE A 200 13126 14065 15851 -1834 -1493 -2856 C ATOM 1396 CG1 ILE A 200 33.866 -20.825 -18.689 1.00105.55 C ANISOU 1396 CG1 ILE A 200 12227 13310 14568 -1666 -1521 -2812 C ATOM 1397 CG2 ILE A 200 35.202 -19.366 -20.213 1.00111.07 C ANISOU 1397 CG2 ILE A 200 12646 13800 15756 -1942 -1468 -2719 C ATOM 1398 CD1 ILE A 200 33.647 -21.805 -19.820 1.00104.27 C ANISOU 1398 CD1 ILE A 200 12055 13217 14346 -1595 -1410 -2556 C ATOM 1399 N PHE A 201 34.251 -16.427 -19.213 1.00139.84 N ANISOU 1399 N PHE A 201 16451 16949 19734 -2132 -1492 -3077 N ATOM 1400 CA PHE A 201 34.708 -15.186 -19.828 1.00147.80 C ANISOU 1400 CA PHE A 201 17369 17732 21057 -2313 -1454 -3077 C ATOM 1401 C PHE A 201 34.938 -14.077 -18.803 1.00158.16 C ANISOU 1401 C PHE A 201 18716 18900 22477 -2414 -1595 -3351 C ATOM 1402 O PHE A 201 35.759 -13.186 -19.019 1.00163.14 O ANISOU 1402 O PHE A 201 19222 19392 23373 -2598 -1636 -3406 O ATOM 1403 CB PHE A 201 33.728 -14.729 -20.910 1.00148.94 C ANISOU 1403 CB PHE A 201 17605 17692 21295 -2287 -1255 -2892 C ATOM 1404 CG PHE A 201 33.634 -15.673 -22.075 1.00151.19 C ANISOU 1404 CG PHE A 201 17845 18083 21518 -2206 -1128 -2623 C ATOM 1405 CD1 PHE A 201 34.520 -15.576 -23.136 1.00151.16 C ANISOU 1405 CD1 PHE A 201 17683 18057 21693 -2300 -1059 -2463 C ATOM 1406 CD2 PHE A 201 32.662 -16.660 -22.109 1.00153.24 C ANISOU 1406 CD2 PHE A 201 18224 18458 21540 -2031 -1079 -2530 C ATOM 1407 CE1 PHE A 201 34.440 -16.443 -24.209 1.00150.30 C ANISOU 1407 CE1 PHE A 201 17557 18042 21509 -2203 -950 -2222 C ATOM 1408 CE2 PHE A 201 32.575 -17.531 -23.179 1.00151.76 C ANISOU 1408 CE2 PHE A 201 18012 18355 21293 -1952 -985 -2296 C ATOM 1409 CZ PHE A 201 33.465 -17.421 -24.232 1.00151.08 C ANISOU 1409 CZ PHE A 201 17789 18248 21368 -2028 -924 -2145 C ATOM 1410 N ALA A 202 34.217 -14.136 -17.688 1.00161.64 N ANISOU 1410 N ALA A 202 19331 19368 22715 -2291 -1668 -3521 N ATOM 1411 CA ALA A 202 34.390 -13.156 -16.622 1.00166.71 C ANISOU 1411 CA ALA A 202 20043 19883 23417 -2352 -1823 -3800 C ATOM 1412 C ALA A 202 35.761 -13.307 -15.972 1.00169.10 C ANISOU 1412 C ALA A 202 20183 20311 23757 -2447 -2041 -3967 C ATOM 1413 O ALA A 202 36.418 -12.318 -15.645 1.00170.51 O ANISOU 1413 O ALA A 202 20301 20340 24146 -2605 -2168 -4142 O ATOM 1414 CB ALA A 202 33.290 -13.296 -15.583 1.00166.06 C ANISOU 1414 CB ALA A 202 20194 19827 23074 -2161 -1835 -3925 C ATOM 1415 N ALA A 203 36.185 -14.554 -15.792 1.00168.48 N ANISOU 1415 N ALA A 203 20033 20503 23477 -2349 -2090 -3912 N ATOM 1416 CA ALA A 203 37.478 -14.850 -15.187 1.00171.57 C ANISOU 1416 CA ALA A 203 20262 21053 23874 -2408 -2301 -4059 C ATOM 1417 C ALA A 203 38.603 -14.744 -16.210 1.00170.35 C ANISOU 1417 C ALA A 203 19832 20901 23992 -2591 -2274 -3921 C ATOM 1418 O ALA A 203 39.716 -14.336 -15.881 1.00171.40 O ANISOU 1418 O ALA A 203 19789 21041 24295 -2735 -2441 -4066 O ATOM 1419 CB ALA A 203 37.462 -16.235 -14.558 1.00168.83 C ANISOU 1419 CB ALA A 203 19969 20994 23185 -2208 -2360 -4054 C ATOM 1420 N ALA A 204 38.303 -15.114 -17.451 1.00164.21 N ANISOU 1420 N ALA A 204 19017 20120 23257 -2579 -2063 -3640 N ATOM 1421 CA ALA A 204 39.289 -15.072 -18.526 1.00161.18 C ANISOU 1421 CA ALA A 204 18388 19744 23110 -2721 -1994 -3468 C ATOM 1422 C ALA A 204 39.817 -13.658 -18.744 1.00168.28 C ANISOU 1422 C ALA A 204 19176 20387 24377 -2960 -2011 -3548 C ATOM 1423 O ALA A 204 41.007 -13.463 -18.992 1.00174.25 O ANISOU 1423 O ALA A 204 19685 21172 25351 -3118 -2070 -3546 O ATOM 1424 CB ALA A 204 38.696 -15.624 -19.813 1.00155.09 C ANISOU 1424 CB ALA A 204 17651 18978 22297 -2636 -1759 -3160 C ATOM 1425 N ARG A 205 38.928 -12.675 -18.647 1.00170.48 N ANISOU 1425 N ARG A 205 19635 20412 24729 -2986 -1955 -3616 N ATOM 1426 CA ARG A 205 39.312 -11.278 -18.819 1.00178.87 C ANISOU 1426 CA ARG A 205 20635 21193 26135 -3208 -1967 -3698 C ATOM 1427 C ARG A 205 40.037 -10.741 -17.588 1.00186.56 C ANISOU 1427 C ARG A 205 21558 22147 27181 -3315 -2241 -4020 C ATOM 1428 O ARG A 205 40.764 -9.751 -17.671 1.00193.44 O ANISOU 1428 O ARG A 205 22296 22833 28369 -3539 -2304 -4104 O ATOM 1429 CB ARG A 205 38.091 -10.412 -19.141 1.00183.83 C ANISOU 1429 CB ARG A 205 21494 21553 26802 -3178 -1817 -3662 C ATOM 1430 CG ARG A 205 37.709 -10.395 -20.616 1.00189.63 C ANISOU 1430 CG ARG A 205 22217 22196 27636 -3172 -1554 -3352 C ATOM 1431 CD ARG A 205 37.455 -11.799 -21.146 1.00191.94 C ANISOU 1431 CD ARG A 205 22498 22749 27680 -2989 -1461 -3142 C ATOM 1432 NE ARG A 205 37.040 -11.795 -22.546 1.00193.15 N ANISOU 1432 NE ARG A 205 22667 22814 27906 -2957 -1226 -2858 N ATOM 1433 CZ ARG A 205 35.775 -11.757 -22.952 1.00190.76 C ANISOU 1433 CZ ARG A 205 22564 22420 27495 -2820 -1094 -2762 C ATOM 1434 NH1 ARG A 205 34.791 -11.718 -22.062 1.00189.39 N ANISOU 1434 NH1 ARG A 205 22581 22235 27144 -2708 -1155 -2916 N ATOM 1435 NH2 ARG A 205 35.492 -11.756 -24.247 1.00188.66 N ANISOU 1435 NH2 ARG A 205 22308 22079 27297 -2784 -900 -2511 N ATOM 1436 N ARG A 206 39.833 -11.394 -16.448 1.00185.81 N ANISOU 1436 N ARG A 206 21574 22232 26791 -3152 -2405 -4200 N ATOM 1437 CA ARG A 206 40.561 -11.042 -15.233 1.00189.38 C ANISOU 1437 CA ARG A 206 21987 22704 27265 -3215 -2693 -4515 C ATOM 1438 C ARG A 206 41.983 -11.589 -15.299 1.00185.69 C ANISOU 1438 C ARG A 206 21210 22445 26898 -3313 -2822 -4513 C ATOM 1439 O ARG A 206 42.919 -10.980 -14.779 1.00187.39 O ANISOU 1439 O ARG A 206 21274 22607 27317 -3478 -3033 -4719 O ATOM 1440 CB ARG A 206 39.843 -11.566 -13.986 1.00192.14 C ANISOU 1440 CB ARG A 206 22581 23179 27242 -2978 -2813 -4699 C ATOM 1441 CG ARG A 206 38.514 -10.884 -13.702 1.00195.89 C ANISOU 1441 CG ARG A 206 23353 23445 27633 -2882 -2722 -4755 C ATOM 1442 CD ARG A 206 38.028 -11.175 -12.286 1.00199.35 C ANISOU 1442 CD ARG A 206 24014 23983 27748 -2673 -2878 -4990 C ATOM 1443 NE ARG A 206 37.762 -12.595 -12.067 1.00200.02 N ANISOU 1443 NE ARG A 206 24137 24362 27498 -2459 -2834 -4883 N ATOM 1444 CZ ARG A 206 36.567 -13.162 -12.208 1.00200.51 C ANISOU 1444 CZ ARG A 206 24378 24471 27337 -2276 -2646 -4731 C ATOM 1445 NH1 ARG A 206 35.522 -12.429 -12.566 1.00201.34 N ANISOU 1445 NH1 ARG A 206 24630 24362 27509 -2268 -2487 -4673 N ATOM 1446 NH2 ARG A 206 36.416 -14.462 -11.989 1.00199.39 N ANISOU 1446 NH2 ARG A 206 24262 24585 26911 -2101 -2618 -4638 N ATOM 1447 N GLN A 207 42.137 -12.741 -15.945 1.00177.61 N ANISOU 1447 N GLN A 207 20092 21657 25734 -3207 -2702 -4283 N ATOM 1448 CA GLN A 207 43.454 -13.321 -16.168 1.00168.33 C ANISOU 1448 CA GLN A 207 18614 20693 24649 -3278 -2786 -4236 C ATOM 1449 C GLN A 207 44.294 -12.358 -16.993 1.00160.84 C ANISOU 1449 C GLN A 207 17413 19562 24138 -3556 -2728 -4161 C ATOM 1450 O GLN A 207 45.478 -12.160 -16.724 1.00165.93 O ANISOU 1450 O GLN A 207 17798 20265 24981 -3708 -2898 -4276 O ATOM 1451 CB GLN A 207 43.340 -14.663 -16.894 1.00166.79 C ANISOU 1451 CB GLN A 207 18399 20743 24232 -3104 -2625 -3966 C ATOM 1452 CG GLN A 207 42.497 -15.702 -16.174 1.00169.76 C ANISOU 1452 CG GLN A 207 19019 21296 24186 -2837 -2653 -4002 C ATOM 1453 CD GLN A 207 43.125 -16.174 -14.876 1.00176.94 C ANISOU 1453 CD GLN A 207 19910 22407 24911 -2752 -2927 -4257 C ATOM 1454 OE1 GLN A 207 44.288 -15.888 -14.595 1.00184.93 O ANISOU 1454 OE1 GLN A 207 20692 23471 26102 -2883 -3108 -4391 O ATOM 1455 NE2 GLN A 207 42.354 -16.906 -14.078 1.00173.55 N ANISOU 1455 NE2 GLN A 207 19723 22093 24124 -2525 -2959 -4322 N ATOM 1456 N LEU A 208 43.666 -11.758 -18.000 1.00153.23 N ANISOU 1456 N LEU A 208 16522 18373 23326 -3618 -2485 -3963 N ATOM 1457 CA LEU A 208 44.345 -10.810 -18.873 1.00155.69 C ANISOU 1457 CA LEU A 208 16626 18480 24051 -3873 -2382 -3855 C ATOM 1458 C LEU A 208 44.662 -9.507 -18.147 1.00169.60 C ANISOU 1458 C LEU A 208 18373 19985 26081 -4088 -2568 -4130 C ATOM 1459 O LEU A 208 45.605 -8.803 -18.506 1.00178.16 O ANISOU 1459 O LEU A 208 19212 20949 27531 -4335 -2583 -4122 O ATOM 1460 CB LEU A 208 43.502 -10.523 -20.117 1.00149.53 C ANISOU 1460 CB LEU A 208 15971 17518 23325 -3848 -2072 -3574 C ATOM 1461 CG LEU A 208 43.221 -11.713 -21.036 1.00148.87 C ANISOU 1461 CG LEU A 208 15896 17646 23023 -3654 -1877 -3281 C ATOM 1462 CD1 LEU A 208 42.356 -11.287 -22.211 1.00151.19 C ANISOU 1462 CD1 LEU A 208 16332 17731 23383 -3628 -1600 -3037 C ATOM 1463 CD2 LEU A 208 44.520 -12.335 -21.523 1.00150.10 C ANISOU 1463 CD2 LEU A 208 15732 18017 23281 -3711 -1874 -3150 C ATOM 1464 N LYS A 209 43.872 -9.189 -17.127 1.00176.59 N ANISOU 1464 N LYS A 209 19525 20784 26789 -3993 -2706 -4369 N ATOM 1465 CA LYS A 209 44.089 -7.973 -16.353 1.00193.93 C ANISOU 1465 CA LYS A 209 21756 22728 29201 -4167 -2907 -4655 C ATOM 1466 C LYS A 209 45.258 -8.137 -15.387 1.00203.91 C ANISOU 1466 C LYS A 209 22811 24149 30516 -4248 -3230 -4914 C ATOM 1467 O LYS A 209 46.040 -7.209 -15.184 1.00208.73 O ANISOU 1467 O LYS A 209 23263 24584 31461 -4493 -3381 -5070 O ATOM 1468 CB LYS A 209 42.824 -7.576 -15.593 1.00200.92 C ANISOU 1468 CB LYS A 209 23013 23469 29859 -4009 -2939 -4821 C ATOM 1469 CG LYS A 209 42.952 -6.262 -14.839 1.00212.20 C ANISOU 1469 CG LYS A 209 24524 24604 31497 -4170 -3138 -5115 C ATOM 1470 CD LYS A 209 41.651 -5.896 -14.145 1.00217.28 C ANISOU 1470 CD LYS A 209 25548 25114 31894 -3980 -3140 -5255 C ATOM 1471 CE LYS A 209 41.773 -4.572 -13.409 1.00223.99 C ANISOU 1471 CE LYS A 209 26507 25657 32942 -4126 -3344 -5553 C ATOM 1472 NZ LYS A 209 40.502 -4.202 -12.728 1.00224.34 N ANISOU 1472 NZ LYS A 209 26929 25577 32735 -3918 -3337 -5686 N ATOM 1473 N GLN A 210 45.370 -9.320 -14.790 1.00207.00 N ANISOU 1473 N GLN A 210 23206 24866 30578 -4038 -3341 -4960 N ATOM 1474 CA GLN A 210 46.493 -9.623 -13.912 1.00212.60 C ANISOU 1474 CA GLN A 210 23713 25768 31299 -4075 -3648 -5190 C ATOM 1475 C GLN A 210 47.778 -9.702 -14.725 1.00210.93 C ANISOU 1475 C GLN A 210 23090 25643 31411 -4282 -3613 -5036 C ATOM 1476 O GLN A 210 48.851 -9.327 -14.251 1.00214.63 O ANISOU 1476 O GLN A 210 23315 26123 32111 -4455 -3853 -5228 O ATOM 1477 CB GLN A 210 46.261 -10.938 -13.168 1.00215.73 C ANISOU 1477 CB GLN A 210 24230 26495 31242 -3776 -3741 -5239 C ATOM 1478 CG GLN A 210 45.036 -10.937 -12.269 1.00220.60 C ANISOU 1478 CG GLN A 210 25239 27056 31524 -3554 -3775 -5391 C ATOM 1479 CD GLN A 210 44.885 -12.231 -11.494 1.00223.56 C ANISOU 1479 CD GLN A 210 25727 27751 31465 -3267 -3864 -5438 C ATOM 1480 OE1 GLN A 210 45.777 -13.080 -11.503 1.00223.56 O ANISOU 1480 OE1 GLN A 210 25515 28013 31413 -3235 -3949 -5402 O ATOM 1481 NE2 GLN A 210 43.754 -12.387 -10.817 1.00224.92 N ANISOU 1481 NE2 GLN A 210 26234 27903 31324 -3051 -3838 -5511 N ATOM 1482 N MET A 211 47.659 -10.195 -15.953 1.00205.57 N ANISOU 1482 N MET A 211 22333 25027 30747 -4254 -3314 -4690 N ATOM 1483 CA MET A 211 48.791 -10.261 -16.867 1.00205.89 C ANISOU 1483 CA MET A 211 21998 25141 31090 -4428 -3220 -4494 C ATOM 1484 C MET A 211 49.007 -8.909 -17.534 1.00215.65 C ANISOU 1484 C MET A 211 23128 26027 32781 -4728 -3107 -4438 C ATOM 1485 O MET A 211 49.984 -8.707 -18.254 1.00224.12 O ANISOU 1485 O MET A 211 23876 27101 34178 -4920 -3026 -4292 O ATOM 1486 CB MET A 211 48.563 -11.340 -17.925 1.00196.55 C ANISOU 1486 CB MET A 211 20803 24159 29717 -4252 -2943 -4144 C ATOM 1487 CG MET A 211 48.400 -12.739 -17.357 1.00192.38 C ANISOU 1487 CG MET A 211 20372 23971 28751 -3964 -3035 -4170 C ATOM 1488 SD MET A 211 48.158 -13.975 -18.646 1.00183.31 S ANISOU 1488 SD MET A 211 19221 23029 27400 -3767 -2725 -3765 S ATOM 1489 CE MET A 211 49.663 -13.761 -19.589 1.00265.58 C ANISOU 1489 CE MET A 211 29182 33505 38220 -3985 -2645 -3586 C ATOM 1490 N GLU A 212 48.082 -7.986 -17.291 1.00216.20 N ANISOU 1490 N GLU A 212 23480 25794 32871 -4757 -3092 -4547 N ATOM 1491 CA GLU A 212 48.199 -6.627 -17.803 1.00221.22 C ANISOU 1491 CA GLU A 212 24069 26060 33923 -5033 -3003 -4524 C ATOM 1492 C GLU A 212 49.033 -5.789 -16.842 1.00224.07 C ANISOU 1492 C GLU A 212 24288 26294 34555 -5263 -3332 -4860 C ATOM 1493 O GLU A 212 49.537 -4.724 -17.201 1.00225.68 O ANISOU 1493 O GLU A 212 24345 26224 35178 -5549 -3312 -4861 O ATOM 1494 CB GLU A 212 46.813 -6.005 -17.985 1.00224.58 C ANISOU 1494 CB GLU A 212 24874 26213 34241 -4945 -2841 -4491 C ATOM 1495 CG GLU A 212 46.822 -4.610 -18.586 1.00231.43 C ANISOU 1495 CG GLU A 212 25742 26679 35511 -5202 -2719 -4442 C ATOM 1496 CD GLU A 212 45.427 -4.030 -18.730 1.00232.26 C ANISOU 1496 CD GLU A 212 26232 26533 35482 -5083 -2569 -4418 C ATOM 1497 OE1 GLU A 212 44.450 -4.731 -18.386 1.00228.40 O ANISOU 1497 OE1 GLU A 212 25988 26193 34600 -4808 -2553 -4429 O ATOM 1498 OE2 GLU A 212 45.306 -2.874 -19.187 1.00235.60 O ANISOU 1498 OE2 GLU A 212 26710 26610 36198 -5263 -2464 -4384 O ATOM 1499 N SER A 213 49.178 -6.286 -15.617 1.00225.25 N ANISOU 1499 N SER A 213 24487 26639 34461 -5131 -3641 -5146 N ATOM 1500 CA SER A 213 49.958 -5.602 -14.594 1.00232.97 C ANISOU 1500 CA SER A 213 25347 27526 35646 -5310 -4002 -5501 C ATOM 1501 C SER A 213 51.131 -6.462 -14.136 1.00241.11 C ANISOU 1501 C SER A 213 26056 28906 36649 -5293 -4229 -5592 C ATOM 1502 O SER A 213 51.470 -6.486 -12.953 1.00245.10 O ANISOU 1502 O SER A 213 26578 29490 37058 -5252 -4578 -5922 O ATOM 1503 CB SER A 213 49.073 -5.244 -13.398 1.00229.71 C ANISOU 1503 CB SER A 213 25319 26993 34968 -5156 -4213 -5816 C ATOM 1504 OG SER A 213 47.991 -4.418 -13.791 1.00227.01 O ANISOU 1504 OG SER A 213 25270 26330 34652 -5162 -4012 -5742 O ATOM 1505 N GLN A 214 51.747 -7.167 -15.080 1.00244.18 N ANISOU 1505 N GLN A 214 26161 29506 37111 -5306 -4033 -5299 N ATOM 1506 CA GLN A 214 52.878 -8.036 -14.772 1.00247.39 C ANISOU 1506 CA GLN A 214 26242 30262 37492 -5273 -4214 -5346 C ATOM 1507 C GLN A 214 54.197 -7.416 -15.224 1.00259.45 C ANISOU 1507 C GLN A 214 27312 31725 39543 -5611 -4255 -5315 C ATOM 1508 O GLN A 214 54.279 -6.841 -16.310 1.00261.64 O ANISOU 1508 O GLN A 214 27470 31808 40133 -5801 -3977 -5060 O ATOM 1509 CB GLN A 214 52.690 -9.413 -15.413 1.00239.09 C ANISOU 1509 CB GLN A 214 25193 29538 36110 -5009 -3989 -5053 C ATOM 1510 CG GLN A 214 52.573 -9.379 -16.927 1.00234.86 C ANISOU 1510 CG GLN A 214 24568 28924 35743 -5076 -3588 -4649 C ATOM 1511 CD GLN A 214 52.334 -10.752 -17.525 1.00231.22 C ANISOU 1511 CD GLN A 214 24148 28773 34933 -4797 -3390 -4380 C ATOM 1512 OE1 GLN A 214 52.233 -11.746 -16.806 1.00231.95 O ANISOU 1512 OE1 GLN A 214 24339 29133 34656 -4558 -3541 -4488 O ATOM 1513 NE2 GLN A 214 52.236 -10.813 -18.848 1.00227.81 N ANISOU 1513 NE2 GLN A 214 23656 28294 34608 -4818 -3050 -4028 N ATOM 1514 N PRO A 215 55.235 -7.530 -14.381 1.00265.02 N ANISOU 1514 N PRO A 215 27756 32594 40346 -5682 -4603 -5574 N ATOM 1515 CA PRO A 215 56.572 -6.984 -14.649 1.00271.50 C ANISOU 1515 CA PRO A 215 28099 33383 41675 -6008 -4694 -5585 C ATOM 1516 C PRO A 215 57.331 -7.766 -15.720 1.00274.54 C ANISOU 1516 C PRO A 215 28128 34033 42151 -6000 -4440 -5232 C ATOM 1517 O PRO A 215 58.551 -7.636 -15.818 1.00275.88 O ANISOU 1517 O PRO A 215 27857 34293 42670 -6204 -4543 -5244 O ATOM 1518 CB PRO A 215 57.288 -7.130 -13.299 1.00272.17 C ANISOU 1518 CB PRO A 215 28070 33632 41710 -5988 -5171 -5989 C ATOM 1519 CG PRO A 215 56.200 -7.345 -12.290 1.00269.52 C ANISOU 1519 CG PRO A 215 28218 33283 40905 -5707 -5323 -6221 C ATOM 1520 CD PRO A 215 55.135 -8.087 -13.024 1.00265.25 C ANISOU 1520 CD PRO A 215 27956 32820 40009 -5454 -4953 -5905 C ATOM 1521 N LEU A 216 56.620 -8.566 -16.508 1.00278.63 N ANISOU 1521 N LEU A 216 28832 34672 42361 -5761 -4118 -4925 N ATOM 1522 CA LEU A 216 57.252 -9.362 -17.557 1.00280.42 C ANISOU 1522 CA LEU A 216 28773 35149 42623 -5708 -3861 -4578 C ATOM 1523 C LEU A 216 56.322 -9.591 -18.747 1.00275.68 C ANISOU 1523 C LEU A 216 28410 34465 41871 -5576 -3436 -4209 C ATOM 1524 O LEU A 216 55.101 -9.613 -18.591 1.00278.27 O ANISOU 1524 O LEU A 216 29152 34674 41904 -5412 -3375 -4232 O ATOM 1525 CB LEU A 216 57.752 -10.699 -16.992 1.00278.81 C ANISOU 1525 CB LEU A 216 28472 35389 42075 -5443 -4044 -4648 C ATOM 1526 CG LEU A 216 56.796 -11.544 -16.143 1.00273.40 C ANISOU 1526 CG LEU A 216 28201 34849 40828 -5100 -4170 -4798 C ATOM 1527 CD1 LEU A 216 55.691 -12.160 -16.990 1.00266.66 C ANISOU 1527 CD1 LEU A 216 27662 33998 39660 -4874 -3819 -4492 C ATOM 1528 CD2 LEU A 216 57.565 -12.631 -15.407 1.00273.28 C ANISOU 1528 CD2 LEU A 216 28026 35236 40572 -4904 -4427 -4935 C ATOM 1529 N PRO A 217 56.902 -9.754 -19.946 1.00261.97 N ANISOU 1529 N PRO A 217 26406 32790 40339 -5640 -3143 -3867 N ATOM 1530 CA PRO A 217 56.131 -10.013 -21.167 1.00249.78 C ANISOU 1530 CA PRO A 217 25062 31185 38660 -5502 -2742 -3501 C ATOM 1531 C PRO A 217 55.255 -11.257 -21.036 1.00232.75 C ANISOU 1531 C PRO A 217 23228 29263 35944 -5123 -2714 -3452 C ATOM 1532 O PRO A 217 54.028 -11.147 -21.026 1.00230.63 O ANISOU 1532 O PRO A 217 23347 28834 35450 -5003 -2631 -3453 O ATOM 1533 CB PRO A 217 57.217 -10.243 -22.221 1.00250.32 C ANISOU 1533 CB PRO A 217 24721 31396 38995 -5588 -2518 -3194 C ATOM 1534 CG PRO A 217 58.399 -9.498 -21.710 1.00258.00 C ANISOU 1534 CG PRO A 217 25286 32321 40420 -5906 -2742 -3386 C ATOM 1535 CD PRO A 217 58.345 -9.636 -20.219 1.00262.19 C ANISOU 1535 CD PRO A 217 25917 32941 40763 -5854 -3176 -3808 C ATOM 1536 N GLY A 218 55.886 -12.423 -20.935 1.00219.22 N ANISOU 1536 N GLY A 218 21349 27923 34020 -4939 -2781 -3408 N ATOM 1537 CA GLY A 218 55.167 -13.675 -20.790 1.00202.71 C ANISOU 1537 CA GLY A 218 19541 26066 31412 -4588 -2766 -3360 C ATOM 1538 C GLY A 218 54.067 -13.844 -21.820 1.00186.86 C ANISOU 1538 C GLY A 218 17834 23931 29232 -4446 -2432 -3073 C ATOM 1539 O GLY A 218 52.899 -14.023 -21.472 1.00179.49 O ANISOU 1539 O GLY A 218 17275 22923 28001 -4290 -2442 -3143 O ATOM 1540 N GLU A 219 54.441 -13.782 -23.094 1.00181.76 N ANISOU 1540 N GLU A 219 17021 23260 28778 -4494 -2135 -2746 N ATOM 1541 CA GLU A 219 53.477 -13.921 -24.179 1.00175.61 C ANISOU 1541 CA GLU A 219 16510 22360 27856 -4355 -1817 -2460 C ATOM 1542 C GLU A 219 53.064 -15.376 -24.371 1.00175.98 C ANISOU 1542 C GLU A 219 16735 22689 27441 -4012 -1770 -2332 C ATOM 1543 O GLU A 219 52.084 -15.667 -25.057 1.00176.69 O ANISOU 1543 O GLU A 219 17106 22703 27326 -3850 -1572 -2151 O ATOM 1544 CB GLU A 219 54.039 -13.347 -25.481 1.00174.35 C ANISOU 1544 CB GLU A 219 16127 22071 28047 -4504 -1511 -2150 C ATOM 1545 CG GLU A 219 54.323 -11.858 -25.413 1.00179.25 C ANISOU 1545 CG GLU A 219 16611 22359 29136 -4852 -1515 -2242 C ATOM 1546 CD GLU A 219 53.109 -11.059 -24.981 1.00180.49 C ANISOU 1546 CD GLU A 219 17135 22201 29242 -4891 -1562 -2409 C ATOM 1547 OE1 GLU A 219 53.273 -10.094 -24.207 1.00179.83 O ANISOU 1547 OE1 GLU A 219 17003 21920 29404 -5124 -1757 -2666 O ATOM 1548 OE2 GLU A 219 51.985 -11.403 -25.404 1.00184.11 O ANISOU 1548 OE2 GLU A 219 17930 22612 29411 -4683 -1414 -2290 O ATOM 1549 N ARG A 220 53.818 -16.287 -23.766 1.00178.23 N ANISOU 1549 N ARG A 220 16857 23296 27568 -3900 -1961 -2430 N ATOM 1550 CA ARG A 220 53.463 -17.701 -23.783 1.00179.63 C ANISOU 1550 CA ARG A 220 17215 23740 27295 -3576 -1957 -2346 C ATOM 1551 C ARG A 220 52.138 -17.916 -23.064 1.00174.07 C ANISOU 1551 C ARG A 220 16923 22952 26263 -3436 -2053 -2507 C ATOM 1552 O ARG A 220 51.248 -18.601 -23.568 1.00164.85 O ANISOU 1552 O ARG A 220 16025 21800 24812 -3229 -1906 -2345 O ATOM 1553 CB ARG A 220 54.560 -18.538 -23.125 1.00185.63 C ANISOU 1553 CB ARG A 220 17724 24847 27961 -3491 -2175 -2460 C ATOM 1554 CG ARG A 220 55.739 -18.831 -24.032 1.00192.90 C ANISOU 1554 CG ARG A 220 18283 25947 29065 -3502 -2023 -2215 C ATOM 1555 CD ARG A 220 55.395 -19.911 -25.047 1.00197.28 C ANISOU 1555 CD ARG A 220 18999 26639 29318 -3220 -1785 -1907 C ATOM 1556 NE ARG A 220 56.450 -20.077 -26.042 1.00206.84 N ANISOU 1556 NE ARG A 220 19886 27987 30716 -3221 -1592 -1641 N ATOM 1557 CZ ARG A 220 56.392 -19.593 -27.278 1.00212.14 C ANISOU 1557 CZ ARG A 220 20526 28495 31581 -3279 -1282 -1355 C ATOM 1558 NH1 ARG A 220 55.323 -18.917 -27.677 1.00213.47 N ANISOU 1558 NH1 ARG A 220 20972 28357 31781 -3338 -1142 -1305 N ATOM 1559 NH2 ARG A 220 57.400 -19.789 -28.119 1.00213.96 N ANISOU 1559 NH2 ARG A 220 20456 28873 31967 -3260 -1105 -1114 N ATOM 1560 N ALA A 221 52.014 -17.320 -21.883 1.00176.64 N ANISOU 1560 N ALA A 221 17294 23187 26634 -3548 -2302 -2826 N ATOM 1561 CA ALA A 221 50.795 -17.435 -21.094 1.00169.20 C ANISOU 1561 CA ALA A 221 16727 22164 25399 -3422 -2396 -2994 C ATOM 1562 C ALA A 221 49.640 -16.692 -21.755 1.00162.46 C ANISOU 1562 C ALA A 221 16119 20997 24613 -3470 -2179 -2875 C ATOM 1563 O ALA A 221 48.493 -17.129 -21.685 1.00160.36 O ANISOU 1563 O ALA A 221 16168 20703 24057 -3294 -2124 -2851 O ATOM 1564 CB ALA A 221 51.025 -16.920 -19.681 1.00172.63 C ANISOU 1564 CB ALA A 221 17145 22575 25873 -3519 -2717 -3366 C ATOM 1565 N ARG A 222 49.944 -15.566 -22.395 1.00160.48 N ANISOU 1565 N ARG A 222 15718 20508 24749 -3708 -2054 -2798 N ATOM 1566 CA ARG A 222 48.921 -14.787 -23.084 1.00156.88 C ANISOU 1566 CA ARG A 222 15483 19746 24378 -3753 -1842 -2677 C ATOM 1567 C ARG A 222 48.401 -15.515 -24.317 1.00160.92 C ANISOU 1567 C ARG A 222 16117 20309 24716 -3561 -1568 -2346 C ATOM 1568 O ARG A 222 47.192 -15.650 -24.503 1.00166.98 O ANISOU 1568 O ARG A 222 17188 20977 25280 -3425 -1477 -2295 O ATOM 1569 CB ARG A 222 49.449 -13.406 -23.478 1.00153.80 C ANISOU 1569 CB ARG A 222 14903 19080 24454 -4056 -1771 -2667 C ATOM 1570 CG ARG A 222 48.911 -12.274 -22.619 1.00157.21 C ANISOU 1570 CG ARG A 222 15487 19233 25011 -4209 -1921 -2941 C ATOM 1571 CD ARG A 222 49.128 -10.926 -23.280 1.00169.66 C ANISOU 1571 CD ARG A 222 16965 20479 27017 -4476 -1774 -2862 C ATOM 1572 NE ARG A 222 48.645 -9.829 -22.446 1.00184.20 N ANISOU 1572 NE ARG A 222 18965 22044 28979 -4619 -1929 -3134 N ATOM 1573 CZ ARG A 222 49.415 -9.119 -21.628 1.00201.52 C ANISOU 1573 CZ ARG A 222 20981 24159 31430 -4841 -2168 -3390 C ATOM 1574 NH1 ARG A 222 50.711 -9.389 -21.533 1.00208.81 N ANISOU 1574 NH1 ARG A 222 21538 25270 32531 -4955 -2278 -3408 N ATOM 1575 NH2 ARG A 222 48.888 -8.137 -20.908 1.00206.23 N ANISOU 1575 NH2 ARG A 222 21765 24488 32106 -4943 -2303 -3633 N ATOM 1576 N SER A 223 49.318 -15.979 -25.159 1.00157.74 N ANISOU 1576 N SER A 223 15475 20063 24395 -3543 -1441 -2123 N ATOM 1577 CA SER A 223 48.942 -16.711 -26.361 1.00157.43 C ANISOU 1577 CA SER A 223 15545 20084 24185 -3344 -1194 -1808 C ATOM 1578 C SER A 223 48.116 -17.943 -26.008 1.00162.07 C ANISOU 1578 C SER A 223 16401 20851 24327 -3067 -1267 -1831 C ATOM 1579 O SER A 223 47.082 -18.205 -26.622 1.00163.48 O ANISOU 1579 O SER A 223 16837 20944 24334 -2924 -1123 -1689 O ATOM 1580 CB SER A 223 50.183 -17.120 -27.156 1.00157.27 C ANISOU 1580 CB SER A 223 15213 20250 24293 -3340 -1077 -1592 C ATOM 1581 OG SER A 223 49.821 -17.783 -28.354 1.00153.17 O ANISOU 1581 OG SER A 223 14821 19772 23603 -3134 -839 -1289 O ATOM 1582 N THR A 224 48.577 -18.693 -25.013 1.00164.69 N ANISOU 1582 N THR A 224 16670 21427 24478 -2993 -1493 -2011 N ATOM 1583 CA THR A 224 47.870 -19.886 -24.561 1.00162.54 C ANISOU 1583 CA THR A 224 16643 21326 23787 -2742 -1573 -2044 C ATOM 1584 C THR A 224 46.495 -19.530 -24.003 1.00157.27 C ANISOU 1584 C THR A 224 16293 20469 22994 -2719 -1605 -2180 C ATOM 1585 O THR A 224 45.499 -20.185 -24.308 1.00152.44 O ANISOU 1585 O THR A 224 15931 19859 22130 -2541 -1519 -2075 O ATOM 1586 CB THR A 224 48.670 -20.643 -23.483 1.00164.60 C ANISOU 1586 CB THR A 224 16781 21869 23891 -2673 -1823 -2236 C ATOM 1587 OG1 THR A 224 49.952 -21.011 -24.007 1.00164.86 O ANISOU 1587 OG1 THR A 224 16505 22098 24036 -2677 -1791 -2105 O ATOM 1588 CG2 THR A 224 47.928 -21.897 -23.047 1.00162.76 C ANISOU 1588 CG2 THR A 224 16818 21796 23225 -2411 -1883 -2250 C ATOM 1589 N LEU A 225 46.453 -18.487 -23.181 1.00153.99 N ANISOU 1589 N LEU A 225 15860 19889 22759 -2899 -1734 -2417 N ATOM 1590 CA LEU A 225 45.204 -18.022 -22.594 1.00145.66 C ANISOU 1590 CA LEU A 225 15090 18649 21608 -2882 -1764 -2559 C ATOM 1591 C LEU A 225 44.222 -17.632 -23.692 1.00143.19 C ANISOU 1591 C LEU A 225 14945 18117 21344 -2862 -1518 -2345 C ATOM 1592 O LEU A 225 43.047 -17.991 -23.640 1.00143.81 O ANISOU 1592 O LEU A 225 15285 18159 21198 -2716 -1473 -2325 O ATOM 1593 CB LEU A 225 45.467 -16.836 -21.661 1.00145.49 C ANISOU 1593 CB LEU A 225 15002 18461 21816 -3091 -1935 -2837 C ATOM 1594 CG LEU A 225 44.365 -16.391 -20.694 1.00144.16 C ANISOU 1594 CG LEU A 225 15110 18147 21516 -3056 -2033 -3056 C ATOM 1595 CD1 LEU A 225 43.226 -15.697 -21.427 1.00145.59 C ANISOU 1595 CD1 LEU A 225 15491 18058 21769 -3069 -1825 -2928 C ATOM 1596 CD2 LEU A 225 43.848 -17.572 -19.884 1.00139.98 C ANISOU 1596 CD2 LEU A 225 14765 17839 20581 -2817 -2137 -3133 C ATOM 1597 N GLN A 226 44.711 -16.903 -24.690 1.00144.73 N ANISOU 1597 N GLN A 226 14986 18170 21836 -3002 -1355 -2180 N ATOM 1598 CA GLN A 226 43.868 -16.454 -25.793 1.00150.75 C ANISOU 1598 CA GLN A 226 15902 18716 22661 -2977 -1119 -1971 C ATOM 1599 C GLN A 226 43.369 -17.618 -26.645 1.00156.35 C ANISOU 1599 C GLN A 226 16744 19565 23099 -2735 -989 -1735 C ATOM 1600 O GLN A 226 42.288 -17.547 -27.232 1.00157.44 O ANISOU 1600 O GLN A 226 17099 19564 23156 -2641 -861 -1625 O ATOM 1601 CB GLN A 226 44.612 -15.442 -26.668 1.00153.91 C ANISOU 1601 CB GLN A 226 16102 18939 23438 -3174 -964 -1834 C ATOM 1602 CG GLN A 226 44.969 -14.150 -25.958 1.00162.37 C ANISOU 1602 CG GLN A 226 17073 19805 24815 -3433 -1075 -2055 C ATOM 1603 CD GLN A 226 45.612 -13.137 -26.884 1.00175.76 C ANISOU 1603 CD GLN A 226 18592 21295 26895 -3633 -893 -1895 C ATOM 1604 OE1 GLN A 226 45.465 -13.213 -28.103 1.00176.67 O ANISOU 1604 OE1 GLN A 226 18738 21358 27030 -3558 -652 -1616 O ATOM 1605 NE2 GLN A 226 46.330 -12.179 -26.308 1.00186.50 N ANISOU 1605 NE2 GLN A 226 19771 22528 28562 -3886 -1009 -2070 N ATOM 1606 N LYS A 227 44.158 -18.685 -26.712 1.00162.27 N ANISOU 1606 N LYS A 227 17365 20583 23707 -2629 -1032 -1664 N ATOM 1607 CA LYS A 227 43.776 -19.863 -27.481 1.00169.80 C ANISOU 1607 CA LYS A 227 18449 21675 24393 -2393 -934 -1452 C ATOM 1608 C LYS A 227 42.774 -20.727 -26.720 1.00170.34 C ANISOU 1608 C LYS A 227 18763 21831 24128 -2229 -1051 -1564 C ATOM 1609 O LYS A 227 41.910 -21.365 -27.322 1.00170.03 O ANISOU 1609 O LYS A 227 18919 21784 23900 -2065 -962 -1421 O ATOM 1610 CB LYS A 227 45.009 -20.680 -27.871 1.00177.20 C ANISOU 1610 CB LYS A 227 19167 22862 25299 -2325 -927 -1325 C ATOM 1611 CG LYS A 227 45.924 -19.974 -28.857 1.00184.20 C ANISOU 1611 CG LYS A 227 19820 23673 26496 -2449 -754 -1143 C ATOM 1612 CD LYS A 227 47.140 -20.819 -29.198 1.00190.14 C ANISOU 1612 CD LYS A 227 20346 24694 27205 -2362 -744 -1016 C ATOM 1613 CE LYS A 227 48.062 -20.091 -30.163 1.00197.10 C ANISOU 1613 CE LYS A 227 20978 25502 28411 -2488 -549 -823 C ATOM 1614 NZ LYS A 227 49.278 -20.887 -30.485 1.00199.97 N ANISOU 1614 NZ LYS A 227 21100 26139 28740 -2395 -529 -694 N ATOM 1615 N GLU A 228 42.895 -20.741 -25.397 1.00171.71 N ANISOU 1615 N GLU A 228 18925 22083 24235 -2272 -1252 -1819 N ATOM 1616 CA GLU A 228 41.942 -21.450 -24.550 1.00169.94 C ANISOU 1616 CA GLU A 228 18932 21925 23713 -2130 -1353 -1936 C ATOM 1617 C GLU A 228 40.602 -20.723 -24.543 1.00163.30 C ANISOU 1617 C GLU A 228 18304 20843 22902 -2152 -1280 -1970 C ATOM 1618 O GLU A 228 39.544 -21.346 -24.441 1.00158.07 O ANISOU 1618 O GLU A 228 17853 20191 22016 -2009 -1262 -1944 O ATOM 1619 CB GLU A 228 42.482 -21.584 -23.125 1.00173.19 C ANISOU 1619 CB GLU A 228 19281 22480 24045 -2157 -1583 -2201 C ATOM 1620 CG GLU A 228 43.675 -22.519 -22.999 1.00174.00 C ANISOU 1620 CG GLU A 228 19205 22860 24046 -2084 -1678 -2181 C ATOM 1621 CD GLU A 228 43.308 -23.969 -23.252 1.00170.69 C ANISOU 1621 CD GLU A 228 18942 22618 23296 -1847 -1648 -2040 C ATOM 1622 OE1 GLU A 228 42.112 -24.310 -23.131 1.00170.63 O ANISOU 1622 OE1 GLU A 228 19182 22542 23108 -1748 -1611 -2027 O ATOM 1623 OE2 GLU A 228 44.215 -24.768 -23.566 1.00166.85 O ANISOU 1623 OE2 GLU A 228 18327 22336 22733 -1760 -1664 -1943 O ATOM 1624 N VAL A 229 40.658 -19.399 -24.652 1.00158.82 N ANISOU 1624 N VAL A 229 17674 20053 22618 -2331 -1238 -2027 N ATOM 1625 CA VAL A 229 39.454 -18.584 -24.741 1.00149.27 C ANISOU 1625 CA VAL A 229 16654 18599 21464 -2351 -1156 -2049 C ATOM 1626 C VAL A 229 38.812 -18.745 -26.114 1.00147.58 C ANISOU 1626 C VAL A 229 16536 18294 21243 -2255 -953 -1784 C ATOM 1627 O VAL A 229 37.588 -18.733 -26.243 1.00149.54 O ANISOU 1627 O VAL A 229 16984 18440 21393 -2166 -896 -1759 O ATOM 1628 CB VAL A 229 39.758 -17.097 -24.486 1.00143.84 C ANISOU 1628 CB VAL A 229 15883 17684 21087 -2570 -1172 -2186 C ATOM 1629 CG1 VAL A 229 38.553 -16.237 -24.833 1.00145.66 C ANISOU 1629 CG1 VAL A 229 16308 17651 21385 -2572 -1052 -2161 C ATOM 1630 CG2 VAL A 229 40.170 -16.883 -23.038 1.00140.74 C ANISOU 1630 CG2 VAL A 229 15449 17353 20675 -2643 -1399 -2482 C ATOM 1631 N HIS A 230 39.645 -18.904 -27.137 1.00145.51 N ANISOU 1631 N HIS A 230 16128 18075 21083 -2263 -847 -1587 N ATOM 1632 CA HIS A 230 39.154 -19.113 -28.493 1.00143.09 C ANISOU 1632 CA HIS A 230 15917 17696 20753 -2146 -663 -1329 C ATOM 1633 C HIS A 230 38.407 -20.439 -28.590 1.00135.90 C ANISOU 1633 C HIS A 230 15176 16935 19523 -1928 -690 -1256 C ATOM 1634 O HIS A 230 37.441 -20.565 -29.342 1.00135.73 O ANISOU 1634 O HIS A 230 15321 16817 19434 -1817 -593 -1127 O ATOM 1635 CB HIS A 230 40.307 -19.086 -29.496 1.00149.25 C ANISOU 1635 CB HIS A 230 16503 18519 21687 -2178 -544 -1133 C ATOM 1636 CG HIS A 230 39.873 -19.248 -30.917 1.00153.68 C ANISOU 1636 CG HIS A 230 17174 18999 22220 -2042 -353 -867 C ATOM 1637 ND1 HIS A 230 39.590 -18.175 -31.738 1.00154.82 N ANISOU 1637 ND1 HIS A 230 17355 18894 22575 -2106 -188 -760 N ATOM 1638 CD2 HIS A 230 39.666 -20.355 -31.669 1.00156.04 C ANISOU 1638 CD2 HIS A 230 17570 19423 22295 -1831 -309 -691 C ATOM 1639 CE1 HIS A 230 39.233 -18.615 -32.929 1.00155.17 C ANISOU 1639 CE1 HIS A 230 17513 18924 22519 -1932 -52 -531 C ATOM 1640 NE2 HIS A 230 39.270 -19.937 -32.914 1.00156.18 N ANISOU 1640 NE2 HIS A 230 17680 19275 22386 -1765 -128 -489 N ATOM 1641 N ALA A 231 38.863 -21.425 -27.826 1.00129.91 N ANISOU 1641 N ALA A 231 14377 16408 18574 -1866 -828 -1340 N ATOM 1642 CA ALA A 231 38.215 -22.730 -27.795 1.00127.53 C ANISOU 1642 CA ALA A 231 14238 16246 17971 -1673 -867 -1284 C ATOM 1643 C ALA A 231 36.929 -22.672 -26.976 1.00129.01 C ANISOU 1643 C ALA A 231 14613 16357 18047 -1648 -922 -1425 C ATOM 1644 O ALA A 231 35.908 -23.239 -27.363 1.00126.49 O ANISOU 1644 O ALA A 231 14462 16012 17586 -1523 -879 -1332 O ATOM 1645 CB ALA A 231 39.160 -23.778 -27.229 1.00128.18 C ANISOU 1645 CB ALA A 231 14225 16593 17885 -1608 -990 -1326 C ATOM 1646 N ALA A 232 36.989 -21.985 -25.840 1.00131.65 N ANISOU 1646 N ALA A 232 14916 16656 18449 -1763 -1019 -1649 N ATOM 1647 CA ALA A 232 35.817 -21.812 -24.989 1.00131.42 C ANISOU 1647 CA ALA A 232 15056 16552 18326 -1737 -1058 -1789 C ATOM 1648 C ALA A 232 34.750 -21.001 -25.716 1.00130.68 C ANISOU 1648 C ALA A 232 15071 16225 18357 -1746 -925 -1709 C ATOM 1649 O ALA A 232 33.553 -21.228 -25.539 1.00127.52 O ANISOU 1649 O ALA A 232 14829 15783 17840 -1658 -905 -1713 O ATOM 1650 CB ALA A 232 36.200 -21.137 -23.682 1.00130.84 C ANISOU 1650 CB ALA A 232 14931 16474 18307 -1847 -1191 -2047 C ATOM 1651 N LYS A 233 35.195 -20.053 -26.535 1.00130.99 N ANISOU 1651 N LYS A 233 15020 16112 18637 -1849 -829 -1630 N ATOM 1652 CA LYS A 233 34.283 -19.238 -27.328 1.00128.05 C ANISOU 1652 CA LYS A 233 14752 15512 18389 -1846 -696 -1541 C ATOM 1653 C LYS A 233 33.645 -20.077 -28.429 1.00121.92 C ANISOU 1653 C LYS A 233 14079 14764 17483 -1680 -609 -1323 C ATOM 1654 O LYS A 233 32.436 -20.013 -28.650 1.00120.99 O ANISOU 1654 O LYS A 233 14107 14547 17318 -1599 -566 -1295 O ATOM 1655 CB LYS A 233 35.017 -18.039 -27.932 1.00132.81 C ANISOU 1655 CB LYS A 233 15236 15941 19283 -1997 -607 -1501 C ATOM 1656 CG LYS A 233 34.119 -17.101 -28.724 1.00142.80 C ANISOU 1656 CG LYS A 233 16623 16956 20679 -1989 -467 -1415 C ATOM 1657 CD LYS A 233 34.885 -15.882 -29.215 1.00154.59 C ANISOU 1657 CD LYS A 233 18007 18262 22467 -2152 -375 -1382 C ATOM 1658 CE LYS A 233 33.969 -14.916 -29.950 1.00162.76 C ANISOU 1658 CE LYS A 233 19185 19037 23618 -2129 -237 -1305 C ATOM 1659 NZ LYS A 233 34.693 -13.699 -30.411 1.00167.58 N ANISOU 1659 NZ LYS A 233 19708 19442 24524 -2293 -134 -1266 N ATOM 1660 N SER A 234 34.467 -20.863 -29.115 1.00120.23 N ANISOU 1660 N SER A 234 13786 14684 17210 -1621 -592 -1174 N ATOM 1661 CA SER A 234 33.979 -21.757 -30.158 1.00121.16 C ANISOU 1661 CA SER A 234 14011 14839 17187 -1449 -534 -974 C ATOM 1662 C SER A 234 32.949 -22.728 -29.593 1.00108.52 C ANISOU 1662 C SER A 234 12553 13324 15356 -1337 -619 -1025 C ATOM 1663 O SER A 234 31.977 -23.077 -30.262 1.00 98.77 O ANISOU 1663 O SER A 234 11448 12029 14051 -1223 -580 -919 O ATOM 1664 CB SER A 234 35.137 -22.535 -30.786 1.00134.90 C ANISOU 1664 CB SER A 234 15646 16740 18870 -1390 -521 -831 C ATOM 1665 OG SER A 234 36.072 -21.662 -31.396 1.00142.10 O ANISOU 1665 OG SER A 234 16413 17571 20008 -1490 -417 -755 O ATOM 1666 N ALA A 235 33.172 -23.159 -28.355 1.00110.62 N ANISOU 1666 N ALA A 235 12793 13728 15510 -1367 -736 -1186 N ATOM 1667 CA ALA A 235 32.258 -24.071 -27.682 1.00113.36 C ANISOU 1667 CA ALA A 235 13268 14158 15646 -1273 -804 -1237 C ATOM 1668 C ALA A 235 30.961 -23.361 -27.318 1.00112.43 C ANISOU 1668 C ALA A 235 13251 13885 15583 -1290 -770 -1319 C ATOM 1669 O ALA A 235 29.885 -23.958 -27.344 1.00110.93 O ANISOU 1669 O ALA A 235 13175 13693 15278 -1197 -767 -1278 O ATOM 1670 CB ALA A 235 32.910 -24.654 -26.441 1.00118.62 C ANISOU 1670 CB ALA A 235 13888 15008 16173 -1288 -927 -1384 C ATOM 1671 N ALA A 236 31.072 -22.082 -26.977 1.00112.10 N ANISOU 1671 N ALA A 236 13162 13708 15724 -1410 -745 -1435 N ATOM 1672 CA ALA A 236 29.908 -21.277 -26.635 1.00108.80 C ANISOU 1672 CA ALA A 236 12838 13135 15368 -1418 -706 -1518 C ATOM 1673 C ALA A 236 28.990 -21.121 -27.841 1.00108.63 C ANISOU 1673 C ALA A 236 12896 12977 15402 -1338 -604 -1354 C ATOM 1674 O ALA A 236 27.770 -21.054 -27.700 1.00102.57 O ANISOU 1674 O ALA A 236 12223 12146 14603 -1277 -582 -1371 O ATOM 1675 CB ALA A 236 30.341 -19.915 -26.117 1.00102.83 C ANISOU 1675 CB ALA A 236 12024 12245 14801 -1560 -707 -1671 C ATOM 1676 N ILE A 237 29.588 -21.065 -29.027 1.00112.06 N ANISOU 1676 N ILE A 237 13289 13373 15917 -1326 -542 -1195 N ATOM 1677 CA ILE A 237 28.830 -20.904 -30.261 1.00111.55 C ANISOU 1677 CA ILE A 237 13309 13179 15897 -1230 -453 -1036 C ATOM 1678 C ILE A 237 28.099 -22.189 -30.634 1.00107.43 C ANISOU 1678 C ILE A 237 12875 12757 15187 -1083 -498 -934 C ATOM 1679 O ILE A 237 27.006 -22.150 -31.197 1.00103.70 O ANISOU 1679 O ILE A 237 12493 12190 14717 -996 -470 -872 O ATOM 1680 CB ILE A 237 29.741 -20.482 -31.430 1.00115.39 C ANISOU 1680 CB ILE A 237 13738 13595 16510 -1241 -362 -884 C ATOM 1681 CG1 ILE A 237 30.582 -19.267 -31.038 1.00116.70 C ANISOU 1681 CG1 ILE A 237 13796 13660 16884 -1413 -324 -980 C ATOM 1682 CG2 ILE A 237 28.913 -20.183 -32.669 1.00117.32 C ANISOU 1682 CG2 ILE A 237 14093 13686 16795 -1125 -271 -733 C ATOM 1683 CD1 ILE A 237 31.501 -18.780 -32.136 1.00118.01 C ANISOU 1683 CD1 ILE A 237 13891 13748 17200 -1440 -209 -822 C ATOM 1684 N ILE A 238 28.706 -23.328 -30.317 1.00115.54 N ANISOU 1684 N ILE A 238 13875 13969 16055 -1055 -575 -922 N ATOM 1685 CA ILE A 238 28.095 -24.621 -30.599 1.00128.08 C ANISOU 1685 CA ILE A 238 15554 15648 17464 -929 -630 -834 C ATOM 1686 C ILE A 238 26.854 -24.824 -29.739 1.00139.89 C ANISOU 1686 C ILE A 238 17114 17140 18900 -920 -663 -931 C ATOM 1687 O ILE A 238 25.832 -25.324 -30.210 1.00143.95 O ANISOU 1687 O ILE A 238 17707 17619 19369 -833 -672 -856 O ATOM 1688 CB ILE A 238 29.076 -25.779 -30.347 1.00132.13 C ANISOU 1688 CB ILE A 238 16035 16358 17812 -898 -705 -809 C ATOM 1689 CG1 ILE A 238 30.362 -25.573 -31.150 1.00144.57 C ANISOU 1689 CG1 ILE A 238 17522 17955 19452 -902 -660 -708 C ATOM 1690 CG2 ILE A 238 28.429 -27.112 -30.699 1.00123.28 C ANISOU 1690 CG2 ILE A 238 15028 15302 16513 -770 -765 -713 C ATOM 1691 CD1 ILE A 238 31.430 -26.611 -30.875 1.00149.32 C ANISOU 1691 CD1 ILE A 238 18074 18759 19900 -866 -730 -691 C ATOM 1692 N ALA A 239 26.952 -24.431 -28.474 1.00143.84 N ANISOU 1692 N ALA A 239 17576 17676 19401 -1006 -683 -1099 N ATOM 1693 CA ALA A 239 25.835 -24.555 -27.545 1.00145.53 C ANISOU 1693 CA ALA A 239 17844 17894 19555 -993 -692 -1192 C ATOM 1694 C ALA A 239 24.712 -23.587 -27.900 1.00148.77 C ANISOU 1694 C ALA A 239 18290 18132 20106 -981 -619 -1194 C ATOM 1695 O ALA A 239 23.537 -23.947 -27.871 1.00151.48 O ANISOU 1695 O ALA A 239 18682 18460 20414 -917 -612 -1168 O ATOM 1696 CB ALA A 239 26.305 -24.322 -26.120 1.00144.54 C ANISOU 1696 CB ALA A 239 17688 17849 19382 -1064 -731 -1374 C ATOM 1697 N GLY A 240 25.085 -22.356 -28.235 1.00146.10 N ANISOU 1697 N GLY A 240 17920 17659 19933 -1041 -563 -1222 N ATOM 1698 CA GLY A 240 24.117 -21.331 -28.580 1.00136.52 C ANISOU 1698 CA GLY A 240 16748 16271 18853 -1021 -490 -1229 C ATOM 1699 C GLY A 240 23.223 -21.737 -29.734 1.00126.37 C ANISOU 1699 C GLY A 240 15518 14932 17565 -904 -474 -1075 C ATOM 1700 O GLY A 240 22.022 -21.473 -29.721 1.00124.61 O ANISOU 1700 O GLY A 240 15331 14639 17374 -849 -450 -1087 O ATOM 1701 N LEU A 241 23.812 -22.381 -30.736 1.00125.18 N ANISOU 1701 N LEU A 241 15372 14817 17374 -855 -494 -934 N ATOM 1702 CA LEU A 241 23.063 -22.823 -31.906 1.00129.34 C ANISOU 1702 CA LEU A 241 15965 15291 17885 -729 -503 -791 C ATOM 1703 C LEU A 241 22.112 -23.964 -31.562 1.00125.53 C ANISOU 1703 C LEU A 241 15510 14903 17283 -673 -579 -785 C ATOM 1704 O LEU A 241 21.124 -24.187 -32.259 1.00123.35 O ANISOU 1704 O LEU A 241 15278 14567 17020 -581 -601 -713 O ATOM 1705 CB LEU A 241 24.016 -23.247 -33.026 1.00140.88 C ANISOU 1705 CB LEU A 241 17441 16772 19314 -673 -505 -644 C ATOM 1706 CG LEU A 241 24.900 -22.139 -33.603 1.00152.61 C ANISOU 1706 CG LEU A 241 18897 18146 20940 -717 -406 -606 C ATOM 1707 CD1 LEU A 241 25.860 -22.697 -34.644 1.00156.51 C ANISOU 1707 CD1 LEU A 241 19401 18688 21379 -645 -396 -448 C ATOM 1708 CD2 LEU A 241 24.046 -21.027 -34.194 1.00153.96 C ANISOU 1708 CD2 LEU A 241 19128 18122 21248 -672 -331 -589 C ATOM 1709 N PHE A 242 22.413 -24.684 -30.487 1.00124.15 N ANISOU 1709 N PHE A 242 15309 14870 16994 -727 -622 -859 N ATOM 1710 CA PHE A 242 21.542 -25.758 -30.026 1.00122.01 C ANISOU 1710 CA PHE A 242 15062 14680 16617 -692 -677 -853 C ATOM 1711 C PHE A 242 20.234 -25.178 -29.500 1.00116.45 C ANISOU 1711 C PHE A 242 14344 13908 15992 -691 -629 -923 C ATOM 1712 O PHE A 242 19.153 -25.537 -29.962 1.00112.10 O ANISOU 1712 O PHE A 242 13807 13321 15467 -627 -650 -860 O ATOM 1713 CB PHE A 242 22.231 -26.586 -28.939 1.00124.47 C ANISOU 1713 CB PHE A 242 15362 15152 16779 -741 -717 -917 C ATOM 1714 CG PHE A 242 21.440 -27.787 -28.495 1.00123.93 C ANISOU 1714 CG PHE A 242 15330 15162 16596 -708 -762 -889 C ATOM 1715 CD1 PHE A 242 21.686 -29.036 -29.042 1.00123.54 C ANISOU 1715 CD1 PHE A 242 15334 15176 16431 -655 -841 -782 C ATOM 1716 CD2 PHE A 242 20.453 -27.667 -27.529 1.00122.87 C ANISOU 1716 CD2 PHE A 242 15182 15033 16472 -727 -718 -965 C ATOM 1717 CE1 PHE A 242 20.960 -30.141 -28.637 1.00120.81 C ANISOU 1717 CE1 PHE A 242 15025 14881 15995 -639 -880 -753 C ATOM 1718 CE2 PHE A 242 19.726 -28.769 -27.119 1.00125.28 C ANISOU 1718 CE2 PHE A 242 15511 15401 16689 -708 -742 -925 C ATOM 1719 CZ PHE A 242 19.981 -30.007 -27.673 1.00122.63 C ANISOU 1719 CZ PHE A 242 15227 15114 16252 -673 -825 -820 C ATOM 1720 N ALA A 243 20.345 -24.273 -28.533 1.00114.93 N ANISOU 1720 N ALA A 243 14124 13700 15844 -755 -571 -1056 N ATOM 1721 CA ALA A 243 19.177 -23.615 -27.963 1.00112.17 C ANISOU 1721 CA ALA A 243 13766 13290 15563 -739 -510 -1130 C ATOM 1722 C ALA A 243 18.428 -22.823 -29.029 1.00108.92 C ANISOU 1722 C ALA A 243 13367 12727 15293 -672 -478 -1068 C ATOM 1723 O ALA A 243 17.203 -22.719 -28.995 1.00110.27 O ANISOU 1723 O ALA A 243 13524 12863 15511 -616 -455 -1066 O ATOM 1724 CB ALA A 243 19.591 -22.705 -26.817 1.00111.15 C ANISOU 1724 CB ALA A 243 13631 13155 15446 -805 -465 -1291 C ATOM 1725 N LEU A 244 19.173 -22.270 -29.979 1.00104.56 N ANISOU 1725 N LEU A 244 12836 12085 14807 -670 -469 -1014 N ATOM 1726 CA LEU A 244 18.586 -21.466 -31.043 1.00101.82 C ANISOU 1726 CA LEU A 244 12522 11583 14580 -591 -434 -951 C ATOM 1727 C LEU A 244 17.797 -22.332 -32.022 1.00 99.89 C ANISOU 1727 C LEU A 244 12299 11347 14309 -482 -504 -826 C ATOM 1728 O LEU A 244 16.918 -21.840 -32.729 1.00 92.49 O ANISOU 1728 O LEU A 244 11382 10305 13455 -391 -495 -789 O ATOM 1729 CB LEU A 244 19.678 -20.694 -31.786 1.00102.56 C ANISOU 1729 CB LEU A 244 12641 11579 14746 -617 -390 -910 C ATOM 1730 CG LEU A 244 19.225 -19.614 -32.769 1.00 99.45 C ANISOU 1730 CG LEU A 244 12303 11002 14480 -539 -326 -858 C ATOM 1731 CD1 LEU A 244 18.561 -18.465 -32.029 1.00 97.81 C ANISOU 1731 CD1 LEU A 244 12099 10697 14365 -559 -260 -983 C ATOM 1732 CD2 LEU A 244 20.402 -19.111 -33.587 1.00 98.68 C ANISOU 1732 CD2 LEU A 244 12230 10824 14438 -562 -275 -779 C ATOM 1733 N CYS A 245 18.113 -23.623 -32.055 1.00110.20 N ANISOU 1733 N CYS A 245 13605 12770 15495 -485 -585 -769 N ATOM 1734 CA CYS A 245 17.476 -24.544 -32.993 1.00122.25 C ANISOU 1734 CA CYS A 245 15163 14297 16988 -389 -678 -658 C ATOM 1735 C CYS A 245 16.468 -25.474 -32.320 1.00126.58 C ANISOU 1735 C CYS A 245 15667 14928 17500 -402 -728 -676 C ATOM 1736 O CYS A 245 15.812 -26.271 -32.991 1.00124.33 O ANISOU 1736 O CYS A 245 15396 14637 17206 -338 -821 -599 O ATOM 1737 CB CYS A 245 18.530 -25.374 -33.732 1.00127.44 C ANISOU 1737 CB CYS A 245 15878 15003 17539 -360 -741 -559 C ATOM 1738 SG CYS A 245 19.625 -24.427 -34.819 1.00156.35 S ANISOU 1738 SG CYS A 245 19591 18562 21254 -316 -672 -485 S ATOM 1739 N TRP A 246 16.349 -25.376 -31.000 1.00132.00 N ANISOU 1739 N TRP A 246 16302 15685 18167 -483 -668 -776 N ATOM 1740 CA TRP A 246 15.422 -26.229 -30.261 1.00133.52 C ANISOU 1740 CA TRP A 246 16446 15956 18327 -501 -684 -783 C ATOM 1741 C TRP A 246 14.368 -25.433 -29.497 1.00129.03 C ANISOU 1741 C TRP A 246 15812 15363 17851 -498 -591 -862 C ATOM 1742 O TRP A 246 13.248 -25.905 -29.308 1.00127.50 O ANISOU 1742 O TRP A 246 15557 15192 17697 -480 -595 -837 O ATOM 1743 CB TRP A 246 16.177 -27.163 -29.313 1.00139.28 C ANISOU 1743 CB TRP A 246 17192 16820 18907 -571 -694 -806 C ATOM 1744 CG TRP A 246 16.884 -28.279 -30.016 1.00147.21 C ANISOU 1744 CG TRP A 246 18259 17867 19808 -553 -798 -711 C ATOM 1745 CD1 TRP A 246 18.139 -28.247 -30.552 1.00152.70 C ANISOU 1745 CD1 TRP A 246 19004 18573 20443 -543 -824 -683 C ATOM 1746 CD2 TRP A 246 16.378 -29.597 -30.260 1.00148.97 C ANISOU 1746 CD2 TRP A 246 18504 18123 19975 -535 -889 -629 C ATOM 1747 NE1 TRP A 246 18.446 -29.463 -31.115 1.00153.31 N ANISOU 1747 NE1 TRP A 246 19143 18694 20414 -503 -923 -590 N ATOM 1748 CE2 TRP A 246 17.381 -30.309 -30.949 1.00151.26 C ANISOU 1748 CE2 TRP A 246 18876 18440 20154 -502 -972 -560 C ATOM 1749 CE3 TRP A 246 15.174 -30.244 -29.963 1.00147.32 C ANISOU 1749 CE3 TRP A 246 18250 17918 19807 -547 -905 -605 C ATOM 1750 CZ2 TRP A 246 17.217 -31.635 -31.346 1.00150.71 C ANISOU 1750 CZ2 TRP A 246 18868 18391 20004 -473 -1081 -477 C ATOM 1751 CZ3 TRP A 246 15.012 -31.560 -30.360 1.00148.70 C ANISOU 1751 CZ3 TRP A 246 18471 18107 19921 -539 -1015 -520 C ATOM 1752 CH2 TRP A 246 16.028 -32.241 -31.043 1.00151.41 C ANISOU 1752 CH2 TRP A 246 18919 18467 20143 -500 -1107 -462 C ATOM 1753 N LEU A 247 14.727 -24.230 -29.061 1.00128.12 N ANISOU 1753 N LEU A 247 15707 15198 17776 -514 -506 -956 N ATOM 1754 CA LEU A 247 13.778 -23.370 -28.361 1.00127.81 C ANISOU 1754 CA LEU A 247 15624 15125 17811 -488 -413 -1037 C ATOM 1755 C LEU A 247 12.486 -23.168 -29.150 1.00130.11 C ANISOU 1755 C LEU A 247 15867 15345 18225 -396 -426 -977 C ATOM 1756 O LEU A 247 11.400 -23.327 -28.600 1.00133.35 O ANISOU 1756 O LEU A 247 16199 15796 18671 -373 -386 -986 O ATOM 1757 CB LEU A 247 14.406 -22.020 -28.004 1.00128.24 C ANISOU 1757 CB LEU A 247 15724 15100 17903 -509 -341 -1145 C ATOM 1758 CG LEU A 247 15.278 -21.976 -26.749 1.00130.44 C ANISOU 1758 CG LEU A 247 16025 15457 18080 -589 -313 -1259 C ATOM 1759 CD1 LEU A 247 15.776 -20.561 -26.503 1.00132.80 C ANISOU 1759 CD1 LEU A 247 16367 15644 18447 -611 -260 -1372 C ATOM 1760 CD2 LEU A 247 14.510 -22.492 -25.541 1.00130.10 C ANISOU 1760 CD2 LEU A 247 15949 15521 17961 -577 -263 -1303 C ATOM 1761 N PRO A 248 12.595 -22.816 -30.442 1.00127.16 N ANISOU 1761 N PRO A 248 15534 14867 17914 -332 -480 -913 N ATOM 1762 CA PRO A 248 11.383 -22.622 -31.247 1.00124.54 C ANISOU 1762 CA PRO A 248 15160 14468 17691 -226 -514 -863 C ATOM 1763 C PRO A 248 10.426 -23.810 -31.170 1.00125.33 C ANISOU 1763 C PRO A 248 15168 14652 17800 -228 -586 -807 C ATOM 1764 O PRO A 248 9.216 -23.620 -31.045 1.00126.75 O ANISOU 1764 O PRO A 248 15254 14830 18076 -178 -565 -813 O ATOM 1765 CB PRO A 248 11.931 -22.475 -32.668 1.00120.06 C ANISOU 1765 CB PRO A 248 14680 13802 17133 -158 -587 -783 C ATOM 1766 CG PRO A 248 13.297 -21.922 -32.481 1.00123.09 C ANISOU 1766 CG PRO A 248 15138 14160 17469 -225 -527 -817 C ATOM 1767 CD PRO A 248 13.819 -22.533 -31.213 1.00124.69 C ANISOU 1767 CD PRO A 248 15307 14494 17576 -342 -504 -881 C ATOM 1768 N LEU A 249 10.971 -25.020 -31.241 1.00121.73 N ANISOU 1768 N LEU A 249 14737 14266 17249 -286 -668 -751 N ATOM 1769 CA LEU A 249 10.163 -26.234 -31.223 1.00112.66 C ANISOU 1769 CA LEU A 249 13515 13177 16114 -306 -747 -691 C ATOM 1770 C LEU A 249 9.515 -26.455 -29.859 1.00114.96 C ANISOU 1770 C LEU A 249 13709 13561 16409 -369 -640 -732 C ATOM 1771 O LEU A 249 8.389 -26.942 -29.767 1.00112.47 O ANISOU 1771 O LEU A 249 13283 13268 16182 -367 -654 -695 O ATOM 1772 CB LEU A 249 11.013 -27.446 -31.605 1.00103.68 C ANISOU 1772 CB LEU A 249 12459 12078 14857 -346 -856 -624 C ATOM 1773 CG LEU A 249 10.288 -28.791 -31.658 1.00 97.77 C ANISOU 1773 CG LEU A 249 11661 11368 14120 -378 -957 -557 C ATOM 1774 CD1 LEU A 249 9.040 -28.680 -32.504 1.00104.03 C ANISOU 1774 CD1 LEU A 249 12372 12087 15066 -303 -1044 -526 C ATOM 1775 CD2 LEU A 249 11.203 -29.866 -32.206 1.00 95.04 C ANISOU 1775 CD2 LEU A 249 11429 11035 13645 -387 -1075 -494 C ATOM 1776 N HIS A 250 10.232 -26.089 -28.802 1.00126.23 N ANISOU 1776 N HIS A 250 15177 15041 17743 -419 -534 -808 N ATOM 1777 CA HIS A 250 9.712 -26.214 -27.447 1.00133.77 C ANISOU 1777 CA HIS A 250 16069 16085 18674 -453 -414 -851 C ATOM 1778 C HIS A 250 8.728 -25.091 -27.144 1.00131.63 C ANISOU 1778 C HIS A 250 15723 15776 18514 -380 -309 -906 C ATOM 1779 O HIS A 250 7.713 -25.306 -26.484 1.00132.35 O ANISOU 1779 O HIS A 250 15710 15923 18653 -370 -231 -892 O ATOM 1780 CB HIS A 250 10.852 -26.210 -26.428 1.00144.35 C ANISOU 1780 CB HIS A 250 17496 17493 19857 -510 -357 -926 C ATOM 1781 CG HIS A 250 11.800 -27.359 -26.575 1.00148.57 C ANISOU 1781 CG HIS A 250 18100 18085 20267 -568 -448 -874 C ATOM 1782 ND1 HIS A 250 13.137 -27.190 -26.865 1.00150.02 N ANISOU 1782 ND1 HIS A 250 18374 18263 20366 -588 -497 -902 N ATOM 1783 CD2 HIS A 250 11.603 -28.695 -26.470 1.00148.28 C ANISOU 1783 CD2 HIS A 250 18055 18109 20176 -607 -497 -794 C ATOM 1784 CE1 HIS A 250 13.724 -28.371 -26.930 1.00150.93 C ANISOU 1784 CE1 HIS A 250 18535 18443 20368 -622 -572 -843 C ATOM 1785 NE2 HIS A 250 12.816 -29.302 -26.698 1.00150.58 N ANISOU 1785 NE2 HIS A 250 18445 18433 20337 -634 -576 -778 N ATOM 1786 N ILE A 251 9.037 -23.892 -27.629 1.00131.17 N ANISOU 1786 N ILE A 251 15721 15619 18497 -324 -299 -961 N ATOM 1787 CA ILE A 251 8.165 -22.739 -27.435 1.00134.48 C ANISOU 1787 CA ILE A 251 16095 15986 19013 -236 -206 -1017 C ATOM 1788 C ILE A 251 6.777 -23.011 -28.003 1.00127.98 C ANISOU 1788 C ILE A 251 15136 15162 18328 -169 -240 -944 C ATOM 1789 O ILE A 251 5.769 -22.615 -27.420 1.00116.22 O ANISOU 1789 O ILE A 251 13550 13703 16904 -112 -142 -965 O ATOM 1790 CB ILE A 251 8.752 -21.465 -28.076 1.00136.66 C ANISOU 1790 CB ILE A 251 16473 16130 19322 -186 -206 -1070 C ATOM 1791 CG1 ILE A 251 10.011 -21.025 -27.327 1.00134.83 C ANISOU 1791 CG1 ILE A 251 16347 15897 18986 -259 -160 -1164 C ATOM 1792 CG2 ILE A 251 7.724 -20.346 -28.073 1.00141.18 C ANISOU 1792 CG2 ILE A 251 17007 16635 20000 -71 -128 -1112 C ATOM 1793 CD1 ILE A 251 10.677 -19.797 -27.915 1.00136.79 C ANISOU 1793 CD1 ILE A 251 16692 16001 19281 -238 -152 -1210 C ATOM 1794 N ILE A 252 6.734 -23.697 -29.140 1.00130.31 N ANISOU 1794 N ILE A 252 15422 15425 18664 -168 -386 -860 N ATOM 1795 CA ILE A 252 5.470 -24.099 -29.745 1.00131.09 C ANISOU 1795 CA ILE A 252 15384 15523 18900 -116 -459 -795 C ATOM 1796 C ILE A 252 4.686 -25.009 -28.807 1.00133.94 C ANISOU 1796 C ILE A 252 15605 15997 19289 -185 -399 -759 C ATOM 1797 O ILE A 252 3.481 -24.838 -28.622 1.00138.33 O ANISOU 1797 O ILE A 252 16008 16579 19971 -136 -350 -746 O ATOM 1798 CB ILE A 252 5.692 -24.824 -31.086 1.00130.12 C ANISOU 1798 CB ILE A 252 15306 15345 18790 -105 -649 -719 C ATOM 1799 CG1 ILE A 252 6.024 -23.814 -32.187 1.00128.66 C ANISOU 1799 CG1 ILE A 252 15226 15037 18622 10 -695 -732 C ATOM 1800 CG2 ILE A 252 4.464 -25.635 -31.466 1.00129.50 C ANISOU 1800 CG2 ILE A 252 15072 15290 18843 -98 -751 -657 C ATOM 1801 CD1 ILE A 252 6.127 -24.430 -33.567 1.00124.90 C ANISOU 1801 CD1 ILE A 252 14805 14500 18150 64 -881 -659 C ATOM 1802 N ASN A 253 5.378 -25.976 -28.213 1.00134.99 N ANISOU 1802 N ASN A 253 15788 16196 19305 -293 -396 -737 N ATOM 1803 CA ASN A 253 4.743 -26.915 -27.295 1.00139.70 C ANISOU 1803 CA ASN A 253 16276 16891 19914 -365 -324 -687 C ATOM 1804 C ASN A 253 4.326 -26.262 -25.981 1.00142.41 C ANISOU 1804 C ASN A 253 16572 17302 20235 -332 -119 -743 C ATOM 1805 O ASN A 253 3.450 -26.767 -25.279 1.00144.52 O ANISOU 1805 O ASN A 253 16710 17644 20558 -353 -24 -692 O ATOM 1806 CB ASN A 253 5.655 -28.113 -27.029 1.00141.00 C ANISOU 1806 CB ASN A 253 16536 17099 19939 -471 -375 -648 C ATOM 1807 CG ASN A 253 5.825 -28.997 -28.251 1.00139.19 C ANISOU 1807 CG ASN A 253 16338 16811 19738 -496 -577 -576 C ATOM 1808 OD1 ASN A 253 5.304 -28.698 -29.326 1.00139.87 O ANISOU 1808 OD1 ASN A 253 16381 16822 19941 -430 -688 -561 O ATOM 1809 ND2 ASN A 253 6.558 -30.093 -28.090 1.00135.58 N ANISOU 1809 ND2 ASN A 253 15969 16386 19161 -575 -630 -535 N ATOM 1810 N CYS A 254 4.956 -25.140 -25.650 1.00144.30 N ANISOU 1810 N CYS A 254 16921 17512 20396 -276 -49 -844 N ATOM 1811 CA CYS A 254 4.592 -24.390 -24.453 1.00146.52 C ANISOU 1811 CA CYS A 254 17189 17842 20641 -217 133 -913 C ATOM 1812 C CYS A 254 3.270 -23.659 -24.662 1.00149.97 C ANISOU 1812 C CYS A 254 17483 18261 21237 -106 193 -905 C ATOM 1813 O CYS A 254 2.450 -23.562 -23.749 1.00149.99 O ANISOU 1813 O CYS A 254 17390 18339 21260 -59 344 -900 O ATOM 1814 CB CYS A 254 5.697 -23.401 -24.075 1.00142.33 C ANISOU 1814 CB CYS A 254 16829 17264 19986 -196 164 -1036 C ATOM 1815 SG CYS A 254 7.253 -24.178 -23.583 1.00231.87 S ANISOU 1815 SG CYS A 254 28316 28653 31129 -310 113 -1062 S ATOM 1816 N PHE A 255 3.069 -23.150 -25.873 1.00148.01 N ANISOU 1816 N PHE A 255 17224 17917 21095 -49 78 -901 N ATOM 1817 CA PHE A 255 1.823 -22.484 -26.229 1.00143.31 C ANISOU 1817 CA PHE A 255 16491 17306 20656 71 105 -892 C ATOM 1818 C PHE A 255 0.666 -23.473 -26.263 1.00141.88 C ANISOU 1818 C PHE A 255 16091 17204 20614 37 90 -789 C ATOM 1819 O PHE A 255 -0.406 -23.207 -25.721 1.00146.61 O ANISOU 1819 O PHE A 255 16535 17866 21304 106 212 -775 O ATOM 1820 CB PHE A 255 1.955 -21.788 -27.585 1.00142.89 C ANISOU 1820 CB PHE A 255 16500 17126 20666 149 -30 -907 C ATOM 1821 CG PHE A 255 2.614 -20.440 -27.515 1.00146.58 C ANISOU 1821 CG PHE A 255 17132 17497 21065 222 32 -1007 C ATOM 1822 CD1 PHE A 255 3.855 -20.291 -26.920 1.00150.62 C ANISOU 1822 CD1 PHE A 255 17802 17996 21432 145 71 -1071 C ATOM 1823 CD2 PHE A 255 1.998 -19.324 -28.052 1.00146.84 C ANISOU 1823 CD2 PHE A 255 17161 17447 21183 369 44 -1039 C ATOM 1824 CE1 PHE A 255 4.463 -19.052 -26.854 1.00152.46 C ANISOU 1824 CE1 PHE A 255 18179 18124 21623 194 118 -1167 C ATOM 1825 CE2 PHE A 255 2.604 -18.083 -27.990 1.00147.65 C ANISOU 1825 CE2 PHE A 255 17428 17441 21231 428 102 -1128 C ATOM 1826 CZ PHE A 255 3.837 -17.948 -27.390 1.00150.14 C ANISOU 1826 CZ PHE A 255 17893 17734 21419 331 138 -1192 C ATOM 1827 N THR A 256 0.890 -24.616 -26.903 1.00136.79 N ANISOU 1827 N THR A 256 15430 16552 19991 -67 -61 -717 N ATOM 1828 CA THR A 256 -0.137 -25.643 -27.021 1.00133.32 C ANISOU 1828 CA THR A 256 14787 16167 19703 -127 -105 -619 C ATOM 1829 C THR A 256 -0.568 -26.170 -25.655 1.00131.16 C ANISOU 1829 C THR A 256 14416 16008 19412 -185 89 -574 C ATOM 1830 O THR A 256 -1.761 -26.275 -25.371 1.00141.66 O ANISOU 1830 O THR A 256 15532 17397 20894 -163 170 -519 O ATOM 1831 CB THR A 256 0.341 -26.819 -27.897 1.00128.70 C ANISOU 1831 CB THR A 256 14248 15536 19116 -233 -311 -559 C ATOM 1832 OG1 THR A 256 0.516 -26.369 -29.246 1.00128.05 O ANISOU 1832 OG1 THR A 256 14234 15351 19069 -151 -489 -583 O ATOM 1833 CG2 THR A 256 -0.677 -27.946 -27.877 1.00128.49 C ANISOU 1833 CG2 THR A 256 14017 15553 19252 -321 -353 -462 C ATOM 1834 N PHE A 257 0.406 -26.494 -24.811 1.00119.64 N ANISOU 1834 N PHE A 257 13109 14582 17766 -249 167 -595 N ATOM 1835 CA PHE A 257 0.123 -27.054 -23.494 1.00121.85 C ANISOU 1835 CA PHE A 257 13338 14966 17993 -291 355 -548 C ATOM 1836 C PHE A 257 -0.454 -26.014 -22.538 1.00131.03 C ANISOU 1836 C PHE A 257 14459 16186 19140 -160 569 -598 C ATOM 1837 O PHE A 257 -1.631 -26.072 -22.183 1.00138.79 O ANISOU 1837 O PHE A 257 15242 17233 20258 -122 688 -532 O ATOM 1838 CB PHE A 257 1.388 -27.670 -22.893 1.00126.26 C ANISOU 1838 CB PHE A 257 14094 15544 18334 -372 361 -566 C ATOM 1839 CG PHE A 257 1.175 -28.304 -21.547 1.00127.55 C ANISOU 1839 CG PHE A 257 14239 15809 18416 -401 553 -512 C ATOM 1840 CD1 PHE A 257 0.917 -29.660 -21.438 1.00125.66 C ANISOU 1840 CD1 PHE A 257 13932 15595 18218 -520 542 -392 C ATOM 1841 CD2 PHE A 257 1.237 -27.544 -20.389 1.00129.95 C ANISOU 1841 CD2 PHE A 257 14609 16173 18595 -301 744 -580 C ATOM 1842 CE1 PHE A 257 0.725 -30.246 -20.200 1.00129.62 C ANISOU 1842 CE1 PHE A 257 14430 16182 18637 -537 736 -329 C ATOM 1843 CE2 PHE A 257 1.044 -28.124 -19.151 1.00132.85 C ANISOU 1843 CE2 PHE A 257 14978 16633 18868 -303 930 -525 C ATOM 1844 CZ PHE A 257 0.787 -29.476 -19.057 1.00133.76 C ANISOU 1844 CZ PHE A 257 15023 16775 19025 -421 934 -393 C ATOM 1845 N PHE A 258 0.383 -25.069 -22.120 1.00136.17 N ANISOU 1845 N PHE A 258 15297 16812 19630 -88 617 -715 N ATOM 1846 CA PHE A 258 -0.023 -24.061 -21.143 1.00146.08 C ANISOU 1846 CA PHE A 258 16563 18109 20833 50 811 -781 C ATOM 1847 C PHE A 258 -1.234 -23.248 -21.593 1.00146.54 C ANISOU 1847 C PHE A 258 16452 18157 21069 176 845 -773 C ATOM 1848 O PHE A 258 -2.026 -22.791 -20.769 1.00142.42 O ANISOU 1848 O PHE A 258 15850 17706 20558 288 1031 -770 O ATOM 1849 CB PHE A 258 1.142 -23.124 -20.815 1.00147.53 C ANISOU 1849 CB PHE A 258 16986 18234 20835 95 806 -926 C ATOM 1850 CG PHE A 258 2.237 -23.775 -20.021 1.00151.38 C ANISOU 1850 CG PHE A 258 17630 18764 21124 12 818 -951 C ATOM 1851 CD1 PHE A 258 3.408 -24.183 -20.635 1.00158.92 C ANISOU 1851 CD1 PHE A 258 18704 19666 22012 -94 651 -971 C ATOM 1852 CD2 PHE A 258 2.091 -23.983 -18.660 1.00153.05 C ANISOU 1852 CD2 PHE A 258 17871 19073 21208 58 998 -951 C ATOM 1853 CE1 PHE A 258 4.417 -24.782 -19.906 1.00163.12 C ANISOU 1853 CE1 PHE A 258 19372 20247 22360 -157 655 -998 C ATOM 1854 CE2 PHE A 258 3.094 -24.583 -17.924 1.00160.04 C ANISOU 1854 CE2 PHE A 258 18909 20001 21900 0 999 -980 C ATOM 1855 CZ PHE A 258 4.260 -24.982 -18.547 1.00164.73 C ANISOU 1855 CZ PHE A 258 19609 20545 22434 -109 822 -1007 C ATOM 1856 N CYS A 259 -1.375 -23.070 -22.902 1.00147.99 N ANISOU 1856 N CYS A 259 16591 18257 21383 175 667 -769 N ATOM 1857 CA CYS A 259 -2.485 -22.295 -23.439 1.00152.61 C ANISOU 1857 CA CYS A 259 17022 18828 22133 308 671 -768 C ATOM 1858 C CYS A 259 -3.284 -23.097 -24.463 1.00158.35 C ANISOU 1858 C CYS A 259 17540 19556 23069 250 517 -670 C ATOM 1859 O CYS A 259 -3.023 -23.014 -25.665 1.00156.53 O ANISOU 1859 O CYS A 259 17356 19232 22887 249 320 -686 O ATOM 1860 CB CYS A 259 -1.978 -20.992 -24.061 1.00147.83 C ANISOU 1860 CB CYS A 259 16584 18102 21483 418 605 -880 C ATOM 1861 SG CYS A 259 -3.282 -19.812 -24.489 1.00250.51 S ANISOU 1861 SG CYS A 259 29451 31091 34641 631 649 -900 S ATOM 1862 N PRO A 260 -4.261 -23.883 -23.985 1.00159.92 N ANISOU 1862 N PRO A 260 17511 19857 23395 203 605 -567 N ATOM 1863 CA PRO A 260 -5.131 -24.669 -24.864 1.00151.88 C ANISOU 1863 CA PRO A 260 16264 18840 22602 137 456 -479 C ATOM 1864 C PRO A 260 -5.916 -23.767 -25.808 1.00142.53 C ANISOU 1864 C PRO A 260 14973 17618 21565 288 358 -517 C ATOM 1865 O PRO A 260 -6.233 -24.172 -26.926 1.00140.84 O ANISOU 1865 O PRO A 260 14671 17354 21489 261 144 -493 O ATOM 1866 CB PRO A 260 -6.083 -25.363 -23.884 1.00155.53 C ANISOU 1866 CB PRO A 260 16496 19426 23171 86 644 -369 C ATOM 1867 CG PRO A 260 -5.350 -25.381 -22.586 1.00157.10 C ANISOU 1867 CG PRO A 260 16870 19675 23147 76 847 -385 C ATOM 1868 CD PRO A 260 -4.566 -24.107 -22.562 1.00160.52 C ANISOU 1868 CD PRO A 260 17538 20047 23407 207 855 -525 C ATOM 1869 N ASP A 261 -6.223 -22.555 -25.356 1.00136.40 N ANISOU 1869 N ASP A 261 14218 16861 20747 460 507 -581 N ATOM 1870 CA ASP A 261 -6.932 -21.586 -26.183 1.00144.94 C ANISOU 1870 CA ASP A 261 15227 17904 21942 633 432 -624 C ATOM 1871 C ASP A 261 -6.079 -21.132 -27.360 1.00147.99 C ANISOU 1871 C ASP A 261 15829 18142 22256 662 228 -694 C ATOM 1872 O ASP A 261 -6.563 -21.036 -28.488 1.00144.77 O ANISOU 1872 O ASP A 261 15346 17686 21974 728 50 -691 O ATOM 1873 CB ASP A 261 -7.358 -20.375 -25.351 1.00154.57 C ANISOU 1873 CB ASP A 261 16460 19166 23102 821 652 -679 C ATOM 1874 CG ASP A 261 -8.577 -20.654 -24.495 1.00162.38 C ANISOU 1874 CG ASP A 261 17169 20308 24220 858 842 -593 C ATOM 1875 OD1 ASP A 261 -9.130 -21.770 -24.593 1.00168.21 O ANISOU 1875 OD1 ASP A 261 17684 21110 25118 725 799 -488 O ATOM 1876 OD2 ASP A 261 -8.986 -19.754 -23.731 1.00158.15 O ANISOU 1876 OD2 ASP A 261 16637 19822 23629 1025 1039 -628 O ATOM 1877 N CYS A 262 -4.809 -20.850 -27.087 1.00158.26 N ANISOU 1877 N CYS A 262 17399 19374 23359 619 255 -756 N ATOM 1878 CA CYS A 262 -3.882 -20.411 -28.123 1.00162.33 C ANISOU 1878 CA CYS A 262 18131 19750 23798 638 96 -810 C ATOM 1879 C CYS A 262 -3.913 -21.363 -29.312 1.00161.85 C ANISOU 1879 C CYS A 262 18014 19652 23831 563 -143 -749 C ATOM 1880 O CYS A 262 -3.591 -22.544 -29.181 1.00161.67 O ANISOU 1880 O CYS A 262 17967 19663 23798 403 -199 -692 O ATOM 1881 CB CYS A 262 -2.462 -20.308 -27.563 1.00161.75 C ANISOU 1881 CB CYS A 262 18307 19630 23519 549 153 -865 C ATOM 1882 SG CYS A 262 -2.300 -19.185 -26.153 1.00143.28 S ANISOU 1882 SG CYS A 262 16077 17314 21048 641 402 -960 S ATOM 1883 N SER A 263 -4.307 -20.838 -30.468 1.00158.81 N ANISOU 1883 N SER A 263 17623 19190 23527 694 -288 -765 N ATOM 1884 CA SER A 263 -4.430 -21.637 -31.683 1.00157.77 C ANISOU 1884 CA SER A 263 17451 19014 23481 665 -536 -721 C ATOM 1885 C SER A 263 -3.279 -22.626 -31.836 1.00163.58 C ANISOU 1885 C SER A 263 18339 19714 24098 499 -626 -691 C ATOM 1886 O SER A 263 -2.127 -22.231 -32.019 1.00164.28 O ANISOU 1886 O SER A 263 18662 19725 24032 498 -619 -726 O ATOM 1887 CB SER A 263 -4.520 -20.732 -32.915 1.00152.44 C ANISOU 1887 CB SER A 263 16876 18227 22818 852 -667 -761 C ATOM 1888 OG SER A 263 -3.402 -19.867 -32.995 1.00155.06 O ANISOU 1888 OG SER A 263 17478 18453 22984 892 -602 -811 O ATOM 1889 N HIS A 264 -3.602 -23.913 -31.752 1.00168.05 N ANISOU 1889 N HIS A 264 18768 20338 24746 360 -707 -624 N ATOM 1890 CA HIS A 264 -2.602 -24.967 -31.888 1.00166.38 C ANISOU 1890 CA HIS A 264 18692 20099 24425 212 -800 -590 C ATOM 1891 C HIS A 264 -1.771 -24.752 -33.145 1.00165.19 C ANISOU 1891 C HIS A 264 18755 19827 24182 286 -975 -611 C ATOM 1892 O HIS A 264 -2.315 -24.549 -34.230 1.00169.11 O ANISOU 1892 O HIS A 264 19221 20265 24767 405 -1140 -615 O ATOM 1893 CB HIS A 264 -3.269 -26.343 -31.932 1.00162.40 C ANISOU 1893 CB HIS A 264 18005 19638 24060 80 -913 -514 C ATOM 1894 CG HIS A 264 -4.142 -26.632 -30.749 1.00151.04 C ANISOU 1894 CG HIS A 264 16339 18317 22731 5 -728 -470 C ATOM 1895 ND1 HIS A 264 -3.634 -27.016 -29.526 1.00148.39 N ANISOU 1895 ND1 HIS A 264 16053 18049 22282 -105 -538 -445 N ATOM 1896 CD2 HIS A 264 -5.486 -26.601 -30.607 1.00138.71 C ANISOU 1896 CD2 HIS A 264 14500 16822 21383 36 -699 -439 C ATOM 1897 CE1 HIS A 264 -4.631 -27.203 -28.680 1.00138.53 C ANISOU 1897 CE1 HIS A 264 14575 16896 21162 -135 -386 -393 C ATOM 1898 NE2 HIS A 264 -5.765 -26.959 -29.308 1.00134.41 N ANISOU 1898 NE2 HIS A 264 13842 16380 20849 -57 -475 -386 N ATOM 1899 N ALA A 265 -0.452 -24.794 -32.990 1.00160.32 N ANISOU 1899 N ALA A 265 18352 19177 23384 226 -937 -622 N ATOM 1900 CA ALA A 265 0.457 -24.550 -34.101 1.00159.49 C ANISOU 1900 CA ALA A 265 18459 18963 23178 297 -1063 -628 C ATOM 1901 C ALA A 265 0.102 -25.384 -35.326 1.00148.97 C ANISOU 1901 C ALA A 265 17110 17580 21910 331 -1317 -585 C ATOM 1902 O ALA A 265 -0.100 -26.596 -35.226 1.00146.13 O ANISOU 1902 O ALA A 265 16673 17258 21592 213 -1412 -541 O ATOM 1903 CB ALA A 265 1.892 -24.810 -33.679 1.00166.03 C ANISOU 1903 CB ALA A 265 19471 19790 23823 193 -998 -629 C ATOM 1904 N PRO A 266 0.016 -24.724 -36.490 1.00138.18 N ANISOU 1904 N PRO A 266 15832 16120 20550 502 -1432 -599 N ATOM 1905 CA PRO A 266 -0.285 -25.372 -37.771 1.00138.64 C ANISOU 1905 CA PRO A 266 15913 16115 20647 579 -1692 -572 C ATOM 1906 C PRO A 266 0.772 -26.411 -38.115 1.00148.80 C ANISOU 1906 C PRO A 266 17367 17375 21797 492 -1795 -529 C ATOM 1907 O PRO A 266 1.863 -26.386 -37.542 1.00156.25 O ANISOU 1907 O PRO A 266 18431 18335 22601 408 -1661 -522 O ATOM 1908 CB PRO A 266 -0.219 -24.219 -38.779 1.00130.55 C ANISOU 1908 CB PRO A 266 15026 14989 19587 797 -1725 -596 C ATOM 1909 CG PRO A 266 0.477 -23.101 -38.077 1.00125.10 C ANISOU 1909 CG PRO A 266 14434 14288 18810 797 -1484 -626 C ATOM 1910 CD PRO A 266 0.198 -23.270 -36.625 1.00128.73 C ANISOU 1910 CD PRO A 266 14735 14862 19316 644 -1313 -644 C ATOM 1911 N LEU A 267 0.453 -27.318 -39.031 1.00151.57 N ANISOU 1911 N LEU A 267 17723 17684 22185 521 -2038 -505 N ATOM 1912 CA LEU A 267 1.408 -28.337 -39.445 1.00155.28 C ANISOU 1912 CA LEU A 267 18364 18120 22514 466 -2153 -463 C ATOM 1913 C LEU A 267 2.567 -27.749 -40.242 1.00158.30 C ANISOU 1913 C LEU A 267 19004 18425 22716 599 -2138 -448 C ATOM 1914 O LEU A 267 3.710 -28.181 -40.096 1.00161.52 O ANISOU 1914 O LEU A 267 19557 18840 22973 533 -2094 -415 O ATOM 1915 CB LEU A 267 0.715 -29.430 -40.255 1.00156.13 C ANISOU 1915 CB LEU A 267 18426 18187 22711 477 -2435 -451 C ATOM 1916 CG LEU A 267 -0.280 -30.286 -39.475 1.00160.23 C ANISOU 1916 CG LEU A 267 18694 18772 23414 304 -2457 -444 C ATOM 1917 CD1 LEU A 267 -0.930 -31.311 -40.389 1.00163.28 C ANISOU 1917 CD1 LEU A 267 19047 19092 23900 317 -2766 -443 C ATOM 1918 CD2 LEU A 267 0.413 -30.964 -38.306 1.00157.10 C ANISOU 1918 CD2 LEU A 267 18311 18445 22935 105 -2293 -407 C ATOM 1919 N TRP A 268 2.272 -26.769 -41.090 1.00153.33 N ANISOU 1919 N TRP A 268 18432 17723 22104 793 -2170 -465 N ATOM 1920 CA TRP A 268 3.305 -26.178 -41.934 1.00146.82 C ANISOU 1920 CA TRP A 268 17851 16812 21122 933 -2147 -435 C ATOM 1921 C TRP A 268 4.368 -25.515 -41.070 1.00142.59 C ANISOU 1921 C TRP A 268 17377 16303 20497 835 -1893 -433 C ATOM 1922 O TRP A 268 5.543 -25.466 -41.430 1.00144.00 O ANISOU 1922 O TRP A 268 17735 16445 20534 855 -1851 -391 O ATOM 1923 CB TRP A 268 2.702 -25.153 -42.894 1.00145.01 C ANISOU 1923 CB TRP A 268 17667 16496 20934 1165 -2200 -452 C ATOM 1924 CG TRP A 268 2.338 -23.872 -42.225 1.00141.13 C ANISOU 1924 CG TRP A 268 17090 16015 20520 1179 -1996 -494 C ATOM 1925 CD1 TRP A 268 1.116 -23.525 -41.733 1.00139.40 C ANISOU 1925 CD1 TRP A 268 16658 15845 20461 1184 -1981 -545 C ATOM 1926 CD2 TRP A 268 3.209 -22.766 -41.957 1.00137.79 C ANISOU 1926 CD2 TRP A 268 16793 15544 20017 1193 -1779 -491 C ATOM 1927 NE1 TRP A 268 1.169 -22.269 -41.179 1.00137.84 N ANISOU 1927 NE1 TRP A 268 16465 15634 20272 1215 -1769 -576 N ATOM 1928 CE2 TRP A 268 2.443 -21.781 -41.304 1.00136.51 C ANISOU 1928 CE2 TRP A 268 16506 15397 19963 1213 -1648 -548 C ATOM 1929 CE3 TRP A 268 4.561 -22.512 -42.207 1.00131.88 C ANISOU 1929 CE3 TRP A 268 16245 14740 19125 1188 -1682 -444 C ATOM 1930 CZ2 TRP A 268 2.983 -20.563 -40.899 1.00133.63 C ANISOU 1930 CZ2 TRP A 268 16229 14979 19564 1226 -1439 -568 C ATOM 1931 CZ3 TRP A 268 5.096 -21.303 -41.803 1.00126.75 C ANISOU 1931 CZ3 TRP A 268 15658 14039 18461 1185 -1472 -460 C ATOM 1932 CH2 TRP A 268 4.309 -20.344 -41.156 1.00128.41 C ANISOU 1932 CH2 TRP A 268 15761 14252 18778 1202 -1358 -526 C ATOM 1933 N LEU A 269 3.939 -24.997 -39.925 1.00135.98 N ANISOU 1933 N LEU A 269 16387 15532 19748 734 -1728 -482 N ATOM 1934 CA LEU A 269 4.848 -24.367 -38.982 1.00125.29 C ANISOU 1934 CA LEU A 269 15077 14204 18323 634 -1505 -502 C ATOM 1935 C LEU A 269 5.470 -25.421 -38.082 1.00125.07 C ANISOU 1935 C LEU A 269 15024 14272 18225 443 -1475 -489 C ATOM 1936 O LEU A 269 6.582 -25.255 -37.586 1.00127.68 O ANISOU 1936 O LEU A 269 15443 14622 18449 367 -1355 -492 O ATOM 1937 CB LEU A 269 4.101 -23.344 -38.128 1.00118.99 C ANISOU 1937 CB LEU A 269 14150 13430 17631 634 -1347 -566 C ATOM 1938 CG LEU A 269 4.966 -22.529 -37.169 1.00106.01 C ANISOU 1938 CG LEU A 269 12563 11793 15922 550 -1131 -607 C ATOM 1939 CD1 LEU A 269 5.940 -21.672 -37.957 1.00 99.55 C ANISOU 1939 CD1 LEU A 269 11942 10857 15026 641 -1091 -587 C ATOM 1940 CD2 LEU A 269 4.096 -21.670 -36.271 1.00106.52 C ANISOU 1940 CD2 LEU A 269 12501 11888 16085 562 -994 -675 C ATOM 1941 N MET A 270 4.739 -26.508 -37.868 1.00127.15 N ANISOU 1941 N MET A 270 15163 14593 18555 368 -1587 -476 N ATOM 1942 CA MET A 270 5.208 -27.575 -36.997 1.00136.95 C ANISOU 1942 CA MET A 270 16384 15919 19732 197 -1559 -458 C ATOM 1943 C MET A 270 6.465 -28.225 -37.560 1.00147.27 C ANISOU 1943 C MET A 270 17882 17203 20871 198 -1633 -411 C ATOM 1944 O MET A 270 7.445 -28.419 -36.841 1.00152.91 O ANISOU 1944 O MET A 270 18653 17974 21473 100 -1528 -411 O ATOM 1945 CB MET A 270 4.115 -28.625 -36.784 1.00139.34 C ANISOU 1945 CB MET A 270 16521 16263 20160 119 -1672 -441 C ATOM 1946 CG MET A 270 4.514 -29.737 -35.820 1.00141.31 C ANISOU 1946 CG MET A 270 16754 16592 20346 -55 -1627 -414 C ATOM 1947 SD MET A 270 4.892 -29.129 -34.167 1.00168.31 S ANISOU 1947 SD MET A 270 20122 20113 23714 -160 -1345 -457 S ATOM 1948 CE MET A 270 3.317 -28.411 -33.701 1.00179.66 C ANISOU 1948 CE MET A 270 21322 21579 25360 -128 -1258 -488 C ATOM 1949 N TYR A 271 6.435 -28.555 -38.847 1.00149.28 N ANISOU 1949 N TYR A 271 18240 17379 21102 325 -1818 -372 N ATOM 1950 CA TYR A 271 7.574 -29.206 -39.485 1.00152.08 C ANISOU 1950 CA TYR A 271 18783 17711 21289 358 -1895 -318 C ATOM 1951 C TYR A 271 8.801 -28.299 -39.502 1.00144.67 C ANISOU 1951 C TYR A 271 17966 16760 20243 392 -1735 -308 C ATOM 1952 O TYR A 271 9.924 -28.764 -39.343 1.00146.23 O ANISOU 1952 O TYR A 271 18258 16997 20306 342 -1702 -277 O ATOM 1953 CB TYR A 271 7.226 -29.665 -40.908 1.00162.72 C ANISOU 1953 CB TYR A 271 20233 18967 22626 521 -2130 -283 C ATOM 1954 CG TYR A 271 7.543 -28.655 -41.994 1.00176.61 C ANISOU 1954 CG TYR A 271 22131 20634 24337 723 -2122 -263 C ATOM 1955 CD1 TYR A 271 8.843 -28.492 -42.459 1.00180.36 C ANISOU 1955 CD1 TYR A 271 22788 21086 24653 787 -2056 -206 C ATOM 1956 CD2 TYR A 271 6.541 -27.879 -42.566 1.00186.16 C ANISOU 1956 CD2 TYR A 271 23290 21780 25662 858 -2175 -292 C ATOM 1957 CE1 TYR A 271 9.141 -27.573 -43.449 1.00184.75 C ANISOU 1957 CE1 TYR A 271 23477 21550 25168 972 -2026 -171 C ATOM 1958 CE2 TYR A 271 6.828 -26.961 -43.559 1.00192.21 C ANISOU 1958 CE2 TYR A 271 24203 22454 26375 1054 -2158 -265 C ATOM 1959 CZ TYR A 271 8.130 -26.813 -43.996 1.00192.12 C ANISOU 1959 CZ TYR A 271 24378 22412 26207 1108 -2077 -200 C ATOM 1960 OH TYR A 271 8.422 -25.902 -44.985 1.00197.17 O ANISOU 1960 OH TYR A 271 25170 22951 26796 1305 -2038 -156 O ATOM 1961 N LEU A 272 8.581 -27.003 -39.700 1.00133.13 N ANISOU 1961 N LEU A 272 16497 15240 18845 477 -1637 -335 N ATOM 1962 CA LEU A 272 9.678 -26.043 -39.744 1.00122.35 C ANISOU 1962 CA LEU A 272 15236 13840 17411 498 -1482 -325 C ATOM 1963 C LEU A 272 10.471 -26.079 -38.442 1.00122.97 C ANISOU 1963 C LEU A 272 15266 14012 17443 320 -1332 -364 C ATOM 1964 O LEU A 272 11.700 -26.016 -38.451 1.00129.96 O ANISOU 1964 O LEU A 272 16241 14909 18228 292 -1266 -337 O ATOM 1965 CB LEU A 272 9.153 -24.630 -40.021 1.00119.40 C ANISOU 1965 CB LEU A 272 14855 13377 17134 604 -1395 -355 C ATOM 1966 CG LEU A 272 10.184 -23.510 -40.199 1.00119.62 C ANISOU 1966 CG LEU A 272 14996 13333 17122 634 -1235 -339 C ATOM 1967 CD1 LEU A 272 9.633 -22.402 -41.085 1.00118.74 C ANISOU 1967 CD1 LEU A 272 14950 13093 17073 815 -1222 -329 C ATOM 1968 CD2 LEU A 272 10.640 -22.952 -38.857 1.00118.89 C ANISOU 1968 CD2 LEU A 272 14828 13293 17052 468 -1060 -413 C ATOM 1969 N ALA A 273 9.760 -26.186 -37.325 1.00116.74 N ANISOU 1969 N ALA A 273 14332 13296 16728 209 -1279 -425 N ATOM 1970 CA ALA A 273 10.399 -26.278 -36.017 1.00116.30 C ANISOU 1970 CA ALA A 273 14236 13335 16619 57 -1151 -471 C ATOM 1971 C ALA A 273 11.111 -27.617 -35.864 1.00122.50 C ANISOU 1971 C ALA A 273 15070 14197 17277 -17 -1228 -427 C ATOM 1972 O ALA A 273 12.144 -27.712 -35.203 1.00122.09 O ANISOU 1972 O ALA A 273 15053 14209 17127 -99 -1149 -444 O ATOM 1973 CB ALA A 273 9.373 -26.090 -34.912 1.00110.20 C ANISOU 1973 CB ALA A 273 13310 12618 15944 -12 -1070 -536 C ATOM 1974 N ILE A 274 10.548 -28.649 -36.484 1.00124.86 N ANISOU 1974 N ILE A 274 15376 14485 17580 18 -1391 -376 N ATOM 1975 CA ILE A 274 11.132 -29.985 -36.447 1.00125.91 C ANISOU 1975 CA ILE A 274 15577 14672 17592 -33 -1483 -329 C ATOM 1976 C ILE A 274 12.367 -30.060 -37.339 1.00125.86 C ANISOU 1976 C ILE A 274 15734 14639 17448 56 -1520 -272 C ATOM 1977 O ILE A 274 13.380 -30.652 -36.966 1.00126.92 O ANISOU 1977 O ILE A 274 15928 14844 17452 2 -1499 -254 O ATOM 1978 CB ILE A 274 10.117 -31.053 -36.896 1.00128.03 C ANISOU 1978 CB ILE A 274 15812 14913 17921 -23 -1664 -296 C ATOM 1979 CG1 ILE A 274 8.844 -30.965 -36.051 1.00134.71 C ANISOU 1979 CG1 ILE A 274 16468 15790 18925 -108 -1613 -337 C ATOM 1980 CG2 ILE A 274 10.723 -32.440 -36.800 1.00127.80 C ANISOU 1980 CG2 ILE A 274 15872 14925 17759 -77 -1755 -250 C ATOM 1981 CD1 ILE A 274 7.752 -31.909 -36.499 1.00142.19 C ANISOU 1981 CD1 ILE A 274 17347 16700 19978 -113 -1792 -309 C ATOM 1982 N VAL A 275 12.275 -29.458 -38.520 1.00123.52 N ANISOU 1982 N VAL A 275 15511 14243 17175 204 -1569 -239 N ATOM 1983 CA VAL A 275 13.399 -29.418 -39.448 1.00121.34 C ANISOU 1983 CA VAL A 275 15391 13935 16777 313 -1579 -169 C ATOM 1984 C VAL A 275 14.543 -28.610 -38.853 1.00129.49 C ANISOU 1984 C VAL A 275 16417 15008 17775 242 -1395 -186 C ATOM 1985 O VAL A 275 15.714 -28.949 -39.022 1.00138.36 O ANISOU 1985 O VAL A 275 17618 16173 18778 250 -1375 -137 O ATOM 1986 CB VAL A 275 12.998 -28.802 -40.803 1.00111.53 C ANISOU 1986 CB VAL A 275 14237 12570 15568 505 -1645 -126 C ATOM 1987 CG1 VAL A 275 14.212 -28.679 -41.710 1.00109.32 C ANISOU 1987 CG1 VAL A 275 14118 12259 15158 625 -1615 -39 C ATOM 1988 CG2 VAL A 275 11.917 -29.636 -41.467 1.00108.79 C ANISOU 1988 CG2 VAL A 275 13901 12179 15254 586 -1862 -119 C ATOM 1989 N LEU A 276 14.194 -27.541 -38.146 1.00125.71 N ANISOU 1989 N LEU A 276 15841 14516 17408 175 -1265 -259 N ATOM 1990 CA LEU A 276 15.186 -26.675 -37.520 1.00127.28 C ANISOU 1990 CA LEU A 276 16023 14734 17602 94 -1104 -296 C ATOM 1991 C LEU A 276 16.022 -27.439 -36.495 1.00134.58 C ANISOU 1991 C LEU A 276 16920 15791 18424 -36 -1082 -325 C ATOM 1992 O LEU A 276 17.199 -27.138 -36.291 1.00135.18 O ANISOU 1992 O LEU A 276 17012 15900 18449 -79 -1004 -326 O ATOM 1993 CB LEU A 276 14.506 -25.474 -36.858 1.00123.01 C ANISOU 1993 CB LEU A 276 15394 14148 17196 51 -991 -385 C ATOM 1994 CG LEU A 276 15.428 -24.430 -36.226 1.00121.24 C ANISOU 1994 CG LEU A 276 15160 13914 16993 -34 -839 -442 C ATOM 1995 CD1 LEU A 276 16.389 -23.861 -37.259 1.00119.31 C ANISOU 1995 CD1 LEU A 276 15013 13583 16736 41 -796 -362 C ATOM 1996 CD2 LEU A 276 14.611 -23.323 -35.581 1.00124.28 C ANISOU 1996 CD2 LEU A 276 15479 14243 17499 -55 -747 -535 C ATOM 1997 N ALA A 277 15.408 -28.429 -35.856 1.00138.39 N ANISOU 1997 N ALA A 277 17355 16345 18881 -96 -1151 -345 N ATOM 1998 CA ALA A 277 16.095 -29.237 -34.853 1.00134.82 C ANISOU 1998 CA ALA A 277 16892 16018 18317 -201 -1136 -370 C ATOM 1999 C ALA A 277 17.047 -30.242 -35.495 1.00125.67 C ANISOU 1999 C ALA A 277 15843 14899 17009 -146 -1226 -286 C ATOM 2000 O ALA A 277 18.133 -30.497 -34.976 1.00121.39 O ANISOU 2000 O ALA A 277 15313 14447 16362 -195 -1186 -296 O ATOM 2001 CB ALA A 277 15.089 -29.949 -33.964 1.00141.61 C ANISOU 2001 CB ALA A 277 17676 16929 19201 -276 -1160 -404 C ATOM 2002 N HIS A 278 16.635 -30.809 -36.624 1.00129.33 N ANISOU 2002 N HIS A 278 16389 15296 17456 -31 -1356 -210 N ATOM 2003 CA HIS A 278 17.464 -31.772 -37.340 1.00135.50 C ANISOU 2003 CA HIS A 278 17298 16102 18085 53 -1450 -126 C ATOM 2004 C HIS A 278 18.630 -31.081 -38.036 1.00134.98 C ANISOU 2004 C HIS A 278 17290 16023 17975 133 -1371 -73 C ATOM 2005 O HIS A 278 19.616 -31.722 -38.397 1.00138.67 O ANISOU 2005 O HIS A 278 17841 16545 18304 192 -1398 -8 O ATOM 2006 CB HIS A 278 16.636 -32.557 -38.360 1.00142.91 C ANISOU 2006 CB HIS A 278 18323 16958 19017 166 -1628 -70 C ATOM 2007 CG HIS A 278 15.507 -33.332 -37.756 1.00148.60 C ANISOU 2007 CG HIS A 278 18977 17684 19800 77 -1712 -107 C ATOM 2008 ND1 HIS A 278 15.492 -34.282 -36.791 1.00147.23 N ANISOU 2008 ND1 HIS A 278 18746 17425 19769 102 -1792 -123 N ATOM 2009 CD2 HIS A 278 14.195 -33.159 -38.143 1.00150.86 C ANISOU 2009 CD2 HIS A 278 19239 18048 20032 -36 -1722 -124 C ATOM 2010 CE1 HIS A 278 14.184 -34.664 -36.617 1.00146.05 C ANISOU 2010 CE1 HIS A 278 18525 17302 19667 -4 -1843 -144 C ATOM 2011 NE2 HIS A 278 13.421 -33.972 -37.445 1.00148.41 N ANISOU 2011 NE2 HIS A 278 18852 17694 19844 -87 -1795 -141 N ATOM 2012 N THR A 279 18.510 -29.770 -38.218 1.00129.80 N ANISOU 2012 N THR A 279 16587 15292 17440 139 -1265 -94 N ATOM 2013 CA THR A 279 19.559 -28.982 -38.853 1.00129.85 C ANISOU 2013 CA THR A 279 16633 15266 17439 198 -1163 -36 C ATOM 2014 C THR A 279 20.735 -28.775 -37.904 1.00136.78 C ANISOU 2014 C THR A 279 17433 16250 18289 70 -1056 -80 C ATOM 2015 O THR A 279 21.875 -28.596 -38.335 1.00140.86 O ANISOU 2015 O THR A 279 17972 16788 18761 105 -995 -15 O ATOM 2016 CB THR A 279 19.026 -27.609 -39.306 1.00125.07 C ANISOU 2016 CB THR A 279 16012 14529 16981 239 -1078 -46 C ATOM 2017 OG1 THR A 279 17.992 -27.796 -40.279 1.00125.44 O ANISOU 2017 OG1 THR A 279 16135 14482 17044 384 -1193 -5 O ATOM 2018 CG2 THR A 279 20.141 -26.774 -39.916 1.00123.72 C ANISOU 2018 CG2 THR A 279 15877 14313 16817 283 -951 25 C ATOM 2019 N ASN A 280 20.448 -28.809 -36.608 1.00139.28 N ANISOU 2019 N ASN A 280 17654 16634 18632 -72 -1035 -189 N ATOM 2020 CA ASN A 280 21.461 -28.593 -35.583 1.00142.08 C ANISOU 2020 CA ASN A 280 17933 17090 18962 -193 -956 -257 C ATOM 2021 C ASN A 280 22.631 -29.569 -35.694 1.00150.61 C ANISOU 2021 C ASN A 280 19054 18288 19883 -161 -998 -196 C ATOM 2022 O ASN A 280 23.771 -29.230 -35.375 1.00158.74 O ANISOU 2022 O ASN A 280 20028 19383 20901 -213 -930 -212 O ATOM 2023 CB ASN A 280 20.829 -28.685 -34.194 1.00138.78 C ANISOU 2023 CB ASN A 280 17438 16730 18561 -312 -947 -378 C ATOM 2024 CG ASN A 280 21.760 -28.213 -33.097 1.00135.86 C ANISOU 2024 CG ASN A 280 16994 16444 18184 -427 -871 -476 C ATOM 2025 OD1 ASN A 280 21.355 -28.422 -31.853 1.00139.58 O ANISOU 2025 OD1 ASN A 280 17443 16915 18676 -441 -819 -462 O ATOM 2026 ND2 ASN A 280 22.827 -27.660 -33.364 1.00132.67 N ANISOU 2026 ND2 ASN A 280 16547 16108 17753 -507 -865 -576 N ATOM 2027 N SER A 281 22.342 -30.782 -36.153 1.00147.84 N ANISOU 2027 N SER A 281 18799 17960 19413 -73 -1116 -129 N ATOM 2028 CA SER A 281 23.361 -31.820 -36.270 1.00145.27 C ANISOU 2028 CA SER A 281 18535 17746 18916 -19 -1167 -69 C ATOM 2029 C SER A 281 24.342 -31.548 -37.409 1.00136.17 C ANISOU 2029 C SER A 281 17432 16576 17731 102 -1125 44 C ATOM 2030 O SER A 281 25.406 -32.164 -37.485 1.00126.79 O ANISOU 2030 O SER A 281 16266 15492 16415 149 -1131 96 O ATOM 2031 CB SER A 281 22.703 -33.189 -36.458 1.00144.89 C ANISOU 2031 CB SER A 281 18596 17702 18754 45 -1313 -31 C ATOM 2032 OG SER A 281 21.885 -33.207 -37.613 1.00144.40 O ANISOU 2032 OG SER A 281 18620 17513 18732 162 -1390 33 O ATOM 2033 N VAL A 282 23.981 -30.619 -38.288 1.00134.77 N ANISOU 2033 N VAL A 282 17272 16268 17666 164 -1072 89 N ATOM 2034 CA VAL A 282 24.781 -30.330 -39.475 1.00130.03 C ANISOU 2034 CA VAL A 282 16736 15631 17037 302 -1014 217 C ATOM 2035 C VAL A 282 25.722 -29.140 -39.281 1.00134.46 C ANISOU 2035 C VAL A 282 17180 16191 17719 213 -848 212 C ATOM 2036 O VAL A 282 26.795 -29.081 -39.884 1.00136.91 O ANISOU 2036 O VAL A 282 17494 16535 17990 283 -776 314 O ATOM 2037 CB VAL A 282 23.879 -30.076 -40.704 1.00116.69 C ANISOU 2037 CB VAL A 282 15167 13789 15379 458 -1056 288 C ATOM 2038 CG1 VAL A 282 24.707 -29.626 -41.899 1.00118.31 C ANISOU 2038 CG1 VAL A 282 15446 13948 15559 611 -963 428 C ATOM 2039 CG2 VAL A 282 23.086 -31.327 -41.043 1.00108.29 C ANISOU 2039 CG2 VAL A 282 14225 12721 14199 556 -1242 301 C ATOM 2040 N VAL A 283 25.320 -28.199 -38.434 1.00131.70 N ANISOU 2040 N VAL A 283 16724 15797 17519 61 -788 96 N ATOM 2041 CA VAL A 283 26.088 -26.974 -38.235 1.00133.31 C ANISOU 2041 CA VAL A 283 16821 15964 17865 -40 -644 76 C ATOM 2042 C VAL A 283 27.448 -27.222 -37.585 1.00137.07 C ANISOU 2042 C VAL A 283 17189 16590 18300 -129 -614 55 C ATOM 2043 O VAL A 283 28.391 -26.457 -37.791 1.00136.00 O ANISOU 2043 O VAL A 283 16973 16438 18261 -174 -502 93 O ATOM 2044 CB VAL A 283 25.304 -25.950 -37.389 1.00131.10 C ANISOU 2044 CB VAL A 283 16471 15600 17742 -176 -604 -62 C ATOM 2045 CG1 VAL A 283 23.998 -25.585 -38.075 1.00132.62 C ANISOU 2045 CG1 VAL A 283 16752 15647 17991 -78 -624 -39 C ATOM 2046 CG2 VAL A 283 25.046 -26.499 -35.994 1.00128.79 C ANISOU 2046 CG2 VAL A 283 16115 15423 17397 -293 -675 -202 C ATOM 2047 N ASN A 284 27.545 -28.291 -36.801 1.00138.51 N ANISOU 2047 N ASN A 284 17367 16916 18345 -152 -715 -3 N ATOM 2048 CA ASN A 284 28.774 -28.594 -36.071 1.00137.35 C ANISOU 2048 CA ASN A 284 17116 16928 18145 -226 -710 -42 C ATOM 2049 C ASN A 284 29.991 -28.820 -36.971 1.00130.15 C ANISOU 2049 C ASN A 284 16195 16076 17179 -124 -656 103 C ATOM 2050 O ASN A 284 31.010 -28.151 -36.811 1.00121.24 O ANISOU 2050 O ASN A 284 14933 14982 16151 -207 -566 101 O ATOM 2051 CB ASN A 284 28.568 -29.784 -35.130 1.00142.02 C ANISOU 2051 CB ASN A 284 17736 17652 18572 -238 -830 -117 C ATOM 2052 CG ASN A 284 27.479 -29.533 -34.107 1.00147.18 C ANISOU 2052 CG ASN A 284 18377 18265 19280 -344 -857 -256 C ATOM 2053 OD1 ASN A 284 27.109 -28.389 -33.845 1.00147.45 O ANISOU 2053 OD1 ASN A 284 18350 18199 19473 -432 -787 -329 O ATOM 2054 ND2 ASN A 284 26.958 -30.605 -33.521 1.00149.62 N ANISOU 2054 ND2 ASN A 284 18748 18646 19455 -328 -949 -288 N ATOM 2055 N PRO A 285 29.891 -29.762 -37.922 1.00134.38 N ANISOU 2055 N PRO A 285 16872 16624 17561 61 -710 230 N ATOM 2056 CA PRO A 285 31.024 -30.022 -38.816 1.00131.96 C ANISOU 2056 CA PRO A 285 16573 16383 17184 190 -647 381 C ATOM 2057 C PRO A 285 31.539 -28.748 -39.483 1.00125.61 C ANISOU 2057 C PRO A 285 15690 15477 16561 167 -478 462 C ATOM 2058 O PRO A 285 32.743 -28.611 -39.696 1.00125.56 O ANISOU 2058 O PRO A 285 15581 15551 16573 172 -386 539 O ATOM 2059 CB PRO A 285 30.429 -30.962 -39.865 1.00134.33 C ANISOU 2059 CB PRO A 285 17081 16638 17318 406 -735 493 C ATOM 2060 CG PRO A 285 29.325 -31.659 -39.153 1.00135.16 C ANISOU 2060 CG PRO A 285 17252 16738 17364 358 -880 381 C ATOM 2061 CD PRO A 285 28.746 -30.643 -38.212 1.00135.78 C ANISOU 2061 CD PRO A 285 17209 16755 17626 162 -836 240 C ATOM 2062 N PHE A 286 30.634 -27.830 -39.802 1.00122.61 N ANISOU 2062 N PHE A 286 15352 14920 16315 143 -433 448 N ATOM 2063 CA PHE A 286 31.009 -26.587 -40.465 1.00122.44 C ANISOU 2063 CA PHE A 286 15283 14770 16467 126 -265 530 C ATOM 2064 C PHE A 286 31.547 -25.549 -39.484 1.00120.53 C ANISOU 2064 C PHE A 286 14849 14522 16426 -110 -189 412 C ATOM 2065 O PHE A 286 32.323 -24.672 -39.864 1.00115.23 O ANISOU 2065 O PHE A 286 14088 13792 15902 -159 -43 486 O ATOM 2066 CB PHE A 286 29.821 -26.009 -41.238 1.00129.43 C ANISOU 2066 CB PHE A 286 16310 15463 17405 218 -251 564 C ATOM 2067 CG PHE A 286 29.391 -26.848 -42.406 1.00137.18 C ANISOU 2067 CG PHE A 286 17488 16422 18212 468 -319 693 C ATOM 2068 CD1 PHE A 286 28.371 -27.774 -42.273 1.00142.93 C ANISOU 2068 CD1 PHE A 286 18325 17164 18816 530 -495 631 C ATOM 2069 CD2 PHE A 286 30.011 -26.712 -43.638 1.00138.34 C ANISOU 2069 CD2 PHE A 286 17715 16530 18319 644 -208 877 C ATOM 2070 CE1 PHE A 286 27.975 -28.548 -43.348 1.00145.47 C ANISOU 2070 CE1 PHE A 286 18836 17455 18984 758 -583 734 C ATOM 2071 CE2 PHE A 286 29.619 -27.484 -44.715 1.00141.49 C ANISOU 2071 CE2 PHE A 286 18315 16904 18540 895 -285 986 C ATOM 2072 CZ PHE A 286 28.599 -28.404 -44.569 1.00144.99 C ANISOU 2072 CZ PHE A 286 18869 17354 18865 949 -485 906 C ATOM 2073 N ILE A 287 31.133 -25.647 -38.225 1.00127.05 N ANISOU 2073 N ILE A 287 15616 15399 17258 -251 -288 231 N ATOM 2074 CA ILE A 287 31.571 -24.692 -37.214 1.00135.55 C ANISOU 2074 CA ILE A 287 16531 16463 18509 -466 -247 92 C ATOM 2075 C ILE A 287 32.991 -24.998 -36.744 1.00135.79 C ANISOU 2075 C ILE A 287 16400 16665 18531 -537 -245 83 C ATOM 2076 O ILE A 287 33.679 -24.126 -36.216 1.00138.32 O ANISOU 2076 O ILE A 287 16566 16967 19024 -702 -192 9 O ATOM 2077 CB ILE A 287 30.619 -24.654 -36.001 1.00143.58 C ANISOU 2077 CB ILE A 287 17555 17475 19523 -570 -347 -102 C ATOM 2078 CG1 ILE A 287 30.809 -23.357 -35.213 1.00150.26 C ANISOU 2078 CG1 ILE A 287 18287 18230 20575 -762 -292 -239 C ATOM 2079 CG2 ILE A 287 30.836 -25.861 -35.103 1.00144.55 C ANISOU 2079 CG2 ILE A 287 17663 17795 19465 -570 -476 -180 C ATOM 2080 CD1 ILE A 287 29.924 -23.254 -33.993 1.00153.58 C ANISOU 2080 CD1 ILE A 287 18722 18649 20984 -846 -375 -428 C ATOM 2081 N TYR A 288 33.425 -26.240 -36.938 1.00130.53 N ANISOU 2081 N TYR A 288 15769 16162 17665 -409 -312 154 N ATOM 2082 CA TYR A 288 34.789 -26.629 -36.602 1.00119.75 C ANISOU 2082 CA TYR A 288 14251 14978 16270 -440 -313 163 C ATOM 2083 C TYR A 288 35.740 -26.210 -37.713 1.00114.25 C ANISOU 2083 C TYR A 288 13488 14259 15664 -377 -155 351 C ATOM 2084 O TYR A 288 36.833 -25.709 -37.452 1.00119.49 O ANISOU 2084 O TYR A 288 13955 14981 16465 -493 -90 346 O ATOM 2085 CB TYR A 288 34.886 -28.137 -36.373 1.00117.19 C ANISOU 2085 CB TYR A 288 14006 14835 15685 -309 -441 170 C ATOM 2086 CG TYR A 288 34.032 -28.643 -35.234 1.00121.43 C ANISOU 2086 CG TYR A 288 14605 15407 16126 -367 -580 1 C ATOM 2087 CD1 TYR A 288 34.227 -28.185 -33.938 1.00124.57 C ANISOU 2087 CD1 TYR A 288 14879 15851 16601 -540 -622 -182 C ATOM 2088 CD2 TYR A 288 33.039 -29.588 -35.452 1.00122.01 C ANISOU 2088 CD2 TYR A 288 14862 15463 16031 -245 -668 28 C ATOM 2089 CE1 TYR A 288 33.450 -28.646 -32.893 1.00125.93 C ANISOU 2089 CE1 TYR A 288 15118 16056 16674 -574 -728 -323 C ATOM 2090 CE2 TYR A 288 32.257 -30.055 -34.413 1.00124.25 C ANISOU 2090 CE2 TYR A 288 15195 15776 16238 -301 -771 -108 C ATOM 2091 CZ TYR A 288 32.468 -29.581 -33.136 1.00126.72 C ANISOU 2091 CZ TYR A 288 15391 16140 16618 -458 -791 -277 C ATOM 2092 OH TYR A 288 31.693 -30.044 -32.098 1.00128.60 O ANISOU 2092 OH TYR A 288 15687 16408 16768 -495 -875 -399 O ATOM 2093 N ALA A 289 35.313 -26.419 -38.954 1.00106.65 N ANISOU 2093 N ALA A 289 12688 13211 14624 -188 -96 519 N ATOM 2094 CA ALA A 289 36.122 -26.069 -40.115 1.00106.51 C ANISOU 2094 CA ALA A 289 12642 13162 14664 -88 74 724 C ATOM 2095 C ALA A 289 36.358 -24.564 -40.209 1.00126.83 C ANISOU 2095 C ALA A 289 15095 15571 17522 -253 232 732 C ATOM 2096 O ALA A 289 37.308 -24.115 -40.847 1.00140.01 O ANISOU 2096 O ALA A 289 16661 17235 19301 -245 392 878 O ATOM 2097 CB ALA A 289 35.470 -26.588 -41.389 1.00 90.52 C ANISOU 2097 CB ALA A 289 10855 11062 12477 169 86 884 C ATOM 2098 N TYR A 290 35.490 -23.786 -39.574 1.00134.99 N ANISOU 2098 N TYR A 290 16147 16465 18678 -397 193 580 N ATOM 2099 CA TYR A 290 35.617 -22.333 -39.601 1.00148.86 C ANISOU 2099 CA TYR A 290 17817 18039 20704 -557 329 570 C ATOM 2100 C TYR A 290 36.334 -21.800 -38.364 1.00149.54 C ANISOU 2100 C TYR A 290 17682 18179 20959 -812 288 395 C ATOM 2101 O TYR A 290 37.321 -21.071 -38.474 1.00149.48 O ANISOU 2101 O TYR A 290 17503 18142 21149 -933 405 445 O ATOM 2102 CB TYR A 290 34.242 -21.673 -39.733 1.00159.72 C ANISOU 2102 CB TYR A 290 19357 19207 22121 -544 322 515 C ATOM 2103 CG TYR A 290 34.279 -20.163 -39.632 1.00170.94 C ANISOU 2103 CG TYR A 290 20714 20424 23811 -714 445 479 C ATOM 2104 CD1 TYR A 290 34.472 -19.376 -40.759 1.00175.12 C ANISOU 2104 CD1 TYR A 290 21292 20788 24457 -650 635 661 C ATOM 2105 CD2 TYR A 290 34.120 -19.526 -38.408 1.00174.66 C ANISOU 2105 CD2 TYR A 290 21094 20858 24413 -927 372 264 C ATOM 2106 CE1 TYR A 290 34.507 -17.996 -40.670 1.00177.59 C ANISOU 2106 CE1 TYR A 290 21561 20895 25019 -808 752 633 C ATOM 2107 CE2 TYR A 290 34.154 -18.147 -38.309 1.00176.86 C ANISOU 2107 CE2 TYR A 290 21330 20933 24935 -1081 475 224 C ATOM 2108 CZ TYR A 290 34.347 -17.388 -39.443 1.00178.20 C ANISOU 2108 CZ TYR A 290 21547 20932 25227 -1027 665 410 C ATOM 2109 OH TYR A 290 34.380 -16.016 -39.348 1.00180.15 O ANISOU 2109 OH TYR A 290 21769 20959 25722 -1183 770 375 O ATOM 2110 N ARG A 291 35.830 -22.164 -37.189 1.00151.08 N ANISOU 2110 N ARG A 291 17881 18448 21075 -888 120 191 N ATOM 2111 CA ARG A 291 36.386 -21.681 -35.930 1.00153.22 C ANISOU 2111 CA ARG A 291 17974 18766 21479 -1109 49 -4 C ATOM 2112 C ARG A 291 37.787 -22.220 -35.671 1.00154.61 C ANISOU 2112 C ARG A 291 17950 19152 21643 -1142 26 15 C ATOM 2113 O ARG A 291 38.702 -21.463 -35.349 1.00161.87 O ANISOU 2113 O ARG A 291 18671 20057 22774 -1314 68 -28 O ATOM 2114 CB ARG A 291 35.465 -22.044 -34.764 1.00153.53 C ANISOU 2114 CB ARG A 291 18093 18844 21398 -1140 -117 -213 C ATOM 2115 CG ARG A 291 34.179 -21.239 -34.718 1.00150.78 C ANISOU 2115 CG ARG A 291 17881 18287 21120 -1162 -98 -280 C ATOM 2116 CD ARG A 291 34.465 -19.776 -34.425 1.00147.31 C ANISOU 2116 CD ARG A 291 17347 17672 20951 -1354 -23 -362 C ATOM 2117 NE ARG A 291 35.105 -19.600 -33.125 1.00144.89 N ANISOU 2117 NE ARG A 291 16894 17454 20704 -1525 -132 -565 N ATOM 2118 CZ ARG A 291 35.487 -18.427 -32.633 1.00147.92 C ANISOU 2118 CZ ARG A 291 17179 17706 21317 -1715 -113 -679 C ATOM 2119 NH1 ARG A 291 35.297 -17.317 -33.335 1.00148.48 N ANISOU 2119 NH1 ARG A 291 17285 17546 21584 -1763 27 -601 N ATOM 2120 NH2 ARG A 291 36.060 -18.361 -31.439 1.00151.59 N ANISOU 2120 NH2 ARG A 291 17522 18263 21813 -1850 -241 -876 N ATOM 2121 N ILE A 292 37.951 -23.531 -35.810 1.00147.17 N ANISOU 2121 N ILE A 292 17059 18400 20457 -975 -46 76 N ATOM 2122 CA ILE A 292 39.236 -24.162 -35.538 1.00142.50 C ANISOU 2122 CA ILE A 292 16290 18033 19822 -974 -80 92 C ATOM 2123 C ILE A 292 40.072 -24.325 -36.803 1.00138.19 C ANISOU 2123 C ILE A 292 15694 17524 19286 -844 80 342 C ATOM 2124 O ILE A 292 39.707 -25.064 -37.718 1.00120.74 O ANISOU 2124 O ILE A 292 13657 15327 16890 -624 113 496 O ATOM 2125 CB ILE A 292 39.062 -25.521 -34.843 1.00139.34 C ANISOU 2125 CB ILE A 292 15969 17832 19140 -864 -253 7 C ATOM 2126 CG1 ILE A 292 38.298 -25.340 -33.529 1.00140.66 C ANISOU 2126 CG1 ILE A 292 16177 17971 19295 -987 -393 -234 C ATOM 2127 CG2 ILE A 292 40.415 -26.166 -34.592 1.00142.00 C ANISOU 2127 CG2 ILE A 292 16125 18407 19423 -841 -290 26 C ATOM 2128 CD1 ILE A 292 38.111 -26.619 -32.744 1.00141.57 C ANISOU 2128 CD1 ILE A 292 16375 18269 19145 -891 -550 -321 C ATOM 2129 N ARG A 293 41.200 -23.623 -36.840 1.00153.21 N ANISOU 2129 N ARG A 293 17357 19441 21413 -978 179 380 N ATOM 2130 CA ARG A 293 42.100 -23.655 -37.987 1.00163.24 C ANISOU 2130 CA ARG A 293 18544 20750 22728 -871 363 627 C ATOM 2131 C ARG A 293 42.824 -24.994 -38.097 1.00152.51 C ANISOU 2131 C ARG A 293 17158 19658 21131 -683 306 704 C ATOM 2132 O ARG A 293 43.392 -25.321 -39.139 1.00148.47 O ANISOU 2132 O ARG A 293 16644 19201 20565 -514 446 926 O ATOM 2133 CB ARG A 293 43.115 -22.515 -37.893 1.00178.13 C ANISOU 2133 CB ARG A 293 20152 22577 24951 -1095 483 638 C ATOM 2134 CG ARG A 293 42.488 -21.130 -37.839 1.00187.52 C ANISOU 2134 CG ARG A 293 21377 23483 26389 -1279 553 574 C ATOM 2135 CD ARG A 293 43.540 -20.060 -37.598 1.00199.15 C ANISOU 2135 CD ARG A 293 22563 24897 28207 -1529 642 558 C ATOM 2136 NE ARG A 293 44.177 -20.204 -36.291 1.00207.20 N ANISOU 2136 NE ARG A 293 23376 26075 29277 -1697 449 330 N ATOM 2137 CZ ARG A 293 45.204 -19.469 -35.875 1.00213.34 C ANISOU 2137 CZ ARG A 293 23867 26851 30341 -1924 462 273 C ATOM 2138 NH1 ARG A 293 45.719 -18.538 -36.666 1.00216.44 N ANISOU 2138 NH1 ARG A 293 24141 27087 31008 -2023 678 441 N ATOM 2139 NH2 ARG A 293 45.719 -19.669 -34.670 1.00214.25 N ANISOU 2139 NH2 ARG A 293 23817 27117 30471 -2048 258 49 N ATOM 2140 N GLU A 294 42.804 -25.764 -37.015 1.00143.87 N ANISOU 2140 N GLU A 294 16054 18726 19885 -699 105 524 N ATOM 2141 CA GLU A 294 43.417 -27.085 -37.007 1.00138.36 C ANISOU 2141 CA GLU A 294 15357 18277 18938 -514 30 575 C ATOM 2142 C GLU A 294 42.510 -28.104 -37.685 1.00132.12 C ANISOU 2142 C GLU A 294 14873 17469 17856 -263 -5 671 C ATOM 2143 O GLU A 294 42.979 -29.000 -38.386 1.00129.08 O ANISOU 2143 O GLU A 294 14547 17211 17288 -45 27 827 O ATOM 2144 CB GLU A 294 43.727 -27.527 -35.576 1.00145.43 C ANISOU 2144 CB GLU A 294 16146 19344 19769 -614 -172 345 C ATOM 2145 CG GLU A 294 44.288 -28.937 -35.466 1.00154.06 C ANISOU 2145 CG GLU A 294 17265 20689 20580 -412 -267 381 C ATOM 2146 CD GLU A 294 45.659 -29.080 -36.099 1.00161.39 C ANISOU 2146 CD GLU A 294 17981 21780 21560 -332 -150 550 C ATOM 2147 OE1 GLU A 294 46.131 -30.228 -36.242 1.00157.41 O ANISOU 2147 OE1 GLU A 294 17521 21474 20816 -126 -196 620 O ATOM 2148 OE2 GLU A 294 46.267 -28.047 -36.451 1.00169.73 O ANISOU 2148 OE2 GLU A 294 18826 22765 22898 -472 -5 618 O ATOM 2149 N PHE A 295 41.206 -27.959 -37.470 1.00130.72 N ANISOU 2149 N PHE A 295 14891 17133 17644 -292 -76 575 N ATOM 2150 CA PHE A 295 40.227 -28.864 -38.058 1.00122.24 C ANISOU 2150 CA PHE A 295 14103 16019 16326 -83 -132 644 C ATOM 2151 C PHE A 295 40.150 -28.730 -39.575 1.00112.66 C ANISOU 2151 C PHE A 295 13011 14697 15099 100 25 878 C ATOM 2152 O PHE A 295 40.242 -29.722 -40.296 1.00108.20 O ANISOU 2152 O PHE A 295 12591 14210 14311 337 12 1008 O ATOM 2153 CB PHE A 295 38.842 -28.631 -37.448 1.00125.67 C ANISOU 2153 CB PHE A 295 14680 16305 16765 -176 -235 485 C ATOM 2154 CG PHE A 295 38.531 -29.528 -36.282 1.00128.50 C ANISOU 2154 CG PHE A 295 15083 16789 16951 -195 -420 316 C ATOM 2155 CD1 PHE A 295 38.111 -30.831 -36.488 1.00125.91 C ANISOU 2155 CD1 PHE A 295 14950 16532 16357 -9 -519 361 C ATOM 2156 CD2 PHE A 295 38.649 -29.067 -34.983 1.00128.60 C ANISOU 2156 CD2 PHE A 295 14960 16839 17064 -392 -495 113 C ATOM 2157 CE1 PHE A 295 37.822 -31.659 -35.419 1.00119.91 C ANISOU 2157 CE1 PHE A 295 14242 15875 15441 -26 -671 220 C ATOM 2158 CE2 PHE A 295 38.360 -29.890 -33.910 1.00123.56 C ANISOU 2158 CE2 PHE A 295 14380 16314 16254 -391 -650 -32 C ATOM 2159 CZ PHE A 295 37.946 -31.186 -34.130 1.00118.13 C ANISOU 2159 CZ PHE A 295 13882 15693 15308 -211 -729 28 C ATOM 2160 N ARG A 296 39.981 -27.501 -40.054 1.00108.89 N ANISOU 2160 N ARG A 296 12491 14032 14850 4 172 931 N ATOM 2161 CA ARG A 296 39.797 -27.262 -41.481 1.00112.25 C ANISOU 2161 CA ARG A 296 13058 14330 15264 185 329 1148 C ATOM 2162 C ARG A 296 40.957 -27.792 -42.318 1.00125.27 C ANISOU 2162 C ARG A 296 14650 16125 16822 372 449 1358 C ATOM 2163 O ARG A 296 40.758 -28.272 -43.434 1.00126.60 O ANISOU 2163 O ARG A 296 15015 16264 16824 626 504 1528 O ATOM 2164 CB ARG A 296 39.564 -25.774 -41.764 1.00106.81 C ANISOU 2164 CB ARG A 296 12313 13417 14854 35 483 1170 C ATOM 2165 CG ARG A 296 40.700 -24.858 -41.349 1.00109.75 C ANISOU 2165 CG ARG A 296 12388 13813 15499 -185 601 1161 C ATOM 2166 CD ARG A 296 40.389 -23.414 -41.713 1.00121.94 C ANISOU 2166 CD ARG A 296 13919 15104 17308 -318 758 1196 C ATOM 2167 NE ARG A 296 41.532 -22.534 -41.494 1.00147.05 N ANISOU 2167 NE ARG A 296 16817 18286 20771 -522 890 1220 N ATOM 2168 CZ ARG A 296 41.546 -21.238 -41.790 1.00161.78 C ANISOU 2168 CZ ARG A 296 18630 19936 22903 -664 1050 1268 C ATOM 2169 NH1 ARG A 296 42.633 -20.515 -41.557 1.00168.54 N ANISOU 2169 NH1 ARG A 296 19214 20797 24027 -864 1157 1287 N ATOM 2170 NH2 ARG A 296 40.474 -20.666 -42.320 1.00163.13 N ANISOU 2170 NH2 ARG A 296 19020 19883 23079 -606 1100 1295 N ATOM 2171 N GLN A 297 42.167 -27.706 -41.777 1.00134.60 N ANISOU 2171 N GLN A 297 15562 17469 18111 257 486 1342 N ATOM 2172 CA GLN A 297 43.346 -28.204 -42.474 1.00142.26 C ANISOU 2172 CA GLN A 297 16440 18606 19008 430 608 1538 C ATOM 2173 C GLN A 297 43.374 -29.728 -42.464 1.00142.46 C ANISOU 2173 C GLN A 297 16618 18814 18694 664 459 1544 C ATOM 2174 O GLN A 297 43.981 -30.353 -43.334 1.00146.58 O ANISOU 2174 O GLN A 297 17194 19438 19062 907 546 1732 O ATOM 2175 CB GLN A 297 44.619 -27.643 -41.843 1.00154.50 C ANISOU 2175 CB GLN A 297 17627 20281 20796 224 676 1507 C ATOM 2176 CG GLN A 297 44.696 -26.129 -41.864 1.00170.09 C ANISOU 2176 CG GLN A 297 19441 22061 23123 -20 827 1508 C ATOM 2177 CD GLN A 297 45.986 -25.602 -41.268 1.00188.37 C ANISOU 2177 CD GLN A 297 21385 24496 25693 -232 879 1476 C ATOM 2178 OE1 GLN A 297 46.925 -26.360 -41.018 1.00192.08 O ANISOU 2178 OE1 GLN A 297 21701 25208 26071 -162 836 1492 O ATOM 2179 NE2 GLN A 297 46.040 -24.294 -41.039 1.00195.53 N ANISOU 2179 NE2 GLN A 297 22143 25227 26925 -490 965 1426 N ATOM 2180 N THR A 298 42.710 -30.319 -41.476 1.00138.77 N ANISOU 2180 N THR A 298 16233 18383 18110 597 242 1341 N ATOM 2181 CA THR A 298 42.617 -31.769 -41.379 1.00135.42 C ANISOU 2181 CA THR A 298 15980 18103 17369 799 87 1330 C ATOM 2182 C THR A 298 41.650 -32.306 -42.428 1.00138.93 C ANISOU 2182 C THR A 298 16755 18414 17618 1035 65 1438 C ATOM 2183 O THR A 298 41.959 -33.263 -43.139 1.00136.47 O ANISOU 2183 O THR A 298 16589 18190 17074 1297 59 1569 O ATOM 2184 CB THR A 298 42.148 -32.218 -39.982 1.00127.52 C ANISOU 2184 CB THR A 298 14980 17164 16309 653 -126 1088 C ATOM 2185 OG1 THR A 298 42.992 -31.636 -38.981 1.00129.73 O ANISOU 2185 OG1 THR A 298 14963 17553 16776 434 -128 965 O ATOM 2186 CG2 THR A 298 42.202 -33.732 -39.865 1.00122.17 C ANISOU 2186 CG2 THR A 298 14469 16640 15311 860 -271 1090 C ATOM 2187 N PHE A 299 40.479 -31.683 -42.521 1.00147.83 N ANISOU 2187 N PHE A 299 18002 19327 18839 949 45 1377 N ATOM 2188 CA PHE A 299 39.479 -32.078 -43.506 1.00154.90 C ANISOU 2188 CA PHE A 299 19198 20078 19580 1157 7 1460 C ATOM 2189 C PHE A 299 40.013 -31.875 -44.919 1.00154.99 C ANISOU 2189 C PHE A 299 19276 20055 19559 1385 194 1704 C ATOM 2190 O PHE A 299 39.948 -32.776 -45.757 1.00156.99 O ANISOU 2190 O PHE A 299 19750 20331 19570 1662 156 1819 O ATOM 2191 CB PHE A 299 38.190 -31.271 -43.328 1.00159.99 C ANISOU 2191 CB PHE A 299 19913 20506 20370 1010 -30 1350 C ATOM 2192 CG PHE A 299 37.609 -31.340 -41.943 1.00161.64 C ANISOU 2192 CG PHE A 299 20057 20735 20625 789 -185 1120 C ATOM 2193 CD1 PHE A 299 37.205 -32.552 -41.405 1.00161.67 C ANISOU 2193 CD1 PHE A 299 20184 20827 20417 847 -371 1032 C ATOM 2194 CD2 PHE A 299 37.445 -30.190 -41.189 1.00161.32 C ANISOU 2194 CD2 PHE A 299 19848 20614 20833 533 -140 995 C ATOM 2195 CE1 PHE A 299 36.665 -32.619 -40.135 1.00160.32 C ANISOU 2195 CE1 PHE A 299 19963 20673 20279 660 -494 835 C ATOM 2196 CE2 PHE A 299 36.904 -30.250 -39.918 1.00159.75 C ANISOU 2196 CE2 PHE A 299 19606 20435 20658 355 -274 787 C ATOM 2197 CZ PHE A 299 36.514 -31.467 -39.392 1.00159.66 C ANISOU 2197 CZ PHE A 299 19712 20521 20431 422 -443 713 C ATOM 2198 N ARG A 300 40.539 -30.680 -45.172 1.00150.74 N ANISOU 2198 N ARG A 300 18556 19452 19265 1271 399 1785 N ATOM 2199 CA ARG A 300 41.066 -30.312 -46.481 1.00151.18 C ANISOU 2199 CA ARG A 300 18657 19461 19325 1469 619 2030 C ATOM 2200 C ARG A 300 41.988 -31.391 -47.040 1.00151.88 C ANISOU 2200 C ARG A 300 18792 19743 19172 1742 645 2183 C ATOM 2201 O ARG A 300 42.007 -31.643 -48.244 1.00149.29 O ANISOU 2201 O ARG A 300 18659 19371 18691 2026 737 2371 O ATOM 2202 CB ARG A 300 41.809 -28.978 -46.384 1.00158.20 C ANISOU 2202 CB ARG A 300 19269 20304 20537 1256 839 2084 C ATOM 2203 CG ARG A 300 42.340 -28.443 -47.702 1.00170.24 C ANISOU 2203 CG ARG A 300 20824 21757 22102 1437 1105 2352 C ATOM 2204 CD ARG A 300 42.972 -27.073 -47.501 1.00185.34 C ANISOU 2204 CD ARG A 300 22458 23592 24370 1180 1313 2388 C ATOM 2205 NE ARG A 300 43.551 -26.540 -48.730 1.00201.62 N ANISOU 2205 NE ARG A 300 24533 25587 26486 1344 1597 2663 N ATOM 2206 CZ ARG A 300 44.151 -25.356 -48.819 1.00213.41 C ANISOU 2206 CZ ARG A 300 25811 26989 28285 1162 1823 2753 C ATOM 2207 NH1 ARG A 300 44.250 -24.581 -47.748 1.00216.79 N ANISOU 2207 NH1 ARG A 300 26001 27379 28990 810 1777 2574 N ATOM 2208 NH2 ARG A 300 44.653 -24.947 -49.977 1.00218.00 N ANISOU 2208 NH2 ARG A 300 26426 27509 28895 1336 2097 3023 N ATOM 2209 N LYS A 301 42.745 -32.028 -46.153 1.00156.56 N ANISOU 2209 N LYS A 301 19216 20551 19720 1671 560 2097 N ATOM 2210 CA LYS A 301 43.677 -33.077 -46.546 1.00159.28 C ANISOU 2210 CA LYS A 301 19585 21101 19834 1925 575 2226 C ATOM 2211 C LYS A 301 42.961 -34.388 -46.862 1.00163.03 C ANISOU 2211 C LYS A 301 20400 21573 19971 2176 376 2205 C ATOM 2212 O LYS A 301 43.257 -35.040 -47.864 1.00163.37 O ANISOU 2212 O LYS A 301 20625 21652 19794 2490 424 2375 O ATOM 2213 CB LYS A 301 44.717 -33.293 -45.447 1.00156.65 C ANISOU 2213 CB LYS A 301 18953 21000 19568 1768 538 2129 C ATOM 2214 CG LYS A 301 45.497 -34.590 -45.564 1.00157.15 C ANISOU 2214 CG LYS A 301 19067 21291 19350 2022 482 2200 C ATOM 2215 CD LYS A 301 45.273 -35.455 -44.337 1.00156.72 C ANISOU 2215 CD LYS A 301 19029 21349 19169 1932 233 1983 C ATOM 2216 CE LYS A 301 45.546 -34.669 -43.064 1.00157.54 C ANISOU 2216 CE LYS A 301 18820 21498 19539 1586 203 1798 C ATOM 2217 NZ LYS A 301 45.090 -35.398 -41.849 1.00157.20 N ANISOU 2217 NZ LYS A 301 18836 21520 19374 1493 -37 1576 N ATOM 2218 N ILE A 302 42.021 -34.769 -46.002 1.00164.50 N ANISOU 2218 N ILE A 302 20675 21709 20120 2039 155 1999 N ATOM 2219 CA ILE A 302 41.271 -36.008 -46.183 1.00162.17 C ANISOU 2219 CA ILE A 302 20689 21391 19539 2231 -52 1959 C ATOM 2220 C ILE A 302 40.541 -36.028 -47.522 1.00162.21 C ANISOU 2220 C ILE A 302 20986 21215 19431 2475 -34 2088 C ATOM 2221 O ILE A 302 40.573 -37.026 -48.244 1.00160.43 O ANISOU 2221 O ILE A 302 21004 21016 18938 2766 -105 2177 O ATOM 2222 CB ILE A 302 40.241 -36.216 -45.056 1.00156.93 C ANISOU 2222 CB ILE A 302 20054 20665 18906 2010 -262 1726 C ATOM 2223 CG1 ILE A 302 40.931 -36.219 -43.691 1.00153.78 C ANISOU 2223 CG1 ILE A 302 19393 20443 18593 1790 -296 1585 C ATOM 2224 CG2 ILE A 302 39.474 -37.511 -45.270 1.00156.49 C ANISOU 2224 CG2 ILE A 302 20311 20571 18576 2194 -471 1695 C ATOM 2225 CD1 ILE A 302 39.981 -36.420 -42.531 1.00148.36 C ANISOU 2225 CD1 ILE A 302 18735 19708 17928 1588 -479 1367 C ATOM 2226 N ILE A 303 39.882 -34.920 -47.845 1.00164.45 N ANISOU 2226 N ILE A 303 21257 21311 19913 2366 52 2091 N ATOM 2227 CA ILE A 303 39.118 -34.811 -49.083 1.00166.92 C ANISOU 2227 CA ILE A 303 21844 21440 20137 2591 63 2198 C ATOM 2228 C ILE A 303 40.010 -34.992 -50.308 1.00172.03 C ANISOU 2228 C ILE A 303 22584 22144 20634 2914 237 2443 C ATOM 2229 O ILE A 303 39.716 -35.802 -51.188 1.00171.01 O ANISOU 2229 O ILE A 303 22751 21978 20248 3217 149 2520 O ATOM 2230 CB ILE A 303 38.393 -33.453 -49.181 1.00161.52 C ANISOU 2230 CB ILE A 303 21100 20558 19712 2416 157 2170 C ATOM 2231 CG1 ILE A 303 37.461 -33.257 -47.982 1.00150.60 C ANISOU 2231 CG1 ILE A 303 19635 19118 18468 2119 -7 1932 C ATOM 2232 CG2 ILE A 303 37.616 -33.356 -50.485 1.00160.31 C ANISOU 2232 CG2 ILE A 303 21240 20221 19450 2676 159 2279 C ATOM 2233 CD1 ILE A 303 36.746 -31.925 -47.977 1.00143.22 C ANISOU 2233 CD1 ILE A 303 18639 17995 17784 1945 78 1889 C ATOM 2234 N ARG A 304 41.098 -34.232 -50.357 1.00176.11 N ANISOU 2234 N ARG A 304 22849 22749 21316 2850 484 2566 N ATOM 2235 CA ARG A 304 42.038 -34.308 -51.471 1.00181.14 C ANISOU 2235 CA ARG A 304 23533 23455 21837 3145 695 2819 C ATOM 2236 C ARG A 304 42.583 -35.722 -51.640 1.00180.93 C ANISOU 2236 C ARG A 304 23648 23605 21491 3416 589 2864 C ATOM 2237 O ARG A 304 42.664 -36.239 -52.755 1.00180.49 O ANISOU 2237 O ARG A 304 23849 23532 21198 3769 623 3023 O ATOM 2238 CB ARG A 304 43.189 -33.320 -51.272 1.00188.05 C ANISOU 2238 CB ARG A 304 24052 24420 22979 2976 969 2925 C ATOM 2239 CG ARG A 304 42.767 -31.862 -51.332 1.00196.93 C ANISOU 2239 CG ARG A 304 25070 25346 24408 2756 1116 2926 C ATOM 2240 CD ARG A 304 43.959 -30.936 -51.159 1.00207.84 C ANISOU 2240 CD ARG A 304 26098 26808 26065 2584 1382 3038 C ATOM 2241 NE ARG A 304 43.606 -29.542 -51.408 1.00216.13 N ANISOU 2241 NE ARG A 304 27088 27642 27388 2418 1551 3076 N ATOM 2242 CZ ARG A 304 44.467 -28.531 -51.356 1.00221.80 C ANISOU 2242 CZ ARG A 304 27521 28360 28392 2241 1796 3179 C ATOM 2243 NH1 ARG A 304 44.055 -27.294 -51.601 1.00224.94 N ANISOU 2243 NH1 ARG A 304 27907 28537 29024 2102 1937 3209 N ATOM 2244 NH2 ARG A 304 45.741 -28.755 -51.061 1.00222.46 N ANISOU 2244 NH2 ARG A 304 27329 28660 28536 2204 1897 3250 N ATOM 2245 N SER A 305 42.955 -36.343 -50.526 1.00181.58 N ANISOU 2245 N SER A 305 23579 23856 21559 3264 458 2723 N ATOM 2246 CA SER A 305 43.481 -37.702 -50.544 1.00183.09 C ANISOU 2246 CA SER A 305 23897 24218 21450 3503 346 2748 C ATOM 2247 C SER A 305 42.410 -38.712 -50.148 1.00179.79 C ANISOU 2247 C SER A 305 23744 23721 20846 3515 37 2571 C ATOM 2248 O SER A 305 41.595 -39.124 -50.973 1.00177.94 O ANISOU 2248 O SER A 305 23830 23335 20444 3723 -70 2598 O ATOM 2249 CB SER A 305 44.687 -37.820 -49.610 1.00186.65 C ANISOU 2249 CB SER A 305 24018 24921 21980 3367 404 2721 C ATOM 2250 OG SER A 305 45.216 -39.135 -49.623 1.00188.52 O ANISOU 2250 OG SER A 305 24386 25327 21916 3614 299 2748 O TER 2251 SER A 305 HETATM 2252 N1 CFF A 330 9.174 -33.156 -31.881 1.00147.73 N HETATM 2253 C2 CFF A 330 9.511 -33.973 -32.948 1.00148.15 C HETATM 2254 C10 CFF A 330 10.180 -32.790 -30.862 1.00138.32 C HETATM 2255 C6 CFF A 330 7.880 -32.698 -31.748 1.00147.40 C HETATM 2256 N3 CFF A 330 8.560 -34.329 -33.882 1.00149.30 N HETATM 2257 O11 CFF A 330 10.781 -34.432 -33.079 1.00142.40 O HETATM 2258 C12 CFF A 330 8.923 -35.204 -35.004 1.00147.42 C HETATM 2259 C4 CFF A 330 7.287 -33.864 -33.735 1.00146.85 C HETATM 2260 C5 CFF A 330 6.925 -33.068 -32.699 1.00145.81 C HETATM 2261 N9 CFF A 330 6.240 -34.112 -34.550 1.00147.23 N HETATM 2262 O13 CFF A 330 7.552 -31.908 -30.705 1.00147.52 O HETATM 2263 N7 CFF A 330 5.617 -32.775 -32.828 1.00147.22 N HETATM 2264 C8 CFF A 330 5.235 -33.422 -33.954 1.00148.06 C HETATM 2265 C14 CFF A 330 4.727 -31.975 -31.994 1.00145.92 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 2253 2254 2255 CONECT 2253 2252 2256 2257 CONECT 2254 2252 CONECT 2255 2252 2260 2262 CONECT 2256 2253 2258 2259 CONECT 2257 2253 CONECT 2258 2256 CONECT 2259 2256 2260 2261 CONECT 2260 2255 2259 2263 CONECT 2261 2259 2264 CONECT 2262 2255 CONECT 2263 2260 2264 2265 CONECT 2264 2261 2263 CONECT 2265 2263 MASTER 306 0 1 17 2 0 2 6 2264 1 22 26 END