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*** HYDROLASE 11-APR-14 4Q3J ***elNémo ID: 2502181839412293432Job options:ID = 2502181839412293432 JOBID = HYDROLASE 11-APR-14 4Q3J USERID = unknown PRIVAT = 0 NMODES = 5 DQMIN = -100 DQMAX = 100 DQSTEP = 20 DOGRAPHS = on DOPROJMODS = 0 DORMSD = 0 NRBL = 0 CUTOFF = 0 CAONLY = 0 Input data for this run:HEADER HYDROLASE 11-APR-14 4Q3J TITLE CRYSTAL STRUCTURE OF NFKB-P65-DEGRADING ZINC PROTEASE FAMILY PROTEIN COMPND MOL_ID: 1; COMPND 2 MOLECULE: NFKB-P65-DEGRADING ZINC PROTEASE FAMILY PROTEIN; COMPND 3 CHAIN: A; COMPND 4 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI; SOURCE 3 ORGANISM_TAXID: 386585; SOURCE 4 STRAIN: SAKAI; SOURCE 5 GENE: S1M_1031; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562 KEYWDS HYDROLASE, ALPHA BETA, CYTOSOL EXPDTA X-RAY DIFFRACTION AUTHOR M.C.SOUSA,M.M.TURCO REVDAT 3 28-FEB-24 4Q3J 1 REMARK SEQADV LINK REVDAT 2 03-SEP-14 4Q3J 1 JRNL REVDAT 1 30-JUL-14 4Q3J 0 JRNL AUTH M.M.TURCO,M.C.SOUSA JRNL TITL THE STRUCTURE AND SPECIFICITY OF THE TYPE III SECRETION JRNL TITL 2 SYSTEM EFFECTOR NLEC SUGGEST A DNA MIMICRY MECHANISM OF JRNL TITL 3 SUBSTRATE RECOGNITION. JRNL REF BIOCHEMISTRY V. 53 5131 2014 JRNL REFN ISSN 0006-2960 JRNL PMID 25040221 JRNL DOI 10.1021/BI500593E REMARK 2 REMARK 2 RESOLUTION. 1.86 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.7.1_743) REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE, REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER, REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY, REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON, REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI, REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART REMARK 3 REMARK 3 REFINEMENT TARGET : MLHL REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.86 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 34.94 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.000 REMARK 3 COMPLETENESS FOR RANGE (%) : 92.0 REMARK 3 NUMBER OF REFLECTIONS : 19840 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.183 REMARK 3 R VALUE (WORKING SET) : 0.180 REMARK 3 FREE R VALUE : 0.218 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 9.600 REMARK 3 FREE R VALUE TEST SET COUNT : 1905 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 34.9480 - 4.4845 0.88 1333 142 0.1634 0.1495 REMARK 3 2 4.4845 - 3.5606 0.92 1317 141 0.1473 0.1902 REMARK 3 3 3.5606 - 3.1108 0.94 1323 142 0.1670 0.2224 REMARK 3 4 3.1108 - 2.8265 0.95 1309 141 0.1740 0.2058 REMARK 3 5 2.8265 - 2.6240 0.96 1346 141 0.1688 0.1935 REMARK 3 6 2.6240 - 2.4694 0.96 1342 144 0.1654 0.2019 REMARK 3 7 2.4694 - 2.3457 0.96 1328 141 0.1813 0.2529 REMARK 3 8 2.3457 - 2.2436 0.94 1295 137 0.1836 0.2509 REMARK 3 9 2.2436 - 2.1573 0.93 1275 135 0.2107 0.2717 REMARK 3 10 2.1573 - 2.0828 0.96 1316 143 0.1856 0.2334 REMARK 3 11 2.0828 - 2.0177 0.92 1273 137 0.2208 0.2832 REMARK 3 12 2.0177 - 1.9600 0.92 1254 133 0.2149 0.2749 REMARK 3 13 1.9600 - 1.9085 0.85 1173 119 0.2540 0.3128 REMARK 3 14 1.9085 - 1.8619 0.77 1051 109 0.3201 0.4117 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL REMARK 3 SOLVENT RADIUS : 1.10 REMARK 3 SHRINKAGE RADIUS : 0.83 REMARK 3 K_SOL : 0.36 REMARK 3 B_SOL : 30.62 REMARK 3 REMARK 3 ERROR ESTIMATES. REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.450 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 22.180 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : -0.90420 REMARK 3 B22 (A**2) : -5.65210 REMARK 3 B33 (A**2) : 6.55630 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 : 0.014 2116 REMARK 3 ANGLE : 0.993 2877 REMARK 3 CHIRALITY : 0.070 307 REMARK 3 PLANARITY : 0.003 388 REMARK 3 DIHEDRAL : 13.103 786 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 1 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: ALL REMARK 3 ORIGIN FOR THE GROUP (A): 8.0022 28.7335 51.6032 REMARK 3 T TENSOR REMARK 3 T11: 0.0758 T22: 0.1292 REMARK 3 T33: 0.0970 T12: -0.0121 REMARK 3 T13: -0.0077 T23: 0.0055 REMARK 3 L TENSOR REMARK 3 L11: 1.1147 L22: 2.1839 REMARK 3 L33: 1.1421 L12: -0.3549 REMARK 3 L13: -0.3603 L23: 0.7131 REMARK 3 S TENSOR REMARK 3 S11: 0.0165 S12: -0.0449 S13: -0.0019 REMARK 3 S21: 0.0744 S22: 0.0148 S23: -0.1152 REMARK 3 S31: -0.0148 S32: 0.0745 S33: -0.0032 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 4Q3J COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-APR-14. REMARK 100 THE DEPOSITION ID IS D_1000085558. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 06-OCT-11 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 6.0 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : ALS REMARK 200 BEAMLINE : 8.2.1 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.2574,1.2831,1.2835 REMARK 200 MONOCHROMATOR : CRYSTAL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4 REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000 REMARK 200 DATA SCALING SOFTWARE : HKL-2000 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 19840 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.862 REMARK 200 RESOLUTION RANGE LOW (A) : 50.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 96.4 REMARK 200 DATA REDUNDANCY : NULL REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : NULL REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL REMARK 200 COMPLETENESS FOR SHELL (%) : NULL REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : NULL REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: MAD REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD REMARK 200 SOFTWARE USED: PHENIX 1.7.1_743 REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 26.18 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.67 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 10% PEG-3350, 50 MM MG(CHO2)2, 0.1 M REMARK 280 MES PH 6.0, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 289K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X+1/2,-Y,Z+1/2 REMARK 290 3555 -X,Y+1/2,-Z+1/2 REMARK 290 4555 X+1/2,-Y+1/2,-Z REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 22.60250 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 40.84400 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 33.74000 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 40.84400 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 22.60250 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 33.74000 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 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 LYS A 2 REMARK 465 ILE A 3 REMARK 465 PRO A 4 REMARK 465 SER A 5 REMARK 465 LEU A 6 REMARK 465 GLN A 7 REMARK 465 SER A 8 REMARK 465 ASN A 9 REMARK 465 PHE A 10 REMARK 465 ASN A 11 REMARK 465 PHE A 12 REMARK 465 SER A 13 REMARK 465 ALA A 14 REMARK 465 PRO A 15 REMARK 465 ALA A 16 REMARK 465 GLY A 17 REMARK 465 TYR A 18 REMARK 465 SER A 19 REMARK 465 ALA A 20 REMARK 465 PRO A 21 REMARK 465 VAL A 281 REMARK 465 SER A 282 REMARK 465 ASN A 283 REMARK 465 ILE A 284 REMARK 465 GLY A 285 REMARK 465 TYR A 286 REMARK 465 GLY A 287 REMARK 465 PHE A 288 REMARK 465 ILE A 289 REMARK 465 GLN A 290 REMARK 465 GLN A 291 REMARK 465 HIS A 292 REMARK 465 ASP A 293 REMARK 465 PHE A 294 REMARK 465 PRO A 295 REMARK 465 GLY A 296 REMARK 465 LEU A 297 REMARK 465 ALA A 298 REMARK 465 ILE A 299 REMARK 465 ASN A 300 REMARK 465 ASP A 301 REMARK 465 ASN A 302 REMARK 465 LEU A 303 REMARK 465 GLN A 304 REMARK 465 ASP A 305 REMARK 465 ALA A 306 REMARK 465 ASN A 307 REMARK 465 GLN A 308 REMARK 465 ILE A 309 REMARK 465 GLN A 310 REMARK 465 LEU A 311 REMARK 465 TYR A 312 REMARK 465 HIS A 313 REMARK 465 GLY A 314 REMARK 465 ALA A 315 REMARK 465 PRO A 316 REMARK 465 TYR A 317 REMARK 465 ILE A 318 REMARK 465 PHE A 319 REMARK 465 THR A 320 REMARK 465 PHE A 321 REMARK 465 GLY A 322 REMARK 465 ASP A 323 REMARK 465 VAL A 324 REMARK 465 ASP A 325 REMARK 465 LYS A 326 REMARK 465 HIS A 327 REMARK 465 ASN A 328 REMARK 465 GLN A 329 REMARK 465 GLN A 330 REMARK 465 PRO A 331 REMARK 465 GLY A 332 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT REMARK 500 REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT. REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE REMARK 500 O HOH A 525 O HOH A 604 1.93 REMARK 500 O HOH A 590 O HOH A 664 2.05 REMARK 500 O HOH A 641 O HOH A 642 2.07 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS REMARK 500 REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15 REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375 REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS. REMARK 500 REMARK 500 DISTANCE CUTOFF: REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE REMARK 500 O HOH A 502 O HOH A 532 4456 1.93 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 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 LYS A 102 -153.20 -105.47 REMARK 500 ASN A 112 68.48 -115.15 REMARK 500 REMARK 500 REMARK: NULL REMARK 620 REMARK 620 METAL COORDINATION REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE): REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 ZN A 401 ZN REMARK 620 N RES CSSEQI ATOM REMARK 620 1 HIS A 183 NE2 REMARK 620 2 HIS A 187 NE2 94.9 REMARK 620 3 ASP A 194 OD2 138.9 104.8 REMARK 620 4 ASP A 194 OD1 86.3 92.2 57.7 REMARK 620 5 TYR A 227 OH 79.6 174.4 78.8 86.0 REMARK 620 6 HOH A 529 O 110.2 92.8 104.5 162.2 90.5 REMARK 620 N 1 2 3 4 5 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 MG A 402 MG REMARK 620 N RES CSSEQI ATOM REMARK 620 1 HOH A 625 O REMARK 620 2 HOH A 626 O 112.2 REMARK 620 3 HOH A 628 O 69.0 70.2 REMARK 620 4 HOH A 629 O 71.6 64.2 99.0 REMARK 620 N 1 2 3 REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 401 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 402 DBREF 4Q3J A 1 330 UNP U1C6A4 U1C6A4_ECOLX 1 330 SEQADV 4Q3J PRO A 331 UNP U1C6A4 EXPRESSION TAG SEQADV 4Q3J GLY A 332 UNP U1C6A4 EXPRESSION TAG SEQRES 1 A 332 MET LYS ILE PRO SER LEU GLN SER ASN PHE ASN PHE SER SEQRES 2 A 332 ALA PRO ALA GLY TYR SER ALA PRO ILE ALA PRO ASN ARG SEQRES 3 A 332 ALA GLU ASN ALA TYR ALA ASP TYR VAL LEU ASP ILE GLY SEQRES 4 A 332 LYS ARG ILE PRO LEU SER ALA ALA ASP LEU SER ASN VAL SEQRES 5 A 332 TYR GLU SER VAL ILE ARG ALA VAL HIS ASP SER ARG SER SEQRES 6 A 332 ARG LEU ILE ASP GLN HIS THR VAL ASP MET ILE GLY ASN SEQRES 7 A 332 THR VAL LEU ASP ALA LEU SER ARG SER GLN THR PHE ARG SEQRES 8 A 332 ASP ALA VAL SER TYR GLY ILE HIS ASN GLU LYS VAL HIS SEQRES 9 A 332 ILE GLY CYS ILE LYS TYR ARG ASN GLU TYR GLU LEU ASN SEQRES 10 A 332 GLU GLU SER SER VAL LYS ILE ASP ASP ILE GLN SER LEU SEQRES 11 A 332 THR CYS ASN GLU LEU TYR GLU TYR ASP VAL GLY GLN GLU SEQRES 12 A 332 PRO ILE PHE PRO ILE CYS GLU ALA GLY GLU ASN ASP ASN SEQRES 13 A 332 GLU GLU PRO TYR VAL SER PHE SER VAL ALA PRO ASP THR SEQRES 14 A 332 ASP SER TYR GLU MET PRO SER TRP GLN GLU GLY LEU ILE SEQRES 15 A 332 HIS GLU ILE ILE HIS HIS VAL THR GLY SER SER ASP PRO SEQRES 16 A 332 SER GLY ASP SER ASN ILE GLU LEU GLY PRO THR GLU ILE SEQRES 17 A 332 LEU ALA ARG ARG VAL ALA GLN GLU LEU GLY TRP SER VAL SEQRES 18 A 332 PRO ASP PHE LYS GLY TYR ALA GLU PRO GLU ARG GLU ALA SEQRES 19 A 332 HIS LEU ARG LEU ARG ASN LEU ASN ALA LEU ARG GLN ALA SEQRES 20 A 332 ALA MET ARG HIS GLU GLU ASN GLU ARG ALA PHE PHE GLU SEQRES 21 A 332 ARG LEU GLY THR ILE SER ASP ARG TYR GLU ALA SER PRO SEQRES 22 A 332 ASP PHE THR GLU TYR SER ALA VAL SER ASN ILE GLY TYR SEQRES 23 A 332 GLY PHE ILE GLN GLN HIS ASP PHE PRO GLY LEU ALA ILE SEQRES 24 A 332 ASN ASP ASN LEU GLN ASP ALA ASN GLN ILE GLN LEU TYR SEQRES 25 A 332 HIS GLY ALA PRO TYR ILE PHE THR PHE GLY ASP VAL ASP SEQRES 26 A 332 LYS HIS ASN GLN GLN PRO GLY HET ZN A 401 1 HET MG A 402 1 HETNAM ZN ZINC ION HETNAM MG MAGNESIUM ION FORMUL 2 ZN ZN 2+ FORMUL 3 MG MG 2+ FORMUL 4 HOH *186(H2 O) HELIX 1 1 ASN A 29 LYS A 40 1 12 HELIX 2 2 SER A 45 ASP A 62 1 18 HELIX 3 3 SER A 63 LEU A 67 5 5 HELIX 4 4 ASP A 69 SER A 87 1 19 HELIX 5 5 SER A 87 ASN A 100 1 14 HELIX 6 6 HIS A 104 ILE A 108 5 5 HELIX 7 7 ASP A 126 LEU A 130 5 5 HELIX 8 8 THR A 131 GLU A 137 1 7 HELIX 9 9 GLU A 173 GLY A 191 1 19 HELIX 10 10 GLY A 204 GLY A 218 1 15 HELIX 11 11 GLU A 229 HIS A 251 1 23 HELIX 12 12 ASN A 254 ASP A 267 1 14 HELIX 13 13 PHE A 275 SER A 279 5 5 SHEET 1 A 3 LYS A 109 ARG A 111 0 SHEET 2 A 3 PRO A 159 SER A 162 1 O VAL A 161 N ARG A 111 SHEET 3 A 3 GLU A 150 GLU A 153 -1 N GLY A 152 O TYR A 160 SHEET 1 B 2 TYR A 114 LEU A 116 0 SHEET 2 B 2 ILE A 145 PRO A 147 -1 O PHE A 146 N GLU A 115 LINK NE2 HIS A 183 ZN ZN A 401 1555 1555 2.02 LINK NE2 HIS A 187 ZN ZN A 401 1555 1555 2.12 LINK OD2 ASP A 194 ZN ZN A 401 1555 1555 2.05 LINK OD1 ASP A 194 ZN ZN A 401 1555 1555 2.36 LINK OH TYR A 227 ZN ZN A 401 1555 1555 2.29 LINK ZN ZN A 401 O HOH A 529 1555 1555 2.36 LINK MG MG A 402 O HOH A 625 1555 1555 2.57 LINK MG MG A 402 O HOH A 626 1555 1555 2.55 LINK MG MG A 402 O HOH A 628 1555 1555 2.58 LINK MG MG A 402 O HOH A 629 1555 1555 2.72 SITE 1 AC1 5 HIS A 183 HIS A 187 ASP A 194 TYR A 227 SITE 2 AC1 5 HOH A 529 SITE 1 AC2 4 HOH A 625 HOH A 626 HOH A 628 HOH A 629 CRYST1 45.205 67.480 81.688 90.00 90.00 90.00 P 21 21 21 4 ORIGX1 1.000000 0.000000 0.000000 0.00000 ORIGX2 0.000000 1.000000 0.000000 0.00000 ORIGX3 0.000000 0.000000 1.000000 0.00000 SCALE1 0.022121 0.000000 0.000000 0.00000 SCALE2 0.000000 0.014819 0.000000 0.00000 SCALE3 0.000000 0.000000 0.012242 0.00000 ATOM 1 N ILE A 22 9.061 59.334 58.589 1.00 43.58 N ANISOU 1 N ILE A 22 6035 4017 6508 -759 800 -911 N ATOM 2 CA ILE A 22 10.048 58.334 58.992 1.00 52.79 C ANISOU 2 CA ILE A 22 7086 5313 7660 -828 716 -974 C ATOM 3 C ILE A 22 9.415 56.968 59.272 1.00 56.29 C ANISOU 3 C ILE A 22 7513 5878 7997 -778 637 -962 C ATOM 4 O ILE A 22 8.578 56.828 60.167 1.00 62.83 O ANISOU 4 O ILE A 22 8369 6757 8747 -721 586 -1007 O ATOM 5 CB ILE A 22 10.855 58.783 60.231 1.00 52.28 C ANISOU 5 CB ILE A 22 6955 5285 7624 -897 646 -1126 C ATOM 6 CG1 ILE A 22 11.677 60.034 59.914 1.00 53.96 C ANISOU 6 CG1 ILE A 22 7162 5383 7958 -965 728 -1149 C ATOM 7 CG2 ILE A 22 11.773 57.667 60.701 1.00 52.41 C ANISOU 7 CG2 ILE A 22 6857 5446 7610 -939 535 -1186 C ATOM 8 CD1 ILE A 22 12.598 60.457 61.039 1.00 55.96 C ANISOU 8 CD1 ILE A 22 7339 5669 8253 -1037 655 -1301 C ATOM 9 N ALA A 23 9.830 55.966 58.502 1.00 46.71 N ANISOU 9 N ALA A 23 6247 4737 6762 -783 623 -884 N ATOM 10 CA ALA A 23 9.333 54.605 58.654 1.00 42.75 C ANISOU 10 CA ALA A 23 5710 4400 6133 -709 530 -827 C ATOM 11 C ALA A 23 9.889 53.945 59.911 1.00 36.49 C ANISOU 11 C ALA A 23 4843 3730 5292 -743 412 -943 C ATOM 12 O ALA A 23 10.977 54.288 60.366 1.00 31.33 O ANISOU 12 O ALA A 23 4130 3057 4715 -834 388 -1057 O ATOM 13 CB ALA A 23 9.703 53.784 57.435 1.00 47.53 C ANISOU 13 CB ALA A 23 6283 5044 6733 -703 550 -712 C ATOM 14 N PRO A 24 9.134 53.000 60.486 1.00 29.45 N ANISOU 14 N PRO A 24 3958 2961 4273 -667 338 -917 N ATOM 15 CA PRO A 24 9.684 52.148 61.543 1.00 27.01 C ANISOU 15 CA PRO A 24 3595 2777 3891 -682 221 -996 C ATOM 16 C PRO A 24 10.850 51.331 60.995 1.00 30.09 C ANISOU 16 C PRO A 24 3886 3225 4322 -729 179 -979 C ATOM 17 O PRO A 24 10.935 51.109 59.786 1.00 25.16 O ANISOU 17 O PRO A 24 3246 2574 3740 -727 241 -879 O ATOM 18 CB PRO A 24 8.526 51.194 61.861 1.00 19.86 C ANISOU 18 CB PRO A 24 2728 1969 2849 -586 192 -923 C ATOM 19 CG PRO A 24 7.295 51.915 61.422 1.00 25.26 C ANISOU 19 CG PRO A 24 3483 2569 3546 -527 282 -866 C ATOM 20 CD PRO A 24 7.709 52.733 60.231 1.00 23.77 C ANISOU 20 CD PRO A 24 3297 2258 3475 -563 363 -820 C ATOM 21 N ASN A 25 11.730 50.875 61.878 1.00 26.79 N ANISOU 21 N ASN A 25 3405 2887 3887 -761 69 -1079 N ATOM 22 CA ASN A 25 12.732 49.895 61.490 1.00 21.50 C ANISOU 22 CA ASN A 25 2635 2293 3243 -782 11 -1065 C ATOM 23 C ASN A 25 12.083 48.607 60.965 1.00 27.03 C ANISOU 23 C ASN A 25 3348 3080 3843 -702 2 -928 C ATOM 24 O ASN A 25 11.035 48.176 61.456 1.00 24.52 O ANISOU 24 O ASN A 25 3099 2808 3407 -630 -15 -886 O ATOM 25 CB ASN A 25 13.645 49.583 62.670 1.00 38.08 C ANISOU 25 CB ASN A 25 4675 4473 5322 -805 -131 -1199 C ATOM 26 CG ASN A 25 14.775 48.654 62.293 1.00 49.70 C ANISOU 26 CG ASN A 25 6027 6014 6842 -820 -196 -1195 C ATOM 27 OD1 ASN A 25 14.653 47.434 62.410 1.00 51.56 O ANISOU 27 OD1 ASN A 25 6259 6350 6983 -757 -267 -1138 O ATOM 28 ND2 ASN A 25 15.883 49.227 61.818 1.00 51.40 N ANISOU 28 ND2 ASN A 25 6157 6181 7193 -877 -159 -1218 N ATOM 29 N ARG A 26 12.719 47.975 59.984 1.00 18.16 N ANISOU 29 N ARG A 26 2154 1972 2772 -717 20 -869 N ATOM 30 CA ARG A 26 12.127 46.813 59.325 1.00 17.71 C ANISOU 30 CA ARG A 26 2109 1981 2638 -648 23 -744 C ATOM 31 C ARG A 26 11.909 45.621 60.257 1.00 18.19 C ANISOU 31 C ARG A 26 2174 2159 2577 -589 -88 -744 C ATOM 32 O ARG A 26 11.208 44.681 59.904 1.00 21.29 O ANISOU 32 O ARG A 26 2591 2600 2898 -530 -83 -649 O ATOM 33 CB ARG A 26 12.998 46.393 58.139 1.00 26.18 C ANISOU 33 CB ARG A 26 3106 3047 3794 -682 66 -699 C ATOM 34 CG ARG A 26 14.466 46.221 58.511 1.00 35.10 C ANISOU 34 CG ARG A 26 4118 4207 5012 -745 0 -805 C ATOM 35 CD ARG A 26 15.349 46.017 57.292 1.00 47.07 C ANISOU 35 CD ARG A 26 5556 5694 6635 -791 77 -773 C ATOM 36 NE ARG A 26 15.062 44.747 56.635 1.00 64.49 N ANISOU 36 NE ARG A 26 7763 7972 8770 -726 67 -670 N ATOM 37 CZ ARG A 26 15.779 44.239 55.638 1.00 71.45 C ANISOU 37 CZ ARG A 26 8579 8854 9714 -747 120 -637 C ATOM 38 NH1 ARG A 26 16.838 44.897 55.179 1.00 74.84 N ANISOU 38 NH1 ARG A 26 8934 9218 10286 -833 195 -698 N ATOM 39 NH2 ARG A 26 15.438 43.072 55.102 1.00 69.04 N ANISOU 39 NH2 ARG A 26 8283 8612 9337 -684 106 -551 N ATOM 40 N ALA A 27 12.508 45.653 61.444 1.00 21.65 N ANISOU 40 N ALA A 27 2597 2639 2990 -603 -188 -851 N ATOM 41 CA ALA A 27 12.405 44.512 62.349 1.00 23.90 C ANISOU 41 CA ALA A 27 2904 3026 3149 -541 -293 -845 C ATOM 42 C ALA A 27 11.404 44.727 63.480 1.00 26.55 C ANISOU 42 C ALA A 27 3353 3375 3360 -499 -302 -867 C ATOM 43 O ALA A 27 11.130 43.805 64.248 1.00 24.19 O ANISOU 43 O ALA A 27 3105 3149 2938 -444 -364 -847 O ATOM 44 CB ALA A 27 13.791 44.135 62.919 1.00 22.26 C ANISOU 44 CB ALA A 27 2611 2875 2973 -561 -421 -941 C ATOM 45 N GLU A 28 10.850 45.929 63.594 1.00 19.80 N ANISOU 45 N GLU A 28 2545 2443 2534 -523 -231 -907 N ATOM 46 CA GLU A 28 9.882 46.157 64.663 1.00 20.95 C ANISOU 46 CA GLU A 28 2796 2597 2566 -483 -224 -935 C ATOM 47 C GLU A 28 8.444 45.899 64.218 1.00 18.43 C ANISOU 47 C GLU A 28 2530 2267 2207 -429 -125 -829 C ATOM 48 O GLU A 28 8.114 46.006 63.032 1.00 16.23 O ANISOU 48 O GLU A 28 2217 1944 2004 -429 -55 -751 O ATOM 49 CB GLU A 28 10.043 47.549 65.287 1.00 29.99 C ANISOU 49 CB GLU A 28 3971 3672 3753 -528 -214 -1060 C ATOM 50 CG GLU A 28 10.150 48.683 64.306 1.00 38.36 C ANISOU 50 CG GLU A 28 4995 4617 4964 -584 -120 -1061 C ATOM 51 CD GLU A 28 10.390 50.023 65.000 1.00 55.47 C ANISOU 51 CD GLU A 28 7190 6705 7180 -635 -113 -1197 C ATOM 52 OE1 GLU A 28 9.675 50.327 65.986 1.00 57.99 O ANISOU 52 OE1 GLU A 28 7597 7030 7407 -601 -113 -1249 O ATOM 53 OE2 GLU A 28 11.297 50.769 64.565 1.00 58.67 O ANISOU 53 OE2 GLU A 28 7531 7038 7721 -712 -99 -1259 O ATOM 54 N ASN A 29 7.593 45.550 65.176 1.00 19.70 N ANISOU 54 N ASN A 29 2773 2465 2246 -382 -119 -830 N ATOM 55 CA ASN A 29 6.209 45.192 64.866 1.00 20.38 C ANISOU 55 CA ASN A 29 2891 2548 2303 -333 -28 -745 C ATOM 56 C ASN A 29 5.509 46.323 64.123 1.00 16.24 C ANISOU 56 C ASN A 29 2361 1932 1879 -335 64 -738 C ATOM 57 O ASN A 29 4.702 46.077 63.226 1.00 17.97 O ANISOU 57 O ASN A 29 2557 2138 2133 -301 120 -654 O ATOM 58 CB ASN A 29 5.443 44.806 66.137 1.00 23.51 C ANISOU 58 CB ASN A 29 3383 2986 2563 -294 -13 -767 C ATOM 59 CG ASN A 29 6.038 43.580 66.837 1.00 40.64 C ANISOU 59 CG ASN A 29 5583 5240 4617 -275 -101 -752 C ATOM 60 OD1 ASN A 29 6.453 42.607 66.192 1.00 32.00 O ANISOU 60 OD1 ASN A 29 4436 4182 3542 -268 -139 -680 O ATOM 61 ND2 ASN A 29 6.088 43.630 68.165 1.00 49.64 N ANISOU 61 ND2 ASN A 29 6822 6408 5631 -259 -135 -821 N ATOM 62 N ALA A 30 5.846 47.560 64.494 1.00 17.16 N ANISOU 62 N ALA A 30 2498 1981 2041 -370 72 -830 N ATOM 63 CA ALA A 30 5.259 48.736 63.869 1.00 22.00 C ANISOU 63 CA ALA A 30 3120 2489 2749 -367 157 -828 C ATOM 64 C ALA A 30 5.411 48.706 62.350 1.00 21.70 C ANISOU 64 C ALA A 30 3029 2412 2805 -369 186 -733 C ATOM 65 O ALA A 30 4.626 49.315 61.626 1.00 16.56 O ANISOU 65 O ALA A 30 2395 1691 2208 -333 253 -688 O ATOM 66 CB ALA A 30 5.873 50.023 64.448 1.00 18.57 C ANISOU 66 CB ALA A 30 2712 1977 2365 -420 155 -949 C ATOM 67 N TYR A 31 6.416 47.990 61.858 1.00 16.92 N ANISOU 67 N TYR A 31 2365 1850 2212 -403 133 -704 N ATOM 68 CA TYR A 31 6.708 48.025 60.427 1.00 18.14 C ANISOU 68 CA TYR A 31 2482 1963 2448 -412 169 -624 C ATOM 69 C TYR A 31 5.562 47.426 59.607 1.00 15.65 C ANISOU 69 C TYR A 31 2173 1668 2105 -339 202 -519 C ATOM 70 O TYR A 31 5.317 47.828 58.469 1.00 16.54 O ANISOU 70 O TYR A 31 2294 1720 2271 -319 249 -455 O ATOM 71 CB TYR A 31 8.021 47.306 60.127 1.00 18.31 C ANISOU 71 CB TYR A 31 2432 2033 2491 -461 113 -626 C ATOM 72 CG TYR A 31 8.509 47.477 58.714 1.00 15.48 C ANISOU 72 CG TYR A 31 2043 1621 2217 -485 168 -561 C ATOM 73 CD1 TYR A 31 9.121 48.660 58.305 1.00 20.72 C ANISOU 73 CD1 TYR A 31 2713 2177 2984 -545 230 -596 C ATOM 74 CD2 TYR A 31 8.358 46.458 57.782 1.00 14.58 C ANISOU 74 CD2 TYR A 31 1905 1556 2077 -451 167 -466 C ATOM 75 CE1 TYR A 31 9.573 48.818 56.993 1.00 18.12 C ANISOU 75 CE1 TYR A 31 2374 1789 2720 -567 300 -530 C ATOM 76 CE2 TYR A 31 8.813 46.603 56.483 1.00 20.91 C ANISOU 76 CE2 TYR A 31 2696 2309 2939 -469 225 -407 C ATOM 77 CZ TYR A 31 9.417 47.780 56.092 1.00 21.49 C ANISOU 77 CZ TYR A 31 2785 2275 3105 -526 295 -435 C ATOM 78 OH TYR A 31 9.867 47.910 54.794 1.00 19.75 O ANISOU 78 OH TYR A 31 2572 2000 2931 -544 370 -370 O ATOM 79 N ALA A 32 4.863 46.463 60.193 1.00 14.43 N ANISOU 79 N ALA A 32 2020 1594 1868 -299 178 -504 N ATOM 80 CA ALA A 32 3.767 45.812 59.496 1.00 13.72 C ANISOU 80 CA ALA A 32 1919 1530 1765 -236 201 -423 C ATOM 81 C ALA A 32 2.667 46.818 59.150 1.00 19.43 C ANISOU 81 C ALA A 32 2672 2176 2535 -185 261 -417 C ATOM 82 O ALA A 32 2.217 46.881 58.006 1.00 21.55 O ANISOU 82 O ALA A 32 2932 2416 2839 -143 275 -350 O ATOM 83 CB ALA A 32 3.207 44.664 60.328 1.00 13.40 C ANISOU 83 CB ALA A 32 1876 1574 1640 -214 183 -421 C ATOM 84 N ASP A 33 2.231 47.603 60.133 1.00 15.45 N ANISOU 84 N ASP A 33 2208 1637 2027 -180 292 -489 N ATOM 85 CA ASP A 33 1.142 48.540 59.876 1.00 19.88 C ANISOU 85 CA ASP A 33 2791 2122 2640 -120 347 -490 C ATOM 86 C ASP A 33 1.590 49.664 58.954 1.00 15.73 C ANISOU 86 C ASP A 33 2296 1487 2193 -125 370 -468 C ATOM 87 O ASP A 33 0.798 50.156 58.153 1.00 15.92 O ANISOU 87 O ASP A 33 2335 1453 2259 -56 394 -421 O ATOM 88 CB ASP A 33 0.539 49.089 61.170 1.00 18.88 C ANISOU 88 CB ASP A 33 2702 1981 2490 -111 387 -579 C ATOM 89 CG ASP A 33 -0.431 48.105 61.825 1.00 24.71 C ANISOU 89 CG ASP A 33 3420 2802 3168 -78 405 -580 C ATOM 90 OD1 ASP A 33 -0.571 46.966 61.334 1.00 27.64 O ANISOU 90 OD1 ASP A 33 3745 3240 3517 -69 379 -516 O ATOM 91 OD2 ASP A 33 -1.053 48.462 62.845 1.00 23.46 O ANISOU 91 OD2 ASP A 33 3295 2635 2985 -64 456 -648 O ATOM 92 N TYR A 34 2.859 50.054 59.064 1.00 18.96 N ANISOU 92 N TYR A 34 2715 1864 2623 -204 362 -504 N ATOM 93 CA TYR A 34 3.449 51.038 58.164 1.00 16.59 C ANISOU 93 CA TYR A 34 2449 1453 2403 -227 402 -479 C ATOM 94 C TYR A 34 3.294 50.566 56.726 1.00 16.04 C ANISOU 94 C TYR A 34 2375 1387 2333 -184 403 -365 C ATOM 95 O TYR A 34 2.852 51.320 55.861 1.00 20.27 O ANISOU 95 O TYR A 34 2964 1831 2906 -132 442 -312 O ATOM 96 CB TYR A 34 4.937 51.214 58.481 1.00 16.98 C ANISOU 96 CB TYR A 34 2478 1491 2485 -332 390 -541 C ATOM 97 CG TYR A 34 5.695 52.001 57.444 1.00 23.77 C ANISOU 97 CG TYR A 34 3362 2240 3431 -374 450 -506 C ATOM 98 CD1 TYR A 34 5.619 53.392 57.412 1.00 25.98 C ANISOU 98 CD1 TYR A 34 3708 2378 3787 -384 520 -536 C ATOM 99 CD2 TYR A 34 6.501 51.363 56.497 1.00 24.19 C ANISOU 99 CD2 TYR A 34 3379 2319 3492 -406 450 -444 C ATOM 100 CE1 TYR A 34 6.312 54.122 56.469 1.00 27.91 C ANISOU 100 CE1 TYR A 34 3989 2506 4109 -427 594 -498 C ATOM 101 CE2 TYR A 34 7.201 52.092 55.550 1.00 25.78 C ANISOU 101 CE2 TYR A 34 3614 2412 3769 -450 528 -410 C ATOM 102 CZ TYR A 34 7.100 53.468 55.542 1.00 34.19 C ANISOU 102 CZ TYR A 34 4751 3332 4906 -462 603 -434 C ATOM 103 OH TYR A 34 7.791 54.204 54.601 1.00 44.80 O ANISOU 103 OH TYR A 34 6144 4553 6327 -509 700 -394 O ATOM 104 N VAL A 35 3.675 49.315 56.479 1.00 15.64 N ANISOU 104 N VAL A 35 2270 1438 2235 -200 356 -330 N ATOM 105 CA VAL A 35 3.631 48.745 55.138 1.00 14.69 C ANISOU 105 CA VAL A 35 2146 1332 2102 -165 351 -234 C ATOM 106 C VAL A 35 2.208 48.792 54.570 1.00 14.65 C ANISOU 106 C VAL A 35 2163 1320 2085 -57 345 -183 C ATOM 107 O VAL A 35 1.993 49.190 53.425 1.00 17.58 O ANISOU 107 O VAL A 35 2583 1632 2465 -6 360 -114 O ATOM 108 CB VAL A 35 4.153 47.288 55.128 1.00 20.88 C ANISOU 108 CB VAL A 35 2864 2232 2837 -193 299 -219 C ATOM 109 CG1 VAL A 35 3.769 46.577 53.842 1.00 25.07 C ANISOU 109 CG1 VAL A 35 3393 2792 3341 -139 287 -131 C ATOM 110 CG2 VAL A 35 5.665 47.272 55.301 1.00 28.06 C ANISOU 110 CG2 VAL A 35 3743 3140 3778 -286 300 -258 C ATOM 111 N LEU A 36 1.241 48.390 55.380 1.00 15.29 N ANISOU 111 N LEU A 36 2206 1458 2145 -20 324 -221 N ATOM 112 CA LEU A 36 -0.151 48.349 54.939 1.00 18.90 C ANISOU 112 CA LEU A 36 2653 1919 2610 81 311 -193 C ATOM 113 C LEU A 36 -0.698 49.746 54.666 1.00 19.74 C ANISOU 113 C LEU A 36 2823 1908 2771 145 345 -192 C ATOM 114 O LEU A 36 -1.350 49.974 53.646 1.00 21.78 O ANISOU 114 O LEU A 36 3105 2132 3039 233 324 -134 O ATOM 115 CB LEU A 36 -1.011 47.609 55.960 1.00 14.24 C ANISOU 115 CB LEU A 36 2001 1410 2001 92 304 -245 C ATOM 116 CG LEU A 36 -0.622 46.130 56.056 1.00 17.86 C ANISOU 116 CG LEU A 36 2408 1975 2405 49 269 -228 C ATOM 117 CD1 LEU A 36 -1.527 45.351 57.010 1.00 19.68 C ANISOU 117 CD1 LEU A 36 2591 2272 2616 58 281 -269 C ATOM 118 CD2 LEU A 36 -0.619 45.493 54.666 1.00 17.12 C ANISOU 118 CD2 LEU A 36 2297 1904 2303 81 228 -154 C ATOM 119 N ASP A 37 -0.413 50.680 55.570 1.00 16.14 N ANISOU 119 N ASP A 37 2401 1385 2348 105 391 -258 N ATOM 120 CA ASP A 37 -0.862 52.059 55.425 1.00 17.22 C ANISOU 120 CA ASP A 37 2605 1393 2545 161 433 -265 C ATOM 121 C ASP A 37 -0.319 52.674 54.140 1.00 21.35 C ANISOU 121 C ASP A 37 3209 1819 3083 176 451 -180 C ATOM 122 O ASP A 37 -1.068 53.259 53.357 1.00 24.77 O ANISOU 122 O ASP A 37 3694 2182 3535 278 446 -127 O ATOM 123 CB ASP A 37 -0.409 52.890 56.624 1.00 21.87 C ANISOU 123 CB ASP A 37 3220 1927 3164 94 482 -361 C ATOM 124 CG ASP A 37 -1.180 54.190 56.757 1.00 30.43 C ANISOU 124 CG ASP A 37 4360 2889 4315 165 528 -389 C ATOM 125 OD1 ASP A 37 -2.374 54.223 56.402 1.00 34.56 O ANISOU 125 OD1 ASP A 37 4866 3409 4855 275 512 -364 O ATOM 126 OD2 ASP A 37 -0.596 55.181 57.227 1.00 23.46 O ANISOU 126 OD2 ASP A 37 3532 1908 3474 112 577 -445 O ATOM 127 N ILE A 38 0.986 52.531 53.926 1.00 19.60 N ANISOU 127 N ILE A 38 3000 1592 2854 77 474 -168 N ATOM 128 CA ILE A 38 1.632 53.054 52.726 1.00 20.65 C ANISOU 128 CA ILE A 38 3218 1630 2998 74 517 -87 C ATOM 129 C ILE A 38 1.173 52.287 51.479 1.00 21.21 C ANISOU 129 C ILE A 38 3299 1756 3005 155 468 10 C ATOM 130 O ILE A 38 0.995 52.866 50.408 1.00 22.85 O ANISOU 130 O ILE A 38 3604 1876 3202 223 487 90 O ATOM 131 CB ILE A 38 3.169 53.007 52.841 1.00 23.48 C ANISOU 131 CB ILE A 38 3563 1977 3380 -61 563 -113 C ATOM 132 CG1 ILE A 38 3.649 53.901 53.991 1.00 24.41 C ANISOU 132 CG1 ILE A 38 3680 2028 3567 -139 603 -220 C ATOM 133 CG2 ILE A 38 3.823 53.419 51.513 1.00 21.74 C ANISOU 133 CG2 ILE A 38 3432 1662 3166 -69 630 -22 C ATOM 134 CD1 ILE A 38 3.587 55.366 53.699 1.00 25.15 C ANISOU 134 CD1 ILE A 38 3878 1945 3732 -124 685 -210 C ATOM 135 N GLY A 39 0.949 50.992 51.636 1.00 16.56 N ANISOU 135 N GLY A 39 2618 1305 2369 153 403 0 N ATOM 136 CA GLY A 39 0.566 50.146 50.517 1.00 16.18 C ANISOU 136 CA GLY A 39 2569 1319 2261 218 349 72 C ATOM 137 C GLY A 39 -0.825 50.460 49.995 1.00 25.01 C ANISOU 137 C GLY A 39 3709 2417 3376 359 296 100 C ATOM 138 O GLY A 39 -1.088 50.335 48.806 1.00 29.72 O ANISOU 138 O GLY A 39 4360 3006 3924 436 259 172 O ATOM 139 N LYS A 40 -1.716 50.887 50.884 1.00 17.03 N ANISOU 139 N LYS A 40 2658 1397 2417 398 290 37 N ATOM 140 CA LYS A 40 -3.073 51.229 50.492 1.00 23.54 C ANISOU 140 CA LYS A 40 3481 2202 3262 538 236 46 C ATOM 141 C LYS A 40 -3.164 52.553 49.730 1.00 28.13 C ANISOU 141 C LYS A 40 4196 2636 3858 622 259 108 C ATOM 142 O LYS A 40 -4.198 52.860 49.154 1.00 28.14 O ANISOU 142 O LYS A 40 4214 2613 3866 758 197 132 O ATOM 143 CB LYS A 40 -3.988 51.282 51.723 1.00 28.30 C ANISOU 143 CB LYS A 40 3991 2834 3926 551 242 -48 C ATOM 144 CG LYS A 40 -4.264 49.925 52.361 1.00 27.83 C ANISOU 144 CG LYS A 40 3808 2914 3850 502 217 -98 C ATOM 145 CD LYS A 40 -5.119 50.064 53.615 1.00 33.18 C ANISOU 145 CD LYS A 40 4415 3607 4584 508 252 -189 C ATOM 146 CE LYS A 40 -5.351 48.706 54.286 1.00 38.39 C ANISOU 146 CE LYS A 40 4973 4391 5222 452 248 -231 C ATOM 147 NZ LYS A 40 -6.202 47.801 53.455 1.00 36.21 N ANISOU 147 NZ LYS A 40 4618 4186 4955 517 177 -212 N ATOM 148 N ARG A 41 -2.095 53.341 49.722 1.00 25.67 N ANISOU 148 N ARG A 41 3979 2219 3556 546 346 131 N ATOM 149 CA ARG A 41 -2.160 54.640 49.056 1.00 30.83 C ANISOU 149 CA ARG A 41 4777 2711 4226 621 386 194 C ATOM 150 C ARG A 41 -2.232 54.507 47.545 1.00 33.37 C ANISOU 150 C ARG A 41 5202 3014 4464 712 346 307 C ATOM 151 O ARG A 41 -2.888 55.296 46.875 1.00 27.78 O ANISOU 151 O ARG A 41 4596 2210 3748 843 321 364 O ATOM 152 CB ARG A 41 -0.992 55.531 49.462 1.00 32.73 C ANISOU 152 CB ARG A 41 5088 2832 4514 503 505 180 C ATOM 153 CG ARG A 41 -1.171 56.123 50.838 1.00 36.76 C ANISOU 153 CG ARG A 41 5547 3313 5108 460 540 71 C ATOM 154 CD ARG A 41 0.013 56.967 51.237 1.00 46.72 C ANISOU 154 CD ARG A 41 6866 4459 6426 335 646 39 C ATOM 155 NE ARG A 41 -0.024 57.252 52.665 1.00 59.14 N ANISOU 155 NE ARG A 41 8372 6042 8056 274 663 -86 N ATOM 156 CZ ARG A 41 0.953 57.854 53.333 1.00 63.94 C ANISOU 156 CZ ARG A 41 8993 6579 8721 154 734 -156 C ATOM 157 NH1 ARG A 41 2.052 58.243 52.697 1.00 60.48 N ANISOU 157 NH1 ARG A 41 8621 6051 8308 73 807 -114 N ATOM 158 NH2 ARG A 41 0.829 58.063 54.636 1.00 68.15 N ANISOU 158 NH2 ARG A 41 9473 7132 9287 112 736 -275 N ATOM 159 N ILE A 42 -1.553 53.504 47.014 1.00 32.80 N ANISOU 159 N ILE A 42 5110 3031 4322 649 337 337 N ATOM 160 CA ILE A 42 -1.625 53.212 45.593 1.00 38.86 C ANISOU 160 CA ILE A 42 5975 3801 4990 733 293 433 C ATOM 161 C ILE A 42 -2.016 51.757 45.386 1.00 39.10 C ANISOU 161 C ILE A 42 5887 3999 4969 744 191 407 C ATOM 162 O ILE A 42 -1.163 50.895 45.184 1.00 42.71 O ANISOU 162 O ILE A 42 6318 4525 5385 652 216 413 O ATOM 163 CB ILE A 42 -0.288 53.469 44.890 1.00 44.58 C ANISOU 163 CB ILE A 42 6821 4445 5671 646 408 505 C ATOM 164 CG1 ILE A 42 0.243 54.860 45.238 1.00 48.83 C ANISOU 164 CG1 ILE A 42 7459 4810 6285 600 530 514 C ATOM 165 CG2 ILE A 42 -0.445 53.300 43.383 1.00 40.95 C ANISOU 165 CG2 ILE A 42 6497 3972 5088 751 371 612 C ATOM 166 CD1 ILE A 42 1.664 55.084 44.788 1.00 52.44 C ANISOU 166 CD1 ILE A 42 7999 5189 6738 477 668 557 C ATOM 167 N PRO A 43 -3.317 51.481 45.449 1.00 36.44 N ANISOU 167 N PRO A 43 5472 3724 4648 856 80 371 N ATOM 168 CA PRO A 43 -3.859 50.139 45.242 1.00 34.74 C ANISOU 168 CA PRO A 43 5139 3657 4402 874 -20 335 C ATOM 169 C PRO A 43 -3.576 49.609 43.834 1.00 38.81 C ANISOU 169 C PRO A 43 5748 4199 4801 919 -66 410 C ATOM 170 O PRO A 43 -3.459 50.383 42.882 1.00 36.02 O ANISOU 170 O PRO A 43 5558 3749 4381 1000 -58 495 O ATOM 171 CB PRO A 43 -5.365 50.347 45.418 1.00 38.21 C ANISOU 171 CB PRO A 43 5503 4113 4901 1007 -119 285 C ATOM 172 CG PRO A 43 -5.585 51.797 45.171 1.00 43.49 C ANISOU 172 CG PRO A 43 6303 4634 5587 1104 -97 334 C ATOM 173 CD PRO A 43 -4.371 52.475 45.695 1.00 39.69 C ANISOU 173 CD PRO A 43 5899 4058 5123 977 46 354 C ATOM 174 N LEU A 44 -3.469 48.294 43.700 1.00 34.75 N ANISOU 174 N LEU A 44 5141 3807 4254 871 -109 379 N ATOM 175 CA LEU A 44 -3.363 47.707 42.376 1.00 34.28 C ANISOU 175 CA LEU A 44 5161 3785 4080 927 -167 432 C ATOM 176 C LEU A 44 -4.698 47.858 41.654 1.00 31.89 C ANISOU 176 C LEU A 44 4871 3494 3750 1102 -314 430 C ATOM 177 O LEU A 44 -5.736 47.470 42.176 1.00 36.28 O ANISOU 177 O LEU A 44 5280 4119 4386 1140 -397 348 O ATOM 178 CB LEU A 44 -2.975 46.230 42.470 1.00 35.81 C ANISOU 178 CB LEU A 44 5244 4104 4261 834 -180 387 C ATOM 179 CG LEU A 44 -1.590 45.931 43.050 1.00 32.31 C ANISOU 179 CG LEU A 44 4782 3659 3835 675 -57 387 C ATOM 180 CD1 LEU A 44 -1.411 44.439 43.283 1.00 35.39 C ANISOU 180 CD1 LEU A 44 5049 4171 4227 604 -87 334 C ATOM 181 CD2 LEU A 44 -0.491 46.477 42.152 1.00 33.19 C ANISOU 181 CD2 LEU A 44 5054 3685 3871 652 37 473 C ATOM 182 N SER A 45 -4.674 48.432 40.458 1.00 31.95 N ANISOU 182 N SER A 45 5057 3434 3649 1210 -343 517 N ATOM 183 CA SER A 45 -5.860 48.449 39.616 1.00 38.17 C ANISOU 183 CA SER A 45 5831 4270 4404 1338 -489 493 C ATOM 184 C SER A 45 -6.173 47.011 39.212 1.00 40.37 C ANISOU 184 C SER A 45 6002 4687 4649 1329 -588 430 C ATOM 185 O SER A 45 -5.330 46.120 39.368 1.00 37.09 O ANISOU 185 O SER A 45 5572 4314 4206 1241 -537 434 O ATOM 186 CB SER A 45 -5.619 49.302 38.374 1.00 44.03 C ANISOU 186 CB SER A 45 6759 4939 5030 1387 -468 577 C ATOM 187 OG SER A 45 -4.721 48.651 37.490 1.00 43.62 O ANISOU 187 OG SER A 45 6795 4917 4860 1331 -423 616 O ATOM 188 N ALA A 46 -7.377 46.775 38.702 1.00 39.36 N ANISOU 188 N ALA A 46 5796 4626 4533 1415 -725 367 N ATOM 189 CA ALA A 46 -7.749 45.429 38.266 1.00 41.08 C ANISOU 189 CA ALA A 46 5910 4966 4732 1399 -817 293 C ATOM 190 C ALA A 46 -6.808 44.937 37.170 1.00 37.91 C ANISOU 190 C ALA A 46 5645 4576 4182 1364 -783 348 C ATOM 191 O ALA A 46 -6.452 43.754 37.127 1.00 35.42 O ANISOU 191 O ALA A 46 5268 4338 3851 1298 -787 310 O ATOM 192 CB ALA A 46 -9.183 45.391 37.794 1.00 41.21 C ANISOU 192 CB ALA A 46 5837 5035 4788 1494 -960 215 C ATOM 193 N ALA A 47 -6.390 45.850 36.299 1.00 32.88 N ANISOU 193 N ALA A 47 5193 3858 3441 1406 -738 433 N ATOM 194 CA ALA A 47 -5.434 45.514 35.243 1.00 41.22 C ANISOU 194 CA ALA A 47 6392 4911 4360 1372 -678 486 C ATOM 195 C ALA A 47 -4.049 45.249 35.827 1.00 42.75 C ANISOU 195 C ALA A 47 6609 5077 4559 1244 -524 532 C ATOM 196 O ALA A 47 -3.343 44.320 35.398 1.00 34.81 O ANISOU 196 O ALA A 47 5613 4120 3492 1182 -489 528 O ATOM 197 CB ALA A 47 -5.370 46.622 34.200 1.00 42.47 C ANISOU 197 CB ALA A 47 6742 4980 4412 1450 -655 563 C ATOM 198 N ASP A 48 -3.668 46.073 36.801 1.00 37.78 N ANISOU 198 N ASP A 48 5985 4363 4008 1205 -430 570 N ATOM 199 CA ASP A 48 -2.429 45.875 37.541 1.00 33.41 C ANISOU 199 CA ASP A 48 5432 3777 3485 1080 -288 602 C ATOM 200 C ASP A 48 -2.398 44.490 38.155 1.00 29.80 C ANISOU 200 C ASP A 48 4808 3438 3079 1007 -325 524 C ATOM 201 O ASP A 48 -1.406 43.784 38.045 1.00 25.09 O ANISOU 201 O ASP A 48 4205 2870 2457 904 -243 527 O ATOM 202 CB ASP A 48 -2.293 46.900 38.662 1.00 35.10 C ANISOU 202 CB ASP A 48 5641 3892 3806 1053 -208 621 C ATOM 203 CG ASP A 48 -2.043 48.292 38.144 1.00 53.36 C ANISOU 203 CG ASP A 48 8109 6078 6089 1077 -127 692 C ATOM 204 OD1 ASP A 48 -1.629 48.422 36.970 1.00 56.34 O ANISOU 204 OD1 ASP A 48 8610 6438 6358 1086 -92 738 O ATOM 205 OD2 ASP A 48 -2.260 49.255 38.914 1.00 61.46 O ANISOU 205 OD2 ASP A 48 9133 7017 7202 1087 -93 695 O ATOM 206 N LEU A 49 -3.495 44.122 38.808 1.00 27.24 N ANISOU 206 N LEU A 49 4323 3180 2847 1041 -432 440 N ATOM 207 CA LEU A 49 -3.577 42.865 39.525 1.00 27.77 C ANISOU 207 CA LEU A 49 4206 3352 2992 947 -448 351 C ATOM 208 C LEU A 49 -3.517 41.732 38.518 1.00 25.03 C ANISOU 208 C LEU A 49 3873 3083 2553 964 -514 333 C ATOM 209 O LEU A 49 -2.839 40.735 38.725 1.00 24.73 O ANISOU 209 O LEU A 49 3773 3097 2526 860 -463 306 O ATOM 210 CB LEU A 49 -4.872 42.799 40.333 1.00 27.23 C ANISOU 210 CB LEU A 49 3978 3324 3043 989 -536 265 C ATOM 211 CG LEU A 49 -5.072 41.579 41.236 1.00 36.28 C ANISOU 211 CG LEU A 49 4939 4562 4285 890 -533 175 C ATOM 212 CD1 LEU A 49 -3.931 41.437 42.223 1.00 32.30 C ANISOU 212 CD1 LEU A 49 4413 4043 3817 744 -395 189 C ATOM 213 CD2 LEU A 49 -6.402 41.680 41.963 1.00 35.23 C ANISOU 213 CD2 LEU A 49 4662 4452 4272 939 -598 94 C ATOM 214 N SER A 50 -4.229 41.911 37.416 1.00 26.39 N ANISOU 214 N SER A 50 4130 3261 2637 1093 -628 340 N ATOM 215 CA SER A 50 -4.253 40.946 36.335 1.00 30.08 C ANISOU 215 CA SER A 50 4611 3795 3021 1096 -682 304 C ATOM 216 C SER A 50 -2.840 40.643 35.856 1.00 28.71 C ANISOU 216 C SER A 50 4555 3602 2752 1020 -558 367 C ATOM 217 O SER A 50 -2.470 39.484 35.672 1.00 28.36 O ANISOU 217 O SER A 50 4465 3625 2687 968 -560 327 O ATOM 218 CB SER A 50 -5.090 41.497 35.177 1.00 37.06 C ANISOU 218 CB SER A 50 5578 4665 3839 1206 -773 299 C ATOM 219 OG SER A 50 -5.495 40.462 34.305 1.00 46.16 O ANISOU 219 OG SER A 50 6698 5894 4945 1222 -862 229 O ATOM 220 N ASN A 51 -2.052 41.693 35.656 1.00 24.86 N ANISOU 220 N ASN A 51 4213 3016 2218 1009 -440 459 N ATOM 221 CA ASN A 51 -0.673 41.535 35.213 1.00 26.32 C ANISOU 221 CA ASN A 51 4497 3168 2334 925 -295 514 C ATOM 222 C ASN A 51 0.229 40.901 36.275 1.00 28.49 C ANISOU 222 C ASN A 51 4659 3467 2697 792 -200 495 C ATOM 223 O ASN A 51 1.109 40.100 35.950 1.00 25.55 O ANISOU 223 O ASN A 51 4287 3125 2295 721 -132 487 O ATOM 224 CB ASN A 51 -0.112 42.878 34.729 1.00 32.48 C ANISOU 224 CB ASN A 51 5439 3828 3072 932 -180 600 C ATOM 225 CG ASN A 51 -0.809 43.374 33.468 1.00 42.58 C ANISOU 225 CG ASN A 51 6835 5091 4253 1047 -255 612 C ATOM 226 OD1 ASN A 51 -1.066 42.602 32.541 1.00 44.24 O ANISOU 226 OD1 ASN A 51 7061 5363 4384 1085 -327 574 O ATOM 227 ND2 ASN A 51 -1.134 44.660 33.437 1.00 46.54 N ANISOU 227 ND2 ASN A 51 7421 5503 4759 1104 -242 661 N ATOM 228 N VAL A 52 0.013 41.248 37.544 1.00 24.15 N ANISOU 228 N VAL A 52 3985 2907 2284 740 -188 464 N ATOM 229 CA VAL A 52 0.769 40.619 38.623 1.00 25.02 C ANISOU 229 CA VAL A 52 3954 3049 2502 602 -112 419 C ATOM 230 C VAL A 52 0.456 39.123 38.663 1.00 23.30 C ANISOU 230 C VAL A 52 3614 2938 2300 581 -188 344 C ATOM 231 O VAL A 52 1.345 38.275 38.781 1.00 16.66 O ANISOU 231 O VAL A 52 2727 2128 1473 494 -127 327 O ATOM 232 CB VAL A 52 0.422 41.226 39.990 1.00 20.86 C ANISOU 232 CB VAL A 52 3327 2499 2100 565 -104 391 C ATOM 233 CG1 VAL A 52 0.968 40.335 41.129 1.00 18.18 C ANISOU 233 CG1 VAL A 52 2837 2216 1854 445 -67 333 C ATOM 234 CG2 VAL A 52 0.962 42.642 40.090 1.00 16.84 C ANISOU 234 CG2 VAL A 52 2927 1874 1598 556 -5 455 C ATOM 235 N TYR A 53 -0.831 38.821 38.570 1.00 18.80 N ANISOU 235 N TYR A 53 2987 2418 1739 663 -322 293 N ATOM 236 CA TYR A 53 -1.324 37.454 38.510 1.00 17.48 C ANISOU 236 CA TYR A 53 2708 2341 1594 652 -402 214 C ATOM 237 C TYR A 53 -0.568 36.653 37.452 1.00 15.17 C ANISOU 237 C TYR A 53 2493 2072 1198 642 -379 222 C ATOM 238 O TYR A 53 -0.102 35.544 37.708 1.00 20.56 O ANISOU 238 O TYR A 53 3094 2799 1919 565 -351 180 O ATOM 239 CB TYR A 53 -2.812 37.496 38.166 1.00 28.43 C ANISOU 239 CB TYR A 53 4057 3761 2985 767 -554 162 C ATOM 240 CG TYR A 53 -3.631 36.373 38.745 1.00 40.51 C ANISOU 240 CG TYR A 53 5410 5364 4619 734 -622 60 C ATOM 241 CD1 TYR A 53 -4.158 36.462 40.027 1.00 45.01 C ANISOU 241 CD1 TYR A 53 5848 5934 5321 689 -600 22 C ATOM 242 CD2 TYR A 53 -3.899 35.231 37.998 1.00 38.75 C ANISOU 242 CD2 TYR A 53 5158 5203 4362 747 -698 -2 C ATOM 243 CE1 TYR A 53 -4.923 35.430 40.555 1.00 51.44 C ANISOU 243 CE1 TYR A 53 6507 6803 6234 653 -640 -68 C ATOM 244 CE2 TYR A 53 -4.659 34.198 38.513 1.00 43.62 C ANISOU 244 CE2 TYR A 53 5614 5873 5088 709 -747 -98 C ATOM 245 CZ TYR A 53 -5.171 34.301 39.791 1.00 50.01 C ANISOU 245 CZ TYR A 53 6295 6676 6030 660 -711 -127 C ATOM 246 OH TYR A 53 -5.930 33.271 40.302 1.00 52.11 O ANISOU 246 OH TYR A 53 6409 6983 6407 616 -738 -220 O ATOM 247 N GLU A 54 -0.448 37.227 36.263 1.00 20.66 N ANISOU 247 N GLU A 54 3356 2733 1759 724 -386 278 N ATOM 248 CA GLU A 54 0.249 36.567 35.175 1.00 24.77 C ANISOU 248 CA GLU A 54 3975 3273 2165 723 -353 286 C ATOM 249 C GLU A 54 1.737 36.398 35.471 1.00 25.54 C ANISOU 249 C GLU A 54 4073 3339 2291 604 -186 318 C ATOM 250 O GLU A 54 2.336 35.378 35.120 1.00 23.66 O ANISOU 250 O GLU A 54 3815 3139 2034 560 -153 286 O ATOM 251 CB GLU A 54 0.057 37.327 33.863 1.00 29.39 C ANISOU 251 CB GLU A 54 4739 3813 2614 823 -373 337 C ATOM 252 CG GLU A 54 -1.287 37.064 33.207 1.00 52.79 C ANISOU 252 CG GLU A 54 7669 6824 5567 917 -539 266 C ATOM 253 CD GLU A 54 -1.551 35.579 33.012 1.00 68.60 C ANISOU 253 CD GLU A 54 9569 8913 7584 892 -612 169 C ATOM 254 OE1 GLU A 54 -2.421 35.030 33.724 1.00 71.15 O ANISOU 254 OE1 GLU A 54 9735 9287 8013 887 -705 91 O ATOM 255 OE2 GLU A 54 -0.884 34.960 32.152 1.00 71.85 O ANISOU 255 OE2 GLU A 54 10055 9335 7911 874 -566 166 O ATOM 256 N SER A 55 2.344 37.391 36.109 1.00 21.29 N ANISOU 256 N SER A 55 3551 2730 1808 553 -82 373 N ATOM 257 CA SER A 55 3.778 37.307 36.352 1.00 17.24 C ANISOU 257 CA SER A 55 3028 2187 1335 444 71 393 C ATOM 258 C SER A 55 4.073 36.197 37.365 1.00 18.16 C ANISOU 258 C SER A 55 2966 2366 1570 356 63 323 C ATOM 259 O SER A 55 5.073 35.499 37.248 1.00 20.73 O ANISOU 259 O SER A 55 3264 2704 1909 293 139 309 O ATOM 260 CB SER A 55 4.356 38.651 36.805 1.00 21.63 C ANISOU 260 CB SER A 55 3636 2648 1935 405 180 453 C ATOM 261 OG SER A 55 3.862 39.003 38.086 1.00 28.25 O ANISOU 261 OG SER A 55 4357 3487 2888 380 135 424 O ATOM 262 N VAL A 56 3.199 36.031 38.353 1.00 13.43 N ANISOU 262 N VAL A 56 2249 1799 1054 357 -24 280 N ATOM 263 CA VAL A 56 3.360 34.955 39.326 1.00 12.35 C ANISOU 263 CA VAL A 56 1964 1714 1015 285 -35 223 C ATOM 264 C VAL A 56 3.221 33.580 38.670 1.00 20.28 C ANISOU 264 C VAL A 56 2943 2777 1985 297 -83 173 C ATOM 265 O VAL A 56 3.989 32.660 38.949 1.00 13.00 O ANISOU 265 O VAL A 56 1960 1875 1106 235 -39 149 O ATOM 266 CB VAL A 56 2.354 35.093 40.491 1.00 15.20 C ANISOU 266 CB VAL A 56 2223 2090 1462 287 -102 190 C ATOM 267 CG1 VAL A 56 2.432 33.880 41.413 1.00 17.62 C ANISOU 267 CG1 VAL A 56 2402 2444 1848 222 -111 137 C ATOM 268 CG2 VAL A 56 2.649 36.359 41.275 1.00 13.30 C ANISOU 268 CG2 VAL A 56 2000 1790 1265 261 -44 226 C ATOM 269 N ILE A 57 2.253 33.437 37.779 1.00 13.06 N ANISOU 269 N ILE A 57 2078 1888 996 382 -178 153 N ATOM 270 CA ILE A 57 2.063 32.144 37.140 1.00 15.82 C ANISOU 270 CA ILE A 57 2404 2289 1316 392 -230 92 C ATOM 271 C ILE A 57 3.328 31.766 36.381 1.00 18.97 C ANISOU 271 C ILE A 57 2879 2677 1652 361 -129 112 C ATOM 272 O ILE A 57 3.784 30.630 36.442 1.00 17.97 O ANISOU 272 O ILE A 57 2690 2576 1561 317 -109 68 O ATOM 273 CB ILE A 57 0.879 32.173 36.169 1.00 19.59 C ANISOU 273 CB ILE A 57 2937 2796 1711 497 -360 59 C ATOM 274 CG1 ILE A 57 -0.432 32.239 36.952 1.00 20.82 C ANISOU 274 CG1 ILE A 57 2973 2974 1963 519 -461 10 C ATOM 275 CG2 ILE A 57 0.916 30.952 35.262 1.00 23.79 C ANISOU 275 CG2 ILE A 57 3482 3372 2186 508 -398 -4 C ATOM 276 CD1 ILE A 57 -1.660 32.515 36.087 1.00 25.13 C ANISOU 276 CD1 ILE A 57 3558 3545 2446 637 -606 -27 C ATOM 277 N ARG A 58 3.887 32.742 35.672 1.00 20.12 N ANISOU 277 N ARG A 58 3162 2775 1709 387 -55 179 N ATOM 278 CA ARG A 58 5.107 32.564 34.894 1.00 17.02 C ANISOU 278 CA ARG A 58 2853 2360 1255 357 68 202 C ATOM 279 C ARG A 58 6.289 32.238 35.803 1.00 17.31 C ANISOU 279 C ARG A 58 2778 2385 1415 253 172 195 C ATOM 280 O ARG A 58 7.059 31.316 35.535 1.00 16.53 O ANISOU 280 O ARG A 58 2650 2303 1328 219 226 163 O ATOM 281 CB ARG A 58 5.388 33.845 34.112 1.00 19.53 C ANISOU 281 CB ARG A 58 3343 2611 1465 399 143 285 C ATOM 282 CG ARG A 58 6.145 33.659 32.829 1.00 42.05 C ANISOU 282 CG ARG A 58 6339 5447 4190 416 240 304 C ATOM 283 CD ARG A 58 6.122 34.948 32.006 1.00 58.14 C ANISOU 283 CD ARG A 58 8557 7411 6124 470 291 386 C ATOM 284 NE ARG A 58 6.971 36.001 32.567 1.00 69.51 N ANISOU 284 NE ARG A 58 10002 8769 7641 399 433 446 N ATOM 285 CZ ARG A 58 8.153 36.365 32.069 1.00 80.98 C ANISOU 285 CZ ARG A 58 11500 10159 9109 337 596 472 C ATOM 286 NH1 ARG A 58 8.641 35.767 30.991 1.00 84.95 N ANISOU 286 NH1 ARG A 58 12061 10672 9542 343 647 452 N ATOM 287 NH2 ARG A 58 8.851 37.335 32.648 1.00 86.53 N ANISOU 287 NH2 ARG A 58 12186 10787 9906 267 710 508 N ATOM 288 N ALA A 59 6.418 33.002 36.882 1.00 16.20 N ANISOU 288 N ALA A 59 2574 2214 1366 209 193 220 N ATOM 289 CA ALA A 59 7.487 32.801 37.846 1.00 14.98 C ANISOU 289 CA ALA A 59 2311 2051 1329 120 267 207 C ATOM 290 C ALA A 59 7.451 31.398 38.442 1.00 18.45 C ANISOU 290 C ALA A 59 2628 2545 1838 96 211 147 C ATOM 291 O ALA A 59 8.481 30.747 38.610 1.00 11.63 O ANISOU 291 O ALA A 59 1706 1685 1029 50 271 126 O ATOM 292 CB ALA A 59 7.383 33.831 38.957 1.00 16.24 C ANISOU 292 CB ALA A 59 2429 2178 1564 90 267 229 C ATOM 293 N VAL A 60 6.260 30.945 38.799 1.00 11.39 N ANISOU 293 N VAL A 60 1692 1686 951 129 101 118 N ATOM 294 CA VAL A 60 6.144 29.658 39.447 1.00 13.69 C ANISOU 294 CA VAL A 60 1878 2012 1313 103 58 67 C ATOM 295 C VAL A 60 6.437 28.559 38.436 1.00 11.70 C ANISOU 295 C VAL A 60 1651 1779 1016 118 68 29 C ATOM 296 O VAL A 60 7.112 27.579 38.752 1.00 12.63 O ANISOU 296 O VAL A 60 1703 1902 1193 84 95 2 O ATOM 297 CB VAL A 60 4.768 29.465 40.109 1.00 19.63 C ANISOU 297 CB VAL A 60 2574 2787 2099 122 -41 40 C ATOM 298 CG1 VAL A 60 4.613 28.047 40.607 1.00 17.39 C ANISOU 298 CG1 VAL A 60 2204 2525 1879 95 -68 -9 C ATOM 299 CG2 VAL A 60 4.607 30.438 41.260 1.00 17.03 C ANISOU 299 CG2 VAL A 60 2212 2437 1822 100 -35 69 C ATOM 300 N HIS A 61 5.941 28.728 37.217 1.00 13.93 N ANISOU 300 N HIS A 61 2035 2069 1189 177 42 26 N ATOM 301 CA HIS A 61 6.191 27.737 36.182 1.00 16.25 C ANISOU 301 CA HIS A 61 2369 2381 1425 196 51 -19 C ATOM 302 C HIS A 61 7.699 27.635 35.918 1.00 21.03 C ANISOU 302 C HIS A 61 2988 2961 2041 155 185 -3 C ATOM 303 O HIS A 61 8.240 26.544 35.735 1.00 17.54 O ANISOU 303 O HIS A 61 2507 2528 1628 139 212 -48 O ATOM 304 CB HIS A 61 5.460 28.105 34.897 1.00 13.55 C ANISOU 304 CB HIS A 61 2157 2051 940 276 -3 -22 C ATOM 305 CG HIS A 61 5.484 27.025 33.867 1.00 21.31 C ANISOU 305 CG HIS A 61 3183 3059 1854 302 -19 -86 C ATOM 306 ND1 HIS A 61 4.871 25.803 34.056 1.00 21.02 N ANISOU 306 ND1 HIS A 61 3059 3052 1877 294 -100 -168 N ATOM 307 CD2 HIS A 61 6.048 26.976 32.635 1.00 25.91 C ANISOU 307 CD2 HIS A 61 3893 3637 2313 334 43 -87 C ATOM 308 CE1 HIS A 61 5.050 25.053 32.982 1.00 14.78 C ANISOU 308 CE1 HIS A 61 2335 2275 1005 321 -96 -221 C ATOM 309 NE2 HIS A 61 5.765 25.739 32.107 1.00 24.63 N ANISOU 309 NE2 HIS A 61 3717 3506 2135 348 -10 -173 N ATOM 310 N ASP A 62 8.373 28.779 35.896 1.00 19.89 N ANISOU 310 N ASP A 62 2894 2779 1884 137 274 55 N ATOM 311 CA ASP A 62 9.818 28.792 35.682 1.00 15.06 C ANISOU 311 CA ASP A 62 2276 2139 1306 90 414 62 C ATOM 312 C ASP A 62 10.601 28.275 36.896 1.00 19.06 C ANISOU 312 C ASP A 62 2629 2648 1963 30 426 38 C ATOM 313 O ASP A 62 11.821 28.111 36.822 1.00 17.48 O ANISOU 313 O ASP A 62 2389 2431 1820 -7 526 25 O ATOM 314 CB ASP A 62 10.296 30.201 35.320 1.00 18.29 C ANISOU 314 CB ASP A 62 2780 2495 1673 79 517 126 C ATOM 315 CG ASP A 62 11.374 30.183 34.255 1.00 38.93 C ANISOU 315 CG ASP A 62 5474 5081 4238 66 669 130 C ATOM 316 OD1 ASP A 62 11.347 29.261 33.405 1.00 46.76 O ANISOU 316 OD1 ASP A 62 6509 6098 5159 99 669 91 O ATOM 317 OD2 ASP A 62 12.255 31.070 34.275 1.00 39.80 O ANISOU 317 OD2 ASP A 62 5599 5137 4386 17 797 164 O ATOM 318 N SER A 63 9.909 28.015 38.004 1.00 18.09 N ANISOU 318 N SER A 63 2425 2545 1904 25 325 30 N ATOM 319 CA SER A 63 10.576 27.520 39.212 1.00 13.57 C ANISOU 319 CA SER A 63 1728 1975 1453 -17 319 13 C ATOM 320 C SER A 63 10.677 25.989 39.239 1.00 19.94 C ANISOU 320 C SER A 63 2480 2800 2298 -7 289 -36 C ATOM 321 O SER A 63 11.306 25.412 40.127 1.00 11.70 O ANISOU 321 O SER A 63 1346 1754 1345 -27 282 -49 O ATOM 322 CB SER A 63 9.852 27.987 40.479 1.00 12.31 C ANISOU 322 CB SER A 63 1522 1820 1334 -28 242 31 C ATOM 323 OG SER A 63 9.906 29.400 40.620 1.00 16.05 O ANISOU 323 OG SER A 63 2035 2268 1797 -43 275 69 O ATOM 324 N ARG A 64 10.040 25.340 38.274 1.00 11.29 N ANISOU 324 N ARG A 64 1444 1717 1130 29 265 -64 N ATOM 325 CA ARG A 64 9.996 23.878 38.229 1.00 12.22 C ANISOU 325 CA ARG A 64 1519 1840 1282 39 237 -117 C ATOM 326 C ARG A 64 11.359 23.214 38.404 1.00 14.71 C ANISOU 326 C ARG A 64 1769 2139 1681 23 308 -136 C ATOM 327 O ARG A 64 11.478 22.240 39.122 1.00 11.71 O ANISOU 327 O ARG A 64 1321 1752 1378 22 273 -155 O ATOM 328 CB ARG A 64 9.359 23.399 36.930 1.00 12.45 C ANISOU 328 CB ARG A 64 1633 1883 1213 78 219 -159 C ATOM 329 CG ARG A 64 7.839 23.609 36.888 1.00 12.99 C ANISOU 329 CG ARG A 64 1730 1973 1234 104 111 -168 C ATOM 330 CD ARG A 64 7.261 23.228 35.523 1.00 15.68 C ANISOU 330 CD ARG A 64 2159 2332 1465 151 77 -220 C ATOM 331 NE ARG A 64 7.951 23.934 34.453 1.00 17.25 N ANISOU 331 NE ARG A 64 2472 2527 1554 175 159 -193 N ATOM 332 CZ ARG A 64 8.094 23.463 33.223 1.00 19.15 C ANISOU 332 CZ ARG A 64 2803 2775 1696 210 183 -237 C ATOM 333 NH1 ARG A 64 7.577 22.284 32.910 1.00 16.90 N ANISOU 333 NH1 ARG A 64 2497 2505 1418 223 119 -318 N ATOM 334 NH2 ARG A 64 8.748 24.171 32.304 1.00 19.67 N ANISOU 334 NH2 ARG A 64 2988 2830 1657 229 279 -202 N ATOM 335 N SER A 65 12.383 23.751 37.754 1.00 12.09 N ANISOU 335 N SER A 65 1459 1797 1338 12 412 -132 N ATOM 336 CA SER A 65 13.681 23.090 37.771 1.00 17.09 C ANISOU 336 CA SER A 65 2018 2416 2059 4 484 -166 C ATOM 337 C SER A 65 14.275 23.072 39.175 1.00 16.05 C ANISOU 337 C SER A 65 1769 2279 2049 -16 445 -156 C ATOM 338 O SER A 65 15.224 22.334 39.440 1.00 16.74 O ANISOU 338 O SER A 65 1775 2357 2228 -8 465 -188 O ATOM 339 CB SER A 65 14.629 23.756 36.784 1.00 19.01 C ANISOU 339 CB SER A 65 2305 2645 2275 -11 622 -167 C ATOM 340 OG SER A 65 14.753 25.119 37.093 1.00 20.30 O ANISOU 340 OG SER A 65 2480 2797 2437 -45 653 -120 O ATOM 341 N ARG A 66 13.704 23.864 40.082 1.00 16.43 N ANISOU 341 N ARG A 66 1812 2335 2096 -33 382 -116 N ATOM 342 CA ARG A 66 14.202 23.889 41.459 1.00 13.99 C ANISOU 342 CA ARG A 66 1410 2026 1880 -46 332 -109 C ATOM 343 C ARG A 66 13.203 23.447 42.520 1.00 13.84 C ANISOU 343 C ARG A 66 1390 2013 1855 -34 227 -88 C ATOM 344 O ARG A 66 13.455 23.616 43.719 1.00 11.59 O ANISOU 344 O ARG A 66 1056 1730 1619 -40 178 -75 O ATOM 345 CB ARG A 66 14.803 25.256 41.791 1.00 14.67 C ANISOU 345 CB ARG A 66 1471 2108 1995 -87 372 -93 C ATOM 346 CG ARG A 66 16.048 25.493 40.970 1.00 18.55 C ANISOU 346 CG ARG A 66 1932 2584 2534 -107 492 -124 C ATOM 347 CD ARG A 66 16.671 26.813 41.263 1.00 33.33 C ANISOU 347 CD ARG A 66 3773 4438 4452 -158 545 -118 C ATOM 348 NE ARG A 66 17.856 27.001 40.439 1.00 43.29 N ANISOU 348 NE ARG A 66 5000 5678 5772 -187 682 -153 N ATOM 349 CZ ARG A 66 19.100 26.940 40.894 1.00 36.56 C ANISOU 349 CZ ARG A 66 4013 4821 5057 -209 709 -206 C ATOM 350 NH1 ARG A 66 19.324 26.712 42.180 1.00 26.33 N ANISOU 350 NH1 ARG A 66 2619 3546 3838 -198 592 -226 N ATOM 351 NH2 ARG A 66 20.114 27.133 40.065 1.00 32.19 N ANISOU 351 NH2 ARG A 66 3426 4243 4563 -241 855 -242 N ATOM 352 N LEU A 67 12.078 22.872 42.080 1.00 15.36 N ANISOU 352 N LEU A 67 1638 2206 1990 -17 196 -92 N ATOM 353 CA LEU A 67 11.096 22.325 43.006 1.00 9.71 C ANISOU 353 CA LEU A 67 921 1487 1283 -13 121 -79 C ATOM 354 C LEU A 67 11.045 20.792 42.937 1.00 13.08 C ANISOU 354 C LEU A 67 1336 1888 1745 9 109 -108 C ATOM 355 O LEU A 67 11.358 20.196 41.904 1.00 12.97 O ANISOU 355 O LEU A 67 1336 1868 1725 24 148 -147 O ATOM 356 CB LEU A 67 9.711 22.922 42.738 1.00 9.43 C ANISOU 356 CB LEU A 67 938 1465 1179 -17 91 -70 C ATOM 357 CG LEU A 67 9.662 24.445 42.888 1.00 11.43 C ANISOU 357 CG LEU A 67 1212 1729 1400 -33 101 -37 C ATOM 358 CD1 LEU A 67 8.382 25.038 42.306 1.00 9.25 C ANISOU 358 CD1 LEU A 67 995 1466 1056 -18 72 -33 C ATOM 359 CD2 LEU A 67 9.824 24.823 44.367 1.00 9.86 C ANISOU 359 CD2 LEU A 67 971 1528 1247 -51 70 -12 C ATOM 360 N ILE A 68 10.628 20.158 44.027 1.00 9.71 N ANISOU 360 N ILE A 68 896 1440 1352 12 63 -90 N ATOM 361 CA ILE A 68 10.734 18.701 44.124 1.00 10.49 C ANISOU 361 CA ILE A 68 989 1497 1499 34 60 -109 C ATOM 362 C ILE A 68 9.753 17.965 43.209 1.00 11.68 C ANISOU 362 C ILE A 68 1174 1633 1631 28 65 -154 C ATOM 363 O ILE A 68 10.042 16.876 42.728 1.00 14.08 O ANISOU 363 O ILE A 68 1478 1903 1968 45 84 -191 O ATOM 364 CB ILE A 68 10.507 18.225 45.563 1.00 11.93 C ANISOU 364 CB ILE A 68 1172 1649 1711 39 20 -68 C ATOM 365 CG1 ILE A 68 10.920 16.755 45.711 1.00 10.49 C ANISOU 365 CG1 ILE A 68 991 1409 1587 73 23 -77 C ATOM 366 CG2 ILE A 68 9.035 18.423 45.970 1.00 17.01 C ANISOU 366 CG2 ILE A 68 1849 2290 2325 7 6 -55 C ATOM 367 CD1 ILE A 68 12.349 16.490 45.278 1.00 15.01 C ANISOU 367 CD1 ILE A 68 1516 1981 2207 112 39 -101 C ATOM 368 N ASP A 69 8.579 18.538 42.992 1.00 12.78 N ANISOU 368 N ASP A 69 1336 1795 1723 6 43 -159 N ATOM 369 CA ASP A 69 7.572 17.845 42.196 1.00 12.83 C ANISOU 369 CA ASP A 69 1362 1791 1722 0 29 -217 C ATOM 370 C ASP A 69 6.495 18.789 41.688 1.00 12.22 C ANISOU 370 C ASP A 69 1303 1756 1584 -7 -6 -230 C ATOM 371 O ASP A 69 6.426 19.948 42.111 1.00 10.43 O ANISOU 371 O ASP A 69 1079 1557 1328 -10 -14 -186 O ATOM 372 CB ASP A 69 6.978 16.641 42.950 1.00 10.44 C ANISOU 372 CB ASP A 69 1047 1430 1491 -16 24 -225 C ATOM 373 CG ASP A 69 6.256 17.028 44.229 1.00 15.22 C ANISOU 373 CG ASP A 69 1644 2028 2111 -41 12 -177 C ATOM 374 OD1 ASP A 69 6.044 18.234 44.478 1.00 13.81 O ANISOU 374 OD1 ASP A 69 1463 1893 1890 -46 -4 -149 O ATOM 375 OD2 ASP A 69 5.885 16.108 44.987 1.00 14.54 O ANISOU 375 OD2 ASP A 69 1561 1885 2079 -56 27 -169 O ATOM 376 N GLN A 70 5.666 18.285 40.774 1.00 17.16 N ANISOU 376 N GLN A 70 1942 2384 2193 -3 -34 -298 N ATOM 377 CA GLN A 70 4.580 19.070 40.199 1.00 17.41 C ANISOU 377 CA GLN A 70 1989 2457 2170 6 -89 -323 C ATOM 378 C GLN A 70 3.592 19.502 41.284 1.00 16.83 C ANISOU 378 C GLN A 70 1870 2381 2142 -19 -113 -300 C ATOM 379 O GLN A 70 3.092 20.632 41.270 1.00 17.18 O ANISOU 379 O GLN A 70 1923 2460 2147 -5 -143 -280 O ATOM 380 CB GLN A 70 3.858 18.281 39.106 1.00 12.77 C ANISOU 380 CB GLN A 70 1411 1872 1569 17 -131 -418 C ATOM 381 CG GLN A 70 2.844 19.127 38.342 1.00 16.02 C ANISOU 381 CG GLN A 70 1845 2333 1909 48 -208 -451 C ATOM 382 CD GLN A 70 3.510 20.147 37.426 1.00 25.28 C ANISOU 382 CD GLN A 70 3106 3541 2959 94 -196 -414 C ATOM 383 OE1 GLN A 70 4.420 19.810 36.658 1.00 25.63 O ANISOU 383 OE1 GLN A 70 3204 3582 2954 109 -148 -424 O ATOM 384 NE2 GLN A 70 3.053 21.393 37.493 1.00 28.03 N ANISOU 384 NE2 GLN A 70 3475 3916 3260 118 -229 -372 N ATOM 385 N HIS A 71 3.333 18.621 42.244 1.00 15.27 N ANISOU 385 N HIS A 71 1635 2137 2028 -53 -91 -299 N ATOM 386 CA HIS A 71 2.439 18.985 43.336 1.00 14.75 C ANISOU 386 CA HIS A 71 1535 2065 2005 -81 -91 -276 C ATOM 387 C HIS A 71 2.871 20.266 44.040 1.00 15.21 C ANISOU 387 C HIS A 71 1609 2150 2021 -71 -83 -204 C ATOM 388 O HIS A 71 2.043 21.119 44.345 1.00 10.75 O ANISOU 388 O HIS A 71 1028 1606 1452 -72 -103 -201 O ATOM 389 CB HIS A 71 2.312 17.872 44.377 1.00 17.86 C ANISOU 389 CB HIS A 71 1913 2393 2480 -118 -43 -265 C ATOM 390 CG HIS A 71 1.297 18.173 45.442 1.00 15.52 C ANISOU 390 CG HIS A 71 1589 2084 2225 -152 -23 -251 C ATOM 391 ND1 HIS A 71 1.643 18.424 46.755 1.00 17.23 N ANISOU 391 ND1 HIS A 71 1831 2281 2436 -160 17 -177 N ATOM 392 CD2 HIS A 71 -0.053 18.294 45.374 1.00 16.92 C ANISOU 392 CD2 HIS A 71 1712 2267 2451 -176 -36 -308 C ATOM 393 CE1 HIS A 71 0.544 18.665 47.456 1.00 12.24 C ANISOU 393 CE1 HIS A 71 1171 1640 1840 -191 42 -185 C ATOM 394 NE2 HIS A 71 -0.494 18.600 46.642 1.00 19.94 N ANISOU 394 NE2 HIS A 71 2088 2629 2858 -202 13 -266 N ATOM 395 N THR A 72 4.166 20.391 44.315 1.00 9.27 N ANISOU 395 N THR A 72 881 1394 1248 -60 -56 -154 N ATOM 396 CA THR A 72 4.674 21.568 44.998 1.00 11.92 C ANISOU 396 CA THR A 72 1226 1750 1554 -57 -50 -98 C ATOM 397 C THR A 72 4.578 22.795 44.091 1.00 15.30 C ANISOU 397 C THR A 72 1679 2216 1920 -36 -68 -100 C ATOM 398 O THR A 72 4.232 23.881 44.550 1.00 11.87 O ANISOU 398 O THR A 72 1248 1794 1469 -36 -75 -74 O ATOM 399 CB THR A 72 6.124 21.356 45.503 1.00 11.60 C ANISOU 399 CB THR A 72 1188 1696 1522 -51 -27 -62 C ATOM 400 OG1 THR A 72 6.134 20.309 46.480 1.00 12.41 O ANISOU 400 OG1 THR A 72 1288 1758 1671 -58 -19 -47 O ATOM 401 CG2 THR A 72 6.656 22.628 46.160 1.00 14.23 C ANISOU 401 CG2 THR A 72 1524 2051 1833 -54 -27 -21 C ATOM 402 N VAL A 73 4.866 22.623 42.803 1.00 12.31 N ANISOU 402 N VAL A 73 1328 1848 1500 -13 -70 -129 N ATOM 403 CA VAL A 73 4.660 23.698 41.836 1.00 16.07 C ANISOU 403 CA VAL A 73 1853 2352 1901 18 -85 -126 C ATOM 404 C VAL A 73 3.219 24.211 41.889 1.00 17.81 C ANISOU 404 C VAL A 73 2061 2587 2119 33 -145 -147 C ATOM 405 O VAL A 73 2.988 25.419 41.985 1.00 13.52 O ANISOU 405 O VAL A 73 1540 2052 1545 50 -153 -115 O ATOM 406 CB VAL A 73 4.983 23.265 40.383 1.00 16.04 C ANISOU 406 CB VAL A 73 1900 2357 1837 46 -81 -164 C ATOM 407 CG1 VAL A 73 4.699 24.411 39.404 1.00 14.44 C ANISOU 407 CG1 VAL A 73 1775 2176 1537 88 -99 -150 C ATOM 408 CG2 VAL A 73 6.434 22.811 40.260 1.00 11.38 C ANISOU 408 CG2 VAL A 73 1312 1751 1260 35 -10 -152 C ATOM 409 N ASP A 74 2.254 23.299 41.833 1.00 13.40 N ANISOU 409 N ASP A 74 1459 2027 1605 26 -182 -206 N ATOM 410 CA ASP A 74 0.851 23.697 41.833 1.00 16.34 C ANISOU 410 CA ASP A 74 1795 2415 1997 41 -242 -244 C ATOM 411 C ASP A 74 0.486 24.432 43.133 1.00 15.71 C ANISOU 411 C ASP A 74 1682 2326 1962 20 -218 -204 C ATOM 412 O ASP A 74 -0.189 25.472 43.094 1.00 13.92 O ANISOU 412 O ASP A 74 1455 2114 1719 51 -251 -201 O ATOM 413 CB ASP A 74 -0.079 22.498 41.633 1.00 17.70 C ANISOU 413 CB ASP A 74 1907 2580 2238 23 -275 -329 C ATOM 414 CG ASP A 74 0.187 21.738 40.317 1.00 36.21 C ANISOU 414 CG ASP A 74 4289 4935 4536 46 -307 -387 C ATOM 415 OD1 ASP A 74 0.692 22.325 39.331 1.00 36.77 O ANISOU 415 OD1 ASP A 74 4436 5030 4503 93 -324 -371 O ATOM 416 OD2 ASP A 74 -0.116 20.528 40.277 1.00 44.00 O ANISOU 416 OD2 ASP A 74 5233 5897 5587 15 -306 -450 O ATOM 417 N MET A 75 0.945 23.900 44.270 1.00 11.29 N ANISOU 417 N MET A 75 1103 1738 1449 -25 -161 -174 N ATOM 418 CA MET A 75 0.550 24.427 45.579 1.00 11.39 C ANISOU 418 CA MET A 75 1093 1739 1495 -47 -132 -145 C ATOM 419 C MET A 75 1.132 25.823 45.824 1.00 13.22 C ANISOU 419 C MET A 75 1366 1981 1675 -29 -126 -93 C ATOM 420 O MET A 75 0.495 26.676 46.432 1.00 12.46 O ANISOU 420 O MET A 75 1258 1886 1590 -26 -124 -87 O ATOM 421 CB MET A 75 0.979 23.487 46.712 1.00 9.29 C ANISOU 421 CB MET A 75 824 1437 1269 -89 -77 -120 C ATOM 422 CG MET A 75 0.216 22.160 46.779 1.00 15.42 C ANISOU 422 CG MET A 75 1562 2181 2117 -120 -60 -168 C ATOM 423 SD MET A 75 -1.567 22.490 46.871 1.00 30.46 S ANISOU 423 SD MET A 75 3389 4093 4090 -131 -71 -234 S ATOM 424 CE MET A 75 -2.058 22.097 45.186 1.00 80.36 C ANISOU 424 CE MET A 75 9677 10441 10414 -101 -155 -321 C ATOM 425 N ILE A 76 2.360 26.042 45.379 1.00 10.28 N ANISOU 425 N ILE A 76 1036 1610 1258 -23 -112 -61 N ATOM 426 CA ILE A 76 2.930 27.364 45.488 1.00 8.55 C ANISOU 426 CA ILE A 76 855 1392 1003 -14 -98 -20 C ATOM 427 C ILE A 76 2.088 28.325 44.671 1.00 16.59 C ANISOU 427 C ILE A 76 1899 2419 1985 31 -135 -29 C ATOM 428 O ILE A 76 1.689 29.383 45.158 1.00 16.30 O ANISOU 428 O ILE A 76 1868 2373 1951 41 -135 -13 O ATOM 429 CB ILE A 76 4.381 27.413 44.986 1.00 9.93 C ANISOU 429 CB ILE A 76 1060 1562 1150 -19 -65 3 C ATOM 430 CG1 ILE A 76 5.306 26.730 45.991 1.00 12.43 C ANISOU 430 CG1 ILE A 76 1347 1869 1506 -51 -43 15 C ATOM 431 CG2 ILE A 76 4.808 28.884 44.785 1.00 11.36 C ANISOU 431 CG2 ILE A 76 1286 1733 1298 -12 -42 36 C ATOM 432 CD1 ILE A 76 6.738 26.517 45.459 1.00 9.31 C ANISOU 432 CD1 ILE A 76 954 1471 1112 -54 -11 20 C ATOM 433 N GLY A 77 1.808 27.946 43.429 1.00 14.95 N ANISOU 433 N GLY A 77 1713 2226 1741 66 -171 -57 N ATOM 434 CA GLY A 77 0.980 28.757 42.559 1.00 15.20 C ANISOU 434 CA GLY A 77 1780 2268 1727 127 -227 -66 C ATOM 435 C GLY A 77 -0.385 29.038 43.166 1.00 19.70 C ANISOU 435 C GLY A 77 2287 2844 2356 142 -269 -100 C ATOM 436 O GLY A 77 -0.835 30.188 43.225 1.00 17.43 O ANISOU 436 O GLY A 77 2019 2547 2056 180 -287 -82 O ATOM 437 N ASN A 78 -1.052 27.986 43.624 1.00 13.55 N ANISOU 437 N ASN A 78 1428 2072 1649 110 -277 -152 N ATOM 438 CA ASN A 78 -2.383 28.150 44.207 1.00 16.82 C ANISOU 438 CA ASN A 78 1764 2489 2138 116 -301 -197 C ATOM 439 C ASN A 78 -2.366 29.077 45.397 1.00 13.80 C ANISOU 439 C ASN A 78 1381 2087 1777 99 -248 -158 C ATOM 440 O ASN A 78 -3.281 29.870 45.590 1.00 13.68 O ANISOU 440 O ASN A 78 1335 2071 1791 134 -271 -177 O ATOM 441 CB ASN A 78 -2.947 26.807 44.661 1.00 22.11 C ANISOU 441 CB ASN A 78 2352 3154 2895 64 -282 -255 C ATOM 442 CG ASN A 78 -3.187 25.876 43.518 1.00 29.45 C ANISOU 442 CG ASN A 78 3267 4100 3822 78 -341 -318 C ATOM 443 OD1 ASN A 78 -3.204 26.291 42.360 1.00 28.93 O ANISOU 443 OD1 ASN A 78 3246 4059 3685 140 -414 -330 O ATOM 444 ND2 ASN A 78 -3.373 24.600 43.829 1.00 34.05 N ANISOU 444 ND2 ASN A 78 3797 4664 4476 23 -310 -361 N ATOM 445 N THR A 79 -1.314 28.954 46.195 1.00 15.96 N ANISOU 445 N THR A 79 1686 2343 2035 51 -184 -110 N ATOM 446 CA THR A 79 -1.215 29.667 47.454 1.00 19.57 C ANISOU 446 CA THR A 79 2147 2782 2505 28 -134 -82 C ATOM 447 C THR A 79 -0.993 31.156 47.218 1.00 20.98 C ANISOU 447 C THR A 79 2378 2949 2644 66 -144 -51 C ATOM 448 O THR A 79 -1.681 31.990 47.807 1.00 13.64 O ANISOU 448 O THR A 79 1434 2007 1741 81 -136 -60 O ATOM 449 CB THR A 79 -0.090 29.081 48.330 1.00 14.22 C ANISOU 449 CB THR A 79 1494 2094 1816 -24 -84 -47 C ATOM 450 OG1 THR A 79 -0.462 27.756 48.732 1.00 16.73 O ANISOU 450 OG1 THR A 79 1774 2406 2177 -56 -63 -70 O ATOM 451 CG2 THR A 79 0.128 29.936 49.559 1.00 22.10 C ANISOU 451 CG2 THR A 79 2512 3077 2806 -41 -47 -25 C ATOM 452 N VAL A 80 -0.049 31.490 46.346 1.00 12.54 N ANISOU 452 N VAL A 80 1373 1876 1517 80 -150 -16 N ATOM 453 CA VAL A 80 0.230 32.895 46.059 1.00 14.37 C ANISOU 453 CA VAL A 80 1668 2079 1712 111 -143 20 C ATOM 454 C VAL A 80 -0.933 33.567 45.329 1.00 14.64 C ANISOU 454 C VAL A 80 1711 2112 1740 189 -203 4 C ATOM 455 O VAL A 80 -1.335 34.671 45.676 1.00 15.28 O ANISOU 455 O VAL A 80 1808 2164 1834 217 -199 13 O ATOM 456 CB VAL A 80 1.527 33.065 45.250 1.00 11.72 C ANISOU 456 CB VAL A 80 1401 1729 1321 102 -113 60 C ATOM 457 CG1 VAL A 80 1.797 34.549 44.981 1.00 14.04 C ANISOU 457 CG1 VAL A 80 1771 1977 1587 126 -88 100 C ATOM 458 CG2 VAL A 80 2.663 32.439 46.009 1.00 10.35 C ANISOU 458 CG2 VAL A 80 1202 1560 1170 37 -69 65 C ATOM 459 N LEU A 81 -1.468 32.899 44.319 1.00 11.64 N ANISOU 459 N LEU A 81 1321 1760 1342 229 -266 -26 N ATOM 460 CA LEU A 81 -2.601 33.438 43.585 1.00 14.99 C ANISOU 460 CA LEU A 81 1746 2189 1759 317 -348 -52 C ATOM 461 C LEU A 81 -3.852 33.597 44.450 1.00 16.83 C ANISOU 461 C LEU A 81 1879 2428 2088 327 -365 -105 C ATOM 462 O LEU A 81 -4.598 34.572 44.311 1.00 15.59 O ANISOU 462 O LEU A 81 1727 2255 1942 398 -406 -110 O ATOM 463 CB LEU A 81 -2.889 32.578 42.355 1.00 14.38 C ANISOU 463 CB LEU A 81 1674 2149 1639 356 -424 -90 C ATOM 464 CG LEU A 81 -1.705 32.468 41.391 1.00 19.61 C ANISOU 464 CG LEU A 81 2446 2805 2199 355 -396 -42 C ATOM 465 CD1 LEU A 81 -2.038 31.481 40.270 1.00 24.15 C ANISOU 465 CD1 LEU A 81 3024 3420 2731 389 -471 -95 C ATOM 466 CD2 LEU A 81 -1.306 33.838 40.829 1.00 20.82 C ANISOU 466 CD2 LEU A 81 2724 2914 2272 409 -379 29 C ATOM 467 N ASP A 82 -4.106 32.641 45.337 1.00 13.69 N ANISOU 467 N ASP A 82 1394 2046 1762 260 -326 -145 N ATOM 468 CA ASP A 82 -5.249 32.772 46.235 1.00 16.20 C ANISOU 468 CA ASP A 82 1617 2363 2177 258 -312 -197 C ATOM 469 C ASP A 82 -5.057 33.988 47.148 1.00 13.34 C ANISOU 469 C ASP A 82 1293 1964 1814 258 -255 -161 C ATOM 470 O ASP A 82 -5.987 34.731 47.426 1.00 15.11 O ANISOU 470 O ASP A 82 1476 2176 2091 304 -266 -191 O ATOM 471 CB ASP A 82 -5.421 31.513 47.087 1.00 16.73 C ANISOU 471 CB ASP A 82 1609 2438 2309 176 -251 -233 C ATOM 472 CG ASP A 82 -6.763 31.470 47.785 1.00 34.13 C ANISOU 472 CG ASP A 82 3704 4642 4624 173 -229 -303 C ATOM 473 OD1 ASP A 82 -7.784 31.791 47.132 1.00 30.10 O ANISOU 473 OD1 ASP A 82 3127 4145 4163 239 -306 -361 O ATOM 474 OD2 ASP A 82 -6.798 31.123 48.985 1.00 40.37 O ANISOU 474 OD2 ASP A 82 4474 5415 5452 108 -134 -303 O ATOM 475 N ALA A 83 -3.832 34.177 47.623 1.00 13.38 N ANISOU 475 N ALA A 83 1369 1949 1767 207 -195 -104 N ATOM 476 CA ALA A 83 -3.542 35.283 48.520 1.00 15.19 C ANISOU 476 CA ALA A 83 1636 2141 1994 197 -143 -80 C ATOM 477 C ALA A 83 -3.762 36.604 47.776 1.00 16.83 C ANISOU 477 C ALA A 83 1901 2314 2180 277 -182 -58 C ATOM 478 O ALA A 83 -4.378 37.522 48.309 1.00 15.05 O ANISOU 478 O ALA A 83 1666 2059 1994 308 -168 -74 O ATOM 479 CB ALA A 83 -2.122 35.169 49.060 1.00 14.25 C ANISOU 479 CB ALA A 83 1573 2013 1829 130 -90 -38 C ATOM 480 N LEU A 84 -3.294 36.679 46.533 1.00 16.80 N ANISOU 480 N LEU A 84 1965 2307 2111 315 -225 -21 N ATOM 481 CA LEU A 84 -3.530 37.865 45.701 1.00 18.18 C ANISOU 481 CA LEU A 84 2218 2440 2250 403 -264 11 C ATOM 482 C LEU A 84 -5.014 38.115 45.440 1.00 23.27 C ANISOU 482 C LEU A 84 2801 3096 2946 496 -346 -40 C ATOM 483 O LEU A 84 -5.471 39.265 45.428 1.00 21.20 O ANISOU 483 O LEU A 84 2573 2787 2697 566 -360 -28 O ATOM 484 CB LEU A 84 -2.803 37.740 44.366 1.00 16.59 C ANISOU 484 CB LEU A 84 2113 2236 1954 429 -288 59 C ATOM 485 CG LEU A 84 -1.296 37.934 44.459 1.00 19.13 C ANISOU 485 CG LEU A 84 2508 2526 2235 355 -200 113 C ATOM 486 CD1 LEU A 84 -0.609 37.441 43.189 1.00 18.98 C ANISOU 486 CD1 LEU A 84 2562 2518 2131 366 -206 145 C ATOM 487 CD2 LEU A 84 -0.980 39.404 44.724 1.00 21.59 C ANISOU 487 CD2 LEU A 84 2896 2759 2549 365 -148 154 C ATOM 488 N SER A 85 -5.771 37.043 45.228 1.00 16.06 N ANISOU 488 N SER A 85 1790 2238 2073 499 -400 -103 N ATOM 489 CA SER A 85 -7.187 37.184 44.901 1.00 20.42 C ANISOU 489 CA SER A 85 2259 2808 2691 589 -491 -169 C ATOM 490 C SER A 85 -8.059 37.569 46.087 1.00 19.27 C ANISOU 490 C SER A 85 2014 2650 2659 580 -443 -221 C ATOM 491 O SER A 85 -9.031 38.313 45.939 1.00 23.66 O ANISOU 491 O SER A 85 2530 3191 3268 672 -499 -256 O ATOM 492 CB SER A 85 -7.731 35.894 44.284 1.00 28.10 C ANISOU 492 CB SER A 85 3146 3842 3688 586 -564 -237 C ATOM 493 OG SER A 85 -7.229 35.727 42.977 1.00 43.13 O ANISOU 493 OG SER A 85 5147 5758 5481 633 -634 -204 O ATOM 494 N ARG A 86 -7.729 37.050 47.261 1.00 15.75 N ANISOU 494 N ARG A 86 1529 2207 2247 476 -340 -230 N ATOM 495 CA ARG A 86 -8.680 37.064 48.363 1.00 18.62 C ANISOU 495 CA ARG A 86 1785 2569 2719 457 -282 -295 C ATOM 496 C ARG A 86 -8.202 37.796 49.617 1.00 20.28 C ANISOU 496 C ARG A 86 2046 2739 2922 408 -175 -269 C ATOM 497 O ARG A 86 -8.965 37.971 50.561 1.00 19.94 O ANISOU 497 O ARG A 86 1933 2686 2955 398 -113 -321 O ATOM 498 CB ARG A 86 -9.051 35.627 48.740 1.00 17.86 C ANISOU 498 CB ARG A 86 1588 2513 2684 380 -247 -351 C ATOM 499 CG ARG A 86 -9.846 34.851 47.690 1.00 24.94 C ANISOU 499 CG ARG A 86 2396 3451 3629 421 -351 -417 C ATOM 500 CD ARG A 86 -9.970 33.387 48.146 1.00 32.66 C ANISOU 500 CD ARG A 86 3295 4449 4663 322 -289 -460 C ATOM 501 NE ARG A 86 -10.508 33.337 49.499 1.00 37.58 N ANISOU 501 NE ARG A 86 3855 5052 5372 264 -167 -492 N ATOM 502 CZ ARG A 86 -10.069 32.549 50.473 1.00 36.56 C ANISOU 502 CZ ARG A 86 3747 4910 5234 167 -53 -471 C ATOM 503 NH1 ARG A 86 -9.073 31.701 50.265 1.00 26.66 N ANISOU 503 NH1 ARG A 86 2563 3661 3905 117 -52 -420 N ATOM 504 NH2 ARG A 86 -10.651 32.608 51.667 1.00 47.75 N ANISOU 504 NH2 ARG A 86 5121 6305 6716 125 63 -501 N ATOM 505 N SER A 87 -6.944 38.208 49.640 1.00 14.93 N ANISOU 505 N SER A 87 1483 2035 2155 376 -149 -198 N ATOM 506 CA SER A 87 -6.411 38.873 50.820 1.00 13.07 C ANISOU 506 CA SER A 87 1296 1763 1907 327 -61 -184 C ATOM 507 C SER A 87 -6.028 40.318 50.511 1.00 15.23 C ANISOU 507 C SER A 87 1661 1973 2153 379 -70 -146 C ATOM 508 O SER A 87 -5.067 40.573 49.781 1.00 18.81 O ANISOU 508 O SER A 87 2201 2406 2539 377 -89 -86 O ATOM 509 CB SER A 87 -5.179 38.116 51.344 1.00 11.99 C ANISOU 509 CB SER A 87 1205 1644 1708 231 -15 -149 C ATOM 510 OG SER A 87 -4.508 38.909 52.312 1.00 17.49 O ANISOU 510 OG SER A 87 1963 2305 2379 195 44 -139 O ATOM 511 N GLN A 88 -6.775 41.259 51.075 1.00 15.17 N ANISOU 511 N GLN A 88 1636 1927 2202 423 -45 -181 N ATOM 512 CA GLN A 88 -6.476 42.674 50.895 1.00 13.84 C ANISOU 512 CA GLN A 88 1558 1681 2020 471 -41 -149 C ATOM 513 C GLN A 88 -5.105 42.989 51.477 1.00 15.91 C ANISOU 513 C GLN A 88 1907 1914 2226 383 23 -115 C ATOM 514 O GLN A 88 -4.363 43.824 50.955 1.00 21.47 O ANISOU 514 O GLN A 88 2704 2558 2896 393 24 -66 O ATOM 515 CB GLN A 88 -7.540 43.532 51.580 1.00 19.48 C ANISOU 515 CB GLN A 88 2227 2358 2818 528 -13 -207 C ATOM 516 CG GLN A 88 -7.403 45.017 51.272 1.00 32.17 C ANISOU 516 CG GLN A 88 3928 3871 4423 597 -16 -176 C ATOM 517 CD GLN A 88 -7.404 45.291 49.778 1.00 31.66 C ANISOU 517 CD GLN A 88 3926 3784 4320 689 -110 -114 C ATOM 518 OE1 GLN A 88 -8.411 45.096 49.102 1.00 38.24 O ANISOU 518 OE1 GLN A 88 4698 4643 5188 784 -195 -137 O ATOM 519 NE2 GLN A 88 -6.266 45.734 49.254 1.00 32.19 N ANISOU 519 NE2 GLN A 88 4117 3801 4312 662 -92 -40 N ATOM 520 N THR A 89 -4.762 42.301 52.557 1.00 14.18 N ANISOU 520 N THR A 89 1658 1732 1996 298 76 -142 N ATOM 521 CA THR A 89 -3.483 42.519 53.212 1.00 12.86 C ANISOU 521 CA THR A 89 1556 1548 1782 218 118 -128 C ATOM 522 C THR A 89 -2.329 42.124 52.310 1.00 15.93 C ANISOU 522 C THR A 89 1986 1945 2120 187 89 -70 C ATOM 523 O THR A 89 -1.358 42.862 52.171 1.00 17.43 O ANISOU 523 O THR A 89 2242 2086 2293 159 109 -46 O ATOM 524 CB THR A 89 -3.416 41.778 54.548 1.00 14.10 C ANISOU 524 CB THR A 89 1684 1749 1923 150 166 -168 C ATOM 525 OG1 THR A 89 -4.377 42.353 55.443 1.00 18.64 O ANISOU 525 OG1 THR A 89 2238 2302 2541 174 217 -224 O ATOM 526 CG2 THR A 89 -2.021 41.911 55.171 1.00 18.72 C ANISOU 526 CG2 THR A 89 2329 2327 2456 76 182 -160 C ATOM 527 N PHE A 90 -2.436 40.960 51.683 1.00 19.10 N ANISOU 527 N PHE A 90 2347 2406 2506 188 50 -55 N ATOM 528 CA PHE A 90 -1.394 40.530 50.775 1.00 14.85 C ANISOU 528 CA PHE A 90 1846 1878 1921 164 31 -7 C ATOM 529 C PHE A 90 -1.280 41.486 49.585 1.00 14.35 C ANISOU 529 C PHE A 90 1858 1755 1839 223 15 39 C ATOM 530 O PHE A 90 -0.175 41.823 49.160 1.00 16.69 O ANISOU 530 O PHE A 90 2217 2017 2107 188 45 77 O ATOM 531 CB PHE A 90 -1.628 39.091 50.312 1.00 10.80 C ANISOU 531 CB PHE A 90 1276 1432 1397 160 -7 -9 C ATOM 532 CG PHE A 90 -0.443 38.484 49.636 1.00 12.89 C ANISOU 532 CG PHE A 90 1570 1711 1615 122 -11 29 C ATOM 533 CD1 PHE A 90 0.744 38.298 50.334 1.00 14.46 C ANISOU 533 CD1 PHE A 90 1778 1913 1804 50 24 31 C ATOM 534 CD2 PHE A 90 -0.499 38.118 48.300 1.00 17.29 C ANISOU 534 CD2 PHE A 90 2147 2282 2142 164 -52 55 C ATOM 535 CE1 PHE A 90 1.856 37.748 49.713 1.00 21.21 C ANISOU 535 CE1 PHE A 90 2645 2780 2633 19 26 58 C ATOM 536 CE2 PHE A 90 0.607 37.555 47.679 1.00 17.27 C ANISOU 536 CE2 PHE A 90 2172 2290 2100 129 -40 83 C ATOM 537 CZ PHE A 90 1.783 37.372 48.388 1.00 18.44 C ANISOU 537 CZ PHE A 90 2314 2439 2254 56 3 84 C ATOM 538 N ARG A 91 -2.416 41.930 49.056 1.00 12.17 N ANISOU 538 N ARG A 91 1579 1462 1582 315 -28 36 N ATOM 539 CA ARG A 91 -2.409 42.879 47.944 1.00 19.34 C ANISOU 539 CA ARG A 91 2583 2307 2460 389 -48 88 C ATOM 540 C ARG A 91 -1.784 44.217 48.343 1.00 21.79 C ANISOU 540 C ARG A 91 2973 2521 2785 367 21 107 C ATOM 541 O ARG A 91 -1.084 44.849 47.548 1.00 20.44 O ANISOU 541 O ARG A 91 2903 2286 2578 373 49 164 O ATOM 542 CB ARG A 91 -3.818 43.099 47.390 1.00 18.38 C ANISOU 542 CB ARG A 91 2435 2187 2361 508 -127 71 C ATOM 543 CG ARG A 91 -4.324 41.956 46.521 1.00 16.95 C ANISOU 543 CG ARG A 91 2203 2082 2154 545 -211 59 C ATOM 544 CD ARG A 91 -5.592 42.339 45.760 1.00 25.92 C ANISOU 544 CD ARG A 91 3328 3214 3306 679 -311 42 C ATOM 545 NE ARG A 91 -6.656 42.805 46.640 1.00 23.39 N ANISOU 545 NE ARG A 91 2918 2883 3086 714 -309 -20 N ATOM 546 CZ ARG A 91 -7.570 42.017 47.199 1.00 29.01 C ANISOU 546 CZ ARG A 91 3488 3656 3878 702 -324 -100 C ATOM 547 NH1 ARG A 91 -7.561 40.705 46.971 1.00 20.61 N ANISOU 547 NH1 ARG A 91 2359 2665 2808 654 -349 -126 N ATOM 548 NH2 ARG A 91 -8.504 42.544 47.985 1.00 26.56 N ANISOU 548 NH2 ARG A 91 3102 3327 3662 735 -304 -158 N ATOM 549 N ASP A 92 -2.044 44.651 49.573 1.00 17.19 N ANISOU 549 N ASP A 92 2352 1923 2256 339 57 55 N ATOM 550 CA ASP A 92 -1.423 45.866 50.092 1.00 19.33 C ANISOU 550 CA ASP A 92 2690 2104 2551 305 123 53 C ATOM 551 C ASP A 92 0.083 45.674 50.269 1.00 20.39 C ANISOU 551 C ASP A 92 2844 2237 2666 196 172 62 C ATOM 552 O ASP A 92 0.874 46.561 49.942 1.00 17.07 O ANISOU 552 O ASP A 92 2499 1732 2253 169 224 89 O ATOM 553 CB ASP A 92 -2.046 46.271 51.427 1.00 19.63 C ANISOU 553 CB ASP A 92 2681 2135 2642 297 150 -19 C ATOM 554 CG ASP A 92 -3.524 46.640 51.305 1.00 31.76 C ANISOU 554 CG ASP A 92 4184 3659 4222 407 115 -40 C ATOM 555 OD1 ASP A 92 -3.931 47.147 50.235 1.00 34.35 O ANISOU 555 OD1 ASP A 92 4564 3942 4546 500 73 6 O ATOM 556 OD2 ASP A 92 -4.281 46.420 52.286 1.00 30.75 O ANISOU 556 OD2 ASP A 92 3981 3566 4135 405 130 -105 O ATOM 557 N ALA A 93 0.487 44.522 50.798 1.00 14.83 N ANISOU 557 N ALA A 93 2070 1620 1947 134 158 36 N ATOM 558 CA ALA A 93 1.914 44.266 50.960 1.00 14.71 C ANISOU 558 CA ALA A 93 2055 1610 1924 42 189 35 C ATOM 559 C ALA A 93 2.581 44.219 49.588 1.00 19.60 C ANISOU 559 C ALA A 93 2728 2204 2515 47 205 99 C ATOM 560 O ALA A 93 3.654 44.781 49.383 1.00 17.90 O ANISOU 560 O ALA A 93 2551 1932 2318 -10 263 110 O ATOM 561 CB ALA A 93 2.164 42.970 51.742 1.00 12.28 C ANISOU 561 CB ALA A 93 1670 1396 1598 -6 160 2 C ATOM 562 N VAL A 94 1.926 43.570 48.636 1.00 15.85 N ANISOU 562 N VAL A 94 2256 1768 1997 113 159 136 N ATOM 563 CA VAL A 94 2.504 43.426 47.309 1.00 14.82 C ANISOU 563 CA VAL A 94 2191 1622 1819 125 176 195 C ATOM 564 C VAL A 94 2.591 44.776 46.609 1.00 16.81 C ANISOU 564 C VAL A 94 2562 1760 2064 161 228 246 C ATOM 565 O VAL A 94 3.587 45.101 45.962 1.00 16.45 O ANISOU 565 O VAL A 94 2583 1661 2006 120 301 284 O ATOM 566 CB VAL A 94 1.688 42.440 46.451 1.00 16.24 C ANISOU 566 CB VAL A 94 2355 1870 1946 197 101 210 C ATOM 567 CG1 VAL A 94 1.961 42.671 44.969 1.00 14.01 C ANISOU 567 CG1 VAL A 94 2183 1549 1592 244 115 276 C ATOM 568 CG2 VAL A 94 2.001 40.998 46.874 1.00 12.84 C ANISOU 568 CG2 VAL A 94 1829 1531 1517 142 77 175 C ATOM 569 N SER A 95 1.547 45.574 46.757 1.00 17.52 N ANISOU 569 N SER A 95 2682 1806 2169 239 200 246 N ATOM 570 CA SER A 95 1.532 46.876 46.125 1.00 21.21 C ANISOU 570 CA SER A 95 3276 2153 2630 288 246 301 C ATOM 571 C SER A 95 2.551 47.774 46.793 1.00 20.80 C ANISOU 571 C SER A 95 3245 2014 2642 190 346 280 C ATOM 572 O SER A 95 3.139 48.640 46.154 1.00 20.46 O ANISOU 572 O SER A 95 3311 1865 2599 180 427 331 O ATOM 573 CB SER A 95 0.148 47.515 46.203 1.00 27.52 C ANISOU 573 CB SER A 95 4091 2923 3444 405 185 296 C ATOM 574 OG SER A 95 0.192 48.820 45.656 1.00 38.74 O ANISOU 574 OG SER A 95 5647 4211 4860 456 234 354 O ATOM 575 N TYR A 96 2.760 47.580 48.086 1.00 17.54 N ANISOU 575 N TYR A 96 2735 1643 2286 118 343 203 N ATOM 576 CA TYR A 96 3.757 48.381 48.760 1.00 15.23 C ANISOU 576 CA TYR A 96 2449 1277 2060 22 422 164 C ATOM 577 C TYR A 96 5.106 48.148 48.099 1.00 17.98 C ANISOU 577 C TYR A 96 2811 1610 2410 -59 491 189 C ATOM 578 O TYR A 96 5.844 49.087 47.796 1.00 24.26 O ANISOU 578 O TYR A 96 3675 2296 3248 -108 586 204 O ATOM 579 CB TYR A 96 3.849 48.025 50.237 1.00 17.08 C ANISOU 579 CB TYR A 96 2580 1577 2331 -39 391 71 C ATOM 580 CG TYR A 96 5.053 48.667 50.897 1.00 17.27 C ANISOU 580 CG TYR A 96 2595 1545 2423 -147 452 14 C ATOM 581 CD1 TYR A 96 4.999 49.971 51.360 1.00 20.84 C ANISOU 581 CD1 TYR A 96 3098 1887 2933 -160 501 -20 C ATOM 582 CD2 TYR A 96 6.249 47.966 51.036 1.00 23.52 C ANISOU 582 CD2 TYR A 96 3318 2390 3229 -235 456 -15 C ATOM 583 CE1 TYR A 96 6.108 50.574 51.955 1.00 20.22 C ANISOU 583 CE1 TYR A 96 3002 1754 2928 -266 553 -88 C ATOM 584 CE2 TYR A 96 7.362 48.553 51.627 1.00 20.41 C ANISOU 584 CE2 TYR A 96 2897 1948 2911 -334 499 -83 C ATOM 585 CZ TYR A 96 7.282 49.853 52.092 1.00 21.14 C ANISOU 585 CZ TYR A 96 3038 1932 3061 -353 546 -123 C ATOM 586 OH TYR A 96 8.389 50.436 52.684 1.00 27.13 O ANISOU 586 OH TYR A 96 3760 2641 3906 -457 584 -207 O ATOM 587 N GLY A 97 5.420 46.881 47.872 1.00 16.81 N ANISOU 587 N GLY A 97 2596 1566 2223 -76 452 189 N ATOM 588 CA GLY A 97 6.716 46.522 47.334 1.00 16.15 C ANISOU 588 CA GLY A 97 2502 1482 2153 -153 517 198 C ATOM 589 C GLY A 97 6.904 47.083 45.948 1.00 19.67 C ANISOU 589 C GLY A 97 3077 1837 2557 -123 601 284 C ATOM 590 O GLY A 97 7.974 47.584 45.601 1.00 20.28 O ANISOU 590 O GLY A 97 3187 1839 2681 -199 711 290 O ATOM 591 N ILE A 98 5.858 47.001 45.141 1.00 17.60 N ANISOU 591 N ILE A 98 2896 1583 2210 -10 550 346 N ATOM 592 CA ILE A 98 5.944 47.494 43.775 1.00 19.96 C ANISOU 592 CA ILE A 98 3347 1799 2440 39 618 437 C ATOM 593 C ILE A 98 6.186 48.998 43.717 1.00 26.00 C ANISOU 593 C ILE A 98 4225 2405 3250 24 722 469 C ATOM 594 O ILE A 98 6.949 49.468 42.880 1.00 27.39 O ANISOU 594 O ILE A 98 4506 2489 3413 -9 844 524 O ATOM 595 CB ILE A 98 4.680 47.133 42.981 1.00 19.39 C ANISOU 595 CB ILE A 98 3337 1770 2261 180 513 486 C ATOM 596 CG1 ILE A 98 4.673 45.630 42.670 1.00 18.19 C ANISOU 596 CG1 ILE A 98 3104 1751 2057 183 443 465 C ATOM 597 CG2 ILE A 98 4.588 47.969 41.702 1.00 20.45 C ANISOU 597 CG2 ILE A 98 3666 1793 2310 258 571 586 C ATOM 598 CD1 ILE A 98 3.300 45.118 42.260 1.00 23.59 C ANISOU 598 CD1 ILE A 98 3790 2503 2672 307 309 471 C ATOM 599 N HIS A 99 5.545 49.746 44.613 1.00 26.99 N ANISOU 599 N HIS A 99 4332 2490 3432 45 688 432 N ATOM 600 CA HIS A 99 5.597 51.202 44.561 1.00 30.01 C ANISOU 600 CA HIS A 99 4831 2710 3860 47 779 462 C ATOM 601 C HIS A 99 6.646 51.828 45.476 1.00 27.45 C ANISOU 601 C HIS A 99 4447 2321 3664 -93 872 385 C ATOM 602 O HIS A 99 6.885 53.025 45.407 1.00 27.32 O ANISOU 602 O HIS A 99 4524 2154 3701 -116 970 403 O ATOM 603 CB HIS A 99 4.219 51.801 44.864 1.00 35.54 C ANISOU 603 CB HIS A 99 5567 3383 4551 169 693 468 C ATOM 604 CG HIS A 99 3.168 51.419 43.871 1.00 37.44 C ANISOU 604 CG HIS A 99 5880 3666 4681 319 598 539 C ATOM 605 ND1 HIS A 99 2.169 50.511 44.156 1.00 38.46 N ANISOU 605 ND1 HIS A 99 5903 3927 4784 387 461 498 N ATOM 606 CD2 HIS A 99 2.971 51.805 42.588 1.00 40.13 C ANISOU 606 CD2 HIS A 99 6388 3932 4926 413 617 642 C ATOM 607 CE1 HIS A 99 1.398 50.360 43.094 1.00 34.25 C ANISOU 607 CE1 HIS A 99 5453 3403 4155 517 389 562 C ATOM 608 NE2 HIS A 99 1.864 51.131 42.127 1.00 37.25 N ANISOU 608 NE2 HIS A 99 6009 3664 4482 541 475 653 N ATOM 609 N ASN A 100 7.277 51.029 46.327 1.00 20.75 N ANISOU 609 N ASN A 100 3444 1577 2864 -184 837 297 N ATOM 610 CA ASN A 100 8.244 51.577 47.271 1.00 21.15 C ANISOU 610 CA ASN A 100 3421 1579 3036 -310 896 204 C ATOM 611 C ASN A 100 9.589 50.853 47.248 1.00 23.27 C ANISOU 611 C ASN A 100 3586 1903 3353 -422 938 158 C ATOM 612 O ASN A 100 10.235 50.683 48.282 1.00 23.86 O ANISOU 612 O ASN A 100 3537 2022 3506 -506 907 55 O ATOM 613 CB ASN A 100 7.666 51.597 48.684 1.00 19.85 C ANISOU 613 CB ASN A 100 3169 1472 2903 -305 800 112 C ATOM 614 CG ASN A 100 6.379 52.406 48.773 1.00 27.59 C ANISOU 614 CG ASN A 100 4236 2386 3861 -198 772 141 C ATOM 615 OD1 ASN A 100 6.390 53.566 49.180 1.00 34.97 O ANISOU 615 OD1 ASN A 100 5221 3201 4865 -219 829 111 O ATOM 616 ND2 ASN A 100 5.269 51.801 48.375 1.00 20.95 N ANISOU 616 ND2 ASN A 100 3407 1620 2934 -82 685 192 N ATOM 617 N GLU A 101 9.988 50.413 46.061 1.00 21.64 N ANISOU 617 N GLU A 101 3432 1694 3094 -415 1002 232 N ATOM 618 CA GLU A 101 11.363 49.992 45.818 1.00 22.68 C ANISOU 618 CA GLU A 101 3485 1837 3293 -524 1087 195 C ATOM 619 C GLU A 101 11.780 48.703 46.536 1.00 26.74 C ANISOU 619 C GLU A 101 3829 2507 3822 -554 981 117 C ATOM 620 O GLU A 101 12.942 48.534 46.903 1.00 27.86 O ANISOU 620 O GLU A 101 3859 2661 4066 -655 1016 40 O ATOM 621 CB GLU A 101 12.314 51.134 46.172 1.00 27.16 C ANISOU 621 CB GLU A 101 4031 2299 3991 -626 1187 129 C ATOM 622 CG GLU A 101 12.138 52.375 45.300 1.00 44.90 C ANISOU 622 CG GLU A 101 6430 4422 6209 -582 1285 201 C ATOM 623 CD GLU A 101 12.583 52.151 43.860 1.00 59.31 C ANISOU 623 CD GLU A 101 8333 6244 7958 -555 1372 278 C ATOM 624 OE1 GLU A 101 13.607 52.743 43.456 1.00 63.83 O ANISOU 624 OE1 GLU A 101 8899 6760 8594 -618 1485 251 O ATOM 625 OE2 GLU A 101 11.914 51.385 43.132 1.00 65.25 O ANISOU 625 OE2 GLU A 101 9156 7049 8588 -467 1327 357 O ATOM 626 N LYS A 102 10.834 47.794 46.738 1.00 23.81 N ANISOU 626 N LYS A 102 3438 2250 3358 -465 851 135 N ATOM 627 CA LYS A 102 11.171 46.463 47.231 1.00 25.20 C ANISOU 627 CA LYS A 102 3482 2563 3530 -478 761 84 C ATOM 628 C LYS A 102 11.056 45.486 46.064 1.00 22.58 C ANISOU 628 C LYS A 102 3186 2285 3109 -425 766 155 C ATOM 629 O LYS A 102 11.193 45.878 44.915 1.00 24.38 O ANISOU 629 O LYS A 102 3521 2440 3301 -413 866 223 O ATOM 630 CB LYS A 102 10.240 46.047 48.375 1.00 18.64 C ANISOU 630 CB LYS A 102 2600 1818 2665 -429 625 45 C ATOM 631 CG LYS A 102 10.156 47.064 49.518 1.00 16.16 C ANISOU 631 CG LYS A 102 2277 1450 2415 -465 616 -25 C ATOM 632 CD LYS A 102 11.537 47.382 50.079 1.00 24.15 C ANISOU 632 CD LYS A 102 3200 2435 3542 -580 655 -117 C ATOM 633 CE LYS A 102 11.442 48.143 51.388 1.00 29.18 C ANISOU 633 CE LYS A 102 3812 3047 4227 -612 613 -208 C ATOM 634 NZ LYS A 102 11.063 49.557 51.168 1.00 39.36 N ANISOU 634 NZ LYS A 102 5205 4196 5553 -614 699 -191 N ATOM 635 N VAL A 103 10.781 44.221 46.351 1.00 20.23 N ANISOU 635 N VAL A 103 2810 2107 2767 -390 664 138 N ATOM 636 CA VAL A 103 10.665 43.235 45.283 1.00 16.13 C ANISOU 636 CA VAL A 103 2321 1641 2168 -342 662 190 C ATOM 637 C VAL A 103 9.251 43.167 44.691 1.00 21.64 C ANISOU 637 C VAL A 103 3117 2352 2755 -230 599 255 C ATOM 638 O VAL A 103 8.259 43.105 45.424 1.00 18.60 O ANISOU 638 O VAL A 103 2706 2004 2356 -184 505 238 O ATOM 639 CB VAL A 103 11.108 41.830 45.763 1.00 19.15 C ANISOU 639 CB VAL A 103 2575 2135 2565 -358 589 140 C ATOM 640 CG1 VAL A 103 10.822 40.772 44.693 1.00 20.17 C ANISOU 640 CG1 VAL A 103 2738 2317 2607 -300 578 185 C ATOM 641 CG2 VAL A 103 12.602 41.839 46.128 1.00 16.41 C ANISOU 641 CG2 VAL A 103 2125 1778 2333 -455 647 73 C ATOM 642 N HIS A 104 9.173 43.197 43.362 1.00 14.63 N ANISOU 642 N HIS A 104 2340 1431 1787 -185 654 324 N ATOM 643 CA HIS A 104 7.937 42.922 42.638 1.00 15.62 C ANISOU 643 CA HIS A 104 2549 1586 1802 -72 575 374 C ATOM 644 C HIS A 104 7.722 41.423 42.735 1.00 15.57 C ANISOU 644 C HIS A 104 2446 1698 1770 -56 485 338 C ATOM 645 O HIS A 104 8.617 40.647 42.414 1.00 21.02 O ANISOU 645 O HIS A 104 3096 2423 2470 -101 527 323 O ATOM 646 CB HIS A 104 8.089 43.329 41.172 1.00 24.93 C ANISOU 646 CB HIS A 104 3888 2697 2889 -30 661 453 C ATOM 647 CG HIS A 104 6.867 43.086 40.339 1.00 35.52 C ANISOU 647 CG HIS A 104 5322 4068 4106 98 564 499 C ATOM 648 ND1 HIS A 104 6.203 41.877 40.317 1.00 33.60 N ANISOU 648 ND1 HIS A 104 5005 3936 3825 143 446 464 N ATOM 649 CD2 HIS A 104 6.203 43.896 39.478 1.00 37.11 C ANISOU 649 CD2 HIS A 104 5685 4199 4217 193 563 571 C ATOM 650 CE1 HIS A 104 5.177 41.954 39.486 1.00 30.44 C ANISOU 650 CE1 HIS A 104 4703 3540 3323 257 370 501 C ATOM 651 NE2 HIS A 104 5.154 43.168 38.965 1.00 36.49 N ANISOU 651 NE2 HIS A 104 5615 4200 4049 297 432 569 N ATOM 652 N ILE A 105 6.545 41.014 43.178 1.00 18.24 N ANISOU 652 N ILE A 105 2747 2094 2088 5 371 321 N ATOM 653 CA ILE A 105 6.307 39.602 43.481 1.00 16.91 C ANISOU 653 CA ILE A 105 2480 2027 1918 7 292 280 C ATOM 654 C ILE A 105 6.520 38.690 42.267 1.00 15.42 C ANISOU 654 C ILE A 105 2329 1874 1656 34 298 298 C ATOM 655 O ILE A 105 6.939 37.547 42.409 1.00 17.05 O ANISOU 655 O ILE A 105 2458 2141 1881 4 283 264 O ATOM 656 CB ILE A 105 4.909 39.380 44.084 1.00 12.66 C ANISOU 656 CB ILE A 105 1900 1533 1379 65 188 256 C ATOM 657 CG1 ILE A 105 4.765 37.935 44.583 1.00 17.64 C ANISOU 657 CG1 ILE A 105 2426 2251 2026 47 130 212 C ATOM 658 CG2 ILE A 105 3.838 39.741 43.076 1.00 17.07 C ANISOU 658 CG2 ILE A 105 2547 2076 1863 167 139 293 C ATOM 659 CD1 ILE A 105 3.561 37.718 45.489 1.00 20.28 C ANISOU 659 CD1 ILE A 105 2698 2619 2388 74 59 177 C ATOM 660 N GLY A 106 6.240 39.204 41.076 1.00 15.87 N ANISOU 660 N GLY A 106 2516 1888 1624 96 321 352 N ATOM 661 CA GLY A 106 6.482 38.450 39.857 1.00 20.00 C ANISOU 661 CA GLY A 106 3099 2438 2060 125 336 367 C ATOM 662 C GLY A 106 7.938 38.109 39.578 1.00 24.64 C ANISOU 662 C GLY A 106 3672 3014 2678 45 456 361 C ATOM 663 O GLY A 106 8.224 37.240 38.751 1.00 19.16 O ANISOU 663 O GLY A 106 2997 2354 1927 57 470 355 O ATOM 664 N CYS A 107 8.869 38.782 40.251 1.00 13.71 N ANISOU 664 N CYS A 107 2243 1579 1388 -38 542 353 N ATOM 665 CA CYS A 107 10.286 38.480 40.059 1.00 18.53 C ANISOU 665 CA CYS A 107 2809 2177 2055 -117 656 332 C ATOM 666 C CYS A 107 10.756 37.290 40.896 1.00 19.10 C ANISOU 666 C CYS A 107 2721 2328 2207 -158 601 263 C ATOM 667 O CYS A 107 11.842 36.754 40.663 1.00 23.79 O ANISOU 667 O CYS A 107 3262 2931 2847 -205 672 236 O ATOM 668 CB CYS A 107 11.155 39.695 40.406 1.00 22.08 C ANISOU 668 CB CYS A 107 3263 2535 2592 -195 773 336 C ATOM 669 SG CYS A 107 10.901 41.137 39.327 1.00 31.66 S ANISOU 669 SG CYS A 107 4688 3622 3719 -158 884 429 S ATOM 670 N ILE A 108 9.963 36.899 41.886 1.00 17.20 N ANISOU 670 N ILE A 108 2410 2139 1987 -137 481 237 N ATOM 671 CA ILE A 108 10.385 35.856 42.823 1.00 15.96 C ANISOU 671 CA ILE A 108 2120 2043 1900 -170 427 182 C ATOM 672 C ILE A 108 10.247 34.441 42.252 1.00 16.54 C ANISOU 672 C ILE A 108 2176 2176 1933 -135 390 168 C ATOM 673 O ILE A 108 9.174 34.072 41.772 1.00 15.39 O ANISOU 673 O ILE A 108 2080 2055 1713 -75 328 182 O ATOM 674 CB ILE A 108 9.581 35.934 44.124 1.00 14.38 C ANISOU 674 CB ILE A 108 1869 1869 1727 -162 331 162 C ATOM 675 CG1 ILE A 108 9.776 37.319 44.768 1.00 13.57 C ANISOU 675 CG1 ILE A 108 1780 1706 1672 -200 367 160 C ATOM 676 CG2 ILE A 108 9.967 34.772 45.061 1.00 12.38 C ANISOU 676 CG2 ILE A 108 1506 1674 1523 -182 273 117 C ATOM 677 CD1 ILE A 108 8.849 37.592 45.918 1.00 16.31 C ANISOU 677 CD1 ILE A 108 2104 2068 2027 -183 289 144 C ATOM 678 N LYS A 109 11.332 33.662 42.311 1.00 12.67 N ANISOU 678 N LYS A 109 1609 1705 1501 -172 425 134 N ATOM 679 CA LYS A 109 11.296 32.234 41.930 1.00 10.94 C ANISOU 679 CA LYS A 109 1361 1535 1263 -143 391 112 C ATOM 680 C LYS A 109 11.348 31.392 43.200 1.00 11.64 C ANISOU 680 C LYS A 109 1343 1662 1419 -153 309 77 C ATOM 681 O LYS A 109 11.689 31.908 44.272 1.00 12.89 O ANISOU 681 O LYS A 109 1448 1813 1636 -185 290 64 O ATOM 682 CB LYS A 109 12.451 31.894 40.977 1.00 11.67 C ANISOU 682 CB LYS A 109 1454 1613 1366 -163 497 98 C ATOM 683 CG LYS A 109 12.340 32.604 39.610 1.00 26.68 C ANISOU 683 CG LYS A 109 3494 3472 3170 -144 589 141 C ATOM 684 CD LYS A 109 13.239 31.996 38.541 1.00 43.15 C ANISOU 684 CD LYS A 109 5600 5555 5241 -150 695 124 C ATOM 685 CE LYS A 109 14.717 32.216 38.841 1.00 57.38 C ANISOU 685 CE LYS A 109 7304 7328 7170 -222 804 90 C ATOM 686 NZ LYS A 109 15.592 31.832 37.688 1.00 60.32 N ANISOU 686 NZ LYS A 109 7708 7684 7527 -231 941 75 N ATOM 687 N TYR A 110 11.019 30.104 43.089 1.00 11.81 N ANISOU 687 N TYR A 110 1344 1718 1426 -123 261 61 N ATOM 688 CA TYR A 110 10.860 29.249 44.262 1.00 10.90 C ANISOU 688 CA TYR A 110 1158 1628 1355 -121 185 42 C ATOM 689 C TYR A 110 11.764 28.027 44.214 1.00 11.95 C ANISOU 689 C TYR A 110 1230 1772 1537 -117 191 13 C ATOM 690 O TYR A 110 12.037 27.502 43.140 1.00 12.49 O ANISOU 690 O TYR A 110 1319 1839 1586 -104 237 1 O ATOM 691 CB TYR A 110 9.393 28.834 44.404 1.00 10.81 C ANISOU 691 CB TYR A 110 1177 1633 1296 -89 118 50 C ATOM 692 CG TYR A 110 8.518 30.054 44.514 1.00 15.31 C ANISOU 692 CG TYR A 110 1795 2190 1832 -83 108 73 C ATOM 693 CD1 TYR A 110 8.212 30.603 45.755 1.00 15.94 C ANISOU 693 CD1 TYR A 110 1852 2268 1939 -99 78 75 C ATOM 694 CD2 TYR A 110 8.063 30.703 43.377 1.00 12.01 C ANISOU 694 CD2 TYR A 110 1454 1758 1350 -55 129 92 C ATOM 695 CE1 TYR A 110 7.425 31.757 45.860 1.00 17.06 C ANISOU 695 CE1 TYR A 110 2034 2390 2057 -89 74 91 C ATOM 696 CE2 TYR A 110 7.295 31.853 43.463 1.00 12.73 C ANISOU 696 CE2 TYR A 110 1592 1829 1415 -38 117 115 C ATOM 697 CZ TYR A 110 6.977 32.374 44.705 1.00 15.88 C ANISOU 697 CZ TYR A 110 1955 2223 1855 -56 92 112 C ATOM 698 OH TYR A 110 6.218 33.511 44.772 1.00 18.99 O ANISOU 698 OH TYR A 110 2393 2591 2231 -34 84 130 O ATOM 699 N ARG A 111 12.238 27.592 45.382 1.00 9.94 N ANISOU 699 N ARG A 111 909 1527 1341 -122 142 -1 N ATOM 700 CA ARG A 111 13.115 26.417 45.466 1.00 10.89 C ANISOU 700 CA ARG A 111 968 1652 1518 -104 134 -28 C ATOM 701 C ARG A 111 12.778 25.556 46.672 1.00 12.61 C ANISOU 701 C ARG A 111 1170 1877 1745 -80 51 -20 C ATOM 702 O ARG A 111 12.241 26.051 47.653 1.00 14.21 O ANISOU 702 O ARG A 111 1390 2084 1927 -88 8 -3 O ATOM 703 CB ARG A 111 14.567 26.847 45.645 1.00 12.98 C ANISOU 703 CB ARG A 111 1152 1913 1866 -128 167 -60 C ATOM 704 CG ARG A 111 15.049 27.874 44.679 1.00 17.88 C ANISOU 704 CG ARG A 111 1788 2514 2492 -166 269 -65 C ATOM 705 CD ARG A 111 16.454 28.272 45.063 1.00 15.57 C ANISOU 705 CD ARG A 111 1392 2215 2311 -199 297 -112 C ATOM 706 NE ARG A 111 16.996 29.258 44.148 1.00 20.28 N ANISOU 706 NE ARG A 111 2001 2777 2926 -247 421 -119 N ATOM 707 CZ ARG A 111 18.254 29.662 44.183 1.00 23.28 C ANISOU 707 CZ ARG A 111 2284 3142 3419 -289 482 -170 C ATOM 708 NH1 ARG A 111 19.072 29.158 45.098 1.00 19.47 N ANISOU 708 NH1 ARG A 111 1680 2684 3035 -277 406 -223 N ATOM 709 NH2 ARG A 111 18.696 30.562 43.317 1.00 31.11 N ANISOU 709 NH2 ARG A 111 3301 4091 4428 -340 618 -170 N ATOM 710 N ASN A 112 13.150 24.278 46.617 1.00 11.90 N ANISOU 710 N ASN A 112 1056 1780 1686 -48 38 -33 N ATOM 711 CA ASN A 112 13.045 23.399 47.782 1.00 11.03 C ANISOU 711 CA ASN A 112 943 1662 1588 -18 -31 -19 C ATOM 712 C ASN A 112 14.417 22.948 48.246 1.00 14.19 C ANISOU 712 C ASN A 112 1270 2062 2061 12 -63 -43 C ATOM 713 O ASN A 112 14.748 21.770 48.110 1.00 12.08 O ANISOU 713 O ASN A 112 989 1774 1825 52 -71 -50 O ATOM 714 CB ASN A 112 12.228 22.142 47.472 1.00 12.59 C ANISOU 714 CB ASN A 112 1181 1836 1768 2 -30 -10 C ATOM 715 CG ASN A 112 10.776 22.443 47.165 1.00 15.59 C ANISOU 715 CG ASN A 112 1615 2218 2090 -21 -19 2 C ATOM 716 OD1 ASN A 112 10.215 21.901 46.207 1.00 14.63 O ANISOU 716 OD1 ASN A 112 1513 2089 1957 -19 3 -17 O ATOM 717 ND2 ASN A 112 10.158 23.325 47.960 1.00 11.69 N ANISOU 717 ND2 ASN A 112 1140 1735 1565 -39 -39 24 N ATOM 718 N GLU A 113 15.220 23.866 48.780 1.00 16.48 N ANISOU 718 N GLU A 113 1506 2369 2385 -4 -84 -65 N ATOM 719 CA GLU A 113 16.566 23.513 49.238 1.00 16.60 C ANISOU 719 CA GLU A 113 1432 2391 2485 29 -130 -104 C ATOM 720 C GLU A 113 16.518 22.905 50.626 1.00 15.28 C ANISOU 720 C GLU A 113 1289 2222 2293 82 -238 -81 C ATOM 721 O GLU A 113 15.827 23.409 51.504 1.00 16.44 O ANISOU 721 O GLU A 113 1497 2377 2374 71 -276 -54 O ATOM 722 CB GLU A 113 17.500 24.736 49.244 1.00 15.81 C ANISOU 722 CB GLU A 113 1250 2307 2449 -14 -113 -152 C ATOM 723 CG GLU A 113 17.801 25.283 47.863 1.00 25.79 C ANISOU 723 CG GLU A 113 2494 3561 3744 -61 11 -173 C ATOM 724 CD GLU A 113 18.658 26.543 47.878 1.00 25.99 C ANISOU 724 CD GLU A 113 2445 3587 3843 -118 51 -220 C ATOM 725 OE1 GLU A 113 18.976 27.062 48.971 1.00 25.58 O ANISOU 725 OE1 GLU A 113 2353 3550 3818 -123 -30 -246 O ATOM 726 OE2 GLU A 113 19.012 27.010 46.777 1.00 23.76 O ANISOU 726 OE2 GLU A 113 2153 3287 3589 -159 169 -234 O ATOM 727 N TYR A 114 17.249 21.812 50.813 1.00 14.23 N ANISOU 727 N TYR A 114 1120 2074 2211 147 -283 -91 N ATOM 728 CA TYR A 114 17.343 21.156 52.109 1.00 13.73 C ANISOU 728 CA TYR A 114 1095 2002 2118 214 -390 -64 C ATOM 729 C TYR A 114 18.763 21.086 52.578 1.00 15.09 C ANISOU 729 C TYR A 114 1164 2194 2377 269 -477 -118 C ATOM 730 O TYR A 114 19.693 21.360 51.816 1.00 17.28 O ANISOU 730 O TYR A 114 1325 2484 2756 252 -437 -180 O ATOM 731 CB TYR A 114 16.766 19.739 52.059 1.00 12.75 C ANISOU 731 CB TYR A 114 1048 1827 1967 261 -380 -15 C ATOM 732 CG TYR A 114 15.274 19.774 52.187 1.00 13.68 C ANISOU 732 CG TYR A 114 1275 1928 1995 218 -334 37 C ATOM 733 CD1 TYR A 114 14.497 20.417 51.229 1.00 11.15 C ANISOU 733 CD1 TYR A 114 957 1620 1659 150 -252 28 C ATOM 734 CD2 TYR A 114 14.635 19.190 53.274 1.00 15.32 C ANISOU 734 CD2 TYR A 114 1584 2104 2135 250 -371 94 C ATOM 735 CE1 TYR A 114 13.136 20.485 51.338 1.00 11.84 C ANISOU 735 CE1 TYR A 114 1121 1695 1682 115 -218 62 C ATOM 736 CE2 TYR A 114 13.244 19.240 53.392 1.00 12.35 C ANISOU 736 CE2 TYR A 114 1289 1708 1694 204 -314 131 C ATOM 737 CZ TYR A 114 12.507 19.897 52.429 1.00 16.55 C ANISOU 737 CZ TYR A 114 1799 2260 2228 137 -244 109 C ATOM 738 OH TYR A 114 11.132 19.960 52.549 1.00 16.84 O ANISOU 738 OH TYR A 114 1898 2282 2219 97 -196 133 O ATOM 739 N GLU A 115 18.920 20.682 53.833 1.00 17.44 N ANISOU 739 N GLU A 115 1505 2490 2632 338 -593 -96 N ATOM 740 CA GLU A 115 20.218 20.670 54.491 1.00 27.61 C ANISOU 740 CA GLU A 115 2697 3803 3990 405 -713 -154 C ATOM 741 C GLU A 115 20.273 19.498 55.447 1.00 27.11 C ANISOU 741 C GLU A 115 2719 3708 3875 518 -819 -103 C ATOM 742 O GLU A 115 19.317 19.253 56.194 1.00 25.30 O ANISOU 742 O GLU A 115 2636 3455 3522 528 -829 -28 O ATOM 743 CB GLU A 115 20.412 21.968 55.273 1.00 31.41 C ANISOU 743 CB GLU A 115 3153 4331 4449 366 -777 -197 C ATOM 744 CG GLU A 115 21.796 22.159 55.828 1.00 51.79 C ANISOU 744 CG GLU A 115 5649 6933 7095 397 -857 -264 C ATOM 745 CD GLU A 115 21.933 23.464 56.592 1.00 64.09 C ANISOU 745 CD GLU A 115 7204 8525 8622 343 -897 -307 C ATOM 746 OE1 GLU A 115 20.899 24.149 56.781 1.00 62.27 O ANISOU 746 OE1 GLU A 115 7045 8302 8312 295 -875 -281 O ATOM 747 OE2 GLU A 115 23.070 23.796 57.003 1.00 67.95 O ANISOU 747 OE2 GLU A 115 7617 9030 9172 351 -952 -374 O ATOM 748 N LEU A 116 21.385 18.772 55.416 1.00 24.63 N ANISOU 748 N LEU A 116 2324 3384 3649 596 -877 -138 N ATOM 749 CA LEU A 116 21.620 17.689 56.360 1.00 32.01 C ANISOU 749 CA LEU A 116 3349 4281 4531 708 -974 -87 C ATOM 750 C LEU A 116 21.658 18.226 57.784 1.00 36.51 C ANISOU 750 C LEU A 116 4000 4881 4990 727 -1079 -74 C ATOM 751 O LEU A 116 22.276 19.257 58.048 1.00 39.38 O ANISOU 751 O LEU A 116 4286 5296 5379 681 -1108 -142 O ATOM 752 CB LEU A 116 22.933 16.986 56.041 1.00 29.46 C ANISOU 752 CB LEU A 116 2923 3947 4322 767 -994 -135 C ATOM 753 CG LEU A 116 22.986 16.205 54.732 1.00 32.89 C ANISOU 753 CG LEU A 116 3297 4341 4858 769 -892 -148 C ATOM 754 CD1 LEU A 116 24.353 15.565 54.581 1.00 38.63 C ANISOU 754 CD1 LEU A 116 3926 5061 5690 833 -920 -201 C ATOM 755 CD2 LEU A 116 21.901 15.152 54.693 1.00 30.15 C ANISOU 755 CD2 LEU A 116 3081 3920 4454 817 -872 -63 C ATOM 756 N ASN A 117 20.986 17.532 58.696 1.00 30.86 N ANISOU 756 N ASN A 117 3451 4125 4149 792 -1123 14 N ATOM 757 CA ASN A 117 21.007 17.901 60.104 1.00 30.92 C ANISOU 757 CA ASN A 117 3559 4154 4034 820 -1214 31 C ATOM 758 C ASN A 117 22.244 17.327 60.781 1.00 35.88 C ANISOU 758 C ASN A 117 4161 4783 4687 913 -1323 6 C ATOM 759 O ASN A 117 22.503 16.135 60.700 1.00 32.54 O ANISOU 759 O ASN A 117 3770 4307 4287 995 -1335 48 O ATOM 760 CB ASN A 117 19.739 17.413 60.805 1.00 31.90 C ANISOU 760 CB ASN A 117 3890 4228 4004 842 -1189 139 C ATOM 761 CG ASN A 117 19.849 17.466 62.315 1.00 37.25 C ANISOU 761 CG ASN A 117 4696 4913 4545 893 -1275 166 C ATOM 762 OD1 ASN A 117 20.794 18.038 62.867 1.00 33.52 O ANISOU 762 OD1 ASN A 117 4154 4492 4089 907 -1367 95 O ATOM 763 ND2 ASN A 117 18.879 16.865 62.996 1.00 38.76 N ANISOU 763 ND2 ASN A 117 5078 5046 4602 919 -1236 265 N ATOM 764 N GLU A 118 23.004 18.178 61.455 1.00 52.80 N ANISOU 764 N GLU A 118 6249 6982 6831 905 -1406 -66 N ATOM 765 CA GLU A 118 24.263 17.745 62.046 1.00 65.32 C ANISOU 765 CA GLU A 118 7787 8577 8456 993 -1523 -109 C ATOM 766 C GLU A 118 24.100 16.792 63.226 1.00 68.62 C ANISOU 766 C GLU A 118 8380 8954 8738 1104 -1606 -26 C ATOM 767 O GLU A 118 24.898 15.874 63.396 1.00 75.49 O ANISOU 767 O GLU A 118 9237 9798 9647 1201 -1674 -23 O ATOM 768 CB GLU A 118 25.114 18.954 62.442 1.00 76.87 C ANISOU 768 CB GLU A 118 9139 10105 9963 951 -1591 -219 C ATOM 769 CG GLU A 118 25.565 19.779 61.251 1.00 83.72 C ANISOU 769 CG GLU A 118 9824 10999 10988 850 -1503 -306 C ATOM 770 CD GLU A 118 26.188 18.924 60.156 1.00 91.89 C ANISOU 770 CD GLU A 118 10751 12005 12159 875 -1447 -320 C ATOM 771 OE1 GLU A 118 26.625 17.789 60.453 1.00 94.54 O ANISOU 771 OE1 GLU A 118 11117 12310 12495 981 -1512 -290 O ATOM 772 OE2 GLU A 118 26.234 19.384 58.994 1.00 93.87 O ANISOU 772 OE2 GLU A 118 10893 12260 12514 790 -1333 -361 O ATOM 773 N GLU A 119 23.068 17.003 64.034 1.00 67.42 N ANISOU 773 N GLU A 119 8397 8791 8427 1091 -1591 42 N ATOM 774 CA GLU A 119 22.871 16.194 65.234 1.00 70.32 C ANISOU 774 CA GLU A 119 8953 9116 8650 1188 -1653 123 C ATOM 775 C GLU A 119 22.409 14.770 64.916 1.00 66.99 C ANISOU 775 C GLU A 119 8631 8601 8219 1246 -1590 228 C ATOM 776 O GLU A 119 22.469 13.883 65.772 1.00 66.74 O ANISOU 776 O GLU A 119 8741 8519 8097 1339 -1637 296 O ATOM 777 CB GLU A 119 21.868 16.872 66.167 1.00 78.01 C ANISOU 777 CB GLU A 119 10082 10101 9457 1147 -1629 161 C ATOM 778 CG GLU A 119 22.260 18.284 66.569 1.00 85.13 C ANISOU 778 CG GLU A 119 10902 11083 10360 1091 -1689 59 C ATOM 779 CD GLU A 119 21.086 19.089 67.093 1.00 90.60 C ANISOU 779 CD GLU A 119 11717 11786 10921 1021 -1622 88 C ATOM 780 OE1 GLU A 119 19.924 18.672 66.878 1.00 92.36 O ANISOU 780 OE1 GLU A 119 12054 11960 11080 994 -1509 177 O ATOM 781 OE2 GLU A 119 21.326 20.144 67.716 1.00 92.95 O ANISOU 781 OE2 GLU A 119 11995 12138 11185 992 -1679 16 O ATOM 782 N SER A 120 21.957 14.553 63.684 1.00 57.10 N ANISOU 782 N SER A 120 7312 7322 7063 1192 -1481 237 N ATOM 783 CA SER A 120 21.382 13.269 63.304 1.00 49.61 C ANISOU 783 CA SER A 120 6462 6275 6114 1232 -1404 331 C ATOM 784 C SER A 120 22.385 12.133 63.432 1.00 56.79 C ANISOU 784 C SER A 120 7356 7140 7081 1348 -1477 340 C ATOM 785 O SER A 120 23.555 12.273 63.075 1.00 57.72 O ANISOU 785 O SER A 120 7310 7305 7318 1375 -1547 253 O ATOM 786 CB SER A 120 20.832 13.315 61.877 1.00 48.77 C ANISOU 786 CB SER A 120 6264 6151 6114 1157 -1288 317 C ATOM 787 OG SER A 120 20.159 12.108 61.554 1.00 44.11 O ANISOU 787 OG SER A 120 5784 5455 5521 1189 -1206 404 O ATOM 788 N SER A 121 21.916 11.004 63.948 1.00 60.53 N ANISOU 788 N SER A 121 8005 7519 7474 1414 -1452 445 N ATOM 789 CA SER A 121 22.730 9.802 64.012 1.00 72.16 C ANISOU 789 CA SER A 121 9483 8932 9001 1528 -1507 469 C ATOM 790 C SER A 121 22.756 9.130 62.644 1.00 67.09 C ANISOU 790 C SER A 121 8741 8238 8514 1516 -1418 457 C ATOM 791 O SER A 121 23.630 8.308 62.364 1.00 65.35 O ANISOU 791 O SER A 121 8456 7984 8389 1599 -1458 441 O ATOM 792 CB SER A 121 22.185 8.843 65.075 1.00 82.74 C ANISOU 792 CB SER A 121 11060 10178 10198 1597 -1497 589 C ATOM 793 OG SER A 121 20.773 8.731 64.984 1.00 86.97 O ANISOU 793 OG SER A 121 11734 10649 10661 1518 -1351 669 O ATOM 794 N VAL A 122 21.797 9.496 61.794 1.00 60.01 N ANISOU 794 N VAL A 122 7830 7331 7640 1417 -1298 459 N ATOM 795 CA VAL A 122 21.677 8.910 60.464 1.00 56.10 C ANISOU 795 CA VAL A 122 7253 6781 7280 1400 -1204 441 C ATOM 796 C VAL A 122 23.032 8.893 59.770 1.00 56.39 C ANISOU 796 C VAL A 122 7086 6867 7470 1438 -1257 339 C ATOM 797 O VAL A 122 23.788 9.864 59.839 1.00 57.61 O ANISOU 797 O VAL A 122 7109 7124 7658 1411 -1324 253 O ATOM 798 CB VAL A 122 20.643 9.660 59.594 1.00 57.10 C ANISOU 798 CB VAL A 122 7350 6926 7419 1284 -1098 421 C ATOM 799 CG1 VAL A 122 20.615 9.097 58.179 1.00 53.18 C ANISOU 799 CG1 VAL A 122 6761 6380 7067 1270 -1009 382 C ATOM 800 CG2 VAL A 122 19.262 9.571 60.224 1.00 58.12 C ANISOU 800 CG2 VAL A 122 7682 6993 7408 1243 -1024 521 C ATOM 801 N LYS A 123 23.344 7.777 59.123 1.00 59.66 N ANISOU 801 N LYS A 123 7480 7203 7984 1496 -1217 347 N ATOM 802 CA LYS A 123 24.639 7.627 58.470 1.00 60.88 C ANISOU 802 CA LYS A 123 7452 7394 8286 1537 -1250 253 C ATOM 803 C LYS A 123 24.516 7.694 56.952 1.00 54.83 C ANISOU 803 C LYS A 123 6560 6625 7648 1468 -1128 183 C ATOM 804 O LYS A 123 24.344 6.676 56.272 1.00 49.25 O ANISOU 804 O LYS A 123 5878 5828 7007 1499 -1053 199 O ATOM 805 CB LYS A 123 25.344 6.347 58.931 1.00 64.34 C ANISOU 805 CB LYS A 123 7943 7756 8748 1670 -1310 296 C ATOM 806 CG LYS A 123 25.793 6.420 60.383 1.00 66.84 C ANISOU 806 CG LYS A 123 8345 8099 8953 1747 -1453 333 C ATOM 807 CD LYS A 123 26.735 5.294 60.752 1.00 73.64 C ANISOU 807 CD LYS A 123 9217 8903 9860 1886 -1533 353 C ATOM 808 CE LYS A 123 27.290 5.506 62.150 1.00 77.11 C ANISOU 808 CE LYS A 123 9722 9385 10191 1965 -1692 368 C ATOM 809 NZ LYS A 123 28.077 4.343 62.625 1.00 83.36 N ANISOU 809 NZ LYS A 123 10558 10110 11006 2113 -1778 404 N ATOM 810 N ILE A 124 24.584 8.918 56.438 1.00 50.35 N ANISOU 810 N ILE A 124 5866 6153 7110 1370 -1105 104 N ATOM 811 CA ILE A 124 24.538 9.162 55.007 1.00 37.52 C ANISOU 811 CA ILE A 124 4118 4542 5595 1294 -987 29 C ATOM 812 C ILE A 124 25.457 10.323 54.665 1.00 34.11 C ANISOU 812 C ILE A 124 3509 4219 5234 1229 -996 -76 C ATOM 813 O ILE A 124 25.525 11.320 55.392 1.00 32.01 O ANISOU 813 O ILE A 124 3235 4020 4906 1192 -1063 -86 O ATOM 814 CB ILE A 124 23.117 9.497 54.536 1.00 37.03 C ANISOU 814 CB ILE A 124 4134 4456 5481 1208 -896 63 C ATOM 815 CG1 ILE A 124 22.555 10.647 55.373 1.00 28.94 C ANISOU 815 CG1 ILE A 124 3159 3498 4338 1151 -948 90 C ATOM 816 CG2 ILE A 124 22.221 8.260 54.604 1.00 37.82 C ANISOU 816 CG2 ILE A 124 4398 4424 5548 1257 -852 150 C ATOM 817 CD1 ILE A 124 21.184 11.106 54.934 1.00 36.05 C ANISOU 817 CD1 ILE A 124 4126 4388 5183 1053 -855 118 C ATOM 818 N ASP A 125 26.163 10.183 53.551 1.00 36.93 N ANISOU 818 N ASP A 125 3731 4581 5718 1210 -916 -157 N ATOM 819 CA ASP A 125 27.090 11.204 53.095 1.00 35.77 C ANISOU 819 CA ASP A 125 3421 4517 5653 1140 -894 -257 C ATOM 820 C ASP A 125 26.370 12.394 52.484 1.00 30.68 C ANISOU 820 C ASP A 125 2755 3921 4982 1010 -802 -278 C ATOM 821 O ASP A 125 26.910 13.504 52.469 1.00 33.77 O ANISOU 821 O ASP A 125 3052 4376 5401 940 -800 -338 O ATOM 822 CB ASP A 125 28.059 10.615 52.070 1.00 40.83 C ANISOU 822 CB ASP A 125 3941 5139 6432 1161 -819 -332 C ATOM 823 CG ASP A 125 29.066 9.672 52.698 1.00 49.38 C ANISOU 823 CG ASP A 125 5004 6194 7565 1288 -923 -335 C ATOM 824 OD1 ASP A 125 29.376 9.861 53.896 1.00 50.96 O ANISOU 824 OD1 ASP A 125 5233 6419 7712 1340 -1061 -312 O ATOM 825 OD2 ASP A 125 29.553 8.754 51.998 1.00 49.35 O ANISOU 825 OD2 ASP A 125 4958 6142 7651 1338 -868 -362 O ATOM 826 N ASP A 126 25.157 12.166 51.980 1.00 22.28 N ANISOU 826 N ASP A 126 1779 2817 3870 977 -725 -230 N ATOM 827 CA ASP A 126 24.437 13.205 51.250 1.00 23.98 C ANISOU 827 CA ASP A 126 1974 3073 4067 859 -628 -251 C ATOM 828 C ASP A 126 22.932 12.953 51.202 1.00 19.51 C ANISOU 828 C ASP A 126 1532 2461 3422 844 -599 -181 C ATOM 829 O ASP A 126 22.455 11.852 51.472 1.00 20.35 O ANISOU 829 O ASP A 126 1751 2489 3494 903 -610 -120 O ATOM 830 CB ASP A 126 24.984 13.352 49.825 1.00 27.80 C ANISOU 830 CB ASP A 126 2348 3567 4648 800 -489 -330 C ATOM 831 CG ASP A 126 24.997 12.027 49.056 1.00 35.05 C ANISOU 831 CG ASP A 126 3285 4413 5621 858 -424 -336 C ATOM 832 OD1 ASP A 126 24.013 11.257 49.154 1.00 28.11 O ANISOU 832 OD1 ASP A 126 2514 3468 4699 892 -427 -279 O ATOM 833 OD2 ASP A 126 25.990 11.751 48.348 1.00 38.30 O ANISOU 833 OD2 ASP A 126 3606 4824 6124 866 -366 -402 O ATOM 834 N ILE A 127 22.196 13.989 50.841 1.00 18.29 N ANISOU 834 N ILE A 127 1397 2352 3200 727 -526 -178 N ATOM 835 CA ILE A 127 20.750 13.900 50.677 1.00 19.42 C ANISOU 835 CA ILE A 127 1684 2466 3227 657 -454 -110 C ATOM 836 C ILE A 127 20.365 12.866 49.624 1.00 23.02 C ANISOU 836 C ILE A 127 2176 2859 3711 653 -351 -117 C ATOM 837 O ILE A 127 19.352 12.166 49.762 1.00 19.02 O ANISOU 837 O ILE A 127 1791 2293 3141 644 -327 -61 O ATOM 838 CB ILE A 127 20.198 15.259 50.290 1.00 16.02 C ANISOU 838 CB ILE A 127 1244 2100 2744 542 -392 -123 C ATOM 839 CG1 ILE A 127 20.452 16.237 51.438 1.00 19.85 C ANISOU 839 CG1 ILE A 127 1713 2636 3193 544 -495 -117 C ATOM 840 CG2 ILE A 127 18.720 15.160 49.943 1.00 15.72 C ANISOU 840 CG2 ILE A 127 1328 2036 2607 474 -316 -72 C ATOM 841 CD1 ILE A 127 20.210 17.672 51.087 1.00 22.61 C ANISOU 841 CD1 ILE A 127 2027 3043 3520 441 -441 -144 C ATOM 842 N GLN A 128 21.192 12.767 48.583 1.00 20.17 N ANISOU 842 N GLN A 128 1706 2507 3449 656 -286 -194 N ATOM 843 CA GLN A 128 20.963 11.828 47.484 1.00 19.19 C ANISOU 843 CA GLN A 128 1607 2328 3355 655 -186 -221 C ATOM 844 C GLN A 128 20.852 10.385 47.956 1.00 18.23 C ANISOU 844 C GLN A 128 1561 2109 3255 745 -227 -182 C ATOM 845 O GLN A 128 20.199 9.556 47.320 1.00 29.32 O ANISOU 845 O GLN A 128 3038 3452 4651 728 -155 -183 O ATOM 846 CB GLN A 128 22.072 11.939 46.429 1.00 21.36 C ANISOU 846 CB GLN A 128 1748 2626 3740 660 -110 -315 C ATOM 847 CG GLN A 128 21.952 13.159 45.505 1.00 21.45 C ANISOU 847 CG GLN A 128 1727 2704 3719 554 -8 -351 C ATOM 848 CD GLN A 128 22.583 14.430 46.080 1.00 29.99 C ANISOU 848 CD GLN A 128 2715 3853 4826 526 -53 -366 C ATOM 849 OE1 GLN A 128 22.948 14.488 47.256 1.00 22.20 O ANISOU 849 OE1 GLN A 128 1699 2876 3860 579 -177 -346 O ATOM 850 NE2 GLN A 128 22.717 15.456 45.238 1.00 22.52 N ANISOU 850 NE2 GLN A 128 1730 2950 3877 443 50 -402 N ATOM 851 N SER A 129 21.483 10.098 49.086 1.00 22.44 N ANISOU 851 N SER A 129 2087 2626 3814 843 -347 -149 N ATOM 852 CA SER A 129 21.591 8.733 49.586 1.00 21.29 C ANISOU 852 CA SER A 129 2015 2378 3698 951 -393 -108 C ATOM 853 C SER A 129 20.481 8.391 50.563 1.00 26.20 C ANISOU 853 C SER A 129 2807 2943 4204 944 -422 -3 C ATOM 854 O SER A 129 20.343 7.251 50.972 1.00 29.99 O ANISOU 854 O SER A 129 3384 3320 4691 1017 -436 47 O ATOM 855 CB SER A 129 22.939 8.532 50.278 1.00 21.60 C ANISOU 855 CB SER A 129 1958 2422 3826 1083 -518 -130 C ATOM 856 OG SER A 129 23.973 8.447 49.326 1.00 32.76 O ANISOU 856 OG SER A 129 3242 3865 5340 1079 -452 -220 O ATOM 857 N LEU A 130 19.713 9.394 50.953 1.00 22.40 N ANISOU 857 N LEU A 130 2366 2523 3621 858 -422 29 N ATOM 858 CA LEU A 130 18.629 9.202 51.900 1.00 28.65 C ANISOU 858 CA LEU A 130 3313 3268 4304 841 -431 122 C ATOM 859 C LEU A 130 17.614 8.170 51.388 1.00 32.82 C ANISOU 859 C LEU A 130 3940 3697 4835 800 -326 143 C ATOM 860 O LEU A 130 17.455 7.979 50.180 1.00 32.05 O ANISOU 860 O LEU A 130 3791 3597 4790 748 -241 77 O ATOM 861 CB LEU A 130 17.956 10.549 52.177 1.00 26.06 C ANISOU 861 CB LEU A 130 2988 3029 3884 743 -427 131 C ATOM 862 CG LEU A 130 17.198 10.719 53.489 1.00 34.54 C ANISOU 862 CG LEU A 130 4196 4087 4840 744 -467 218 C ATOM 863 CD1 LEU A 130 18.023 10.221 54.668 1.00 32.83 C ANISOU 863 CD1 LEU A 130 4032 3838 4605 877 -593 266 C ATOM 864 CD2 LEU A 130 16.787 12.177 53.690 1.00 34.49 C ANISOU 864 CD2 LEU A 130 4161 4178 4766 659 -471 205 C ATOM 865 N THR A 131 16.956 7.478 52.314 1.00 25.64 N ANISOU 865 N THR A 131 3176 2699 3869 825 -329 230 N ATOM 866 CA THR A 131 15.852 6.597 51.960 1.00 32.38 C ANISOU 866 CA THR A 131 4123 3452 4728 766 -221 247 C ATOM 867 C THR A 131 14.600 6.957 52.751 1.00 36.19 C ANISOU 867 C THR A 131 4714 3925 5110 690 -183 313 C ATOM 868 O THR A 131 14.673 7.589 53.805 1.00 31.82 O ANISOU 868 O THR A 131 4206 3413 4472 715 -248 369 O ATOM 869 CB THR A 131 16.181 5.087 52.178 1.00 31.97 C ANISOU 869 CB THR A 131 4155 3255 4737 863 -215 283 C ATOM 870 OG1 THR A 131 16.439 4.838 53.564 1.00 34.50 O ANISOU 870 OG1 THR A 131 4591 3528 4991 960 -296 384 O ATOM 871 CG2 THR A 131 17.372 4.663 51.352 1.00 34.36 C ANISOU 871 CG2 THR A 131 4344 3559 5154 941 -240 208 C ATOM 872 N CYS A 132 13.450 6.559 52.221 1.00 35.42 N ANISOU 872 N CYS A 132 4653 3776 5030 596 -76 297 N ATOM 873 CA CYS A 132 12.184 6.756 52.902 1.00 38.69 C ANISOU 873 CA CYS A 132 5160 4165 5376 518 -16 349 C ATOM 874 C CYS A 132 12.295 6.240 54.334 1.00 37.82 C ANISOU 874 C CYS A 132 5199 3971 5199 596 -42 460 C ATOM 875 O CYS A 132 11.832 6.880 55.277 1.00 43.19 O ANISOU 875 O CYS A 132 5946 4682 5782 576 -48 515 O ATOM 876 CB CYS A 132 11.070 6.020 52.156 1.00 42.70 C ANISOU 876 CB CYS A 132 5683 4594 5948 426 99 306 C ATOM 877 SG CYS A 132 9.529 6.959 51.981 1.00 72.36 S ANISOU 877 SG CYS A 132 9410 8415 9667 284 167 273 S ATOM 878 N ASN A 133 12.940 5.092 54.490 1.00 41.22 N ANISOU 878 N ASN A 133 5692 4294 5676 694 -58 494 N ATOM 879 CA ASN A 133 13.087 4.472 55.798 1.00 51.33 C ANISOU 879 CA ASN A 133 7140 5477 6885 786 -84 608 C ATOM 880 C ASN A 133 13.699 5.391 56.851 1.00 50.64 C ANISOU 880 C ASN A 133 7075 5484 6683 858 -209 654 C ATOM 881 O ASN A 133 13.095 5.635 57.892 1.00 46.95 O ANISOU 881 O ASN A 133 6736 5001 6103 845 -189 729 O ATOM 882 CB ASN A 133 13.885 3.174 55.683 1.00 61.30 C ANISOU 882 CB ASN A 133 8447 6617 8226 902 -106 628 C ATOM 883 CG ASN A 133 13.099 2.070 54.999 1.00 72.18 C ANISOU 883 CG ASN A 133 9867 7859 9700 834 33 606 C ATOM 884 OD1 ASN A 133 11.886 1.947 55.185 1.00 71.01 O ANISOU 884 OD1 ASN A 133 9790 7654 9535 727 149 628 O ATOM 885 ND2 ASN A 133 13.788 1.261 54.199 1.00 76.95 N ANISOU 885 ND2 ASN A 133 10415 8406 10414 891 26 553 N ATOM 886 N GLU A 134 14.891 5.905 56.581 1.00 50.54 N ANISOU 886 N GLU A 134 6935 5567 6702 930 -332 599 N ATOM 887 CA GLU A 134 15.577 6.742 57.558 1.00 54.36 C ANISOU 887 CA GLU A 134 7425 6139 7091 1003 -469 623 C ATOM 888 C GLU A 134 14.790 8.007 57.859 1.00 47.21 C ANISOU 888 C GLU A 134 6510 5331 6096 895 -441 614 C ATOM 889 O GLU A 134 15.017 8.672 58.867 1.00 47.99 O ANISOU 889 O GLU A 134 6661 5484 6089 937 -527 646 O ATOM 890 CB GLU A 134 16.988 7.084 57.085 1.00 63.04 C ANISOU 890 CB GLU A 134 8356 7323 8275 1082 -592 543 C ATOM 891 CG GLU A 134 17.218 6.827 55.614 1.00 66.31 C ANISOU 891 CG GLU A 134 8624 7742 8830 1035 -523 450 C ATOM 892 CD GLU A 134 18.556 6.179 55.351 1.00 68.59 C ANISOU 892 CD GLU A 134 8830 8008 9224 1166 -608 412 C ATOM 893 OE1 GLU A 134 19.228 5.785 56.329 1.00 68.11 O ANISOU 893 OE1 GLU A 134 8837 7911 9129 1301 -727 467 O ATOM 894 OE2 GLU A 134 18.936 6.060 54.167 1.00 71.18 O ANISOU 894 OE2 GLU A 134 9028 8351 9665 1139 -558 326 O ATOM 895 N LEU A 135 13.851 8.329 56.983 1.00 39.77 N ANISOU 895 N LEU A 135 5504 4409 5196 763 -325 566 N ATOM 896 CA LEU A 135 13.018 9.500 57.167 1.00 36.51 C ANISOU 896 CA LEU A 135 5077 4079 4715 661 -288 552 C ATOM 897 C LEU A 135 11.963 9.226 58.229 1.00 37.86 C ANISOU 897 C LEU A 135 5423 4175 4787 635 -210 640 C ATOM 898 O LEU A 135 11.621 10.104 59.018 1.00 34.35 O ANISOU 898 O LEU A 135 5023 3788 4243 613 -224 660 O ATOM 899 CB LEU A 135 12.346 9.851 55.844 1.00 34.66 C ANISOU 899 CB LEU A 135 4723 3883 4561 545 -199 471 C ATOM 900 CG LEU A 135 11.835 11.260 55.663 1.00 27.73 C ANISOU 900 CG LEU A 135 3774 3117 3646 457 -192 429 C ATOM 901 CD1 LEU A 135 12.979 12.203 55.916 1.00 29.95 C ANISOU 901 CD1 LEU A 135 3979 3495 3906 511 -311 402 C ATOM 902 CD2 LEU A 135 11.283 11.429 54.257 1.00 27.64 C ANISOU 902 CD2 LEU A 135 3659 3132 3712 369 -121 351 C ATOM 903 N TYR A 136 11.452 7.996 58.245 1.00 46.09 N ANISOU 903 N TYR A 136 6567 5082 5862 635 -116 688 N ATOM 904 CA TYR A 136 10.347 7.635 59.136 1.00 49.80 C ANISOU 904 CA TYR A 136 7201 5461 6259 591 0 767 C ATOM 905 C TYR A 136 10.826 7.041 60.450 1.00 52.88 C ANISOU 905 C TYR A 136 7786 5770 6534 714 -48 880 C ATOM 906 O TYR A 136 10.041 6.871 61.379 1.00 57.72 O ANISOU 906 O TYR A 136 8560 6315 7055 691 43 958 O ATOM 907 CB TYR A 136 9.384 6.658 58.453 1.00 45.41 C ANISOU 907 CB TYR A 136 6654 4789 5809 504 152 752 C ATOM 908 CG TYR A 136 8.530 7.267 57.357 1.00 50.09 C ANISOU 908 CG TYR A 136 7094 5453 6484 372 215 649 C ATOM 909 CD1 TYR A 136 7.214 7.657 57.601 1.00 46.56 C ANISOU 909 CD1 TYR A 136 6663 5003 6025 263 328 644 C ATOM 910 CD2 TYR A 136 9.039 7.443 56.075 1.00 58.58 C ANISOU 910 CD2 TYR A 136 8013 6596 7650 365 163 556 C ATOM 911 CE1 TYR A 136 6.429 8.204 56.593 1.00 51.82 C ANISOU 911 CE1 TYR A 136 7188 5734 6767 158 367 546 C ATOM 912 CE2 TYR A 136 8.269 7.993 55.062 1.00 61.52 C ANISOU 912 CE2 TYR A 136 8265 7032 8080 260 208 466 C ATOM 913 CZ TYR A 136 6.966 8.370 55.324 1.00 62.75 C ANISOU 913 CZ TYR A 136 8434 7186 8223 162 300 461 C ATOM 914 OH TYR A 136 6.207 8.913 54.310 1.00 67.28 O ANISOU 914 OH TYR A 136 8885 7824 8854 73 325 368 O ATOM 915 N GLU A 137 12.113 6.719 60.527 1.00 53.71 N ANISOU 915 N GLU A 137 7880 5882 6646 848 -190 888 N ATOM 916 CA GLU A 137 12.667 6.116 61.732 1.00 60.57 C ANISOU 916 CA GLU A 137 8893 6704 7416 957 -260 969 C ATOM 917 C GLU A 137 13.243 7.172 62.669 1.00 63.10 C ANISOU 917 C GLU A 137 9206 7156 7615 1000 -394 958 C ATOM 918 O GLU A 137 14.069 6.861 63.528 1.00 66.87 O ANISOU 918 O GLU A 137 9729 7645 8031 1095 -500 982 O ATOM 919 CB GLU A 137 13.748 5.088 61.377 1.00 69.69 C ANISOU 919 CB GLU A 137 10011 7806 8665 1065 -340 963 C ATOM 920 CG GLU A 137 13.303 4.008 60.386 1.00 78.98 C ANISOU 920 CG GLU A 137 11185 8849 9976 1028 -216 956 C ATOM 921 CD GLU A 137 12.713 2.770 61.050 1.00 89.58 C ANISOU 921 CD GLU A 137 12690 10050 11297 1011 -106 1035 C ATOM 922 OE1 GLU A 137 12.305 2.846 62.233 1.00 93.36 O ANISOU 922 OE1 GLU A 137 13298 10528 11645 1002 -82 1100 O ATOM 923 OE2 GLU A 137 12.665 1.713 60.381 1.00 90.79 O ANISOU 923 OE2 GLU A 137 12841 10089 11565 1008 -39 1024 O ATOM 924 N TYR A 138 12.816 8.420 62.499 1.00 63.94 N ANISOU 924 N TYR A 138 9249 7356 7687 931 -391 916 N ATOM 925 CA TYR A 138 13.285 9.506 63.361 1.00 64.69 C ANISOU 925 CA TYR A 138 9331 7575 7675 955 -508 889 C ATOM 926 C TYR A 138 12.234 10.582 63.565 1.00 58.70 C ANISOU 926 C TYR A 138 8595 6866 6843 852 -424 881 C ATOM 927 O TYR A 138 11.678 11.111 62.606 1.00 60.16 O ANISOU 927 O TYR A 138 8660 7086 7113 752 -353 824 O ATOM 928 CB TYR A 138 14.580 10.120 62.819 1.00 64.60 C ANISOU 928 CB TYR A 138 9137 7669 7739 1015 -673 801 C ATOM 929 CG TYR A 138 15.718 9.131 62.780 1.00 71.85 C ANISOU 929 CG TYR A 138 10023 8551 8728 1124 -762 801 C ATOM 930 CD1 TYR A 138 16.408 8.790 63.937 1.00 75.67 C ANISOU 930 CD1 TYR A 138 10584 9039 9127 1210 -857 831 C ATOM 931 CD2 TYR A 138 16.083 8.514 61.591 1.00 75.07 C ANISOU 931 CD2 TYR A 138 10325 8915 9284 1144 -748 768 C ATOM 932 CE1 TYR A 138 17.442 7.871 63.904 1.00 80.67 C ANISOU 932 CE1 TYR A 138 11188 9636 9828 1315 -938 832 C ATOM 933 CE2 TYR A 138 17.111 7.594 61.547 1.00 78.13 C ANISOU 933 CE2 TYR A 138 10678 9265 9743 1243 -819 764 C ATOM 934 CZ TYR A 138 17.792 7.277 62.702 1.00 80.23 C ANISOU 934 CZ TYR A 138 11018 9538 9928 1329 -916 799 C ATOM 935 OH TYR A 138 18.821 6.361 62.651 1.00 75.97 O ANISOU 935 OH TYR A 138 10441 8961 9464 1434 -989 797 O ATOM 936 N ASP A 139 11.966 10.891 64.828 1.00 58.22 N ANISOU 936 N ASP A 139 8649 6826 6647 851 -419 909 N ATOM 937 CA ASP A 139 11.039 11.958 65.183 1.00 68.28 C ANISOU 937 CA ASP A 139 9945 8152 7845 761 -345 893 C ATOM 938 C ASP A 139 11.754 13.310 65.208 1.00 68.64 C ANISOU 938 C ASP A 139 9877 8335 7868 775 -487 813 C ATOM 939 O ASP A 139 12.973 13.383 65.026 1.00 69.50 O ANISOU 939 O ASP A 139 9886 8497 8024 848 -638 767 O ATOM 940 CB ASP A 139 10.390 11.676 66.545 1.00 78.74 C ANISOU 940 CB ASP A 139 11446 9431 9040 754 -260 950 C ATOM 941 CG ASP A 139 11.385 11.740 67.703 1.00 88.02 C ANISOU 941 CG ASP A 139 12687 10651 10105 860 -408 952 C ATOM 942 OD1 ASP A 139 12.547 11.301 67.535 1.00 89.40 O ANISOU 942 OD1 ASP A 139 12809 10837 10324 953 -545 941 O ATOM 943 OD2 ASP A 139 10.998 12.232 68.787 1.00 92.16 O ANISOU 943 OD2 ASP A 139 13314 11198 10504 850 -383 959 O ATOM 944 N VAL A 140 10.993 14.378 65.431 1.00 66.51 N ANISOU 944 N VAL A 140 9612 8118 7542 697 -431 788 N ATOM 945 CA VAL A 140 11.569 15.711 65.572 1.00 67.59 C ANISOU 945 CA VAL A 140 9653 8375 7654 697 -550 707 C ATOM 946 C VAL A 140 12.678 15.709 66.629 1.00 70.59 C ANISOU 946 C VAL A 140 10060 8795 7967 789 -698 687 C ATOM 947 O VAL A 140 12.526 15.127 67.709 1.00 70.40 O ANISOU 947 O VAL A 140 10186 8721 7839 829 -674 743 O ATOM 948 CB VAL A 140 10.493 16.753 65.945 1.00 64.99 C ANISOU 948 CB VAL A 140 9364 8079 7251 608 -452 691 C ATOM 949 CG1 VAL A 140 11.139 18.076 66.314 1.00 70.65 C ANISOU 949 CG1 VAL A 140 10005 8906 7932 613 -576 606 C ATOM 950 CG2 VAL A 140 9.513 16.936 64.800 1.00 57.34 C ANISOU 950 CG2 VAL A 140 8279 7101 6408 489 -311 662 C ATOM 951 N GLY A 141 13.795 16.352 66.308 1.00 66.71 N ANISOU 951 N GLY A 141 9419 8388 7539 819 -843 604 N ATOM 952 CA GLY A 141 14.936 16.379 67.201 1.00 62.69 C ANISOU 952 CA GLY A 141 8909 7919 6991 902 -989 570 C ATOM 953 C GLY A 141 16.131 15.674 66.595 1.00 61.89 C ANISOU 953 C GLY A 141 8692 7814 7011 976 -1090 547 C ATOM 954 O GLY A 141 17.272 16.105 66.768 1.00 65.53 O ANISOU 954 O GLY A 141 9044 8340 7513 1016 -1223 470 O ATOM 955 N GLN A 142 15.870 14.587 65.876 1.00 56.76 N ANISOU 955 N GLN A 142 8058 7083 6427 990 -1019 606 N ATOM 956 CA GLN A 142 16.946 13.806 65.279 1.00 54.62 C ANISOU 956 CA GLN A 142 7683 6795 6275 1064 -1097 585 C ATOM 957 C GLN A 142 16.702 13.510 63.801 1.00 43.58 C ANISOU 957 C GLN A 142 6176 5366 5015 1024 -1023 575 C ATOM 958 O GLN A 142 17.337 12.622 63.233 1.00 41.85 O ANISOU 958 O GLN A 142 5900 5105 4896 1082 -1045 575 O ATOM 959 CB GLN A 142 17.141 12.489 66.040 1.00 67.04 C ANISOU 959 CB GLN A 142 9403 8280 7790 1159 -1107 668 C ATOM 960 CG GLN A 142 17.571 12.643 67.501 1.00 77.54 C ANISOU 960 CG GLN A 142 10844 9636 8983 1225 -1203 674 C ATOM 961 CD GLN A 142 16.400 12.878 68.449 1.00 82.69 C ANISOU 961 CD GLN A 142 11683 10260 9476 1178 -1100 735 C ATOM 962 OE1 GLN A 142 15.271 13.107 68.015 1.00 83.44 O ANISOU 962 OE1 GLN A 142 11803 10329 9569 1085 -959 760 O ATOM 963 NE2 GLN A 142 16.667 12.814 69.751 1.00 85.23 N ANISOU 963 NE2 GLN A 142 12136 10585 9664 1246 -1166 754 N ATOM 964 N GLU A 143 15.782 14.242 63.181 1.00 38.19 N ANISOU 964 N GLU A 143 5470 4703 4339 931 -936 563 N ATOM 965 CA GLU A 143 15.463 13.989 61.779 1.00 36.26 C ANISOU 965 CA GLU A 143 5119 4432 4226 872 -845 542 C ATOM 966 C GLU A 143 16.664 14.300 60.895 1.00 33.47 C ANISOU 966 C GLU A 143 4557 4144 4015 892 -931 445 C ATOM 967 O GLU A 143 17.441 15.207 61.193 1.00 27.82 O ANISOU 967 O GLU A 143 3753 3514 3302 907 -1040 377 O ATOM 968 CB GLU A 143 14.216 14.751 61.324 1.00 29.45 C ANISOU 968 CB GLU A 143 4236 3592 3360 726 -699 526 C ATOM 969 CG GLU A 143 14.345 16.258 61.306 1.00 31.25 C ANISOU 969 CG GLU A 143 4363 3928 3583 665 -739 449 C ATOM 970 CD GLU A 143 13.978 16.900 62.634 1.00 39.29 C ANISOU 970 CD GLU A 143 5514 4969 4445 678 -773 476 C ATOM 971 OE1 GLU A 143 14.301 16.324 63.693 1.00 46.27 O ANISOU 971 OE1 GLU A 143 6541 5819 5222 780 -851 533 O ATOM 972 OE2 GLU A 143 13.366 17.988 62.617 1.00 40.31 O ANISOU 972 OE2 GLU A 143 5614 5148 4554 591 -722 439 O ATOM 973 N PRO A 144 16.821 13.530 59.809 1.00 29.86 N ANISOU 973 N PRO A 144 4021 3642 3681 885 -868 430 N ATOM 974 CA PRO A 144 18.020 13.523 58.963 1.00 23.82 C ANISOU 974 CA PRO A 144 3075 2915 3059 920 -929 346 C ATOM 975 C PRO A 144 18.283 14.831 58.214 1.00 23.23 C ANISOU 975 C PRO A 144 2832 2940 3055 824 -911 250 C ATOM 976 O PRO A 144 19.451 15.197 58.051 1.00 21.47 O ANISOU 976 O PRO A 144 2469 2770 2919 864 -1001 174 O ATOM 977 CB PRO A 144 17.733 12.398 57.962 1.00 30.55 C ANISOU 977 CB PRO A 144 3923 3683 4000 909 -820 362 C ATOM 978 CG PRO A 144 16.686 11.561 58.608 1.00 28.49 C ANISOU 978 CG PRO A 144 3859 3322 3644 914 -749 465 C ATOM 979 CD PRO A 144 15.849 12.509 59.384 1.00 31.13 C ANISOU 979 CD PRO A 144 4273 3701 3854 847 -728 491 C ATOM 980 N ILE A 145 17.229 15.505 57.751 1.00 18.02 N ANISOU 980 N ILE A 145 2183 2297 2366 703 -794 251 N ATOM 981 CA ILE A 145 17.385 16.747 57.006 1.00 19.89 C ANISOU 981 CA ILE A 145 2286 2611 2659 613 -762 173 C ATOM 982 C ILE A 145 16.354 17.792 57.382 1.00 19.24 C ANISOU 982 C ILE A 145 2264 2561 2485 526 -713 187 C ATOM 983 O ILE A 145 15.303 17.461 57.931 1.00 17.29 O ANISOU 983 O ILE A 145 2151 2272 2148 513 -663 254 O ATOM 984 CB ILE A 145 17.320 16.530 55.481 1.00 19.22 C ANISOU 984 CB ILE A 145 2108 2516 2679 555 -651 135 C ATOM 985 CG1 ILE A 145 16.045 15.805 55.083 1.00 23.00 C ANISOU 985 CG1 ILE A 145 2687 2931 3123 510 -540 189 C ATOM 986 CG2 ILE A 145 18.509 15.712 55.015 1.00 28.85 C ANISOU 986 CG2 ILE A 145 3236 3716 4011 635 -693 97 C ATOM 987 CD1 ILE A 145 15.905 15.714 53.581 1.00 30.69 C ANISOU 987 CD1 ILE A 145 3580 3904 4175 452 -442 142 C ATOM 988 N PHE A 146 16.663 19.045 57.038 1.00 17.47 N ANISOU 988 N PHE A 146 1938 2404 2298 465 -715 121 N ATOM 989 CA PHE A 146 15.849 20.211 57.349 1.00 19.35 C ANISOU 989 CA PHE A 146 2211 2674 2466 388 -678 118 C ATOM 990 C PHE A 146 15.614 20.995 56.069 1.00 16.60 C ANISOU 990 C PHE A 146 1771 2349 2188 297 -582 76 C ATOM 991 O PHE A 146 16.530 21.154 55.265 1.00 18.30 O ANISOU 991 O PHE A 146 1869 2583 2502 292 -580 21 O ATOM 992 CB PHE A 146 16.628 21.133 58.296 1.00 21.98 C ANISOU 992 CB PHE A 146 2516 3062 2774 411 -795 69 C ATOM 993 CG PHE A 146 16.850 20.567 59.658 1.00 32.09 C ANISOU 993 CG PHE A 146 3907 4330 3955 508 -909 107 C ATOM 994 CD1 PHE A 146 15.839 19.891 60.318 1.00 36.79 C ANISOU 994 CD1 PHE A 146 4671 4873 4435 527 -864 195 C ATOM 995 CD2 PHE A 146 18.074 20.724 60.290 1.00 38.03 C ANISOU 995 CD2 PHE A 146 4600 5121 4729 583 -1061 50 C ATOM 996 CE1 PHE A 146 16.045 19.376 61.582 1.00 43.15 C ANISOU 996 CE1 PHE A 146 5606 5660 5128 623 -961 240 C ATOM 997 CE2 PHE A 146 18.286 20.214 61.556 1.00 42.02 C ANISOU 997 CE2 PHE A 146 5226 5613 5129 665 -1147 89 C ATOM 998 CZ PHE A 146 17.270 19.535 62.203 1.00 43.80 C ANISOU 998 CZ PHE A 146 5639 5784 5219 698 -1111 188 C ATOM 999 N PRO A 147 14.403 21.520 55.875 1.00 15.81 N ANISOU 999 N PRO A 147 1724 2246 2038 228 -498 99 N ATOM 1000 CA PRO A 147 14.318 22.407 54.714 1.00 22.13 C ANISOU 1000 CA PRO A 147 2446 3070 2894 158 -427 58 C ATOM 1001 C PRO A 147 15.005 23.721 55.035 1.00 21.02 C ANISOU 1001 C PRO A 147 2243 2972 2771 131 -469 4 C ATOM 1002 O PRO A 147 15.110 24.110 56.205 1.00 17.66 O ANISOU 1002 O PRO A 147 1857 2563 2292 151 -543 -1 O ATOM 1003 CB PRO A 147 12.813 22.630 54.547 1.00 20.65 C ANISOU 1003 CB PRO A 147 2332 2867 2648 107 -348 93 C ATOM 1004 CG PRO A 147 12.246 22.432 55.900 1.00 13.34 C ANISOU 1004 CG PRO A 147 1508 1927 1634 131 -378 135 C ATOM 1005 CD PRO A 147 13.125 21.418 56.599 1.00 15.25 C ANISOU 1005 CD PRO A 147 1775 2149 1869 212 -459 154 C ATOM 1006 N ILE A 148 15.502 24.390 54.009 1.00 18.31 N ANISOU 1006 N ILE A 148 1810 2642 2505 85 -418 -40 N ATOM 1007 CA ILE A 148 15.939 25.765 54.180 1.00 21.23 C ANISOU 1007 CA ILE A 148 2129 3036 2900 38 -426 -91 C ATOM 1008 C ILE A 148 14.797 26.713 53.821 1.00 25.35 C ANISOU 1008 C ILE A 148 2709 3550 3373 -22 -348 -69 C ATOM 1009 O ILE A 148 14.341 26.750 52.676 1.00 24.11 O ANISOU 1009 O ILE A 148 2554 3380 3228 -50 -264 -53 O ATOM 1010 CB ILE A 148 17.177 26.072 53.340 1.00 22.21 C ANISOU 1010 CB ILE A 148 2127 3168 3144 17 -400 -154 C ATOM 1011 CG1 ILE A 148 18.386 25.321 53.909 1.00 16.41 C ANISOU 1011 CG1 ILE A 148 1314 2447 2473 85 -502 -195 C ATOM 1012 CG2 ILE A 148 17.453 27.562 53.363 1.00 21.70 C ANISOU 1012 CG2 ILE A 148 2021 3111 3114 -51 -376 -204 C ATOM 1013 CD1 ILE A 148 19.420 25.002 52.883 1.00 23.04 C ANISOU 1013 CD1 ILE A 148 2034 3282 3436 84 -452 -243 C ATOM 1014 N CYS A 149 14.316 27.456 54.815 1.00 17.51 N ANISOU 1014 N CYS A 149 1768 2565 2319 -34 -381 -70 N ATOM 1015 CA CYS A 149 13.209 28.375 54.608 1.00 19.89 C ANISOU 1015 CA CYS A 149 2122 2856 2579 -79 -315 -53 C ATOM 1016 C CYS A 149 13.739 29.804 54.715 1.00 25.84 C ANISOU 1016 C CYS A 149 2834 3611 3371 -127 -313 -107 C ATOM 1017 O CYS A 149 14.101 30.261 55.802 1.00 30.45 O ANISOU 1017 O CYS A 149 3421 4210 3938 -123 -383 -145 O ATOM 1018 CB CYS A 149 12.106 28.110 55.639 1.00 27.34 C ANISOU 1018 CB CYS A 149 3165 3796 3427 -60 -330 -14 C ATOM 1019 SG CYS A 149 11.453 26.402 55.586 1.00 30.90 S ANISOU 1019 SG CYS A 149 3670 4225 3846 -16 -315 47 S ATOM 1020 N GLU A 150 13.801 30.499 53.583 1.00 21.18 N ANISOU 1020 N GLU A 150 2213 3002 2831 -170 -232 -113 N ATOM 1021 CA GLU A 150 14.467 31.794 53.542 1.00 23.02 C ANISOU 1021 CA GLU A 150 2401 3220 3125 -222 -211 -166 C ATOM 1022 C GLU A 150 14.103 32.591 52.300 1.00 23.31 C ANISOU 1022 C GLU A 150 2457 3219 3179 -262 -102 -144 C ATOM 1023 O GLU A 150 13.817 32.037 51.233 1.00 17.42 O ANISOU 1023 O GLU A 150 1728 2469 2423 -249 -48 -105 O ATOM 1024 CB GLU A 150 15.987 31.605 53.558 1.00 18.91 C ANISOU 1024 CB GLU A 150 1768 2713 2705 -228 -247 -230 C ATOM 1025 CG GLU A 150 16.529 31.114 52.225 1.00 32.47 C ANISOU 1025 CG GLU A 150 3431 4418 4487 -235 -167 -223 C ATOM 1026 CD GLU A 150 18.045 30.942 52.199 1.00 51.16 C ANISOU 1026 CD GLU A 150 5667 6795 6976 -241 -189 -297 C ATOM 1027 OE1 GLU A 150 18.708 31.209 53.227 1.00 48.62 O ANISOU 1027 OE1 GLU A 150 5287 6494 6692 -238 -284 -360 O ATOM 1028 OE2 GLU A 150 18.571 30.528 51.139 1.00 58.95 O ANISOU 1028 OE2 GLU A 150 6605 7771 8022 -247 -112 -299 O ATOM 1029 N ALA A 151 14.129 33.906 52.446 1.00 19.74 N ANISOU 1029 N ALA A 151 2014 2737 2750 -308 -71 -171 N ATOM 1030 CA ALA A 151 14.056 34.788 51.302 1.00 17.67 C ANISOU 1030 CA ALA A 151 1775 2426 2514 -345 35 -152 C ATOM 1031 C ALA A 151 15.493 35.167 50.982 1.00 19.36 C ANISOU 1031 C ALA A 151 1895 2619 2841 -397 77 -212 C ATOM 1032 O ALA A 151 16.111 35.931 51.719 1.00 25.86 O ANISOU 1032 O ALA A 151 2670 3430 3726 -438 52 -277 O ATOM 1033 CB ALA A 151 13.217 36.035 51.634 1.00 16.15 C ANISOU 1033 CB ALA A 151 1653 2194 2291 -362 55 -145 C ATOM 1034 N GLY A 152 16.031 34.627 49.895 1.00 22.08 N ANISOU 1034 N GLY A 152 2210 2960 3220 -398 145 -199 N ATOM 1035 CA GLY A 152 17.392 34.949 49.496 1.00 19.98 C ANISOU 1035 CA GLY A 152 1845 2669 3076 -452 210 -259 C ATOM 1036 C GLY A 152 17.467 35.566 48.113 1.00 18.73 C ANISOU 1036 C GLY A 152 1738 2451 2928 -491 364 -224 C ATOM 1037 O GLY A 152 16.447 35.801 47.473 1.00 20.42 O ANISOU 1037 O GLY A 152 2069 2643 3045 -467 403 -153 O ATOM 1038 N GLU A 153 18.689 35.839 47.659 1.00 19.61 N ANISOU 1038 N GLU A 153 1761 2533 3158 -548 454 -278 N ATOM 1039 CA GLU A 153 18.943 36.313 46.300 1.00 24.33 C ANISOU 1039 CA GLU A 153 2411 3068 3766 -586 623 -246 C ATOM 1040 C GLU A 153 20.069 35.485 45.707 1.00 27.34 C ANISOU 1040 C GLU A 153 2710 3466 4213 -578 665 -282 C ATOM 1041 O GLU A 153 21.004 35.125 46.415 1.00 30.47 O ANISOU 1041 O GLU A 153 2990 3892 4696 -571 586 -353 O ATOM 1042 CB GLU A 153 19.339 37.794 46.297 1.00 36.27 C ANISOU 1042 CB GLU A 153 3946 4497 5340 -656 707 -267 C ATOM 1043 CG GLU A 153 18.158 38.750 46.385 1.00 54.08 C ANISOU 1043 CG GLU A 153 6328 6705 7515 -658 720 -207 C ATOM 1044 CD GLU A 153 18.578 40.210 46.494 1.00 65.17 C ANISOU 1044 CD GLU A 153 7752 8018 8992 -725 797 -236 C ATOM 1045 OE1 GLU A 153 17.750 41.091 46.164 1.00 68.56 O ANISOU 1045 OE1 GLU A 153 8308 8380 9364 -728 857 -174 O ATOM 1046 OE2 GLU A 153 19.726 40.474 46.916 1.00 63.31 O ANISOU 1046 OE2 GLU A 153 7415 7777 8864 -761 786 -319 O ATOM 1047 N ASN A 154 19.978 35.176 44.416 1.00 32.63 N ANISOU 1047 N ASN A 154 3455 4116 4828 -565 778 -233 N ATOM 1048 CA ASN A 154 21.046 34.430 43.751 1.00 32.44 C ANISOU 1048 CA ASN A 154 3370 4099 4858 -553 829 -269 C ATOM 1049 C ASN A 154 22.214 35.317 43.357 1.00 42.70 C ANISOU 1049 C ASN A 154 4642 5331 6250 -608 933 -313 C ATOM 1050 O ASN A 154 22.313 36.464 43.798 1.00 36.46 O ANISOU 1050 O ASN A 154 3859 4495 5501 -656 945 -330 O ATOM 1051 CB ASN A 154 20.530 33.639 42.537 1.00 26.09 C ANISOU 1051 CB ASN A 154 2658 3304 3952 -512 903 -212 C ATOM 1052 CG ASN A 154 20.120 34.530 41.370 1.00 29.93 C ANISOU 1052 CG ASN A 154 3303 3722 4345 -529 1039 -145 C ATOM 1053 OD1 ASN A 154 20.493 35.703 41.293 1.00 31.45 O ANISOU 1053 OD1 ASN A 154 3527 3848 4576 -577 1106 -147 O ATOM 1054 ND2 ASN A 154 19.351 33.966 40.449 1.00 33.18 N ANISOU 1054 ND2 ASN A 154 3828 4149 4632 -483 1074 -88 N ATOM 1055 N ASP A 155 23.087 34.766 42.518 1.00 62.10 N ANISOU 1055 N ASP A 155 7069 7779 8745 -603 1015 -338 N ATOM 1056 CA ASP A 155 24.280 35.460 42.044 1.00 76.56 C ANISOU 1056 CA ASP A 155 8866 9545 10677 -657 1131 -389 C ATOM 1057 C ASP A 155 23.935 36.763 41.316 1.00 71.70 C ANISOU 1057 C ASP A 155 8390 8842 10011 -701 1262 -335 C ATOM 1058 O ASP A 155 24.533 37.812 41.581 1.00 72.28 O ANISOU 1058 O ASP A 155 8435 8856 10172 -758 1309 -378 O ATOM 1059 CB ASP A 155 25.100 34.545 41.127 1.00 91.53 C ANISOU 1059 CB ASP A 155 10728 11445 12604 -638 1209 -415 C ATOM 1060 CG ASP A 155 25.783 33.411 41.888 1.00102.58 C ANISOU 1060 CG ASP A 155 11972 12911 14093 -596 1089 -485 C ATOM 1061 OD1 ASP A 155 25.881 33.507 43.133 1.00105.83 O ANISOU 1061 OD1 ASP A 155 12295 13355 14559 -591 954 -526 O ATOM 1062 OD2 ASP A 155 26.234 32.431 41.248 1.00105.82 O ANISOU 1062 OD2 ASP A 155 12356 13336 14515 -564 1127 -501 O ATOM 1063 N ASN A 156 22.973 36.691 40.400 1.00 62.74 N ANISOU 1063 N ASN A 156 7411 7697 8732 -669 1318 -244 N ATOM 1064 CA ASN A 156 22.547 37.862 39.649 1.00 56.89 C ANISOU 1064 CA ASN A 156 6828 6869 7919 -690 1430 -179 C ATOM 1065 C ASN A 156 21.604 38.757 40.448 1.00 52.41 C ANISOU 1065 C ASN A 156 6309 6285 7318 -697 1361 -145 C ATOM 1066 O ASN A 156 20.955 39.641 39.889 1.00 54.27 O ANISOU 1066 O ASN A 156 6695 6455 7468 -692 1427 -74 O ATOM 1067 CB ASN A 156 21.898 37.440 38.326 1.00 64.76 C ANISOU 1067 CB ASN A 156 7985 7860 8759 -638 1501 -98 C ATOM 1068 CG ASN A 156 22.818 36.599 37.460 1.00 73.98 C ANISOU 1068 CG ASN A 156 9120 9037 9954 -634 1584 -135 C ATOM 1069 OD1 ASN A 156 24.040 36.739 37.504 1.00 78.09 O ANISOU 1069 OD1 ASN A 156 9537 9526 10608 -681 1648 -207 O ATOM 1070 ND2 ASN A 156 22.227 35.713 36.664 1.00 75.17 N ANISOU 1070 ND2 ASN A 156 9358 9226 9978 -575 1584 -91 N ATOM 1071 N GLU A 157 21.528 38.516 41.754 1.00 43.93 N ANISOU 1071 N GLU A 157 5115 5268 6308 -702 1226 -195 N ATOM 1072 CA GLU A 157 20.748 39.366 42.642 1.00 44.31 C ANISOU 1072 CA GLU A 157 5192 5300 6345 -716 1160 -180 C ATOM 1073 C GLU A 157 19.236 39.198 42.427 1.00 44.33 C ANISOU 1073 C GLU A 157 5326 5320 6199 -662 1124 -86 C ATOM 1074 O GLU A 157 18.444 40.042 42.831 1.00 41.52 O ANISOU 1074 O GLU A 157 5039 4926 5810 -666 1106 -53 O ATOM 1075 CB GLU A 157 21.158 40.835 42.469 1.00 59.34 C ANISOU 1075 CB GLU A 157 7146 7098 8303 -772 1264 -189 C ATOM 1076 CG GLU A 157 20.548 41.789 43.489 1.00 73.54 C ANISOU 1076 CG GLU A 157 8955 8869 10116 -794 1200 -197 C ATOM 1077 CD GLU A 157 20.646 43.249 43.070 1.00 81.58 C ANISOU 1077 CD GLU A 157 10074 9770 11153 -833 1321 -177 C ATOM 1078 OE1 GLU A 157 21.472 43.563 42.185 1.00 79.47 O ANISOU 1078 OE1 GLU A 157 9830 9443 10922 -859 1452 -184 O ATOM 1079 OE2 GLU A 157 19.889 44.080 43.622 1.00 85.25 O ANISOU 1079 OE2 GLU A 157 10597 10196 11598 -837 1290 -157 O ATOM 1080 N GLU A 158 18.841 38.095 41.798 1.00 43.45 N ANISOU 1080 N GLU A 158 5246 5263 6002 -609 1115 -50 N ATOM 1081 CA GLU A 158 17.426 37.791 41.596 1.00 35.23 C ANISOU 1081 CA GLU A 158 4317 4249 4821 -551 1072 28 C ATOM 1082 C GLU A 158 16.843 37.109 42.829 1.00 24.94 C ANISOU 1082 C GLU A 158 2930 3028 3519 -512 888 -2 C ATOM 1083 O GLU A 158 17.427 36.171 43.352 1.00 24.21 O ANISOU 1083 O GLU A 158 2712 2994 3492 -512 825 -59 O ATOM 1084 CB GLU A 158 17.258 36.882 40.386 1.00 43.55 C ANISOU 1084 CB GLU A 158 5449 5329 5768 -497 1117 67 C ATOM 1085 CG GLU A 158 17.835 37.444 39.106 1.00 54.95 C ANISOU 1085 CG GLU A 158 6999 6702 7178 -501 1249 93 C ATOM 1086 CD GLU A 158 17.816 36.428 37.981 1.00 67.98 C ANISOU 1086 CD GLU A 158 8710 8386 8732 -450 1284 110 C ATOM 1087 OE1 GLU A 158 17.332 35.296 38.214 1.00 67.35 O ANISOU 1087 OE1 GLU A 158 8589 8384 8618 -412 1206 99 O ATOM 1088 OE2 GLU A 158 18.283 36.758 36.868 1.00 73.66 O ANISOU 1088 OE2 GLU A 158 9523 9052 9412 -449 1394 129 O ATOM 1089 N PRO A 159 15.671 37.572 43.288 1.00 25.27 N ANISOU 1089 N PRO A 159 3048 3069 3485 -472 801 38 N ATOM 1090 CA PRO A 159 15.109 37.078 44.547 1.00 16.95 C ANISOU 1090 CA PRO A 159 1928 2081 2431 -443 645 10 C ATOM 1091 C PRO A 159 14.491 35.686 44.406 1.00 19.39 C ANISOU 1091 C PRO A 159 2235 2465 2666 -374 557 26 C ATOM 1092 O PRO A 159 13.813 35.396 43.409 1.00 16.71 O ANISOU 1092 O PRO A 159 1991 2128 2231 -326 576 75 O ATOM 1093 CB PRO A 159 14.013 38.094 44.853 1.00 14.17 C ANISOU 1093 CB PRO A 159 1670 1690 2022 -422 615 50 C ATOM 1094 CG PRO A 159 13.564 38.550 43.471 1.00 18.46 C ANISOU 1094 CG PRO A 159 2358 2180 2476 -390 708 124 C ATOM 1095 CD PRO A 159 14.811 38.584 42.648 1.00 23.89 C ANISOU 1095 CD PRO A 159 3031 2828 3220 -446 850 112 C ATOM 1096 N TYR A 160 14.718 34.839 45.403 1.00 16.19 N ANISOU 1096 N TYR A 160 1731 2117 2303 -366 459 -18 N ATOM 1097 CA TYR A 160 14.049 33.545 45.460 1.00 18.31 C ANISOU 1097 CA TYR A 160 2001 2444 2512 -306 376 -4 C ATOM 1098 C TYR A 160 13.569 33.240 46.877 1.00 14.74 C ANISOU 1098 C TYR A 160 1511 2028 2060 -290 258 -20 C ATOM 1099 O TYR A 160 14.033 33.823 47.857 1.00 15.87 O ANISOU 1099 O TYR A 160 1605 2166 2257 -321 228 -58 O ATOM 1100 CB TYR A 160 14.971 32.419 44.974 1.00 13.91 C ANISOU 1100 CB TYR A 160 1376 1911 1998 -300 401 -32 C ATOM 1101 CG TYR A 160 16.093 32.139 45.939 1.00 14.82 C ANISOU 1101 CG TYR A 160 1362 2045 2223 -324 358 -96 C ATOM 1102 CD1 TYR A 160 17.314 32.785 45.812 1.00 16.67 C ANISOU 1102 CD1 TYR A 160 1520 2249 2565 -382 436 -145 C ATOM 1103 CD2 TYR A 160 15.927 31.242 46.988 1.00 14.88 C ANISOU 1103 CD2 TYR A 160 1326 2097 2230 -286 240 -109 C ATOM 1104 CE1 TYR A 160 18.345 32.552 46.698 1.00 20.99 C ANISOU 1104 CE1 TYR A 160 1935 2818 3222 -397 379 -217 C ATOM 1105 CE2 TYR A 160 16.956 31.001 47.887 1.00 20.74 C ANISOU 1105 CE2 TYR A 160 1959 2859 3063 -291 180 -167 C ATOM 1106 CZ TYR A 160 18.163 31.661 47.733 1.00 23.25 C ANISOU 1106 CZ TYR A 160 2187 3155 3493 -345 241 -226 C ATOM 1107 OH TYR A 160 19.199 31.433 48.608 1.00 23.20 O ANISOU 1107 OH TYR A 160 2057 3172 3585 -344 166 -299 O ATOM 1108 N VAL A 161 12.622 32.322 46.965 1.00 12.47 N ANISOU 1108 N VAL A 161 1252 1775 1711 -241 197 4 N ATOM 1109 CA VAL A 161 12.177 31.818 48.241 1.00 9.58 C ANISOU 1109 CA VAL A 161 864 1439 1336 -223 105 -5 C ATOM 1110 C VAL A 161 12.448 30.327 48.255 1.00 12.79 C ANISOU 1110 C VAL A 161 1233 1876 1750 -191 69 -10 C ATOM 1111 O VAL A 161 12.019 29.613 47.353 1.00 15.87 O ANISOU 1111 O VAL A 161 1652 2270 2109 -167 90 7 O ATOM 1112 CB VAL A 161 10.687 32.062 48.445 1.00 9.07 C ANISOU 1112 CB VAL A 161 868 1376 1204 -198 79 26 C ATOM 1113 CG1 VAL A 161 10.132 31.116 49.530 1.00 11.19 C ANISOU 1113 CG1 VAL A 161 1125 1674 1453 -174 9 25 C ATOM 1114 CG2 VAL A 161 10.425 33.557 48.767 1.00 9.28 C ANISOU 1114 CG2 VAL A 161 927 1367 1231 -221 100 26 C ATOM 1115 N SER A 162 13.220 29.881 49.242 1.00 11.28 N ANISOU 1115 N SER A 162 981 1702 1602 -187 11 -39 N ATOM 1116 CA SER A 162 13.391 28.462 49.486 1.00 10.47 C ANISOU 1116 CA SER A 162 857 1618 1505 -146 -35 -38 C ATOM 1117 C SER A 162 12.453 28.095 50.617 1.00 15.68 C ANISOU 1117 C SER A 162 1565 2285 2107 -123 -98 -13 C ATOM 1118 O SER A 162 12.270 28.865 51.568 1.00 15.30 O ANISOU 1118 O SER A 162 1533 2240 2039 -136 -129 -20 O ATOM 1119 CB SER A 162 14.841 28.136 49.872 1.00 10.36 C ANISOU 1119 CB SER A 162 751 1613 1573 -140 -67 -83 C ATOM 1120 OG SER A 162 14.971 26.741 50.109 1.00 12.84 O ANISOU 1120 OG SER A 162 1056 1934 1889 -88 -114 -75 O ATOM 1121 N PHE A 163 11.846 26.926 50.511 1.00 9.88 N ANISOU 1121 N PHE A 163 859 1549 1348 -93 -106 12 N ATOM 1122 CA PHE A 163 10.837 26.524 51.468 1.00 8.85 C ANISOU 1122 CA PHE A 163 783 1414 1166 -79 -136 39 C ATOM 1123 C PHE A 163 10.631 25.013 51.386 1.00 15.52 C ANISOU 1123 C PHE A 163 1642 2243 2013 -48 -141 57 C ATOM 1124 O PHE A 163 10.999 24.362 50.391 1.00 13.80 O ANISOU 1124 O PHE A 163 1397 2019 1829 -38 -117 46 O ATOM 1125 CB PHE A 163 9.524 27.275 51.186 1.00 18.07 C ANISOU 1125 CB PHE A 163 1991 2578 2296 -100 -100 51 C ATOM 1126 CG PHE A 163 8.582 27.311 52.359 1.00 14.16 C ANISOU 1126 CG PHE A 163 1542 2079 1758 -99 -113 66 C ATOM 1127 CD1 PHE A 163 8.965 27.900 53.554 1.00 12.12 C ANISOU 1127 CD1 PHE A 163 1300 1828 1477 -101 -148 57 C ATOM 1128 CD2 PHE A 163 7.320 26.745 52.268 1.00 11.41 C ANISOU 1128 CD2 PHE A 163 1220 1719 1396 -97 -87 79 C ATOM 1129 CE1 PHE A 163 8.102 27.932 54.640 1.00 15.62 C ANISOU 1129 CE1 PHE A 163 1799 2266 1869 -98 -145 70 C ATOM 1130 CE2 PHE A 163 6.451 26.775 53.348 1.00 11.62 C ANISOU 1130 CE2 PHE A 163 1288 1738 1391 -102 -76 90 C ATOM 1131 CZ PHE A 163 6.850 27.361 54.539 1.00 10.54 C ANISOU 1131 CZ PHE A 163 1181 1607 1216 -100 -100 89 C ATOM 1132 N SER A 164 10.068 24.460 52.454 1.00 13.40 N ANISOU 1132 N SER A 164 1423 1961 1708 -32 -164 84 N ATOM 1133 CA SER A 164 9.670 23.058 52.517 1.00 9.74 C ANISOU 1133 CA SER A 164 992 1464 1247 -9 -154 107 C ATOM 1134 C SER A 164 8.956 22.575 51.252 1.00 14.82 C ANISOU 1134 C SER A 164 1622 2095 1916 -26 -105 93 C ATOM 1135 O SER A 164 8.216 23.328 50.622 1.00 13.16 O ANISOU 1135 O SER A 164 1405 1900 1694 -52 -80 79 O ATOM 1136 CB SER A 164 8.719 22.869 53.711 1.00 14.27 C ANISOU 1136 CB SER A 164 1639 2017 1767 -11 -146 140 C ATOM 1137 OG SER A 164 8.015 21.636 53.610 1.00 13.13 O ANISOU 1137 OG SER A 164 1527 1827 1636 -9 -107 160 O ATOM 1138 N VAL A 165 9.154 21.308 50.891 1.00 12.54 N ANISOU 1138 N VAL A 165 1332 1774 1657 -5 -98 94 N ATOM 1139 CA VAL A 165 8.331 20.709 49.858 1.00 8.98 C ANISOU 1139 CA VAL A 165 879 1306 1226 -21 -60 71 C ATOM 1140 C VAL A 165 6.884 20.845 50.342 1.00 8.85 C ANISOU 1140 C VAL A 165 892 1279 1193 -52 -36 78 C ATOM 1141 O VAL A 165 6.632 21.031 51.548 1.00 10.31 O ANISOU 1141 O VAL A 165 1114 1454 1349 -54 -36 110 O ATOM 1142 CB VAL A 165 8.645 19.223 49.695 1.00 10.64 C ANISOU 1142 CB VAL A 165 1098 1468 1477 4 -52 70 C ATOM 1143 CG1 VAL A 165 10.069 19.033 49.188 1.00 11.49 C ANISOU 1143 CG1 VAL A 165 1163 1585 1617 40 -69 53 C ATOM 1144 CG2 VAL A 165 8.444 18.508 51.027 1.00 11.57 C ANISOU 1144 CG2 VAL A 165 1274 1539 1584 20 -57 117 C ATOM 1145 N ALA A 166 5.931 20.750 49.424 1.00 8.76 N ANISOU 1145 N ALA A 166 862 1268 1196 -73 -16 43 N ATOM 1146 CA ALA A 166 4.521 20.841 49.818 1.00 11.88 C ANISOU 1146 CA ALA A 166 1261 1653 1600 -103 9 34 C ATOM 1147 C ALA A 166 3.994 19.536 50.417 1.00 13.71 C ANISOU 1147 C ALA A 166 1518 1822 1871 -119 51 42 C ATOM 1148 O ALA A 166 4.265 18.447 49.900 1.00 15.50 O ANISOU 1148 O ALA A 166 1744 2012 2133 -113 58 27 O ATOM 1149 CB ALA A 166 3.668 21.247 48.652 1.00 12.80 C ANISOU 1149 CB ALA A 166 1340 1796 1727 -112 -1 -17 C ATOM 1150 N PRO A 167 3.229 19.650 51.508 1.00 11.44 N ANISOU 1150 N PRO A 167 1258 1512 1575 -141 92 65 N ATOM 1151 CA PRO A 167 2.545 18.499 52.093 1.00 11.45 C ANISOU 1151 CA PRO A 167 1291 1442 1617 -168 158 74 C ATOM 1152 C PRO A 167 1.400 18.083 51.177 1.00 15.33 C ANISOU 1152 C PRO A 167 1717 1921 2188 -209 182 2 C ATOM 1153 O PRO A 167 1.101 18.784 50.205 1.00 14.37 O ANISOU 1153 O PRO A 167 1537 1854 2070 -205 136 -48 O ATOM 1154 CB PRO A 167 2.019 19.048 53.423 1.00 12.31 C ANISOU 1154 CB PRO A 167 1448 1544 1685 -183 203 110 C ATOM 1155 CG PRO A 167 1.772 20.506 53.138 1.00 12.63 C ANISOU 1155 CG PRO A 167 1441 1655 1703 -181 167 83 C ATOM 1156 CD PRO A 167 2.891 20.915 52.196 1.00 12.21 C ANISOU 1156 CD PRO A 167 1361 1646 1630 -147 91 77 C ATOM 1157 N ASP A 168 0.779 16.949 51.469 1.00 16.51 N ANISOU 1157 N ASP A 168 1879 1994 2398 -245 250 -7 N ATOM 1158 CA ASP A 168 -0.318 16.460 50.647 1.00 14.48 C ANISOU 1158 CA ASP A 168 1548 1720 2235 -290 269 -93 C ATOM 1159 C ASP A 168 -1.499 17.420 50.683 1.00 13.93 C ANISOU 1159 C ASP A 168 1409 1693 2190 -315 275 -139 C ATOM 1160 O ASP A 168 -1.707 18.145 51.657 1.00 16.82 O ANISOU 1160 O ASP A 168 1800 2070 2519 -317 310 -99 O ATOM 1161 CB ASP A 168 -0.779 15.087 51.140 1.00 17.33 C ANISOU 1161 CB ASP A 168 1939 1975 2672 -336 363 -92 C ATOM 1162 CG ASP A 168 0.207 13.972 50.791 1.00 25.92 C ANISOU 1162 CG ASP A 168 3077 3009 3764 -308 351 -72 C ATOM 1163 OD1 ASP A 168 1.107 14.173 49.931 1.00 22.54 O ANISOU 1163 OD1 ASP A 168 2634 2631 3300 -261 272 -84 O ATOM 1164 OD2 ASP A 168 0.070 12.887 51.383 1.00 22.94 O ANISOU 1164 OD2 ASP A 168 2755 2530 3430 -332 431 -45 O ATOM 1165 N THR A 169 -2.281 17.426 49.614 1.00 23.51 N ANISOU 1165 N THR A 169 2535 2933 3466 -327 234 -230 N ATOM 1166 CA THR A 169 -3.526 18.166 49.635 1.00 15.96 C ANISOU 1166 CA THR A 169 1497 2007 2561 -346 238 -287 C ATOM 1167 C THR A 169 -4.348 17.625 50.795 1.00 14.99 C ANISOU 1167 C THR A 169 1374 1812 2510 -409 364 -282 C ATOM 1168 O THR A 169 -4.393 16.402 51.037 1.00 17.45 O ANISOU 1168 O THR A 169 1711 2042 2879 -452 437 -281 O ATOM 1169 CB THR A 169 -4.341 17.995 48.323 1.00 31.89 C ANISOU 1169 CB THR A 169 3415 4052 4650 -349 166 -402 C ATOM 1170 OG1 THR A 169 -4.946 16.699 48.296 1.00 45.63 O ANISOU 1170 OG1 THR A 169 5116 5719 6503 -411 226 -464 O ATOM 1171 CG2 THR A 169 -3.457 18.145 47.111 1.00 28.79 C ANISOU 1171 CG2 THR A 169 3051 3708 4179 -293 66 -406 C ATOM 1172 N ASP A 170 -5.003 18.525 51.511 1.00 21.40 N ANISOU 1172 N ASP A 170 2164 2645 3321 -415 402 -277 N ATOM 1173 CA ASP A 170 -5.911 18.124 52.593 1.00 23.49 C ANISOU 1173 CA ASP A 170 2424 2843 3657 -478 542 -281 C ATOM 1174 C ASP A 170 -5.182 17.668 53.862 1.00 20.92 C ANISOU 1174 C ASP A 170 2243 2456 3249 -483 633 -172 C ATOM 1175 O ASP A 170 -5.821 17.275 54.832 1.00 22.99 O ANISOU 1175 O ASP A 170 2536 2651 3547 -534 767 -157 O ATOM 1176 CB ASP A 170 -6.897 17.037 52.134 1.00 28.02 C ANISOU 1176 CB ASP A 170 2904 3356 4384 -547 596 -377 C ATOM 1177 CG ASP A 170 -7.783 17.487 50.973 1.00 36.31 C ANISOU 1177 CG ASP A 170 3822 4471 5504 -524 488 -493 C ATOM 1178 OD1 ASP A 170 -7.819 18.703 50.682 1.00 31.42 O ANISOU 1178 OD1 ASP A 170 3166 3931 4841 -474 408 -500 O ATOM 1179 OD2 ASP A 170 -8.453 16.621 50.356 1.00 31.34 O ANISOU 1179 OD2 ASP A 170 3141 3808 4960 -546 478 -574 O ATOM 1180 N SER A 171 -3.854 17.746 53.864 1.00 13.67 N ANISOU 1180 N SER A 171 1415 1559 2220 -427 560 -97 N ATOM 1181 CA SER A 171 -3.073 17.385 55.042 1.00 18.58 C ANISOU 1181 CA SER A 171 2178 2133 2749 -410 613 4 C ATOM 1182 C SER A 171 -3.285 18.401 56.161 1.00 16.86 C ANISOU 1182 C SER A 171 2009 1942 2456 -402 655 40 C ATOM 1183 O SER A 171 -3.656 19.549 55.912 1.00 12.88 O ANISOU 1183 O SER A 171 1435 1505 1953 -391 613 -1 O ATOM 1184 CB SER A 171 -1.577 17.343 54.693 1.00 12.57 C ANISOU 1184 CB SER A 171 1471 1401 1903 -344 504 55 C ATOM 1185 OG SER A 171 -1.132 18.634 54.278 1.00 14.12 O ANISOU 1185 OG SER A 171 1629 1691 2044 -304 407 45 O ATOM 1186 N TYR A 172 -3.062 17.967 57.397 1.00 17.23 N ANISOU 1186 N TYR A 172 2185 1928 2432 -403 740 115 N ATOM 1187 CA TYR A 172 -3.054 18.884 58.527 1.00 14.97 C ANISOU 1187 CA TYR A 172 1976 1668 2046 -385 771 153 C ATOM 1188 C TYR A 172 -2.077 20.023 58.272 1.00 13.71 C ANISOU 1188 C TYR A 172 1807 1599 1802 -323 631 160 C ATOM 1189 O TYR A 172 -2.327 21.182 58.619 1.00 12.82 O ANISOU 1189 O TYR A 172 1681 1536 1655 -316 624 141 O ATOM 1190 CB TYR A 172 -2.662 18.138 59.799 1.00 16.32 C ANISOU 1190 CB TYR A 172 2319 1763 2118 -373 852 245 C ATOM 1191 CG TYR A 172 -2.399 19.059 60.962 1.00 18.07 C ANISOU 1191 CG TYR A 172 2643 2018 2203 -339 856 285 C ATOM 1192 CD1 TYR A 172 -3.428 19.814 61.518 1.00 19.79 C ANISOU 1192 CD1 TYR A 172 2842 2246 2433 -376 956 248 C ATOM 1193 CD2 TYR A 172 -1.119 19.179 61.511 1.00 16.59 C ANISOU 1193 CD2 TYR A 172 2568 1854 1881 -266 755 350 C ATOM 1194 CE1 TYR A 172 -3.199 20.667 62.586 1.00 22.83 C ANISOU 1194 CE1 TYR A 172 3327 2660 2687 -345 962 275 C ATOM 1195 CE2 TYR A 172 -0.882 20.043 62.583 1.00 18.06 C ANISOU 1195 CE2 TYR A 172 2850 2075 1939 -234 747 372 C ATOM 1196 CZ TYR A 172 -1.925 20.779 63.109 1.00 25.23 C ANISOU 1196 CZ TYR A 172 3748 2989 2851 -275 854 335 C ATOM 1197 OH TYR A 172 -1.706 21.629 64.170 1.00 24.02 O ANISOU 1197 OH TYR A 172 3695 2866 2565 -244 850 348 O ATOM 1198 N GLU A 173 -0.958 19.683 57.650 1.00 13.36 N ANISOU 1198 N GLU A 173 1768 1572 1737 -282 528 182 N ATOM 1199 CA GLU A 173 0.144 20.626 57.479 1.00 17.37 C ANISOU 1199 CA GLU A 173 2275 2151 2172 -230 408 192 C ATOM 1200 C GLU A 173 -0.122 21.746 56.469 1.00 15.66 C ANISOU 1200 C GLU A 173 1947 2003 1999 -231 349 130 C ATOM 1201 O GLU A 173 0.574 22.761 56.479 1.00 17.19 O ANISOU 1201 O GLU A 173 2143 2248 2139 -201 279 133 O ATOM 1202 CB GLU A 173 1.407 19.876 57.083 1.00 12.55 C ANISOU 1202 CB GLU A 173 1690 1532 1545 -187 330 225 C ATOM 1203 CG GLU A 173 1.994 18.982 58.179 1.00 17.07 C ANISOU 1203 CG GLU A 173 2396 2044 2044 -153 351 300 C ATOM 1204 CD GLU A 173 1.184 17.722 58.449 1.00 21.18 C ANISOU 1204 CD GLU A 173 2967 2467 2613 -192 470 322 C ATOM 1205 OE1 GLU A 173 0.376 17.316 57.579 1.00 14.28 O ANISOU 1205 OE1 GLU A 173 2004 1573 1851 -243 515 267 O ATOM 1206 OE2 GLU A 173 1.381 17.122 59.539 1.00 16.64 O ANISOU 1206 OE2 GLU A 173 2529 1831 1963 -168 516 393 O ATOM 1207 N MET A 174 -1.112 21.573 55.599 1.00 10.95 N ANISOU 1207 N MET A 174 1258 1404 1500 -263 372 71 N ATOM 1208 CA MET A 174 -1.269 22.513 54.480 1.00 10.35 C ANISOU 1208 CA MET A 174 1092 1388 1453 -247 298 19 C ATOM 1209 C MET A 174 -1.404 23.996 54.879 1.00 10.10 C ANISOU 1209 C MET A 174 1060 1399 1380 -230 283 14 C ATOM 1210 O MET A 174 -0.644 24.816 54.392 1.00 13.17 O ANISOU 1210 O MET A 174 1446 1827 1730 -199 209 20 O ATOM 1211 CB MET A 174 -2.370 22.083 53.494 1.00 10.64 C ANISOU 1211 CB MET A 174 1029 1419 1596 -273 306 -54 C ATOM 1212 CG MET A 174 -2.441 22.946 52.233 1.00 16.40 C ANISOU 1212 CG MET A 174 1690 2207 2334 -239 213 -99 C ATOM 1213 SD MET A 174 -0.916 22.904 51.255 1.00 20.59 S ANISOU 1213 SD MET A 174 2257 2766 2800 -198 124 -67 S ATOM 1214 CE MET A 174 -0.994 21.244 50.551 1.00 17.39 C ANISOU 1214 CE MET A 174 1831 2318 2458 -221 135 -100 C ATOM 1215 N PRO A 175 -2.360 24.347 55.759 1.00 12.97 N ANISOU 1215 N PRO A 175 1425 1746 1755 -252 363 0 N ATOM 1216 CA PRO A 175 -2.469 25.796 56.026 1.00 13.61 C ANISOU 1216 CA PRO A 175 1503 1863 1804 -229 344 -14 C ATOM 1217 C PRO A 175 -1.209 26.392 56.649 1.00 12.62 C ANISOU 1217 C PRO A 175 1463 1757 1577 -204 296 32 C ATOM 1218 O PRO A 175 -0.838 27.538 56.360 1.00 11.74 O ANISOU 1218 O PRO A 175 1339 1676 1446 -182 242 21 O ATOM 1219 CB PRO A 175 -3.639 25.903 57.016 1.00 11.62 C ANISOU 1219 CB PRO A 175 1250 1583 1580 -259 458 -37 C ATOM 1220 CG PRO A 175 -3.774 24.508 57.615 1.00 16.37 C ANISOU 1220 CG PRO A 175 1904 2128 2188 -298 546 -8 C ATOM 1221 CD PRO A 175 -3.341 23.555 56.521 1.00 18.70 C ANISOU 1221 CD PRO A 175 2160 2417 2527 -297 484 -8 C ATOM 1222 N SER A 176 -0.558 25.637 57.522 1.00 12.52 N ANISOU 1222 N SER A 176 1537 1720 1500 -205 314 79 N ATOM 1223 CA SER A 176 0.643 26.164 58.154 1.00 12.84 C ANISOU 1223 CA SER A 176 1648 1782 1450 -176 252 108 C ATOM 1224 C SER A 176 1.726 26.350 57.087 1.00 15.11 C ANISOU 1224 C SER A 176 1886 2099 1754 -156 156 106 C ATOM 1225 O SER A 176 2.469 27.339 57.096 1.00 16.63 O ANISOU 1225 O SER A 176 2078 2320 1919 -142 102 97 O ATOM 1226 CB SER A 176 1.113 25.228 59.271 1.00 15.92 C ANISOU 1226 CB SER A 176 2147 2138 1762 -166 275 160 C ATOM 1227 OG SER A 176 2.308 25.718 59.868 1.00 19.59 O ANISOU 1227 OG SER A 176 2668 2631 2143 -131 193 174 O ATOM 1228 N TRP A 177 1.814 25.396 56.166 1.00 11.08 N ANISOU 1228 N TRP A 177 1337 1578 1295 -157 145 109 N ATOM 1229 CA TRP A 177 2.782 25.468 55.063 1.00 8.92 C ANISOU 1229 CA TRP A 177 1021 1330 1040 -139 75 104 C ATOM 1230 C TRP A 177 2.518 26.714 54.200 1.00 9.85 C ANISOU 1230 C TRP A 177 1087 1476 1179 -138 54 72 C ATOM 1231 O TRP A 177 3.440 27.445 53.815 1.00 10.64 O ANISOU 1231 O TRP A 177 1182 1597 1266 -127 12 72 O ATOM 1232 CB TRP A 177 2.690 24.192 54.195 1.00 10.70 C ANISOU 1232 CB TRP A 177 1217 1532 1316 -143 81 102 C ATOM 1233 CG TRP A 177 3.629 24.172 52.999 1.00 10.45 C ANISOU 1233 CG TRP A 177 1146 1522 1301 -125 27 92 C ATOM 1234 CD1 TRP A 177 4.911 23.704 52.968 1.00 13.62 C ANISOU 1234 CD1 TRP A 177 1558 1923 1692 -102 -10 110 C ATOM 1235 CD2 TRP A 177 3.340 24.628 51.673 1.00 8.28 C ANISOU 1235 CD2 TRP A 177 822 1270 1052 -123 10 58 C ATOM 1236 NE1 TRP A 177 5.441 23.857 51.712 1.00 9.52 N ANISOU 1236 NE1 TRP A 177 997 1425 1197 -95 -31 89 N ATOM 1237 CE2 TRP A 177 4.495 24.417 50.896 1.00 10.84 C ANISOU 1237 CE2 TRP A 177 1138 1605 1375 -106 -20 61 C ATOM 1238 CE3 TRP A 177 2.211 25.194 51.066 1.00 10.05 C ANISOU 1238 CE3 TRP A 177 1013 1507 1299 -126 15 24 C ATOM 1239 CZ2 TRP A 177 4.564 24.754 49.542 1.00 14.00 C ANISOU 1239 CZ2 TRP A 177 1515 2024 1780 -96 -33 37 C ATOM 1240 CZ3 TRP A 177 2.277 25.532 49.720 1.00 14.73 C ANISOU 1240 CZ3 TRP A 177 1583 2121 1892 -107 -19 3 C ATOM 1241 CH2 TRP A 177 3.450 25.318 48.974 1.00 13.71 C ANISOU 1241 CH2 TRP A 177 1465 1999 1745 -95 -36 13 C ATOM 1242 N GLN A 178 1.245 26.958 53.902 1.00 12.49 N ANISOU 1242 N GLN A 178 1385 1807 1552 -147 87 43 N ATOM 1243 CA GLN A 178 0.872 28.096 53.083 1.00 10.36 C ANISOU 1243 CA GLN A 178 1079 1557 1299 -130 62 18 C ATOM 1244 C GLN A 178 1.206 29.413 53.784 1.00 9.19 C ANISOU 1244 C GLN A 178 965 1413 1114 -126 60 21 C ATOM 1245 O GLN A 178 1.715 30.351 53.169 1.00 13.79 O ANISOU 1245 O GLN A 178 1546 2002 1690 -113 30 21 O ATOM 1246 CB GLN A 178 -0.622 28.042 52.762 1.00 12.56 C ANISOU 1246 CB GLN A 178 1304 1832 1638 -130 87 -24 C ATOM 1247 CG GLN A 178 -1.010 26.870 51.878 1.00 8.89 C ANISOU 1247 CG GLN A 178 794 1363 1221 -137 76 -48 C ATOM 1248 CD GLN A 178 -2.481 26.849 51.606 1.00 15.46 C ANISOU 1248 CD GLN A 178 1554 2194 2128 -138 90 -106 C ATOM 1249 OE1 GLN A 178 -3.283 26.546 52.494 1.00 15.79 O ANISOU 1249 OE1 GLN A 178 1576 2212 2210 -169 161 -123 O ATOM 1250 NE2 GLN A 178 -2.861 27.205 50.389 1.00 14.87 N ANISOU 1250 NE2 GLN A 178 1437 2143 2071 -102 24 -141 N ATOM 1251 N GLU A 179 0.918 29.480 55.079 1.00 8.76 N ANISOU 1251 N GLU A 179 947 1347 1032 -138 101 22 N ATOM 1252 CA GLU A 179 1.180 30.699 55.827 1.00 10.77 C ANISOU 1252 CA GLU A 179 1237 1603 1251 -136 101 13 C ATOM 1253 C GLU A 179 2.682 30.982 55.869 1.00 17.43 C ANISOU 1253 C GLU A 179 2105 2458 2061 -136 45 26 C ATOM 1254 O GLU A 179 3.115 32.138 55.762 1.00 11.96 O ANISOU 1254 O GLU A 179 1413 1762 1369 -137 28 10 O ATOM 1255 CB GLU A 179 0.612 30.588 57.228 1.00 13.28 C ANISOU 1255 CB GLU A 179 1606 1908 1531 -148 160 8 C ATOM 1256 CG GLU A 179 0.597 31.896 57.982 1.00 18.25 C ANISOU 1256 CG GLU A 179 2270 2536 2129 -144 170 -18 C ATOM 1257 CD GLU A 179 1.727 31.992 58.959 1.00 28.54 C ANISOU 1257 CD GLU A 179 3644 3848 3354 -146 132 -12 C ATOM 1258 OE1 GLU A 179 2.486 31.006 59.075 1.00 30.72 O ANISOU 1258 OE1 GLU A 179 3941 4132 3601 -143 97 19 O ATOM 1259 OE2 GLU A 179 1.859 33.048 59.616 1.00 34.55 O ANISOU 1259 OE2 GLU A 179 4437 4606 4084 -147 130 -43 O ATOM 1260 N GLY A 180 3.461 29.912 56.016 1.00 12.83 N ANISOU 1260 N GLY A 180 1534 1880 1460 -136 20 49 N ATOM 1261 CA GLY A 180 4.915 29.981 56.031 1.00 10.52 C ANISOU 1261 CA GLY A 180 1241 1600 1155 -132 -37 52 C ATOM 1262 C GLY A 180 5.504 30.419 54.707 1.00 13.56 C ANISOU 1262 C GLY A 180 1576 1990 1588 -135 -53 45 C ATOM 1263 O GLY A 180 6.493 31.169 54.659 1.00 13.27 O ANISOU 1263 O GLY A 180 1526 1955 1560 -145 -78 28 O ATOM 1264 N LEU A 181 4.912 29.945 53.620 1.00 12.72 N ANISOU 1264 N LEU A 181 1443 1881 1510 -128 -35 53 N ATOM 1265 CA LEU A 181 5.339 30.361 52.292 1.00 14.79 C ANISOU 1265 CA LEU A 181 1680 2144 1797 -125 -38 52 C ATOM 1266 C LEU A 181 5.071 31.864 52.089 1.00 13.17 C ANISOU 1266 C LEU A 181 1488 1923 1593 -127 -24 42 C ATOM 1267 O LEU A 181 5.910 32.589 51.568 1.00 13.74 O ANISOU 1267 O LEU A 181 1561 1984 1677 -137 -19 42 O ATOM 1268 CB LEU A 181 4.612 29.542 51.214 1.00 9.69 C ANISOU 1268 CB LEU A 181 1016 1500 1165 -110 -32 54 C ATOM 1269 CG LEU A 181 4.841 30.011 49.775 1.00 14.22 C ANISOU 1269 CG LEU A 181 1590 2074 1740 -96 -32 55 C ATOM 1270 CD1 LEU A 181 6.257 29.660 49.332 1.00 13.77 C ANISOU 1270 CD1 LEU A 181 1522 2019 1691 -106 -28 60 C ATOM 1271 CD2 LEU A 181 3.815 29.419 48.811 1.00 12.67 C ANISOU 1271 CD2 LEU A 181 1383 1884 1545 -72 -42 42 C ATOM 1272 N ILE A 182 3.895 32.317 52.513 1.00 14.53 N ANISOU 1272 N ILE A 182 1671 2087 1761 -117 -9 33 N ATOM 1273 CA ILE A 182 3.519 33.732 52.414 1.00 14.20 C ANISOU 1273 CA ILE A 182 1649 2022 1726 -108 5 24 C ATOM 1274 C ILE A 182 4.486 34.581 53.218 1.00 10.17 C ANISOU 1274 C ILE A 182 1157 1496 1210 -137 5 8 C ATOM 1275 O ILE A 182 4.920 35.661 52.780 1.00 12.65 O ANISOU 1275 O ILE A 182 1485 1779 1541 -145 19 5 O ATOM 1276 CB ILE A 182 2.093 33.969 52.916 1.00 13.88 C ANISOU 1276 CB ILE A 182 1603 1976 1694 -89 24 6 C ATOM 1277 CG1 ILE A 182 1.106 33.314 51.959 1.00 16.15 C ANISOU 1277 CG1 ILE A 182 1855 2275 2006 -60 12 4 C ATOM 1278 CG2 ILE A 182 1.801 35.461 52.996 1.00 13.02 C ANISOU 1278 CG2 ILE A 182 1519 1834 1595 -75 38 -7 C ATOM 1279 CD1 ILE A 182 1.224 33.811 50.544 1.00 17.52 C ANISOU 1279 CD1 ILE A 182 2040 2441 2175 -27 -14 18 C ATOM 1280 N HIS A 183 4.838 34.066 54.388 1.00 9.80 N ANISOU 1280 N HIS A 183 1117 1468 1139 -152 -10 -4 N ATOM 1281 CA HIS A 183 5.823 34.696 55.252 1.00 15.19 C ANISOU 1281 CA HIS A 183 1812 2146 1812 -176 -32 -34 C ATOM 1282 C HIS A 183 7.113 35.011 54.495 1.00 11.68 C ANISOU 1282 C HIS A 183 1334 1693 1411 -198 -43 -40 C ATOM 1283 O HIS A 183 7.634 36.126 54.572 1.00 13.23 O ANISOU 1283 O HIS A 183 1531 1861 1635 -225 -33 -69 O ATOM 1284 CB HIS A 183 6.141 33.789 56.444 1.00 12.18 C ANISOU 1284 CB HIS A 183 1451 1794 1384 -172 -67 -38 C ATOM 1285 CG HIS A 183 7.232 34.316 57.324 1.00 14.14 C ANISOU 1285 CG HIS A 183 1706 2048 1618 -188 -116 -80 C ATOM 1286 ND1 HIS A 183 6.978 34.965 58.516 1.00 16.94 N ANISOU 1286 ND1 HIS A 183 2112 2400 1925 -190 -122 -117 N ATOM 1287 CD2 HIS A 183 8.581 34.314 57.179 1.00 9.99 C ANISOU 1287 CD2 HIS A 183 1136 1532 1128 -202 -164 -104 C ATOM 1288 CE1 HIS A 183 8.122 35.322 59.075 1.00 15.62 C ANISOU 1288 CE1 HIS A 183 1934 2242 1758 -204 -184 -164 C ATOM 1289 NE2 HIS A 183 9.109 34.942 58.280 1.00 11.82 N ANISOU 1289 NE2 HIS A 183 1386 1768 1335 -212 -211 -159 N ATOM 1290 N GLU A 184 7.639 34.035 53.764 1.00 18.44 N ANISOU 1290 N GLU A 184 2158 2567 2281 -192 -52 -19 N ATOM 1291 CA GLU A 184 8.914 34.250 53.087 1.00 17.34 C ANISOU 1291 CA GLU A 184 1978 2420 2191 -217 -46 -31 C ATOM 1292 C GLU A 184 8.774 35.278 51.967 1.00 11.56 C ANISOU 1292 C GLU A 184 1265 1645 1481 -228 14 -17 C ATOM 1293 O GLU A 184 9.650 36.119 51.763 1.00 13.47 O ANISOU 1293 O GLU A 184 1493 1855 1769 -265 43 -39 O ATOM 1294 CB GLU A 184 9.503 32.935 52.548 1.00 17.05 C ANISOU 1294 CB GLU A 184 1904 2409 2166 -202 -61 -16 C ATOM 1295 CG GLU A 184 9.677 31.830 53.609 1.00 21.22 C ANISOU 1295 CG GLU A 184 2429 2967 2667 -180 -121 -18 C ATOM 1296 CD GLU A 184 10.663 32.193 54.723 1.00 29.93 C ANISOU 1296 CD GLU A 184 3512 4081 3778 -189 -179 -63 C ATOM 1297 OE1 GLU A 184 11.425 33.170 54.579 1.00 26.61 O ANISOU 1297 OE1 GLU A 184 3055 3647 3409 -224 -172 -104 O ATOM 1298 OE2 GLU A 184 10.677 31.482 55.751 1.00 30.92 O ANISOU 1298 OE2 GLU A 184 3665 4227 3858 -160 -234 -61 O ATOM 1299 N ILE A 185 7.669 35.217 51.238 1.00 12.41 N ANISOU 1299 N ILE A 185 1409 1748 1560 -194 32 17 N ATOM 1300 CA ILE A 185 7.432 36.184 50.176 1.00 12.25 C ANISOU 1300 CA ILE A 185 1431 1683 1542 -186 79 40 C ATOM 1301 C ILE A 185 7.361 37.603 50.765 1.00 11.24 C ANISOU 1301 C ILE A 185 1331 1505 1434 -205 100 21 C ATOM 1302 O ILE A 185 7.870 38.566 50.188 1.00 12.70 O ANISOU 1302 O ILE A 185 1545 1635 1646 -226 152 27 O ATOM 1303 CB ILE A 185 6.138 35.846 49.414 1.00 13.99 C ANISOU 1303 CB ILE A 185 1681 1913 1723 -131 67 69 C ATOM 1304 CG1 ILE A 185 6.304 34.509 48.677 1.00 16.82 C ANISOU 1304 CG1 ILE A 185 2016 2309 2067 -118 52 79 C ATOM 1305 CG2 ILE A 185 5.737 37.000 48.455 1.00 12.35 C ANISOU 1305 CG2 ILE A 185 1538 1652 1501 -102 100 98 C ATOM 1306 CD1 ILE A 185 5.023 33.997 48.051 1.00 13.43 C ANISOU 1306 CD1 ILE A 185 1597 1897 1608 -69 23 87 C ATOM 1307 N ILE A 186 6.728 37.724 51.925 1.00 11.89 N ANISOU 1307 N ILE A 186 1414 1600 1504 -199 71 -5 N ATOM 1308 CA ILE A 186 6.566 39.034 52.545 1.00 10.59 C ANISOU 1308 CA ILE A 186 1279 1386 1357 -213 91 -33 C ATOM 1309 C ILE A 186 7.924 39.671 52.855 1.00 11.63 C ANISOU 1309 C ILE A 186 1390 1490 1539 -274 105 -75 C ATOM 1310 O ILE A 186 8.106 40.888 52.675 1.00 12.28 O ANISOU 1310 O ILE A 186 1503 1504 1659 -297 151 -86 O ATOM 1311 CB ILE A 186 5.675 38.943 53.792 1.00 11.44 C ANISOU 1311 CB ILE A 186 1393 1517 1436 -196 67 -61 C ATOM 1312 CG1 ILE A 186 4.235 38.635 53.374 1.00 14.59 C ANISOU 1312 CG1 ILE A 186 1800 1925 1817 -141 71 -33 C ATOM 1313 CG2 ILE A 186 5.721 40.234 54.588 1.00 11.47 C ANISOU 1313 CG2 ILE A 186 1426 1473 1458 -217 85 -107 C ATOM 1314 CD1 ILE A 186 3.334 38.337 54.526 1.00 21.61 C ANISOU 1314 CD1 ILE A 186 2688 2839 2685 -130 69 -60 C ATOM 1315 N HIS A 187 8.886 38.862 53.306 1.00 17.41 N ANISOU 1315 N HIS A 187 2066 2267 2282 -299 65 -102 N ATOM 1316 CA HIS A 187 10.258 39.357 53.450 1.00 14.59 C ANISOU 1316 CA HIS A 187 1662 1889 1993 -358 72 -154 C ATOM 1317 C HIS A 187 10.669 40.127 52.196 1.00 19.34 C ANISOU 1317 C HIS A 187 2280 2423 2646 -386 162 -129 C ATOM 1318 O HIS A 187 11.129 41.275 52.278 1.00 16.59 O ANISOU 1318 O HIS A 187 1939 2009 2356 -433 208 -163 O ATOM 1319 CB HIS A 187 11.254 38.220 53.695 1.00 13.30 C ANISOU 1319 CB HIS A 187 1426 1784 1845 -363 17 -176 C ATOM 1320 CG HIS A 187 11.292 37.738 55.110 1.00 16.78 C ANISOU 1320 CG HIS A 187 1859 2274 2244 -347 -73 -216 C ATOM 1321 ND1 HIS A 187 11.475 38.587 56.180 1.00 22.34 N ANISOU 1321 ND1 HIS A 187 2573 2965 2950 -371 -106 -282 N ATOM 1322 CD2 HIS A 187 11.205 36.491 55.629 1.00 15.03 C ANISOU 1322 CD2 HIS A 187 1634 2107 1970 -307 -134 -199 C ATOM 1323 CE1 HIS A 187 11.470 37.885 57.301 1.00 19.90 C ANISOU 1323 CE1 HIS A 187 2276 2708 2578 -340 -187 -302 C ATOM 1324 NE2 HIS A 187 11.311 36.609 56.993 1.00 21.49 N ANISOU 1324 NE2 HIS A 187 2472 2947 2746 -301 -203 -247 N ATOM 1325 N HIS A 188 10.488 39.502 51.034 1.00 17.16 N ANISOU 1325 N HIS A 188 2020 2156 2344 -357 193 -70 N ATOM 1326 CA HIS A 188 10.923 40.121 49.783 1.00 21.88 C ANISOU 1326 CA HIS A 188 2654 2690 2970 -377 289 -37 C ATOM 1327 C HIS A 188 10.102 41.333 49.405 1.00 18.25 C ANISOU 1327 C HIS A 188 2290 2153 2491 -356 337 -1 C ATOM 1328 O HIS A 188 10.652 42.391 49.114 1.00 13.66 O ANISOU 1328 O HIS A 188 1739 1489 1963 -401 416 -6 O ATOM 1329 CB HIS A 188 10.879 39.130 48.622 1.00 13.10 C ANISOU 1329 CB HIS A 188 1553 1609 1814 -342 306 14 C ATOM 1330 CG HIS A 188 12.102 38.281 48.506 1.00 18.99 C ANISOU 1330 CG HIS A 188 2213 2390 2611 -376 313 -19 C ATOM 1331 ND1 HIS A 188 13.378 38.799 48.592 1.00 20.87 N ANISOU 1331 ND1 HIS A 188 2390 2593 2946 -445 367 -69 N ATOM 1332 CD2 HIS A 188 12.249 36.954 48.282 1.00 18.24 C ANISOU 1332 CD2 HIS A 188 2077 2355 2496 -348 276 -14 C ATOM 1333 CE1 HIS A 188 14.256 37.823 48.443 1.00 23.98 C ANISOU 1333 CE1 HIS A 188 2701 3031 3378 -453 358 -96 C ATOM 1334 NE2 HIS A 188 13.595 36.694 48.250 1.00 18.37 N ANISOU 1334 NE2 HIS A 188 2009 2376 2594 -392 304 -59 N ATOM 1335 N VAL A 189 8.784 41.189 49.391 1.00 15.35 N ANISOU 1335 N VAL A 189 1970 1805 2057 -287 294 34 N ATOM 1336 CA VAL A 189 7.963 42.253 48.825 1.00 15.98 C ANISOU 1336 CA VAL A 189 2144 1811 2117 -244 331 77 C ATOM 1337 C VAL A 189 7.796 43.457 49.755 1.00 18.84 C ANISOU 1337 C VAL A 189 2523 2111 2523 -267 344 36 C ATOM 1338 O VAL A 189 7.424 44.530 49.307 1.00 17.42 O ANISOU 1338 O VAL A 189 2424 1846 2349 -244 393 67 O ATOM 1339 CB VAL A 189 6.585 41.745 48.372 1.00 17.49 C ANISOU 1339 CB VAL A 189 2368 2042 2237 -154 276 117 C ATOM 1340 CG1 VAL A 189 6.740 40.575 47.406 1.00 11.15 C ANISOU 1340 CG1 VAL A 189 1555 1294 1389 -133 262 147 C ATOM 1341 CG2 VAL A 189 5.765 41.321 49.562 1.00 16.37 C ANISOU 1341 CG2 VAL A 189 2172 1955 2094 -138 208 76 C ATOM 1342 N THR A 190 8.079 43.298 51.041 1.00 14.89 N ANISOU 1342 N THR A 190 1958 1650 2050 -305 299 -33 N ATOM 1343 CA THR A 190 7.982 44.453 51.940 1.00 15.80 C ANISOU 1343 CA THR A 190 2093 1704 2205 -330 312 -85 C ATOM 1344 C THR A 190 9.338 44.855 52.539 1.00 17.90 C ANISOU 1344 C THR A 190 2305 1948 2549 -422 329 -161 C ATOM 1345 O THR A 190 9.466 45.923 53.132 1.00 18.48 O ANISOU 1345 O THR A 190 2397 1955 2670 -458 352 -215 O ATOM 1346 CB THR A 190 6.994 44.213 53.100 1.00 21.45 C ANISOU 1346 CB THR A 190 2799 2470 2879 -292 249 -119 C ATOM 1347 OG1 THR A 190 7.586 43.325 54.061 1.00 14.58 O ANISOU 1347 OG1 THR A 190 1864 1679 1996 -324 189 -169 O ATOM 1348 CG2 THR A 190 5.664 43.632 52.588 1.00 11.82 C ANISOU 1348 CG2 THR A 190 1600 1287 1604 -208 225 -63 C ATOM 1349 N GLY A 191 10.342 43.995 52.404 1.00 16.79 N ANISOU 1349 N GLY A 191 2090 1861 2429 -459 311 -177 N ATOM 1350 CA GLY A 191 11.619 44.223 53.062 1.00 18.64 C ANISOU 1350 CA GLY A 191 2245 2091 2746 -538 301 -267 C ATOM 1351 C GLY A 191 11.570 44.096 54.579 1.00 22.15 C ANISOU 1351 C GLY A 191 2658 2590 3169 -539 203 -347 C ATOM 1352 O GLY A 191 12.508 44.510 55.275 1.00 17.27 O ANISOU 1352 O GLY A 191 1982 1962 2617 -599 177 -440 O ATOM 1353 N SER A 192 10.479 43.537 55.099 1.00 22.53 N ANISOU 1353 N SER A 192 2744 2693 3124 -473 151 -318 N ATOM 1354 CA SER A 192 10.323 43.334 56.540 1.00 17.69 C ANISOU 1354 CA SER A 192 2128 2132 2462 -464 69 -382 C ATOM 1355 C SER A 192 11.290 42.251 57.020 1.00 23.39 C ANISOU 1355 C SER A 192 2776 2933 3176 -472 -16 -415 C ATOM 1356 O SER A 192 11.710 41.403 56.229 1.00 19.46 O ANISOU 1356 O SER A 192 2236 2464 2694 -464 -12 -371 O ATOM 1357 CB SER A 192 8.876 42.947 56.887 1.00 15.97 C ANISOU 1357 CB SER A 192 1970 1944 2152 -395 61 -337 C ATOM 1358 OG SER A 192 8.516 41.689 56.328 1.00 16.72 O ANISOU 1358 OG SER A 192 2051 2098 2205 -353 46 -267 O ATOM 1359 N SER A 193 11.642 42.295 58.306 1.00 13.92 N ANISOU 1359 N SER A 193 1570 1767 1950 -479 -98 -496 N ATOM 1360 CA SER A 193 12.509 41.286 58.932 1.00 23.32 C ANISOU 1360 CA SER A 193 2705 3035 3121 -466 -202 -531 C ATOM 1361 C SER A 193 11.756 40.502 60.011 1.00 21.92 C ANISOU 1361 C SER A 193 2599 2918 2811 -404 -266 -513 C ATOM 1362 O SER A 193 10.582 40.747 60.269 1.00 23.53 O ANISOU 1362 O SER A 193 2881 3108 2953 -379 -220 -483 O ATOM 1363 CB SER A 193 13.735 41.951 59.565 1.00 25.00 C ANISOU 1363 CB SER A 193 2850 3239 3411 -522 -262 -653 C ATOM 1364 OG SER A 193 14.565 42.549 58.583 1.00 29.76 O ANISOU 1364 OG SER A 193 3375 3783 4150 -589 -190 -673 O ATOM 1365 N ASP A 194 12.433 39.545 60.625 1.00 16.11 N ANISOU 1365 N ASP A 194 1838 2246 2037 -375 -365 -532 N ATOM 1366 CA ASP A 194 11.908 38.870 61.802 1.00 20.40 C ANISOU 1366 CA ASP A 194 2466 2837 2446 -318 -426 -523 C ATOM 1367 C ASP A 194 12.544 39.562 63.022 1.00 20.18 C ANISOU 1367 C ASP A 194 2453 2822 2391 -330 -519 -637 C ATOM 1368 O ASP A 194 13.426 40.403 62.863 1.00 20.48 O ANISOU 1368 O ASP A 194 2415 2834 2533 -385 -538 -721 O ATOM 1369 CB ASP A 194 12.266 37.369 61.770 1.00 20.82 C ANISOU 1369 CB ASP A 194 2505 2944 2462 -266 -486 -468 C ATOM 1370 CG ASP A 194 11.699 36.628 60.543 1.00 23.67 C ANISOU 1370 CG ASP A 194 2848 3294 2853 -257 -403 -370 C ATOM 1371 OD1 ASP A 194 10.544 36.831 60.125 1.00 23.78 O ANISOU 1371 OD1 ASP A 194 2906 3281 2850 -257 -316 -320 O ATOM 1372 OD2 ASP A 194 12.408 35.774 59.993 1.00 23.96 O ANISOU 1372 OD2 ASP A 194 2822 3351 2932 -243 -432 -349 O ATOM 1373 N PRO A 195 12.091 39.233 64.246 1.00 20.98 N ANISOU 1373 N PRO A 195 2659 2959 2354 -282 -570 -646 N ATOM 1374 CA PRO A 195 12.626 39.956 65.409 1.00 22.79 C ANISOU 1374 CA PRO A 195 2918 3200 2541 -289 -662 -764 C ATOM 1375 C PRO A 195 14.137 39.779 65.507 1.00 27.73 C ANISOU 1375 C PRO A 195 3437 3861 3238 -295 -797 -846 C ATOM 1376 O PRO A 195 14.639 38.712 65.156 1.00 22.32 O ANISOU 1376 O PRO A 195 2704 3212 2566 -257 -844 -796 O ATOM 1377 CB PRO A 195 11.916 39.294 66.598 1.00 21.40 C ANISOU 1377 CB PRO A 195 2887 3063 2179 -220 -691 -734 C ATOM 1378 CG PRO A 195 10.628 38.743 66.001 1.00 18.60 C ANISOU 1378 CG PRO A 195 2576 2687 1802 -206 -558 -613 C ATOM 1379 CD PRO A 195 11.033 38.275 64.622 1.00 25.90 C ANISOU 1379 CD PRO A 195 3385 3603 2853 -225 -533 -556 C ATOM 1380 N SER A 196 14.843 40.811 65.957 1.00 35.29 N ANISOU 1380 N SER A 196 4350 4804 4254 -342 -855 -977 N ATOM 1381 CA SER A 196 16.307 40.785 66.012 1.00 43.06 C ANISOU 1381 CA SER A 196 5219 5801 5339 -353 -943 -1029 C ATOM 1382 C SER A 196 16.827 39.823 67.066 1.00 48.31 C ANISOU 1382 C SER A 196 5934 6533 5889 -266 -1074 -1013 C ATOM 1383 O SER A 196 17.816 39.130 66.846 1.00 55.55 O ANISOU 1383 O SER A 196 6761 7477 6870 -239 -1134 -1001 O ATOM 1384 CB SER A 196 16.867 42.187 66.262 1.00 43.11 C ANISOU 1384 CB SER A 196 5182 5756 5443 -425 -933 -1137 C ATOM 1385 OG SER A 196 16.592 43.039 65.164 1.00 44.92 O ANISOU 1385 OG SER A 196 5357 5908 5803 -506 -801 -1140 O ATOM 1386 N GLY A 197 16.163 39.796 68.215 1.00 48.51 N ANISOU 1386 N GLY A 197 6106 6581 5744 -221 -1107 -1013 N ATOM 1387 CA GLY A 197 16.448 38.812 69.242 1.00 50.43 C ANISOU 1387 CA GLY A 197 6429 6879 5850 -132 -1209 -976 C ATOM 1388 C GLY A 197 15.404 37.710 69.203 1.00 51.91 C ANISOU 1388 C GLY A 197 6733 7081 5908 -71 -1160 -858 C ATOM 1389 O GLY A 197 14.350 37.869 68.586 1.00 48.38 O ANISOU 1389 O GLY A 197 6319 6608 5455 -97 -1054 -823 O ATOM 1390 N ASP A 198 15.692 36.586 69.850 1.00 47.06 N ANISOU 1390 N ASP A 198 6181 6503 5195 12 -1231 -797 N ATOM 1391 CA ASP A 198 14.736 35.493 69.911 1.00 48.89 C ANISOU 1391 CA ASP A 198 6534 6736 5304 69 -1173 -679 C ATOM 1392 C ASP A 198 13.682 35.792 70.966 1.00 49.56 C ANISOU 1392 C ASP A 198 6795 6817 5218 83 -1114 -671 C ATOM 1393 O ASP A 198 14.001 36.034 72.131 1.00 49.49 O ANISOU 1393 O ASP A 198 6858 6830 5117 111 -1179 -714 O ATOM 1394 CB ASP A 198 15.450 34.178 70.189 1.00 57.02 C ANISOU 1394 CB ASP A 198 7571 7790 6305 153 -1257 -614 C ATOM 1395 CG ASP A 198 16.483 33.853 69.130 1.00 64.13 C ANISOU 1395 CG ASP A 198 8295 8692 7380 141 -1297 -625 C ATOM 1396 OD1 ASP A 198 16.205 34.109 67.935 1.00 63.89 O ANISOU 1396 OD1 ASP A 198 8175 8640 7461 82 -1218 -620 O ATOM 1397 OD2 ASP A 198 17.573 33.359 69.491 1.00 64.20 O ANISOU 1397 OD2 ASP A 198 8255 8722 7416 193 -1403 -644 O ATOM 1398 N SER A 199 12.422 35.792 70.549 1.00 42.35 N ANISOU 1398 N SER A 199 5949 5876 4266 65 -986 -619 N ATOM 1399 CA SER A 199 11.356 36.255 71.421 1.00 43.14 C ANISOU 1399 CA SER A 199 6196 5962 4233 65 -897 -625 C ATOM 1400 C SER A 199 10.225 35.244 71.548 1.00 42.88 C ANISOU 1400 C SER A 199 6289 5910 4092 102 -780 -505 C ATOM 1401 O SER A 199 9.943 34.497 70.616 1.00 39.24 O ANISOU 1401 O SER A 199 5793 5433 3683 103 -736 -430 O ATOM 1402 CB SER A 199 10.802 37.587 70.915 1.00 40.04 C ANISOU 1402 CB SER A 199 5766 5535 3914 -6 -824 -707 C ATOM 1403 OG SER A 199 9.618 37.941 71.613 1.00 41.26 O ANISOU 1403 OG SER A 199 6058 5667 3952 -4 -708 -702 O ATOM 1404 N ASN A 200 9.578 35.239 72.709 1.00 31.90 N ANISOU 1404 N ASN A 200 5042 4517 2560 126 -719 -491 N ATOM 1405 CA ASN A 200 8.414 34.398 72.930 1.00 39.11 C ANISOU 1405 CA ASN A 200 6073 5399 3389 146 -574 -387 C ATOM 1406 C ASN A 200 7.143 35.244 72.966 1.00 44.65 C ANISOU 1406 C ASN A 200 6818 6067 4078 100 -416 -416 C ATOM 1407 O ASN A 200 6.034 34.719 73.096 1.00 46.36 O ANISOU 1407 O ASN A 200 7108 6251 4254 98 -266 -344 O ATOM 1408 CB ASN A 200 8.566 33.596 74.231 1.00 51.54 C ANISOU 1408 CB ASN A 200 7780 6982 4820 213 -599 -336 C ATOM 1409 CG ASN A 200 9.766 32.650 74.205 1.00 62.11 C ANISOU 1409 CG ASN A 200 9082 8342 6174 271 -746 -299 C ATOM 1410 OD1 ASN A 200 10.655 32.770 73.356 1.00 65.26 O ANISOU 1410 OD1 ASN A 200 9340 8761 6696 258 -846 -336 O ATOM 1411 ND2 ASN A 200 9.796 31.706 75.143 1.00 63.60 N ANISOU 1411 ND2 ASN A 200 9399 8521 6246 337 -753 -229 N ATOM 1412 N ILE A 201 7.308 36.559 72.839 1.00 39.08 N ANISOU 1412 N ILE A 201 6059 5362 3426 58 -443 -526 N ATOM 1413 CA ILE A 201 6.182 37.468 72.989 1.00 40.97 C ANISOU 1413 CA ILE A 201 6342 5565 3660 22 -300 -568 C ATOM 1414 C ILE A 201 5.981 38.390 71.796 1.00 41.49 C ANISOU 1414 C ILE A 201 6254 5596 3915 -42 -256 -603 C ATOM 1415 O ILE A 201 4.925 39.006 71.661 1.00 53.81 O ANISOU 1415 O ILE A 201 7809 7118 5520 -68 -120 -612 O ATOM 1416 CB ILE A 201 6.279 38.287 74.288 1.00 49.03 C ANISOU 1416 CB ILE A 201 7437 6602 4588 33 -321 -655 C ATOM 1417 CG1 ILE A 201 7.680 38.889 74.441 1.00 50.71 C ANISOU 1417 CG1 ILE A 201 7579 6851 4837 26 -504 -753 C ATOM 1418 CG2 ILE A 201 5.946 37.406 75.486 1.00 48.72 C ANISOU 1418 CG2 ILE A 201 7534 6578 4399 87 -280 -586 C ATOM 1419 CD1 ILE A 201 7.815 39.818 75.637 1.00 51.23 C ANISOU 1419 CD1 ILE A 201 7709 6932 4822 25 -530 -856 C ATOM 1420 N GLU A 202 6.972 38.477 70.917 1.00 35.19 N ANISOU 1420 N GLU A 202 5318 4808 3243 -63 -360 -615 N ATOM 1421 CA GLU A 202 6.765 39.220 69.677 1.00 38.05 C ANISOU 1421 CA GLU A 202 5537 5131 3791 -118 -301 -619 C ATOM 1422 C GLU A 202 6.987 38.377 68.414 1.00 30.93 C ANISOU 1422 C GLU A 202 4521 4231 3001 -125 -303 -530 C ATOM 1423 O GLU A 202 7.910 37.560 68.334 1.00 24.78 O ANISOU 1423 O GLU A 202 3718 3486 2211 -101 -404 -506 O ATOM 1424 CB GLU A 202 7.588 40.511 69.644 1.00 50.09 C ANISOU 1424 CB GLU A 202 6999 6639 5393 -159 -375 -736 C ATOM 1425 CG GLU A 202 9.086 40.307 69.636 1.00 67.35 C ANISOU 1425 CG GLU A 202 9120 8865 7606 -159 -539 -784 C ATOM 1426 CD GLU A 202 9.839 41.610 69.834 1.00 83.33 C ANISOU 1426 CD GLU A 202 11095 10868 9701 -207 -603 -921 C ATOM 1427 OE1 GLU A 202 9.185 42.621 70.175 1.00 87.48 O ANISOU 1427 OE1 GLU A 202 11669 11349 10219 -230 -528 -977 O ATOM 1428 OE2 GLU A 202 11.076 41.622 69.649 1.00 86.67 O ANISOU 1428 OE2 GLU A 202 11424 11312 10194 -223 -725 -978 O ATOM 1429 N LEU A 203 6.125 38.592 67.428 1.00 20.88 N ANISOU 1429 N LEU A 203 3179 2921 1834 -150 -193 -486 N ATOM 1430 CA LEU A 203 6.178 37.830 66.191 1.00 20.14 C ANISOU 1430 CA LEU A 203 2989 2826 1835 -155 -183 -407 C ATOM 1431 C LEU A 203 7.089 38.484 65.160 1.00 19.40 C ANISOU 1431 C LEU A 203 2778 2719 1874 -192 -232 -437 C ATOM 1432 O LEU A 203 7.627 37.815 64.289 1.00 16.97 O ANISOU 1432 O LEU A 203 2398 2423 1628 -193 -261 -391 O ATOM 1433 CB LEU A 203 4.775 37.692 65.603 1.00 20.10 C ANISOU 1433 CB LEU A 203 2968 2792 1875 -157 -52 -352 C ATOM 1434 CG LEU A 203 3.804 36.840 66.407 1.00 28.52 C ANISOU 1434 CG LEU A 203 4130 3864 2843 -132 29 -311 C ATOM 1435 CD1 LEU A 203 2.413 36.889 65.772 1.00 31.37 C ANISOU 1435 CD1 LEU A 203 4443 4194 3284 -140 154 -283 C ATOM 1436 CD2 LEU A 203 4.321 35.412 66.487 1.00 33.73 C ANISOU 1436 CD2 LEU A 203 4818 4550 3447 -106 -20 -243 C ATOM 1437 N GLY A 204 7.246 39.798 65.245 1.00 17.50 N ANISOU 1437 N GLY A 204 2525 2444 1680 -225 -228 -514 N ATOM 1438 CA GLY A 204 7.967 40.506 64.205 1.00 15.48 C ANISOU 1438 CA GLY A 204 2168 2154 1558 -269 -238 -535 C ATOM 1439 C GLY A 204 6.992 40.873 63.100 1.00 18.39 C ANISOU 1439 C GLY A 204 2508 2475 2005 -273 -132 -478 C ATOM 1440 O GLY A 204 5.940 40.245 62.956 1.00 17.87 O ANISOU 1440 O GLY A 204 2465 2419 1908 -241 -74 -416 O ATOM 1441 N PRO A 205 7.340 41.882 62.292 1.00 15.50 N ANISOU 1441 N PRO A 205 2093 2054 1744 -310 -108 -500 N ATOM 1442 CA PRO A 205 6.353 42.376 61.328 1.00 17.42 C ANISOU 1442 CA PRO A 205 2329 2244 2044 -297 -19 -449 C ATOM 1443 C PRO A 205 6.082 41.403 60.186 1.00 15.37 C ANISOU 1443 C PRO A 205 2028 2008 1806 -274 -4 -358 C ATOM 1444 O PRO A 205 4.952 41.344 59.706 1.00 16.51 O ANISOU 1444 O PRO A 205 2179 2139 1956 -241 50 -314 O ATOM 1445 CB PRO A 205 6.988 43.675 60.807 1.00 16.90 C ANISOU 1445 CB PRO A 205 2242 2105 2076 -343 1 -493 C ATOM 1446 CG PRO A 205 8.438 43.499 61.017 1.00 14.18 C ANISOU 1446 CG PRO A 205 1847 1785 1757 -387 -73 -545 C ATOM 1447 CD PRO A 205 8.590 42.657 62.258 1.00 17.17 C ANISOU 1447 CD PRO A 205 2257 2240 2028 -362 -154 -575 C ATOM 1448 N THR A 206 7.086 40.646 59.753 1.00 17.38 N ANISOU 1448 N THR A 206 2233 2295 2076 -289 -53 -339 N ATOM 1449 CA THR A 206 6.852 39.663 58.698 1.00 11.36 C ANISOU 1449 CA THR A 206 1436 1554 1327 -267 -39 -262 C ATOM 1450 C THR A 206 5.787 38.646 59.089 1.00 16.32 C ANISOU 1450 C THR A 206 2093 2219 1890 -227 -26 -222 C ATOM 1451 O THR A 206 4.828 38.411 58.355 1.00 14.06 O ANISOU 1451 O THR A 206 1796 1925 1621 -203 17 -179 O ATOM 1452 CB THR A 206 8.124 38.905 58.348 1.00 16.24 C ANISOU 1452 CB THR A 206 1997 2203 1969 -284 -93 -258 C ATOM 1453 OG1 THR A 206 9.174 39.846 58.094 1.00 14.09 O ANISOU 1453 OG1 THR A 206 1687 1895 1772 -333 -95 -309 O ATOM 1454 CG2 THR A 206 7.888 38.014 57.111 1.00 10.60 C ANISOU 1454 CG2 THR A 206 1252 1500 1273 -264 -68 -186 C ATOM 1455 N GLU A 207 5.972 38.017 60.239 1.00 15.14 N ANISOU 1455 N GLU A 207 1981 2106 1664 -219 -63 -240 N ATOM 1456 CA GLU A 207 5.002 37.041 60.717 1.00 13.96 C ANISOU 1456 CA GLU A 207 1872 1980 1454 -190 -31 -202 C ATOM 1457 C GLU A 207 3.637 37.689 61.004 1.00 15.77 C ANISOU 1457 C GLU A 207 2129 2181 1682 -179 50 -216 C ATOM 1458 O GLU A 207 2.594 37.115 60.703 1.00 15.68 O ANISOU 1458 O GLU A 207 2103 2170 1683 -162 104 -183 O ATOM 1459 CB GLU A 207 5.545 36.316 61.948 1.00 15.03 C ANISOU 1459 CB GLU A 207 2068 2149 1492 -177 -83 -212 C ATOM 1460 CG GLU A 207 4.698 35.135 62.409 1.00 15.48 C ANISOU 1460 CG GLU A 207 2177 2218 1485 -153 -36 -161 C ATOM 1461 CD GLU A 207 4.456 34.092 61.315 1.00 24.71 C ANISOU 1461 CD GLU A 207 3288 3388 2712 -148 -19 -101 C ATOM 1462 OE1 GLU A 207 5.105 34.146 60.245 1.00 24.19 O ANISOU 1462 OE1 GLU A 207 3152 3325 2716 -157 -54 -94 O ATOM 1463 OE2 GLU A 207 3.593 33.212 61.526 1.00 24.64 O ANISOU 1463 OE2 GLU A 207 3307 3374 2680 -140 40 -65 O ATOM 1464 N ILE A 208 3.642 38.891 61.571 1.00 15.37 N ANISOU 1464 N ILE A 208 2109 2102 1628 -189 60 -275 N ATOM 1465 CA ILE A 208 2.391 39.614 61.782 1.00 15.84 C ANISOU 1465 CA ILE A 208 2186 2129 1704 -172 139 -297 C ATOM 1466 C ILE A 208 1.576 39.709 60.482 1.00 13.75 C ANISOU 1466 C ILE A 208 1856 1841 1526 -150 173 -257 C ATOM 1467 O ILE A 208 0.396 39.369 60.452 1.00 14.33 O ANISOU 1467 O ILE A 208 1912 1916 1615 -126 227 -247 O ATOM 1468 CB ILE A 208 2.637 41.038 62.338 1.00 14.64 C ANISOU 1468 CB ILE A 208 2069 1935 1558 -186 142 -371 C ATOM 1469 CG1 ILE A 208 2.912 40.973 63.843 1.00 16.91 C ANISOU 1469 CG1 ILE A 208 2440 2247 1737 -192 127 -425 C ATOM 1470 CG2 ILE A 208 1.451 41.952 62.029 1.00 15.73 C ANISOU 1470 CG2 ILE A 208 2198 2022 1758 -160 218 -384 C ATOM 1471 CD1 ILE A 208 3.299 42.304 64.469 1.00 25.17 C ANISOU 1471 CD1 ILE A 208 3523 3255 2783 -211 116 -514 C ATOM 1472 N LEU A 209 2.211 40.186 59.415 1.00 15.88 N ANISOU 1472 N LEU A 209 2093 2087 1854 -157 141 -240 N ATOM 1473 CA LEU A 209 1.553 40.289 58.112 1.00 12.53 C ANISOU 1473 CA LEU A 209 1627 1643 1492 -125 155 -200 C ATOM 1474 C LEU A 209 1.105 38.921 57.593 1.00 13.00 C ANISOU 1474 C LEU A 209 1645 1747 1546 -111 147 -156 C ATOM 1475 O LEU A 209 0.003 38.770 57.064 1.00 10.53 O ANISOU 1475 O LEU A 209 1297 1432 1270 -76 168 -147 O ATOM 1476 CB LEU A 209 2.497 40.942 57.097 1.00 11.34 C ANISOU 1476 CB LEU A 209 1471 1455 1382 -140 132 -181 C ATOM 1477 CG LEU A 209 2.832 42.414 57.358 1.00 11.53 C ANISOU 1477 CG LEU A 209 1532 1411 1437 -157 153 -224 C ATOM 1478 CD1 LEU A 209 3.875 42.898 56.388 1.00 16.18 C ANISOU 1478 CD1 LEU A 209 2118 1960 2069 -185 150 -202 C ATOM 1479 CD2 LEU A 209 1.546 43.224 57.235 1.00 11.87 C ANISOU 1479 CD2 LEU A 209 1590 1409 1512 -103 195 -230 C ATOM 1480 N ALA A 210 1.967 37.922 57.717 1.00 10.18 N ANISOU 1480 N ALA A 210 1287 1427 1154 -135 112 -135 N ATOM 1481 CA ALA A 210 1.626 36.605 57.188 1.00 14.19 C ANISOU 1481 CA ALA A 210 1760 1967 1665 -126 107 -97 C ATOM 1482 C ALA A 210 0.415 36.031 57.927 1.00 13.64 C ANISOU 1482 C ALA A 210 1692 1905 1585 -117 163 -108 C ATOM 1483 O ALA A 210 -0.466 35.414 57.321 1.00 18.70 O ANISOU 1483 O ALA A 210 2285 2553 2268 -103 180 -98 O ATOM 1484 CB ALA A 210 2.806 35.669 57.297 1.00 12.49 C ANISOU 1484 CB ALA A 210 1549 1781 1417 -147 62 -76 C ATOM 1485 N ARG A 211 0.366 36.255 59.239 1.00 11.11 N ANISOU 1485 N ARG A 211 1428 1583 1211 -128 194 -135 N ATOM 1486 CA ARG A 211 -0.777 35.826 60.037 1.00 13.40 C ANISOU 1486 CA ARG A 211 1730 1871 1489 -126 274 -149 C ATOM 1487 C ARG A 211 -2.071 36.529 59.654 1.00 15.57 C ANISOU 1487 C ARG A 211 1949 2123 1843 -101 325 -182 C ATOM 1488 O ARG A 211 -3.144 35.925 59.688 1.00 14.72 O ANISOU 1488 O ARG A 211 1800 2017 1778 -98 384 -190 O ATOM 1489 CB ARG A 211 -0.492 36.024 61.524 1.00 15.40 C ANISOU 1489 CB ARG A 211 2077 2125 1648 -138 301 -173 C ATOM 1490 CG ARG A 211 0.559 35.051 62.046 1.00 22.95 C ANISOU 1490 CG ARG A 211 3092 3107 2521 -147 250 -139 C ATOM 1491 CD ARG A 211 -0.064 33.683 62.304 1.00 22.19 C ANISOU 1491 CD ARG A 211 3014 3010 2407 -151 311 -99 C ATOM 1492 NE ARG A 211 -1.164 33.800 63.253 1.00 27.73 N ANISOU 1492 NE ARG A 211 3762 3694 3082 -155 424 -123 N ATOM 1493 CZ ARG A 211 -1.004 33.867 64.574 1.00 36.13 C ANISOU 1493 CZ ARG A 211 4942 4756 4031 -153 455 -133 C ATOM 1494 NH1 ARG A 211 0.214 33.807 65.103 1.00 29.83 N ANISOU 1494 NH1 ARG A 211 4218 3979 3138 -140 363 -124 N ATOM 1495 NH2 ARG A 211 -2.064 33.990 65.368 1.00 32.46 N ANISOU 1495 NH2 ARG A 211 4518 4270 3547 -159 579 -158 N ATOM 1496 N ARG A 212 -1.979 37.808 59.306 1.00 13.11 N ANISOU 1496 N ARG A 212 1635 1784 1561 -80 303 -204 N ATOM 1497 CA ARG A 212 -3.166 38.531 58.854 1.00 18.11 C ANISOU 1497 CA ARG A 212 2215 2392 2276 -38 333 -234 C ATOM 1498 C ARG A 212 -3.665 37.966 57.524 1.00 13.18 C ANISOU 1498 C ARG A 212 1511 1781 1716 -10 292 -209 C ATOM 1499 O ARG A 212 -4.864 37.827 57.291 1.00 14.13 O ANISOU 1499 O ARG A 212 1562 1902 1906 18 319 -238 O ATOM 1500 CB ARG A 212 -2.876 40.027 58.723 1.00 23.41 C ANISOU 1500 CB ARG A 212 2915 3016 2961 -16 317 -255 C ATOM 1501 CG ARG A 212 -2.703 40.720 60.043 1.00 32.07 C ANISOU 1501 CG ARG A 212 4080 4095 4011 -36 363 -303 C ATOM 1502 CD ARG A 212 -2.857 42.223 59.901 1.00 42.99 C ANISOU 1502 CD ARG A 212 5479 5416 5440 -6 370 -338 C ATOM 1503 NE ARG A 212 -2.851 42.879 61.207 1.00 46.19 N ANISOU 1503 NE ARG A 212 5947 5801 5802 -22 421 -401 N ATOM 1504 CZ ARG A 212 -2.049 43.885 61.545 1.00 45.77 C ANISOU 1504 CZ ARG A 212 5950 5708 5731 -41 403 -435 C ATOM 1505 NH1 ARG A 212 -1.179 44.376 60.673 1.00 44.29 N ANISOU 1505 NH1 ARG A 212 5762 5490 5576 -52 347 -407 N ATOM 1506 NH2 ARG A 212 -2.117 44.402 62.761 1.00 49.91 N ANISOU 1506 NH2 ARG A 212 6537 6219 6209 -53 448 -502 N ATOM 1507 N VAL A 213 -2.730 37.628 56.651 1.00 11.24 N ANISOU 1507 N VAL A 213 1274 1549 1450 -18 226 -166 N ATOM 1508 CA VAL A 213 -3.094 37.060 55.372 1.00 13.82 C ANISOU 1508 CA VAL A 213 1543 1892 1817 10 180 -147 C ATOM 1509 C VAL A 213 -3.767 35.720 55.612 1.00 15.09 C ANISOU 1509 C VAL A 213 1653 2081 2001 -13 212 -158 C ATOM 1510 O VAL A 213 -4.811 35.438 55.030 1.00 18.55 O ANISOU 1510 O VAL A 213 2015 2526 2508 15 206 -186 O ATOM 1511 CB VAL A 213 -1.866 36.904 54.474 1.00 16.45 C ANISOU 1511 CB VAL A 213 1907 2231 2114 -1 123 -100 C ATOM 1512 CG1 VAL A 213 -2.189 36.055 53.260 1.00 11.62 C ANISOU 1512 CG1 VAL A 213 1248 1643 1524 22 79 -86 C ATOM 1513 CG2 VAL A 213 -1.357 38.272 54.057 1.00 12.97 C ANISOU 1513 CG2 VAL A 213 1511 1746 1670 20 108 -90 C ATOM 1514 N ALA A 214 -3.178 34.895 56.482 1.00 10.39 N ANISOU 1514 N ALA A 214 1100 1497 1351 -60 244 -140 N ATOM 1515 CA ALA A 214 -3.751 33.590 56.788 1.00 15.42 C ANISOU 1515 CA ALA A 214 1708 2144 2008 -88 292 -143 C ATOM 1516 C ALA A 214 -5.174 33.729 57.341 1.00 15.52 C ANISOU 1516 C ALA A 214 1668 2142 2087 -85 377 -196 C ATOM 1517 O ALA A 214 -6.082 32.971 56.984 1.00 14.14 O ANISOU 1517 O ALA A 214 1413 1969 1990 -92 402 -224 O ATOM 1518 CB ALA A 214 -2.869 32.838 57.772 1.00 15.08 C ANISOU 1518 CB ALA A 214 1745 2103 1880 -125 314 -108 C ATOM 1519 N GLN A 215 -5.366 34.708 58.214 1.00 13.49 N ANISOU 1519 N GLN A 215 1449 1868 1810 -77 424 -221 N ATOM 1520 CA GLN A 215 -6.686 34.953 58.777 1.00 14.61 C ANISOU 1520 CA GLN A 215 1537 1994 2021 -71 518 -279 C ATOM 1521 C GLN A 215 -7.692 35.337 57.683 1.00 21.37 C ANISOU 1521 C GLN A 215 2273 2851 2996 -19 474 -322 C ATOM 1522 O GLN A 215 -8.836 34.868 57.680 1.00 19.40 O ANISOU 1522 O GLN A 215 1926 2600 2843 -23 528 -374 O ATOM 1523 CB GLN A 215 -6.619 36.036 59.856 1.00 20.18 C ANISOU 1523 CB GLN A 215 2314 2678 2676 -64 572 -303 C ATOM 1524 CG GLN A 215 -7.938 36.243 60.585 1.00 35.18 C ANISOU 1524 CG GLN A 215 4166 4558 4643 -62 693 -367 C ATOM 1525 CD GLN A 215 -7.877 37.358 61.612 1.00 57.78 C ANISOU 1525 CD GLN A 215 7105 7396 7451 -51 748 -400 C ATOM 1526 OE1 GLN A 215 -6.833 37.983 61.815 1.00 65.05 O ANISOU 1526 OE1 GLN A 215 8115 8316 8287 -49 689 -379 O ATOM 1527 NE2 GLN A 215 -9.005 37.616 62.266 1.00 64.74 N ANISOU 1527 NE2 GLN A 215 7947 8258 8392 -45 866 -462 N ATOM 1528 N GLU A 216 -7.270 36.187 56.751 1.00 17.09 N ANISOU 1528 N GLU A 216 1737 2307 2448 32 375 -305 N ATOM 1529 CA GLU A 216 -8.151 36.606 55.670 1.00 18.21 C ANISOU 1529 CA GLU A 216 1787 2451 2682 99 311 -340 C ATOM 1530 C GLU A 216 -8.515 35.456 54.724 1.00 13.73 C ANISOU 1530 C GLU A 216 1139 1914 2163 95 259 -350 C ATOM 1531 O GLU A 216 -9.611 35.428 54.179 1.00 23.44 O ANISOU 1531 O GLU A 216 2260 3151 3493 136 232 -408 O ATOM 1532 CB GLU A 216 -7.558 37.794 54.908 1.00 16.66 C ANISOU 1532 CB GLU A 216 1646 2233 2450 158 228 -307 C ATOM 1533 CG GLU A 216 -7.528 39.063 55.755 1.00 22.73 C ANISOU 1533 CG GLU A 216 2469 2959 3208 173 278 -323 C ATOM 1534 CD GLU A 216 -6.763 40.212 55.113 1.00 32.26 C ANISOU 1534 CD GLU A 216 3752 4127 4377 213 217 -283 C ATOM 1535 OE1 GLU A 216 -6.206 40.036 54.008 1.00 27.23 O ANISOU 1535 OE1 GLU A 216 3135 3498 3712 229 143 -236 O ATOM 1536 OE2 GLU A 216 -6.719 41.298 55.726 1.00 35.26 O ANISOU 1536 OE2 GLU A 216 4178 4463 4758 225 255 -301 O ATOM 1537 N LEU A 217 -7.612 34.501 54.556 1.00 16.00 N ANISOU 1537 N LEU A 217 1474 2218 2387 47 244 -302 N ATOM 1538 CA LEU A 217 -7.847 33.409 53.623 1.00 14.57 C ANISOU 1538 CA LEU A 217 1229 2060 2246 41 193 -315 C ATOM 1539 C LEU A 217 -8.471 32.180 54.279 1.00 20.23 C ANISOU 1539 C LEU A 217 1891 2773 3024 -25 285 -349 C ATOM 1540 O LEU A 217 -8.785 31.204 53.600 1.00 22.49 O ANISOU 1540 O LEU A 217 2113 3070 3362 -40 256 -375 O ATOM 1541 CB LEU A 217 -6.539 33.023 52.925 1.00 13.83 C ANISOU 1541 CB LEU A 217 1212 1980 2062 31 127 -250 C ATOM 1542 CG LEU A 217 -5.941 34.197 52.141 1.00 24.50 C ANISOU 1542 CG LEU A 217 2621 3326 3363 90 53 -216 C ATOM 1543 CD1 LEU A 217 -4.559 33.862 51.600 1.00 16.05 C ANISOU 1543 CD1 LEU A 217 1626 2263 2210 69 17 -156 C ATOM 1544 CD2 LEU A 217 -6.875 34.620 51.014 1.00 24.68 C ANISOU 1544 CD2 LEU A 217 2582 3356 3439 169 -30 -254 C ATOM 1545 N GLY A 218 -8.648 32.226 55.594 1.00 15.66 N ANISOU 1545 N GLY A 218 1344 2170 2434 -65 402 -351 N ATOM 1546 CA GLY A 218 -9.203 31.092 56.317 1.00 20.11 C ANISOU 1546 CA GLY A 218 1880 2714 3045 -132 517 -372 C ATOM 1547 C GLY A 218 -8.250 29.916 56.467 1.00 24.16 C ANISOU 1547 C GLY A 218 2477 3220 3484 -182 525 -308 C ATOM 1548 O GLY A 218 -8.680 28.765 56.558 1.00 18.92 O ANISOU 1548 O GLY A 218 1778 2534 2877 -231 589 -324 O ATOM 1549 N TRP A 219 -6.949 30.189 56.489 1.00 12.08 N ANISOU 1549 N TRP A 219 1052 1702 1838 -168 464 -241 N ATOM 1550 CA TRP A 219 -5.979 29.132 56.744 1.00 18.24 C ANISOU 1550 CA TRP A 219 1913 2472 2547 -202 468 -181 C ATOM 1551 C TRP A 219 -5.854 28.969 58.249 1.00 23.87 C ANISOU 1551 C TRP A 219 2725 3157 3188 -233 575 -152 C ATOM 1552 O TRP A 219 -5.462 29.900 58.931 1.00 22.32 O ANISOU 1552 O TRP A 219 2595 2968 2919 -215 574 -142 O ATOM 1553 CB TRP A 219 -4.611 29.501 56.174 1.00 13.22 C ANISOU 1553 CB TRP A 219 1334 1861 1829 -173 360 -132 C ATOM 1554 CG TRP A 219 -4.580 29.632 54.674 1.00 15.28 C ANISOU 1554 CG TRP A 219 1531 2145 2129 -139 262 -148 C ATOM 1555 CD1 TRP A 219 -5.472 29.109 53.783 1.00 18.05 C ANISOU 1555 CD1 TRP A 219 1788 2502 2568 -134 241 -198 C ATOM 1556 CD2 TRP A 219 -3.596 30.326 53.897 1.00 12.52 C ANISOU 1556 CD2 TRP A 219 1215 1814 1726 -104 176 -119 C ATOM 1557 NE1 TRP A 219 -5.105 29.438 52.500 1.00 16.34 N ANISOU 1557 NE1 TRP A 219 1560 2310 2337 -90 139 -197 N ATOM 1558 CE2 TRP A 219 -3.960 30.191 52.545 1.00 17.91 C ANISOU 1558 CE2 TRP A 219 1840 2514 2452 -74 109 -144 C ATOM 1559 CE3 TRP A 219 -2.460 31.070 54.217 1.00 14.89 C ANISOU 1559 CE3 TRP A 219 1588 2116 1953 -99 154 -80 C ATOM 1560 CZ2 TRP A 219 -3.214 30.758 51.509 1.00 17.44 C ANISOU 1560 CZ2 TRP A 219 1811 2468 2348 -37 36 -119 C ATOM 1561 CZ3 TRP A 219 -1.722 31.634 53.190 1.00 14.89 C ANISOU 1561 CZ3 TRP A 219 1600 2126 1932 -72 87 -62 C ATOM 1562 CH2 TRP A 219 -2.104 31.476 51.854 1.00 16.80 C ANISOU 1562 CH2 TRP A 219 1799 2379 2203 -41 36 -76 C ATOM 1563 N SER A 220 -6.169 27.792 58.773 1.00 24.57 N ANISOU 1563 N SER A 220 2837 3209 3291 -279 668 -139 N ATOM 1564 CA SER A 220 -6.119 27.598 60.223 1.00 24.92 C ANISOU 1564 CA SER A 220 2999 3220 3249 -302 780 -105 C ATOM 1565 C SER A 220 -4.706 27.325 60.712 1.00 20.39 C ANISOU 1565 C SER A 220 2560 2651 2537 -283 718 -30 C ATOM 1566 O SER A 220 -4.159 26.249 60.492 1.00 26.34 O ANISOU 1566 O SER A 220 3345 3386 3278 -290 697 13 O ATOM 1567 CB SER A 220 -7.047 26.463 60.662 1.00 33.49 C ANISOU 1567 CB SER A 220 4074 4249 4403 -359 926 -115 C ATOM 1568 OG SER A 220 -8.394 26.897 60.717 1.00 49.92 O ANISOU 1568 OG SER A 220 6046 6321 6600 -379 1018 -194 O ATOM 1569 N VAL A 221 -4.114 28.298 61.386 1.00 17.75 N ANISOU 1569 N VAL A 221 2299 2339 2105 -255 684 -22 N ATOM 1570 CA VAL A 221 -2.777 28.113 61.928 1.00 21.84 C ANISOU 1570 CA VAL A 221 2934 2867 2498 -231 612 33 C ATOM 1571 C VAL A 221 -2.809 28.351 63.438 1.00 26.02 C ANISOU 1571 C VAL A 221 3599 3381 2906 -228 687 45 C ATOM 1572 O VAL A 221 -3.682 29.057 63.935 1.00 25.49 O ANISOU 1572 O VAL A 221 3526 3307 2851 -239 775 1 O ATOM 1573 CB VAL A 221 -1.749 29.028 61.237 1.00 28.89 C ANISOU 1573 CB VAL A 221 3791 3805 3380 -200 474 23 C ATOM 1574 CG1 VAL A 221 -1.707 28.747 59.720 1.00 17.92 C ANISOU 1574 CG1 VAL A 221 2291 2429 2090 -198 410 16 C ATOM 1575 CG2 VAL A 221 -2.055 30.494 61.519 1.00 27.54 C ANISOU 1575 CG2 VAL A 221 3610 3649 3205 -189 478 -26 C ATOM 1576 N PRO A 222 -1.872 27.741 64.179 1.00 22.33 N ANISOU 1576 N PRO A 222 3261 2907 2318 -206 652 101 N ATOM 1577 CA PRO A 222 -1.893 27.909 65.630 1.00 27.29 C ANISOU 1577 CA PRO A 222 4043 3521 2806 -194 717 114 C ATOM 1578 C PRO A 222 -1.648 29.367 66.001 1.00 26.20 C ANISOU 1578 C PRO A 222 3909 3422 2622 -175 665 57 C ATOM 1579 O PRO A 222 -0.958 30.083 65.268 1.00 22.79 O ANISOU 1579 O PRO A 222 3399 3028 2233 -162 546 30 O ATOM 1580 CB PRO A 222 -0.739 27.020 66.111 1.00 23.01 C ANISOU 1580 CB PRO A 222 3623 2972 2148 -154 636 183 C ATOM 1581 CG PRO A 222 -0.525 26.042 65.026 1.00 24.51 C ANISOU 1581 CG PRO A 222 3726 3146 2439 -162 599 213 C ATOM 1582 CD PRO A 222 -0.846 26.777 63.749 1.00 25.26 C ANISOU 1582 CD PRO A 222 3649 3277 2674 -185 559 154 C ATOM 1583 N ASP A 223 -2.218 29.790 67.124 1.00 24.62 N ANISOU 1583 N ASP A 223 3808 3208 2339 -178 767 35 N ATOM 1584 CA ASP A 223 -2.150 31.181 67.555 1.00 25.12 C ANISOU 1584 CA ASP A 223 3882 3298 2365 -165 742 -31 C ATOM 1585 C ASP A 223 -0.920 31.391 68.411 1.00 22.31 C ANISOU 1585 C ASP A 223 3657 2969 1851 -125 628 -24 C ATOM 1586 O ASP A 223 -1.023 31.467 69.628 1.00 33.57 O ANISOU 1586 O ASP A 223 5232 4387 3137 -109 684 -29 O ATOM 1587 CB ASP A 223 -3.401 31.545 68.359 1.00 33.97 C ANISOU 1587 CB ASP A 223 5043 4389 3476 -185 917 -70 C ATOM 1588 CG ASP A 223 -3.375 32.978 68.874 1.00 45.02 C ANISOU 1588 CG ASP A 223 6465 5807 4835 -169 901 -145 C ATOM 1589 OD1 ASP A 223 -2.608 33.802 68.322 1.00 47.36 O ANISOU 1589 OD1 ASP A 223 6702 6132 5162 -154 766 -175 O ATOM 1590 OD2 ASP A 223 -4.127 33.283 69.830 1.00 50.36 O ANISOU 1590 OD2 ASP A 223 7222 6461 5453 -175 1036 -178 O ATOM 1591 N PHE A 224 0.242 31.486 67.775 1.00 20.97 N ANISOU 1591 N PHE A 224 3433 2833 1704 -106 470 -21 N ATOM 1592 CA PHE A 224 1.497 31.691 68.501 1.00 22.91 C ANISOU 1592 CA PHE A 224 3773 3110 1823 -66 337 -31 C ATOM 1593 C PHE A 224 1.737 33.170 68.834 1.00 21.72 C ANISOU 1593 C PHE A 224 3614 2981 1657 -69 291 -121 C ATOM 1594 O PHE A 224 1.320 34.061 68.092 1.00 24.02 O ANISOU 1594 O PHE A 224 3794 3267 2068 -96 314 -164 O ATOM 1595 CB PHE A 224 2.678 31.148 67.693 1.00 20.90 C ANISOU 1595 CB PHE A 224 3446 2878 1618 -48 195 -2 C ATOM 1596 CG PHE A 224 2.629 29.665 67.477 1.00 22.15 C ANISOU 1596 CG PHE A 224 3629 3009 1776 -36 223 82 C ATOM 1597 CD1 PHE A 224 2.651 28.798 68.557 1.00 26.16 C ANISOU 1597 CD1 PHE A 224 4304 3493 2142 0 253 136 C ATOM 1598 CD2 PHE A 224 2.570 29.138 66.198 1.00 23.26 C ANISOU 1598 CD2 PHE A 224 3643 3142 2054 -58 220 105 C ATOM 1599 CE1 PHE A 224 2.602 27.431 68.375 1.00 28.66 C ANISOU 1599 CE1 PHE A 224 4656 3769 2465 11 288 216 C ATOM 1600 CE2 PHE A 224 2.527 27.753 66.003 1.00 22.37 C ANISOU 1600 CE2 PHE A 224 3555 2995 1949 -49 249 174 C ATOM 1601 CZ PHE A 224 2.536 26.906 67.100 1.00 26.42 C ANISOU 1601 CZ PHE A 224 4232 3474 2331 -16 286 231 C ATOM 1602 N LYS A 225 2.424 33.420 69.945 1.00 20.92 N ANISOU 1602 N LYS A 225 3640 2901 1408 -35 220 -150 N ATOM 1603 CA LYS A 225 2.694 34.785 70.396 1.00 27.46 C ANISOU 1603 CA LYS A 225 4478 3744 2212 -40 175 -247 C ATOM 1604 C LYS A 225 4.075 35.303 69.973 1.00 30.62 C ANISOU 1604 C LYS A 225 4798 4176 2659 -37 0 -295 C ATOM 1605 O LYS A 225 4.233 36.493 69.695 1.00 34.47 O ANISOU 1605 O LYS A 225 5217 4660 3221 -64 -23 -371 O ATOM 1606 CB LYS A 225 2.555 34.873 71.920 1.00 41.27 C ANISOU 1606 CB LYS A 225 6419 5496 3765 -8 206 -274 C ATOM 1607 CG LYS A 225 1.357 35.676 72.397 1.00 49.48 C ANISOU 1607 CG LYS A 225 7494 6506 4798 -31 365 -325 C ATOM 1608 CD LYS A 225 0.063 35.158 71.789 1.00 53.43 C ANISOU 1608 CD LYS A 225 7922 6968 5410 -63 534 -272 C ATOM 1609 CE LYS A 225 -1.143 35.901 72.349 1.00 60.83 C ANISOU 1609 CE LYS A 225 8872 7876 6365 -77 689 -325 C ATOM 1610 NZ LYS A 225 -2.410 35.503 71.675 1.00 62.79 N ANISOU 1610 NZ LYS A 225 9020 8089 6750 -109 843 -298 N ATOM 1611 N GLY A 226 5.071 34.418 69.943 1.00 27.02 N ANISOU 1611 N GLY A 226 4351 3747 2169 -3 -116 -256 N ATOM 1612 CA GLY A 226 6.436 34.802 69.600 1.00 28.66 C ANISOU 1612 CA GLY A 226 4473 3987 2431 1 -279 -309 C ATOM 1613 C GLY A 226 7.028 33.995 68.453 1.00 26.51 C ANISOU 1613 C GLY A 226 4080 3719 2273 0 -327 -252 C ATOM 1614 O GLY A 226 6.714 32.811 68.301 1.00 25.99 O ANISOU 1614 O GLY A 226 4046 3642 2188 22 -286 -166 O ATOM 1615 N TYR A 227 7.887 34.627 67.651 1.00 27.37 N ANISOU 1615 N TYR A 227 4056 3838 2506 -29 -403 -303 N ATOM 1616 CA TYR A 227 8.488 33.971 66.484 1.00 23.21 C ANISOU 1616 CA TYR A 227 3410 3315 2095 -34 -436 -260 C ATOM 1617 C TYR A 227 9.317 32.771 66.905 1.00 25.17 C ANISOU 1617 C TYR A 227 3700 3588 2275 29 -540 -223 C ATOM 1618 O TYR A 227 9.398 31.789 66.180 1.00 28.54 O ANISOU 1618 O TYR A 227 4082 4006 2754 41 -527 -157 O ATOM 1619 CB TYR A 227 9.390 34.940 65.712 1.00 23.60 C ANISOU 1619 CB TYR A 227 3326 3366 2275 -78 -491 -332 C ATOM 1620 CG TYR A 227 9.716 34.563 64.256 1.00 23.46 C ANISOU 1620 CG TYR A 227 3181 3338 2393 -101 -470 -291 C ATOM 1621 CD1 TYR A 227 8.706 34.370 63.312 1.00 31.06 C ANISOU 1621 CD1 TYR A 227 4121 4273 3408 -120 -357 -229 C ATOM 1622 CD2 TYR A 227 11.033 34.459 63.819 1.00 25.35 C ANISOU 1622 CD2 TYR A 227 3322 3596 2712 -103 -563 -326 C ATOM 1623 CE1 TYR A 227 9.004 34.056 61.968 1.00 31.18 C ANISOU 1623 CE1 TYR A 227 4037 4280 3530 -137 -340 -197 C ATOM 1624 CE2 TYR A 227 11.346 34.145 62.480 1.00 30.74 C ANISOU 1624 CE2 TYR A 227 3900 4268 3512 -124 -528 -294 C ATOM 1625 CZ TYR A 227 10.331 33.943 61.546 1.00 31.89 C ANISOU 1625 CZ TYR A 227 4043 4387 3688 -140 -418 -227 C ATOM 1626 OH TYR A 227 10.642 33.662 60.191 1.00 30.01 O ANISOU 1626 OH TYR A 227 3716 4137 3548 -157 -385 -199 O ATOM 1627 N ALA A 228 9.937 32.867 68.078 1.00 26.17 N ANISOU 1627 N ALA A 228 3915 3744 2284 75 -649 -270 N ATOM 1628 CA ALA A 228 10.867 31.844 68.551 1.00 27.18 C ANISOU 1628 CA ALA A 228 4085 3898 2345 153 -779 -245 C ATOM 1629 C ALA A 228 10.310 31.055 69.741 1.00 31.06 C ANISOU 1629 C ALA A 228 4768 4376 2656 214 -749 -178 C ATOM 1630 O ALA A 228 11.058 30.409 70.480 1.00 29.70 O ANISOU 1630 O ALA A 228 4632 4216 2436 275 -836 -159 O ATOM 1631 CB ALA A 228 12.202 32.482 68.909 1.00 31.29 C ANISOU 1631 CB ALA A 228 4529 4459 2900 164 -940 -351 C ATOM 1632 N GLU A 229 8.994 31.119 69.925 1.00 28.85 N ANISOU 1632 N GLU A 229 4585 4064 2315 186 -595 -138 N ATOM 1633 CA GLU A 229 8.322 30.381 70.995 1.00 24.97 C ANISOU 1633 CA GLU A 229 4252 3543 1690 222 -512 -67 C ATOM 1634 C GLU A 229 8.615 28.886 70.796 1.00 24.91 C ANISOU 1634 C GLU A 229 4265 3510 1689 272 -527 33 C ATOM 1635 O GLU A 229 8.545 28.391 69.677 1.00 26.82 O ANISOU 1635 O GLU A 229 4432 3737 2022 255 -505 70 O ATOM 1636 CB GLU A 229 6.820 30.662 70.907 1.00 28.93 C ANISOU 1636 CB GLU A 229 4808 4006 2176 168 -320 -45 C ATOM 1637 CG GLU A 229 5.983 30.258 72.093 1.00 43.11 C ANISOU 1637 CG GLU A 229 6748 5770 3861 184 -202 0 C ATOM 1638 CD GLU A 229 4.515 30.604 71.881 1.00 45.13 C ANISOU 1638 CD GLU A 229 7013 5989 4147 123 -5 4 C ATOM 1639 OE1 GLU A 229 4.217 31.374 70.937 1.00 34.15 O ANISOU 1639 OE1 GLU A 229 5512 4603 2862 72 23 -43 O ATOM 1640 OE2 GLU A 229 3.662 30.103 72.649 1.00 52.69 O ANISOU 1640 OE2 GLU A 229 8065 6907 5050 124 124 50 O ATOM 1641 N PRO A 230 8.973 28.171 71.872 1.00 23.62 N ANISOU 1641 N PRO A 230 4209 3337 1429 336 -567 72 N ATOM 1642 CA PRO A 230 9.277 26.737 71.738 1.00 25.28 C ANISOU 1642 CA PRO A 230 4451 3510 1645 390 -581 164 C ATOM 1643 C PRO A 230 8.157 25.929 71.056 1.00 24.83 C ANISOU 1643 C PRO A 230 4419 3389 1625 351 -414 249 C ATOM 1644 O PRO A 230 8.441 25.039 70.258 1.00 23.25 O ANISOU 1644 O PRO A 230 4170 3165 1498 366 -430 298 O ATOM 1645 CB PRO A 230 9.475 26.279 73.190 1.00 27.86 C ANISOU 1645 CB PRO A 230 4932 3822 1831 458 -610 192 C ATOM 1646 CG PRO A 230 9.905 27.531 73.918 1.00 34.21 C ANISOU 1646 CG PRO A 230 5729 4685 2585 454 -697 89 C ATOM 1647 CD PRO A 230 9.152 28.658 73.252 1.00 28.58 C ANISOU 1647 CD PRO A 230 4939 3985 1934 367 -609 31 C ATOM 1648 N GLU A 231 6.901 26.234 71.363 1.00 25.05 N ANISOU 1648 N GLU A 231 4513 3388 1618 298 -251 259 N ATOM 1649 CA GLU A 231 5.791 25.517 70.738 1.00 29.05 C ANISOU 1649 CA GLU A 231 5022 3833 2184 249 -81 324 C ATOM 1650 C GLU A 231 5.750 25.811 69.241 1.00 26.84 C ANISOU 1650 C GLU A 231 4598 3570 2032 201 -84 302 C ATOM 1651 O GLU A 231 5.422 24.943 68.430 1.00 18.62 O ANISOU 1651 O GLU A 231 3495 2487 1092 177 -19 350 O ATOM 1652 CB GLU A 231 4.451 25.879 71.393 1.00 39.18 C ANISOU 1652 CB GLU A 231 6375 5083 3429 198 98 320 C ATOM 1653 CG GLU A 231 4.313 25.449 72.851 1.00 57.86 C ANISOU 1653 CG GLU A 231 8901 7416 5667 241 133 354 C ATOM 1654 CD GLU A 231 5.196 26.253 73.805 1.00 72.63 C ANISOU 1654 CD GLU A 231 10822 9347 7429 294 -11 294 C ATOM 1655 OE1 GLU A 231 5.573 27.400 73.464 1.00 72.15 O ANISOU 1655 OE1 GLU A 231 10670 9345 7398 275 -91 209 O ATOM 1656 OE2 GLU A 231 5.512 25.733 74.901 1.00 78.91 O ANISOU 1656 OE2 GLU A 231 11748 10123 8110 355 -44 328 O ATOM 1657 N ARG A 232 6.086 27.041 68.870 1.00 17.87 N ANISOU 1657 N ARG A 232 3342 2489 959 172 -152 213 N ATOM 1658 CA ARG A 232 6.109 27.387 67.457 1.00 19.56 C ANISOU 1658 CA ARG A 232 3359 2716 1355 117 -153 181 C ATOM 1659 C ARG A 232 7.242 26.630 66.763 1.00 19.56 C ANISOU 1659 C ARG A 232 3283 2726 1423 156 -270 201 C ATOM 1660 O ARG A 232 7.055 26.049 65.679 1.00 17.87 O ANISOU 1660 O ARG A 232 2973 2490 1325 130 -228 227 O ATOM 1661 CB ARG A 232 6.221 28.912 67.253 1.00 15.91 C ANISOU 1661 CB ARG A 232 2807 2296 942 79 -186 88 C ATOM 1662 CG ARG A 232 6.250 29.334 65.774 1.00 14.54 C ANISOU 1662 CG ARG A 232 2453 2130 942 29 -180 62 C ATOM 1663 CD ARG A 232 6.174 30.856 65.580 1.00 19.67 C ANISOU 1663 CD ARG A 232 3035 2798 1640 -12 -182 -18 C ATOM 1664 NE ARG A 232 5.969 31.137 64.164 1.00 20.83 N ANISOU 1664 NE ARG A 232 3045 2939 1932 -52 -150 -21 N ATOM 1665 CZ ARG A 232 6.944 31.177 63.265 1.00 22.66 C ANISOU 1665 CZ ARG A 232 3176 3186 2248 -56 -225 -34 C ATOM 1666 NH1 ARG A 232 8.201 31.000 63.644 1.00 26.39 N ANISOU 1666 NH1 ARG A 232 3647 3684 2696 -24 -342 -56 N ATOM 1667 NH2 ARG A 232 6.663 31.405 61.987 1.00 24.70 N ANISOU 1667 NH2 ARG A 232 3336 3434 2615 -87 -184 -30 N ATOM 1668 N GLU A 233 8.409 26.606 67.406 1.00 18.17 N ANISOU 1668 N GLU A 233 3150 2582 1171 224 -421 182 N ATOM 1669 CA GLU A 233 9.574 25.936 66.836 1.00 27.22 C ANISOU 1669 CA GLU A 233 4215 3740 2388 271 -542 188 C ATOM 1670 C GLU A 233 9.303 24.447 66.630 1.00 24.98 C ANISOU 1670 C GLU A 233 3991 3395 2105 303 -485 284 C ATOM 1671 O GLU A 233 9.639 23.877 65.589 1.00 21.95 O ANISOU 1671 O GLU A 233 3497 3000 1842 297 -491 294 O ATOM 1672 CB GLU A 233 10.799 26.122 67.735 1.00 39.83 C ANISOU 1672 CB GLU A 233 5856 5382 3898 352 -723 144 C ATOM 1673 CG GLU A 233 11.095 27.577 68.112 1.00 58.21 C ANISOU 1673 CG GLU A 233 8140 7761 6217 319 -783 38 C ATOM 1674 CD GLU A 233 12.051 28.267 67.149 1.00 70.37 C ANISOU 1674 CD GLU A 233 9481 9338 7920 282 -861 -45 C ATOM 1675 OE1 GLU A 233 12.093 27.881 65.958 1.00 72.72 O ANISOU 1675 OE1 GLU A 233 9661 9618 8349 251 -810 -20 O ATOM 1676 OE2 GLU A 233 12.766 29.195 67.592 1.00 73.57 O ANISOU 1676 OE2 GLU A 233 9843 9782 8329 277 -958 -138 O ATOM 1677 N ALA A 234 8.687 23.832 67.633 1.00 21.82 N ANISOU 1677 N ALA A 234 3774 2950 1569 335 -419 351 N ATOM 1678 CA ALA A 234 8.299 22.431 67.568 1.00 19.32 C ANISOU 1678 CA ALA A 234 3540 2555 1247 358 -338 446 C ATOM 1679 C ALA A 234 7.260 22.191 66.470 1.00 17.27 C ANISOU 1679 C ALA A 234 3176 2257 1128 266 -185 453 C ATOM 1680 O ALA A 234 7.378 21.259 65.692 1.00 18.59 O ANISOU 1680 O ALA A 234 3291 2386 1385 268 -171 485 O ATOM 1681 CB ALA A 234 7.777 21.964 68.927 1.00 20.01 C ANISOU 1681 CB ALA A 234 3802 2594 1206 382 -262 498 C ATOM 1682 N HIS A 235 6.250 23.044 66.417 1.00 17.70 N ANISOU 1682 N HIS A 235 3200 2325 1203 192 -79 416 N ATOM 1683 CA HIS A 235 5.241 22.964 65.371 1.00 17.62 C ANISOU 1683 CA HIS A 235 3076 2291 1329 111 43 404 C ATOM 1684 C HIS A 235 5.860 22.984 63.966 1.00 18.29 C ANISOU 1684 C HIS A 235 2989 2405 1556 98 -30 368 C ATOM 1685 O HIS A 235 5.542 22.139 63.133 1.00 17.83 O ANISOU 1685 O HIS A 235 2879 2308 1588 77 22 389 O ATOM 1686 CB HIS A 235 4.238 24.116 65.516 1.00 17.43 C ANISOU 1686 CB HIS A 235 3023 2289 1312 50 132 352 C ATOM 1687 CG HIS A 235 3.319 24.265 64.343 1.00 18.56 C ANISOU 1687 CG HIS A 235 3022 2426 1603 -19 216 320 C ATOM 1688 ND1 HIS A 235 2.148 23.550 64.222 1.00 21.73 N ANISOU 1688 ND1 HIS A 235 3430 2769 2056 -65 359 342 N ATOM 1689 CD2 HIS A 235 3.407 25.040 63.236 1.00 20.49 C ANISOU 1689 CD2 HIS A 235 3118 2713 1953 -47 171 264 C ATOM 1690 CE1 HIS A 235 1.547 23.884 63.091 1.00 25.95 C ANISOU 1690 CE1 HIS A 235 3818 3319 2723 -111 382 294 C ATOM 1691 NE2 HIS A 235 2.292 24.780 62.473 1.00 23.21 N ANISOU 1691 NE2 HIS A 235 3386 3031 2401 -97 271 253 N ATOM 1692 N LEU A 236 6.722 23.966 63.699 1.00 14.61 N ANISOU 1692 N LEU A 236 2437 2003 1109 107 -140 310 N ATOM 1693 CA LEU A 236 7.361 24.102 62.392 1.00 17.06 C ANISOU 1693 CA LEU A 236 2597 2342 1545 93 -195 274 C ATOM 1694 C LEU A 236 8.215 22.897 62.021 1.00 13.43 C ANISOU 1694 C LEU A 236 2127 1858 1119 144 -253 308 C ATOM 1695 O LEU A 236 8.189 22.405 60.881 1.00 16.91 O ANISOU 1695 O LEU A 236 2480 2284 1661 123 -226 305 O ATOM 1696 CB LEU A 236 8.234 25.360 62.349 1.00 23.47 C ANISOU 1696 CB LEU A 236 3335 3213 2368 92 -291 205 C ATOM 1697 CG LEU A 236 7.465 26.669 62.495 1.00 33.03 C ANISOU 1697 CG LEU A 236 4536 4443 3572 40 -236 160 C ATOM 1698 CD1 LEU A 236 8.430 27.852 62.526 1.00 32.48 C ANISOU 1698 CD1 LEU A 236 4404 4419 3519 37 -330 90 C ATOM 1699 CD2 LEU A 236 6.436 26.814 61.381 1.00 33.82 C ANISOU 1699 CD2 LEU A 236 4556 4527 3766 -15 -137 158 C ATOM 1700 N ARG A 237 8.981 22.424 62.989 1.00 16.46 N ANISOU 1700 N ARG A 237 2606 2235 1413 220 -338 337 N ATOM 1701 CA ARG A 237 9.861 21.306 62.743 1.00 24.59 C ANISOU 1701 CA ARG A 237 3631 3238 2475 285 -405 369 C ATOM 1702 C ARG A 237 9.028 20.082 62.363 1.00 20.71 C ANISOU 1702 C ARG A 237 3186 2667 2017 268 -289 430 C ATOM 1703 O ARG A 237 9.372 19.323 61.444 1.00 16.08 O ANISOU 1703 O ARG A 237 2528 2055 1525 275 -292 432 O ATOM 1704 CB ARG A 237 10.687 21.035 63.993 1.00 29.24 C ANISOU 1704 CB ARG A 237 4337 3830 2943 383 -524 393 C ATOM 1705 CG ARG A 237 12.025 20.428 63.705 1.00 42.96 C ANISOU 1705 CG ARG A 237 6010 5576 4736 463 -654 383 C ATOM 1706 CD ARG A 237 12.977 20.633 64.864 1.00 42.12 C ANISOU 1706 CD ARG A 237 5974 5505 4524 559 -814 367 C ATOM 1707 NE ARG A 237 14.038 19.645 64.817 1.00 43.19 N ANISOU 1707 NE ARG A 237 6089 5621 4700 656 -919 383 N ATOM 1708 CZ ARG A 237 15.139 19.692 65.556 1.00 46.66 C ANISOU 1708 CZ ARG A 237 6504 6094 5131 716 -1040 342 C ATOM 1709 NH1 ARG A 237 15.332 20.698 66.401 1.00 39.32 N ANISOU 1709 NH1 ARG A 237 5585 5220 4137 701 -1094 285 N ATOM 1710 NH2 ARG A 237 16.051 18.737 65.437 1.00 50.93 N ANISOU 1710 NH2 ARG A 237 7008 6609 5732 793 -1109 352 N ATOM 1711 N LEU A 238 7.922 19.895 63.069 1.00 20.22 N ANISOU 1711 N LEU A 238 3241 2558 1884 239 -178 474 N ATOM 1712 CA LEU A 238 7.101 18.704 62.856 1.00 20.71 C ANISOU 1712 CA LEU A 238 3357 2531 1983 215 -56 528 C ATOM 1713 C LEU A 238 6.309 18.832 61.550 1.00 14.40 C ANISOU 1713 C LEU A 238 2416 1736 1320 129 25 478 C ATOM 1714 O LEU A 238 6.130 17.860 60.818 1.00 21.42 O ANISOU 1714 O LEU A 238 3274 2571 2292 116 68 488 O ATOM 1715 CB LEU A 238 6.191 18.473 64.060 1.00 20.65 C ANISOU 1715 CB LEU A 238 3520 2466 1861 208 54 586 C ATOM 1716 CG LEU A 238 5.323 17.226 64.120 1.00 25.55 C ANISOU 1716 CG LEU A 238 4226 2975 2507 179 201 647 C ATOM 1717 CD1 LEU A 238 6.174 15.957 64.088 1.00 18.02 C ANISOU 1717 CD1 LEU A 238 3338 1954 1556 259 143 708 C ATOM 1718 CD2 LEU A 238 4.495 17.289 65.390 1.00 25.51 C ANISOU 1718 CD2 LEU A 238 4390 2926 2377 167 319 695 C ATOM 1719 N ARG A 239 5.859 20.043 61.245 1.00 13.61 N ANISOU 1719 N ARG A 239 2233 1697 1240 77 35 421 N ATOM 1720 CA ARG A 239 5.224 20.301 59.961 1.00 13.59 C ANISOU 1720 CA ARG A 239 2098 1711 1355 14 80 369 C ATOM 1721 C ARG A 239 6.163 19.974 58.804 1.00 17.16 C ANISOU 1721 C ARG A 239 2452 2182 1886 36 4 345 C ATOM 1722 O ARG A 239 5.770 19.336 57.829 1.00 14.91 O ANISOU 1722 O ARG A 239 2110 1869 1684 8 46 329 O ATOM 1723 CB ARG A 239 4.843 21.766 59.835 1.00 19.04 C ANISOU 1723 CB ARG A 239 2724 2465 2045 -22 76 315 C ATOM 1724 CG ARG A 239 4.203 22.066 58.503 1.00 22.08 C ANISOU 1724 CG ARG A 239 2986 2867 2535 -70 106 266 C ATOM 1725 CD ARG A 239 4.249 23.526 58.191 1.00 23.03 C ANISOU 1725 CD ARG A 239 3044 3049 2660 -83 69 220 C ATOM 1726 NE ARG A 239 5.602 23.978 57.914 1.00 29.44 N ANISOU 1726 NE ARG A 239 3821 3900 3466 -52 -30 207 N ATOM 1727 CZ ARG A 239 5.993 25.240 58.042 1.00 25.83 C ANISOU 1727 CZ ARG A 239 3340 3483 2991 -56 -71 175 C ATOM 1728 NH1 ARG A 239 5.133 26.157 58.453 1.00 26.36 N ANISOU 1728 NH1 ARG A 239 3422 3556 3036 -81 -26 156 N ATOM 1729 NH2 ARG A 239 7.242 25.579 57.766 1.00 24.08 N ANISOU 1729 NH2 ARG A 239 3074 3289 2784 -36 -149 156 N ATOM 1730 N ASN A 240 7.405 20.430 58.921 1.00 14.88 N ANISOU 1730 N ASN A 240 2141 1940 1574 84 -105 333 N ATOM 1731 CA ASN A 240 8.413 20.196 57.890 1.00 15.77 C ANISOU 1731 CA ASN A 240 2157 2071 1763 106 -167 304 C ATOM 1732 C ASN A 240 8.704 18.710 57.714 1.00 13.90 C ANISOU 1732 C ASN A 240 1954 1768 1558 147 -160 340 C ATOM 1733 O ASN A 240 8.785 18.218 56.588 1.00 16.91 O ANISOU 1733 O ASN A 240 2264 2138 2023 134 -141 315 O ATOM 1734 CB ASN A 240 9.704 20.960 58.199 1.00 19.67 C ANISOU 1734 CB ASN A 240 2612 2622 2239 147 -279 275 C ATOM 1735 CG ASN A 240 9.532 22.481 58.105 1.00 20.42 C ANISOU 1735 CG ASN A 240 2655 2774 2330 99 -280 227 C ATOM 1736 OD1 ASN A 240 8.660 22.982 57.387 1.00 14.04 O ANISOU 1736 OD1 ASN A 240 1809 1971 1555 44 -211 209 O ATOM 1737 ND2 ASN A 240 10.397 23.218 58.802 1.00 14.81 N ANISOU 1737 ND2 ASN A 240 1941 2101 1583 125 -366 200 N ATOM 1738 N LEU A 241 8.848 17.995 58.826 1.00 13.30 N ANISOU 1738 N LEU A 241 1999 1644 1411 201 -173 400 N ATOM 1739 CA LEU A 241 9.148 16.572 58.769 1.00 14.01 C ANISOU 1739 CA LEU A 241 2140 1655 1529 249 -166 444 C ATOM 1740 C LEU A 241 8.000 15.824 58.106 1.00 16.59 C ANISOU 1740 C LEU A 241 2465 1916 1924 182 -42 444 C ATOM 1741 O LEU A 241 8.204 14.957 57.252 1.00 16.08 O ANISOU 1741 O LEU A 241 2359 1811 1940 188 -30 430 O ATOM 1742 CB LEU A 241 9.422 16.021 60.167 1.00 15.30 C ANISOU 1742 CB LEU A 241 2462 1769 1582 326 -199 519 C ATOM 1743 CG LEU A 241 9.748 14.528 60.268 1.00 18.98 C ANISOU 1743 CG LEU A 241 3010 2135 2065 392 -193 578 C ATOM 1744 CD1 LEU A 241 10.896 14.180 59.343 1.00 20.38 C ANISOU 1744 CD1 LEU A 241 3070 2331 2341 442 -278 535 C ATOM 1745 CD2 LEU A 241 10.057 14.125 61.709 1.00 21.08 C ANISOU 1745 CD2 LEU A 241 3455 2357 2196 482 -239 659 C ATOM 1746 N ASN A 242 6.781 16.172 58.494 1.00 15.23 N ANISOU 1746 N ASN A 242 2330 1733 1725 118 51 449 N ATOM 1747 CA ASN A 242 5.623 15.537 57.894 1.00 13.64 C ANISOU 1747 CA ASN A 242 2107 1473 1604 47 166 432 C ATOM 1748 C ASN A 242 5.404 15.886 56.436 1.00 15.54 C ANISOU 1748 C ASN A 242 2204 1762 1938 1 156 352 C ATOM 1749 O ASN A 242 5.066 15.008 55.647 1.00 13.81 O ANISOU 1749 O ASN A 242 1954 1494 1801 -24 198 326 O ATOM 1750 CB ASN A 242 4.381 15.790 58.725 1.00 14.03 C ANISOU 1750 CB ASN A 242 2221 1494 1614 -9 275 449 C ATOM 1751 CG ASN A 242 4.313 14.866 59.906 1.00 19.15 C ANISOU 1751 CG ASN A 242 3038 2048 2192 23 338 535 C ATOM 1752 OD1 ASN A 242 4.527 13.673 59.761 1.00 23.42 O ANISOU 1752 OD1 ASN A 242 3625 2502 2771 44 362 568 O ATOM 1753 ND2 ASN A 242 4.045 15.413 61.088 1.00 19.62 N ANISOU 1753 ND2 ASN A 242 3200 2114 2139 30 368 573 N ATOM 1754 N ALA A 243 5.618 17.148 56.073 1.00 11.87 N ANISOU 1754 N ALA A 243 1663 1388 1459 -7 101 312 N ATOM 1755 CA ALA A 243 5.536 17.526 54.668 1.00 11.10 C ANISOU 1755 CA ALA A 243 1452 1336 1429 -35 85 245 C ATOM 1756 C ALA A 243 6.518 16.703 53.837 1.00 16.66 C ANISOU 1756 C ALA A 243 2126 2024 2181 4 45 233 C ATOM 1757 O ALA A 243 6.183 16.243 52.747 1.00 11.02 O ANISOU 1757 O ALA A 243 1361 1297 1530 -21 69 187 O ATOM 1758 CB ALA A 243 5.805 19.010 54.489 1.00 11.16 C ANISOU 1758 CB ALA A 243 1407 1429 1405 -38 35 219 C ATOM 1759 N LEU A 244 7.730 16.523 54.359 1.00 13.69 N ANISOU 1759 N LEU A 244 1778 1648 1777 69 -19 266 N ATOM 1760 CA LEU A 244 8.754 15.748 53.665 1.00 18.90 C ANISOU 1760 CA LEU A 244 2402 2289 2490 116 -54 251 C ATOM 1761 C LEU A 244 8.394 14.263 53.555 1.00 12.43 C ANISOU 1761 C LEU A 244 1634 1371 1719 122 1 267 C ATOM 1762 O LEU A 244 8.580 13.657 52.505 1.00 13.03 O ANISOU 1762 O LEU A 244 1661 1428 1860 120 13 224 O ATOM 1763 CB LEU A 244 10.104 15.886 54.375 1.00 15.66 C ANISOU 1763 CB LEU A 244 2000 1900 2050 194 -145 275 C ATOM 1764 CG LEU A 244 11.237 15.102 53.710 1.00 17.35 C ANISOU 1764 CG LEU A 244 2163 2095 2334 252 -182 253 C ATOM 1765 CD1 LEU A 244 11.479 15.639 52.309 1.00 14.31 C ANISOU 1765 CD1 LEU A 244 1671 1764 2004 214 -163 183 C ATOM 1766 CD2 LEU A 244 12.503 15.207 54.548 1.00 18.78 C ANISOU 1766 CD2 LEU A 244 2344 2296 2497 336 -284 270 C ATOM 1767 N ARG A 245 7.884 13.681 54.637 1.00 15.11 N ANISOU 1767 N ARG A 245 2080 1639 2021 127 42 329 N ATOM 1768 CA ARG A 245 7.444 12.292 54.615 1.00 16.44 C ANISOU 1768 CA ARG A 245 2310 1695 2240 122 113 349 C ATOM 1769 C ARG A 245 6.332 12.081 53.606 1.00 16.28 C ANISOU 1769 C ARG A 245 2225 1660 2299 36 188 280 C ATOM 1770 O ARG A 245 6.305 11.079 52.892 1.00 13.95 O ANISOU 1770 O ARG A 245 1919 1302 2079 30 218 248 O ATOM 1771 CB ARG A 245 6.942 11.841 55.984 1.00 17.30 C ANISOU 1771 CB ARG A 245 2560 1725 2287 130 170 432 C ATOM 1772 CG ARG A 245 8.020 11.685 57.018 1.00 23.55 C ANISOU 1772 CG ARG A 245 3446 2505 2996 233 89 505 C ATOM 1773 CD ARG A 245 7.397 11.446 58.377 1.00 25.91 C ANISOU 1773 CD ARG A 245 3905 2737 3204 236 155 588 C ATOM 1774 NE ARG A 245 8.401 11.145 59.391 1.00 38.55 N ANISOU 1774 NE ARG A 245 5622 4315 4712 351 66 662 N ATOM 1775 CZ ARG A 245 8.156 11.112 60.696 1.00 44.19 C ANISOU 1775 CZ ARG A 245 6497 4989 5304 383 90 741 C ATOM 1776 NH1 ARG A 245 6.935 11.371 61.153 1.00 47.32 N ANISOU 1776 NH1 ARG A 245 6950 5362 5667 298 218 755 N ATOM 1777 NH2 ARG A 245 9.136 10.830 61.543 1.00 48.39 N ANISOU 1777 NH2 ARG A 245 7135 5507 5746 503 -16 802 N ATOM 1778 N GLN A 246 5.393 13.015 53.578 1.00 16.69 N ANISOU 1778 N GLN A 246 2237 1769 2337 -26 214 252 N ATOM 1779 CA GLN A 246 4.283 12.947 52.641 1.00 15.64 C ANISOU 1779 CA GLN A 246 2030 1635 2277 -100 263 175 C ATOM 1780 C GLN A 246 4.750 13.063 51.189 1.00 17.09 C ANISOU 1780 C GLN A 246 2125 1873 2495 -90 207 102 C ATOM 1781 O GLN A 246 4.307 12.307 50.311 1.00 13.66 O ANISOU 1781 O GLN A 246 1658 1400 2131 -120 233 40 O ATOM 1782 CB GLN A 246 3.286 14.055 52.964 1.00 15.62 C ANISOU 1782 CB GLN A 246 1996 1690 2249 -149 285 159 C ATOM 1783 CG GLN A 246 2.491 13.763 54.221 1.00 18.00 C ANISOU 1783 CG GLN A 246 2381 1923 2536 -181 380 210 C ATOM 1784 CD GLN A 246 1.744 14.975 54.727 1.00 21.07 C ANISOU 1784 CD GLN A 246 2747 2373 2886 -211 398 202 C ATOM 1785 OE1 GLN A 246 1.449 15.898 53.968 1.00 16.61 O ANISOU 1785 OE1 GLN A 246 2089 1886 2335 -225 353 144 O ATOM 1786 NE2 GLN A 246 1.413 14.967 56.014 1.00 17.12 N ANISOU 1786 NE2 GLN A 246 2343 1831 2331 -217 469 262 N ATOM 1787 N ALA A 247 5.628 14.024 50.939 1.00 12.75 N ANISOU 1787 N ALA A 247 1542 1408 1896 -52 136 104 N ATOM 1788 CA ALA A 247 6.201 14.206 49.611 1.00 17.36 C ANISOU 1788 CA ALA A 247 2060 2040 2496 -38 98 45 C ATOM 1789 C ALA A 247 6.925 12.925 49.165 1.00 21.74 C ANISOU 1789 C ALA A 247 2628 2528 3103 -1 106 32 C ATOM 1790 O ALA A 247 6.753 12.457 48.033 1.00 18.81 O ANISOU 1790 O ALA A 247 2224 2150 2773 -16 117 -36 O ATOM 1791 CB ALA A 247 7.157 15.398 49.601 1.00 13.17 C ANISOU 1791 CB ALA A 247 1500 1592 1911 -5 42 60 C ATOM 1792 N ALA A 248 7.714 12.340 50.061 1.00 13.32 N ANISOU 1792 N ALA A 248 1616 1411 2034 53 96 94 N ATOM 1793 CA ALA A 248 8.404 11.093 49.729 1.00 13.10 C ANISOU 1793 CA ALA A 248 1604 1307 2064 98 103 86 C ATOM 1794 C ALA A 248 7.402 10.000 49.393 1.00 16.75 C ANISOU 1794 C ALA A 248 2093 1678 2592 48 175 51 C ATOM 1795 O ALA A 248 7.551 9.282 48.402 1.00 17.73 O ANISOU 1795 O ALA A 248 2191 1771 2772 49 188 -12 O ATOM 1796 CB ALA A 248 9.298 10.648 50.871 1.00 17.64 C ANISOU 1796 CB ALA A 248 2246 1835 2621 176 70 165 C ATOM 1797 N MET A 249 6.372 9.870 50.221 1.00 17.30 N ANISOU 1797 N MET A 249 2213 1699 2660 0 228 86 N ATOM 1798 CA MET A 249 5.370 8.835 49.999 1.00 16.08 C ANISOU 1798 CA MET A 249 2076 1446 2587 -60 309 47 C ATOM 1799 C MET A 249 4.652 9.042 48.653 1.00 14.93 C ANISOU 1799 C MET A 249 1837 1351 2484 -118 302 -69 C ATOM 1800 O MET A 249 4.303 8.085 47.987 1.00 17.49 O ANISOU 1800 O MET A 249 2151 1608 2886 -146 335 -136 O ATOM 1801 CB MET A 249 4.386 8.761 51.178 1.00 19.39 C ANISOU 1801 CB MET A 249 2561 1806 3001 -109 387 103 C ATOM 1802 CG MET A 249 3.514 7.521 51.215 1.00 34.86 C ANISOU 1802 CG MET A 249 4556 3630 5058 -170 492 80 C ATOM 1803 SD MET A 249 4.460 5.989 51.059 1.00 54.33 S ANISOU 1803 SD MET A 249 7098 5964 7581 -105 506 102 S ATOM 1804 CE MET A 249 5.841 6.296 52.168 1.00 41.48 C ANISOU 1804 CE MET A 249 5563 4356 5840 19 432 230 C ATOM 1805 N ARG A 250 4.464 10.290 48.238 1.00 14.39 N ANISOU 1805 N ARG A 250 1707 1397 2362 -128 251 -95 N ATOM 1806 CA ARG A 250 3.882 10.546 46.925 1.00 19.72 C ANISOU 1806 CA ARG A 250 2311 2128 3056 -161 224 -199 C ATOM 1807 C ARG A 250 4.698 9.916 45.802 1.00 22.20 C ANISOU 1807 C ARG A 250 2617 2435 3385 -124 203 -256 C ATOM 1808 O ARG A 250 4.159 9.602 44.750 1.00 18.66 O ANISOU 1808 O ARG A 250 2134 1990 2965 -152 195 -352 O ATOM 1809 CB ARG A 250 3.734 12.045 46.664 1.00 12.41 C ANISOU 1809 CB ARG A 250 1341 1319 2054 -158 169 -201 C ATOM 1810 CG ARG A 250 2.834 12.766 47.644 1.00 20.43 C ANISOU 1810 CG ARG A 250 2354 2350 3059 -194 191 -164 C ATOM 1811 CD ARG A 250 2.350 14.080 47.044 1.00 16.53 C ANISOU 1811 CD ARG A 250 1805 1958 2519 -198 137 -201 C ATOM 1812 NE ARG A 250 3.408 15.078 46.872 1.00 17.51 N ANISOU 1812 NE ARG A 250 1940 2153 2561 -148 90 -160 N ATOM 1813 CZ ARG A 250 3.770 15.949 47.812 1.00 19.52 C ANISOU 1813 CZ ARG A 250 2214 2435 2766 -134 85 -92 C ATOM 1814 NH1 ARG A 250 3.165 15.959 49.004 1.00 14.73 N ANISOU 1814 NH1 ARG A 250 1632 1796 2166 -159 125 -51 N ATOM 1815 NH2 ARG A 250 4.727 16.824 47.560 1.00 14.84 N ANISOU 1815 NH2 ARG A 250 1620 1900 2119 -99 47 -70 N ATOM 1816 N HIS A 251 6.000 9.732 46.032 1.00 13.48 N ANISOU 1816 N HIS A 251 1542 1320 2261 -58 192 -203 N ATOM 1817 CA HIS A 251 6.902 9.234 45.005 1.00 13.74 C ANISOU 1817 CA HIS A 251 1563 1351 2308 -16 183 -256 C ATOM 1818 C HIS A 251 7.554 7.943 45.491 1.00 17.11 C ANISOU 1818 C HIS A 251 2037 1663 2800 27 217 -225 C ATOM 1819 O HIS A 251 8.724 7.663 45.211 1.00 16.66 O ANISOU 1819 O HIS A 251 1976 1602 2752 92 205 -224 O ATOM 1820 CB HIS A 251 7.963 10.287 44.692 1.00 23.62 C ANISOU 1820 CB HIS A 251 2784 2698 3491 31 144 -236 C ATOM 1821 CG HIS A 251 7.391 11.596 44.249 1.00 19.68 C ANISOU 1821 CG HIS A 251 2256 2299 2923 -1 114 -253 C ATOM 1822 ND1 HIS A 251 6.972 11.822 42.955 1.00 16.01 N ANISOU 1822 ND1 HIS A 251 1776 1879 2428 -17 103 -334 N ATOM 1823 CD2 HIS A 251 7.164 12.747 44.927 1.00 15.03 C ANISOU 1823 CD2 HIS A 251 1660 1767 2284 -12 91 -199 C ATOM 1824 CE1 HIS A 251 6.503 13.055 42.859 1.00 14.24 C ANISOU 1824 CE1 HIS A 251 1538 1731 2140 -32 73 -323 C ATOM 1825 NE2 HIS A 251 6.604 13.635 44.041 1.00 17.10 N ANISOU 1825 NE2 HIS A 251 1901 2101 2496 -33 69 -244 N ATOM 1826 N GLU A 252 6.770 7.172 46.231 1.00 15.94 N ANISOU 1826 N GLU A 252 1936 1416 2703 -10 266 -200 N ATOM 1827 CA GLU A 252 7.221 5.930 46.838 1.00 20.35 C ANISOU 1827 CA GLU A 252 2566 1845 3323 30 306 -155 C ATOM 1828 C GLU A 252 7.886 4.989 45.823 1.00 23.23 C ANISOU 1828 C GLU A 252 2920 2160 3748 67 314 -229 C ATOM 1829 O GLU A 252 8.916 4.400 46.113 1.00 28.00 O ANISOU 1829 O GLU A 252 3554 2708 4375 147 309 -189 O ATOM 1830 CB GLU A 252 6.041 5.250 47.537 1.00 29.95 C ANISOU 1830 CB GLU A 252 3833 2952 4593 -39 383 -138 C ATOM 1831 CG GLU A 252 6.403 4.058 48.401 1.00 48.61 C ANISOU 1831 CG GLU A 252 6301 5165 7002 3 436 -62 C ATOM 1832 CD GLU A 252 5.178 3.407 49.021 1.00 56.55 C ANISOU 1832 CD GLU A 252 7362 6054 8069 -81 540 -50 C ATOM 1833 OE1 GLU A 252 4.049 3.772 48.624 1.00 53.39 O ANISOU 1833 OE1 GLU A 252 6894 5691 7699 -175 565 -125 O ATOM 1834 OE2 GLU A 252 5.345 2.536 49.904 1.00 62.23 O ANISOU 1834 OE2 GLU A 252 8193 6641 8810 -51 599 34 O ATOM 1835 N GLU A 253 7.302 4.875 44.633 1.00 21.14 N ANISOU 1835 N GLU A 253 2610 1916 3505 16 322 -344 N ATOM 1836 CA GLU A 253 7.818 4.000 43.582 1.00 34.84 C ANISOU 1836 CA GLU A 253 4341 3607 5290 43 337 -432 C ATOM 1837 C GLU A 253 9.127 4.530 42.975 1.00 33.16 C ANISOU 1837 C GLU A 253 4092 3478 5027 118 302 -438 C ATOM 1838 O GLU A 253 9.870 3.788 42.326 1.00 30.68 O ANISOU 1838 O GLU A 253 3780 3120 4756 165 324 -491 O ATOM 1839 CB GLU A 253 6.752 3.798 42.485 1.00 38.08 C ANISOU 1839 CB GLU A 253 4719 4027 5724 -34 343 -564 C ATOM 1840 CG GLU A 253 6.149 5.104 41.897 1.00 67.49 C ANISOU 1840 CG GLU A 253 8389 7895 9357 -69 285 -601 C ATOM 1841 CD GLU A 253 4.850 5.559 42.583 1.00 61.30 C ANISOU 1841 CD GLU A 253 7585 7121 8586 -143 285 -583 C ATOM 1842 OE1 GLU A 253 3.752 5.315 42.027 1.00 59.90 O ANISOU 1842 OE1 GLU A 253 7372 6935 8452 -208 280 -684 O ATOM 1843 OE2 GLU A 253 4.926 6.172 43.670 1.00 46.08 O ANISOU 1843 OE2 GLU A 253 5671 5211 6626 -134 287 -476 O ATOM 1844 N ASN A 254 9.399 5.813 43.199 1.00 19.35 N ANISOU 1844 N ASN A 254 2311 1845 3197 127 259 -389 N ATOM 1845 CA ASN A 254 10.563 6.490 42.638 1.00 23.05 C ANISOU 1845 CA ASN A 254 2736 2399 3624 181 241 -398 C ATOM 1846 C ASN A 254 11.434 7.070 43.743 1.00 24.63 C ANISOU 1846 C ASN A 254 2922 2625 3810 234 204 -298 C ATOM 1847 O ASN A 254 11.854 8.232 43.679 1.00 15.47 O ANISOU 1847 O ASN A 254 1721 1565 2594 236 178 -282 O ATOM 1848 CB ASN A 254 10.110 7.634 41.732 1.00 25.77 C ANISOU 1848 CB ASN A 254 3052 2860 3881 137 223 -445 C ATOM 1849 CG ASN A 254 9.458 7.150 40.464 1.00 31.35 C ANISOU 1849 CG ASN A 254 3770 3559 4582 104 239 -560 C ATOM 1850 OD1 ASN A 254 10.029 6.344 39.733 1.00 41.71 O ANISOU 1850 OD1 ASN A 254 5091 4828 5927 135 273 -625 O ATOM 1851 ND2 ASN A 254 8.256 7.640 40.190 1.00 29.38 N ANISOU 1851 ND2 ASN A 254 3519 3353 4292 45 209 -594 N ATOM 1852 N GLU A 255 11.694 6.265 44.760 1.00 21.34 N ANISOU 1852 N GLU A 255 2549 2117 3444 279 201 -234 N ATOM 1853 CA GLU A 255 12.339 6.756 45.960 1.00 22.93 C ANISOU 1853 CA GLU A 255 2754 2338 3621 332 148 -140 C ATOM 1854 C GLU A 255 13.706 7.343 45.656 1.00 18.57 C ANISOU 1854 C GLU A 255 2122 1860 3075 394 115 -157 C ATOM 1855 O GLU A 255 14.039 8.440 46.116 1.00 22.03 O ANISOU 1855 O GLU A 255 2523 2381 3465 393 71 -123 O ATOM 1856 CB GLU A 255 12.456 5.631 46.983 1.00 28.24 C ANISOU 1856 CB GLU A 255 3507 2884 4339 388 149 -71 C ATOM 1857 CG GLU A 255 13.054 6.057 48.307 1.00 34.88 C ANISOU 1857 CG GLU A 255 4373 3742 5138 454 80 26 C ATOM 1858 CD GLU A 255 13.077 4.923 49.315 1.00 42.94 C ANISOU 1858 CD GLU A 255 5505 4628 6184 517 82 105 C ATOM 1859 OE1 GLU A 255 12.394 3.901 49.089 1.00 49.88 O ANISOU 1859 OE1 GLU A 255 6444 5394 7113 485 155 92 O ATOM 1860 OE2 GLU A 255 13.777 5.052 50.335 1.00 40.23 O ANISOU 1860 OE2 GLU A 255 5193 4286 5807 601 10 178 O ATOM 1861 N ARG A 256 14.505 6.622 44.886 1.00 16.67 N ANISOU 1861 N ARG A 256 1849 1584 2901 443 143 -217 N ATOM 1862 CA ARG A 256 15.844 7.107 44.584 1.00 17.41 C ANISOU 1862 CA ARG A 256 1853 1739 3024 499 129 -244 C ATOM 1863 C ARG A 256 15.773 8.416 43.818 1.00 19.32 C ANISOU 1863 C ARG A 256 2044 2096 3199 435 150 -280 C ATOM 1864 O ARG A 256 16.521 9.357 44.109 1.00 19.74 O ANISOU 1864 O ARG A 256 2033 2220 3247 448 122 -264 O ATOM 1865 CB ARG A 256 16.655 6.078 43.802 1.00 20.15 C ANISOU 1865 CB ARG A 256 2172 2024 3461 561 174 -314 C ATOM 1866 CG ARG A 256 17.639 5.316 44.663 1.00 44.86 C ANISOU 1866 CG ARG A 256 5288 5082 6674 674 123 -274 C ATOM 1867 CD ARG A 256 18.533 4.407 43.836 1.00 59.99 C ANISOU 1867 CD ARG A 256 7158 6943 8691 742 172 -354 C ATOM 1868 NE ARG A 256 19.659 5.118 43.228 1.00 65.69 N ANISOU 1868 NE ARG A 256 7758 7752 9449 763 192 -415 N ATOM 1869 CZ ARG A 256 19.639 5.646 42.008 1.00 62.18 C ANISOU 1869 CZ ARG A 256 7282 7371 8971 700 277 -491 C ATOM 1870 NH1 ARG A 256 18.540 5.551 41.264 1.00 54.84 N ANISOU 1870 NH1 ARG A 256 6432 6436 7967 622 325 -520 N ATOM 1871 NH2 ARG A 256 20.718 6.268 41.532 1.00 59.19 N ANISOU 1871 NH2 ARG A 256 6796 7058 8636 718 313 -542 N ATOM 1872 N ALA A 257 14.870 8.476 42.843 1.00 16.27 N ANISOU 1872 N ALA A 257 1692 1725 2765 369 197 -331 N ATOM 1873 CA ALA A 257 14.677 9.684 42.035 1.00 15.02 C ANISOU 1873 CA ALA A 257 1515 1665 2528 315 219 -359 C ATOM 1874 C ALA A 257 14.276 10.875 42.885 1.00 14.16 C ANISOU 1874 C ALA A 257 1402 1617 2360 280 170 -290 C ATOM 1875 O ALA A 257 14.651 12.017 42.604 1.00 13.79 O ANISOU 1875 O ALA A 257 1319 1645 2275 261 179 -290 O ATOM 1876 CB ALA A 257 13.606 9.438 40.961 1.00 19.08 C ANISOU 1876 CB ALA A 257 2082 2176 2990 262 251 -424 C ATOM 1877 N PHE A 258 13.484 10.613 43.913 1.00 14.70 N ANISOU 1877 N PHE A 258 1516 1647 2423 268 129 -233 N ATOM 1878 CA PHE A 258 12.983 11.679 44.764 1.00 14.44 C ANISOU 1878 CA PHE A 258 1490 1666 2332 234 88 -173 C ATOM 1879 C PHE A 258 14.140 12.297 45.520 1.00 13.28 C ANISOU 1879 C PHE A 258 1291 1554 2201 279 46 -137 C ATOM 1880 O PHE A 258 14.363 13.506 45.455 1.00 15.62 O ANISOU 1880 O PHE A 258 1551 1923 2462 252 40 -136 O ATOM 1881 CB PHE A 258 11.952 11.128 45.749 1.00 15.99 C ANISOU 1881 CB PHE A 258 1751 1800 2524 215 74 -123 C ATOM 1882 CG PHE A 258 11.430 12.149 46.718 1.00 15.93 C ANISOU 1882 CG PHE A 258 1758 1838 2456 185 40 -64 C ATOM 1883 CD1 PHE A 258 10.444 13.049 46.333 1.00 11.90 C ANISOU 1883 CD1 PHE A 258 1246 1383 1895 123 49 -81 C ATOM 1884 CD2 PHE A 258 11.918 12.204 48.017 1.00 16.64 C ANISOU 1884 CD2 PHE A 258 1869 1914 2539 228 -5 4 C ATOM 1885 CE1 PHE A 258 9.942 13.986 47.230 1.00 16.52 C ANISOU 1885 CE1 PHE A 258 1842 2003 2430 98 26 -33 C ATOM 1886 CE2 PHE A 258 11.425 13.145 48.912 1.00 17.89 C ANISOU 1886 CE2 PHE A 258 2049 2113 2635 201 -31 50 C ATOM 1887 CZ PHE A 258 10.437 14.037 48.514 1.00 12.24 C ANISOU 1887 CZ PHE A 258 1325 1448 1878 133 -9 31 C ATOM 1888 N PHE A 259 14.899 11.470 46.221 1.00 14.02 N ANISOU 1888 N PHE A 259 1379 1593 2354 350 12 -114 N ATOM 1889 CA PHE A 259 16.000 12.014 47.008 1.00 20.31 C ANISOU 1889 CA PHE A 259 2117 2427 3174 401 -51 -93 C ATOM 1890 C PHE A 259 17.141 12.549 46.149 1.00 17.02 C ANISOU 1890 C PHE A 259 1595 2062 2810 409 -19 -158 C ATOM 1891 O PHE A 259 17.827 13.497 46.527 1.00 14.54 O ANISOU 1891 O PHE A 259 1214 1805 2506 409 -52 -160 O ATOM 1892 CB PHE A 259 16.463 11.017 48.059 1.00 20.21 C ANISOU 1892 CB PHE A 259 2137 2342 3200 489 -113 -47 C ATOM 1893 CG PHE A 259 15.446 10.802 49.156 1.00 16.86 C ANISOU 1893 CG PHE A 259 1824 1874 2707 477 -138 32 C ATOM 1894 CD1 PHE A 259 15.195 11.795 50.082 1.00 22.15 C ANISOU 1894 CD1 PHE A 259 2513 2599 3305 455 -186 76 C ATOM 1895 CD2 PHE A 259 14.746 9.618 49.248 1.00 24.33 C ANISOU 1895 CD2 PHE A 259 2858 2719 3665 481 -99 57 C ATOM 1896 CE1 PHE A 259 14.259 11.611 51.086 1.00 17.22 C ANISOU 1896 CE1 PHE A 259 1996 1932 2613 442 -190 145 C ATOM 1897 CE2 PHE A 259 13.820 9.424 50.250 1.00 29.18 C ANISOU 1897 CE2 PHE A 259 3577 3286 4223 462 -97 129 C ATOM 1898 CZ PHE A 259 13.576 10.424 51.168 1.00 15.06 C ANISOU 1898 CZ PHE A 259 1809 1557 2354 444 -140 174 C ATOM 1899 N GLU A 260 17.319 11.986 44.966 1.00 15.26 N ANISOU 1899 N GLU A 260 1358 1819 2622 409 56 -218 N ATOM 1900 CA GLU A 260 18.353 12.521 44.092 1.00 18.22 C ANISOU 1900 CA GLU A 260 1643 2239 3042 408 114 -281 C ATOM 1901 C GLU A 260 17.980 13.931 43.636 1.00 16.51 C ANISOU 1901 C GLU A 260 1429 2095 2750 328 151 -280 C ATOM 1902 O GLU A 260 18.838 14.810 43.552 1.00 17.89 O ANISOU 1902 O GLU A 260 1525 2314 2958 317 172 -301 O ATOM 1903 CB GLU A 260 18.612 11.601 42.901 1.00 17.20 C ANISOU 1903 CB GLU A 260 1513 2070 2953 427 197 -350 C ATOM 1904 CG GLU A 260 19.538 10.440 43.233 1.00 36.42 C ANISOU 1904 CG GLU A 260 3900 4438 5500 522 174 -370 C ATOM 1905 CD GLU A 260 19.606 9.414 42.121 1.00 44.30 C ANISOU 1905 CD GLU A 260 4917 5382 6533 540 258 -439 C ATOM 1906 OE1 GLU A 260 18.669 9.388 41.291 1.00 41.99 O ANISOU 1906 OE1 GLU A 260 4701 5091 6161 481 309 -461 O ATOM 1907 OE2 GLU A 260 20.594 8.644 42.076 1.00 50.15 O ANISOU 1907 OE2 GLU A 260 5596 6079 7381 618 268 -478 O ATOM 1908 N ARG A 261 16.701 14.141 43.349 1.00 13.73 N ANISOU 1908 N ARG A 261 1163 1749 2305 276 159 -259 N ATOM 1909 CA ARG A 261 16.244 15.452 42.918 1.00 13.10 C ANISOU 1909 CA ARG A 261 1102 1729 2148 213 187 -251 C ATOM 1910 C ARG A 261 16.331 16.472 44.056 1.00 19.16 C ANISOU 1910 C ARG A 261 1842 2530 2908 198 125 -203 C ATOM 1911 O ARG A 261 16.713 17.621 43.842 1.00 13.68 O ANISOU 1911 O ARG A 261 1117 1878 2204 164 155 -208 O ATOM 1912 CB ARG A 261 14.815 15.396 42.370 1.00 12.69 C ANISOU 1912 CB ARG A 261 1139 1675 2007 174 192 -249 C ATOM 1913 CG ARG A 261 14.352 16.715 41.784 1.00 13.59 C ANISOU 1913 CG ARG A 261 1283 1844 2038 127 217 -242 C ATOM 1914 CD ARG A 261 12.915 16.624 41.211 1.00 14.03 C ANISOU 1914 CD ARG A 261 1415 1902 2013 102 202 -252 C ATOM 1915 NE ARG A 261 12.534 17.932 40.692 1.00 13.20 N ANISOU 1915 NE ARG A 261 1344 1845 1826 73 216 -238 N ATOM 1916 CZ ARG A 261 12.597 18.296 39.418 1.00 11.89 C ANISOU 1916 CZ ARG A 261 1226 1699 1592 73 271 -268 C ATOM 1917 NH1 ARG A 261 12.981 17.431 38.477 1.00 13.76 N ANISOU 1917 NH1 ARG A 261 1480 1919 1830 94 320 -326 N ATOM 1918 NH2 ARG A 261 12.250 19.529 39.081 1.00 16.88 N ANISOU 1918 NH2 ARG A 261 1901 2363 2149 55 280 -241 N ATOM 1919 N LEU A 262 15.978 16.044 45.262 1.00 13.98 N ANISOU 1919 N LEU A 262 1209 1849 2253 223 47 -157 N ATOM 1920 CA LEU A 262 16.030 16.919 46.424 1.00 14.52 C ANISOU 1920 CA LEU A 262 1266 1948 2303 215 -18 -117 C ATOM 1921 C LEU A 262 17.470 17.345 46.648 1.00 18.17 C ANISOU 1921 C LEU A 262 1623 2435 2845 242 -36 -150 C ATOM 1922 O LEU A 262 17.739 18.500 46.978 1.00 16.91 O ANISOU 1922 O LEU A 262 1427 2317 2680 208 -49 -153 O ATOM 1923 CB LEU A 262 15.506 16.196 47.658 1.00 17.71 C ANISOU 1923 CB LEU A 262 1729 2311 2688 249 -88 -63 C ATOM 1924 CG LEU A 262 15.063 17.099 48.806 1.00 24.43 C ANISOU 1924 CG LEU A 262 2612 3193 3480 228 -144 -18 C ATOM 1925 CD1 LEU A 262 13.884 17.957 48.356 1.00 17.67 C ANISOU 1925 CD1 LEU A 262 1795 2363 2556 157 -99 -12 C ATOM 1926 CD2 LEU A 262 14.675 16.260 50.012 1.00 21.05 C ANISOU 1926 CD2 LEU A 262 2258 2714 3025 272 -197 38 C ATOM 1927 N GLY A 263 18.393 16.406 46.456 1.00 13.80 N ANISOU 1927 N GLY A 263 1014 1853 2377 302 -36 -185 N ATOM 1928 CA GLY A 263 19.816 16.695 46.575 1.00 14.95 C ANISOU 1928 CA GLY A 263 1034 2020 2625 333 -50 -235 C ATOM 1929 C GLY A 263 20.305 17.622 45.477 1.00 17.29 C ANISOU 1929 C GLY A 263 1271 2350 2949 271 60 -287 C ATOM 1930 O GLY A 263 21.056 18.553 45.738 1.00 19.12 O ANISOU 1930 O GLY A 263 1417 2615 3234 247 56 -316 O ATOM 1931 N THR A 264 19.876 17.377 44.242 1.00 14.84 N ANISOU 1931 N THR A 264 1013 2026 2598 244 162 -301 N ATOM 1932 CA THR A 264 20.294 18.214 43.115 1.00 15.96 C ANISOU 1932 CA THR A 264 1130 2190 2743 190 284 -340 C ATOM 1933 C THR A 264 19.921 19.657 43.408 1.00 14.23 C ANISOU 1933 C THR A 264 932 2005 2470 124 282 -309 C ATOM 1934 O THR A 264 20.708 20.570 43.241 1.00 14.71 O ANISOU 1934 O THR A 264 923 2081 2586 86 339 -339 O ATOM 1935 CB THR A 264 19.576 17.800 41.813 1.00 19.36 C ANISOU 1935 CB THR A 264 1660 2606 3090 174 372 -348 C ATOM 1936 OG1 THR A 264 20.014 16.492 41.411 1.00 21.36 O ANISOU 1936 OG1 THR A 264 1891 2821 3403 231 394 -392 O ATOM 1937 CG2 THR A 264 19.855 18.803 40.688 1.00 15.57 C ANISOU 1937 CG2 THR A 264 1195 2145 2576 119 501 -370 C ATOM 1938 N ILE A 265 18.688 19.843 43.851 1.00 16.12 N ANISOU 1938 N ILE A 265 1267 2248 2609 109 223 -252 N ATOM 1939 CA ILE A 265 18.187 21.170 44.143 1.00 13.25 C ANISOU 1939 CA ILE A 265 936 1909 2188 54 217 -220 C ATOM 1940 C ILE A 265 18.936 21.766 45.327 1.00 13.64 C ANISOU 1940 C ILE A 265 899 1976 2309 54 146 -230 C ATOM 1941 O ILE A 265 19.245 22.958 45.339 1.00 18.78 O ANISOU 1941 O ILE A 265 1520 2639 2975 2 179 -242 O ATOM 1942 CB ILE A 265 16.692 21.099 44.467 1.00 15.52 C ANISOU 1942 CB ILE A 265 1329 2196 2372 49 163 -166 C ATOM 1943 CG1 ILE A 265 15.906 20.753 43.199 1.00 16.12 C ANISOU 1943 CG1 ILE A 265 1486 2264 2375 43 225 -171 C ATOM 1944 CG2 ILE A 265 16.221 22.408 45.102 1.00 15.02 C ANISOU 1944 CG2 ILE A 265 1287 2154 2266 7 136 -135 C ATOM 1945 CD1 ILE A 265 14.451 20.420 43.471 1.00 23.95 C ANISOU 1945 CD1 ILE A 265 2555 3250 3294 43 168 -138 C ATOM 1946 N SER A 266 19.233 20.936 46.324 1.00 15.06 N ANISOU 1946 N SER A 266 1044 2150 2529 114 44 -229 N ATOM 1947 CA SER A 266 19.918 21.412 47.522 1.00 17.64 C ANISOU 1947 CA SER A 266 1298 2497 2908 128 -50 -246 C ATOM 1948 C SER A 266 21.362 21.794 47.230 1.00 24.66 C ANISOU 1948 C SER A 266 2041 3398 3932 119 -13 -325 C ATOM 1949 O SER A 266 21.953 22.612 47.932 1.00 22.45 O ANISOU 1949 O SER A 266 1685 3139 3704 99 -64 -360 O ATOM 1950 CB SER A 266 19.867 20.350 48.623 1.00 23.41 C ANISOU 1950 CB SER A 266 2051 3214 3631 210 -172 -218 C ATOM 1951 OG SER A 266 18.530 20.164 49.057 1.00 14.78 O ANISOU 1951 OG SER A 266 1084 2107 2423 203 -195 -150 O ATOM 1952 N ASP A 267 21.930 21.187 46.193 1.00 17.71 N ANISOU 1952 N ASP A 267 1116 2500 3114 132 79 -362 N ATOM 1953 CA ASP A 267 23.275 21.522 45.748 1.00 17.79 C ANISOU 1953 CA ASP A 267 1021 2508 3232 111 144 -429 C ATOM 1954 C ASP A 267 23.236 22.753 44.834 1.00 17.78 C ANISOU 1954 C ASP A 267 1044 2502 3208 17 283 -434 C ATOM 1955 O ASP A 267 24.268 23.185 44.333 1.00 21.83 O ANISOU 1955 O ASP A 267 1506 3001 3789 -17 362 -478 O ATOM 1956 CB ASP A 267 23.905 20.336 45.008 1.00 21.35 C ANISOU 1956 CB ASP A 267 1440 2932 3739 165 195 -462 C ATOM 1957 CG ASP A 267 24.082 19.105 45.894 1.00 38.50 C ANISOU 1957 CG ASP A 267 3593 5092 5942 266 62 -455 C ATOM 1958 OD1 ASP A 267 24.043 19.241 47.137 1.00 43.93 O ANISOU 1958 OD1 ASP A 267 4281 5797 6615 297 -72 -434 O ATOM 1959 OD2 ASP A 267 24.272 17.995 45.340 1.00 36.98 O ANISOU 1959 OD2 ASP A 267 3399 4870 5782 319 96 -471 O ATOM 1960 N ARG A 268 22.035 23.305 44.637 1.00 18.10 N ANISOU 1960 N ARG A 268 1177 2549 3150 -21 312 -384 N ATOM 1961 CA ARG A 268 21.810 24.454 43.754 1.00 15.33 C ANISOU 1961 CA ARG A 268 884 2186 2755 -99 442 -371 C ATOM 1962 C ARG A 268 22.049 24.199 42.260 1.00 20.82 C ANISOU 1962 C ARG A 268 1618 2859 3434 -111 600 -384 C ATOM 1963 O ARG A 268 22.548 25.057 41.538 1.00 22.74 O ANISOU 1963 O ARG A 268 1885 3077 3680 -165 713 -390 O ATOM 1964 CB ARG A 268 22.560 25.692 44.251 1.00 18.26 C ANISOU 1964 CB ARG A 268 1203 2550 3186 -156 442 -396 C ATOM 1965 CG ARG A 268 21.859 26.283 45.475 1.00 28.98 C ANISOU 1965 CG ARG A 268 2573 3929 4509 -163 323 -372 C ATOM 1966 CD ARG A 268 22.575 27.464 46.083 1.00 28.04 C ANISOU 1966 CD ARG A 268 2408 3799 4446 -214 306 -407 C ATOM 1967 NE ARG A 268 21.830 27.953 47.240 1.00 30.52 N ANISOU 1967 NE ARG A 268 2749 4136 4713 -216 193 -388 N ATOM 1968 CZ ARG A 268 22.314 28.790 48.154 1.00 33.36 C ANISOU 1968 CZ ARG A 268 3069 4495 5110 -241 129 -425 C ATOM 1969 NH1 ARG A 268 23.553 29.250 48.049 1.00 33.59 N ANISOU 1969 NH1 ARG A 268 3022 4502 5237 -270 165 -487 N ATOM 1970 NH2 ARG A 268 21.554 29.167 49.176 1.00 35.71 N ANISOU 1970 NH2 ARG A 268 3406 4813 5350 -238 31 -408 N ATOM 1971 N TYR A 269 21.655 23.019 41.800 1.00 16.39 N ANISOU 1971 N TYR A 269 1105 2295 2826 -56 591 -378 N ATOM 1972 CA TYR A 269 21.652 22.732 40.380 1.00 21.35 C ANISOU 1972 CA TYR A 269 1802 2906 3403 -60 729 -389 C ATOM 1973 C TYR A 269 20.220 22.625 39.909 1.00 19.72 C ANISOU 1973 C TYR A 269 1759 2703 3031 -51 700 -329 C ATOM 1974 O TYR A 269 19.309 22.537 40.724 1.00 14.96 O ANISOU 1974 O TYR A 269 1193 2113 2380 -36 578 -287 O ATOM 1975 CB TYR A 269 22.384 21.428 40.092 1.00 18.97 C ANISOU 1975 CB TYR A 269 1427 2595 3187 -3 747 -447 C ATOM 1976 CG TYR A 269 23.837 21.471 40.487 1.00 19.99 C ANISOU 1976 CG TYR A 269 1438 2712 3445 -1 730 -492 C ATOM 1977 CD1 TYR A 269 24.752 22.201 39.736 1.00 19.63 C ANISOU 1977 CD1 TYR A 269 1381 2645 3433 -55 852 -519 C ATOM 1978 CD2 TYR A 269 24.298 20.787 41.601 1.00 18.07 C ANISOU 1978 CD2 TYR A 269 1100 2476 3288 57 593 -510 C ATOM 1979 CE1 TYR A 269 26.079 22.254 40.081 1.00 23.11 C ANISOU 1979 CE1 TYR A 269 1702 3074 4003 -58 840 -574 C ATOM 1980 CE2 TYR A 269 25.656 20.817 41.945 1.00 19.32 C ANISOU 1980 CE2 TYR A 269 1148 2627 3564 64 572 -562 C ATOM 1981 CZ TYR A 269 26.526 21.563 41.182 1.00 20.36 C ANISOU 1981 CZ TYR A 269 1255 2741 3741 3 697 -599 C ATOM 1982 OH TYR A 269 27.855 21.625 41.491 1.00 21.75 O ANISOU 1982 OH TYR A 269 1312 2907 4044 4 683 -662 O ATOM 1983 N GLU A 270 20.038 22.630 38.596 1.00 19.22 N ANISOU 1983 N GLU A 270 1792 2628 2882 -58 814 -332 N ATOM 1984 CA GLU A 270 18.717 22.513 37.999 1.00 15.20 C ANISOU 1984 CA GLU A 270 1433 2127 2218 -41 781 -292 C ATOM 1985 C GLU A 270 18.408 21.047 37.862 1.00 19.09 C ANISOU 1985 C GLU A 270 1930 2616 2707 12 728 -324 C ATOM 1986 O GLU A 270 19.264 20.276 37.422 1.00 16.71 O ANISOU 1986 O GLU A 270 1576 2300 2474 34 796 -379 O ATOM 1987 CB GLU A 270 18.735 23.078 36.580 1.00 23.77 C ANISOU 1987 CB GLU A 270 2632 3198 3199 -59 922 -289 C ATOM 1988 CG GLU A 270 19.265 24.480 36.471 1.00 36.44 C ANISOU 1988 CG GLU A 270 4242 4784 4820 -117 1025 -264 C ATOM 1989 CD GLU A 270 18.252 25.494 36.917 1.00 47.43 C ANISOU 1989 CD GLU A 270 5709 6180 6132 -131 947 -197 C ATOM 1990 OE1 GLU A 270 17.304 25.757 36.143 1.00 55.36 O ANISOU 1990 OE1 GLU A 270 6860 7186 6989 -110 945 -160 O ATOM 1991 OE2 GLU A 270 18.399 26.017 38.039 1.00 52.44 O ANISOU 1991 OE2 GLU A 270 6258 6817 6850 -158 883 -188 O ATOM 1992 N ALA A 271 17.185 20.668 38.211 1.00 13.97 N ANISOU 1992 N ALA A 271 1343 1977 1990 30 617 -295 N ATOM 1993 CA ALA A 271 16.688 19.341 37.910 1.00 18.10 C ANISOU 1993 CA ALA A 271 1895 2486 2496 70 579 -328 C ATOM 1994 C ALA A 271 15.754 19.483 36.686 1.00 16.20 C ANISOU 1994 C ALA A 271 1788 2257 2110 71 603 -335 C ATOM 1995 O ALA A 271 15.505 20.590 36.242 1.00 17.14 O ANISOU 1995 O ALA A 271 1975 2391 2145 50 638 -302 O ATOM 1996 CB ALA A 271 15.952 18.801 39.118 1.00 13.19 C ANISOU 1996 CB ALA A 271 1248 1858 1905 83 451 -299 C ATOM 1997 N SER A 272 15.266 18.384 36.122 1.00 18.27 N ANISOU 1997 N SER A 272 2094 2509 2341 100 582 -382 N ATOM 1998 CA SER A 272 14.347 18.468 34.981 1.00 19.07 C ANISOU 1998 CA SER A 272 2320 2626 2300 110 580 -402 C ATOM 1999 C SER A 272 13.138 19.352 35.308 1.00 13.95 C ANISOU 1999 C SER A 272 1719 2003 1577 98 489 -351 C ATOM 2000 O SER A 272 12.435 19.102 36.292 1.00 13.20 O ANISOU 2000 O SER A 272 1576 1906 1532 90 394 -333 O ATOM 2001 CB SER A 272 13.856 17.063 34.599 1.00 18.74 C ANISOU 2001 CB SER A 272 2296 2565 2261 137 540 -471 C ATOM 2002 OG SER A 272 12.861 17.116 33.592 1.00 16.27 O ANISOU 2002 OG SER A 272 2096 2274 1813 150 506 -504 O ATOM 2003 N PRO A 273 12.892 20.395 34.490 1.00 14.31 N ANISOU 2003 N PRO A 273 1865 2068 1503 100 524 -325 N ATOM 2004 CA PRO A 273 11.694 21.215 34.696 1.00 21.31 C ANISOU 2004 CA PRO A 273 2800 2978 2320 103 432 -284 C ATOM 2005 C PRO A 273 10.437 20.403 34.405 1.00 18.53 C ANISOU 2005 C PRO A 273 2476 2640 1926 128 323 -336 C ATOM 2006 O PRO A 273 9.344 20.800 34.777 1.00 17.42 O ANISOU 2006 O PRO A 273 2337 2515 1766 131 229 -320 O ATOM 2007 CB PRO A 273 11.853 22.346 33.665 1.00 21.01 C ANISOU 2007 CB PRO A 273 2885 2944 2154 115 507 -251 C ATOM 2008 CG PRO A 273 12.717 21.795 32.621 1.00 19.11 C ANISOU 2008 CG PRO A 273 2692 2692 1876 127 620 -297 C ATOM 2009 CD PRO A 273 13.662 20.831 33.314 1.00 15.35 C ANISOU 2009 CD PRO A 273 2081 2196 1555 106 655 -334 C ATOM 2010 N ASP A 274 10.606 19.260 33.756 1.00 19.23 N ANISOU 2010 N ASP A 274 2577 2718 2013 144 340 -409 N ATOM 2011 CA ASP A 274 9.472 18.424 33.410 1.00 19.74 C ANISOU 2011 CA ASP A 274 2661 2789 2050 161 242 -478 C ATOM 2012 C ASP A 274 9.382 17.174 34.280 1.00 18.95 C ANISOU 2012 C ASP A 274 2462 2651 2087 139 211 -511 C ATOM 2013 O ASP A 274 8.598 16.278 33.993 1.00 16.49 O ANISOU 2013 O ASP A 274 2153 2329 1782 142 152 -584 O ATOM 2014 CB ASP A 274 9.534 18.056 31.933 1.00 27.03 C ANISOU 2014 CB ASP A 274 3695 3724 2851 199 272 -547 C ATOM 2015 CG ASP A 274 9.308 19.262 31.033 1.00 35.33 C ANISOU 2015 CG ASP A 274 4877 4808 3739 233 280 -510 C ATOM 2016 OD1 ASP A 274 8.274 19.940 31.201 1.00 35.21 O ANISOU 2016 OD1 ASP A 274 4878 4817 3682 248 179 -485 O ATOM 2017 OD2 ASP A 274 10.170 19.545 30.173 1.00 36.60 O ANISOU 2017 OD2 ASP A 274 5126 4964 3817 248 394 -504 O ATOM 2018 N PHE A 275 10.189 17.119 35.334 1.00 16.61 N ANISOU 2018 N PHE A 275 2083 2329 1899 119 250 -462 N ATOM 2019 CA PHE A 275 10.106 16.032 36.306 1.00 13.34 C ANISOU 2019 CA PHE A 275 1593 1870 1606 106 220 -472 C ATOM 2020 C PHE A 275 10.262 14.659 35.658 1.00 15.42 C ANISOU 2020 C PHE A 275 1867 2093 1899 122 242 -557 C ATOM 2021 O PHE A 275 9.647 13.683 36.091 1.00 18.11 O ANISOU 2021 O PHE A 275 2181 2391 2309 110 200 -589 O ATOM 2022 CB PHE A 275 8.778 16.118 37.074 1.00 12.79 C ANISOU 2022 CB PHE A 275 1501 1802 1556 82 130 -457 C ATOM 2023 CG PHE A 275 8.568 17.443 37.741 1.00 12.11 C ANISOU 2023 CG PHE A 275 1405 1749 1445 70 109 -382 C ATOM 2024 CD1 PHE A 275 9.230 17.749 38.915 1.00 11.74 C ANISOU 2024 CD1 PHE A 275 1306 1691 1466 57 126 -317 C ATOM 2025 CD2 PHE A 275 7.751 18.405 37.168 1.00 15.26 C ANISOU 2025 CD2 PHE A 275 1857 2192 1752 79 68 -379 C ATOM 2026 CE1 PHE A 275 9.070 18.979 39.526 1.00 12.73 C ANISOU 2026 CE1 PHE A 275 1426 1843 1569 43 111 -258 C ATOM 2027 CE2 PHE A 275 7.582 19.638 37.778 1.00 16.33 C ANISOU 2027 CE2 PHE A 275 1986 2347 1870 70 55 -312 C ATOM 2028 CZ PHE A 275 8.241 19.926 38.960 1.00 11.02 C ANISOU 2028 CZ PHE A 275 1258 1660 1268 48 81 -254 C ATOM 2029 N THR A 276 11.097 14.582 34.626 1.00 17.70 N ANISOU 2029 N THR A 276 2200 2388 2138 146 320 -596 N ATOM 2030 CA THR A 276 11.283 13.331 33.905 1.00 17.46 C ANISOU 2030 CA THR A 276 2189 2319 2126 165 350 -687 C ATOM 2031 C THR A 276 11.848 12.223 34.792 1.00 24.33 C ANISOU 2031 C THR A 276 2980 3119 3144 170 364 -687 C ATOM 2032 O THR A 276 11.770 11.048 34.440 1.00 27.61 O ANISOU 2032 O THR A 276 3406 3484 3602 181 372 -760 O ATOM 2033 CB THR A 276 12.197 13.508 32.687 1.00 21.31 C ANISOU 2033 CB THR A 276 2741 2823 2532 192 454 -725 C ATOM 2034 OG1 THR A 276 13.460 14.010 33.122 1.00 20.36 O ANISOU 2034 OG1 THR A 276 2561 2700 2474 193 541 -671 O ATOM 2035 CG2 THR A 276 11.591 14.470 31.675 1.00 16.98 C ANISOU 2035 CG2 THR A 276 2305 2333 1813 201 438 -728 C ATOM 2036 N GLU A 277 12.410 12.586 35.941 1.00 22.15 N ANISOU 2036 N GLU A 277 2635 2837 2946 168 363 -607 N ATOM 2037 CA GLU A 277 12.952 11.591 36.868 1.00 30.25 C ANISOU 2037 CA GLU A 277 3598 3794 4100 188 362 -594 C ATOM 2038 C GLU A 277 11.877 10.640 37.410 1.00 27.99 C ANISOU 2038 C GLU A 277 3324 3450 3862 169 302 -607 C ATOM 2039 O GLU A 277 12.183 9.535 37.841 1.00 29.39 O ANISOU 2039 O GLU A 277 3484 3551 4134 191 312 -617 O ATOM 2040 CB GLU A 277 13.668 12.272 38.038 1.00 37.34 C ANISOU 2040 CB GLU A 277 4430 4706 5053 194 349 -508 C ATOM 2041 CG GLU A 277 14.813 13.206 37.641 1.00 42.77 C ANISOU 2041 CG GLU A 277 5083 5439 5727 202 419 -500 C ATOM 2042 CD GLU A 277 14.374 14.654 37.523 1.00 40.09 C ANISOU 2042 CD GLU A 277 4776 5163 5293 164 411 -456 C ATOM 2043 OE1 GLU A 277 15.258 15.544 37.373 1.00 33.04 O ANISOU 2043 OE1 GLU A 277 3854 4298 4402 158 472 -439 O ATOM 2044 OE2 GLU A 277 13.143 14.888 37.569 1.00 29.43 O ANISOU 2044 OE2 GLU A 277 3476 3828 3879 140 348 -443 O ATOM 2045 N TYR A 278 10.623 11.085 37.396 1.00 14.64 N ANISOU 2045 N TYR A 278 1659 1788 2114 129 245 -607 N ATOM 2046 CA TYR A 278 9.507 10.310 37.936 1.00 29.78 C ANISOU 2046 CA TYR A 278 3575 3651 4088 96 201 -624 C ATOM 2047 C TYR A 278 8.701 9.617 36.843 1.00 40.03 C ANISOU 2047 C TYR A 278 4909 4935 5364 80 187 -739 C ATOM 2048 O TYR A 278 7.734 8.910 37.134 1.00 48.82 O ANISOU 2048 O TYR A 278 6014 5997 6539 43 159 -776 O ATOM 2049 CB TYR A 278 8.535 11.230 38.677 1.00 19.55 C ANISOU 2049 CB TYR A 278 2267 2396 2765 59 147 -567 C ATOM 2050 CG TYR A 278 9.121 12.037 39.812 1.00 18.03 C ANISOU 2050 CG TYR A 278 2046 2224 2581 67 146 -463 C ATOM 2051 CD1 TYR A 278 9.916 11.437 40.778 1.00 19.53 C ANISOU 2051 CD1 TYR A 278 2215 2357 2847 93 163 -413 C ATOM 2052 CD2 TYR A 278 8.852 13.400 39.931 1.00 12.52 C ANISOU 2052 CD2 TYR A 278 1346 1598 1813 54 121 -419 C ATOM 2053 CE1 TYR A 278 10.439 12.174 41.829 1.00 18.83 C ANISOU 2053 CE1 TYR A 278 2102 2292 2759 105 146 -330 C ATOM 2054 CE2 TYR A 278 9.384 14.152 40.970 1.00 19.32 C ANISOU 2054 CE2 TYR A 278 2182 2477 2684 58 117 -337 C ATOM 2055 CZ TYR A 278 10.174 13.530 41.915 1.00 18.08 C ANISOU 2055 CZ TYR A 278 2002 2270 2597 83 125 -297 C ATOM 2056 OH TYR A 278 10.706 14.249 42.955 1.00 15.42 O ANISOU 2056 OH TYR A 278 1641 1954 2264 92 106 -229 O ATOM 2057 N SER A 279 9.075 9.839 35.589 1.00 49.64 N ANISOU 2057 N SER A 279 6170 6197 6494 105 208 -799 N ATOM 2058 CA SER A 279 8.192 9.518 34.466 1.00 61.12 C ANISOU 2058 CA SER A 279 7671 7667 7886 95 168 -912 C ATOM 2059 C SER A 279 7.760 8.049 34.392 1.00 63.20 C ANISOU 2059 C SER A 279 7925 7839 8247 75 167 -1005 C ATOM 2060 O SER A 279 8.505 7.148 34.788 1.00 60.75 O ANISOU 2060 O SER A 279 7601 7449 8031 90 226 -997 O ATOM 2061 CB SER A 279 8.820 9.962 33.142 1.00 68.23 C ANISOU 2061 CB SER A 279 8643 8624 8657 135 206 -955 C ATOM 2062 OG SER A 279 7.842 10.015 32.116 1.00 75.06 O ANISOU 2062 OG SER A 279 9566 9529 9423 135 137 -1048 O ATOM 2063 N ALA A 280 6.551 7.828 33.876 1.00 65.44 N ANISOU 2063 N ALA A 280 8217 8133 8515 43 97 -1099 N ATOM 2064 CA ALA A 280 5.982 6.488 33.732 1.00 65.64 C ANISOU 2064 CA ALA A 280 8230 8069 8640 10 94 -1207 C ATOM 2065 C ALA A 280 6.800 5.619 32.780 1.00 67.40 C ANISOU 2065 C ALA A 280 8506 8253 8851 46 150 -1295 C ATOM 2066 O ALA A 280 6.963 4.418 33.008 1.00 68.38 O ANISOU 2066 O ALA A 280 8619 8270 9091 35 194 -1338 O ATOM 2067 CB ALA A 280 4.531 6.572 33.262 1.00 63.61 C ANISOU 2067 CB ALA A 280 7956 7846 8367 -30 -5 -1309 C TER 2068 ALA A 280 HETATM 2069 ZN ZN A 401 11.096 35.175 58.535 1.00 26.49 ZN ANISOU 2069 ZN ZN A 401 3162 3645 3258 -235 -305 -235 ZN HETATM 2070 MG MG A 402 26.649 16.664 49.071 1.00 47.05 MG ANISOU 2070 MG MG A 402 4544 6151 7181 567 -365 -487 MG HETATM 2071 O HOH A 501 13.550 28.510 41.069 1.00 13.23 O HETATM 2072 O HOH A 502 5.896 15.484 39.975 1.00 15.04 O HETATM 2073 O HOH A 503 6.592 34.771 42.300 1.00 16.29 O HETATM 2074 O HOH A 504 -1.688 15.428 57.672 1.00 14.80 O HETATM 2075 O HOH A 505 5.520 43.069 45.200 1.00 13.53 O HETATM 2076 O HOH A 506 8.317 38.379 61.771 1.00 17.86 O HETATM 2077 O HOH A 507 2.014 47.039 63.311 1.00 13.43 O HETATM 2078 O HOH A 508 3.025 20.592 62.924 1.00 16.45 O HETATM 2079 O HOH A 509 18.412 25.358 44.548 1.00 26.06 O HETATM 2080 O HOH A 510 9.895 19.879 54.823 1.00 18.95 O HETATM 2081 O HOH A 511 1.818 11.348 50.816 1.00 15.46 O HETATM 2082 O HOH A 512 6.959 48.308 67.117 1.00 23.02 O HETATM 2083 O HOH A 513 3.620 15.978 41.628 1.00 15.49 O HETATM 2084 O HOH A 514 7.404 36.513 36.195 1.00 23.05 O HETATM 2085 O HOH A 515 -2.374 13.949 55.438 1.00 21.82 O HETATM 2086 O HOH A 516 8.160 30.919 56.756 1.00 22.83 O HETATM 2087 O HOH A 517 -1.917 49.868 58.853 1.00 19.82 O HETATM 2088 O HOH A 518 11.936 19.170 60.639 1.00 28.24 O HETATM 2089 O HOH A 519 12.444 21.776 60.098 1.00 26.13 O HETATM 2090 O HOH A 520 -4.843 21.820 59.198 1.00 24.23 O HETATM 2091 O HOH A 521 13.172 43.378 49.761 1.00 18.90 O HETATM 2092 O HOH A 522 2.639 18.063 61.819 1.00 20.23 O HETATM 2093 O HOH A 523 6.798 9.403 41.375 1.00 23.62 O HETATM 2094 O HOH A 524 12.080 25.593 35.471 1.00 20.69 O HETATM 2095 O HOH A 525 23.897 17.635 42.202 1.00 19.32 O HETATM 2096 O HOH A 526 0.879 24.479 37.717 1.00 26.99 O HETATM 2097 O HOH A 527 14.066 27.520 38.484 1.00 23.19 O HETATM 2098 O HOH A 528 1.529 26.712 39.702 1.00 26.96 O HETATM 2099 O HOH A 529 12.273 33.523 57.321 1.00 35.77 O HETATM 2100 O HOH A 530 -1.092 23.307 59.932 1.00 20.49 O HETATM 2101 O HOH A 531 15.667 30.210 41.942 1.00 25.53 O HETATM 2102 O HOH A 532 28.271 19.398 43.246 1.00 26.85 O HETATM 2103 O HOH A 533 -5.497 32.110 60.759 1.00 26.93 O HETATM 2104 O HOH A 534 -3.528 46.849 46.022 1.00 21.54 O HETATM 2105 O HOH A 535 13.631 6.158 41.601 1.00 25.78 O HETATM 2106 O HOH A 536 -5.519 25.553 53.023 1.00 21.70 O HETATM 2107 O HOH A 537 -4.868 45.280 54.866 1.00 24.42 O HETATM 2108 O HOH A 538 16.027 12.915 40.319 1.00 22.96 O HETATM 2109 O HOH A 539 -5.765 20.920 54.727 1.00 32.47 O HETATM 2110 O HOH A 540 14.739 41.170 48.814 1.00 26.72 O HETATM 2111 O HOH A 541 3.228 23.771 35.636 1.00 30.44 O HETATM 2112 O HOH A 542 7.929 25.093 48.521 1.00 29.00 O HETATM 2113 O HOH A 543 13.936 4.059 43.591 1.00 33.27 O HETATM 2114 O HOH A 544 -6.697 32.680 42.458 1.00 37.90 O HETATM 2115 O HOH A 545 5.411 31.692 59.293 1.00 26.01 O HETATM 2116 O HOH A 546 1.552 21.754 60.638 1.00 28.73 O HETATM 2117 O HOH A 547 -9.198 28.683 53.367 1.00 25.11 O HETATM 2118 O HOH A 548 8.427 31.780 59.679 1.00 39.61 O HETATM 2119 O HOH A 549 -3.338 48.272 47.994 1.00 30.31 O HETATM 2120 O HOH A 550 1.591 9.151 44.566 1.00 28.28 O HETATM 2121 O HOH A 551 12.639 51.265 57.687 1.00 27.08 O HETATM 2122 O HOH A 552 22.298 23.139 36.555 1.00 29.32 O HETATM 2123 O HOH A 553 -4.138 14.375 53.443 1.00 28.87 O HETATM 2124 O HOH A 554 1.109 51.052 47.132 1.00 37.59 O HETATM 2125 O HOH A 555 -7.423 25.711 56.984 1.00 20.18 O HETATM 2126 O HOH A 556 16.688 28.341 38.213 1.00 35.71 O HETATM 2127 O HOH A 557 12.459 17.844 58.042 1.00 30.75 O HETATM 2128 O HOH A 558 3.296 14.183 43.917 1.00 34.38 O HETATM 2129 O HOH A 559 -1.564 15.373 47.821 1.00 26.52 O HETATM 2130 O HOH A 560 -4.297 53.936 54.524 1.00 29.09 O HETATM 2131 O HOH A 561 -5.162 29.893 43.795 1.00 36.02 O HETATM 2132 O HOH A 562 -0.564 18.472 39.020 1.00 30.28 O HETATM 2133 O HOH A 563 1.714 9.967 53.347 1.00 29.00 O HETATM 2134 O HOH A 564 18.037 14.935 40.326 1.00 34.51 O HETATM 2135 O HOH A 565 1.866 28.242 61.537 1.00 28.78 O HETATM 2136 O HOH A 566 15.758 27.603 57.401 1.00 32.72 O HETATM 2137 O HOH A 567 2.064 12.742 57.752 1.00 22.74 O HETATM 2138 O HOH A 568 19.770 17.564 37.082 1.00 27.98 O HETATM 2139 O HOH A 569 -5.968 45.774 46.041 1.00 26.74 O HETATM 2140 O HOH A 570 -9.345 40.597 52.379 1.00 28.82 O HETATM 2141 O HOH A 571 -1.455 39.330 62.765 1.00 25.94 O HETATM 2142 O HOH A 572 2.537 40.296 33.518 1.00 35.99 O HETATM 2143 O HOH A 573 2.376 52.996 48.119 1.00 35.65 O HETATM 2144 O HOH A 574 -5.083 21.145 50.240 1.00 41.54 O HETATM 2145 O HOH A 575 -6.013 30.266 62.822 1.00 40.17 O HETATM 2146 O HOH A 576 -3.707 27.845 68.949 1.00 37.22 O HETATM 2147 O HOH A 577 17.733 24.808 57.754 1.00 38.67 O HETATM 2148 O HOH A 578 11.250 3.086 44.497 1.00 36.08 O HETATM 2149 O HOH A 579 7.527 28.413 58.194 1.00 32.55 O HETATM 2150 O HOH A 580 -2.039 24.401 62.194 1.00 37.40 O HETATM 2151 O HOH A 581 2.508 38.461 69.901 1.00 33.46 O HETATM 2152 O HOH A 582 12.575 18.693 29.921 1.00 47.69 O HETATM 2153 O HOH A 583 -3.528 33.895 61.429 1.00 30.81 O HETATM 2154 O HOH A 584 -6.273 51.906 49.217 1.00 49.53 O HETATM 2155 O HOH A 585 7.010 30.384 32.699 1.00 29.17 O HETATM 2156 O HOH A 586 2.273 28.257 37.401 1.00 33.97 O HETATM 2157 O HOH A 587 -10.252 40.314 48.766 1.00 37.94 O HETATM 2158 O HOH A 588 27.016 16.693 45.818 1.00 31.21 O HETATM 2159 O HOH A 589 9.456 22.351 30.081 1.00 38.16 O HETATM 2160 O HOH A 590 17.323 21.585 33.940 1.00 32.86 O HETATM 2161 O HOH A 591 -5.688 22.659 52.956 1.00 31.74 O HETATM 2162 O HOH A 592 11.916 30.771 58.174 1.00 38.41 O HETATM 2163 O HOH A 593 13.959 34.670 55.206 1.00 31.16 O HETATM 2164 O HOH A 594 -9.301 24.461 54.081 1.00 43.51 O HETATM 2165 O HOH A 595 11.662 25.140 63.944 1.00 44.23 O HETATM 2166 O HOH A 596 1.394 27.471 34.552 1.00 38.62 O HETATM 2167 O HOH A 597 9.611 27.217 47.672 1.00 31.38 O HETATM 2168 O HOH A 598 16.127 41.345 62.614 1.00 42.09 O HETATM 2169 O HOH A 599 -7.649 26.067 54.485 1.00 33.83 O HETATM 2170 O HOH A 600 -5.961 28.689 49.888 1.00 27.82 O HETATM 2171 O HOH A 601 3.860 40.216 68.182 1.00 31.21 O HETATM 2172 O HOH A 602 -3.132 47.573 59.267 1.00 27.31 O HETATM 2173 O HOH A 603 -4.244 31.439 64.980 1.00 36.71 O HETATM 2174 O HOH A 604 23.601 17.529 40.301 1.00 34.61 O HETATM 2175 O HOH A 605 11.620 43.431 41.786 1.00 28.70 O HETATM 2176 O HOH A 606 10.968 23.787 70.590 1.00 29.13 O HETATM 2177 O HOH A 607 -2.563 56.993 53.882 1.00 43.66 O HETATM 2178 O HOH A 608 -2.867 12.081 51.301 1.00 41.43 O HETATM 2179 O HOH A 609 3.883 30.599 62.181 1.00 45.86 O HETATM 2180 O HOH A 610 21.640 20.484 36.428 1.00 44.32 O HETATM 2181 O HOH A 611 10.372 25.829 33.421 1.00 33.75 O HETATM 2182 O HOH A 612 15.196 52.534 45.889 1.00 53.91 O HETATM 2183 O HOH A 613 13.751 41.715 41.808 1.00 36.81 O HETATM 2184 O HOH A 614 0.626 9.522 49.276 1.00 31.03 O HETATM 2185 O HOH A 615 1.045 30.341 63.312 1.00 30.29 O HETATM 2186 O HOH A 616 1.325 33.937 32.737 1.00 31.60 O HETATM 2187 O HOH A 617 11.041 26.172 59.226 1.00 41.67 O HETATM 2188 O HOH A 618 -0.980 27.995 35.910 1.00 45.94 O HETATM 2189 O HOH A 619 -5.287 46.701 57.228 1.00 35.51 O HETATM 2190 O HOH A 620 9.438 42.620 66.473 1.00 40.24 O HETATM 2191 O HOH A 621 14.593 40.451 39.547 1.00 47.81 O HETATM 2192 O HOH A 622 -5.401 54.984 50.904 1.00 43.13 O HETATM 2193 O HOH A 623 -6.683 22.806 57.123 1.00 32.38 O HETATM 2194 O HOH A 624 8.166 53.247 52.473 1.00 42.18 O HETATM 2195 O HOH A 625 28.636 15.117 49.588 1.00 22.87 O HETATM 2196 O HOH A 626 26.588 18.701 50.608 1.00 37.26 O HETATM 2197 O HOH A 627 29.053 17.107 51.409 1.00 35.77 O HETATM 2198 O HOH A 628 28.885 17.945 48.913 1.00 42.70 O HETATM 2199 O HOH A 629 26.651 16.133 51.742 1.00 25.52 O HETATM 2200 O HOH A 630 8.627 46.948 40.761 1.00 38.52 O HETATM 2201 O HOH A 631 30.161 4.953 63.365 1.00 34.21 O HETATM 2202 O HOH A 632 27.979 13.120 47.608 1.00 31.07 O HETATM 2203 O HOH A 633 17.984 7.324 47.799 1.00 29.08 O HETATM 2204 O HOH A 634 15.316 48.864 44.706 1.00 43.58 O HETATM 2205 O HOH A 635 9.664 47.777 43.164 1.00 55.73 O HETATM 2206 O HOH A 636 -4.782 27.525 47.843 1.00 37.46 O HETATM 2207 O HOH A 637 10.563 40.210 37.231 1.00 38.09 O HETATM 2208 O HOH A 638 22.870 18.858 37.581 1.00 36.49 O HETATM 2209 O HOH A 639 -0.449 11.507 58.036 1.00 33.20 O HETATM 2210 O HOH A 640 -1.238 25.456 36.513 1.00 37.38 O HETATM 2211 O HOH A 641 23.430 16.781 48.802 1.00 33.30 O HETATM 2212 O HOH A 642 23.760 16.385 50.804 1.00 33.08 O HETATM 2213 O HOH A 643 14.174 36.534 64.579 1.00 35.61 O HETATM 2214 O HOH A 644 21.462 31.032 44.824 1.00 36.18 O HETATM 2215 O HOH A 645 16.797 43.390 60.495 1.00 38.74 O HETATM 2216 O HOH A 646 12.893 35.589 67.205 1.00 38.78 O HETATM 2217 O HOH A 647 10.204 28.660 59.301 1.00 33.91 O HETATM 2218 O HOH A 648 4.755 30.325 31.313 1.00 43.72 O HETATM 2219 O HOH A 649 -2.302 41.785 63.238 1.00 48.64 O HETATM 2220 O HOH A 650 -6.400 48.928 48.905 1.00 39.50 O HETATM 2221 O HOH A 651 -2.091 24.483 48.515 1.00 47.59 O HETATM 2222 O HOH A 652 14.859 49.561 58.923 1.00 38.62 O HETATM 2223 O HOH A 653 12.579 25.944 71.324 1.00 43.32 O HETATM 2224 O HOH A 654 25.727 33.324 46.042 1.00 47.16 O HETATM 2225 O HOH A 655 -6.215 39.671 59.546 1.00 46.37 O HETATM 2226 O HOH A 656 10.814 30.484 61.942 1.00 38.10 O HETATM 2227 O HOH A 657 -3.942 23.882 64.543 1.00 41.67 O HETATM 2228 O HOH A 658 -4.274 52.814 41.576 1.00 45.71 O HETATM 2229 O HOH A 659 0.401 7.440 42.836 1.00 42.22 O HETATM 2230 O HOH A 660 -7.916 46.902 56.792 1.00 41.88 O HETATM 2231 O HOH A 661 -7.726 18.801 56.175 1.00 39.59 O HETATM 2232 O HOH A 662 21.660 13.836 58.570 1.00 41.28 O HETATM 2233 O HOH A 663 13.882 49.738 42.725 1.00 47.27 O HETATM 2234 O HOH A 664 16.947 23.527 33.409 1.00 46.38 O HETATM 2235 O HOH A 665 -2.158 12.632 48.868 1.00 51.19 O HETATM 2236 O HOH A 666 1.949 6.918 46.963 1.00 44.45 O HETATM 2237 O HOH A 667 -0.904 37.316 64.880 1.00 43.48 O HETATM 2238 O HOH A 668 20.712 35.964 49.969 1.00 48.59 O HETATM 2239 O HOH A 669 2.146 29.059 32.574 1.00 47.22 O HETATM 2240 O HOH A 670 11.442 44.649 39.279 1.00 45.06 O HETATM 2241 O HOH A 671 22.321 29.754 41.999 1.00 27.83 O HETATM 2242 O HOH A 672 11.709 31.351 65.267 1.00 40.93 O HETATM 2243 O HOH A 673 4.255 38.182 32.528 1.00 42.24 O HETATM 2244 O HOH A 674 9.361 51.140 43.571 1.00 44.68 O HETATM 2245 O HOH A 675 -4.099 38.541 62.145 1.00 43.72 O HETATM 2246 O HOH A 676 11.039 43.572 71.344 1.00 48.07 O HETATM 2247 O HOH A 677 20.831 5.501 52.818 1.00 44.06 O HETATM 2248 O HOH A 678 7.462 12.499 34.818 1.00 49.57 O HETATM 2249 O HOH A 679 28.731 20.412 45.320 1.00 39.68 O HETATM 2250 O HOH A 680 16.599 19.524 31.747 1.00 42.35 O HETATM 2251 O HOH A 681 -9.826 40.041 43.493 1.00 42.78 O HETATM 2252 O HOH A 682 16.406 31.417 66.772 1.00 46.29 O HETATM 2253 O HOH A 683 20.624 20.314 64.451 1.00 55.02 O HETATM 2254 O HOH A 684 23.041 24.802 54.623 1.00 47.14 O HETATM 2255 O HOH A 685 20.150 30.827 40.258 1.00 51.44 O HETATM 2256 O HOH A 686 15.237 12.091 33.499 1.00 45.65 O CONECT 1289 2069 CONECT 1324 2069 CONECT 1371 2069 CONECT 1372 2069 CONECT 1626 2069 CONECT 2069 1289 1324 1371 1372 CONECT 2069 1626 2099 CONECT 2070 2195 2196 2198 2199 CONECT 2099 2069 CONECT 2195 2070 CONECT 2196 2070 CONECT 2198 2070 CONECT 2199 2070 MASTER 380 0 2 13 5 0 3 6 2255 1 13 26 END If you find results from this site helpful for your research, please cite one of our papers:
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