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Diffstat (limited to 'plip/test/pdb/4qnb.pdb')
| -rw-r--r-- | plip/test/pdb/4qnb.pdb | 4070 |
1 files changed, 0 insertions, 4070 deletions
diff --git a/plip/test/pdb/4qnb.pdb b/plip/test/pdb/4qnb.pdb deleted file mode 100644 index 54c5363..0000000 --- a/plip/test/pdb/4qnb.pdb +++ /dev/null @@ -1,4070 +0,0 @@ -HEADER VIRAL PROTEIN/INHIBITOR 17-JUN-14 4QNB -TITLE DISULFIDE STABILIZED HIV-1 CA HEXAMER IN COMPLEX WITH PHENYL-L- -TITLE 2 PHENYLALANINAMIDE INHIBITOR -COMPND MOL_ID: 1; -COMPND 2 MOLECULE: CAPSID PROTEIN P24; -COMPND 3 CHAIN: A; -COMPND 4 ENGINEERED: YES; -COMPND 5 MUTATION: YES -SOURCE MOL_ID: 1; -SOURCE 2 ORGANISM_SCIENTIFIC: HUMAN IMMUNODEFICIENCY VIRUS TYPE 1 (NEW YORK-5 -SOURCE 3 ISOLATE); -SOURCE 4 ORGANISM_COMMON: HIV-1; -SOURCE 5 ORGANISM_TAXID: 11698; -SOURCE 6 GENE: GAG-POL; -SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI; -SOURCE 8 EXPRESSION_SYSTEM_TAXID: 562; -SOURCE 9 EXPRESSION_SYSTEM_STRAIN: BL21(DE3); -SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; -SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PET11A -KEYWDS CAPSID PROTEIN, DISULFIDE CROSSLINK, VIRAL PROTEIN, VIRAL PROTEIN- -KEYWDS 2 INHIBITOR COMPLEX -EXPDTA X-RAY DIFFRACTION -AUTHOR O.PORNILLOS -REVDAT 1 31-DEC-14 4QNB 0 -JRNL AUTH A.BHATTACHARYA,S.L.ALAM,T.FRICKE,K.ZADROZNY,J.SEDZICKI, -JRNL AUTH 2 A.B.TAYLOR,B.DEMELER,O.PORNILLOS,B.K.GANSER-PORNILLOS, -JRNL AUTH 3 F.DIAZ-GRIFFERO,D.N.IVANOV,M.YEAGER -JRNL TITL STRUCTURAL BASIS OF HIV-1 CAPSID RECOGNITION BY PF74 AND -JRNL TITL 2 CPSF6. -JRNL REF PROC.NATL.ACAD.SCI.USA 2014 -JRNL REFN ESSN 1091-6490 -JRNL PMID 25518861 -JRNL DOI 10.1073/PNAS.1419945112 -REMARK 2 -REMARK 2 RESOLUTION. 2.00 ANGSTROMS. -REMARK 3 -REMARK 3 REFINEMENT. -REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.9_1692) -REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN -REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE- -REMARK 3 : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO, -REMARK 3 : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL -REMARK 3 : MORIARTY,REETAL PAI,RANDY READ,JANE -REMARK 3 : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM -REMARK 3 : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH, -REMARK 3 : LAURENT STORONI,TOM TERWILLIGER,PETER -REMARK 3 : ZWART -REMARK 3 -REMARK 3 REFINEMENT TARGET : ML -REMARK 3 -REMARK 3 DATA USED IN REFINEMENT. -REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00 -REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 26.64 -REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340 -REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8 -REMARK 3 NUMBER OF REFLECTIONS : 18417 -REMARK 3 -REMARK 3 FIT TO DATA USED IN REFINEMENT. -REMARK 3 R VALUE (WORKING + TEST SET) : 0.223 -REMARK 3 R VALUE (WORKING SET) : 0.220 -REMARK 3 FREE R VALUE : 0.271 -REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.870 -REMARK 3 FREE R VALUE TEST SET COUNT : 897 -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 26.6444 - 3.6252 1.00 2983 154 0.2212 0.2564 -REMARK 3 2 3.6252 - 2.8785 1.00 2922 152 0.2313 0.2818 -REMARK 3 3 2.8785 - 2.5150 1.00 2933 130 0.2210 0.2823 -REMARK 3 4 2.5150 - 2.2851 1.00 2885 160 0.2140 0.2942 -REMARK 3 5 2.2851 - 2.1214 1.00 2922 140 0.2019 0.2633 -REMARK 3 6 2.1214 - 1.9964 1.00 2875 161 0.2074 0.2649 -REMARK 3 -REMARK 3 BULK SOLVENT MODELLING. -REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL -REMARK 3 SOLVENT RADIUS : 1.11 -REMARK 3 SHRINKAGE RADIUS : 0.90 -REMARK 3 K_SOL : NULL -REMARK 3 B_SOL : NULL -REMARK 3 -REMARK 3 ERROR ESTIMATES. -REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.220 -REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.530 -REMARK 3 -REMARK 3 B VALUES. -REMARK 3 FROM WILSON PLOT (A**2) : 28.00 -REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL -REMARK 3 OVERALL ANISOTROPIC B VALUE. -REMARK 3 B11 (A**2) : NULL -REMARK 3 B22 (A**2) : NULL -REMARK 3 B33 (A**2) : NULL -REMARK 3 B12 (A**2) : NULL -REMARK 3 B13 (A**2) : NULL -REMARK 3 B23 (A**2) : NULL -REMARK 3 -REMARK 3 TWINNING INFORMATION. -REMARK 3 FRACTION: NULL -REMARK 3 OPERATOR: NULL -REMARK 3 -REMARK 3 DEVIATIONS FROM IDEAL VALUES. -REMARK 3 RMSD COUNT -REMARK 3 BOND : 0.008 1734 -REMARK 3 ANGLE : 0.997 2356 -REMARK 3 CHIRALITY : 0.040 262 -REMARK 3 PLANARITY : 0.005 306 -REMARK 3 DIHEDRAL : 14.198 647 -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): 24.8716 10.3507 -0.7647 -REMARK 3 T TENSOR -REMARK 3 T11: 0.1573 T22: 0.1716 -REMARK 3 T33: 0.1686 T12: -0.0086 -REMARK 3 T13: 0.0037 T23: -0.0232 -REMARK 3 L TENSOR -REMARK 3 L11: 0.7925 L22: 1.0844 -REMARK 3 L33: 1.4389 L12: -0.3571 -REMARK 3 L13: 0.5725 L23: -0.6160 -REMARK 3 S TENSOR -REMARK 3 S11: 0.0229 S12: 0.1284 S13: 0.0101 -REMARK 3 S21: -0.0656 S22: -0.0921 S23: -0.0280 -REMARK 3 S31: -0.0118 S32: 0.1688 S33: 0.0598 -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 4QNB COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 -REMARK 100 -REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-JUL-14. -REMARK 100 THE RCSB ID CODE IS RCSB086270. -REMARK 200 -REMARK 200 EXPERIMENTAL DETAILS -REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION -REMARK 200 DATE OF DATA COLLECTION : 11-JAN-11 -REMARK 200 TEMPERATURE (KELVIN) : 100 -REMARK 200 PH : 8 -REMARK 200 NUMBER OF CRYSTALS USED : NULL -REMARK 200 -REMARK 200 SYNCHROTRON (Y/N) : Y -REMARK 200 RADIATION SOURCE : APS -REMARK 200 BEAMLINE : 22-BM -REMARK 200 X-RAY GENERATOR MODEL : NULL -REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M -REMARK 200 WAVELENGTH OR RANGE (A) : 1 -REMARK 200 MONOCHROMATOR : NULL -REMARK 200 OPTICS : NULL -REMARK 200 -REMARK 200 DETECTOR TYPE : CCD -REMARK 200 DETECTOR MANUFACTURER : MAR SCANNER 345 MM PLATE -REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000 -REMARK 200 DATA SCALING SOFTWARE : HKL-2000 -REMARK 200 -REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 18424 -REMARK 200 RESOLUTION RANGE HIGH (A) : 1.996 -REMARK 200 RESOLUTION RANGE LOW (A) : 50.000 -REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000 -REMARK 200 -REMARK 200 OVERALL. -REMARK 200 COMPLETENESS FOR RANGE (%) : NULL -REMARK 200 DATA REDUNDANCY : 11.100 -REMARK 200 R MERGE (I) : NULL -REMARK 200 R SYM (I) : 0.08700 -REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 43.9000 -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 <I/SIGMA(I)> FOR SHELL : NULL -REMARK 200 -REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH -REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT -REMARK 200 SOFTWARE USED: MOLREP -REMARK 200 STARTING MODEL: 3H47 -REMARK 200 -REMARK 200 REMARK: NULL -REMARK 280 -REMARK 280 CRYSTAL -REMARK 280 SOLVENT CONTENT, VS (%): 54.08 -REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.68 -REMARK 280 -REMARK 280 CRYSTALLIZATION CONDITIONS: 10% PEG 8,000, 2% TACSIMATE, 100 MM -REMARK 280 TRIS, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K -REMARK 290 -REMARK 290 CRYSTALLOGRAPHIC SYMMETRY -REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 6 -REMARK 290 -REMARK 290 SYMOP SYMMETRY -REMARK 290 NNNMMM OPERATOR -REMARK 290 1555 X,Y,Z -REMARK 290 2555 -Y,X-Y,Z -REMARK 290 3555 -X+Y,-X,Z -REMARK 290 4555 -X,-Y,Z -REMARK 290 5555 Y,-X+Y,Z -REMARK 290 6555 X-Y,X,Z -REMARK 290 -REMARK 290 WHERE NNN -> OPERATOR NUMBER -REMARK 290 MMM -> TRANSLATION VECTOR -REMARK 290 -REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS -REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM -REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY -REMARK 290 RELATED MOLECULES. -REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 -REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 -REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 -REMARK 290 SMTRY1 2 -0.500000 -0.866025 0.000000 0.00000 -REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000 -REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000 -REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000 -REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000 -REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000 -REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000 -REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000 -REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 0.00000 -REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000 -REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000 -REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000 -REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000 -REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000 -REMARK 290 SMTRY3 6 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: HEXAMERIC -REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC -REMARK 350 SOFTWARE USED: PISA -REMARK 350 TOTAL BURIED SURFACE AREA: 14990 ANGSTROM**2 -REMARK 350 SURFACE AREA OF THE COMPLEX: 61050 ANGSTROM**2 -REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -98.0 KCAL/MOL -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 350 BIOMT1 2 -0.500000 -0.866025 0.000000 0.00000 -REMARK 350 BIOMT2 2 0.866025 -0.500000 0.000000 0.00000 -REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000 -REMARK 350 BIOMT1 3 -0.500000 0.866025 0.000000 0.00000 -REMARK 350 BIOMT2 3 -0.866025 -0.500000 0.000000 0.00000 -REMARK 350 BIOMT3 3 0.000000 0.000000 1.000000 0.00000 -REMARK 350 BIOMT1 4 -1.000000 0.000000 0.000000 0.00000 -REMARK 350 BIOMT2 4 0.000000 -1.000000 0.000000 0.00000 -REMARK 350 BIOMT3 4 0.000000 0.000000 1.000000 0.00000 -REMARK 350 BIOMT1 5 0.500000 0.866025 0.000000 0.00000 -REMARK 350 BIOMT2 5 -0.866025 0.500000 0.000000 0.00000 -REMARK 350 BIOMT3 5 0.000000 0.000000 1.000000 0.00000 -REMARK 350 BIOMT1 6 0.500000 -0.866025 0.000000 0.00000 -REMARK 350 BIOMT2 6 0.866025 0.500000 0.000000 0.00000 -REMARK 350 BIOMT3 6 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 LYS A 182 -REMARK 465 ASN A 183 -REMARK 465 ALA A 184 -REMARK 465 ALA A 185 -REMARK 465 GLY A 220 -REMARK 465 VAL A 221 -REMARK 465 GLY A 222 -REMARK 465 GLY A 223 -REMARK 465 PRO A 224 -REMARK 465 GLY A 225 -REMARK 465 HIS A 226 -REMARK 465 LYS A 227 -REMARK 465 ALA A 228 -REMARK 465 ARG A 229 -REMARK 465 VAL A 230 -REMARK 465 LEU A 231 -REMARK 470 -REMARK 470 MISSING ATOM -REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; -REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; -REMARK 470 I=INSERTION CODE): -REMARK 470 M RES CSSEQI ATOMS -REMARK 470 GLN A 4 CG CD OE1 NE2 -REMARK 470 LEU A 6 CG CD1 CD2 -REMARK 470 GLN A 7 CG CD OE1 NE2 -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 NH1 ARG A 100 O HOH A 450 2.16 -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 ASN A 5 -157.95 -97.04 -REMARK 500 ALA A 31 -132.83 55.82 -REMARK 500 -REMARK 500 REMARK: NULL -REMARK 800 -REMARK 800 SITE -REMARK 800 SITE_IDENTIFIER: AC1 -REMARK 800 EVIDENCE_CODE: SOFTWARE -REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1B0 A 301 -REMARK 900 -REMARK 900 RELATED ENTRIES -REMARK 900 RELATED ID: 3H47 RELATED DB: PDB -DBREF 4QNB A 1 231 UNP P12497 POL_HV1N5 133 363 -SEQADV 4QNB CYS A 14 UNP P12497 ALA 146 ENGINEERED MUTATION -SEQADV 4QNB CYS A 45 UNP P12497 GLU 177 ENGINEERED MUTATION -SEQADV 4QNB ALA A 184 UNP P12497 TRP 316 ENGINEERED MUTATION -SEQADV 4QNB ALA A 185 UNP P12497 MET 317 ENGINEERED MUTATION -SEQRES 1 A 231 PRO ILE VAL GLN ASN LEU GLN GLY GLN MET VAL HIS GLN -SEQRES 2 A 231 CYS ILE SER PRO ARG THR LEU ASN ALA TRP VAL LYS VAL -SEQRES 3 A 231 VAL GLU GLU LYS ALA PHE SER PRO GLU VAL ILE PRO MET -SEQRES 4 A 231 PHE SER ALA LEU SER CYS GLY ALA THR PRO GLN ASP LEU -SEQRES 5 A 231 ASN THR MET LEU ASN THR VAL GLY GLY HIS GLN ALA ALA -SEQRES 6 A 231 MET GLN MET LEU LYS GLU THR ILE ASN GLU GLU ALA ALA -SEQRES 7 A 231 GLU TRP ASP ARG LEU HIS PRO VAL HIS ALA GLY PRO ILE -SEQRES 8 A 231 ALA PRO GLY GLN MET ARG GLU PRO ARG GLY SER ASP ILE -SEQRES 9 A 231 ALA GLY THR THR SER THR LEU GLN GLU GLN ILE GLY TRP -SEQRES 10 A 231 MET THR HIS ASN PRO PRO ILE PRO VAL GLY GLU ILE TYR -SEQRES 11 A 231 LYS ARG TRP ILE ILE LEU GLY LEU ASN LYS ILE VAL ARG -SEQRES 12 A 231 MET TYR SER PRO THR SER ILE LEU ASP ILE ARG GLN GLY -SEQRES 13 A 231 PRO LYS GLU PRO PHE ARG ASP TYR VAL ASP ARG PHE TYR -SEQRES 14 A 231 LYS THR LEU ARG ALA GLU GLN ALA SER GLN GLU VAL LYS -SEQRES 15 A 231 ASN ALA ALA THR GLU THR LEU LEU VAL GLN ASN ALA ASN -SEQRES 16 A 231 PRO ASP CYS LYS THR ILE LEU LYS ALA LEU GLY PRO GLY -SEQRES 17 A 231 ALA THR LEU GLU GLU MET MET THR ALA CYS GLN GLY VAL -SEQRES 18 A 231 GLY GLY PRO GLY HIS LYS ALA ARG VAL LEU -HET 1B0 A 301 59 -HETNAM 1B0 N-METHYL-NALPHA-[(2-METHYL-1H-INDOL-3-YL)ACETYL]-N- -HETNAM 2 1B0 PHENYL-L-PHENYLALANINAMIDE -FORMUL 2 1B0 C27 H27 N3 O2 -FORMUL 3 HOH *100(H2 O) -HELIX 1 1 SER A 16 ALA A 31 1 16 -HELIX 2 2 GLU A 35 SER A 44 1 10 -HELIX 3 3 THR A 48 THR A 58 1 11 -HELIX 4 4 HIS A 62 HIS A 84 1 23 -HELIX 5 5 ARG A 100 ALA A 105 1 6 -HELIX 6 6 THR A 110 HIS A 120 1 11 -HELIX 7 7 PRO A 125 SER A 146 1 22 -HELIX 8 8 SER A 149 ILE A 153 5 5 -HELIX 9 9 PRO A 160 GLN A 176 1 17 -HELIX 10 10 GLU A 187 ASN A 193 1 7 -HELIX 11 11 ASN A 195 ALA A 204 1 10 -HELIX 12 12 THR A 210 CYS A 218 1 9 -SHEET 1 A 2 ILE A 2 GLN A 4 0 -SHEET 2 A 2 MET A 10 HIS A 12 -1 O VAL A 11 N VAL A 3 -SSBOND 1 CYS A 14 CYS A 45 1555 6555 2.06 -CISPEP 1 GLN A 7 GLY A 8 0 -3.47 -CISPEP 2 ASN A 121 PRO A 122 0 -1.06 -SITE 1 AC1 11 ASN A 53 LEU A 56 ASN A 57 GLN A 63 -SITE 2 AC1 11 MET A 66 LYS A 70 THR A 107 TYR A 130 -SITE 3 AC1 11 ARG A 173 SER A 178 GLU A 180 -CRYST1 91.383 91.383 56.587 90.00 90.00 120.00 P 6 6 -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 0.010943 0.006318 0.000000 0.00000 -SCALE2 0.000000 0.012636 0.000000 0.00000 -SCALE3 0.000000 0.000000 0.017672 0.00000 -ATOM 1 N PRO A 1 9.981 12.464 -12.296 1.00 29.41 N -ANISOU 1 N PRO A 1 3777 3613 3786 32 -584 -351 N -ATOM 2 CA PRO A 1 11.174 11.956 -12.979 1.00 28.03 C -ANISOU 2 CA PRO A 1 3679 3445 3525 51 -568 -381 C -ATOM 3 C PRO A 1 10.958 11.828 -14.477 1.00 28.46 C -ANISOU 3 C PRO A 1 3802 3502 3509 76 -641 -398 C -ATOM 4 O PRO A 1 9.854 12.075 -14.963 1.00 29.85 O -ANISOU 4 O PRO A 1 3963 3669 3711 70 -714 -386 O -ATOM 5 CB PRO A 1 11.397 10.578 -12.327 1.00 30.38 C -ANISOU 5 CB PRO A 1 3973 3718 3851 29 -569 -414 C -ATOM 6 CG PRO A 1 10.239 10.377 -11.355 1.00 31.90 C -ANISOU 6 CG PRO A 1 4082 3894 4146 -11 -590 -392 C -ATOM 7 CD PRO A 1 9.716 11.732 -11.045 1.00 28.75 C -ANISOU 7 CD PRO A 1 3632 3516 3775 1 -561 -351 C -ATOM 8 N ILE A 2 12.012 11.461 -15.192 1.00 26.97 N -ANISOU 8 N ILE A 2 3688 3332 3229 111 -619 -422 N -ATOM 9 CA ILE A 2 11.908 11.127 -16.612 1.00 28.30 C -ANISOU 9 CA ILE A 2 3939 3503 3311 147 -688 -448 C -ATOM 10 C ILE A 2 11.986 9.616 -16.754 1.00 30.65 C -ANISOU 10 C ILE A 2 4290 3763 3591 154 -738 -508 C -ATOM 11 O ILE A 2 12.921 8.993 -16.253 1.00 31.92 O -ANISOU 11 O ILE A 2 4463 3927 3738 169 -681 -528 O -ATOM 12 CB ILE A 2 13.031 11.797 -17.451 1.00 32.25 C -ANISOU 12 CB ILE A 2 4494 4058 3700 196 -627 -427 C -ATOM 13 CG1 ILE A 2 13.160 13.269 -17.085 1.00 32.10 C -ANISOU 13 CG1 ILE A 2 4424 4062 3708 178 -571 -363 C -ATOM 14 CG2 ILE A 2 12.779 11.634 -18.973 1.00 28.39 C -ANISOU 14 CG2 ILE A 2 4097 3579 3112 242 -698 -448 C -ATOM 15 CD1 ILE A 2 12.125 14.136 -17.728 1.00 35.70 C -ANISOU 15 CD1 ILE A 2 4881 4510 4173 176 -635 -336 C -ATOM 16 N VAL A 3 10.984 9.037 -17.405 1.00 35.39 N -ANISOU 16 N VAL A 3 4924 4323 4198 142 -854 -534 N -ATOM 17 CA VAL A 3 10.951 7.608 -17.725 1.00 42.60 C -ANISOU 17 CA VAL A 3 5915 5183 5088 148 -933 -595 C -ATOM 18 C VAL A 3 10.570 7.429 -19.192 1.00 43.61 C -ANISOU 18 C VAL A 3 6146 5298 5125 185 -1035 -628 C -ATOM 19 O VAL A 3 10.121 8.369 -19.831 1.00 41.54 O -ANISOU 19 O VAL A 3 5875 5066 4841 191 -1054 -596 O -ATOM 20 CB VAL A 3 9.942 6.844 -16.856 1.00 45.25 C -ANISOU 20 CB VAL A 3 6186 5460 5546 71 -1002 -591 C -ATOM 21 CG1 VAL A 3 10.278 7.007 -15.389 1.00 47.43 C -ANISOU 21 CG1 VAL A 3 6367 5751 5902 40 -901 -558 C -ATOM 22 CG2 VAL A 3 8.544 7.346 -17.135 1.00 46.40 C -ANISOU 22 CG2 VAL A 3 6274 5600 5754 26 -1090 -554 C -ATOM 23 N GLN A 4 10.741 6.224 -19.724 1.00 48.04 N -ANISOU 23 N GLN A 4 6815 5810 5629 215 -1108 -693 N -ATOM 24 CA GLN A 4 10.354 5.948 -21.108 1.00 51.42 C -ANISOU 24 CA GLN A 4 7360 6216 5961 254 -1221 -734 C -ATOM 25 C GLN A 4 8.932 5.398 -21.174 1.00 52.82 C -ANISOU 25 C GLN A 4 7526 6319 6226 176 -1381 -740 C -ATOM 26 O GLN A 4 8.527 4.629 -20.310 1.00 52.70 O -ANISOU 26 O GLN A 4 7462 6248 6311 110 -1418 -739 O -ATOM 27 CB GLN A 4 11.332 4.963 -21.757 1.00 52.77 C -ANISOU 27 CB GLN A 4 7674 6370 6004 346 -1221 -808 C -ATOM 28 N ASN A 5 8.167 5.807 -22.182 1.00 56.10 N -ANISOU 28 N ASN A 5 7977 6735 6604 177 -1479 -735 N -ATOM 29 CA ASN A 5 6.830 5.245 -22.375 1.00 58.00 C -ANISOU 29 CA ASN A 5 8208 6906 6921 101 -1649 -736 C -ATOM 30 C ASN A 5 6.870 4.125 -23.415 1.00 61.76 C -ANISOU 30 C ASN A 5 8860 7308 7297 137 -1786 -819 C -ATOM 31 O ASN A 5 7.924 3.539 -23.655 1.00 62.75 O -ANISOU 31 O ASN A 5 9098 7425 7319 217 -1737 -879 O -ATOM 32 CB ASN A 5 5.812 6.333 -22.759 1.00 56.00 C -ANISOU 32 CB ASN A 5 7877 6693 6707 72 -1694 -674 C -ATOM 33 CG ASN A 5 6.123 7.020 -24.088 1.00 56.66 C -ANISOU 33 CG ASN A 5 8062 6818 6647 152 -1702 -688 C -ATOM 34 OD1 ASN A 5 6.816 6.481 -24.952 1.00 58.92 O -ANISOU 34 OD1 ASN A 5 8498 7092 6798 225 -1722 -752 O -ATOM 35 ND2 ASN A 5 5.585 8.221 -24.257 1.00 54.48 N -ANISOU 35 ND2 ASN A 5 7711 6593 6397 146 -1688 -626 N -ATOM 36 N LEU A 6 5.730 3.826 -24.026 1.00 65.26 N -ANISOU 36 N LEU A 6 9312 7703 7780 85 -1925 -804 N -ATOM 37 CA LEU A 6 5.644 2.687 -24.938 1.00 67.95 C -ANISOU 37 CA LEU A 6 9787 7965 8066 112 -2006 -847 C -ATOM 38 C LEU A 6 5.923 3.078 -26.385 1.00 69.77 C -ANISOU 38 C LEU A 6 10142 8225 8144 208 -2017 -877 C -ATOM 39 O LEU A 6 5.887 2.234 -27.278 1.00 71.49 O -ANISOU 39 O LEU A 6 10484 8381 8298 247 -2086 -916 O -ATOM 40 CB LEU A 6 4.267 2.026 -24.837 1.00 69.61 C -ANISOU 40 CB LEU A 6 9941 8100 8406 1 -2145 -805 C -ATOM 41 N GLN A 7 6.195 4.359 -26.611 1.00 70.28 N -ANISOU 41 N GLN A 7 10174 8381 8147 247 -1952 -852 N -ATOM 42 CA GLN A 7 6.509 4.856 -27.951 1.00 73.21 C -ANISOU 42 CA GLN A 7 10654 8795 8367 339 -1946 -867 C -ATOM 43 C GLN A 7 7.783 4.260 -28.584 1.00 74.73 C -ANISOU 43 C GLN A 7 10989 8998 8407 462 -1866 -927 C -ATOM 44 O GLN A 7 7.825 4.099 -29.807 1.00 76.59 O -ANISOU 44 O GLN A 7 11340 9229 8532 531 -1901 -951 O -ATOM 45 CB GLN A 7 6.620 6.385 -27.932 1.00 73.47 C -ANISOU 45 CB GLN A 7 10618 8928 8370 354 -1883 -815 C -ATOM 46 N GLY A 8 8.823 3.948 -27.801 1.00 73.18 N -ANISOU 46 N GLY A 8 10784 8821 8200 498 -1755 -948 N -ATOM 47 CA GLY A 8 8.899 4.188 -26.368 1.00 69.82 C -ANISOU 47 CA GLY A 8 10230 8406 7891 427 -1702 -924 C -ATOM 48 C GLY A 8 9.812 5.353 -26.041 1.00 65.65 C -ANISOU 48 C GLY A 8 9644 7989 7313 471 -1551 -886 C -ATOM 49 O GLY A 8 11.031 5.260 -26.172 1.00 64.83 O -ANISOU 49 O GLY A 8 9590 7936 7106 562 -1436 -904 O -ATOM 50 N GLN A 9 9.216 6.450 -25.591 1.00 62.76 N -ANISOU 50 N GLN A 9 9140 7661 7046 402 -1520 -807 N -ATOM 51 CA GLN A 9 9.912 7.728 -25.526 1.00 60.64 C -ANISOU 51 CA GLN A 9 8804 7489 6747 433 -1372 -740 C -ATOM 52 C GLN A 9 10.146 8.216 -24.097 1.00 54.33 C -ANISOU 52 C GLN A 9 7854 6710 6080 373 -1256 -686 C -ATOM 53 O GLN A 9 9.438 7.814 -23.174 1.00 52.17 O -ANISOU 53 O GLN A 9 7500 6385 5937 296 -1299 -682 O -ATOM 54 CB GLN A 9 9.122 8.771 -26.313 1.00 63.12 C -ANISOU 54 CB GLN A 9 9108 7831 7044 423 -1430 -692 C -ATOM 55 CG GLN A 9 9.708 10.165 -26.293 1.00 64.74 C -ANISOU 55 CG GLN A 9 9251 8121 7226 442 -1300 -615 C -ATOM 56 CD GLN A 9 9.177 11.013 -27.428 1.00 67.13 C -ANISOU 56 CD GLN A 9 9599 8451 7455 465 -1362 -581 C -ATOM 57 OE1 GLN A 9 8.207 10.643 -28.095 1.00 66.58 O -ANISOU 57 OE1 GLN A 9 9584 8337 7377 454 -1509 -610 O -ATOM 58 NE2 GLN A 9 9.817 12.154 -27.663 1.00 68.33 N -ANISOU 58 NE2 GLN A 9 9732 8675 7556 494 -1258 -514 N -ATOM 59 N MET A 10 11.148 9.076 -23.924 1.00 50.43 N -ANISOU 59 N MET A 10 7322 6292 5546 407 -1114 -640 N -ATOM 60 CA MET A 10 11.466 9.639 -22.614 1.00 46.75 C -ANISOU 60 CA MET A 10 6729 5845 5189 357 -1007 -590 C -ATOM 61 C MET A 10 10.507 10.771 -22.292 1.00 42.07 C -ANISOU 61 C MET A 10 6040 5253 4690 298 -1026 -527 C -ATOM 62 O MET A 10 10.463 11.786 -22.996 1.00 37.62 O -ANISOU 62 O MET A 10 5490 4729 4076 320 -1019 -485 O -ATOM 63 CB MET A 10 12.913 10.141 -22.557 1.00 49.16 C -ANISOU 63 CB MET A 10 7032 6227 5421 407 -862 -557 C -ATOM 64 CG MET A 10 13.965 9.057 -22.807 1.00 51.80 C -ANISOU 64 CG MET A 10 7448 6574 5659 483 -824 -612 C -ATOM 65 SD MET A 10 13.582 7.468 -22.029 1.00 66.35 S -ANISOU 65 SD MET A 10 9311 8319 7580 455 -900 -691 S -ATOM 66 CE MET A 10 13.787 7.841 -20.295 1.00 41.24 C -ANISOU 66 CE MET A 10 5979 5141 4548 375 -806 -641 C -ATOM 67 N VAL A 11 9.734 10.586 -21.226 1.00 38.38 N -ANISOU 67 N VAL A 11 5478 4746 4358 231 -1049 -519 N -ATOM 68 CA VAL A 11 8.739 11.577 -20.845 1.00 36.19 C -ANISOU 68 CA VAL A 11 5105 4471 4174 189 -1068 -463 C -ATOM 69 C VAL A 11 8.775 11.860 -19.352 1.00 32.09 C -ANISOU 69 C VAL A 11 4476 3952 3767 148 -985 -433 C -ATOM 70 O VAL A 11 9.238 11.037 -18.549 1.00 29.62 O -ANISOU 70 O VAL A 11 4148 3621 3485 131 -946 -459 O -ATOM 71 CB VAL A 11 7.319 11.133 -21.216 1.00 37.51 C -ANISOU 71 CB VAL A 11 5259 4596 4396 152 -1214 -471 C -ATOM 72 CG1 VAL A 11 7.154 11.063 -22.738 1.00 40.97 C -ANISOU 72 CG1 VAL A 11 5812 5035 4720 194 -1310 -495 C -ATOM 73 CG2 VAL A 11 7.007 9.801 -20.557 1.00 37.18 C -ANISOU 73 CG2 VAL A 11 5200 4501 4425 103 -1265 -508 C -ATOM 74 N HIS A 12 8.269 13.030 -18.992 1.00 30.84 N -ANISOU 74 N HIS A 12 4246 3808 3663 139 -961 -379 N -ATOM 75 CA HIS A 12 8.197 13.421 -17.599 1.00 29.93 C -ANISOU 75 CA HIS A 12 4035 3693 3644 112 -888 -351 C -ATOM 76 C HIS A 12 7.007 12.763 -16.930 1.00 29.83 C -ANISOU 76 C HIS A 12 3940 3655 3739 68 -949 -349 C -ATOM 77 O HIS A 12 5.930 12.666 -17.516 1.00 30.72 O -ANISOU 77 O HIS A 12 4036 3759 3877 56 -1050 -339 O -ATOM 78 CB HIS A 12 8.097 14.934 -17.468 1.00 30.91 C -ANISOU 78 CB HIS A 12 4130 3835 3780 130 -845 -299 C -ATOM 79 CG HIS A 12 7.959 15.398 -16.055 1.00 32.66 C -ANISOU 79 CG HIS A 12 4269 4052 4090 116 -777 -276 C -ATOM 80 ND1 HIS A 12 6.733 15.617 -15.461 1.00 34.49 N -ANISOU 80 ND1 HIS A 12 4415 4279 4412 110 -807 -252 N -ATOM 81 CD2 HIS A 12 8.890 15.661 -15.108 1.00 31.23 C -ANISOU 81 CD2 HIS A 12 4079 3872 3914 112 -683 -272 C -ATOM 82 CE1 HIS A 12 6.918 16.014 -14.214 1.00 33.45 C -ANISOU 82 CE1 HIS A 12 4235 4146 4329 111 -728 -239 C -ATOM 83 NE2 HIS A 12 8.217 16.042 -13.973 1.00 31.50 N -ANISOU 83 NE2 HIS A 12 4037 3898 4033 108 -659 -253 N -ATOM 84 N GLN A 13 7.222 12.308 -15.703 1.00 28.33 N -ANISOU 84 N GLN A 13 3696 3458 3612 41 -889 -351 N -ATOM 85 CA GLN A 13 6.183 11.703 -14.898 1.00 33.06 C -ANISOU 85 CA GLN A 13 4202 4044 4315 -4 -926 -333 C -ATOM 86 C GLN A 13 6.203 12.340 -13.512 1.00 32.25 C -ANISOU 86 C GLN A 13 4016 3962 4275 -1 -826 -299 C -ATOM 87 O GLN A 13 7.268 12.691 -13.014 1.00 28.73 O -ANISOU 87 O GLN A 13 3601 3521 3795 17 -737 -310 O -ATOM 88 CB GLN A 13 6.399 10.201 -14.810 1.00 38.31 C -ANISOU 88 CB GLN A 13 4900 4671 4985 -42 -969 -373 C -ATOM 89 CG GLN A 13 5.441 9.478 -13.899 1.00 42.95 C -ANISOU 89 CG GLN A 13 5391 5246 5684 -102 -1003 -343 C -ATOM 90 CD GLN A 13 5.698 7.990 -13.908 1.00 46.10 C -ANISOU 90 CD GLN A 13 5842 5591 6083 -142 -1060 -382 C -ATOM 91 OE1 GLN A 13 6.234 7.437 -12.950 1.00 45.99 O -ANISOU 91 OE1 GLN A 13 5814 5566 6093 -157 -999 -387 O -ATOM 92 NE2 GLN A 13 5.333 7.334 -15.005 1.00 48.51 N -ANISOU 92 NE2 GLN A 13 6219 5857 6357 -156 -1185 -412 N -ATOM 93 N CYS A 14 5.031 12.523 -12.905 1.00 32.41 N -ANISOU 93 N CYS A 14 3934 3997 4383 -14 -843 -256 N -ATOM 94 CA CYS A 14 4.976 13.145 -11.584 1.00 30.46 C -ANISOU 94 CA CYS A 14 3616 3772 4183 5 -748 -226 C -ATOM 95 C CYS A 14 5.667 12.248 -10.561 1.00 26.84 C -ANISOU 95 C CYS A 14 3155 3303 3740 -27 -689 -245 C -ATOM 96 O CYS A 14 5.604 11.029 -10.671 1.00 24.91 O -ANISOU 96 O CYS A 14 2917 3037 3513 -73 -740 -260 O -ATOM 97 CB CYS A 14 3.526 13.416 -11.174 1.00 30.43 C -ANISOU 97 CB CYS A 14 3495 3800 4266 9 -774 -170 C -ATOM 98 SG CYS A 14 2.774 14.772 -12.145 1.00 44.80 S -ANISOU 98 SG CYS A 14 5315 5638 6071 68 -823 -142 S -ATOM 99 N ILE A 15 6.329 12.858 -9.584 1.00 23.92 N -ANISOU 99 N ILE A 15 2785 2942 3362 -1 -592 -243 N -ATOM 100 CA ILE A 15 6.918 12.111 -8.480 1.00 26.89 C -ANISOU 100 CA ILE A 15 3151 3312 3755 -26 -534 -253 C -ATOM 101 C ILE A 15 5.792 11.485 -7.668 1.00 28.07 C -ANISOU 101 C ILE A 15 3196 3479 3988 -55 -545 -211 C -ATOM 102 O ILE A 15 4.784 12.133 -7.433 1.00 26.57 O -ANISOU 102 O ILE A 15 2932 3322 3841 -30 -543 -169 O -ATOM 103 CB ILE A 15 7.789 13.015 -7.591 1.00 30.22 C -ANISOU 103 CB ILE A 15 3595 3738 4148 8 -439 -256 C -ATOM 104 CG1 ILE A 15 8.394 12.205 -6.437 1.00 30.09 C -ANISOU 104 CG1 ILE A 15 3568 3717 4146 -17 -385 -265 C -ATOM 105 CG2 ILE A 15 6.969 14.213 -7.095 1.00 32.76 C -ANISOU 105 CG2 ILE A 15 3869 4080 4498 56 -412 -222 C -ATOM 106 CD1 ILE A 15 9.768 12.694 -5.996 1.00 33.30 C -ANISOU 106 CD1 ILE A 15 4036 4116 4501 -3 -320 -286 C -ATOM 107 N SER A 16 5.929 10.223 -7.263 1.00 25.59 N -ANISOU 107 N SER A 16 2875 3147 3702 -107 -559 -216 N -ATOM 108 CA SER A 16 4.778 9.564 -6.637 1.00 25.56 C -ANISOU 108 CA SER A 16 2765 3164 3784 -148 -583 -160 C -ATOM 109 C SER A 16 4.773 9.746 -5.127 1.00 23.83 C -ANISOU 109 C SER A 16 2485 2978 3589 -131 -483 -127 C -ATOM 110 O SER A 16 5.828 9.900 -4.503 1.00 23.78 O -ANISOU 110 O SER A 16 2535 2961 3540 -111 -412 -158 O -ATOM 111 CB SER A 16 4.753 8.071 -6.957 1.00 28.17 C -ANISOU 111 CB SER A 16 3116 3448 4139 -221 -667 -169 C -ATOM 112 OG SER A 16 5.610 7.389 -6.070 1.00 30.37 O -ANISOU 112 OG SER A 16 3424 3707 4409 -236 -611 -185 O -ATOM 113 N PRO A 17 3.578 9.719 -4.535 1.00 25.55 N -ANISOU 113 N PRO A 17 2587 3245 3876 -137 -477 -58 N -ATOM 114 CA PRO A 17 3.434 9.801 -3.079 1.00 26.10 C -ANISOU 114 CA PRO A 17 2594 3357 3965 -115 -380 -18 C -ATOM 115 C PRO A 17 4.227 8.693 -2.418 1.00 26.97 C -ANISOU 115 C PRO A 17 2741 3435 4073 -167 -362 -32 C -ATOM 116 O PRO A 17 4.806 8.910 -1.350 1.00 26.04 O -ANISOU 116 O PRO A 17 2638 3328 3926 -137 -276 -38 O -ATOM 117 CB PRO A 17 1.924 9.637 -2.864 1.00 26.92 C -ANISOU 117 CB PRO A 17 2556 3524 4151 -130 -402 70 C -ATOM 118 CG PRO A 17 1.328 10.233 -4.117 1.00 29.83 C -ANISOU 118 CG PRO A 17 2919 3891 4523 -114 -481 66 C -ATOM 119 CD PRO A 17 2.277 9.792 -5.230 1.00 29.40 C -ANISOU 119 CD PRO A 17 2991 3760 4419 -152 -555 -9 C -ATOM 120 N ARG A 18 4.300 7.541 -3.086 1.00 27.42 N -ANISOU 120 N ARG A 18 2824 3442 4150 -240 -451 -43 N -ATOM 121 CA ARG A 18 5.060 6.408 -2.577 1.00 29.33 C -ANISOU 121 CA ARG A 18 3112 3641 4391 -286 -449 -59 C -ATOM 122 C ARG A 18 6.513 6.814 -2.373 1.00 26.38 C -ANISOU 122 C ARG A 18 2839 3246 3938 -239 -384 -126 C -ATOM 123 O ARG A 18 7.098 6.573 -1.321 1.00 27.51 O -ANISOU 123 O ARG A 18 2990 3393 4071 -235 -319 -123 O -ATOM 124 CB ARG A 18 4.982 5.212 -3.534 1.00 34.67 C -ANISOU 124 CB ARG A 18 3833 4251 5089 -356 -571 -76 C -ATOM 125 CG ARG A 18 3.586 4.650 -3.778 1.00 41.44 C -ANISOU 125 CG ARG A 18 4593 5118 6034 -426 -661 -4 C -ATOM 126 CD ARG A 18 2.882 4.321 -2.474 1.00 48.58 C -ANISOU 126 CD ARG A 18 5378 6075 7006 -459 -605 89 C -ATOM 127 NE ARG A 18 3.681 3.449 -1.614 1.00 53.53 N -ANISOU 127 NE ARG A 18 6050 6666 7624 -485 -569 82 N -ATOM 128 CZ ARG A 18 3.209 2.371 -0.989 1.00 57.95 C -ANISOU 128 CZ ARG A 18 6555 7213 8249 -565 -599 152 C -ATOM 129 NH1 ARG A 18 1.938 2.016 -1.135 1.00 59.96 N -ANISOU 129 NH1 ARG A 18 6700 7494 8590 -634 -668 239 N -ATOM 130 NH2 ARG A 18 4.010 1.641 -0.222 1.00 58.33 N -ANISOU 130 NH2 ARG A 18 6655 7225 8282 -580 -565 141 N -ATOM 131 N THR A 19 7.094 7.448 -3.386 1.00 23.69 N -ANISOU 131 N THR A 19 2572 2888 3541 -204 -404 -179 N -ATOM 132 CA THR A 19 8.484 7.880 -3.302 1.00 21.32 C -ANISOU 132 CA THR A 19 2355 2574 3170 -166 -349 -231 C -ATOM 133 C THR A 19 8.666 8.991 -2.263 1.00 24.94 C -ANISOU 133 C THR A 19 2794 3070 3612 -118 -257 -217 C -ATOM 134 O THR A 19 9.622 8.971 -1.480 1.00 22.46 O -ANISOU 134 O THR A 19 2515 2749 3268 -110 -203 -233 O -ATOM 135 CB THR A 19 8.988 8.359 -4.675 1.00 21.08 C -ANISOU 135 CB THR A 19 2398 2528 3082 -141 -389 -275 C -ATOM 136 OG1 THR A 19 8.882 7.277 -5.609 1.00 20.85 O -ANISOU 136 OG1 THR A 19 2408 2460 3055 -174 -478 -298 O -ATOM 137 CG2 THR A 19 10.434 8.804 -4.598 1.00 21.56 C -ANISOU 137 CG2 THR A 19 2530 2587 3076 -109 -332 -311 C -ATOM 138 N LEU A 20 7.751 9.955 -2.276 1.00 25.66 N -ANISOU 138 N LEU A 20 2836 3195 3720 -83 -247 -188 N -ATOM 139 CA LEU A 20 7.822 11.103 -1.378 1.00 25.87 C -ANISOU 139 CA LEU A 20 2860 3245 3724 -24 -172 -182 C -ATOM 140 C LEU A 20 7.796 10.618 0.059 1.00 25.73 C -ANISOU 140 C LEU A 20 2806 3249 3721 -27 -110 -155 C -ATOM 141 O LEU A 20 8.622 11.022 0.877 1.00 25.22 O -ANISOU 141 O LEU A 20 2789 3178 3615 -2 -56 -175 O -ATOM 142 CB LEU A 20 6.661 12.065 -1.648 1.00 28.25 C -ANISOU 142 CB LEU A 20 3108 3580 4046 24 -179 -151 C -ATOM 143 CG LEU A 20 6.761 12.872 -2.955 1.00 30.22 C -ANISOU 143 CG LEU A 20 3407 3808 4268 43 -230 -176 C -ATOM 144 CD1 LEU A 20 5.414 13.453 -3.362 1.00 31.30 C -ANISOU 144 CD1 LEU A 20 3473 3978 4442 78 -260 -137 C -ATOM 145 CD2 LEU A 20 7.775 13.973 -2.805 1.00 30.44 C -ANISOU 145 CD2 LEU A 20 3519 3810 4235 81 -192 -209 C -ATOM 146 N ASN A 21 6.861 9.717 0.352 1.00 24.36 N -ANISOU 146 N ASN A 21 2549 3101 3606 -64 -124 -104 N -ATOM 147 CA ASN A 21 6.729 9.219 1.711 1.00 26.38 C -ANISOU 147 CA ASN A 21 2763 3386 3875 -69 -63 -64 C -ATOM 148 C ASN A 21 7.933 8.383 2.136 1.00 24.36 C -ANISOU 148 C ASN A 21 2573 3089 3594 -106 -56 -95 C -ATOM 149 O ASN A 21 8.408 8.518 3.267 1.00 21.40 O -ANISOU 149 O ASN A 21 2215 2726 3189 -82 9 -93 O -ATOM 150 CB ASN A 21 5.449 8.411 1.857 1.00 32.16 C -ANISOU 150 CB ASN A 21 3380 4157 4681 -112 -86 14 C -ATOM 151 CG ASN A 21 5.184 8.028 3.287 1.00 37.66 C -ANISOU 151 CG ASN A 21 4023 4900 5387 -107 -11 71 C -ATOM 152 OD1 ASN A 21 5.066 8.895 4.161 1.00 39.69 O -ANISOU 152 OD1 ASN A 21 4272 5202 5606 -30 70 78 O -ATOM 153 ND2 ASN A 21 5.099 6.729 3.547 1.00 36.99 N -ANISOU 153 ND2 ASN A 21 3908 4801 5347 -186 -40 111 N -ATOM 154 N ALA A 22 8.447 7.545 1.227 1.00 24.69 N -ANISOU 154 N ALA A 22 2658 3081 3642 -155 -124 -126 N -ATOM 155 CA ALA A 22 9.633 6.728 1.521 1.00 27.10 C -ANISOU 155 CA ALA A 22 3028 3346 3921 -179 -122 -157 C -ATOM 156 C ALA A 22 10.801 7.579 1.985 1.00 27.20 C -ANISOU 156 C ALA A 22 3103 3359 3871 -134 -66 -196 C -ATOM 157 O ALA A 22 11.449 7.263 2.987 1.00 29.64 O -ANISOU 157 O ALA A 22 3430 3667 4163 -134 -25 -193 O -ATOM 158 CB ALA A 22 10.050 5.905 0.301 1.00 26.86 C -ANISOU 158 CB ALA A 22 3052 3265 3891 -212 -203 -196 C -ATOM 159 N TRP A 23 11.076 8.660 1.259 1.00 21.59 N -ANISOU 159 N TRP A 23 2428 2649 3126 -99 -70 -226 N -ATOM 160 CA TRP A 23 12.231 9.489 1.579 1.00 22.13 C -ANISOU 160 CA TRP A 23 2557 2711 3140 -71 -34 -256 C -ATOM 161 C TRP A 23 12.049 10.188 2.918 1.00 22.82 C -ANISOU 161 C TRP A 23 2637 2820 3214 -35 26 -239 C -ATOM 162 O TRP A 23 12.992 10.264 3.736 1.00 22.34 O -ANISOU 162 O TRP A 23 2618 2751 3121 -32 55 -251 O -ATOM 163 CB TRP A 23 12.475 10.518 0.470 1.00 20.32 C -ANISOU 163 CB TRP A 23 2365 2474 2882 -50 -58 -279 C -ATOM 164 CG TRP A 23 13.499 11.573 0.821 1.00 23.44 C -ANISOU 164 CG TRP A 23 2815 2862 3231 -29 -30 -295 C -ATOM 165 CD1 TRP A 23 13.308 12.925 0.815 1.00 21.49 C -ANISOU 165 CD1 TRP A 23 2591 2610 2966 5 -24 -294 C -ATOM 166 CD2 TRP A 23 14.858 11.365 1.221 1.00 23.08 C -ANISOU 166 CD2 TRP A 23 2808 2806 3154 -45 -15 -308 C -ATOM 167 NE1 TRP A 23 14.456 13.563 1.180 1.00 22.96 N -ANISOU 167 NE1 TRP A 23 2831 2778 3114 2 -13 -305 N -ATOM 168 CE2 TRP A 23 15.427 12.634 1.430 1.00 23.33 C -ANISOU 168 CE2 TRP A 23 2882 2829 3155 -30 -6 -311 C -ATOM 169 CE3 TRP A 23 15.651 10.227 1.420 1.00 22.78 C -ANISOU 169 CE3 TRP A 23 2774 2766 3116 -69 -13 -315 C -ATOM 170 CZ2 TRP A 23 16.750 12.803 1.836 1.00 23.20 C -ANISOU 170 CZ2 TRP A 23 2901 2805 3109 -48 1 -314 C -ATOM 171 CZ3 TRP A 23 16.962 10.395 1.809 1.00 24.34 C -ANISOU 171 CZ3 TRP A 23 3004 2963 3282 -75 1 -320 C -ATOM 172 CH2 TRP A 23 17.502 11.675 2.013 1.00 24.07 C -ANISOU 172 CH2 TRP A 23 3001 2924 3220 -69 7 -317 C -ATOM 173 N VAL A 24 10.850 10.718 3.128 1.00 24.29 N -ANISOU 173 N VAL A 24 2773 3036 3421 -2 43 -210 N -ATOM 174 CA VAL A 24 10.543 11.426 4.360 1.00 28.38 C -ANISOU 174 CA VAL A 24 3289 3578 3914 53 103 -196 C -ATOM 175 C VAL A 24 10.736 10.508 5.567 1.00 25.45 C -ANISOU 175 C VAL A 24 2905 3224 3543 35 142 -172 C -ATOM 176 O VAL A 24 11.319 10.915 6.571 1.00 24.12 O -ANISOU 176 O VAL A 24 2784 3052 3328 64 179 -185 O -ATOM 177 CB VAL A 24 9.110 11.988 4.335 1.00 33.78 C -ANISOU 177 CB VAL A 24 3907 4306 4624 103 119 -160 C -ATOM 178 CG1 VAL A 24 8.573 12.214 5.755 1.00 35.81 C -ANISOU 178 CG1 VAL A 24 4140 4608 4860 162 192 -129 C -ATOM 179 CG2 VAL A 24 9.077 13.277 3.515 1.00 34.11 C -ANISOU 179 CG2 VAL A 24 3991 4325 4644 146 93 -188 C -ATOM 180 N LYS A 25 10.267 9.268 5.458 1.00 25.97 N -ANISOU 180 N LYS A 25 2910 3298 3658 -17 124 -136 N -ATOM 181 CA LYS A 25 10.352 8.324 6.571 1.00 29.37 C -ANISOU 181 CA LYS A 25 3323 3743 4093 -40 157 -101 C -ATOM 182 C LYS A 25 11.779 7.824 6.824 1.00 30.34 C -ANISOU 182 C LYS A 25 3518 3824 4185 -66 146 -137 C -ATOM 183 O LYS A 25 12.183 7.668 7.974 1.00 32.68 O -ANISOU 183 O LYS A 25 3834 4130 4452 -55 186 -127 O -ATOM 184 CB LYS A 25 9.408 7.142 6.323 1.00 30.95 C -ANISOU 184 CB LYS A 25 3440 3956 4363 -98 127 -43 C -ATOM 185 CG LYS A 25 7.965 7.558 6.152 1.00 35.58 C -ANISOU 185 CG LYS A 25 3934 4597 4988 -77 137 9 C -ATOM 186 CD LYS A 25 7.341 7.875 7.499 1.00 41.32 C -ANISOU 186 CD LYS A 25 4613 5394 5694 -22 225 63 C -ATOM 187 CE LYS A 25 6.213 8.876 7.387 1.00 44.55 C -ANISOU 187 CE LYS A 25 4957 5861 6107 49 256 91 C -ATOM 188 NZ LYS A 25 5.705 9.214 8.743 1.00 46.95 N -ANISOU 188 NZ LYS A 25 5228 6238 6372 122 351 137 N -ATOM 189 N VAL A 26 12.533 7.570 5.755 1.00 27.42 N -ANISOU 189 N VAL A 26 3185 3414 3819 -94 94 -177 N -ATOM 190 CA VAL A 26 13.957 7.222 5.853 1.00 28.02 C -ANISOU 190 CA VAL A 26 3323 3460 3864 -107 85 -210 C -ATOM 191 C VAL A 26 14.752 8.248 6.680 1.00 27.88 C -ANISOU 191 C VAL A 26 3354 3448 3791 -71 120 -229 C -ATOM 192 O VAL A 26 15.492 7.913 7.621 1.00 26.52 O -ANISOU 192 O VAL A 26 3208 3272 3595 -75 137 -226 O -ATOM 193 CB VAL A 26 14.592 7.124 4.438 1.00 45.26 C -ANISOU 193 CB VAL A 26 5537 5617 6045 -119 35 -248 C -ATOM 194 CG1 VAL A 26 16.083 7.418 4.485 1.00 45.73 C -ANISOU 194 CG1 VAL A 26 5650 5667 6060 -110 40 -278 C -ATOM 195 CG2 VAL A 26 14.304 5.772 3.810 1.00 46.06 C -ANISOU 195 CG2 VAL A 26 5626 5691 6185 -156 -14 -244 C -ATOM 196 N VAL A 27 14.573 9.516 6.347 1.00 26.26 N -ANISOU 196 N VAL A 27 3168 3246 3566 -38 122 -246 N -ATOM 197 CA VAL A 27 15.244 10.579 7.105 1.00 27.18 C -ANISOU 197 CA VAL A 27 3343 3353 3631 -8 139 -264 C -ATOM 198 C VAL A 27 14.743 10.637 8.546 1.00 27.18 C -ANISOU 198 C VAL A 27 3345 3377 3607 28 187 -244 C -ATOM 199 O VAL A 27 15.538 10.787 9.476 1.00 28.94 O -ANISOU 199 O VAL A 27 3619 3590 3790 34 195 -254 O -ATOM 200 CB VAL A 27 15.048 11.938 6.415 1.00 28.76 C -ANISOU 200 CB VAL A 27 3570 3540 3817 20 122 -283 C -ATOM 201 CG1 VAL A 27 15.630 13.068 7.274 1.00 30.02 C -ANISOU 201 CG1 VAL A 27 3804 3677 3927 50 126 -301 C -ATOM 202 CG2 VAL A 27 15.695 11.896 5.033 1.00 29.23 C -ANISOU 202 CG2 VAL A 27 3635 3585 3888 -15 80 -297 C -ATOM 203 N GLU A 28 13.431 10.509 8.732 1.00 29.40 N -ANISOU 203 N GLU A 28 3567 3694 3910 55 219 -211 N -ATOM 204 CA GLU A 28 12.833 10.537 10.068 1.00 32.56 C -ANISOU 204 CA GLU A 28 3958 4132 4280 102 278 -181 C -ATOM 205 C GLU A 28 13.401 9.415 10.961 1.00 35.41 C -ANISOU 205 C GLU A 28 4322 4497 4635 66 291 -159 C -ATOM 206 O GLU A 28 13.726 9.633 12.134 1.00 34.49 O -ANISOU 206 O GLU A 28 4252 4389 4463 99 321 -159 O -ATOM 207 CB GLU A 28 11.304 10.422 9.978 1.00 32.41 C -ANISOU 207 CB GLU A 28 3850 4167 4298 129 311 -131 C -ATOM 208 CG GLU A 28 10.601 11.718 9.573 1.00 35.62 C -ANISOU 208 CG GLU A 28 4262 4582 4691 199 317 -147 C -ATOM 209 CD GLU A 28 9.076 11.625 9.615 1.00 41.07 C -ANISOU 209 CD GLU A 28 4848 5340 5415 237 357 -87 C -ATOM 210 OE1 GLU A 28 8.537 10.522 9.867 1.00 40.68 O -ANISOU 210 OE1 GLU A 28 4717 5331 5408 194 374 -27 O -ATOM 211 OE2 GLU A 28 8.413 12.664 9.394 1.00 43.74 O -ANISOU 211 OE2 GLU A 28 5185 5693 5741 310 369 -95 O -ATOM 212 N GLU A 29 13.526 8.222 10.395 1.00 32.37 N -ANISOU 212 N GLU A 29 3896 4099 4302 2 261 -141 N -ATOM 213 CA GLU A 29 13.998 7.073 11.154 1.00 35.81 C -ANISOU 213 CA GLU A 29 4334 4532 4740 -33 266 -114 C -ATOM 214 C GLU A 29 15.524 7.027 11.279 1.00 35.76 C -ANISOU 214 C GLU A 29 4397 4488 4702 -47 236 -154 C -ATOM 215 O GLU A 29 16.041 6.673 12.328 1.00 38.27 O -ANISOU 215 O GLU A 29 4744 4809 4989 -45 252 -142 O -ATOM 216 CB GLU A 29 13.469 5.781 10.520 0.60 35.92 C -ANISOU 216 CB GLU A 29 4288 4538 4825 -92 235 -76 C -ATOM 217 CG GLU A 29 11.955 5.653 10.626 0.60 37.55 C -ANISOU 217 CG GLU A 29 4407 4792 5069 -91 263 -13 C -ATOM 218 CD GLU A 29 11.373 4.551 9.752 0.60 39.63 C -ANISOU 218 CD GLU A 29 4615 5033 5410 -161 208 19 C -ATOM 219 OE1 GLU A 29 12.148 3.809 9.120 0.60 39.43 O -ANISOU 219 OE1 GLU A 29 4631 4951 5401 -201 151 -13 O -ATOM 220 OE2 GLU A 29 10.128 4.434 9.697 0.60 41.28 O -ANISOU 220 OE2 GLU A 29 4741 5282 5662 -173 217 79 O -ATOM 221 N LYS A 30 16.248 7.424 10.240 1.00 33.85 N -ANISOU 221 N LYS A 30 4179 4218 4466 -60 194 -196 N -ATOM 222 CA LYS A 30 17.679 7.119 10.172 1.00 32.95 C -ANISOU 222 CA LYS A 30 4104 4078 4337 -81 164 -218 C -ATOM 223 C LYS A 30 18.628 8.314 10.248 1.00 32.87 C -ANISOU 223 C LYS A 30 4148 4059 4285 -68 149 -249 C -ATOM 224 O LYS A 30 19.842 8.130 10.328 1.00 32.91 O -ANISOU 224 O LYS A 30 4174 4054 4277 -86 125 -256 O -ATOM 225 CB LYS A 30 17.975 6.351 8.881 1.00 32.38 C -ANISOU 225 CB LYS A 30 4013 3987 4305 -109 125 -230 C -ATOM 226 CG LYS A 30 17.311 4.977 8.797 1.00 33.03 C -ANISOU 226 CG LYS A 30 4060 4057 4432 -136 115 -202 C -ATOM 227 CD LYS A 30 17.804 4.028 9.868 1.00 34.27 C -ANISOU 227 CD LYS A 30 4231 4208 4584 -147 123 -176 C -ATOM 228 CE LYS A 30 17.386 2.571 9.564 1.00 35.80 C -ANISOU 228 CE LYS A 30 4406 4370 4828 -183 92 -151 C -ATOM 229 NZ LYS A 30 18.335 1.857 8.621 1.00 34.75 N -ANISOU 229 NZ LYS A 30 4304 4197 4701 -182 44 -187 N -ATOM 230 N ALA A 31 18.089 9.530 10.198 1.00 34.55 N -ANISOU 230 N ALA A 31 4380 4271 4477 -38 156 -262 N -ATOM 231 CA ALA A 31 18.927 10.730 10.228 1.00 35.76 C -ANISOU 231 CA ALA A 31 4592 4401 4595 -34 128 -287 C -ATOM 232 C ALA A 31 19.952 10.682 9.104 1.00 35.49 C -ANISOU 232 C ALA A 31 4547 4358 4580 -74 90 -293 C -ATOM 233 O ALA A 31 19.608 10.368 7.968 1.00 38.77 O -ANISOU 233 O ALA A 31 4925 4780 5025 -81 86 -294 O -ATOM 234 CB ALA A 31 19.619 10.873 11.576 1.00 36.77 C -ANISOU 234 CB ALA A 31 4774 4521 4675 -28 124 -288 C -ATOM 235 N PHE A 32 21.213 10.971 9.417 1.00 33.02 N -ANISOU 235 N PHE A 32 4264 4036 4246 -97 60 -293 N -ATOM 236 CA PHE A 32 22.265 10.893 8.398 1.00 31.32 C -ANISOU 236 CA PHE A 32 4025 3830 4045 -129 34 -286 C -ATOM 237 C PHE A 32 23.218 9.723 8.624 1.00 29.75 C -ANISOU 237 C PHE A 32 3800 3651 3854 -142 32 -272 C -ATOM 238 O PHE A 32 24.414 9.804 8.336 1.00 31.83 O -ANISOU 238 O PHE A 32 4051 3929 4114 -163 10 -256 O -ATOM 239 CB PHE A 32 23.015 12.219 8.331 1.00 33.86 C -ANISOU 239 CB PHE A 32 4386 4134 4347 -153 -6 -281 C -ATOM 240 CG PHE A 32 22.128 13.345 7.953 1.00 36.51 C -ANISOU 240 CG PHE A 32 4753 4443 4677 -134 -11 -295 C -ATOM 241 CD1 PHE A 32 21.725 13.500 6.637 1.00 37.83 C -ANISOU 241 CD1 PHE A 32 4892 4619 4864 -133 -8 -293 C -ATOM 242 CD2 PHE A 32 21.618 14.201 8.918 1.00 37.32 C -ANISOU 242 CD2 PHE A 32 4920 4511 4749 -106 -17 -313 C -ATOM 243 CE1 PHE A 32 20.867 14.525 6.283 1.00 39.91 C -ANISOU 243 CE1 PHE A 32 5183 4856 5123 -110 -15 -303 C -ATOM 244 CE2 PHE A 32 20.755 15.226 8.568 1.00 36.82 C -ANISOU 244 CE2 PHE A 32 4889 4420 4679 -74 -21 -327 C -ATOM 245 CZ PHE A 32 20.380 15.385 7.250 1.00 38.28 C -ANISOU 245 CZ PHE A 32 5039 4615 4892 -79 -21 -320 C -ATOM 246 N SER A 33 22.667 8.623 9.125 1.00 30.36 N -ANISOU 246 N SER A 33 3865 3729 3943 -128 56 -270 N -ATOM 247 CA SER A 33 23.362 7.349 9.081 1.00 31.52 C -ANISOU 247 CA SER A 33 3987 3885 4103 -130 53 -260 C -ATOM 248 C SER A 33 23.728 7.085 7.614 1.00 29.16 C -ANISOU 248 C SER A 33 3661 3599 3819 -125 45 -267 C -ATOM 249 O SER A 33 22.982 7.469 6.703 1.00 29.83 O -ANISOU 249 O SER A 33 3741 3681 3912 -121 48 -280 O -ATOM 250 CB SER A 33 22.483 6.234 9.657 1.00 35.63 C -ANISOU 250 CB SER A 33 4501 4394 4641 -122 73 -252 C -ATOM 251 OG SER A 33 23.253 5.070 9.901 1.00 40.67 O -ANISOU 251 OG SER A 33 5135 5031 5288 -121 63 -241 O -ATOM 252 N PRO A 34 24.887 6.463 7.371 1.00 27.32 N -ANISOU 252 N PRO A 34 3411 3386 3583 -118 37 -257 N -ATOM 253 CA PRO A 34 25.342 6.377 5.973 1.00 23.25 C -ANISOU 253 CA PRO A 34 2874 2894 3064 -100 36 -262 C -ATOM 254 C PRO A 34 24.379 5.652 5.018 1.00 21.45 C -ANISOU 254 C PRO A 34 2653 2646 2850 -78 37 -289 C -ATOM 255 O PRO A 34 24.336 6.023 3.843 1.00 22.22 O -ANISOU 255 O PRO A 34 2747 2760 2937 -67 36 -297 O -ATOM 256 CB PRO A 34 26.684 5.620 6.081 1.00 26.85 C -ANISOU 256 CB PRO A 34 3308 3381 3513 -79 34 -244 C -ATOM 257 CG PRO A 34 26.768 5.118 7.513 1.00 27.32 C -ANISOU 257 CG PRO A 34 3382 3419 3578 -89 27 -234 C -ATOM 258 CD PRO A 34 25.924 6.036 8.332 1.00 25.60 C -ANISOU 258 CD PRO A 34 3191 3179 3356 -120 27 -237 C -ATOM 259 N GLU A 35 23.597 4.683 5.494 1.00 23.56 N -ANISOU 259 N GLU A 35 2932 2878 3140 -78 33 -296 N -ATOM 260 CA GLU A 35 22.751 3.905 4.576 1.00 26.83 C -ANISOU 260 CA GLU A 35 3357 3266 3573 -66 16 -318 C -ATOM 261 C GLU A 35 21.574 4.744 4.056 1.00 27.70 C -ANISOU 261 C GLU A 35 3460 3372 3693 -84 13 -324 C -ATOM 262 O GLU A 35 20.813 4.299 3.203 1.00 27.83 O -ANISOU 262 O GLU A 35 3482 3368 3724 -81 -11 -340 O -ATOM 263 CB GLU A 35 22.252 2.605 5.232 1.00 25.65 C -ANISOU 263 CB GLU A 35 3219 3073 3453 -74 0 -313 C -ATOM 264 CG GLU A 35 21.178 2.767 6.298 1.00 28.98 C -ANISOU 264 CG GLU A 35 3628 3485 3900 -109 13 -287 C -ATOM 265 CD GLU A 35 21.755 2.968 7.691 1.00 29.05 C -ANISOU 265 CD GLU A 35 3637 3508 3891 -114 36 -263 C -ATOM 266 OE1 GLU A 35 22.933 3.416 7.820 1.00 26.79 O -ANISOU 266 OE1 GLU A 35 3356 3246 3577 -101 40 -265 O -ATOM 267 OE2 GLU A 35 21.021 2.672 8.657 1.00 30.94 O -ANISOU 267 OE2 GLU A 35 3872 3739 4143 -132 49 -236 O -ATOM 268 N VAL A 36 21.467 5.976 4.543 1.00 26.88 N -ANISOU 268 N VAL A 36 3349 3285 3580 -98 31 -312 N -ATOM 269 CA VAL A 36 20.476 6.916 4.055 1.00 28.03 C -ANISOU 269 CA VAL A 36 3489 3430 3730 -102 30 -316 C -ATOM 270 C VAL A 36 20.810 7.408 2.643 1.00 26.90 C -ANISOU 270 C VAL A 36 3351 3302 3566 -90 17 -328 C -ATOM 271 O VAL A 36 19.910 7.683 1.843 1.00 29.12 O -ANISOU 271 O VAL A 36 3630 3577 3856 -88 2 -336 O -ATOM 272 CB VAL A 36 20.350 8.120 5.029 1.00 32.58 C -ANISOU 272 CB VAL A 36 4074 4010 4294 -108 48 -304 C -ATOM 273 CG1 VAL A 36 19.752 9.310 4.343 1.00 32.88 C -ANISOU 273 CG1 VAL A 36 4117 4049 4327 -102 42 -309 C -ATOM 274 CG2 VAL A 36 19.529 7.718 6.251 1.00 30.38 C -ANISOU 274 CG2 VAL A 36 3789 3725 4030 -108 68 -291 C -ATOM 275 N ILE A 37 22.100 7.509 2.344 1.00 23.65 N -ANISOU 275 N ILE A 37 2941 2917 3127 -82 22 -321 N -ATOM 276 CA ILE A 37 22.575 8.062 1.078 1.00 21.13 C -ANISOU 276 CA ILE A 37 2622 2627 2780 -69 20 -318 C -ATOM 277 C ILE A 37 22.207 7.209 -0.139 1.00 22.14 C -ANISOU 277 C ILE A 37 2765 2751 2896 -37 4 -344 C -ATOM 278 O ILE A 37 21.664 7.727 -1.120 1.00 22.90 O -ANISOU 278 O ILE A 37 2870 2850 2980 -32 -9 -350 O -ATOM 279 CB ILE A 37 24.117 8.266 1.062 1.00 37.70 C -ANISOU 279 CB ILE A 37 4703 4769 4851 -67 35 -289 C -ATOM 280 CG1 ILE A 37 24.561 9.314 2.088 1.00 38.27 C -ANISOU 280 CG1 ILE A 37 4771 4840 4930 -108 32 -261 C -ATOM 281 CG2 ILE A 37 24.588 8.661 -0.338 1.00 35.11 C -ANISOU 281 CG2 ILE A 37 4369 4484 4487 -47 41 -276 C -ATOM 282 CD1 ILE A 37 23.581 10.448 2.301 1.00 41.12 C -ANISOU 282 CD1 ILE A 37 5157 5167 5300 -129 20 -265 C -ATOM 283 N PRO A 38 22.518 5.903 -0.099 1.00 22.97 N -ANISOU 283 N PRO A 38 2881 2843 3001 -11 -3 -362 N -ATOM 284 CA PRO A 38 22.070 4.997 -1.171 1.00 22.45 C -ANISOU 284 CA PRO A 38 2850 2756 2923 22 -34 -396 C -ATOM 285 C PRO A 38 20.548 4.916 -1.284 1.00 22.09 C -ANISOU 285 C PRO A 38 2811 2667 2916 -8 -72 -408 C -ATOM 286 O PRO A 38 20.024 4.647 -2.360 1.00 19.84 O -ANISOU 286 O PRO A 38 2554 2367 2618 7 -109 -432 O -ATOM 287 CB PRO A 38 22.652 3.631 -0.752 1.00 21.03 C -ANISOU 287 CB PRO A 38 2690 2554 2746 51 -41 -410 C -ATOM 288 CG PRO A 38 22.898 3.768 0.727 1.00 21.35 C -ANISOU 288 CG PRO A 38 2701 2594 2818 16 -19 -381 C -ATOM 289 CD PRO A 38 23.333 5.200 0.905 1.00 22.15 C -ANISOU 289 CD PRO A 38 2770 2740 2905 -6 10 -352 C -ATOM 290 N MET A 39 19.836 5.106 -0.181 1.00 21.93 N -ANISOU 290 N MET A 39 2763 2630 2940 -48 -66 -389 N -ATOM 291 CA MET A 39 18.385 5.152 -0.281 1.00 23.66 C -ANISOU 291 CA MET A 39 2967 2825 3198 -75 -95 -385 C -ATOM 292 C MET A 39 17.987 6.416 -1.062 1.00 20.14 C -ANISOU 292 C MET A 39 2514 2403 2736 -70 -94 -383 C -ATOM 293 O MET A 39 17.124 6.349 -1.950 1.00 20.03 O -ANISOU 293 O MET A 39 2505 2376 2729 -71 -135 -393 O -ATOM 294 CB MET A 39 17.719 5.117 1.105 1.00 26.53 C -ANISOU 294 CB MET A 39 3295 3181 3605 -107 -75 -355 C -ATOM 295 CG MET A 39 16.194 4.995 1.065 1.00 29.55 C -ANISOU 295 CG MET A 39 3643 3550 4035 -134 -102 -337 C -ATOM 296 SD MET A 39 15.628 3.421 0.337 1.00 32.46 S -ANISOU 296 SD MET A 39 4033 3863 4436 -158 -180 -348 S -ATOM 297 CE MET A 39 15.767 2.295 1.716 1.00 29.51 C -ANISOU 297 CE MET A 39 3651 3463 4097 -187 -169 -317 C -ATOM 298 N PHE A 40 18.621 7.552 -0.751 1.00 21.36 N -ANISOU 298 N PHE A 40 2663 2586 2868 -67 -58 -367 N -ATOM 299 CA PHE A 40 18.332 8.798 -1.476 1.00 20.49 C -ANISOU 299 CA PHE A 40 2555 2491 2741 -63 -62 -360 C -ATOM 300 C PHE A 40 18.569 8.612 -2.963 1.00 20.40 C -ANISOU 300 C PHE A 40 2570 2491 2690 -39 -86 -376 C -ATOM 301 O PHE A 40 17.715 8.944 -3.790 1.00 21.27 O -ANISOU 301 O PHE A 40 2686 2595 2801 -36 -117 -380 O -ATOM 302 CB PHE A 40 19.183 9.976 -0.971 1.00 22.07 C -ANISOU 302 CB PHE A 40 2757 2707 2920 -70 -32 -338 C -ATOM 303 CG PHE A 40 18.954 11.258 -1.740 1.00 25.29 C -ANISOU 303 CG PHE A 40 3177 3121 3312 -68 -43 -325 C -ATOM 304 CD1 PHE A 40 17.797 11.997 -1.541 1.00 24.94 C -ANISOU 304 CD1 PHE A 40 3129 3058 3291 -65 -53 -323 C -ATOM 305 CD2 PHE A 40 19.883 11.711 -2.671 1.00 26.82 C -ANISOU 305 CD2 PHE A 40 3383 3342 3464 -66 -41 -308 C -ATOM 306 CE1 PHE A 40 17.569 13.167 -2.253 1.00 26.44 C -ANISOU 306 CE1 PHE A 40 3336 3245 3466 -59 -69 -310 C -ATOM 307 CE2 PHE A 40 19.664 12.891 -3.382 1.00 26.55 C -ANISOU 307 CE2 PHE A 40 3364 3309 3415 -69 -54 -288 C -ATOM 308 CZ PHE A 40 18.510 13.619 -3.160 1.00 27.30 C -ANISOU 308 CZ PHE A 40 3464 3373 3536 -66 -72 -292 C -ATOM 309 N SER A 41 19.728 8.061 -3.295 1.00 22.18 N -ANISOU 309 N SER A 41 2812 2737 2878 -16 -71 -382 N -ATOM 310 CA SER A 41 20.090 7.843 -4.694 1.00 24.62 C -ANISOU 310 CA SER A 41 3153 3068 3132 23 -84 -397 C -ATOM 311 C SER A 41 19.094 6.962 -5.435 1.00 24.43 C -ANISOU 311 C SER A 41 3163 3005 3113 35 -142 -434 C -ATOM 312 O SER A 41 18.748 7.250 -6.579 1.00 23.16 O -ANISOU 312 O SER A 41 3030 2853 2918 53 -169 -443 O -ATOM 313 CB SER A 41 21.485 7.228 -4.797 1.00 21.32 C -ANISOU 313 CB SER A 41 2742 2685 2672 62 -52 -396 C -ATOM 314 OG SER A 41 21.877 7.201 -6.154 1.00 25.77 O -ANISOU 314 OG SER A 41 3337 3285 3170 111 -52 -403 O -ATOM 315 N ALA A 42 18.630 5.889 -4.795 1.00 24.68 N -ANISOU 315 N ALA A 42 3197 2993 3189 19 -168 -450 N -ATOM 316 CA ALA A 42 17.689 4.984 -5.445 1.00 23.64 C -ANISOU 316 CA ALA A 42 3100 2813 3069 17 -240 -480 C -ATOM 317 C ALA A 42 16.292 5.610 -5.542 1.00 21.61 C -ANISOU 317 C ALA A 42 2808 2545 2857 -23 -275 -462 C -ATOM 318 O ALA A 42 15.635 5.514 -6.562 1.00 21.27 O -ANISOU 318 O ALA A 42 2792 2487 2801 -19 -333 -479 O -ATOM 319 CB ALA A 42 17.631 3.640 -4.705 1.00 24.28 C -ANISOU 319 CB ALA A 42 3194 2844 3189 3 -265 -491 C -ATOM 320 N LEU A 43 15.835 6.266 -4.490 1.00 23.95 N -ANISOU 320 N LEU A 43 3046 2853 3202 -55 -241 -428 N -ATOM 321 CA LEU A 43 14.525 6.923 -4.561 1.00 23.43 C -ANISOU 321 CA LEU A 43 2938 2788 3176 -78 -266 -405 C -ATOM 322 C LEU A 43 14.477 8.051 -5.600 1.00 25.55 C -ANISOU 322 C LEU A 43 3222 3081 3404 -54 -272 -405 C -ATOM 323 O LEU A 43 13.404 8.382 -6.112 1.00 26.27 O -ANISOU 323 O LEU A 43 3295 3168 3516 -61 -315 -396 O -ATOM 324 CB LEU A 43 14.135 7.459 -3.186 1.00 21.36 C -ANISOU 324 CB LEU A 43 2617 2539 2958 -96 -217 -370 C -ATOM 325 CG LEU A 43 13.888 6.326 -2.187 1.00 22.05 C -ANISOU 325 CG LEU A 43 2681 2605 3091 -127 -218 -357 C -ATOM 326 CD1 LEU A 43 13.651 6.895 -0.780 1.00 22.55 C -ANISOU 326 CD1 LEU A 43 2698 2693 3179 -131 -158 -322 C -ATOM 327 CD2 LEU A 43 12.691 5.502 -2.651 1.00 23.23 C -ANISOU 327 CD2 LEU A 43 2810 2727 3290 -162 -292 -346 C -ATOM 328 N SER A 44 15.636 8.623 -5.921 1.00 24.34 N -ANISOU 328 N SER A 44 3099 2955 3194 -27 -232 -407 N -ATOM 329 CA SER A 44 15.703 9.735 -6.882 1.00 25.49 C -ANISOU 329 CA SER A 44 3263 3126 3298 -9 -234 -396 C -ATOM 330 C SER A 44 16.151 9.290 -8.289 1.00 25.57 C -ANISOU 330 C SER A 44 3329 3147 3237 26 -262 -420 C -ATOM 331 O SER A 44 16.633 10.089 -9.090 1.00 24.51 O -ANISOU 331 O SER A 44 3217 3046 3051 47 -248 -404 O -ATOM 332 CB SER A 44 16.631 10.837 -6.347 1.00 24.96 C -ANISOU 332 CB SER A 44 3187 3084 3214 -11 -176 -367 C -ATOM 333 OG SER A 44 17.982 10.397 -6.254 1.00 25.90 O -ANISOU 333 OG SER A 44 3318 3226 3295 0 -139 -368 O -ATOM 334 N CYS A 45 15.973 8.009 -8.590 1.00 25.73 N -ANISOU 334 N CYS A 45 3382 3138 3255 35 -306 -457 N -ATOM 335 CA CYS A 45 16.221 7.483 -9.924 1.00 28.87 C -ANISOU 335 CA CYS A 45 3850 3539 3580 80 -345 -490 C -ATOM 336 C CYS A 45 15.409 8.246 -11.006 1.00 25.48 C -ANISOU 336 C CYS A 45 3437 3116 3127 84 -393 -483 C -ATOM 337 O CYS A 45 14.181 8.359 -10.916 1.00 29.48 O -ANISOU 337 O CYS A 45 3914 3596 3691 49 -447 -475 O -ATOM 338 CB CYS A 45 15.888 5.977 -9.940 1.00 31.31 C -ANISOU 338 CB CYS A 45 4200 3790 3904 81 -409 -534 C -ATOM 339 SG CYS A 45 16.136 5.113 -11.498 1.00 40.12 S -ANISOU 339 SG CYS A 45 5432 4891 4923 149 -473 -591 S -ATOM 340 N GLY A 46 16.096 8.798 -12.001 1.00 20.64 N -ANISOU 340 N GLY A 46 2864 2548 2431 127 -370 -476 N -ATOM 341 CA GLY A 46 15.441 9.546 -13.075 1.00 24.61 C -ANISOU 341 CA GLY A 46 3390 3061 2901 136 -414 -464 C -ATOM 342 C GLY A 46 14.996 10.966 -12.729 1.00 24.82 C -ANISOU 342 C GLY A 46 3363 3098 2968 105 -394 -414 C -ATOM 343 O GLY A 46 14.312 11.630 -13.524 1.00 24.14 O -ANISOU 343 O GLY A 46 3291 3014 2867 110 -437 -400 O -ATOM 344 N ALA A 47 15.391 11.441 -11.547 1.00 25.62 N -ANISOU 344 N ALA A 47 3414 3203 3119 78 -335 -388 N -ATOM 345 CA ALA A 47 14.960 12.744 -11.038 1.00 24.58 C -ANISOU 345 CA ALA A 47 3244 3067 3029 55 -321 -348 C -ATOM 346 C ALA A 47 15.420 13.942 -11.872 1.00 22.73 C -ANISOU 346 C ALA A 47 3037 2860 2738 67 -308 -308 C -ATOM 347 O ALA A 47 16.595 14.062 -12.221 1.00 21.00 O -ANISOU 347 O ALA A 47 2836 2679 2462 77 -265 -288 O -ATOM 348 CB ALA A 47 15.452 12.931 -9.575 1.00 18.42 C -ANISOU 348 CB ALA A 47 2423 2280 2296 30 -264 -336 C -ATOM 349 N THR A 48 14.492 14.856 -12.149 1.00 21.02 N -ANISOU 349 N THR A 48 2816 2627 2542 66 -345 -288 N -ATOM 350 CA THR A 48 14.869 16.198 -12.578 1.00 19.89 C -ANISOU 350 CA THR A 48 2694 2494 2369 66 -332 -238 C -ATOM 351 C THR A 48 15.417 16.970 -11.387 1.00 18.83 C -ANISOU 351 C THR A 48 2537 2342 2275 38 -287 -212 C -ATOM 352 O THR A 48 15.182 16.596 -10.232 1.00 16.86 O -ANISOU 352 O THR A 48 2255 2071 2080 28 -271 -235 O -ATOM 353 CB THR A 48 13.693 16.997 -13.120 1.00 21.35 C -ANISOU 353 CB THR A 48 2885 2658 2570 79 -389 -223 C -ATOM 354 OG1 THR A 48 12.778 17.211 -12.049 1.00 20.51 O -ANISOU 354 OG1 THR A 48 2731 2517 2543 75 -395 -231 O -ATOM 355 CG2 THR A 48 12.999 16.275 -14.253 1.00 22.69 C -ANISOU 355 CG2 THR A 48 3079 2837 2706 101 -452 -250 C -ATOM 356 N PRO A 49 16.117 18.075 -11.660 1.00 19.72 N -ANISOU 356 N PRO A 49 2674 2460 2360 23 -273 -161 N -ATOM 357 CA PRO A 49 16.513 18.979 -10.575 1.00 18.39 C -ANISOU 357 CA PRO A 49 2502 2257 2230 -6 -254 -137 C -ATOM 358 C PRO A 49 15.310 19.430 -9.721 1.00 20.53 C -ANISOU 358 C PRO A 49 2763 2476 2563 12 -277 -159 C -ATOM 359 O PRO A 49 15.450 19.578 -8.508 1.00 17.92 O -ANISOU 359 O PRO A 49 2423 2119 2268 2 -256 -169 O -ATOM 360 CB PRO A 49 17.130 20.154 -11.319 1.00 21.89 C -ANISOU 360 CB PRO A 49 2980 2704 2634 -27 -262 -71 C -ATOM 361 CG PRO A 49 17.730 19.490 -12.568 1.00 22.76 C -ANISOU 361 CG PRO A 49 3095 2883 2669 -12 -245 -57 C -ATOM 362 CD PRO A 49 16.699 18.460 -12.955 1.00 20.51 C -ANISOU 362 CD PRO A 49 2808 2599 2384 30 -274 -119 C -ATOM 363 N GLN A 50 14.151 19.649 -10.340 1.00 20.00 N -ANISOU 363 N GLN A 50 2697 2399 2504 43 -320 -164 N -ATOM 364 CA GLN A 50 12.949 19.983 -9.575 1.00 20.20 C -ANISOU 364 CA GLN A 50 2698 2391 2586 75 -335 -180 C -ATOM 365 C GLN A 50 12.592 18.888 -8.566 1.00 20.72 C -ANISOU 365 C GLN A 50 2710 2468 2694 75 -309 -216 C -ATOM 366 O GLN A 50 12.276 19.177 -7.399 1.00 20.84 O -ANISOU 366 O GLN A 50 2710 2463 2746 90 -286 -223 O -ATOM 367 CB GLN A 50 11.769 20.212 -10.515 1.00 21.08 C -ANISOU 367 CB GLN A 50 2804 2505 2701 109 -390 -173 C -ATOM 368 CG GLN A 50 10.480 20.663 -9.807 1.00 24.03 C -ANISOU 368 CG GLN A 50 3142 2857 3132 154 -402 -177 C -ATOM 369 CD GLN A 50 9.294 20.679 -10.742 1.00 25.80 C -ANISOU 369 CD GLN A 50 3341 3095 3367 185 -461 -167 C -ATOM 370 OE1 GLN A 50 8.955 19.664 -11.342 1.00 30.18 O -ANISOU 370 OE1 GLN A 50 3868 3680 3921 169 -491 -182 O -ATOM 371 NE2 GLN A 50 8.671 21.835 -10.888 1.00 27.73 N -ANISOU 371 NE2 GLN A 50 3604 3312 3620 229 -488 -143 N -ATOM 372 N ASP A 51 12.623 17.635 -9.024 1.00 21.47 N -ANISOU 372 N ASP A 51 2784 2594 2781 61 -315 -238 N -ATOM 373 CA ASP A 51 12.328 16.482 -8.162 1.00 20.14 C -ANISOU 373 CA ASP A 51 2567 2431 2652 51 -298 -265 C -ATOM 374 C ASP A 51 13.323 16.385 -7.009 1.00 18.55 C -ANISOU 374 C ASP A 51 2370 2225 2454 33 -243 -270 C -ATOM 375 O ASP A 51 12.946 16.080 -5.878 1.00 19.54 O -ANISOU 375 O ASP A 51 2462 2344 2617 35 -219 -279 O -ATOM 376 CB ASP A 51 12.347 15.166 -8.957 1.00 20.97 C -ANISOU 376 CB ASP A 51 2673 2555 2741 39 -328 -290 C -ATOM 377 CG ASP A 51 11.229 15.078 -9.977 1.00 27.49 C -ANISOU 377 CG ASP A 51 3493 3382 3572 51 -398 -289 C -ATOM 378 OD1 ASP A 51 10.166 15.698 -9.751 1.00 29.14 O -ANISOU 378 OD1 ASP A 51 3663 3584 3824 68 -417 -270 O -ATOM 379 OD2 ASP A 51 11.415 14.382 -11.005 1.00 25.53 O -ANISOU 379 OD2 ASP A 51 3279 3140 3280 50 -436 -308 O -ATOM 380 N LEU A 52 14.594 16.627 -7.308 1.00 16.68 N -ANISOU 380 N LEU A 52 2170 1997 2172 13 -224 -258 N -ATOM 381 CA LEU A 52 15.633 16.602 -6.278 1.00 19.27 C -ANISOU 381 CA LEU A 52 2500 2322 2501 -10 -183 -255 C -ATOM 382 C LEU A 52 15.397 17.679 -5.220 1.00 19.97 C -ANISOU 382 C LEU A 52 2603 2371 2614 -3 -176 -247 C -ATOM 383 O LEU A 52 15.489 17.405 -4.008 1.00 20.43 O -ANISOU 383 O LEU A 52 2649 2420 2692 -5 -150 -261 O -ATOM 384 CB LEU A 52 17.024 16.748 -6.922 1.00 17.61 C -ANISOU 384 CB LEU A 52 2313 2138 2240 -32 -168 -229 C -ATOM 385 CG LEU A 52 17.443 15.538 -7.765 1.00 19.96 C -ANISOU 385 CG LEU A 52 2605 2477 2501 -21 -163 -245 C -ATOM 386 CD1 LEU A 52 18.563 15.859 -8.795 1.00 24.60 C -ANISOU 386 CD1 LEU A 52 3212 3110 3025 -24 -147 -207 C -ATOM 387 CD2 LEU A 52 17.888 14.394 -6.864 1.00 19.68 C -ANISOU 387 CD2 LEU A 52 2545 2446 2485 -27 -135 -272 C -ATOM 388 N ASN A 53 15.059 18.892 -5.650 1.00 19.36 N -ANISOU 388 N ASN A 53 2560 2267 2530 12 -203 -226 N -ATOM 389 CA ASN A 53 14.722 19.934 -4.683 1.00 20.36 C -ANISOU 389 CA ASN A 53 2717 2346 2673 34 -206 -225 C -ATOM 390 C ASN A 53 13.480 19.595 -3.877 1.00 19.38 C -ANISOU 390 C ASN A 53 2553 2225 2585 83 -190 -250 C -ATOM 391 O ASN A 53 13.395 19.887 -2.675 1.00 21.11 O -ANISOU 391 O ASN A 53 2786 2423 2812 106 -168 -262 O -ATOM 392 CB ASN A 53 14.556 21.283 -5.391 1.00 22.94 C -ANISOU 392 CB ASN A 53 3097 2635 2986 46 -246 -197 C -ATOM 393 CG ASN A 53 15.888 21.851 -5.825 1.00 22.26 C -ANISOU 393 CG ASN A 53 3051 2539 2868 -11 -258 -156 C -ATOM 394 OD1 ASN A 53 16.909 21.580 -5.187 1.00 23.81 O -ANISOU 394 OD1 ASN A 53 3245 2740 3060 -51 -238 -153 O -ATOM 395 ND2 ASN A 53 15.903 22.585 -6.936 1.00 19.14 N -ANISOU 395 ND2 ASN A 53 2684 2136 2450 -17 -290 -118 N -ATOM 396 N THR A 54 12.519 18.951 -4.525 1.00 19.00 N -ANISOU 396 N THR A 54 2454 2207 2557 99 -203 -252 N -ATOM 397 CA THR A 54 11.313 18.537 -3.821 1.00 20.49 C -ANISOU 397 CA THR A 54 2585 2415 2787 138 -188 -259 C -ATOM 398 C THR A 54 11.653 17.616 -2.663 1.00 20.61 C -ANISOU 398 C THR A 54 2574 2445 2814 119 -143 -272 C -ATOM 399 O THR A 54 11.173 17.809 -1.531 1.00 20.11 O -ANISOU 399 O THR A 54 2497 2382 2762 157 -110 -273 O -ATOM 400 CB THR A 54 10.314 17.816 -4.759 1.00 19.94 C -ANISOU 400 CB THR A 54 2456 2377 2744 137 -223 -251 C -ATOM 401 OG1 THR A 54 9.774 18.762 -5.684 1.00 21.90 O -ANISOU 401 OG1 THR A 54 2724 2614 2984 168 -265 -235 O -ATOM 402 CG2 THR A 54 9.172 17.225 -3.947 1.00 21.27 C -ANISOU 402 CG2 THR A 54 2544 2575 2961 160 -204 -242 C -ATOM 403 N MET A 55 12.467 16.599 -2.949 1.00 21.22 N -ANISOU 403 N MET A 55 2646 2536 2882 70 -142 -281 N -ATOM 404 CA MET A 55 12.802 15.615 -1.929 1.00 20.78 C -ANISOU 404 CA MET A 55 2565 2491 2837 50 -107 -290 C -ATOM 405 C MET A 55 13.560 16.268 -0.795 1.00 19.56 C -ANISOU 405 C MET A 55 2455 2314 2662 56 -76 -295 C -ATOM 406 O MET A 55 13.299 15.985 0.374 1.00 20.45 O -ANISOU 406 O MET A 55 2553 2434 2785 72 -43 -298 O -ATOM 407 CB MET A 55 13.618 14.467 -2.530 1.00 20.37 C -ANISOU 407 CB MET A 55 2513 2451 2774 8 -117 -301 C -ATOM 408 CG MET A 55 12.830 13.613 -3.532 1.00 22.45 C -ANISOU 408 CG MET A 55 2747 2727 3058 1 -159 -304 C -ATOM 409 SD MET A 55 13.899 12.420 -4.399 1.00 32.84 S -ANISOU 409 SD MET A 55 4092 4046 4338 -25 -176 -327 S -ATOM 410 CE MET A 55 14.339 11.330 -3.041 1.00 27.17 C -ANISOU 410 CE MET A 55 3354 3325 3645 -45 -139 -334 C -ATOM 411 N LEU A 56 14.486 17.165 -1.138 1.00 17.26 N -ANISOU 411 N LEU A 56 2222 1998 2340 41 -93 -291 N -ATOM 412 CA LEU A 56 15.280 17.836 -0.122 1.00 18.54 C -ANISOU 412 CA LEU A 56 2434 2127 2481 36 -84 -293 C -ATOM 413 C LEU A 56 14.394 18.751 0.730 1.00 20.92 C -ANISOU 413 C LEU A 56 2766 2401 2783 98 -78 -303 C -ATOM 414 O LEU A 56 14.574 18.850 1.960 1.00 24.21 O -ANISOU 414 O LEU A 56 3209 2803 3185 115 -57 -316 O -ATOM 415 CB LEU A 56 16.430 18.630 -0.768 1.00 19.04 C -ANISOU 415 CB LEU A 56 2545 2169 2519 -6 -115 -273 C -ATOM 416 CG LEU A 56 17.542 17.817 -1.460 1.00 23.05 C -ANISOU 416 CG LEU A 56 3027 2715 3014 -55 -109 -258 C -ATOM 417 CD1 LEU A 56 18.589 18.749 -2.068 1.00 21.90 C -ANISOU 417 CD1 LEU A 56 2917 2559 2846 -95 -135 -219 C -ATOM 418 CD2 LEU A 56 18.218 16.833 -0.508 1.00 22.26 C -ANISOU 418 CD2 LEU A 56 2906 2634 2919 -73 -81 -269 C -ATOM 419 N ASN A 57 13.432 19.404 0.076 1.00 18.24 N -ANISOU 419 N ASN A 57 2423 2055 2453 140 -96 -296 N -ATOM 420 CA ASN A 57 12.530 20.321 0.749 1.00 18.55 C -ANISOU 420 CA ASN A 57 2491 2071 2488 219 -89 -304 C -ATOM 421 C ASN A 57 11.515 19.636 1.673 1.00 19.81 C -ANISOU 421 C ASN A 57 2587 2278 2664 270 -37 -305 C -ATOM 422 O ASN A 57 10.964 20.288 2.572 1.00 20.25 O -ANISOU 422 O ASN A 57 2671 2323 2701 346 -14 -315 O -ATOM 423 CB ASN A 57 11.775 21.183 -0.278 1.00 18.71 C -ANISOU 423 CB ASN A 57 2519 2074 2514 256 -126 -291 C -ATOM 424 CG ASN A 57 12.591 22.381 -0.765 1.00 20.04 C -ANISOU 424 CG ASN A 57 2780 2176 2657 233 -176 -283 C -ATOM 425 OD1 ASN A 57 13.472 22.878 -0.058 1.00 21.58 O -ANISOU 425 OD1 ASN A 57 3044 2324 2829 212 -187 -292 O -ATOM 426 ND2 ASN A 57 12.289 22.857 -1.985 1.00 20.98 N -ANISOU 426 ND2 ASN A 57 2902 2290 2782 232 -214 -261 N -ATOM 427 N THR A 58 11.243 18.346 1.462 1.00 20.06 N -ANISOU 427 N THR A 58 2535 2361 2728 233 -21 -292 N -ATOM 428 CA THR A 58 10.217 17.708 2.275 1.00 24.09 C -ANISOU 428 CA THR A 58 2972 2922 3261 272 26 -276 C -ATOM 429 C THR A 58 10.800 17.282 3.609 1.00 26.38 C -ANISOU 429 C THR A 58 3284 3214 3526 268 68 -286 C -ATOM 430 O THR A 58 10.060 16.875 4.506 1.00 28.83 O -ANISOU 430 O THR A 58 3546 3567 3841 307 117 -268 O -ATOM 431 CB THR A 58 9.543 16.483 1.586 1.00 27.95 C -ANISOU 431 CB THR A 58 3362 3456 3800 229 15 -249 C -ATOM 432 OG1 THR A 58 10.525 15.531 1.171 1.00 23.34 O -ANISOU 432 OG1 THR A 58 2789 2863 3218 152 -5 -261 O -ATOM 433 CG2 THR A 58 8.706 16.924 0.386 1.00 31.26 C -ANISOU 433 CG2 THR A 58 3752 3882 4244 246 -29 -235 C -ATOM 434 N VAL A 59 12.118 17.398 3.744 1.00 24.05 N -ANISOU 434 N VAL A 59 3057 2879 3202 222 50 -307 N -ATOM 435 CA VAL A 59 12.770 17.191 5.035 1.00 27.23 C -ANISOU 435 CA VAL A 59 3499 3276 3573 222 77 -319 C -ATOM 436 C VAL A 59 12.463 18.353 5.978 1.00 24.30 C -ANISOU 436 C VAL A 59 3202 2876 3157 304 90 -338 C -ATOM 437 O VAL A 59 12.793 19.511 5.697 1.00 26.10 O -ANISOU 437 O VAL A 59 3510 3046 3363 320 48 -356 O -ATOM 438 CB VAL A 59 14.307 17.050 4.916 1.00 27.53 C -ANISOU 438 CB VAL A 59 3583 3282 3596 149 46 -330 C -ATOM 439 CG1 VAL A 59 14.911 16.801 6.295 1.00 28.82 C -ANISOU 439 CG1 VAL A 59 3783 3440 3727 150 67 -340 C -ATOM 440 CG2 VAL A 59 14.686 15.931 3.948 1.00 27.48 C -ANISOU 440 CG2 VAL A 59 3518 3302 3622 85 35 -318 C -ATOM 441 N GLY A 60 11.836 18.030 7.100 1.00 24.85 N -ANISOU 441 N GLY A 60 3250 2983 3208 361 145 -331 N -ATOM 442 CA GLY A 60 11.426 19.023 8.070 1.00 27.28 C -ANISOU 442 CA GLY A 60 3632 3273 3461 462 167 -352 C -ATOM 443 C GLY A 60 12.535 19.449 9.021 1.00 30.67 C -ANISOU 443 C GLY A 60 4175 3645 3831 453 143 -387 C -ATOM 444 O GLY A 60 12.722 20.637 9.258 1.00 31.52 O -ANISOU 444 O GLY A 60 4391 3687 3897 500 106 -419 O -ATOM 445 N GLY A 61 13.274 18.497 9.576 1.00 30.34 N -ANISOU 445 N GLY A 61 4117 3622 3787 393 154 -380 N -ATOM 446 CA GLY A 61 14.274 18.866 10.577 1.00 32.78 C -ANISOU 446 CA GLY A 61 4531 3883 4039 387 126 -409 C -ATOM 447 C GLY A 61 15.651 19.078 9.971 1.00 27.51 C -ANISOU 447 C GLY A 61 3903 3161 3389 288 52 -415 C -ATOM 448 O GLY A 61 15.760 19.453 8.804 1.00 25.93 O -ANISOU 448 O GLY A 61 3686 2941 3224 251 17 -406 O -ATOM 449 N HIS A 62 16.691 18.844 10.769 1.00 23.52 N -ANISOU 449 N HIS A 62 3443 2637 2856 246 28 -422 N -ATOM 450 CA HIS A 62 18.062 18.791 10.265 1.00 23.56 C -ANISOU 450 CA HIS A 62 3453 2614 2883 146 -32 -411 C -ATOM 451 C HIS A 62 18.477 20.000 9.432 1.00 19.90 C -ANISOU 451 C HIS A 62 3046 2086 2429 116 -102 -412 C -ATOM 452 O HIS A 62 19.177 19.846 8.440 1.00 17.90 O -ANISOU 452 O HIS A 62 2747 1840 2213 41 -127 -384 O -ATOM 453 CB HIS A 62 18.233 17.526 9.416 1.00 24.92 C -ANISOU 453 CB HIS A 62 3511 2847 3112 88 -3 -380 C -ATOM 454 CG HIS A 62 17.817 16.274 10.116 1.00 27.58 C -ANISOU 454 CG HIS A 62 3790 3239 3451 104 56 -369 C -ATOM 455 ND1 HIS A 62 18.478 15.787 11.224 1.00 33.17 N -ANISOU 455 ND1 HIS A 62 4525 3950 4128 93 57 -370 N -ATOM 456 CD2 HIS A 62 16.810 15.404 9.865 1.00 30.15 C -ANISOU 456 CD2 HIS A 62 4033 3617 3808 125 109 -350 C -ATOM 457 CE1 HIS A 62 17.894 14.673 11.627 1.00 32.71 C -ANISOU 457 CE1 HIS A 62 4405 3943 4081 107 113 -350 C -ATOM 458 NE2 HIS A 62 16.879 14.419 10.820 1.00 31.76 N -ANISOU 458 NE2 HIS A 62 4216 3851 4001 123 143 -337 N -ATOM 459 N GLN A 63 18.028 21.192 9.812 1.00 21.83 N -ANISOU 459 N GLN A 63 3392 2268 2636 179 -132 -440 N -ATOM 460 CA GLN A 63 18.251 22.364 8.976 1.00 22.91 C -ANISOU 460 CA GLN A 63 3585 2336 2784 155 -200 -436 C -ATOM 461 C GLN A 63 19.717 22.858 8.996 1.00 22.24 C -ANISOU 461 C GLN A 63 3555 2193 2700 54 -289 -417 C -ATOM 462 O GLN A 63 20.152 23.571 8.090 1.00 20.23 O -ANISOU 462 O GLN A 63 3315 1900 2472 -2 -344 -389 O -ATOM 463 CB GLN A 63 17.281 23.472 9.397 1.00 24.08 C -ANISOU 463 CB GLN A 63 3833 2427 2890 265 -209 -474 C -ATOM 464 CG GLN A 63 15.843 23.125 8.981 1.00 23.53 C -ANISOU 464 CG GLN A 63 3681 2423 2837 352 -130 -471 C -ATOM 465 CD GLN A 63 15.758 22.937 7.474 1.00 27.28 C -ANISOU 465 CD GLN A 63 4068 2924 3373 295 -135 -434 C -ATOM 466 OE1 GLN A 63 16.039 23.870 6.708 1.00 28.42 O -ANISOU 466 OE1 GLN A 63 4263 3008 3527 268 -196 -425 O -ATOM 467 NE2 GLN A 63 15.422 21.720 7.035 1.00 24.19 N -ANISOU 467 NE2 GLN A 63 3554 2617 3019 272 -78 -411 N -ATOM 468 N ALA A 64 20.475 22.486 10.024 1.00 21.50 N -ANISOU 468 N ALA A 64 3490 2097 2581 27 -306 -425 N -ATOM 469 CA ALA A 64 21.914 22.738 9.994 1.00 21.77 C -ANISOU 469 CA ALA A 64 3543 2098 2630 -82 -388 -392 C -ATOM 470 C ALA A 64 22.534 21.953 8.836 1.00 22.98 C -ANISOU 470 C ALA A 64 3565 2324 2840 -160 -361 -337 C -ATOM 471 O ALA A 64 23.230 22.517 7.995 1.00 22.29 O -ANISOU 471 O ALA A 64 3470 2219 2781 -233 -412 -293 O -ATOM 472 CB ALA A 64 22.570 22.363 11.336 1.00 20.34 C -ANISOU 472 CB ALA A 64 3406 1911 2411 -92 -411 -408 C -ATOM 473 N ALA A 65 22.259 20.655 8.783 1.00 24.55 N -ANISOU 473 N ALA A 65 3669 2607 3053 -140 -282 -336 N -ATOM 474 CA ALA A 65 22.721 19.843 7.668 1.00 22.30 C -ANISOU 474 CA ALA A 65 3272 2390 2810 -190 -251 -296 C -ATOM 475 C ALA A 65 22.294 20.423 6.338 1.00 22.60 C -ANISOU 475 C ALA A 65 3294 2423 2869 -192 -254 -277 C -ATOM 476 O ALA A 65 23.090 20.470 5.412 1.00 23.26 O -ANISOU 476 O ALA A 65 3333 2529 2973 -254 -272 -231 O -ATOM 477 CB ALA A 65 22.213 18.427 7.794 1.00 17.98 C -ANISOU 477 CB ALA A 65 2648 1913 2272 -153 -174 -308 C -ATOM 478 N MET A 66 21.037 20.852 6.237 1.00 18.11 N -ANISOU 478 N MET A 66 2757 1833 2293 -119 -234 -308 N -ATOM 479 CA MET A 66 20.516 21.306 4.942 1.00 19.12 C -ANISOU 479 CA MET A 66 2864 1961 2439 -114 -235 -291 C -ATOM 480 C MET A 66 21.221 22.557 4.514 1.00 20.07 C -ANISOU 480 C MET A 66 3050 2017 2560 -170 -312 -258 C -ATOM 481 O MET A 66 21.448 22.761 3.321 1.00 21.50 O -ANISOU 481 O MET A 66 3196 2216 2759 -207 -320 -217 O -ATOM 482 CB MET A 66 18.994 21.544 4.993 1.00 17.06 C -ANISOU 482 CB MET A 66 2619 1692 2172 -19 -202 -326 C -ATOM 483 CG MET A 66 18.177 20.260 5.125 1.00 22.00 C -ANISOU 483 CG MET A 66 3157 2390 2810 22 -128 -339 C -ATOM 484 SD MET A 66 18.595 18.980 3.902 1.00 29.34 S -ANISOU 484 SD MET A 66 3979 3392 3775 -34 -103 -310 S -ATOM 485 CE MET A 66 20.004 18.204 4.693 1.00 48.19 C -ANISOU 485 CE MET A 66 6355 5798 6155 -92 -103 -300 C -ATOM 486 N GLN A 67 21.563 23.416 5.472 1.00 17.48 N -ANISOU 486 N GLN A 67 2822 1611 2209 -177 -374 -273 N -ATOM 487 CA GLN A 67 22.300 24.609 5.087 1.00 20.95 C -ANISOU 487 CA GLN A 67 3327 1978 2656 -246 -463 -232 C -ATOM 488 C GLN A 67 23.719 24.241 4.618 1.00 23.08 C -ANISOU 488 C GLN A 67 3522 2297 2951 -357 -482 -162 C -ATOM 489 O GLN A 67 24.236 24.839 3.675 1.00 23.67 O -ANISOU 489 O GLN A 67 3584 2365 3045 -421 -518 -101 O -ATOM 490 CB GLN A 67 22.351 25.641 6.240 1.00 24.29 C -ANISOU 490 CB GLN A 67 3894 2290 3046 -230 -543 -268 C -ATOM 491 CG GLN A 67 23.307 26.780 5.969 1.00 27.82 C -ANISOU 491 CG GLN A 67 4410 2654 3507 -327 -654 -216 C -ATOM 492 CD GLN A 67 22.884 27.646 4.802 1.00 32.59 C -ANISOU 492 CD GLN A 67 5033 3221 4129 -330 -678 -184 C -ATOM 493 OE1 GLN A 67 21.712 27.682 4.435 1.00 32.60 O -ANISOU 493 OE1 GLN A 67 5036 3230 4122 -237 -629 -219 O -ATOM 494 NE2 GLN A 67 23.839 28.363 4.219 1.00 33.66 N -ANISOU 494 NE2 GLN A 67 5180 3320 4291 -440 -756 -108 N -ATOM 495 N MET A 68 24.347 23.262 5.268 1.00 24.43 N -ANISOU 495 N MET A 68 3638 2522 3122 -375 -455 -164 N -ATOM 496 CA MET A 68 25.644 22.775 4.807 1.00 22.84 C -ANISOU 496 CA MET A 68 3347 2386 2944 -461 -458 -96 C -ATOM 497 C MET A 68 25.541 22.195 3.392 1.00 21.75 C -ANISOU 497 C MET A 68 3112 2332 2820 -455 -394 -63 C -ATOM 498 O MET A 68 26.422 22.399 2.555 1.00 19.27 O -ANISOU 498 O MET A 68 2746 2055 2519 -520 -407 10 O -ATOM 499 CB MET A 68 26.198 21.723 5.764 1.00 21.94 C -ANISOU 499 CB MET A 68 3193 2318 2826 -461 -435 -111 C -ATOM 500 CG MET A 68 26.737 22.301 7.047 1.00 27.25 C -ANISOU 500 CG MET A 68 3952 2919 3482 -494 -517 -122 C -ATOM 501 SD MET A 68 27.847 21.145 7.862 1.00 44.78 S -ANISOU 501 SD MET A 68 6099 5207 5706 -529 -508 -102 S -ATOM 502 CE MET A 68 26.676 19.981 8.473 1.00 21.35 C -ANISOU 502 CE MET A 68 3127 2274 2713 -418 -411 -179 C -ATOM 503 N LEU A 69 24.465 21.462 3.130 1.00 22.30 N -ANISOU 503 N LEU A 69 3156 2433 2882 -376 -325 -112 N -ATOM 504 CA LEU A 69 24.230 20.941 1.796 1.00 23.89 C -ANISOU 504 CA LEU A 69 3288 2701 3089 -361 -275 -92 C -ATOM 505 C LEU A 69 24.100 22.077 0.758 1.00 24.96 C -ANISOU 505 C LEU A 69 3454 2804 3224 -385 -312 -51 C -ATOM 506 O LEU A 69 24.646 21.994 -0.352 1.00 22.26 O -ANISOU 506 O LEU A 69 3058 2519 2880 -416 -298 5 O -ATOM 507 CB LEU A 69 22.980 20.042 1.805 1.00 22.40 C -ANISOU 507 CB LEU A 69 3078 2535 2897 -279 -216 -153 C -ATOM 508 CG LEU A 69 22.570 19.376 0.484 1.00 23.01 C -ANISOU 508 CG LEU A 69 3096 2671 2974 -254 -174 -148 C -ATOM 509 CD1 LEU A 69 23.731 18.568 -0.124 1.00 20.62 C -ANISOU 509 CD1 LEU A 69 2724 2444 2665 -286 -149 -107 C -ATOM 510 CD2 LEU A 69 21.362 18.471 0.733 1.00 23.90 C -ANISOU 510 CD2 LEU A 69 3191 2796 3094 -189 -133 -202 C -ATOM 511 N LYS A 70 23.375 23.136 1.107 1.00 25.34 N -ANISOU 511 N LYS A 70 3593 2764 3269 -362 -358 -75 N -ATOM 512 CA LYS A 70 23.246 24.281 0.211 1.00 26.68 C -ANISOU 512 CA LYS A 70 3807 2890 3441 -385 -404 -33 C -ATOM 513 C LYS A 70 24.603 24.891 -0.122 1.00 27.44 C -ANISOU 513 C LYS A 70 3893 2985 3548 -492 -458 56 C -ATOM 514 O LYS A 70 24.856 25.314 -1.265 1.00 24.36 O -ANISOU 514 O LYS A 70 3480 2618 3159 -528 -463 121 O -ATOM 515 CB LYS A 70 22.367 25.369 0.824 1.00 25.42 C -ANISOU 515 CB LYS A 70 3762 2622 3275 -338 -456 -76 C -ATOM 516 CG LYS A 70 20.897 25.085 0.760 1.00 26.64 C -ANISOU 516 CG LYS A 70 3917 2784 3422 -233 -408 -137 C -ATOM 517 CD LYS A 70 20.161 26.360 1.177 1.00 30.09 C -ANISOU 517 CD LYS A 70 4471 3113 3848 -181 -465 -165 C -ATOM 518 CE LYS A 70 18.679 26.176 1.155 1.00 27.63 C -ANISOU 518 CE LYS A 70 4151 2816 3531 -69 -418 -215 C -ATOM 519 NZ LYS A 70 18.056 27.335 1.877 1.00 26.52 N -ANISOU 519 NZ LYS A 70 4132 2573 3371 2 -466 -252 N -ATOM 520 N GLU A 71 25.471 24.942 0.883 1.00 24.74 N -ANISOU 520 N GLU A 71 3566 2620 3215 -545 -499 65 N -ATOM 521 CA GLU A 71 26.796 25.540 0.710 1.00 25.75 C -ANISOU 521 CA GLU A 71 3676 2746 3362 -659 -562 160 C -ATOM 522 C GLU A 71 27.652 24.677 -0.220 1.00 26.10 C -ANISOU 522 C GLU A 71 3587 2922 3409 -688 -496 229 C -ATOM 523 O GLU A 71 28.382 25.203 -1.075 1.00 26.84 O -ANISOU 523 O GLU A 71 3642 3045 3509 -759 -515 326 O -ATOM 524 CB GLU A 71 27.477 25.760 2.077 1.00 23.89 C -ANISOU 524 CB GLU A 71 3490 2453 3136 -707 -633 150 C -ATOM 525 CG GLU A 71 26.920 27.011 2.795 1.00 29.20 C -ANISOU 525 CG GLU A 71 4318 2978 3800 -698 -728 109 C -ATOM 526 CD GLU A 71 27.631 27.392 4.104 1.00 36.06 C -ANISOU 526 CD GLU A 71 5262 3771 4669 -752 -822 100 C -ATOM 527 OE1 GLU A 71 28.755 26.913 4.377 1.00 38.31 O -ANISOU 527 OE1 GLU A 71 5471 4113 4972 -827 -835 152 O -ATOM 528 OE2 GLU A 71 27.042 28.190 4.873 1.00 37.57 O -ANISOU 528 OE2 GLU A 71 5594 3845 4837 -712 -887 39 O -ATOM 529 N THR A 72 27.534 23.360 -0.078 1.00 22.40 N -ANISOU 529 N THR A 72 3051 2531 2928 -628 -417 183 N -ATOM 530 CA THR A 72 28.214 22.427 -0.974 1.00 21.34 C -ANISOU 530 CA THR A 72 2804 2520 2784 -624 -346 231 C -ATOM 531 C THR A 72 27.691 22.552 -2.404 1.00 21.72 C -ANISOU 531 C THR A 72 2840 2605 2809 -592 -308 252 C -ATOM 532 O THR A 72 28.463 22.604 -3.365 1.00 25.13 O -ANISOU 532 O THR A 72 3207 3113 3228 -626 -287 336 O -ATOM 533 CB THR A 72 28.050 20.958 -0.493 1.00 22.82 C -ANISOU 533 CB THR A 72 2945 2763 2963 -555 -279 164 C -ATOM 534 OG1 THR A 72 28.777 20.774 0.732 1.00 23.44 O -ANISOU 534 OG1 THR A 72 3020 2827 3058 -591 -312 164 O -ATOM 535 CG2 THR A 72 28.587 20.003 -1.539 1.00 20.70 C -ANISOU 535 CG2 THR A 72 2581 2610 2673 -526 -207 200 C -ATOM 536 N ILE A 73 26.374 22.585 -2.552 1.00 24.64 N -ANISOU 536 N ILE A 73 3265 2928 3169 -524 -299 179 N -ATOM 537 CA ILE A 73 25.760 22.803 -3.865 1.00 24.77 C -ANISOU 537 CA ILE A 73 3285 2966 3162 -492 -278 194 C -ATOM 538 C ILE A 73 26.248 24.102 -4.539 1.00 27.08 C -ANISOU 538 C ILE A 73 3602 3232 3456 -566 -331 289 C -ATOM 539 O ILE A 73 26.582 24.116 -5.731 1.00 26.95 O -ANISOU 539 O ILE A 73 3543 3285 3413 -575 -302 354 O -ATOM 540 CB ILE A 73 24.231 22.819 -3.745 1.00 20.23 C -ANISOU 540 CB ILE A 73 2768 2333 2587 -416 -278 109 C -ATOM 541 CG1 ILE A 73 23.726 21.407 -3.409 1.00 21.05 C -ANISOU 541 CG1 ILE A 73 2830 2480 2687 -350 -220 35 C -ATOM 542 CG2 ILE A 73 23.573 23.350 -5.041 1.00 24.13 C -ANISOU 542 CG2 ILE A 73 3281 2827 3060 -394 -283 132 C -ATOM 543 CD1 ILE A 73 22.311 21.351 -2.913 1.00 19.89 C -ANISOU 543 CD1 ILE A 73 2724 2282 2552 -284 -221 -40 C -ATOM 544 N ASN A 74 26.290 25.192 -3.788 1.00 25.30 N -ANISOU 544 N ASN A 74 3452 2902 3257 -618 -412 299 N -ATOM 545 CA ASN A 74 26.739 26.446 -4.356 1.00 29.04 C -ANISOU 545 CA ASN A 74 3959 3333 3740 -698 -477 393 C -ATOM 546 C ASN A 74 28.202 26.381 -4.788 1.00 29.03 C -ANISOU 546 C ASN A 74 3864 3422 3743 -788 -469 512 C -ATOM 547 O ASN A 74 28.571 26.996 -5.788 1.00 26.98 O -ANISOU 547 O ASN A 74 3587 3191 3474 -836 -477 609 O -ATOM 548 CB ASN A 74 26.520 27.594 -3.372 1.00 33.54 C -ANISOU 548 CB ASN A 74 4647 3760 4338 -732 -579 373 C -ATOM 549 CG ASN A 74 25.041 27.939 -3.194 1.00 39.87 C -ANISOU 549 CG ASN A 74 5542 4477 5129 -636 -588 280 C -ATOM 550 OD1 ASN A 74 24.229 27.755 -4.104 1.00 40.96 O -ANISOU 550 OD1 ASN A 74 5666 4648 5248 -574 -546 265 O -ATOM 551 ND2 ASN A 74 24.689 28.440 -2.015 1.00 42.87 N -ANISOU 551 ND2 ASN A 74 6019 4752 5519 -617 -646 219 N -ATOM 552 N GLU A 75 29.024 25.637 -4.042 1.00 25.16 N -ANISOU 552 N GLU A 75 3309 2983 3266 -807 -450 512 N -ATOM 553 CA GLU A 75 30.434 25.446 -4.385 1.00 29.10 C -ANISOU 553 CA GLU A 75 3698 3586 3771 -881 -432 627 C -ATOM 554 C GLU A 75 30.569 24.693 -5.711 1.00 27.97 C -ANISOU 554 C GLU A 75 3468 3579 3580 -823 -331 663 C -ATOM 555 O GLU A 75 31.357 25.080 -6.570 1.00 29.30 O -ANISOU 555 O GLU A 75 3574 3821 3737 -877 -319 783 O -ATOM 556 CB GLU A 75 31.186 24.667 -3.283 1.00 31.66 C -ANISOU 556 CB GLU A 75 3970 3943 4117 -892 -429 607 C -ATOM 557 CG GLU A 75 31.391 25.403 -1.961 1.00 39.17 C -ANISOU 557 CG GLU A 75 4999 4777 5109 -964 -538 593 C -ATOM 558 CD GLU A 75 31.749 24.465 -0.796 1.00 44.19 C -ANISOU 558 CD GLU A 75 5605 5433 5753 -941 -526 537 C -ATOM 559 OE1 GLU A 75 31.963 23.255 -1.029 1.00 46.15 O -ANISOU 559 OE1 GLU A 75 5764 5787 5982 -879 -437 521 O -ATOM 560 OE2 GLU A 75 31.799 24.934 0.361 1.00 46.14 O -ANISOU 560 OE2 GLU A 75 5928 5583 6019 -980 -611 506 O -ATOM 561 N GLU A 76 29.803 23.612 -5.864 1.00 24.61 N -ANISOU 561 N GLU A 76 3041 3186 3122 -713 -261 563 N -ATOM 562 CA GLU A 76 29.858 22.801 -7.086 1.00 26.48 C -ANISOU 562 CA GLU A 76 3218 3541 3302 -643 -173 577 C -ATOM 563 C GLU A 76 29.337 23.572 -8.297 1.00 22.46 C -ANISOU 563 C GLU A 76 2748 3026 2760 -641 -178 620 C -ATOM 564 O GLU A 76 29.845 23.430 -9.408 1.00 26.06 O -ANISOU 564 O GLU A 76 3148 3586 3167 -628 -125 696 O -ATOM 565 CB GLU A 76 29.073 21.495 -6.891 1.00 28.23 C -ANISOU 565 CB GLU A 76 3450 3774 3504 -535 -120 454 C -ATOM 566 CG GLU A 76 29.657 20.583 -5.804 1.00 29.15 C -ANISOU 566 CG GLU A 76 3520 3910 3644 -528 -105 420 C -ATOM 567 CD GLU A 76 31.154 20.279 -6.025 1.00 34.98 C -ANISOU 567 CD GLU A 76 4151 4766 4375 -558 -68 521 C -ATOM 568 OE1 GLU A 76 31.519 19.704 -7.077 1.00 34.76 O -ANISOU 568 OE1 GLU A 76 4068 4845 4294 -502 2 555 O -ATOM 569 OE2 GLU A 76 31.963 20.619 -5.142 1.00 35.63 O -ANISOU 569 OE2 GLU A 76 4203 4836 4501 -634 -112 569 O -ATOM 570 N ALA A 77 28.347 24.425 -8.066 1.00 21.75 N -ANISOU 570 N ALA A 77 2755 2816 2692 -649 -243 577 N -ATOM 571 CA ALA A 77 27.750 25.219 -9.134 1.00 26.43 C -ANISOU 571 CA ALA A 77 3397 3388 3258 -645 -260 613 C -ATOM 572 C ALA A 77 28.711 26.325 -9.594 1.00 28.08 C -ANISOU 572 C ALA A 77 3586 3607 3476 -753 -300 761 C -ATOM 573 O ALA A 77 28.805 26.631 -10.792 1.00 29.92 O -ANISOU 573 O ALA A 77 3805 3899 3666 -754 -275 839 O -ATOM 574 CB ALA A 77 26.421 25.825 -8.670 1.00 25.24 C -ANISOU 574 CB ALA A 77 3353 3104 3132 -614 -321 527 C -ATOM 575 N ALA A 78 29.413 26.926 -8.641 1.00 28.00 N -ANISOU 575 N ALA A 78 3579 3539 3521 -848 -367 805 N -ATOM 576 CA ALA A 78 30.449 27.894 -8.978 1.00 31.65 C -ANISOU 576 CA ALA A 78 4007 4015 4003 -970 -413 959 C -ATOM 577 C ALA A 78 31.531 27.250 -9.840 1.00 32.30 C -ANISOU 577 C ALA A 78 3953 4274 4046 -973 -322 1065 C -ATOM 578 O ALA A 78 32.001 27.847 -10.808 1.00 34.36 O -ANISOU 578 O ALA A 78 4180 4592 4285 -1023 -314 1193 O -ATOM 579 CB ALA A 78 31.057 28.489 -7.717 1.00 34.10 C -ANISOU 579 CB ALA A 78 4342 4233 4381 -1072 -510 979 C -ATOM 580 N GLU A 79 31.915 26.025 -9.490 1.00 33.66 N -ANISOU 580 N GLU A 79 4050 4535 4205 -911 -250 1015 N -ATOM 581 CA GLU A 79 32.938 25.297 -10.238 1.00 32.92 C -ANISOU 581 CA GLU A 79 3827 4616 4065 -887 -154 1104 C -ATOM 582 C GLU A 79 32.429 24.888 -11.624 1.00 30.86 C -ANISOU 582 C GLU A 79 3572 4437 3716 -786 -73 1094 C -ATOM 583 O GLU A 79 33.165 25.000 -12.597 1.00 30.37 O -ANISOU 583 O GLU A 79 3436 4496 3607 -795 -18 1216 O -ATOM 584 CB GLU A 79 33.413 24.073 -9.449 1.00 35.20 C -ANISOU 584 CB GLU A 79 4049 4963 4362 -834 -107 1041 C -ATOM 585 CG GLU A 79 34.328 23.122 -10.219 1.00 40.19 C -ANISOU 585 CG GLU A 79 4559 5776 4935 -767 4 1104 C -ATOM 586 CD GLU A 79 35.750 23.669 -10.452 1.00 42.86 C -ANISOU 586 CD GLU A 79 4772 6223 5292 -866 9 1290 C -ATOM 587 OE1 GLU A 79 36.097 24.757 -9.934 1.00 40.72 O -ANISOU 587 OE1 GLU A 79 4507 5876 5088 -1004 -88 1372 O -ATOM 588 OE2 GLU A 79 36.523 22.995 -11.164 1.00 45.99 O -ANISOU 588 OE2 GLU A 79 5061 6781 5632 -804 107 1358 O -ATOM 589 N TRP A 80 31.176 24.431 -11.717 1.00 29.38 N -ANISOU 589 N TRP A 80 3472 4187 3504 -692 -67 957 N -ATOM 590 CA TRP A 80 30.554 24.197 -13.025 1.00 30.15 C -ANISOU 590 CA TRP A 80 3600 4337 3520 -606 -17 943 C -ATOM 591 C TRP A 80 30.682 25.428 -13.933 1.00 32.16 C -ANISOU 591 C TRP A 80 3871 4593 3757 -676 -46 1071 C -ATOM 592 O TRP A 80 31.053 25.307 -15.107 1.00 35.00 O -ANISOU 592 O TRP A 80 4190 5069 4039 -641 20 1149 O -ATOM 593 CB TRP A 80 29.069 23.815 -12.880 1.00 29.25 C -ANISOU 593 CB TRP A 80 3585 4127 3404 -525 -41 790 C -ATOM 594 CG TRP A 80 28.392 23.589 -14.216 1.00 30.13 C -ANISOU 594 CG TRP A 80 3733 4282 3432 -442 -7 773 C -ATOM 595 CD1 TRP A 80 27.702 24.507 -14.959 1.00 31.20 C -ANISOU 595 CD1 TRP A 80 3935 4369 3549 -455 -49 803 C -ATOM 596 CD2 TRP A 80 28.346 22.361 -14.950 1.00 29.57 C -ANISOU 596 CD2 TRP A 80 3645 4308 3282 -331 67 720 C -ATOM 597 NE1 TRP A 80 27.225 23.921 -16.116 1.00 33.00 N -ANISOU 597 NE1 TRP A 80 4185 4663 3690 -361 -6 773 N -ATOM 598 CE2 TRP A 80 27.616 22.605 -16.134 1.00 31.83 C -ANISOU 598 CE2 TRP A 80 3992 4602 3501 -284 64 720 C -ATOM 599 CE3 TRP A 80 28.852 21.073 -14.719 1.00 30.60 C -ANISOU 599 CE3 TRP A 80 3725 4512 3388 -262 130 670 C -ATOM 600 CZ2 TRP A 80 27.386 21.614 -17.088 1.00 30.84 C -ANISOU 600 CZ2 TRP A 80 3883 4553 3282 -173 116 669 C -ATOM 601 CZ3 TRP A 80 28.617 20.087 -15.672 1.00 32.24 C -ANISOU 601 CZ3 TRP A 80 3953 4792 3505 -147 183 619 C -ATOM 602 CH2 TRP A 80 27.892 20.367 -16.841 1.00 29.77 C -ANISOU 602 CH2 TRP A 80 3706 4482 3123 -106 173 617 C -ATOM 603 N ASP A 81 30.382 26.606 -13.388 1.00 30.99 N -ANISOU 603 N ASP A 81 3789 4312 3675 -769 -145 1093 N -ATOM 604 CA ASP A 81 30.416 27.848 -14.159 1.00 33.55 C -ANISOU 604 CA ASP A 81 4146 4609 3992 -843 -191 1213 C -ATOM 605 C ASP A 81 31.816 28.231 -14.590 1.00 36.20 C -ANISOU 605 C ASP A 81 4374 5058 4323 -937 -165 1396 C -ATOM 606 O ASP A 81 31.996 28.877 -15.621 1.00 38.43 O -ANISOU 606 O ASP A 81 4651 5387 4565 -968 -156 1515 O -ATOM 607 CB ASP A 81 29.807 29.000 -13.360 1.00 33.99 C -ANISOU 607 CB ASP A 81 4309 4482 4124 -916 -314 1188 C -ATOM 608 CG ASP A 81 28.322 28.860 -13.198 1.00 33.09 C -ANISOU 608 CG ASP A 81 4299 4268 4006 -821 -337 1037 C -ATOM 609 OD1 ASP A 81 27.721 28.079 -13.968 1.00 29.90 O -ANISOU 609 OD1 ASP A 81 3891 3930 3539 -718 -273 978 O -ATOM 610 OD2 ASP A 81 27.755 29.523 -12.303 1.00 35.42 O -ANISOU 610 OD2 ASP A 81 4679 4419 4359 -846 -423 981 O -ATOM 611 N ARG A 82 32.801 27.864 -13.782 1.00 38.37 N -ANISOU 611 N ARG A 82 4559 5378 4642 -985 -157 1429 N -ATOM 612 CA ARG A 82 34.191 28.091 -14.140 1.00 41.97 C -ANISOU 612 CA ARG A 82 4885 5965 5098 -1069 -123 1611 C -ATOM 613 C ARG A 82 34.554 27.205 -15.326 1.00 43.49 C -ANISOU 613 C ARG A 82 4994 6347 5183 -958 14 1650 C -ATOM 614 O ARG A 82 35.155 27.663 -16.299 1.00 43.94 O -ANISOU 614 O ARG A 82 4990 6510 5196 -992 54 1804 O -ATOM 615 CB ARG A 82 35.115 27.810 -12.956 1.00 41.85 C -ANISOU 615 CB ARG A 82 4789 5957 5156 -1136 -150 1627 C -ATOM 616 CG ARG A 82 36.588 27.937 -13.289 1.00 46.64 C -ANISOU 616 CG ARG A 82 5236 6717 5767 -1218 -111 1822 C -ATOM 617 CD ARG A 82 37.480 27.504 -12.134 1.00 49.79 C -ANISOU 617 CD ARG A 82 5548 7136 6234 -1267 -135 1829 C -ATOM 618 NE ARG A 82 37.695 26.058 -12.094 1.00 50.45 N -ANISOU 618 NE ARG A 82 5560 7342 6269 -1129 -22 1748 N -ATOM 619 CZ ARG A 82 38.579 25.407 -12.848 1.00 51.99 C -ANISOU 619 CZ ARG A 82 5618 7732 6403 -1067 94 1844 C -ATOM 620 NH1 ARG A 82 39.333 26.067 -13.720 1.00 53.59 N -ANISOU 620 NH1 ARG A 82 5735 8039 6587 -1126 118 2019 N -ATOM 621 NH2 ARG A 82 38.703 24.090 -12.735 1.00 51.41 N -ANISOU 621 NH2 ARG A 82 5502 7744 6285 -932 183 1754 N -ATOM 622 N LEU A 83 34.170 25.936 -15.241 1.00 41.83 N -ANISOU 622 N LEU A 83 4788 6177 4928 -822 83 1510 N -ATOM 623 CA LEU A 83 34.484 24.968 -16.285 1.00 45.62 C -ANISOU 623 CA LEU A 83 5210 6825 5299 -694 208 1522 C -ATOM 624 C LEU A 83 33.670 25.168 -17.569 1.00 45.10 C -ANISOU 624 C LEU A 83 5225 6770 5139 -624 232 1512 C -ATOM 625 O LEU A 83 34.180 24.944 -18.664 1.00 46.00 O -ANISOU 625 O LEU A 83 5288 7034 5157 -565 321 1600 O -ATOM 626 CB LEU A 83 34.274 23.548 -15.757 1.00 46.98 C -ANISOU 626 CB LEU A 83 5382 7012 5455 -573 256 1368 C -ATOM 627 CG LEU A 83 35.422 22.950 -14.949 1.00 47.85 C -ANISOU 627 CG LEU A 83 5372 7202 5606 -589 288 1407 C -ATOM 628 CD1 LEU A 83 34.989 21.646 -14.304 1.00 45.89 C -ANISOU 628 CD1 LEU A 83 5156 6924 5355 -479 310 1239 C -ATOM 629 CD2 LEU A 83 36.629 22.735 -15.850 1.00 48.44 C -ANISOU 629 CD2 LEU A 83 5314 7480 5609 -556 394 1560 C -ATOM 630 N HIS A 84 32.413 25.584 -17.441 1.00 43.80 N -ANISOU 630 N HIS A 84 5188 6455 4999 -623 153 1408 N -ATOM 631 CA HIS A 84 31.536 25.708 -18.607 1.00 42.96 C -ANISOU 631 CA HIS A 84 5166 6351 4808 -551 164 1384 C -ATOM 632 C HIS A 84 30.791 27.039 -18.637 1.00 43.31 C -ANISOU 632 C HIS A 84 5302 6254 4900 -638 60 1413 C -ATOM 633 O HIS A 84 29.572 27.070 -18.450 1.00 40.80 O -ANISOU 633 O HIS A 84 5086 5818 4600 -597 4 1289 O -ATOM 634 CB HIS A 84 30.511 24.566 -18.640 1.00 39.91 C -ANISOU 634 CB HIS A 84 4850 5933 4380 -415 181 1199 C -ATOM 635 CG HIS A 84 31.093 23.210 -18.383 1.00 40.57 C -ANISOU 635 CG HIS A 84 4869 6113 4433 -326 261 1140 C -ATOM 636 ND1 HIS A 84 31.160 22.656 -17.122 1.00 41.20 N -ANISOU 636 ND1 HIS A 84 4927 6134 4592 -339 239 1056 N -ATOM 637 CD2 HIS A 84 31.621 22.291 -19.225 1.00 42.32 C -ANISOU 637 CD2 HIS A 84 5052 6481 4547 -214 360 1151 C -ATOM 638 CE1 HIS A 84 31.714 21.459 -17.196 1.00 41.56 C -ANISOU 638 CE1 HIS A 84 4921 6283 4588 -244 318 1022 C -ATOM 639 NE2 HIS A 84 32.003 21.213 -18.461 1.00 43.39 N -ANISOU 639 NE2 HIS A 84 5143 6638 4705 -163 392 1075 N -ATOM 640 N PRO A 85 31.510 28.142 -18.884 1.00 47.25 N -ANISOU 640 N PRO A 85 5766 6767 5422 -757 32 1583 N -ATOM 641 CA PRO A 85 30.847 29.453 -18.951 1.00 50.57 C -ANISOU 641 CA PRO A 85 6283 7044 5886 -838 -74 1619 C -ATOM 642 C PRO A 85 29.756 29.482 -20.023 1.00 52.82 C -ANISOU 642 C PRO A 85 6663 7318 6090 -745 -70 1567 C -ATOM 643 O PRO A 85 29.937 28.878 -21.078 1.00 53.11 O -ANISOU 643 O PRO A 85 6669 7492 6018 -660 19 1594 O -ATOM 644 CB PRO A 85 31.993 30.411 -19.307 1.00 50.12 C -ANISOU 644 CB PRO A 85 6152 7047 5844 -972 -82 1836 C -ATOM 645 CG PRO A 85 33.020 29.547 -19.961 1.00 49.60 C -ANISOU 645 CG PRO A 85 5955 7196 5696 -917 50 1918 C -ATOM 646 CD PRO A 85 32.934 28.220 -19.260 1.00 48.20 C -ANISOU 646 CD PRO A 85 5752 7043 5519 -814 100 1761 C -ATOM 647 N VAL A 86 28.638 30.151 -19.752 1.00 54.29 N -ANISOU 647 N VAL A 86 6961 7344 6321 -752 -165 1493 N -ATOM 648 CA VAL A 86 27.580 30.253 -20.752 1.00 57.29 C -ANISOU 648 CA VAL A 86 7427 7708 6632 -670 -175 1452 C -ATOM 649 C VAL A 86 27.621 31.608 -21.434 1.00 60.95 C -ANISOU 649 C VAL A 86 7939 8129 7092 -754 -234 1597 C -ATOM 650 O VAL A 86 27.896 32.629 -20.808 1.00 61.17 O -ANISOU 650 O VAL A 86 7987 8050 7205 -869 -316 1666 O -ATOM 651 CB VAL A 86 26.172 30.026 -20.149 1.00 56.49 C -ANISOU 651 CB VAL A 86 7415 7474 6574 -600 -237 1275 C -ATOM 652 CG1 VAL A 86 26.109 28.673 -19.451 1.00 55.26 C -ANISOU 652 CG1 VAL A 86 7215 7356 6426 -526 -185 1140 C -ATOM 653 CG2 VAL A 86 25.791 31.155 -19.195 1.00 55.44 C -ANISOU 653 CG2 VAL A 86 7351 7169 6547 -682 -348 1271 C -ATOM 654 N HIS A 87 27.355 31.608 -22.731 1.00 66.02 N -ANISOU 654 N HIS A 87 8606 8849 7631 -695 -198 1643 N -ATOM 655 CA HIS A 87 27.401 32.838 -23.494 1.00 70.92 C -ANISOU 655 CA HIS A 87 9271 9439 8235 -768 -247 1791 C -ATOM 656 C HIS A 87 26.216 33.727 -23.164 1.00 72.10 C -ANISOU 656 C HIS A 87 9546 9399 8451 -776 -370 1724 C -ATOM 657 O HIS A 87 25.060 33.325 -23.318 1.00 71.14 O -ANISOU 657 O HIS A 87 9487 9235 8306 -672 -387 1591 O -ATOM 658 CB HIS A 87 27.449 32.538 -24.991 1.00 73.59 C -ANISOU 658 CB HIS A 87 9605 9924 8431 -691 -169 1858 C -ATOM 659 CG HIS A 87 28.831 32.570 -25.561 1.00 76.06 C -ANISOU 659 CG HIS A 87 9809 10405 8687 -744 -78 2040 C -ATOM 660 ND1 HIS A 87 29.241 33.527 -26.463 1.00 78.40 N -ANISOU 660 ND1 HIS A 87 10107 10744 8939 -815 -82 2228 N -ATOM 661 CD2 HIS A 87 29.904 31.774 -25.341 1.00 76.41 C -ANISOU 661 CD2 HIS A 87 9731 10590 8712 -736 20 2074 C -ATOM 662 CE1 HIS A 87 30.505 33.314 -26.783 1.00 79.38 C -ANISOU 662 CE1 HIS A 87 10106 11036 9018 -849 15 2374 C -ATOM 663 NE2 HIS A 87 30.931 32.256 -26.117 1.00 78.07 N -ANISOU 663 NE2 HIS A 87 9862 10934 8867 -798 79 2282 N -ATOM 664 N ALA A 88 26.519 34.934 -22.697 1.00 74.02 N -ANISOU 664 N ALA A 88 9823 9527 8776 -900 -460 1820 N -ATOM 665 CA ALA A 88 25.503 35.948 -22.470 1.00 75.08 C -ANISOU 665 CA ALA A 88 10084 9478 8966 -907 -580 1783 C -ATOM 666 C ALA A 88 24.992 36.446 -23.814 1.00 76.69 C -ANISOU 666 C ALA A 88 10348 9705 9087 -872 -590 1857 C -ATOM 667 O ALA A 88 25.470 36.016 -24.866 1.00 77.68 O -ANISOU 667 O ALA A 88 10418 9988 9109 -846 -503 1939 O -ATOM 668 CB ALA A 88 26.062 37.097 -21.644 1.00 76.35 C -ANISOU 668 CB ALA A 88 10278 9504 9229 -1050 -681 1871 C -ATOM 669 N GLY A 89 24.027 37.359 -23.777 1.00 76.75 N -ANISOU 669 N GLY A 89 10472 9558 9133 -862 -696 1831 N -ATOM 670 CA GLY A 89 23.387 37.835 -24.990 1.00 76.00 C -ANISOU 670 CA GLY A 89 10446 9469 8964 -818 -719 1886 C -ATOM 671 C GLY A 89 22.146 37.008 -25.263 1.00 73.93 C -ANISOU 671 C GLY A 89 10211 9222 8656 -667 -703 1723 C -ATOM 672 O GLY A 89 22.016 35.899 -24.741 1.00 73.56 O -ANISOU 672 O GLY A 89 10109 9228 8613 -603 -646 1595 O -ATOM 673 N PRO A 90 21.224 37.538 -26.081 1.00 71.90 N -ANISOU 673 N PRO A 90 10039 8919 8359 -613 -760 1732 N -ATOM 674 CA PRO A 90 19.977 36.811 -26.340 1.00 67.48 C -ANISOU 674 CA PRO A 90 9505 8369 7767 -478 -763 1585 C -ATOM 675 C PRO A 90 20.249 35.503 -27.076 1.00 60.99 C -ANISOU 675 C PRO A 90 8615 7723 6834 -409 -657 1550 C -ATOM 676 O PRO A 90 21.053 35.483 -28.014 1.00 61.30 O -ANISOU 676 O PRO A 90 8629 7883 6779 -432 -597 1671 O -ATOM 677 CB PRO A 90 19.179 37.783 -27.211 1.00 70.12 C -ANISOU 677 CB PRO A 90 9939 8632 8072 -454 -848 1645 C -ATOM 678 CG PRO A 90 20.226 38.589 -27.915 1.00 72.78 C -ANISOU 678 CG PRO A 90 10279 9008 8366 -560 -839 1843 C -ATOM 679 CD PRO A 90 21.347 38.745 -26.918 1.00 73.45 C -ANISOU 679 CD PRO A 90 10304 9073 8530 -675 -820 1892 C -ATOM 680 N ILE A 91 19.603 34.421 -26.659 1.00 53.72 N -ANISOU 680 N ILE A 91 7669 6819 5922 -322 -636 1392 N -ATOM 681 CA ILE A 91 19.837 33.156 -27.333 1.00 49.29 C -ANISOU 681 CA ILE A 91 7063 6408 5256 -250 -549 1348 C -ATOM 682 C ILE A 91 18.964 33.063 -28.578 1.00 46.60 C -ANISOU 682 C ILE A 91 6789 6101 4816 -165 -582 1337 C -ATOM 683 O ILE A 91 18.001 33.814 -28.733 1.00 43.80 O -ANISOU 683 O ILE A 91 6502 5647 4493 -149 -673 1332 O -ATOM 684 CB ILE A 91 19.573 31.956 -26.422 1.00 46.64 C -ANISOU 684 CB ILE A 91 6676 6078 4967 -200 -518 1191 C -ATOM 685 CG1 ILE A 91 20.186 30.696 -27.041 1.00 45.35 C -ANISOU 685 CG1 ILE A 91 6466 6070 4694 -142 -421 1170 C -ATOM 686 CG2 ILE A 91 18.089 31.800 -26.153 1.00 44.10 C -ANISOU 686 CG2 ILE A 91 6398 5664 4694 -128 -596 1062 C -ATOM 687 CD1 ILE A 91 19.720 29.439 -26.424 1.00 42.52 C -ANISOU 687 CD1 ILE A 91 6080 5714 4363 -77 -406 1013 C -ATOM 688 N ALA A 92 19.327 32.146 -29.468 1.00 44.72 N -ANISOU 688 N ALA A 92 6536 6004 4453 -104 -509 1335 N -ATOM 689 CA ALA A 92 18.618 31.957 -30.722 1.00 43.45 C -ANISOU 689 CA ALA A 92 6443 5888 4177 -20 -538 1325 C -ATOM 690 C ALA A 92 17.197 31.464 -30.466 1.00 39.60 C -ANISOU 690 C ALA A 92 5988 5321 3737 53 -620 1171 C -ATOM 691 O ALA A 92 16.977 30.592 -29.619 1.00 36.35 O -ANISOU 691 O ALA A 92 5532 4893 3388 74 -608 1050 O -ATOM 692 CB ALA A 92 19.374 30.981 -31.616 1.00 44.14 C -ANISOU 692 CB ALA A 92 6514 6142 4114 41 -439 1341 C -ATOM 693 N PRO A 93 16.226 32.050 -31.183 1.00 37.84 N -ANISOU 693 N PRO A 93 5839 5050 3490 88 -708 1185 N -ATOM 694 CA PRO A 93 14.803 31.699 -31.093 1.00 36.28 C -ANISOU 694 CA PRO A 93 5665 4785 3333 156 -798 1062 C -ATOM 695 C PRO A 93 14.553 30.201 -31.299 1.00 36.04 C -ANISOU 695 C PRO A 93 5620 4829 3246 228 -777 939 C -ATOM 696 O PRO A 93 14.934 29.628 -32.336 1.00 33.91 O -ANISOU 696 O PRO A 93 5385 4662 2836 275 -741 955 O -ATOM 697 CB PRO A 93 14.167 32.523 -32.221 1.00 38.00 C -ANISOU 697 CB PRO A 93 5966 4987 3484 183 -877 1137 C -ATOM 698 CG PRO A 93 15.064 33.715 -32.358 1.00 38.97 C -ANISOU 698 CG PRO A 93 6105 5097 3602 102 -852 1297 C -ATOM 699 CD PRO A 93 16.461 33.203 -32.070 1.00 39.65 C -ANISOU 699 CD PRO A 93 6125 5280 3660 54 -732 1336 C -ATOM 700 N GLY A 94 13.929 29.584 -30.297 1.00 37.17 N -ANISOU 700 N GLY A 94 5715 4913 3493 237 -799 820 N -ATOM 701 CA GLY A 94 13.498 28.201 -30.377 1.00 37.43 C -ANISOU 701 CA GLY A 94 5739 4987 3497 296 -805 698 C -ATOM 702 C GLY A 94 14.597 27.217 -30.064 1.00 36.28 C -ANISOU 702 C GLY A 94 5552 4919 3314 293 -701 669 C -ATOM 703 O GLY A 94 14.393 26.004 -30.154 1.00 37.80 O -ANISOU 703 O GLY A 94 5746 5143 3471 343 -702 571 O -ATOM 704 N GLN A 95 15.768 27.733 -29.694 1.00 35.54 N -ANISOU 704 N GLN A 95 5422 4854 3230 235 -619 759 N -ATOM 705 CA GLN A 95 16.920 26.877 -29.489 1.00 33.10 C -ANISOU 705 CA GLN A 95 5067 4634 2876 238 -515 752 C -ATOM 706 C GLN A 95 17.208 26.654 -28.019 1.00 31.62 C -ANISOU 706 C GLN A 95 4801 4394 2818 186 -485 703 C -ATOM 707 O GLN A 95 16.866 27.460 -27.155 1.00 31.14 O -ANISOU 707 O GLN A 95 4722 4237 2873 131 -524 714 O -ATOM 708 CB GLN A 95 18.166 27.454 -30.174 1.00 38.85 C -ANISOU 708 CB GLN A 95 5792 5460 3509 211 -433 898 C -ATOM 709 CG GLN A 95 17.979 27.789 -31.646 1.00 42.24 C -ANISOU 709 CG GLN A 95 6303 5950 3798 260 -454 967 C -ATOM 710 CD GLN A 95 17.401 26.633 -32.439 1.00 43.39 C -ANISOU 710 CD GLN A 95 6511 6142 3835 367 -480 858 C -ATOM 711 OE1 GLN A 95 18.005 25.560 -32.531 1.00 43.85 O -ANISOU 711 OE1 GLN A 95 6559 6279 3821 422 -412 807 O -ATOM 712 NE2 GLN A 95 16.209 26.838 -32.994 1.00 42.60 N -ANISOU 712 NE2 GLN A 95 6478 5983 3723 399 -588 821 N -ATOM 713 N MET A 96 17.865 25.542 -27.744 1.00 31.83 N -ANISOU 713 N MET A 96 4791 4485 2818 212 -415 649 N -ATOM 714 CA MET A 96 18.213 25.185 -26.385 1.00 29.76 C -ANISOU 714 CA MET A 96 4457 4185 2665 169 -382 601 C -ATOM 715 C MET A 96 19.390 26.020 -25.896 1.00 31.53 C -ANISOU 715 C MET A 96 4629 4426 2924 87 -323 716 C -ATOM 716 O MET A 96 20.400 26.145 -26.596 1.00 29.84 O -ANISOU 716 O MET A 96 4404 4314 2621 84 -256 815 O -ATOM 717 CB MET A 96 18.531 23.696 -26.324 1.00 31.14 C -ANISOU 717 CB MET A 96 4617 4421 2795 230 -335 508 C -ATOM 718 CG MET A 96 19.021 23.185 -24.990 1.00 32.07 C -ANISOU 718 CG MET A 96 4661 4516 3008 194 -292 463 C -ATOM 719 SD MET A 96 19.244 21.399 -25.083 1.00 43.65 S -ANISOU 719 SD MET A 96 6133 6041 4411 279 -254 350 S -ATOM 720 CE MET A 96 20.517 21.274 -26.343 1.00 42.82 C -ANISOU 720 CE MET A 96 6047 6087 4136 339 -159 441 C -ATOM 721 N ARG A 97 19.258 26.600 -24.699 1.00 29.85 N -ANISOU 721 N ARG A 97 4385 4117 2838 20 -352 709 N -ATOM 722 CA ARG A 97 20.337 27.388 -24.128 1.00 33.61 C -ANISOU 722 CA ARG A 97 4818 4593 3361 -70 -316 813 C -ATOM 723 C ARG A 97 21.240 26.477 -23.301 1.00 32.46 C -ANISOU 723 C ARG A 97 4597 4498 3239 -79 -243 777 C -ATOM 724 O ARG A 97 20.887 25.343 -23.015 1.00 34.86 O -ANISOU 724 O ARG A 97 4891 4811 3542 -20 -231 665 O -ATOM 725 CB ARG A 97 19.793 28.554 -23.282 1.00 33.56 C -ANISOU 725 CB ARG A 97 4837 4448 3468 -132 -394 825 C -ATOM 726 CG ARG A 97 18.963 28.150 -22.073 1.00 29.92 C -ANISOU 726 CG ARG A 97 4364 3898 3107 -113 -429 699 C -ATOM 727 CD ARG A 97 18.384 29.366 -21.329 1.00 32.19 C -ANISOU 727 CD ARG A 97 4692 4051 3488 -151 -505 710 C -ATOM 728 NE ARG A 97 17.702 28.976 -20.089 1.00 32.77 N -ANISOU 728 NE ARG A 97 4747 4054 3649 -128 -522 599 N -ATOM 729 CZ ARG A 97 18.296 28.891 -18.900 1.00 31.91 C -ANISOU 729 CZ ARG A 97 4605 3918 3603 -172 -498 581 C -ATOM 730 NH1 ARG A 97 19.588 29.172 -18.769 1.00 31.34 N -ANISOU 730 NH1 ARG A 97 4507 3877 3524 -249 -464 666 N -ATOM 731 NH2 ARG A 97 17.598 28.519 -17.842 1.00 31.10 N -ANISOU 731 NH2 ARG A 97 4489 3760 3567 -141 -510 483 N -ATOM 732 N GLU A 98 22.419 26.965 -22.951 1.00 31.11 N -ANISOU 732 N GLU A 98 4371 4360 3087 -156 -200 881 N -ATOM 733 CA GLU A 98 23.338 26.200 -22.126 1.00 30.38 C -ANISOU 733 CA GLU A 98 4202 4317 3025 -170 -137 861 C -ATOM 734 C GLU A 98 22.981 26.409 -20.651 1.00 31.18 C -ANISOU 734 C GLU A 98 4295 4297 3255 -220 -187 793 C -ATOM 735 O GLU A 98 22.702 27.527 -20.232 1.00 32.54 O -ANISOU 735 O GLU A 98 4501 4370 3493 -283 -252 831 O -ATOM 736 CB GLU A 98 24.798 26.605 -22.388 1.00 31.91 C -ANISOU 736 CB GLU A 98 4326 4612 3185 -232 -71 1013 C -ATOM 737 CG GLU A 98 25.228 26.641 -23.863 1.00 38.01 C -ANISOU 737 CG GLU A 98 5106 5513 3824 -189 -15 1111 C -ATOM 738 CD GLU A 98 26.310 27.686 -24.129 1.00 45.31 C -ANISOU 738 CD GLU A 98 5979 6491 4747 -289 8 1300 C -ATOM 739 OE1 GLU A 98 27.493 27.296 -24.232 1.00 47.72 O -ANISOU 739 OE1 GLU A 98 6195 6925 5013 -293 97 1380 O -ATOM 740 OE2 GLU A 98 25.982 28.899 -24.236 1.00 46.98 O -ANISOU 740 OE2 GLU A 98 6237 6616 4998 -365 -64 1374 O -ATOM 741 N PRO A 99 22.978 25.326 -19.862 1.00 31.42 N -ANISOU 741 N PRO A 99 4289 4333 3315 -185 -158 692 N -ATOM 742 CA PRO A 99 22.700 25.450 -18.425 1.00 29.94 C -ANISOU 742 CA PRO A 99 4093 4044 3237 -226 -196 630 C -ATOM 743 C PRO A 99 23.930 25.906 -17.629 1.00 30.08 C -ANISOU 743 C PRO A 99 4056 4068 3304 -317 -179 712 C -ATOM 744 O PRO A 99 25.033 25.410 -17.869 1.00 28.73 O -ANISOU 744 O PRO A 99 3818 4006 3091 -323 -110 769 O -ATOM 745 CB PRO A 99 22.281 24.028 -18.024 1.00 28.27 C -ANISOU 745 CB PRO A 99 3864 3850 3026 -153 -169 504 C -ATOM 746 CG PRO A 99 22.968 23.144 -19.006 1.00 32.52 C -ANISOU 746 CG PRO A 99 4379 4514 3461 -96 -100 523 C -ATOM 747 CD PRO A 99 23.021 23.922 -20.305 1.00 30.87 C -ANISOU 747 CD PRO A 99 4206 4350 3173 -94 -103 618 C -ATOM 748 N ARG A 100 23.744 26.853 -16.711 1.00 28.62 N -ANISOU 748 N ARG A 100 3901 3770 3203 -384 -244 719 N -ATOM 749 CA ARG A 100 24.798 27.175 -15.765 1.00 33.04 C -ANISOU 749 CA ARG A 100 4417 4318 3820 -472 -247 775 C -ATOM 750 C ARG A 100 24.477 26.493 -14.437 1.00 25.73 C -ANISOU 750 C ARG A 100 3483 3338 2954 -450 -251 658 C -ATOM 751 O ARG A 100 23.456 25.810 -14.322 1.00 23.05 O -ANISOU 751 O ARG A 100 3167 2977 2614 -372 -249 549 O -ATOM 752 CB ARG A 100 24.963 28.691 -15.605 1.00 45.14 C -ANISOU 752 CB ARG A 100 6000 5754 5398 -568 -327 869 C -ATOM 753 CG ARG A 100 23.702 29.456 -15.286 1.00 53.34 C -ANISOU 753 CG ARG A 100 7138 6652 6477 -543 -409 803 C -ATOM 754 CD ARG A 100 23.841 30.923 -15.726 1.00 60.79 C -ANISOU 754 CD ARG A 100 8144 7521 7432 -619 -482 917 C -ATOM 755 NE ARG A 100 24.356 31.791 -14.667 1.00 63.51 N -ANISOU 755 NE ARG A 100 8522 7759 7851 -712 -554 951 N -ATOM 756 CZ ARG A 100 25.646 32.038 -14.443 1.00 66.02 C -ANISOU 756 CZ ARG A 100 8786 8110 8188 -819 -557 1058 C -ATOM 757 NH1 ARG A 100 26.581 31.476 -15.198 1.00 67.59 N -ANISOU 757 NH1 ARG A 100 8885 8459 8337 -839 -476 1146 N -ATOM 758 NH2 ARG A 100 26.003 32.849 -13.455 1.00 66.78 N -ANISOU 758 NH2 ARG A 100 8930 8090 8352 -904 -642 1078 N -ATOM 759 N GLY A 101 25.343 26.671 -13.446 1.00 25.36 N -ANISOU 759 N GLY A 101 3403 3273 2959 -522 -261 689 N -ATOM 760 CA GLY A 101 25.215 25.953 -12.185 1.00 23.26 C -ANISOU 760 CA GLY A 101 3124 2973 2740 -502 -257 591 C -ATOM 761 C GLY A 101 23.832 26.089 -11.581 1.00 24.50 C -ANISOU 761 C GLY A 101 3354 3023 2932 -449 -302 482 C -ATOM 762 O GLY A 101 23.229 25.100 -11.164 1.00 26.19 O -ANISOU 762 O GLY A 101 3555 3246 3151 -384 -274 385 O -ATOM 763 N SER A 102 23.308 27.314 -11.571 1.00 25.87 N -ANISOU 763 N SER A 102 3604 3096 3130 -473 -374 505 N -ATOM 764 CA SER A 102 22.002 27.579 -10.971 1.00 26.06 C -ANISOU 764 CA SER A 102 3695 3022 3187 -414 -415 413 C -ATOM 765 C SER A 102 20.845 26.922 -11.724 1.00 23.63 C -ANISOU 765 C SER A 102 3382 2748 2847 -322 -391 349 C -ATOM 766 O SER A 102 19.780 26.684 -11.140 1.00 23.36 O -ANISOU 766 O SER A 102 3366 2669 2841 -261 -402 264 O -ATOM 767 CB SER A 102 21.750 29.092 -10.886 1.00 26.54 C -ANISOU 767 CB SER A 102 3847 2964 3273 -451 -501 457 C -ATOM 768 OG SER A 102 21.698 29.671 -12.177 1.00 29.03 O -ANISOU 768 OG SER A 102 4180 3300 3551 -461 -515 536 O -ATOM 769 N ASP A 103 21.024 26.665 -13.021 1.00 23.02 N -ANISOU 769 N ASP A 103 3284 2752 2711 -311 -364 396 N -ATOM 770 CA ASP A 103 20.004 25.946 -13.792 1.00 23.14 C -ANISOU 770 CA ASP A 103 3298 2803 2691 -230 -351 337 C -ATOM 771 C ASP A 103 20.015 24.467 -13.397 1.00 21.29 C -ANISOU 771 C ASP A 103 3008 2626 2454 -190 -298 258 C -ATOM 772 O ASP A 103 18.967 23.850 -13.244 1.00 24.48 O -ANISOU 772 O ASP A 103 3412 3016 2874 -134 -307 179 O -ATOM 773 CB ASP A 103 20.233 26.088 -15.309 1.00 25.06 C -ANISOU 773 CB ASP A 103 3548 3116 2858 -224 -341 408 C -ATOM 774 CG ASP A 103 20.092 27.536 -15.802 1.00 25.87 C -ANISOU 774 CG ASP A 103 3712 3156 2962 -260 -400 490 C -ATOM 775 OD1 ASP A 103 19.086 28.208 -15.452 1.00 24.51 O -ANISOU 775 OD1 ASP A 103 3592 2888 2831 -234 -459 454 O -ATOM 776 OD2 ASP A 103 21.001 27.998 -16.526 1.00 27.77 O -ANISOU 776 OD2 ASP A 103 3947 3445 3161 -311 -387 596 O -ATOM 777 N ILE A 104 21.212 23.915 -13.229 1.00 20.93 N -ANISOU 777 N ILE A 104 2913 2647 2391 -221 -248 288 N -ATOM 778 CA ILE A 104 21.378 22.510 -12.856 1.00 21.06 C -ANISOU 778 CA ILE A 104 2884 2715 2404 -184 -200 221 C -ATOM 779 C ILE A 104 20.817 22.256 -11.446 1.00 22.05 C -ANISOU 779 C ILE A 104 3007 2772 2599 -181 -215 146 C -ATOM 780 O ILE A 104 20.212 21.210 -11.180 1.00 24.60 O -ANISOU 780 O ILE A 104 3313 3102 2931 -135 -201 71 O -ATOM 781 CB ILE A 104 22.859 22.107 -12.949 1.00 22.52 C -ANISOU 781 CB ILE A 104 3013 2988 2557 -214 -143 281 C -ATOM 782 CG1 ILE A 104 23.289 22.077 -14.423 1.00 25.08 C -ANISOU 782 CG1 ILE A 104 3333 3402 2793 -189 -111 345 C -ATOM 783 CG2 ILE A 104 23.143 20.756 -12.244 1.00 25.90 C -ANISOU 783 CG2 ILE A 104 3397 3448 2995 -182 -101 213 C -ATOM 784 CD1 ILE A 104 24.769 22.222 -14.604 1.00 28.13 C -ANISOU 784 CD1 ILE A 104 3661 3876 3152 -233 -62 448 C -ATOM 785 N ALA A 105 21.002 23.230 -10.558 1.00 23.72 N -ANISOU 785 N ALA A 105 3243 2914 2857 -229 -247 169 N -ATOM 786 CA ALA A 105 20.494 23.137 -9.192 1.00 21.96 C -ANISOU 786 CA ALA A 105 3030 2627 2688 -219 -260 104 C -ATOM 787 C ALA A 105 19.012 23.488 -9.159 1.00 23.47 C -ANISOU 787 C ALA A 105 3258 2759 2901 -163 -294 55 C -ATOM 788 O ALA A 105 18.380 23.434 -8.106 1.00 25.19 O -ANISOU 788 O ALA A 105 3483 2931 3156 -136 -299 2 O -ATOM 789 CB ALA A 105 21.305 24.071 -8.242 1.00 20.27 C -ANISOU 789 CB ALA A 105 2841 2354 2505 -286 -291 145 C -ATOM 790 N GLY A 106 18.469 23.868 -10.319 1.00 24.55 N -ANISOU 790 N GLY A 106 3415 2903 3009 -140 -317 78 N -ATOM 791 CA GLY A 106 17.049 24.129 -10.457 1.00 25.97 C -ANISOU 791 CA GLY A 106 3616 3043 3207 -82 -350 40 C -ATOM 792 C GLY A 106 16.547 25.410 -9.817 1.00 27.77 C -ANISOU 792 C GLY A 106 3903 3178 3469 -71 -397 45 C -ATOM 793 O GLY A 106 15.354 25.531 -9.514 1.00 32.24 O -ANISOU 793 O GLY A 106 4475 3713 4062 -9 -413 3 O -ATOM 794 N THR A 107 17.437 26.374 -9.615 1.00 25.28 N -ANISOU 794 N THR A 107 3634 2817 3154 -128 -422 100 N -ATOM 795 CA THR A 107 17.054 27.643 -9.004 1.00 27.50 C -ANISOU 795 CA THR A 107 3994 2992 3461 -117 -477 102 C -ATOM 796 C THR A 107 16.641 28.672 -10.057 1.00 31.27 C -ANISOU 796 C THR A 107 4526 3433 3923 -108 -530 155 C -ATOM 797 O THR A 107 15.822 29.560 -9.798 1.00 32.91 O -ANISOU 797 O THR A 107 4796 3559 4149 -57 -576 140 O -ATOM 798 CB THR A 107 18.201 28.224 -8.151 1.00 31.24 C -ANISOU 798 CB THR A 107 4507 3415 3948 -191 -500 134 C -ATOM 799 OG1 THR A 107 19.328 28.529 -8.986 1.00 32.62 O -ANISOU 799 OG1 THR A 107 4672 3621 4100 -276 -508 227 O -ATOM 800 CG2 THR A 107 18.624 27.221 -7.085 1.00 30.60 C -ANISOU 800 CG2 THR A 107 4376 3371 3881 -198 -453 85 C -ATOM 801 N THR A 108 17.205 28.539 -11.252 1.00 29.08 N -ANISOU 801 N THR A 108 4226 3217 3605 -148 -520 218 N -ATOM 802 CA THR A 108 16.972 29.514 -12.309 1.00 30.22 C -ANISOU 802 CA THR A 108 4423 3332 3726 -151 -569 283 C -ATOM 803 C THR A 108 16.503 28.868 -13.600 1.00 29.14 C -ANISOU 803 C THR A 108 4249 3279 3542 -114 -549 288 C -ATOM 804 O THR A 108 16.518 29.504 -14.648 1.00 30.05 O -ANISOU 804 O THR A 108 4400 3396 3623 -124 -579 354 O -ATOM 805 CB THR A 108 18.250 30.329 -12.611 1.00 30.86 C -ANISOU 805 CB THR A 108 4534 3396 3794 -250 -592 387 C -ATOM 806 OG1 THR A 108 19.287 29.439 -13.037 1.00 26.74 O -ANISOU 806 OG1 THR A 108 3937 2987 3238 -296 -528 423 O -ATOM 807 CG2 THR A 108 18.726 31.090 -11.363 1.00 32.61 C -ANISOU 807 CG2 THR A 108 4811 3517 4063 -296 -636 386 C -ATOM 808 N SER A 109 16.101 27.603 -13.535 1.00 27.44 N -ANISOU 808 N SER A 109 3972 3131 3323 -73 -506 220 N -ATOM 809 CA SER A 109 15.572 26.933 -14.718 1.00 28.97 C -ANISOU 809 CA SER A 109 4144 3393 3471 -34 -502 213 C -ATOM 810 C SER A 109 14.154 26.433 -14.479 1.00 31.89 C -ANISOU 810 C SER A 109 4489 3753 3875 38 -522 138 C -ATOM 811 O SER A 109 13.778 26.129 -13.348 1.00 30.10 O -ANISOU 811 O SER A 109 4235 3501 3699 56 -507 84 O -ATOM 812 CB SER A 109 16.462 25.759 -15.116 1.00 29.21 C -ANISOU 812 CB SER A 109 4127 3520 3453 -54 -443 211 C -ATOM 813 OG SER A 109 16.508 24.799 -14.064 1.00 31.09 O -ANISOU 813 OG SER A 109 4317 3767 3729 -49 -406 143 O -ATOM 814 N THR A 110 13.372 26.339 -15.550 1.00 31.14 N -ANISOU 814 N THR A 110 4399 3682 3750 76 -557 141 N -ATOM 815 CA THR A 110 12.019 25.813 -15.447 1.00 29.16 C -ANISOU 815 CA THR A 110 4111 3433 3535 136 -584 84 C -ATOM 816 C THR A 110 12.023 24.289 -15.587 1.00 28.21 C -ANISOU 816 C THR A 110 3938 3379 3400 134 -557 33 C -ATOM 817 O THR A 110 13.013 23.706 -16.027 1.00 24.65 O -ANISOU 817 O THR A 110 3492 2977 2896 104 -522 43 O -ATOM 818 CB THR A 110 11.107 26.425 -16.519 1.00 27.49 C -ANISOU 818 CB THR A 110 3930 3212 3304 177 -650 113 C -ATOM 819 OG1 THR A 110 11.537 25.992 -17.811 1.00 27.50 O -ANISOU 819 OG1 THR A 110 3950 3273 3225 162 -655 139 O -ATOM 820 CG2 THR A 110 11.141 27.950 -16.452 1.00 27.59 C -ANISOU 820 CG2 THR A 110 4008 3148 3328 180 -684 168 C -ATOM 821 N LEU A 111 10.917 23.640 -15.228 1.00 28.90 N -ANISOU 821 N LEU A 111 3975 3469 3535 168 -577 -15 N -ATOM 822 CA LEU A 111 10.816 22.198 -15.425 1.00 27.63 C -ANISOU 822 CA LEU A 111 3777 3357 3366 163 -572 -61 C -ATOM 823 C LEU A 111 10.934 21.877 -16.916 1.00 26.43 C -ANISOU 823 C LEU A 111 3665 3244 3133 169 -608 -49 C -ATOM 824 O LEU A 111 11.579 20.904 -17.305 1.00 24.12 O -ANISOU 824 O LEU A 111 3382 2992 2790 158 -587 -72 O -ATOM 825 CB LEU A 111 9.501 21.651 -14.868 1.00 27.62 C -ANISOU 825 CB LEU A 111 3710 3350 3435 189 -601 -98 C -ATOM 826 CG LEU A 111 9.219 20.205 -15.297 1.00 29.67 C -ANISOU 826 CG LEU A 111 3942 3645 3685 177 -626 -138 C -ATOM 827 CD1 LEU A 111 10.245 19.261 -14.695 1.00 28.34 C -ANISOU 827 CD1 LEU A 111 3770 3492 3507 145 -566 -168 C -ATOM 828 CD2 LEU A 111 7.788 19.753 -14.947 1.00 30.56 C -ANISOU 828 CD2 LEU A 111 3981 3758 3873 193 -673 -152 C -ATOM 829 N GLN A 112 10.305 22.700 -17.750 1.00 28.63 N -ANISOU 829 N GLN A 112 3975 3510 3392 194 -664 -14 N -ATOM 830 CA GLN A 112 10.355 22.483 -19.190 1.00 29.91 C -ANISOU 830 CA GLN A 112 4186 3710 3468 206 -704 0 C -ATOM 831 C GLN A 112 11.791 22.529 -19.737 1.00 25.97 C -ANISOU 831 C GLN A 112 3734 3253 2882 185 -647 37 C -ATOM 832 O GLN A 112 12.158 21.718 -20.585 1.00 27.15 O -ANISOU 832 O GLN A 112 3912 3452 2952 199 -645 20 O -ATOM 833 CB GLN A 112 9.492 23.510 -19.914 1.00 37.83 C -ANISOU 833 CB GLN A 112 5217 4689 4467 237 -773 42 C -ATOM 834 CG GLN A 112 9.230 23.147 -21.362 1.00 43.47 C -ANISOU 834 CG GLN A 112 5978 5441 5097 258 -832 46 C -ATOM 835 CD GLN A 112 8.437 21.854 -21.494 1.00 50.78 C -ANISOU 835 CD GLN A 112 6873 6382 6039 266 -885 -19 C -ATOM 836 OE1 GLN A 112 7.323 21.740 -20.974 1.00 55.03 O -ANISOU 836 OE1 GLN A 112 7349 6898 6662 274 -929 -36 O -ATOM 837 NE2 GLN A 112 9.014 20.868 -22.179 1.00 50.72 N -ANISOU 837 NE2 GLN A 112 6908 6413 5950 267 -881 -50 N -ATOM 838 N GLU A 113 12.589 23.484 -19.275 1.00 24.79 N -ANISOU 838 N GLU A 113 3593 3084 2743 154 -604 90 N -ATOM 839 CA GLU A 113 13.997 23.560 -19.680 1.00 26.68 C -ANISOU 839 CA GLU A 113 3855 3372 2910 124 -544 142 C -ATOM 840 C GLU A 113 14.767 22.329 -19.182 1.00 26.87 C -ANISOU 840 C GLU A 113 3842 3440 2926 118 -483 95 C -ATOM 841 O GLU A 113 15.563 21.738 -19.921 1.00 26.97 O -ANISOU 841 O GLU A 113 3871 3520 2854 131 -447 105 O -ATOM 842 CB GLU A 113 14.650 24.846 -19.159 1.00 27.65 C -ANISOU 842 CB GLU A 113 3988 3453 3063 77 -527 214 C -ATOM 843 CG GLU A 113 14.079 26.137 -19.777 1.00 30.41 C -ANISOU 843 CG GLU A 113 4390 3756 3409 85 -587 274 C -ATOM 844 CD GLU A 113 14.592 27.411 -19.111 1.00 30.64 C -ANISOU 844 CD GLU A 113 4443 3717 3483 36 -590 336 C -ATOM 845 OE1 GLU A 113 14.877 27.376 -17.895 1.00 28.34 O -ANISOU 845 OE1 GLU A 113 4126 3389 3253 12 -566 306 O -ATOM 846 OE2 GLU A 113 14.705 28.456 -19.804 1.00 31.80 O -ANISOU 846 OE2 GLU A 113 4642 3841 3601 21 -623 415 O -ATOM 847 N GLN A 114 14.537 21.942 -17.928 1.00 25.70 N -ANISOU 847 N GLN A 114 3648 3256 2861 104 -470 46 N -ATOM 848 CA GLN A 114 15.176 20.732 -17.395 1.00 26.81 C -ANISOU 848 CA GLN A 114 3757 3429 3002 101 -420 -1 C -ATOM 849 C GLN A 114 14.852 19.492 -18.227 1.00 26.94 C -ANISOU 849 C GLN A 114 3793 3482 2962 143 -444 -55 C -ATOM 850 O GLN A 114 15.738 18.695 -18.541 1.00 26.94 O -ANISOU 850 O GLN A 114 3803 3533 2900 159 -401 -66 O -ATOM 851 CB GLN A 114 14.763 20.505 -15.944 1.00 24.87 C -ANISOU 851 CB GLN A 114 3463 3135 2852 85 -413 -45 C -ATOM 852 CG GLN A 114 15.224 21.624 -15.025 1.00 25.29 C -ANISOU 852 CG GLN A 114 3513 3147 2950 48 -392 -3 C -ATOM 853 CD GLN A 114 14.608 21.524 -13.644 1.00 24.68 C -ANISOU 853 CD GLN A 114 3401 3021 2956 49 -390 -47 C -ATOM 854 OE1 GLN A 114 14.066 20.483 -13.257 1.00 20.97 O -ANISOU 854 OE1 GLN A 114 2894 2560 2514 64 -389 -101 O -ATOM 855 NE2 GLN A 114 14.681 22.608 -12.899 1.00 22.81 N -ANISOU 855 NE2 GLN A 114 3180 2730 2755 34 -394 -22 N -ATOM 856 N ILE A 115 13.576 19.340 -18.567 1.00 26.25 N -ANISOU 856 N ILE A 115 3712 3365 2897 164 -518 -88 N -ATOM 857 CA ILE A 115 13.109 18.262 -19.433 1.00 27.47 C -ANISOU 857 CA ILE A 115 3900 3537 3000 198 -570 -138 C -ATOM 858 C ILE A 115 13.815 18.272 -20.803 1.00 26.06 C -ANISOU 858 C ILE A 115 3792 3417 2692 234 -560 -112 C -ATOM 859 O ILE A 115 14.292 17.229 -21.291 1.00 24.65 O -ANISOU 859 O ILE A 115 3651 3273 2442 269 -549 -152 O -ATOM 860 CB ILE A 115 11.578 18.363 -19.647 1.00 23.77 C -ANISOU 860 CB ILE A 115 3421 3030 2582 205 -664 -156 C -ATOM 861 CG1 ILE A 115 10.822 17.998 -18.366 1.00 27.83 C -ANISOU 861 CG1 ILE A 115 3859 3504 3212 181 -670 -187 C -ATOM 862 CG2 ILE A 115 11.125 17.464 -20.800 1.00 25.26 C -ANISOU 862 CG2 ILE A 115 3664 3231 2701 235 -739 -196 C -ATOM 863 CD1 ILE A 115 9.330 17.854 -18.596 1.00 29.91 C -ANISOU 863 CD1 ILE A 115 4093 3745 3527 187 -764 -199 C -ATOM 864 N GLY A 116 13.876 19.453 -21.409 1.00 26.19 N -ANISOU 864 N GLY A 116 3833 3444 2676 232 -564 -43 N -ATOM 865 CA GLY A 116 14.579 19.638 -22.671 1.00 29.85 C -ANISOU 865 CA GLY A 116 4357 3972 3013 265 -543 3 C -ATOM 866 C GLY A 116 16.030 19.180 -22.621 1.00 29.51 C -ANISOU 866 C GLY A 116 4307 3998 2909 274 -447 21 C -ATOM 867 O GLY A 116 16.501 18.504 -23.529 1.00 32.00 O -ANISOU 867 O GLY A 116 4672 4374 3114 330 -429 8 O -ATOM 868 N TRP A 117 16.746 19.545 -21.561 1.00 25.53 N -ANISOU 868 N TRP A 117 3742 3486 2471 225 -386 53 N -ATOM 869 CA TRP A 117 18.152 19.174 -21.455 1.00 26.64 C -ANISOU 869 CA TRP A 117 3858 3699 2564 230 -295 83 C -ATOM 870 C TRP A 117 18.298 17.661 -21.331 1.00 24.80 C -ANISOU 870 C TRP A 117 3634 3482 2308 280 -283 -4 C -ATOM 871 O TRP A 117 19.078 17.052 -22.038 1.00 23.51 O -ANISOU 871 O TRP A 117 3499 3392 2042 338 -237 -2 O -ATOM 872 CB TRP A 117 18.811 19.883 -20.268 1.00 26.80 C -ANISOU 872 CB TRP A 117 3813 3697 2672 158 -252 133 C -ATOM 873 CG TRP A 117 19.023 21.348 -20.509 1.00 26.11 C -ANISOU 873 CG TRP A 117 3730 3601 2589 109 -258 235 C -ATOM 874 CD1 TRP A 117 19.433 21.943 -21.675 1.00 27.48 C -ANISOU 874 CD1 TRP A 117 3937 3834 2672 120 -245 318 C -ATOM 875 CD2 TRP A 117 18.813 22.407 -19.569 1.00 26.71 C -ANISOU 875 CD2 TRP A 117 3787 3598 2762 45 -284 265 C -ATOM 876 NE1 TRP A 117 19.497 23.309 -21.510 1.00 28.61 N -ANISOU 876 NE1 TRP A 117 4079 3935 2857 55 -266 404 N -ATOM 877 CE2 TRP A 117 19.122 23.618 -20.226 1.00 29.16 C -ANISOU 877 CE2 TRP A 117 4124 3915 3041 12 -293 368 C -ATOM 878 CE3 TRP A 117 18.398 22.447 -18.228 1.00 22.78 C -ANISOU 878 CE3 TRP A 117 3261 3026 2369 16 -301 216 C -ATOM 879 CZ2 TRP A 117 19.021 24.861 -19.589 1.00 29.43 C -ANISOU 879 CZ2 TRP A 117 4165 3869 3149 -49 -330 417 C -ATOM 880 CZ3 TRP A 117 18.305 23.675 -17.598 1.00 25.17 C -ANISOU 880 CZ3 TRP A 117 3572 3257 2735 -34 -330 261 C -ATOM 881 CH2 TRP A 117 18.613 24.870 -18.279 1.00 27.87 C -ANISOU 881 CH2 TRP A 117 3949 3594 3048 -66 -349 357 C -ATOM 882 N MET A 118 17.481 17.070 -20.469 1.00 24.98 N -ANISOU 882 N MET A 118 3636 3433 2420 263 -328 -78 N -ATOM 883 CA MET A 118 17.586 15.664 -20.125 1.00 26.82 C -ANISOU 883 CA MET A 118 3875 3661 2654 295 -325 -157 C -ATOM 884 C MET A 118 17.163 14.730 -21.244 1.00 27.51 C -ANISOU 884 C MET A 118 4047 3756 2650 364 -381 -218 C -ATOM 885 O MET A 118 17.549 13.556 -21.258 1.00 28.32 O -ANISOU 885 O MET A 118 4180 3867 2715 410 -371 -276 O -ATOM 886 CB MET A 118 16.747 15.375 -18.875 1.00 27.89 C -ANISOU 886 CB MET A 118 3963 3719 2916 248 -363 -204 C -ATOM 887 CG MET A 118 17.308 16.031 -17.628 1.00 29.81 C -ANISOU 887 CG MET A 118 4137 3951 3238 192 -306 -163 C -ATOM 888 SD MET A 118 16.221 15.906 -16.194 1.00 27.59 S -ANISOU 888 SD MET A 118 3803 3589 3092 148 -343 -206 S -ATOM 889 CE MET A 118 16.315 14.152 -15.872 1.00 22.65 C -ANISOU 889 CE MET A 118 3182 2956 2467 171 -346 -283 C -ATOM 890 N THR A 119 16.383 15.238 -22.190 1.00 24.96 N -ANISOU 890 N THR A 119 3772 3425 2285 375 -446 -206 N -ATOM 891 CA THR A 119 15.864 14.378 -23.237 1.00 27.28 C -ANISOU 891 CA THR A 119 4158 3715 2494 436 -519 -269 C -ATOM 892 C THR A 119 16.425 14.761 -24.608 1.00 32.03 C -ANISOU 892 C THR A 119 4830 4394 2945 501 -494 -226 C -ATOM 893 O THR A 119 16.107 14.139 -25.616 1.00 30.79 O -ANISOU 893 O THR A 119 4768 4242 2690 564 -552 -274 O -ATOM 894 CB THR A 119 14.314 14.406 -23.272 1.00 32.68 C -ANISOU 894 CB THR A 119 4846 4323 3249 402 -641 -303 C -ATOM 895 OG1 THR A 119 13.850 15.723 -23.589 1.00 32.43 O -ANISOU 895 OG1 THR A 119 4797 4295 3232 377 -658 -235 O -ATOM 896 CG2 THR A 119 13.756 14.009 -21.914 1.00 33.63 C -ANISOU 896 CG2 THR A 119 4887 4379 3511 343 -656 -334 C -ATOM 897 N HIS A 120 17.282 15.771 -24.639 1.00 36.03 N -ANISOU 897 N HIS A 120 5296 4963 3430 484 -409 -131 N -ATOM 898 CA HIS A 120 17.887 16.185 -25.897 1.00 41.15 C -ANISOU 898 CA HIS A 120 6000 5699 3935 542 -371 -70 C -ATOM 899 C HIS A 120 18.796 15.092 -26.437 1.00 37.53 C -ANISOU 899 C HIS A 120 5595 5313 3353 641 -313 -109 C -ATOM 900 O HIS A 120 19.121 14.142 -25.730 1.00 37.50 O -ANISOU 900 O HIS A 120 5572 5290 3385 655 -293 -169 O -ATOM 901 CB HIS A 120 18.676 17.477 -25.716 1.00 44.87 C -ANISOU 901 CB HIS A 120 6405 6221 4424 489 -292 53 C -ATOM 902 CG HIS A 120 19.181 18.057 -26.999 1.00 50.97 C -ANISOU 902 CG HIS A 120 7226 7085 5058 534 -257 136 C -ATOM 903 ND1 HIS A 120 20.508 18.000 -27.371 1.00 53.35 N -ANISOU 903 ND1 HIS A 120 7507 7501 5263 576 -146 206 N -ATOM 904 CD2 HIS A 120 18.537 18.699 -28.003 1.00 53.92 C -ANISOU 904 CD2 HIS A 120 7663 7457 5368 547 -315 169 C -ATOM 905 CE1 HIS A 120 20.661 18.589 -28.543 1.00 56.74 C -ANISOU 905 CE1 HIS A 120 7985 7999 5575 611 -133 281 C -ATOM 906 NE2 HIS A 120 19.479 19.021 -28.949 1.00 57.58 N -ANISOU 906 NE2 HIS A 120 8148 8034 5697 593 -237 257 N -ATOM 907 N ASN A 121 19.203 15.225 -27.692 1.00 36.82 N -ANISOU 907 N ASN A 121 5575 5307 3110 718 -287 -72 N -ATOM 908 CA ASN A 121 20.179 14.302 -28.267 1.00 41.26 C -ANISOU 908 CA ASN A 121 6188 5954 3534 832 -215 -96 C -ATOM 909 C ASN A 121 21.367 15.058 -28.879 1.00 45.19 C -ANISOU 909 C ASN A 121 6650 6590 3929 864 -93 31 C -ATOM 910 O ASN A 121 21.224 15.733 -29.892 1.00 47.11 O -ANISOU 910 O ASN A 121 6941 6880 4078 884 -100 91 O -ATOM 911 CB ASN A 121 19.501 13.419 -29.317 1.00 44.51 C -ANISOU 911 CB ASN A 121 6745 6339 3827 927 -306 -194 C -ATOM 912 CG ASN A 121 20.361 12.232 -29.745 1.00 49.32 C -ANISOU 912 CG ASN A 121 7427 7008 4303 1060 -251 -253 C -ATOM 913 OD1 ASN A 121 21.131 11.667 -28.953 1.00 49.45 O -ANISOU 913 OD1 ASN A 121 7386 7040 4363 1073 -180 -266 O -ATOM 914 ND2 ASN A 121 20.217 11.838 -31.004 1.00 50.51 N -ANISOU 914 ND2 ASN A 121 7713 7189 4288 1170 -287 -293 N -ATOM 915 N PRO A 122 22.551 14.955 -28.261 1.00 45.68 N -ANISOU 915 N PRO A 122 6622 6723 4011 864 18 82 N -ATOM 916 CA PRO A 122 22.806 14.200 -27.038 1.00 44.03 C -ANISOU 916 CA PRO A 122 6354 6466 3910 840 30 21 C -ATOM 917 C PRO A 122 22.245 14.939 -25.828 1.00 40.19 C -ANISOU 917 C PRO A 122 5783 5883 3605 700 -14 39 C -ATOM 918 O PRO A 122 22.174 16.171 -25.836 1.00 36.14 O -ANISOU 918 O PRO A 122 5227 5373 3130 623 -13 131 O -ATOM 919 CB PRO A 122 24.331 14.131 -26.987 1.00 44.30 C -ANISOU 919 CB PRO A 122 6313 6633 3887 888 168 104 C -ATOM 920 CG PRO A 122 24.759 15.394 -27.652 1.00 44.68 C -ANISOU 920 CG PRO A 122 6322 6771 3884 852 221 248 C -ATOM 921 CD PRO A 122 23.786 15.569 -28.787 1.00 46.51 C -ANISOU 921 CD PRO A 122 6673 6975 4023 892 141 216 C -ATOM 922 N PRO A 123 21.839 14.196 -24.804 1.00 40.98 N -ANISOU 922 N PRO A 123 5866 5895 3810 672 -55 -48 N -ATOM 923 CA PRO A 123 21.262 14.848 -23.625 1.00 40.55 C -ANISOU 923 CA PRO A 123 5737 5752 3916 554 -94 -38 C -ATOM 924 C PRO A 123 22.322 15.509 -22.757 1.00 37.22 C -ANISOU 924 C PRO A 123 5208 5374 3558 490 -10 52 C -ATOM 925 O PRO A 123 23.468 15.059 -22.749 1.00 34.68 O -ANISOU 925 O PRO A 123 4853 5139 3186 536 75 81 O -ATOM 926 CB PRO A 123 20.598 13.689 -22.881 1.00 42.05 C -ANISOU 926 CB PRO A 123 5946 5852 4177 557 -155 -154 C -ATOM 927 CG PRO A 123 21.423 12.504 -23.258 1.00 41.61 C -ANISOU 927 CG PRO A 123 5935 5852 4022 662 -108 -200 C -ATOM 928 CD PRO A 123 21.870 12.730 -24.675 1.00 42.10 C -ANISOU 928 CD PRO A 123 6061 6011 3924 750 -71 -158 C -ATOM 929 N ILE A 124 21.932 16.571 -22.051 1.00 36.51 N -ANISOU 929 N ILE A 124 5071 5226 3577 389 -39 98 N -ATOM 930 CA ILE A 124 22.737 17.146 -20.984 1.00 33.43 C -ANISOU 930 CA ILE A 124 4590 4841 3272 312 10 164 C -ATOM 931 C ILE A 124 22.091 16.702 -19.661 1.00 31.07 C -ANISOU 931 C ILE A 124 4268 4442 3095 270 -34 81 C -ATOM 932 O ILE A 124 21.042 17.217 -19.275 1.00 28.09 O -ANISOU 932 O ILE A 124 3901 3979 2792 225 -101 58 O -ATOM 933 CB ILE A 124 22.819 18.696 -21.084 1.00 34.12 C -ANISOU 933 CB ILE A 124 4654 4924 3388 231 3 275 C -ATOM 934 CG1 ILE A 124 23.659 19.122 -22.295 1.00 35.79 C -ANISOU 934 CG1 ILE A 124 4868 5250 3479 263 63 380 C -ATOM 935 CG2 ILE A 124 23.430 19.305 -19.811 1.00 31.00 C -ANISOU 935 CG2 ILE A 124 4180 4498 3100 138 21 325 C -ATOM 936 CD1 ILE A 124 22.954 19.016 -23.638 1.00 36.66 C -ANISOU 936 CD1 ILE A 124 5070 5379 3479 336 28 357 C -ATOM 937 N PRO A 125 22.689 15.711 -18.980 1.00 29.99 N -ANISOU 937 N PRO A 125 4101 4320 2976 294 5 39 N -ATOM 938 CA PRO A 125 21.950 15.075 -17.879 1.00 26.99 C -ANISOU 938 CA PRO A 125 3713 3848 2693 269 -41 -46 C -ATOM 939 C PRO A 125 21.925 15.908 -16.601 1.00 25.63 C -ANISOU 939 C PRO A 125 3481 3622 2634 178 -46 -13 C -ATOM 940 O PRO A 125 22.558 15.511 -15.628 1.00 26.00 O -ANISOU 940 O PRO A 125 3482 3672 2726 160 -13 -19 O -ATOM 941 CB PRO A 125 22.715 13.759 -17.666 1.00 30.40 C -ANISOU 941 CB PRO A 125 4140 4317 3092 332 3 -92 C -ATOM 942 CG PRO A 125 24.136 14.099 -18.058 1.00 33.98 C -ANISOU 942 CG PRO A 125 4547 4885 3478 353 92 0 C -ATOM 943 CD PRO A 125 24.057 15.179 -19.129 1.00 31.92 C -ANISOU 943 CD PRO A 125 4307 4666 3154 344 92 77 C -ATOM 944 N VAL A 126 21.184 17.017 -16.584 1.00 24.83 N -ANISOU 944 N VAL A 126 3390 3470 2574 130 -91 15 N -ATOM 945 CA VAL A 126 21.252 17.949 -15.453 1.00 25.00 C -ANISOU 945 CA VAL A 126 3373 3440 2686 54 -97 50 C -ATOM 946 C VAL A 126 20.775 17.304 -14.152 1.00 23.02 C -ANISOU 946 C VAL A 126 3100 3127 2518 41 -111 -21 C -ATOM 947 O VAL A 126 21.248 17.662 -13.082 1.00 20.83 O -ANISOU 947 O VAL A 126 2789 2829 2297 -6 -96 -2 O -ATOM 948 CB VAL A 126 20.448 19.255 -15.719 1.00 21.04 C -ANISOU 948 CB VAL A 126 2902 2884 2208 21 -150 86 C -ATOM 949 CG1 VAL A 126 21.100 20.055 -16.851 1.00 22.15 C -ANISOU 949 CG1 VAL A 126 3059 3086 2273 15 -132 181 C -ATOM 950 CG2 VAL A 126 18.980 18.973 -16.051 1.00 20.90 C -ANISOU 950 CG2 VAL A 126 2922 2817 2203 57 -214 19 C -ATOM 951 N GLY A 127 19.860 16.343 -14.241 1.00 23.16 N -ANISOU 951 N GLY A 127 3140 3117 2541 80 -144 -99 N -ATOM 952 CA GLY A 127 19.448 15.605 -13.059 1.00 20.63 C -ANISOU 952 CA GLY A 127 2795 2750 2294 69 -152 -157 C -ATOM 953 C GLY A 127 20.582 14.796 -12.435 1.00 23.30 C -ANISOU 953 C GLY A 127 3102 3123 2628 74 -99 -161 C -ATOM 954 O GLY A 127 20.770 14.810 -11.209 1.00 21.59 O -ANISOU 954 O GLY A 127 2852 2878 2474 38 -86 -164 O -ATOM 955 N GLU A 128 21.330 14.071 -13.265 1.00 24.29 N -ANISOU 955 N GLU A 128 3243 3311 2676 126 -67 -162 N -ATOM 956 CA GLU A 128 22.469 13.287 -12.775 1.00 25.37 C -ANISOU 956 CA GLU A 128 3347 3491 2802 146 -14 -161 C -ATOM 957 C GLU A 128 23.581 14.177 -12.248 1.00 22.60 C -ANISOU 957 C GLU A 128 2939 3181 2469 95 30 -78 C -ATOM 958 O GLU A 128 24.222 13.854 -11.244 1.00 21.63 O -ANISOU 958 O GLU A 128 2774 3058 2385 75 53 -76 O -ATOM 959 CB GLU A 128 23.023 12.383 -13.875 1.00 29.22 C -ANISOU 959 CB GLU A 128 3869 4042 3190 233 12 -178 C -ATOM 960 CG GLU A 128 22.134 11.205 -14.162 1.00 34.04 C -ANISOU 960 CG GLU A 128 4544 4601 3791 280 -41 -269 C -ATOM 961 CD GLU A 128 21.645 10.544 -12.876 1.00 36.19 C -ANISOU 961 CD GLU A 128 4795 4800 4156 243 -68 -316 C -ATOM 962 OE1 GLU A 128 22.484 10.004 -12.112 1.00 35.30 O -ANISOU 962 OE1 GLU A 128 4650 4703 4060 250 -28 -314 O -ATOM 963 OE2 GLU A 128 20.421 10.584 -12.622 1.00 37.23 O -ANISOU 963 OE2 GLU A 128 4937 4865 4344 208 -127 -347 O -ATOM 964 N ILE A 129 23.832 15.286 -12.934 1.00 20.23 N -ANISOU 964 N ILE A 129 2636 2912 2138 70 35 -5 N -ATOM 965 CA ILE A 129 24.872 16.215 -12.481 1.00 22.28 C -ANISOU 965 CA ILE A 129 2842 3203 2419 6 62 86 C -ATOM 966 C ILE A 129 24.506 16.826 -11.123 1.00 22.67 C -ANISOU 966 C ILE A 129 2885 3167 2563 -65 23 75 C -ATOM 967 O ILE A 129 25.346 16.936 -10.224 1.00 20.12 O -ANISOU 967 O ILE A 129 2519 2851 2276 -107 37 106 O -ATOM 968 CB ILE A 129 25.104 17.351 -13.504 1.00 24.89 C -ANISOU 968 CB ILE A 129 3180 3573 2705 -17 64 175 C -ATOM 969 CG1 ILE A 129 25.515 16.772 -14.857 1.00 26.68 C -ANISOU 969 CG1 ILE A 129 3417 3896 2823 64 110 191 C -ATOM 970 CG2 ILE A 129 26.194 18.312 -13.006 1.00 24.63 C -ANISOU 970 CG2 ILE A 129 3089 3565 2705 -100 77 279 C -ATOM 971 CD1 ILE A 129 25.339 17.749 -16.005 1.00 28.96 C -ANISOU 971 CD1 ILE A 129 3735 4212 3055 56 101 260 C -ATOM 972 N TYR A 130 23.245 17.211 -10.960 1.00 19.10 N -ANISOU 972 N TYR A 130 2475 2635 2145 -71 -27 30 N -ATOM 973 CA TYR A 130 22.828 17.803 -9.685 1.00 20.96 C -ANISOU 973 CA TYR A 130 2715 2792 2457 -119 -59 15 C -ATOM 974 C TYR A 130 22.847 16.759 -8.554 1.00 19.74 C -ANISOU 974 C TYR A 130 2538 2623 2340 -108 -45 -44 C -ATOM 975 O TYR A 130 23.262 17.051 -7.424 1.00 20.74 O -ANISOU 975 O TYR A 130 2651 2722 2509 -149 -48 -34 O -ATOM 976 CB TYR A 130 21.440 18.421 -9.832 1.00 22.64 C -ANISOU 976 CB TYR A 130 2972 2938 2693 -110 -108 -16 C -ATOM 977 CG TYR A 130 20.943 19.231 -8.650 1.00 21.78 C -ANISOU 977 CG TYR A 130 2880 2749 2645 -141 -139 -27 C -ATOM 978 CD1 TYR A 130 21.813 19.770 -7.721 1.00 20.01 C -ANISOU 978 CD1 TYR A 130 2649 2506 2447 -193 -140 7 C -ATOM 979 CD2 TYR A 130 19.577 19.469 -8.485 1.00 22.20 C -ANISOU 979 CD2 TYR A 130 2959 2748 2729 -112 -172 -70 C -ATOM 980 CE1 TYR A 130 21.335 20.522 -6.635 1.00 19.33 C -ANISOU 980 CE1 TYR A 130 2598 2342 2405 -208 -173 -11 C -ATOM 981 CE2 TYR A 130 19.103 20.221 -7.416 1.00 21.64 C -ANISOU 981 CE2 TYR A 130 2910 2611 2703 -120 -195 -82 C -ATOM 982 CZ TYR A 130 19.986 20.745 -6.495 1.00 19.23 C -ANISOU 982 CZ TYR A 130 2615 2280 2413 -165 -196 -57 C -ATOM 983 OH TYR A 130 19.495 21.488 -5.425 1.00 19.91 O -ANISOU 983 OH TYR A 130 2741 2294 2531 -161 -222 -78 O -ATOM 984 N LYS A 131 22.417 15.542 -8.865 1.00 21.22 N -ANISOU 984 N LYS A 131 2730 2823 2511 -54 -36 -102 N -ATOM 985 CA LYS A 131 22.443 14.457 -7.886 1.00 23.26 C -ANISOU 985 CA LYS A 131 2971 3066 2801 -43 -25 -151 C -ATOM 986 C LYS A 131 23.863 14.196 -7.348 1.00 22.20 C -ANISOU 986 C LYS A 131 2794 2979 2661 -57 14 -114 C -ATOM 987 O LYS A 131 24.046 13.979 -6.156 1.00 19.23 O -ANISOU 987 O LYS A 131 2401 2576 2328 -80 14 -126 O -ATOM 988 CB LYS A 131 21.866 13.172 -8.488 1.00 23.84 C -ANISOU 988 CB LYS A 131 3065 3142 2851 13 -33 -211 C -ATOM 989 CG LYS A 131 21.562 12.106 -7.412 1.00 23.34 C -ANISOU 989 CG LYS A 131 2993 3041 2835 15 -37 -260 C -ATOM 990 CD LYS A 131 21.288 10.711 -8.021 1.00 27.35 C -ANISOU 990 CD LYS A 131 3529 3547 3316 66 -52 -313 C -ATOM 991 CE LYS A 131 19.925 10.595 -8.676 1.00 30.49 C -ANISOU 991 CE LYS A 131 3959 3905 3720 73 -108 -346 C -ATOM 992 NZ LYS A 131 19.500 9.136 -8.784 1.00 33.17 N -ANISOU 992 NZ LYS A 131 4329 4212 4064 100 -143 -402 N -ATOM 993 N ARG A 132 24.863 14.236 -8.228 1.00 22.53 N -ANISOU 993 N ARG A 132 2814 3097 2648 -40 47 -62 N -ATOM 994 CA ARG A 132 26.250 14.080 -7.800 1.00 23.40 C -ANISOU 994 CA ARG A 132 2868 3267 2756 -53 84 -11 C -ATOM 995 C ARG A 132 26.663 15.162 -6.785 1.00 21.24 C -ANISOU 995 C ARG A 132 2573 2961 2536 -139 59 39 C -ATOM 996 O ARG A 132 27.303 14.856 -5.772 1.00 21.76 O -ANISOU 996 O ARG A 132 2608 3027 2632 -160 62 44 O -ATOM 997 CB ARG A 132 27.187 14.112 -9.012 1.00 25.29 C -ANISOU 997 CB ARG A 132 3078 3607 2923 -18 129 53 C -ATOM 998 CG ARG A 132 28.600 13.642 -8.714 1.00 32.51 C -ANISOU 998 CG ARG A 132 3921 4604 3827 -6 176 103 C -ATOM 999 CD ARG A 132 29.592 14.097 -9.788 1.00 36.59 C -ANISOU 999 CD ARG A 132 4389 5232 4282 7 225 201 C -ATOM 1000 NE ARG A 132 29.037 14.050 -11.139 1.00 41.09 N -ANISOU 1000 NE ARG A 132 5011 5826 4777 69 237 185 N -ATOM 1001 CZ ARG A 132 28.510 15.094 -11.776 1.00 45.34 C -ANISOU 1001 CZ ARG A 132 5578 6344 5303 28 212 220 C -ATOM 1002 NH1 ARG A 132 28.452 16.279 -11.176 1.00 46.71 N -ANISOU 1002 NH1 ARG A 132 5741 6466 5540 -72 170 270 N -ATOM 1003 NH2 ARG A 132 28.035 14.955 -13.015 1.00 45.22 N -ANISOU 1003 NH2 ARG A 132 5613 6357 5213 92 221 204 N -ATOM 1004 N TRP A 133 26.314 16.418 -7.066 1.00 19.36 N -ANISOU 1004 N TRP A 133 2361 2689 2305 -186 26 77 N -ATOM 1005 CA TRP A 133 26.589 17.526 -6.132 1.00 20.67 C -ANISOU 1005 CA TRP A 133 2533 2803 2519 -265 -16 116 C -ATOM 1006 C TRP A 133 25.934 17.296 -4.768 1.00 21.68 C -ANISOU 1006 C TRP A 133 2691 2854 2694 -268 -41 47 C -ATOM 1007 O TRP A 133 26.537 17.551 -3.721 1.00 22.58 O -ANISOU 1007 O TRP A 133 2796 2946 2837 -313 -61 64 O -ATOM 1008 CB TRP A 133 26.098 18.863 -6.690 1.00 22.36 C -ANISOU 1008 CB TRP A 133 2790 2973 2732 -302 -56 154 C -ATOM 1009 CG TRP A 133 26.705 19.293 -7.980 1.00 23.00 C -ANISOU 1009 CG TRP A 133 2848 3126 2767 -311 -35 237 C -ATOM 1010 CD1 TRP A 133 27.740 18.703 -8.638 1.00 24.33 C -ANISOU 1010 CD1 TRP A 133 2951 3402 2890 -290 20 290 C -ATOM 1011 CD2 TRP A 133 26.303 20.409 -8.776 1.00 24.07 C -ANISOU 1011 CD2 TRP A 133 3022 3234 2889 -337 -67 283 C -ATOM 1012 NE1 TRP A 133 28.019 19.397 -9.801 1.00 26.41 N -ANISOU 1012 NE1 TRP A 133 3209 3716 3110 -303 31 371 N -ATOM 1013 CE2 TRP A 133 27.149 20.449 -9.903 1.00 27.32 C -ANISOU 1013 CE2 TRP A 133 3389 3745 3245 -336 -26 369 C -ATOM 1014 CE3 TRP A 133 25.304 21.384 -8.648 1.00 25.10 C -ANISOU 1014 CE3 TRP A 133 3222 3268 3045 -352 -124 263 C -ATOM 1015 CZ2 TRP A 133 27.011 21.409 -10.904 1.00 26.69 C -ANISOU 1015 CZ2 TRP A 133 3335 3670 3137 -359 -42 438 C -ATOM 1016 CZ3 TRP A 133 25.180 22.345 -9.639 1.00 24.57 C -ANISOU 1016 CZ3 TRP A 133 3183 3198 2953 -373 -146 327 C -ATOM 1017 CH2 TRP A 133 26.031 22.352 -10.749 1.00 24.61 C -ANISOU 1017 CH2 TRP A 133 3145 3302 2905 -381 -107 415 C -ATOM 1018 N ILE A 134 24.685 16.834 -4.793 1.00 21.53 N -ANISOU 1018 N ILE A 134 2705 2796 2679 -220 -43 -25 N -ATOM 1019 CA ILE A 134 23.921 16.593 -3.577 1.00 19.66 C -ANISOU 1019 CA ILE A 134 2492 2497 2480 -212 -57 -83 C -ATOM 1020 C ILE A 134 24.554 15.456 -2.763 1.00 19.44 C -ANISOU 1020 C ILE A 134 2429 2495 2461 -203 -31 -102 C -ATOM 1021 O ILE A 134 24.715 15.562 -1.548 1.00 19.30 O -ANISOU 1021 O ILE A 134 2420 2445 2469 -226 -45 -110 O -ATOM 1022 CB ILE A 134 22.449 16.265 -3.896 1.00 17.88 C -ANISOU 1022 CB ILE A 134 2290 2242 2261 -165 -62 -140 C -ATOM 1023 CG1 ILE A 134 21.737 17.495 -4.481 1.00 17.50 C -ANISOU 1023 CG1 ILE A 134 2281 2157 2211 -170 -95 -123 C -ATOM 1024 CG2 ILE A 134 21.713 15.794 -2.639 1.00 16.78 C -ANISOU 1024 CG2 ILE A 134 2158 2062 2157 -152 -62 -189 C -ATOM 1025 CD1 ILE A 134 20.363 17.150 -5.109 1.00 16.15 C -ANISOU 1025 CD1 ILE A 134 2119 1976 2042 -123 -104 -165 C -ATOM 1026 N ILE A 135 24.938 14.384 -3.434 1.00 20.94 N -ANISOU 1026 N ILE A 135 2589 2741 2624 -163 2 -109 N -ATOM 1027 CA ILE A 135 25.532 13.254 -2.722 1.00 22.88 C -ANISOU 1027 CA ILE A 135 2808 3008 2879 -145 23 -126 C -ATOM 1028 C ILE A 135 26.889 13.649 -2.119 1.00 22.97 C -ANISOU 1028 C ILE A 135 2779 3052 2896 -190 23 -66 C -ATOM 1029 O ILE A 135 27.254 13.201 -1.020 1.00 22.64 O -ANISOU 1029 O ILE A 135 2728 2999 2876 -199 18 -76 O -ATOM 1030 CB ILE A 135 25.640 12.014 -3.658 1.00 24.42 C -ANISOU 1030 CB ILE A 135 2994 3248 3037 -79 52 -151 C -ATOM 1031 CG1 ILE A 135 24.232 11.489 -3.940 1.00 25.86 C -ANISOU 1031 CG1 ILE A 135 3217 3381 3228 -50 32 -213 C -ATOM 1032 CG2 ILE A 135 26.490 10.890 -3.029 1.00 24.71 C -ANISOU 1032 CG2 ILE A 135 3002 3311 3076 -53 74 -157 C -ATOM 1033 CD1 ILE A 135 24.181 10.339 -4.926 1.00 27.92 C -ANISOU 1033 CD1 ILE A 135 3494 3664 3449 13 40 -247 C -ATOM 1034 N LEU A 136 27.620 14.505 -2.823 1.00 22.57 N -ANISOU 1034 N LEU A 136 2704 3043 2828 -222 21 3 N -ATOM 1035 CA LEU A 136 28.879 15.040 -2.326 1.00 23.33 C -ANISOU 1035 CA LEU A 136 2755 3170 2938 -282 8 76 C -ATOM 1036 C LEU A 136 28.635 15.784 -1.002 1.00 22.69 C -ANISOU 1036 C LEU A 136 2718 3006 2896 -339 -48 62 C -ATOM 1037 O LEU A 136 29.372 15.616 -0.036 1.00 19.98 O -ANISOU 1037 O LEU A 136 2354 2666 2572 -368 -65 78 O -ATOM 1038 CB LEU A 136 29.511 15.962 -3.388 1.00 27.01 C -ANISOU 1038 CB LEU A 136 3190 3688 3383 -317 10 163 C -ATOM 1039 CG LEU A 136 30.876 16.625 -3.198 1.00 35.37 C -ANISOU 1039 CG LEU A 136 4184 4797 4457 -392 -7 268 C -ATOM 1040 CD1 LEU A 136 31.362 17.183 -4.530 1.00 38.15 C -ANISOU 1040 CD1 LEU A 136 4496 5225 4775 -403 19 355 C -ATOM 1041 CD2 LEU A 136 30.840 17.723 -2.147 1.00 38.98 C -ANISOU 1041 CD2 LEU A 136 4687 5165 4960 -481 -86 281 C -ATOM 1042 N GLY A 137 27.589 16.604 -0.960 1.00 23.79 N -ANISOU 1042 N GLY A 137 2924 3073 3044 -347 -78 32 N -ATOM 1043 CA GLY A 137 27.216 17.300 0.258 1.00 21.18 C -ANISOU 1043 CA GLY A 137 2653 2660 2736 -378 -128 7 C -ATOM 1044 C GLY A 137 26.725 16.371 1.360 1.00 22.66 C -ANISOU 1044 C GLY A 137 2854 2825 2931 -339 -112 -58 C -ATOM 1045 O GLY A 137 27.093 16.543 2.532 1.00 24.75 O -ANISOU 1045 O GLY A 137 3140 3058 3205 -366 -143 -61 O -ATOM 1046 N LEU A 138 25.886 15.406 0.999 1.00 22.61 N -ANISOU 1046 N LEU A 138 2839 2832 2919 -279 -71 -106 N -ATOM 1047 CA LEU A 138 25.324 14.481 1.983 1.00 24.01 C -ANISOU 1047 CA LEU A 138 3025 2990 3106 -246 -54 -157 C -ATOM 1048 C LEU A 138 26.449 13.638 2.611 1.00 23.46 C -ANISOU 1048 C LEU A 138 2916 2958 3039 -255 -46 -139 C -ATOM 1049 O LEU A 138 26.429 13.355 3.813 1.00 24.13 O -ANISOU 1049 O LEU A 138 3020 3018 3131 -256 -55 -158 O -ATOM 1050 CB LEU A 138 24.268 13.566 1.353 1.00 23.41 C -ANISOU 1050 CB LEU A 138 2941 2920 3031 -194 -24 -199 C -ATOM 1051 CG LEU A 138 22.911 14.133 0.935 1.00 23.74 C -ANISOU 1051 CG LEU A 138 3014 2928 3079 -174 -31 -223 C -ATOM 1052 CD1 LEU A 138 22.104 13.075 0.165 1.00 20.85 C -ANISOU 1052 CD1 LEU A 138 2629 2577 2717 -136 -14 -253 C -ATOM 1053 CD2 LEU A 138 22.147 14.696 2.124 1.00 21.35 C -ANISOU 1053 CD2 LEU A 138 2750 2574 2786 -169 -42 -245 C -ATOM 1054 N ASN A 139 27.440 13.275 1.805 1.00 23.44 N -ANISOU 1054 N ASN A 139 2860 3020 3026 -254 -29 -99 N -ATOM 1055 CA ASN A 139 28.582 12.508 2.314 1.00 25.85 C -ANISOU 1055 CA ASN A 139 3118 3370 3334 -253 -21 -74 C -ATOM 1056 C ASN A 139 29.348 13.300 3.381 1.00 23.78 C -ANISOU 1056 C ASN A 139 2861 3088 3085 -318 -70 -37 C -ATOM 1057 O ASN A 139 29.729 12.750 4.424 1.00 23.81 O -ANISOU 1057 O ASN A 139 2863 3088 3097 -318 -81 -44 O -ATOM 1058 CB ASN A 139 29.513 12.100 1.170 1.00 28.94 C -ANISOU 1058 CB ASN A 139 3445 3846 3704 -228 13 -29 C -ATOM 1059 CG ASN A 139 28.953 10.957 0.349 1.00 31.66 C -ANISOU 1059 CG ASN A 139 3797 4205 4028 -151 52 -77 C -ATOM 1060 OD1 ASN A 139 27.985 10.314 0.749 1.00 34.02 O -ANISOU 1060 OD1 ASN A 139 4136 4453 4338 -127 50 -135 O -ATOM 1061 ND2 ASN A 139 29.553 10.705 -0.809 1.00 33.04 N -ANISOU 1061 ND2 ASN A 139 3935 4450 4168 -112 85 -48 N -ATOM 1062 N LYS A 140 29.565 14.587 3.128 1.00 25.54 N -ANISOU 1062 N LYS A 140 3098 3293 3312 -375 -109 4 N -ATOM 1063 CA LYS A 140 30.165 15.479 4.131 1.00 28.25 C -ANISOU 1063 CA LYS A 140 3468 3596 3668 -444 -177 34 C -ATOM 1064 C LYS A 140 29.348 15.480 5.424 1.00 27.73 C -ANISOU 1064 C LYS A 140 3483 3456 3597 -426 -198 -31 C -ATOM 1065 O LYS A 140 29.897 15.468 6.521 1.00 27.76 O -ANISOU 1065 O LYS A 140 3504 3443 3602 -452 -238 -27 O -ATOM 1066 CB LYS A 140 30.285 16.920 3.599 1.00 33.15 C -ANISOU 1066 CB LYS A 140 4114 4186 4295 -508 -227 82 C -ATOM 1067 CG LYS A 140 31.244 17.105 2.431 1.00 37.61 C -ANISOU 1067 CG LYS A 140 4595 4832 4862 -540 -211 170 C -ATOM 1068 CD LYS A 140 31.254 18.549 1.917 1.00 41.36 C -ANISOU 1068 CD LYS A 140 5104 5266 5345 -610 -265 222 C -ATOM 1069 CE LYS A 140 31.637 19.544 3.009 1.00 43.00 C -ANISOU 1069 CE LYS A 140 5372 5392 5575 -691 -364 240 C -ATOM 1070 NZ LYS A 140 31.876 20.933 2.495 1.00 44.51 N -ANISOU 1070 NZ LYS A 140 5592 5538 5780 -774 -432 309 N -ATOM 1071 N ILE A 141 28.026 15.510 5.290 1.00 29.18 N -ANISOU 1071 N ILE A 141 3715 3601 3772 -379 -172 -88 N -ATOM 1072 CA ILE A 141 27.148 15.513 6.447 1.00 26.48 C -ANISOU 1072 CA ILE A 141 3442 3202 3418 -348 -177 -143 C -ATOM 1073 C ILE A 141 27.224 14.197 7.222 1.00 28.42 C -ANISOU 1073 C ILE A 141 3663 3475 3662 -316 -144 -162 C -ATOM 1074 O ILE A 141 27.276 14.197 8.456 1.00 30.48 O -ANISOU 1074 O ILE A 141 3966 3707 3907 -317 -166 -178 O -ATOM 1075 CB ILE A 141 25.698 15.756 6.051 1.00 27.50 C -ANISOU 1075 CB ILE A 141 3605 3301 3541 -299 -148 -186 C -ATOM 1076 CG1 ILE A 141 25.538 17.183 5.500 1.00 26.37 C -ANISOU 1076 CG1 ILE A 141 3509 3113 3397 -325 -191 -171 C -ATOM 1077 CG2 ILE A 141 24.774 15.518 7.261 1.00 28.37 C -ANISOU 1077 CG2 ILE A 141 3765 3378 3636 -253 -133 -234 C -ATOM 1078 CD1 ILE A 141 24.206 17.411 4.864 1.00 25.23 C -ANISOU 1078 CD1 ILE A 141 3382 2953 3252 -274 -164 -202 C -ATOM 1079 N VAL A 142 27.229 13.083 6.500 1.00 23.09 N -ANISOU 1079 N VAL A 142 2927 2849 2996 -285 -97 -162 N -ATOM 1080 CA VAL A 142 27.339 11.767 7.138 1.00 23.58 C -ANISOU 1080 CA VAL A 142 2968 2930 3060 -256 -71 -176 C -ATOM 1081 C VAL A 142 28.648 11.695 7.954 1.00 25.11 C -ANISOU 1081 C VAL A 142 3146 3143 3254 -289 -107 -140 C -ATOM 1082 O VAL A 142 28.677 11.225 9.101 1.00 25.14 O -ANISOU 1082 O VAL A 142 3174 3131 3249 -282 -116 -152 O -ATOM 1083 CB VAL A 142 27.282 10.642 6.082 1.00 21.29 C -ANISOU 1083 CB VAL A 142 2629 2681 2780 -216 -29 -181 C -ATOM 1084 CG1 VAL A 142 27.876 9.342 6.625 1.00 22.86 C -ANISOU 1084 CG1 VAL A 142 2802 2901 2982 -193 -18 -178 C -ATOM 1085 CG2 VAL A 142 25.860 10.432 5.576 1.00 20.65 C -ANISOU 1085 CG2 VAL A 142 2568 2575 2704 -185 -5 -220 C -ATOM 1086 N ARG A 143 29.731 12.175 7.357 1.00 25.24 N -ANISOU 1086 N ARG A 143 3116 3197 3278 -328 -131 -88 N -ATOM 1087 CA ARG A 143 31.020 12.205 8.040 1.00 29.64 C -ANISOU 1087 CA ARG A 143 3642 3779 3841 -369 -175 -41 C -ATOM 1088 C ARG A 143 31.016 13.160 9.249 1.00 28.44 C -ANISOU 1088 C ARG A 143 3566 3562 3677 -415 -244 -48 C -ATOM 1089 O ARG A 143 31.642 12.881 10.262 1.00 27.86 O -ANISOU 1089 O ARG A 143 3499 3488 3598 -430 -280 -37 O -ATOM 1090 CB ARG A 143 32.141 12.581 7.053 1.00 33.34 C -ANISOU 1090 CB ARG A 143 4030 4312 4324 -404 -182 32 C -ATOM 1091 CG ARG A 143 32.525 11.448 6.102 1.00 37.15 C -ANISOU 1091 CG ARG A 143 4436 4873 4805 -343 -117 45 C -ATOM 1092 CD ARG A 143 33.793 11.732 5.305 1.00 42.25 C -ANISOU 1092 CD ARG A 143 4988 5605 5459 -368 -116 131 C -ATOM 1093 NE ARG A 143 33.540 12.732 4.277 1.00 46.15 N -ANISOU 1093 NE ARG A 143 5485 6103 5949 -399 -114 157 N -ATOM 1094 CZ ARG A 143 33.316 12.453 2.996 1.00 44.96 C -ANISOU 1094 CZ ARG A 143 5308 5997 5777 -349 -56 157 C -ATOM 1095 NH1 ARG A 143 33.351 11.199 2.562 1.00 45.89 N -ANISOU 1095 NH1 ARG A 143 5401 6160 5877 -263 0 129 N -ATOM 1096 NH2 ARG A 143 33.071 13.436 2.151 1.00 43.64 N -ANISOU 1096 NH2 ARG A 143 5149 5827 5603 -383 -61 185 N -ATOM 1097 N MET A 144 30.294 14.269 9.165 1.00 30.15 N -ANISOU 1097 N MET A 144 3851 3720 3884 -431 -268 -70 N -ATOM 1098 CA MET A 144 30.279 15.214 10.284 1.00 31.12 C -ANISOU 1098 CA MET A 144 4067 3773 3985 -463 -341 -85 C -ATOM 1099 C MET A 144 29.549 14.645 11.489 1.00 29.90 C -ANISOU 1099 C MET A 144 3973 3590 3796 -408 -320 -139 C -ATOM 1100 O MET A 144 29.997 14.798 12.644 1.00 32.69 O -ANISOU 1100 O MET A 144 4378 3916 4125 -426 -375 -142 O -ATOM 1101 CB MET A 144 29.626 16.545 9.888 1.00 32.53 C -ANISOU 1101 CB MET A 144 4317 3887 4157 -478 -372 -99 C -ATOM 1102 CG MET A 144 29.300 17.440 11.107 1.00 34.43 C -ANISOU 1102 CG MET A 144 4684 4039 4360 -478 -439 -139 C -ATOM 1103 SD MET A 144 28.911 19.120 10.609 1.00 99.49 S -ANISOU 1103 SD MET A 144 13012 12193 12598 -508 -504 -141 S -ATOM 1104 CE MET A 144 30.359 19.497 9.635 1.00 39.99 C -ANISOU 1104 CE MET A 144 5384 4698 5112 -619 -557 -39 C -ATOM 1105 N TYR A 145 28.420 14.004 11.232 1.00 25.81 N -ANISOU 1105 N TYR A 145 3451 3080 3274 -345 -246 -178 N -ATOM 1106 CA TYR A 145 27.581 13.519 12.326 1.00 29.38 C -ANISOU 1106 CA TYR A 145 3955 3514 3693 -293 -217 -218 C -ATOM 1107 C TYR A 145 27.988 12.118 12.808 1.00 27.57 C -ANISOU 1107 C TYR A 145 3678 3328 3470 -278 -189 -205 C -ATOM 1108 O TYR A 145 27.371 11.574 13.712 1.00 27.22 O -ANISOU 1108 O TYR A 145 3666 3276 3400 -240 -162 -225 O -ATOM 1109 CB TYR A 145 26.119 13.524 11.904 1.00 33.12 C -ANISOU 1109 CB TYR A 145 4440 3980 4166 -239 -157 -253 C -ATOM 1110 CG TYR A 145 25.582 14.913 11.625 1.00 37.00 C -ANISOU 1110 CG TYR A 145 4994 4420 4643 -236 -185 -271 C -ATOM 1111 CD1 TYR A 145 26.379 16.046 11.822 1.00 39.12 C -ANISOU 1111 CD1 TYR A 145 5319 4643 4901 -285 -266 -259 C -ATOM 1112 CD2 TYR A 145 24.288 15.095 11.166 1.00 36.91 C -ANISOU 1112 CD2 TYR A 145 4988 4404 4633 -185 -139 -297 C -ATOM 1113 CE1 TYR A 145 25.900 17.317 11.560 1.00 40.34 C -ANISOU 1113 CE1 TYR A 145 5544 4739 5045 -281 -301 -276 C -ATOM 1114 CE2 TYR A 145 23.797 16.365 10.914 1.00 38.59 C -ANISOU 1114 CE2 TYR A 145 5262 4567 4833 -173 -167 -313 C -ATOM 1115 CZ TYR A 145 24.606 17.470 11.108 1.00 39.74 C -ANISOU 1115 CZ TYR A 145 5475 4659 4966 -218 -248 -305 C -ATOM 1116 OH TYR A 145 24.117 18.729 10.856 1.00 44.01 O -ANISOU 1116 OH TYR A 145 6089 5138 5494 -204 -284 -322 O -ATOM 1117 N SER A 146 28.996 11.525 12.176 1.00 28.42 N -ANISOU 1117 N SER A 146 3707 3482 3610 -301 -193 -167 N -ATOM 1118 CA SER A 146 29.618 10.297 12.698 1.00 27.43 C -ANISOU 1118 CA SER A 146 3544 3390 3490 -287 -184 -150 C -ATOM 1119 C SER A 146 30.091 10.560 14.141 1.00 26.69 C -ANISOU 1119 C SER A 146 3509 3270 3360 -306 -240 -146 C -ATOM 1120 O SER A 146 30.980 11.363 14.366 1.00 26.44 O -ANISOU 1120 O SER A 146 3488 3231 3328 -357 -310 -121 O -ATOM 1121 CB SER A 146 30.791 9.867 11.793 1.00 29.13 C -ANISOU 1121 CB SER A 146 3668 3662 3737 -302 -187 -104 C -ATOM 1122 OG SER A 146 31.330 8.601 12.161 1.00 29.85 O -ANISOU 1122 OG SER A 146 3722 3784 3835 -272 -173 -90 O -ATOM 1123 N PRO A 147 29.481 9.902 15.129 1.00 28.09 N -ANISOU 1123 N PRO A 147 3729 3436 3509 -267 -215 -167 N -ATOM 1124 CA PRO A 147 29.791 10.319 16.504 1.00 32.94 C -ANISOU 1124 CA PRO A 147 4421 4022 4073 -277 -270 -171 C -ATOM 1125 C PRO A 147 31.113 9.767 17.059 1.00 32.89 C -ANISOU 1125 C PRO A 147 4381 4041 4073 -305 -324 -130 C -ATOM 1126 O PRO A 147 31.575 10.252 18.088 1.00 30.71 O -ANISOU 1126 O PRO A 147 4168 3740 3758 -326 -392 -129 O -ATOM 1127 CB PRO A 147 28.621 9.758 17.298 1.00 32.92 C -ANISOU 1127 CB PRO A 147 4466 4011 4033 -220 -212 -197 C -ATOM 1128 CG PRO A 147 28.281 8.501 16.577 1.00 32.27 C -ANISOU 1128 CG PRO A 147 4306 3960 3995 -199 -148 -185 C -ATOM 1129 CD PRO A 147 28.552 8.765 15.094 1.00 29.64 C -ANISOU 1129 CD PRO A 147 3909 3643 3712 -219 -144 -180 C -ATOM 1130 N THR A 148 31.717 8.774 16.409 1.00 33.00 N -ANISOU 1130 N THR A 148 4303 4104 4131 -298 -299 -99 N -ATOM 1131 CA THR A 148 32.851 8.104 17.047 1.00 32.17 C -ANISOU 1131 CA THR A 148 4166 4027 4029 -306 -342 -59 C -ATOM 1132 C THR A 148 34.019 7.848 16.101 1.00 29.65 C -ANISOU 1132 C THR A 148 3738 3768 3761 -323 -352 -10 C -ATOM 1133 O THR A 148 33.830 7.542 14.926 1.00 28.65 O -ANISOU 1133 O THR A 148 3555 3667 3664 -299 -297 -11 O -ATOM 1134 CB THR A 148 32.399 6.773 17.682 1.00 36.07 C -ANISOU 1134 CB THR A 148 4672 4522 4510 -254 -297 -66 C -ATOM 1135 OG1 THR A 148 31.397 7.044 18.673 1.00 38.02 O -ANISOU 1135 OG1 THR A 148 5013 4730 4702 -237 -284 -98 O -ATOM 1136 CG2 THR A 148 33.577 6.048 18.341 1.00 33.89 C -ANISOU 1136 CG2 THR A 148 4365 4275 4238 -255 -344 -23 C -ATOM 1137 N SER A 149 35.234 8.013 16.616 1.00 26.89 N -ANISOU 1137 N SER A 149 3357 3442 3417 -361 -425 38 N -ATOM 1138 CA SER A 149 36.429 7.716 15.841 1.00 29.47 C -ANISOU 1138 CA SER A 149 3566 3842 3788 -368 -432 99 C -ATOM 1139 C SER A 149 36.663 6.204 15.862 1.00 27.31 C -ANISOU 1139 C SER A 149 3249 3603 3525 -295 -387 106 C -ATOM 1140 O SER A 149 36.333 5.535 16.844 1.00 25.82 O -ANISOU 1140 O SER A 149 3117 3382 3310 -268 -390 87 O -ATOM 1141 CB SER A 149 37.645 8.471 16.399 1.00 32.47 C -ANISOU 1141 CB SER A 149 3918 4240 4178 -443 -536 159 C -ATOM 1142 OG SER A 149 38.870 7.979 15.872 1.00 33.68 O -ANISOU 1142 OG SER A 149 3943 4480 4373 -438 -539 231 O -ATOM 1143 N ILE A 150 37.217 5.673 14.777 1.00 22.10 N -ANISOU 1143 N ILE A 150 2495 3005 2896 -256 -344 135 N -ATOM 1144 CA ILE A 150 37.553 4.261 14.713 1.00 22.06 C -ANISOU 1144 CA ILE A 150 2453 3028 2900 -177 -310 142 C -ATOM 1145 C ILE A 150 38.567 3.923 15.807 1.00 22.44 C -ANISOU 1145 C ILE A 150 2480 3099 2949 -184 -376 189 C -ATOM 1146 O ILE A 150 38.631 2.794 16.271 1.00 20.87 O -ANISOU 1146 O ILE A 150 2293 2892 2746 -126 -366 185 O -ATOM 1147 CB ILE A 150 38.125 3.864 13.323 1.00 24.38 C -ANISOU 1147 CB ILE A 150 2652 3394 3218 -122 -257 168 C -ATOM 1148 CG1 ILE A 150 38.145 2.336 13.169 1.00 24.41 C -ANISOU 1148 CG1 ILE A 150 2653 3398 3222 -21 -216 151 C -ATOM 1149 CG2 ILE A 150 39.547 4.439 13.128 1.00 27.31 C -ANISOU 1149 CG2 ILE A 150 2911 3855 3613 -156 -297 253 C -ATOM 1150 CD1 ILE A 150 36.733 1.689 13.138 1.00 23.03 C -ANISOU 1150 CD1 ILE A 150 2576 3141 3035 7 -177 79 C -ATOM 1151 N LEU A 151 39.336 4.915 16.241 1.00 22.32 N -ANISOU 1151 N LEU A 151 2439 3103 2939 -260 -453 234 N -ATOM 1152 CA LEU A 151 40.328 4.697 17.290 1.00 27.19 C -ANISOU 1152 CA LEU A 151 3033 3742 3556 -278 -531 283 C -ATOM 1153 C LEU A 151 39.707 4.412 18.656 1.00 27.43 C -ANISOU 1153 C LEU A 151 3181 3700 3540 -277 -562 242 C -ATOM 1154 O LEU A 151 40.379 3.874 19.542 1.00 27.33 O -ANISOU 1154 O LEU A 151 3163 3700 3520 -266 -614 274 O -ATOM 1155 CB LEU A 151 41.267 5.905 17.401 1.00 31.53 C -ANISOU 1155 CB LEU A 151 3531 4323 4126 -375 -622 346 C -ATOM 1156 CG LEU A 151 42.074 6.219 16.143 1.00 34.55 C -ANISOU 1156 CG LEU A 151 3777 4796 4554 -384 -596 413 C -ATOM 1157 CD1 LEU A 151 42.627 7.646 16.190 1.00 35.00 C -ANISOU 1157 CD1 LEU A 151 3811 4856 4632 -505 -688 468 C -ATOM 1158 CD2 LEU A 151 43.199 5.212 16.013 1.00 37.04 C -ANISOU 1158 CD2 LEU A 151 3971 5205 4897 -317 -585 479 C -ATOM 1159 N ASP A 152 38.436 4.767 18.839 1.00 24.28 N -ANISOU 1159 N ASP A 152 2886 3233 3106 -283 -530 178 N -ATOM 1160 CA ASP A 152 37.741 4.463 20.101 1.00 27.55 C -ANISOU 1160 CA ASP A 152 3411 3591 3467 -270 -542 144 C -ATOM 1161 C ASP A 152 36.854 3.220 20.029 1.00 27.91 C -ANISOU 1161 C ASP A 152 3482 3615 3509 -199 -460 116 C -ATOM 1162 O ASP A 152 36.094 2.932 20.958 1.00 27.55 O -ANISOU 1162 O ASP A 152 3522 3526 3418 -187 -450 94 O -ATOM 1163 CB ASP A 152 36.886 5.650 20.540 1.00 32.68 C -ANISOU 1163 CB ASP A 152 4163 4182 4071 -313 -561 99 C -ATOM 1164 CG ASP A 152 37.731 6.870 20.909 1.00 37.70 C -ANISOU 1164 CG ASP A 152 4809 4814 4702 -392 -669 125 C -ATOM 1165 OD1 ASP A 152 38.702 6.714 21.677 1.00 37.15 O -ANISOU 1165 OD1 ASP A 152 4725 4762 4628 -414 -750 167 O -ATOM 1166 OD2 ASP A 152 37.423 7.976 20.425 1.00 39.45 O -ANISOU 1166 OD2 ASP A 152 5054 5010 4926 -435 -681 106 O -ATOM 1167 N ILE A 153 36.926 2.490 18.924 1.00 26.84 N -ANISOU 1167 N ILE A 153 3277 3506 3416 -153 -403 119 N -ATOM 1168 CA ILE A 153 36.170 1.251 18.827 1.00 25.37 C -ANISOU 1168 CA ILE A 153 3119 3288 3232 -92 -345 97 C -ATOM 1169 C ILE A 153 37.065 0.101 19.239 1.00 25.32 C -ANISOU 1169 C ILE A 153 3082 3301 3238 -43 -370 137 C -ATOM 1170 O ILE A 153 37.847 -0.411 18.433 1.00 24.02 O -ANISOU 1170 O ILE A 153 2839 3180 3107 4 -359 158 O -ATOM 1171 CB ILE A 153 35.630 0.991 17.412 1.00 24.87 C -ANISOU 1171 CB ILE A 153 3023 3226 3200 -60 -278 68 C -ATOM 1172 CG1 ILE A 153 34.750 2.158 16.952 1.00 22.53 C -ANISOU 1172 CG1 ILE A 153 2754 2913 2895 -106 -256 33 C -ATOM 1173 CG2 ILE A 153 34.807 -0.314 17.401 1.00 25.60 C -ANISOU 1173 CG2 ILE A 153 3158 3270 3299 -10 -237 48 C -ATOM 1174 CD1 ILE A 153 33.479 2.351 17.812 1.00 21.26 C -ANISOU 1174 CD1 ILE A 153 2684 2697 2697 -123 -239 2 C -ATOM 1175 N ARG A 154 36.931 -0.310 20.497 1.00 22.89 N -ANISOU 1175 N ARG A 154 2838 2963 2896 -45 -400 148 N -ATOM 1176 CA ARG A 154 37.740 -1.393 21.032 1.00 27.23 C -ANISOU 1176 CA ARG A 154 3371 3524 3453 3 -432 188 C -ATOM 1177 C ARG A 154 36.821 -2.448 21.639 1.00 27.60 C -ANISOU 1177 C ARG A 154 3496 3509 3480 31 -403 180 C -ATOM 1178 O ARG A 154 35.747 -2.134 22.184 1.00 29.21 O -ANISOU 1178 O ARG A 154 3773 3678 3649 -1 -380 159 O -ATOM 1179 CB ARG A 154 38.743 -0.868 22.062 1.00 29.72 C -ANISOU 1179 CB ARG A 154 3678 3869 3744 -34 -520 230 C -ATOM 1180 CG ARG A 154 39.601 0.306 21.569 1.00 34.56 C -ANISOU 1180 CG ARG A 154 4214 4537 4379 -86 -563 251 C -ATOM 1181 CD ARG A 154 40.598 0.719 22.637 1.00 40.92 C -ANISOU 1181 CD ARG A 154 5016 5366 5166 -128 -668 297 C -ATOM 1182 NE ARG A 154 41.148 -0.475 23.271 1.00 45.94 N -ANISOU 1182 NE ARG A 154 5643 6009 5801 -70 -690 333 N -ATOM 1183 CZ ARG A 154 41.286 -0.643 24.583 1.00 48.10 C -ANISOU 1183 CZ ARG A 154 5986 6260 6029 -81 -754 350 C -ATOM 1184 NH1 ARG A 154 40.943 0.327 25.424 1.00 47.10 N -ANISOU 1184 NH1 ARG A 154 5946 6103 5846 -145 -804 329 N -ATOM 1185 NH2 ARG A 154 41.785 -1.782 25.049 1.00 49.20 N -ANISOU 1185 NH2 ARG A 154 6114 6407 6173 -23 -771 386 N -ATOM 1186 N GLN A 155 37.220 -3.705 21.509 1.00 25.28 N -ANISOU 1186 N GLN A 155 3187 3205 3212 94 -404 201 N -ATOM 1187 CA GLN A 155 36.371 -4.804 21.948 1.00 26.46 C -ANISOU 1187 CA GLN A 155 3408 3288 3355 116 -382 203 C -ATOM 1188 C GLN A 155 36.249 -4.820 23.474 1.00 27.14 C -ANISOU 1188 C GLN A 155 3562 3361 3388 88 -417 235 C -ATOM 1189 O GLN A 155 37.253 -4.723 24.179 1.00 19.50 O -ANISOU 1189 O GLN A 155 2580 2425 2403 92 -479 268 O -ATOM 1190 CB GLN A 155 36.929 -6.143 21.451 1.00 23.37 C -ANISOU 1190 CB GLN A 155 2998 2879 3003 196 -388 217 C -ATOM 1191 CG GLN A 155 36.119 -7.365 21.877 1.00 22.91 C -ANISOU 1191 CG GLN A 155 3017 2740 2947 212 -380 229 C -ATOM 1192 CD GLN A 155 36.701 -8.665 21.353 1.00 22.14 C -ANISOU 1192 CD GLN A 155 2916 2609 2886 300 -397 237 C -ATOM 1193 OE1 GLN A 155 37.851 -8.709 20.939 1.00 23.67 O -ANISOU 1193 OE1 GLN A 155 3046 2854 3093 360 -416 245 O -ATOM 1194 NE2 GLN A 155 35.900 -9.737 21.368 1.00 21.47 N -ANISOU 1194 NE2 GLN A 155 2902 2439 2817 310 -393 239 N -ATOM 1195 N GLY A 156 35.029 -4.953 23.981 1.00 26.62 N -ANISOU 1195 N GLY A 156 3567 3255 3294 63 -379 230 N -ATOM 1196 CA GLY A 156 34.817 -5.054 25.421 1.00 27.92 C -ANISOU 1196 CA GLY A 156 3802 3410 3396 47 -400 265 C -ATOM 1197 C GLY A 156 35.402 -6.347 25.959 1.00 32.05 C -ANISOU 1197 C GLY A 156 4340 3909 3928 89 -439 315 C -ATOM 1198 O GLY A 156 35.570 -7.311 25.217 1.00 32.72 O -ANISOU 1198 O GLY A 156 4400 3964 4068 132 -433 318 O -ATOM 1199 N PRO A 157 35.735 -6.377 27.256 1.00 34.20 N -ANISOU 1199 N PRO A 157 4663 4191 4142 84 -483 354 N -ATOM 1200 CA PRO A 157 36.314 -7.595 27.824 1.00 33.93 C -ANISOU 1200 CA PRO A 157 4647 4131 4114 126 -526 408 C -ATOM 1201 C PRO A 157 35.338 -8.752 27.737 1.00 34.40 C -ANISOU 1201 C PRO A 157 4750 4125 4197 134 -482 431 C -ATOM 1202 O PRO A 157 35.755 -9.906 27.692 1.00 35.64 O -ANISOU 1202 O PRO A 157 4913 4241 4388 178 -512 462 O -ATOM 1203 CB PRO A 157 36.592 -7.212 29.286 1.00 36.38 C -ANISOU 1203 CB PRO A 157 5018 4464 4339 107 -575 441 C -ATOM 1204 CG PRO A 157 35.656 -6.088 29.568 1.00 36.96 C -ANISOU 1204 CG PRO A 157 5135 4554 4356 62 -532 406 C -ATOM 1205 CD PRO A 157 35.546 -5.323 28.269 1.00 35.07 C -ANISOU 1205 CD PRO A 157 4827 4328 4170 46 -499 349 C -ATOM 1206 N LYS A 158 34.050 -8.435 27.702 1.00 36.91 N -ANISOU 1206 N LYS A 158 5095 4429 4498 92 -418 419 N -ATOM 1207 CA LYS A 158 33.010 -9.452 27.636 1.00 41.47 C -ANISOU 1207 CA LYS A 158 5707 4947 5103 80 -382 452 C -ATOM 1208 C LYS A 158 32.200 -9.372 26.345 1.00 38.06 C -ANISOU 1208 C LYS A 158 5238 4491 4731 64 -334 408 C -ATOM 1209 O LYS A 158 31.169 -10.046 26.197 1.00 36.81 O -ANISOU 1209 O LYS A 158 5101 4284 4600 37 -305 434 O -ATOM 1210 CB LYS A 158 32.073 -9.323 28.838 1.00 47.25 C -ANISOU 1210 CB LYS A 158 6498 5691 5762 43 -346 502 C -ATOM 1211 CG LYS A 158 32.733 -9.629 30.175 1.00 51.80 C -ANISOU 1211 CG LYS A 158 7129 6281 6273 61 -395 556 C -ATOM 1212 CD LYS A 158 31.710 -9.585 31.299 1.00 55.24 C -ANISOU 1212 CD LYS A 158 7626 6734 6630 33 -347 611 C -ATOM 1213 CE LYS A 158 30.719 -10.734 31.188 1.00 56.30 C -ANISOU 1213 CE LYS A 158 7770 6814 6809 7 -310 676 C -ATOM 1214 NZ LYS A 158 31.364 -12.058 31.443 1.00 56.73 N -ANISOU 1214 NZ LYS A 158 7853 6806 6896 30 -373 732 N -ATOM 1215 N GLU A 159 32.660 -8.546 25.412 1.00 32.84 N -ANISOU 1215 N GLU A 159 4522 3865 4091 75 -331 347 N -ATOM 1216 CA GLU A 159 31.928 -8.358 24.168 1.00 28.64 C -ANISOU 1216 CA GLU A 159 3959 3316 3607 62 -289 301 C -ATOM 1217 C GLU A 159 32.282 -9.461 23.176 1.00 31.37 C -ANISOU 1217 C GLU A 159 4296 3605 4017 109 -314 289 C -ATOM 1218 O GLU A 159 33.454 -9.715 22.929 1.00 32.38 O -ANISOU 1218 O GLU A 159 4400 3746 4156 167 -352 282 O -ATOM 1219 CB GLU A 159 32.225 -6.973 23.575 1.00 23.06 C -ANISOU 1219 CB GLU A 159 3203 2670 2891 52 -275 246 C -ATOM 1220 CG GLU A 159 31.419 -6.658 22.328 1.00 25.45 C -ANISOU 1220 CG GLU A 159 3476 2961 3234 38 -231 200 C -ATOM 1221 CD GLU A 159 31.836 -5.351 21.704 1.00 26.78 C -ANISOU 1221 CD GLU A 159 3596 3183 3394 31 -224 154 C -ATOM 1222 OE1 GLU A 159 32.946 -4.864 22.016 1.00 29.83 O -ANISOU 1222 OE1 GLU A 159 3961 3612 3762 42 -263 159 O -ATOM 1223 OE2 GLU A 159 31.068 -4.807 20.893 1.00 26.76 O -ANISOU 1223 OE2 GLU A 159 3578 3182 3409 11 -186 119 O -ATOM 1224 N PRO A 160 31.267 -10.128 22.612 1.00 31.99 N -ANISOU 1224 N PRO A 160 4398 3621 4137 88 -297 289 N -ATOM 1225 CA PRO A 160 31.503 -11.141 21.573 1.00 31.59 C -ANISOU 1225 CA PRO A 160 4360 3502 4141 138 -328 265 C -ATOM 1226 C PRO A 160 32.227 -10.549 20.370 1.00 26.11 C -ANISOU 1226 C PRO A 160 3611 2851 3458 188 -319 200 C -ATOM 1227 O PRO A 160 31.961 -9.416 20.008 1.00 26.28 O -ANISOU 1227 O PRO A 160 3590 2928 3467 156 -282 169 O -ATOM 1228 CB PRO A 160 30.093 -11.599 21.189 1.00 30.77 C -ANISOU 1228 CB PRO A 160 4285 3333 4073 81 -313 274 C -ATOM 1229 CG PRO A 160 29.233 -11.232 22.376 1.00 30.73 C -ANISOU 1229 CG PRO A 160 4287 3357 4032 11 -278 333 C -ATOM 1230 CD PRO A 160 29.834 -9.966 22.920 1.00 30.82 C -ANISOU 1230 CD PRO A 160 4265 3461 3983 20 -253 314 C -ATOM 1231 N PHE A 161 33.125 -11.301 19.746 1.00 27.09 N -ANISOU 1231 N PHE A 161 3737 2952 3603 272 -352 183 N -ATOM 1232 CA PHE A 161 33.922 -10.711 18.669 1.00 25.55 C -ANISOU 1232 CA PHE A 161 3480 2819 3409 329 -336 134 C -ATOM 1233 C PHE A 161 33.044 -10.147 17.526 1.00 22.43 C -ANISOU 1233 C PHE A 161 3074 2422 3028 298 -298 82 C -ATOM 1234 O PHE A 161 33.323 -9.082 16.977 1.00 22.24 O -ANISOU 1234 O PHE A 161 2989 2471 2992 293 -267 56 O -ATOM 1235 CB PHE A 161 34.922 -11.741 18.150 1.00 26.08 C -ANISOU 1235 CB PHE A 161 3557 2860 3490 442 -370 127 C -ATOM 1236 CG PHE A 161 35.923 -11.177 17.189 1.00 22.70 C -ANISOU 1236 CG PHE A 161 3051 2517 3055 512 -347 96 C -ATOM 1237 CD1 PHE A 161 36.918 -10.307 17.632 1.00 22.81 C -ANISOU 1237 CD1 PHE A 161 2982 2635 3052 509 -344 126 C -ATOM 1238 CD2 PHE A 161 35.866 -11.500 15.847 1.00 20.18 C -ANISOU 1238 CD2 PHE A 161 2745 2179 2746 579 -332 44 C -ATOM 1239 CE1 PHE A 161 37.825 -9.774 16.753 1.00 24.46 C -ANISOU 1239 CE1 PHE A 161 3106 2930 3257 565 -321 115 C -ATOM 1240 CE2 PHE A 161 36.788 -10.996 14.964 1.00 22.95 C -ANISOU 1240 CE2 PHE A 161 3019 2619 3083 650 -302 27 C -ATOM 1241 CZ PHE A 161 37.755 -10.114 15.400 1.00 24.57 C -ANISOU 1241 CZ PHE A 161 3126 2933 3276 638 -293 67 C -ATOM 1242 N ARG A 162 31.966 -10.840 17.194 1.00 23.54 N -ANISOU 1242 N ARG A 162 3272 2476 3195 270 -306 73 N -ATOM 1243 CA ARG A 162 31.112 -10.423 16.098 1.00 26.67 C -ANISOU 1243 CA ARG A 162 3663 2864 3608 244 -282 26 C -ATOM 1244 C ARG A 162 30.482 -9.067 16.382 1.00 22.89 C -ANISOU 1244 C ARG A 162 3136 2451 3110 167 -234 28 C -ATOM 1245 O ARG A 162 30.410 -8.210 15.491 1.00 24.82 O -ANISOU 1245 O ARG A 162 3341 2739 3350 166 -206 -12 O -ATOM 1246 CB ARG A 162 30.014 -11.462 15.830 1.00 33.93 C -ANISOU 1246 CB ARG A 162 4654 3673 4565 213 -316 29 C -ATOM 1247 CG ARG A 162 29.125 -11.121 14.617 1.00 40.63 C -ANISOU 1247 CG ARG A 162 5501 4506 5432 188 -305 -20 C -ATOM 1248 CD ARG A 162 27.798 -11.904 14.654 1.00 42.20 C -ANISOU 1248 CD ARG A 162 5752 4607 5674 115 -342 6 C -ATOM 1249 NE ARG A 162 28.030 -13.326 14.877 1.00 46.19 N -ANISOU 1249 NE ARG A 162 6338 5009 6202 147 -410 27 N -ATOM 1250 CZ ARG A 162 27.081 -14.214 15.167 1.00 46.46 C -ANISOU 1250 CZ ARG A 162 6426 4948 6280 79 -458 72 C -ATOM 1251 NH1 ARG A 162 25.814 -13.828 15.282 1.00 42.86 N -ANISOU 1251 NH1 ARG A 162 5937 4500 5849 -22 -440 106 N -ATOM 1252 NH2 ARG A 162 27.412 -15.490 15.352 1.00 46.78 N -ANISOU 1252 NH2 ARG A 162 6549 4886 6340 114 -527 90 N -ATOM 1253 N ASP A 163 30.076 -8.856 17.631 1.00 19.41 N -ANISOU 1253 N ASP A 163 2702 2021 2652 111 -226 77 N -ATOM 1254 CA ASP A 163 29.483 -7.585 18.021 1.00 23.22 C -ANISOU 1254 CA ASP A 163 3153 2562 3107 52 -182 77 C -ATOM 1255 C ASP A 163 30.520 -6.466 17.913 1.00 20.32 C -ANISOU 1255 C ASP A 163 2736 2273 2710 73 -175 55 C -ATOM 1256 O ASP A 163 30.192 -5.349 17.525 1.00 16.67 O -ANISOU 1256 O ASP A 163 2246 1850 2237 45 -147 28 O -ATOM 1257 CB ASP A 163 28.919 -7.663 19.443 1.00 28.20 C -ANISOU 1257 CB ASP A 163 3812 3192 3711 6 -173 136 C -ATOM 1258 CG ASP A 163 27.691 -8.555 19.536 1.00 33.14 C -ANISOU 1258 CG ASP A 163 4468 3753 4370 -37 -172 174 C -ATOM 1259 OD1 ASP A 163 26.958 -8.692 18.531 1.00 32.73 O -ANISOU 1259 OD1 ASP A 163 4409 3668 4359 -54 -171 148 O -ATOM 1260 OD2 ASP A 163 27.451 -9.118 20.625 1.00 35.41 O -ANISOU 1260 OD2 ASP A 163 4786 4024 4643 -59 -177 236 O -ATOM 1261 N TYR A 164 31.779 -6.780 18.209 1.00 22.27 N -ANISOU 1261 N TYR A 164 2971 2542 2949 121 -207 70 N -ATOM 1262 CA TYR A 164 32.850 -5.787 18.087 1.00 21.49 C -ANISOU 1262 CA TYR A 164 2814 2519 2831 133 -212 63 C -ATOM 1263 C TYR A 164 33.114 -5.426 16.612 1.00 19.30 C -ANISOU 1263 C TYR A 164 2490 2270 2573 165 -191 22 C -ATOM 1264 O TYR A 164 33.269 -4.255 16.260 1.00 19.91 O -ANISOU 1264 O TYR A 164 2524 2400 2639 136 -176 10 O -ATOM 1265 CB TYR A 164 34.106 -6.311 18.771 1.00 20.53 C -ANISOU 1265 CB TYR A 164 2680 2418 2702 177 -255 101 C -ATOM 1266 CG TYR A 164 35.403 -5.722 18.285 1.00 20.71 C -ANISOU 1266 CG TYR A 164 2625 2518 2726 210 -268 104 C -ATOM 1267 CD1 TYR A 164 35.681 -4.368 18.445 1.00 20.16 C -ANISOU 1267 CD1 TYR A 164 2515 2506 2638 156 -272 107 C -ATOM 1268 CD2 TYR A 164 36.376 -6.527 17.702 1.00 24.43 C -ANISOU 1268 CD2 TYR A 164 3062 3004 3217 297 -280 112 C -ATOM 1269 CE1 TYR A 164 36.877 -3.829 18.015 1.00 22.42 C -ANISOU 1269 CE1 TYR A 164 2720 2867 2933 173 -289 126 C -ATOM 1270 CE2 TYR A 164 37.583 -5.988 17.267 1.00 25.09 C -ANISOU 1270 CE2 TYR A 164 3056 3175 3303 328 -286 130 C -ATOM 1271 CZ TYR A 164 37.821 -4.644 17.419 1.00 25.19 C -ANISOU 1271 CZ TYR A 164 3020 3247 3304 258 -291 142 C -ATOM 1272 OH TYR A 164 39.006 -4.093 16.988 1.00 24.22 O -ANISOU 1272 OH TYR A 164 2799 3213 3191 274 -302 176 O -ATOM 1273 N VAL A 165 33.133 -6.436 15.754 1.00 20.57 N -ANISOU 1273 N VAL A 165 2668 2391 2758 225 -194 2 N -ATOM 1274 CA VAL A 165 33.371 -6.225 14.320 1.00 19.44 C -ANISOU 1274 CA VAL A 165 2491 2274 2620 271 -172 -37 C -ATOM 1275 C VAL A 165 32.214 -5.420 13.692 1.00 21.65 C -ANISOU 1275 C VAL A 165 2777 2547 2904 212 -141 -70 C -ATOM 1276 O VAL A 165 32.457 -4.519 12.884 1.00 20.80 O -ANISOU 1276 O VAL A 165 2623 2493 2787 212 -118 -87 O -ATOM 1277 CB VAL A 165 33.550 -7.555 13.589 1.00 17.53 C -ANISOU 1277 CB VAL A 165 2292 1978 2392 359 -189 -59 C -ATOM 1278 CG1 VAL A 165 33.926 -7.316 12.097 1.00 17.59 C -ANISOU 1278 CG1 VAL A 165 2268 2026 2388 424 -161 -99 C -ATOM 1279 CG2 VAL A 165 34.618 -8.410 14.294 1.00 18.82 C -ANISOU 1279 CG2 VAL A 165 2455 2141 2554 425 -222 -23 C -ATOM 1280 N ASP A 166 30.964 -5.723 14.073 1.00 21.02 N -ANISOU 1280 N ASP A 166 2746 2403 2836 161 -142 -71 N -ATOM 1281 CA ASP A 166 29.834 -4.899 13.647 1.00 22.30 C -ANISOU 1281 CA ASP A 166 2905 2567 3003 104 -114 -93 C -ATOM 1282 C ASP A 166 30.065 -3.406 13.968 1.00 19.71 C -ANISOU 1282 C ASP A 166 2534 2306 2647 65 -93 -88 C -ATOM 1283 O ASP A 166 29.928 -2.566 13.083 1.00 21.04 O -ANISOU 1283 O ASP A 166 2676 2504 2814 58 -73 -114 O -ATOM 1284 CB ASP A 166 28.526 -5.347 14.307 1.00 25.41 C -ANISOU 1284 CB ASP A 166 3338 2903 3413 49 -115 -72 C -ATOM 1285 CG ASP A 166 27.898 -6.563 13.644 1.00 29.25 C -ANISOU 1285 CG ASP A 166 3869 3309 3936 60 -144 -83 C -ATOM 1286 OD1 ASP A 166 28.235 -6.880 12.469 1.00 31.25 O -ANISOU 1286 OD1 ASP A 166 4131 3547 4194 113 -158 -125 O -ATOM 1287 OD2 ASP A 166 27.033 -7.188 14.308 1.00 27.69 O -ANISOU 1287 OD2 ASP A 166 3701 3062 3759 15 -155 -46 O -ATOM 1288 N ARG A 167 30.395 -3.077 15.224 1.00 17.63 N -ANISOU 1288 N ARG A 167 2275 2062 2362 41 -103 -56 N -ATOM 1289 CA ARG A 167 30.646 -1.666 15.600 1.00 21.45 C -ANISOU 1289 CA ARG A 167 2737 2595 2817 3 -100 -54 C -ATOM 1290 C ARG A 167 31.814 -1.059 14.799 1.00 21.74 C -ANISOU 1290 C ARG A 167 2715 2688 2856 22 -109 -57 C -ATOM 1291 O ARG A 167 31.769 0.103 14.382 1.00 19.49 O -ANISOU 1291 O ARG A 167 2409 2431 2563 -9 -102 -67 O -ATOM 1292 CB ARG A 167 30.940 -1.523 17.109 1.00 22.49 C -ANISOU 1292 CB ARG A 167 2898 2733 2915 -18 -123 -21 C -ATOM 1293 CG ARG A 167 29.802 -1.987 18.021 1.00 24.20 C -ANISOU 1293 CG ARG A 167 3166 2911 3117 -37 -104 -5 C -ATOM 1294 CD ARG A 167 29.999 -1.545 19.472 1.00 23.91 C -ANISOU 1294 CD ARG A 167 3167 2890 3026 -54 -120 21 C -ATOM 1295 NE ARG A 167 31.152 -2.193 20.094 1.00 23.91 N -ANISOU 1295 NE ARG A 167 3168 2897 3020 -31 -166 52 N -ATOM 1296 CZ ARG A 167 32.226 -1.537 20.529 1.00 26.83 C -ANISOU 1296 CZ ARG A 167 3525 3302 3366 -37 -211 60 C -ATOM 1297 NH1 ARG A 167 32.278 -0.212 20.420 1.00 25.43 N -ANISOU 1297 NH1 ARG A 167 3344 3148 3169 -69 -219 38 N -ATOM 1298 NH2 ARG A 167 33.250 -2.200 21.075 1.00 24.46 N -ANISOU 1298 NH2 ARG A 167 3217 3011 3066 -13 -256 95 N -ATOM 1299 N PHE A 168 32.861 -1.854 14.608 1.00 22.46 N -ANISOU 1299 N PHE A 168 2778 2798 2957 76 -126 -39 N -ATOM 1300 CA PHE A 168 34.078 -1.387 13.953 1.00 22.65 C -ANISOU 1300 CA PHE A 168 2731 2893 2984 99 -132 -22 C -ATOM 1301 C PHE A 168 33.790 -0.983 12.505 1.00 21.13 C -ANISOU 1301 C PHE A 168 2514 2719 2797 114 -96 -51 C -ATOM 1302 O PHE A 168 34.130 0.136 12.089 1.00 22.62 O -ANISOU 1302 O PHE A 168 2658 2956 2981 80 -92 -40 O -ATOM 1303 CB PHE A 168 35.148 -2.474 14.020 1.00 22.80 C -ANISOU 1303 CB PHE A 168 2724 2930 3011 174 -149 4 C -ATOM 1304 CG PHE A 168 36.490 -2.064 13.451 1.00 27.59 C -ANISOU 1304 CG PHE A 168 3237 3627 3620 205 -151 40 C -ATOM 1305 CD1 PHE A 168 36.741 -2.162 12.085 1.00 22.79 C -ANISOU 1305 CD1 PHE A 168 2590 3058 3012 264 -112 26 C -ATOM 1306 CD2 PHE A 168 37.511 -1.618 14.291 1.00 26.22 C -ANISOU 1306 CD2 PHE A 168 3013 3503 3445 177 -194 93 C -ATOM 1307 CE1 PHE A 168 37.977 -1.813 11.567 1.00 25.10 C -ANISOU 1307 CE1 PHE A 168 2785 3448 3305 297 -104 73 C -ATOM 1308 CE2 PHE A 168 38.756 -1.262 13.776 1.00 28.46 C -ANISOU 1308 CE2 PHE A 168 3194 3880 3738 199 -197 141 C -ATOM 1309 CZ PHE A 168 38.986 -1.356 12.420 1.00 28.57 C -ANISOU 1309 CZ PHE A 168 3159 3942 3753 260 -147 135 C -ATOM 1310 N TYR A 169 33.165 -1.876 11.736 1.00 18.67 N -ANISOU 1310 N TYR A 169 2236 2364 2493 160 -77 -86 N -ATOM 1311 CA TYR A 169 32.928 -1.571 10.325 1.00 20.33 C -ANISOU 1311 CA TYR A 169 2431 2592 2699 183 -48 -116 C -ATOM 1312 C TYR A 169 31.767 -0.583 10.148 1.00 21.39 C -ANISOU 1312 C TYR A 169 2586 2705 2835 114 -35 -139 C -ATOM 1313 O TYR A 169 31.734 0.125 9.156 1.00 19.39 O -ANISOU 1313 O TYR A 169 2309 2485 2574 112 -15 -149 O -ATOM 1314 CB TYR A 169 32.709 -2.862 9.504 1.00 19.81 C -ANISOU 1314 CB TYR A 169 2409 2482 2636 262 -45 -151 C -ATOM 1315 CG TYR A 169 34.046 -3.534 9.217 1.00 23.18 C -ANISOU 1315 CG TYR A 169 2799 2957 3051 357 -43 -132 C -ATOM 1316 CD1 TYR A 169 34.506 -4.578 9.997 1.00 22.18 C -ANISOU 1316 CD1 TYR A 169 2695 2799 2932 400 -71 -116 C -ATOM 1317 CD2 TYR A 169 34.863 -3.073 8.192 1.00 25.26 C -ANISOU 1317 CD2 TYR A 169 2999 3306 3292 407 -11 -121 C -ATOM 1318 CE1 TYR A 169 35.741 -5.164 9.750 1.00 24.91 C -ANISOU 1318 CE1 TYR A 169 3002 3197 3267 498 -68 -95 C -ATOM 1319 CE2 TYR A 169 36.085 -3.635 7.938 1.00 27.31 C -ANISOU 1319 CE2 TYR A 169 3212 3626 3538 503 -1 -95 C -ATOM 1320 CZ TYR A 169 36.527 -4.677 8.725 1.00 27.18 C -ANISOU 1320 CZ TYR A 169 3218 3577 3532 552 -30 -84 C -ATOM 1321 OH TYR A 169 37.750 -5.231 8.467 1.00 29.93 O -ANISOU 1321 OH TYR A 169 3515 3991 3866 660 -18 -56 O -ATOM 1322 N LYS A 170 30.837 -0.511 11.105 1.00 23.30 N -ANISOU 1322 N LYS A 170 2870 2900 3082 63 -43 -141 N -ATOM 1323 CA LYS A 170 29.773 0.508 11.026 1.00 25.04 C -ANISOU 1323 CA LYS A 170 3104 3109 3300 9 -28 -157 C -ATOM 1324 C LYS A 170 30.381 1.899 11.241 1.00 21.38 C -ANISOU 1324 C LYS A 170 2610 2692 2820 -29 -36 -139 C -ATOM 1325 O LYS A 170 30.027 2.853 10.562 1.00 18.96 O -ANISOU 1325 O LYS A 170 2296 2396 2511 -52 -25 -151 O -ATOM 1326 CB LYS A 170 28.663 0.240 12.051 1.00 32.95 C -ANISOU 1326 CB LYS A 170 4151 4063 4306 -23 -26 -155 C -ATOM 1327 CG LYS A 170 27.506 1.248 11.997 1.00 41.99 C -ANISOU 1327 CG LYS A 170 5305 5202 5446 -63 -6 -170 C -ATOM 1328 CD LYS A 170 26.190 0.632 12.488 1.00 48.06 C -ANISOU 1328 CD LYS A 170 6101 5931 6230 -78 8 -164 C -ATOM 1329 CE LYS A 170 25.028 1.638 12.476 1.00 52.61 C -ANISOU 1329 CE LYS A 170 6677 6512 6801 -104 33 -173 C -ATOM 1330 NZ LYS A 170 24.629 2.086 11.102 1.00 52.22 N -ANISOU 1330 NZ LYS A 170 6609 6465 6769 -101 36 -202 N -ATOM 1331 N THR A 171 31.312 1.994 12.194 1.00 21.43 N -ANISOU 1331 N THR A 171 2605 2720 2817 -40 -64 -107 N -ATOM 1332 CA THR A 171 32.045 3.231 12.440 1.00 23.62 C -ANISOU 1332 CA THR A 171 2858 3034 3083 -84 -91 -82 C -ATOM 1333 C THR A 171 32.886 3.608 11.232 1.00 24.01 C -ANISOU 1333 C THR A 171 2839 3142 3142 -73 -83 -62 C -ATOM 1334 O THR A 171 32.919 4.774 10.809 1.00 26.72 O -ANISOU 1334 O THR A 171 3169 3501 3483 -115 -90 -53 O -ATOM 1335 CB THR A 171 32.964 3.120 13.671 1.00 24.88 C -ANISOU 1335 CB THR A 171 3015 3206 3232 -97 -136 -46 C -ATOM 1336 OG1 THR A 171 32.174 2.836 14.834 1.00 27.79 O -ANISOU 1336 OG1 THR A 171 3452 3527 3580 -106 -139 -59 O -ATOM 1337 CG2 THR A 171 33.745 4.424 13.872 1.00 23.97 C -ANISOU 1337 CG2 THR A 171 2877 3120 3110 -155 -182 -17 C -ATOM 1338 N LEU A 172 33.576 2.623 10.675 1.00 19.51 N -ANISOU 1338 N LEU A 172 2230 2605 2580 -10 -67 -51 N -ATOM 1339 CA LEU A 172 34.372 2.854 9.478 1.00 20.65 C -ANISOU 1339 CA LEU A 172 2305 2819 2724 20 -46 -26 C -ATOM 1340 C LEU A 172 33.529 3.418 8.326 1.00 21.36 C -ANISOU 1340 C LEU A 172 2411 2900 2806 14 -15 -58 C -ATOM 1341 O LEU A 172 33.940 4.340 7.605 1.00 22.78 O -ANISOU 1341 O LEU A 172 2546 3129 2982 -10 -8 -28 O -ATOM 1342 CB LEU A 172 35.046 1.548 9.043 1.00 26.04 C -ANISOU 1342 CB LEU A 172 2961 3530 3404 115 -26 -23 C -ATOM 1343 CG LEU A 172 36.391 1.713 8.343 1.00 31.22 C -ANISOU 1343 CG LEU A 172 3520 4288 4055 154 -10 34 C -ATOM 1344 CD1 LEU A 172 37.404 2.347 9.306 1.00 31.92 C -ANISOU 1344 CD1 LEU A 172 3548 4422 4160 95 -57 100 C -ATOM 1345 CD2 LEU A 172 36.905 0.363 7.817 1.00 33.31 C -ANISOU 1345 CD2 LEU A 172 3776 4575 4307 275 17 24 C -ATOM 1346 N ARG A 173 32.339 2.862 8.156 1.00 18.95 N -ANISOU 1346 N ARG A 173 2166 2531 2501 31 -1 -110 N -ATOM 1347 CA ARG A 173 31.457 3.276 7.070 1.00 16.86 C -ANISOU 1347 CA ARG A 173 1921 2254 2230 29 21 -141 C -ATOM 1348 C ARG A 173 31.026 4.739 7.203 1.00 20.21 C -ANISOU 1348 C ARG A 173 2351 2673 2655 -43 10 -133 C -ATOM 1349 O ARG A 173 30.927 5.442 6.213 1.00 20.55 O -ANISOU 1349 O ARG A 173 2379 2739 2690 -49 23 -131 O -ATOM 1350 CB ARG A 173 30.229 2.367 7.017 1.00 17.68 C -ANISOU 1350 CB ARG A 173 2086 2288 2344 49 24 -190 C -ATOM 1351 CG ARG A 173 29.311 2.640 5.798 1.00 24.11 C -ANISOU 1351 CG ARG A 173 2920 3088 3152 54 37 -224 C -ATOM 1352 CD ARG A 173 27.985 1.902 5.911 1.00 22.43 C -ANISOU 1352 CD ARG A 173 2760 2804 2960 49 26 -260 C -ATOM 1353 NE ARG A 173 27.203 2.029 4.680 1.00 26.86 N -ANISOU 1353 NE ARG A 173 3338 3353 3515 60 27 -291 N -ATOM 1354 CZ ARG A 173 26.054 1.397 4.458 1.00 25.15 C -ANISOU 1354 CZ ARG A 173 3159 3078 3317 54 8 -319 C -ATOM 1355 NH1 ARG A 173 25.556 0.603 5.387 1.00 24.98 N -ANISOU 1355 NH1 ARG A 173 3158 3009 3324 35 -8 -313 N -ATOM 1356 NH2 ARG A 173 25.410 1.556 3.312 1.00 22.27 N -ANISOU 1356 NH2 ARG A 173 2810 2706 2945 63 0 -345 N -ATOM 1357 N ALA A 174 30.748 5.190 8.420 1.00 22.67 N -ANISOU 1357 N ALA A 174 2692 2950 2970 -89 -15 -131 N -ATOM 1358 CA ALA A 174 30.336 6.573 8.615 1.00 25.52 C -ANISOU 1358 CA ALA A 174 3075 3294 3326 -146 -33 -130 C -ATOM 1359 C ALA A 174 31.514 7.530 8.455 1.00 29.47 C -ANISOU 1359 C ALA A 174 3530 3841 3826 -187 -62 -79 C -ATOM 1360 O ALA A 174 31.409 8.541 7.740 1.00 25.11 O -ANISOU 1360 O ALA A 174 2973 3295 3273 -217 -65 -68 O -ATOM 1361 CB ALA A 174 29.701 6.745 9.960 1.00 25.23 C -ANISOU 1361 CB ALA A 174 3095 3210 3281 -168 -50 -146 C -ATOM 1362 N GLU A 175 32.627 7.209 9.128 1.00 31.51 N -ANISOU 1362 N GLU A 175 3752 4131 4089 -193 -88 -40 N -ATOM 1363 CA GLU A 175 33.830 8.042 9.094 1.00 33.36 C -ANISOU 1363 CA GLU A 175 3930 4414 4332 -243 -127 24 C -ATOM 1364 C GLU A 175 34.313 8.222 7.670 1.00 34.22 C -ANISOU 1364 C GLU A 175 3969 4590 4443 -227 -93 60 C -ATOM 1365 O GLU A 175 34.963 9.217 7.354 1.00 37.00 O -ANISOU 1365 O GLU A 175 4280 4975 4803 -284 -119 116 O -ATOM 1366 CB GLU A 175 34.962 7.433 9.942 1.00 34.48 C -ANISOU 1366 CB GLU A 175 4029 4591 4481 -239 -159 65 C -ATOM 1367 CG GLU A 175 34.743 7.468 11.458 1.00 36.04 C -ANISOU 1367 CG GLU A 175 4294 4732 4667 -267 -208 46 C -ATOM 1368 CD GLU A 175 34.933 8.855 12.065 1.00 40.75 C -ANISOU 1368 CD GLU A 175 4927 5297 5258 -351 -280 64 C -ATOM 1369 OE1 GLU A 175 36.098 9.244 12.315 1.00 41.33 O -ANISOU 1369 OE1 GLU A 175 4948 5408 5347 -399 -338 126 O -ATOM 1370 OE2 GLU A 175 33.916 9.551 12.305 1.00 40.47 O -ANISOU 1370 OE2 GLU A 175 4975 5198 5204 -366 -283 19 O -ATOM 1371 N GLN A 176 34.006 7.257 6.811 1.00 33.25 N -ANISOU 1371 N GLN A 176 3839 4486 4310 -150 -37 31 N -ATOM 1372 CA GLN A 176 34.408 7.325 5.411 1.00 37.44 C -ANISOU 1372 CA GLN A 176 4314 5085 4827 -115 4 59 C -ATOM 1373 C GLN A 176 33.228 7.551 4.458 1.00 37.20 C -ANISOU 1373 C GLN A 176 4335 5018 4780 -101 32 9 C -ATOM 1374 O GLN A 176 33.397 7.442 3.238 1.00 35.35 O -ANISOU 1374 O GLN A 176 4073 4835 4523 -56 70 20 O -ATOM 1375 CB GLN A 176 35.141 6.046 5.001 1.00 41.29 C -ANISOU 1375 CB GLN A 176 4755 5632 5301 -20 43 66 C -ATOM 1376 CG GLN A 176 36.574 5.935 5.517 1.00 45.54 C -ANISOU 1376 CG GLN A 176 5204 6245 5853 -23 26 141 C -ATOM 1377 CD GLN A 176 37.177 4.559 5.270 1.00 48.14 C -ANISOU 1377 CD GLN A 176 5504 6620 6168 90 63 137 C -ATOM 1378 OE1 GLN A 176 36.533 3.679 4.692 1.00 46.83 O -ANISOU 1378 OE1 GLN A 176 5393 6420 5979 168 96 75 O -ATOM 1379 NE2 GLN A 176 38.419 4.368 5.708 1.00 49.26 N -ANISOU 1379 NE2 GLN A 176 5559 6833 6322 101 51 205 N -ATOM 1380 N ALA A 177 32.058 7.862 5.021 1.00 37.55 N -ANISOU 1380 N ALA A 177 4453 4982 4833 -132 12 -41 N -ATOM 1381 CA ALA A 177 30.796 8.044 4.271 1.00 38.50 C -ANISOU 1381 CA ALA A 177 4623 5062 4946 -120 29 -89 C -ATOM 1382 C ALA A 177 30.566 6.981 3.190 1.00 41.16 C -ANISOU 1382 C ALA A 177 4960 5416 5262 -42 66 -119 C -ATOM 1383 O ALA A 177 30.257 7.312 2.039 1.00 42.44 O -ANISOU 1383 O ALA A 177 5125 5596 5404 -27 84 -124 O -ATOM 1384 CB ALA A 177 30.740 9.441 3.646 1.00 37.67 C -ANISOU 1384 CB ALA A 177 4513 4964 4836 -171 17 -58 C -ATOM 1385 N SER A 178 30.717 5.710 3.568 1.00 41.22 N -ANISOU 1385 N SER A 178 4976 5414 5273 9 72 -142 N -ATOM 1386 CA SER A 178 30.540 4.576 2.651 1.00 41.60 C -ANISOU 1386 CA SER A 178 5045 5462 5300 90 93 -178 C -ATOM 1387 C SER A 178 31.415 4.624 1.401 1.00 45.23 C -ANISOU 1387 C SER A 178 5463 6005 5719 147 127 -151 C -ATOM 1388 O SER A 178 31.029 4.087 0.360 1.00 46.20 O -ANISOU 1388 O SER A 178 5621 6124 5810 209 141 -188 O -ATOM 1389 CB SER A 178 29.079 4.461 2.215 1.00 38.76 C -ANISOU 1389 CB SER A 178 4746 5036 4944 83 82 -232 C -ATOM 1390 OG SER A 178 28.239 4.256 3.329 1.00 35.23 O -ANISOU 1390 OG SER A 178 4330 4525 4531 44 60 -251 O -ATOM 1391 N GLN A 179 32.588 5.245 1.505 1.00 48.14 N -ANISOU 1391 N GLN A 179 5756 6450 6085 128 139 -82 N -ATOM 1392 CA GLN A 179 33.588 5.203 0.437 1.00 53.75 C -ANISOU 1392 CA GLN A 179 6407 7261 6755 192 183 -37 C -ATOM 1393 C GLN A 179 34.801 4.390 0.899 1.00 57.60 C -ANISOU 1393 C GLN A 179 6837 7807 7243 250 196 -1 C -ATOM 1394 O GLN A 179 35.359 4.659 1.960 1.00 55.60 O -ANISOU 1394 O GLN A 179 6541 7558 7026 195 168 39 O -ATOM 1395 CB GLN A 179 34.031 6.616 0.033 1.00 57.44 C -ANISOU 1395 CB GLN A 179 6815 7787 7222 121 187 37 C -ATOM 1396 CG GLN A 179 32.945 7.685 0.103 1.00 59.56 C -ANISOU 1396 CG GLN A 179 7136 7984 7509 37 154 16 C -ATOM 1397 CD GLN A 179 31.961 7.610 -1.050 1.00 60.41 C -ANISOU 1397 CD GLN A 179 7300 8070 7583 77 171 -33 C -ATOM 1398 OE1 GLN A 179 30.791 7.271 -0.861 1.00 60.95 O -ANISOU 1398 OE1 GLN A 179 7438 8057 7664 76 149 -101 O -ATOM 1399 NE2 GLN A 179 32.427 7.941 -2.251 1.00 61.10 N -ANISOU 1399 NE2 GLN A 179 7355 8234 7626 109 208 8 N -ATOM 1400 N GLU A 180 35.214 3.405 0.108 1.00 64.60 N -ANISOU 1400 N GLU A 180 7725 8735 8085 368 235 -18 N -ATOM 1401 CA GLU A 180 36.346 2.559 0.485 1.00 68.99 C -ANISOU 1401 CA GLU A 180 8228 9348 8638 445 250 13 C -ATOM 1402 C GLU A 180 37.697 3.239 0.262 1.00 70.84 C -ANISOU 1402 C GLU A 180 8331 9717 8866 440 284 120 C -ATOM 1403 O GLU A 180 37.776 4.309 -0.343 1.00 71.22 O -ANISOU 1403 O GLU A 180 8336 9816 8906 384 299 172 O -ATOM 1404 CB GLU A 180 36.314 1.242 -0.293 1.00 72.48 C -ANISOU 1404 CB GLU A 180 8729 9781 9028 589 277 -47 C -ATOM 1405 CG GLU A 180 35.148 0.337 0.054 1.00 74.95 C -ANISOU 1405 CG GLU A 180 9162 9959 9357 593 231 -140 C -ATOM 1406 CD GLU A 180 35.371 -1.098 -0.395 1.00 77.67 C -ANISOU 1406 CD GLU A 180 9569 10281 9660 735 237 -191 C -ATOM 1407 OE1 GLU A 180 36.289 -1.338 -1.213 1.00 78.88 O -ANISOU 1407 OE1 GLU A 180 9685 10530 9757 848 288 -167 O -ATOM 1408 OE2 GLU A 180 34.633 -1.988 0.078 1.00 77.90 O -ANISOU 1408 OE2 GLU A 180 9688 10199 9712 736 189 -251 O -ATOM 1409 N VAL A 181 38.756 2.607 0.761 1.00 72.54 N -ANISOU 1409 N VAL A 181 8481 9991 9090 497 291 162 N -ATOM 1410 CA VAL A 181 40.122 3.055 0.502 1.00 73.83 C -ANISOU 1410 CA VAL A 181 8503 10299 9249 509 327 275 C -ATOM 1411 C VAL A 181 40.988 1.869 0.070 1.00 74.08 C -ANISOU 1411 C VAL A 181 8499 10410 9236 676 380 281 C -ATOM 1412 O VAL A 181 42.186 1.818 0.349 1.00 74.12 O -ANISOU 1412 O VAL A 181 8385 10521 9254 704 396 369 O -ATOM 1413 CB VAL A 181 40.755 3.738 1.740 1.00 74.10 C -ANISOU 1413 CB VAL A 181 8461 10344 9350 390 268 349 C -ATOM 1414 CG1 VAL A 181 39.899 4.914 2.201 1.00 73.02 C -ANISOU 1414 CG1 VAL A 181 8376 10119 9248 240 211 335 C -ATOM 1415 CG2 VAL A 181 40.957 2.736 2.871 1.00 73.75 C -ANISOU 1415 CG2 VAL A 181 8440 10251 9332 426 231 319 C -ATOM 1416 N THR A 186 43.118 -1.501 8.341 1.00 69.10 N -ANISOU 1416 N THR A 186 7867 9530 8858 581 27 327 N -ATOM 1417 CA THR A 186 41.853 -2.129 8.692 1.00 67.06 C -ANISOU 1417 CA THR A 186 7757 9130 8592 576 10 231 C -ATOM 1418 C THR A 186 42.090 -3.449 9.421 1.00 66.79 C -ANISOU 1418 C THR A 186 7767 9047 8562 661 -17 216 C -ATOM 1419 O THR A 186 41.770 -3.574 10.604 1.00 68.54 O -ANISOU 1419 O THR A 186 8041 9199 8804 597 -72 210 O -ATOM 1420 CB THR A 186 40.977 -2.365 7.439 1.00 67.25 C -ANISOU 1420 CB THR A 186 7854 9118 8581 632 63 159 C -ATOM 1421 OG1 THR A 186 39.812 -3.125 7.791 1.00 65.38 O -ANISOU 1421 OG1 THR A 186 7750 8746 8345 630 39 78 O -ATOM 1422 CG2 THR A 186 41.764 -3.098 6.350 1.00 68.46 C -ANISOU 1422 CG2 THR A 186 7963 9354 8696 791 122 169 C -ATOM 1423 N GLU A 187 42.659 -4.423 8.715 1.00 65.36 N -ANISOU 1423 N GLU A 187 7573 8905 8358 812 22 211 N -ATOM 1424 CA GLU A 187 42.939 -5.736 9.288 1.00 64.02 C -ANISOU 1424 CA GLU A 187 7450 8684 8189 910 -5 197 C -ATOM 1425 C GLU A 187 43.737 -5.610 10.576 1.00 61.63 C -ANISOU 1425 C GLU A 187 7081 8415 7921 860 -63 268 C -ATOM 1426 O GLU A 187 43.407 -6.232 11.592 1.00 61.14 O -ANISOU 1426 O GLU A 187 7095 8263 7872 843 -114 250 O -ATOM 1427 CB GLU A 187 43.709 -6.618 8.298 1.00 67.54 C -ANISOU 1427 CB GLU A 187 7868 9195 8599 1095 47 196 C -ATOM 1428 CG GLU A 187 44.406 -7.806 8.964 1.00 71.55 C -ANISOU 1428 CG GLU A 187 8387 9686 9114 1207 15 211 C -ATOM 1429 CD GLU A 187 45.305 -8.594 8.020 1.00 75.12 C -ANISOU 1429 CD GLU A 187 8799 10219 9524 1408 70 218 C -ATOM 1430 OE1 GLU A 187 45.812 -8.015 7.035 1.00 76.60 O -ANISOU 1430 OE1 GLU A 187 8892 10531 9683 1451 137 252 O -ATOM 1431 OE2 GLU A 187 45.506 -9.801 8.269 1.00 76.04 O -ANISOU 1431 OE2 GLU A 187 8984 10275 9633 1528 46 192 O -ATOM 1432 N THR A 188 44.786 -4.793 10.525 1.00 53.39 N -ANISOU 1432 N THR A 188 5893 7502 6891 833 -59 355 N -ATOM 1433 CA THR A 188 45.712 -4.679 11.638 1.00 44.91 C -ANISOU 1433 CA THR A 188 4739 6475 5848 795 -121 433 C -ATOM 1434 C THR A 188 45.094 -3.950 12.825 1.00 33.97 C -ANISOU 1434 C THR A 188 3414 5012 4482 635 -193 426 C -ATOM 1435 O THR A 188 45.255 -4.381 13.968 1.00 32.90 O -ANISOU 1435 O THR A 188 3309 4835 4356 621 -254 439 O -ATOM 1436 CB THR A 188 47.003 -3.956 11.219 1.00 47.50 C -ANISOU 1436 CB THR A 188 4885 6969 6192 797 -105 541 C -ATOM 1437 OG1 THR A 188 47.598 -4.642 10.110 1.00 50.24 O -ANISOU 1437 OG1 THR A 188 5175 7404 6511 965 -26 552 O -ATOM 1438 CG2 THR A 188 47.987 -3.936 12.374 1.00 47.97 C -ANISOU 1438 CG2 THR A 188 4861 7076 6288 762 -182 625 C -ATOM 1439 N LEU A 189 44.407 -2.843 12.563 1.00 29.13 N -ANISOU 1439 N LEU A 189 2821 4381 3868 523 -187 406 N -ATOM 1440 CA LEU A 189 43.762 -2.102 13.644 1.00 30.88 C -ANISOU 1440 CA LEU A 189 3111 4527 4095 386 -249 391 C -ATOM 1441 C LEU A 189 42.637 -2.939 14.296 1.00 26.34 C -ANISOU 1441 C LEU A 189 2683 3823 3505 397 -257 316 C -ATOM 1442 O LEU A 189 42.430 -2.891 15.512 1.00 25.84 O -ANISOU 1442 O LEU A 189 2673 3708 3439 337 -314 319 O -ATOM 1443 CB LEU A 189 43.214 -0.772 13.132 1.00 29.79 C -ANISOU 1443 CB LEU A 189 2972 4390 3955 282 -238 382 C -ATOM 1444 CG LEU A 189 42.668 0.157 14.210 1.00 31.23 C -ANISOU 1444 CG LEU A 189 3223 4505 4137 150 -305 370 C -ATOM 1445 CD1 LEU A 189 43.816 0.697 15.044 1.00 36.12 C -ANISOU 1445 CD1 LEU A 189 3762 5185 4779 88 -388 454 C -ATOM 1446 CD2 LEU A 189 41.879 1.295 13.563 1.00 34.70 C -ANISOU 1446 CD2 LEU A 189 3690 4922 4571 73 -283 341 C -ATOM 1447 N LEU A 190 41.926 -3.709 13.481 1.00 25.89 N -ANISOU 1447 N LEU A 190 2688 3714 3434 474 -203 254 N -ATOM 1448 CA LEU A 190 40.900 -4.598 14.006 1.00 26.28 C -ANISOU 1448 CA LEU A 190 2865 3646 3476 483 -213 198 C -ATOM 1449 C LEU A 190 41.464 -5.601 15.000 1.00 27.15 C -ANISOU 1449 C LEU A 190 2991 3734 3591 535 -259 227 C -ATOM 1450 O LEU A 190 40.858 -5.856 16.032 1.00 28.29 O -ANISOU 1450 O LEU A 190 3215 3802 3731 485 -294 218 O -ATOM 1451 CB LEU A 190 40.198 -5.352 12.872 1.00 27.77 C -ANISOU 1451 CB LEU A 190 3114 3784 3654 563 -163 134 C -ATOM 1452 CG LEU A 190 39.032 -6.230 13.373 1.00 26.25 C -ANISOU 1452 CG LEU A 190 3048 3462 3463 552 -181 85 C -ATOM 1453 CD1 LEU A 190 37.842 -5.403 13.768 1.00 23.83 C -ANISOU 1453 CD1 LEU A 190 2790 3108 3156 432 -181 61 C -ATOM 1454 CD2 LEU A 190 38.646 -7.229 12.289 1.00 29.72 C -ANISOU 1454 CD2 LEU A 190 3548 3849 3895 651 -156 31 C -ATOM 1455 N VAL A 191 42.629 -6.165 14.696 1.00 29.03 N -ANISOU 1455 N VAL A 191 3151 4044 3836 639 -256 268 N -ATOM 1456 CA VAL A 191 43.287 -7.054 15.638 1.00 28.12 C -ANISOU 1456 CA VAL A 191 3040 3918 3728 693 -306 305 C -ATOM 1457 C VAL A 191 43.778 -6.276 16.854 1.00 29.58 C -ANISOU 1457 C VAL A 191 3181 4138 3919 591 -372 364 C -ATOM 1458 O VAL A 191 43.590 -6.723 17.978 1.00 28.74 O -ANISOU 1458 O VAL A 191 3142 3971 3806 569 -422 370 O -ATOM 1459 CB VAL A 191 44.468 -7.805 15.008 1.00 28.50 C -ANISOU 1459 CB VAL A 191 3004 4045 3779 843 -286 340 C -ATOM 1460 CG1 VAL A 191 45.179 -8.627 16.067 1.00 24.92 C -ANISOU 1460 CG1 VAL A 191 2550 3583 3336 893 -346 386 C -ATOM 1461 CG2 VAL A 191 43.976 -8.692 13.850 1.00 30.92 C -ANISOU 1461 CG2 VAL A 191 3382 4300 4067 960 -231 272 C -ATOM 1462 N GLN A 192 44.380 -5.107 16.625 1.00 29.83 N -ANISOU 1462 N GLN A 192 3110 4263 3961 526 -379 408 N -ATOM 1463 CA GLN A 192 44.926 -4.288 17.712 1.00 31.99 C -ANISOU 1463 CA GLN A 192 3346 4569 4242 424 -458 464 C -ATOM 1464 C GLN A 192 43.874 -3.878 18.747 1.00 30.06 C -ANISOU 1464 C GLN A 192 3225 4225 3969 322 -494 422 C -ATOM 1465 O GLN A 192 44.152 -3.839 19.943 1.00 31.12 O -ANISOU 1465 O GLN A 192 3387 4346 4093 281 -566 451 O -ATOM 1466 CB GLN A 192 45.589 -3.028 17.150 1.00 34.85 C -ANISOU 1466 CB GLN A 192 3588 5031 4623 356 -463 516 C -ATOM 1467 CG GLN A 192 46.269 -2.128 18.203 1.00 37.65 C -ANISOU 1467 CG GLN A 192 3900 5417 4989 244 -564 580 C -ATOM 1468 CD GLN A 192 47.516 -2.757 18.823 1.00 40.49 C -ANISOU 1468 CD GLN A 192 4172 5845 5369 299 -622 659 C -ATOM 1469 OE1 GLN A 192 47.436 -3.769 19.521 1.00 43.39 O -ANISOU 1469 OE1 GLN A 192 4604 6161 5722 362 -640 644 O -ATOM 1470 NE2 GLN A 192 48.674 -2.158 18.569 1.00 41.20 N -ANISOU 1470 NE2 GLN A 192 4109 6051 5493 272 -655 751 N -ATOM 1471 N ASN A 193 42.676 -3.548 18.283 1.00 28.64 N -ANISOU 1471 N ASN A 193 3121 3984 3775 286 -445 357 N -ATOM 1472 CA ASN A 193 41.623 -3.089 19.180 1.00 26.18 C -ANISOU 1472 CA ASN A 193 2920 3594 3434 200 -465 321 C -ATOM 1473 C ASN A 193 40.772 -4.251 19.725 1.00 27.48 C -ANISOU 1473 C ASN A 193 3191 3669 3583 242 -450 289 C -ATOM 1474 O ASN A 193 39.798 -4.021 20.446 1.00 27.67 O -ANISOU 1474 O ASN A 193 3305 3632 3578 185 -452 264 O -ATOM 1475 CB ASN A 193 40.735 -2.061 18.469 1.00 25.20 C -ANISOU 1475 CB ASN A 193 2815 3453 3304 138 -423 275 C -ATOM 1476 CG ASN A 193 41.474 -0.752 18.158 1.00 29.04 C -ANISOU 1476 CG ASN A 193 3218 4013 3805 69 -454 314 C -ATOM 1477 OD1 ASN A 193 42.640 -0.581 18.510 1.00 30.91 O -ANISOU 1477 OD1 ASN A 193 3374 4313 4057 58 -511 379 O -ATOM 1478 ND2 ASN A 193 40.791 0.164 17.478 1.00 31.87 N -ANISOU 1478 ND2 ASN A 193 3591 4359 4161 19 -421 281 N -ATOM 1479 N ALA A 194 41.140 -5.490 19.382 1.00 27.16 N -ANISOU 1479 N ALA A 194 3141 3620 3559 342 -437 296 N -ATOM 1480 CA ALA A 194 40.487 -6.673 19.941 1.00 25.50 C -ANISOU 1480 CA ALA A 194 3028 3320 3341 378 -439 283 C -ATOM 1481 C ALA A 194 40.866 -6.829 21.408 1.00 27.75 C -ANISOU 1481 C ALA A 194 3343 3597 3602 352 -506 329 C -ATOM 1482 O ALA A 194 41.881 -6.280 21.832 1.00 29.72 O -ANISOU 1482 O ALA A 194 3525 3915 3850 334 -557 373 O -ATOM 1483 CB ALA A 194 40.873 -7.917 19.159 1.00 28.68 C -ANISOU 1483 CB ALA A 194 3423 3708 3766 500 -420 276 C -ATOM 1484 N ASN A 195 40.078 -7.574 22.189 1.00 26.99 N -ANISOU 1484 N ASN A 195 3347 3420 3486 346 -511 326 N -ATOM 1485 CA ASN A 195 40.434 -7.727 23.606 1.00 30.58 C -ANISOU 1485 CA ASN A 195 3839 3871 3909 325 -573 373 C -ATOM 1486 C ASN A 195 41.585 -8.718 23.725 1.00 31.64 C -ANISOU 1486 C ASN A 195 3932 4025 4065 417 -617 418 C -ATOM 1487 O ASN A 195 41.933 -9.383 22.743 1.00 29.84 O -ANISOU 1487 O ASN A 195 3665 3799 3872 504 -591 407 O -ATOM 1488 CB ASN A 195 39.209 -8.115 24.483 1.00 21.97 C -ANISOU 1488 CB ASN A 195 2864 2701 2781 283 -559 369 C -ATOM 1489 CG ASN A 195 38.647 -9.502 24.201 1.00 25.90 C -ANISOU 1489 CG ASN A 195 3418 3118 3306 337 -538 368 C -ATOM 1490 OD1 ASN A 195 39.367 -10.444 23.863 1.00 27.88 O -ANISOU 1490 OD1 ASN A 195 3651 3357 3587 421 -560 383 O -ATOM 1491 ND2 ASN A 195 37.335 -9.639 24.387 1.00 28.23 N -ANISOU 1491 ND2 ASN A 195 3784 3353 3588 288 -500 356 N -ATOM 1492 N PRO A 196 42.214 -8.788 24.912 1.00 32.07 N -ANISOU 1492 N PRO A 196 3996 4095 4094 406 -688 469 N -ATOM 1493 CA PRO A 196 43.415 -9.611 25.091 1.00 33.35 C -ANISOU 1493 CA PRO A 196 4105 4288 4278 495 -738 521 C -ATOM 1494 C PRO A 196 43.302 -11.044 24.567 1.00 33.09 C -ANISOU 1494 C PRO A 196 4110 4190 4273 603 -714 513 C -ATOM 1495 O PRO A 196 44.161 -11.472 23.799 1.00 34.22 O -ANISOU 1495 O PRO A 196 4178 4375 4448 702 -709 521 O -ATOM 1496 CB PRO A 196 43.608 -9.609 26.619 1.00 35.61 C -ANISOU 1496 CB PRO A 196 4447 4564 4518 453 -814 568 C -ATOM 1497 CG PRO A 196 43.048 -8.294 27.047 1.00 35.36 C -ANISOU 1497 CG PRO A 196 4445 4546 4444 342 -816 543 C -ATOM 1498 CD PRO A 196 41.840 -8.086 26.153 1.00 32.67 C -ANISOU 1498 CD PRO A 196 4137 4164 4113 319 -726 481 C -ATOM 1499 N ASP A 197 42.269 -11.773 24.974 1.00 34.60 N -ANISOU 1499 N ASP A 197 4417 4280 4450 588 -702 501 N -ATOM 1500 CA ASP A 197 42.130 -13.184 24.613 1.00 37.45 C -ANISOU 1500 CA ASP A 197 4837 4557 4837 680 -700 497 C -ATOM 1501 C ASP A 197 41.901 -13.394 23.112 1.00 37.10 C -ANISOU 1501 C ASP A 197 4774 4497 4826 740 -644 438 C -ATOM 1502 O ASP A 197 42.477 -14.301 22.506 1.00 38.22 O -ANISOU 1502 O ASP A 197 4910 4620 4990 859 -651 434 O -ATOM 1503 CB ASP A 197 40.978 -13.822 25.400 1.00 40.81 C -ANISOU 1503 CB ASP A 197 5387 4877 5242 625 -704 510 C -ATOM 1504 CG ASP A 197 41.245 -13.868 26.902 1.00 45.50 C -ANISOU 1504 CG ASP A 197 6018 5478 5793 591 -761 573 C -ATOM 1505 OD1 ASP A 197 42.424 -13.777 27.316 1.00 45.63 O -ANISOU 1505 OD1 ASP A 197 5975 5558 5805 633 -816 611 O -ATOM 1506 OD2 ASP A 197 40.266 -13.995 27.668 1.00 47.99 O -ANISOU 1506 OD2 ASP A 197 6419 5739 6075 523 -752 591 O -ATOM 1507 N CYS A 198 41.045 -12.566 22.519 1.00 32.97 N -ANISOU 1507 N CYS A 198 4247 3979 4300 666 -590 391 N -ATOM 1508 CA CYS A 198 40.815 -12.627 21.086 1.00 33.24 C -ANISOU 1508 CA CYS A 198 4264 4007 4357 716 -540 334 C -ATOM 1509 C CYS A 198 42.062 -12.190 20.309 1.00 36.26 C -ANISOU 1509 C CYS A 198 4524 4504 4749 793 -526 341 C -ATOM 1510 O CYS A 198 42.417 -12.809 19.295 1.00 35.57 O -ANISOU 1510 O CYS A 198 4426 4415 4674 906 -503 315 O -ATOM 1511 CB CYS A 198 39.607 -11.765 20.700 1.00 33.92 C -ANISOU 1511 CB CYS A 198 4371 4080 4437 613 -490 290 C -ATOM 1512 SG CYS A 198 38.003 -12.536 21.091 1.00 42.87 S -ANISOU 1512 SG CYS A 198 5635 5079 5574 549 -488 281 S -ATOM 1513 N LYS A 199 42.736 -11.144 20.786 1.00 36.03 N -ANISOU 1513 N LYS A 199 4404 4573 4711 736 -543 380 N -ATOM 1514 CA LYS A 199 43.951 -10.671 20.121 1.00 36.66 C -ANISOU 1514 CA LYS A 199 4350 4775 4806 794 -534 407 C -ATOM 1515 C LYS A 199 45.002 -11.786 20.060 1.00 39.25 C -ANISOU 1515 C LYS A 199 4645 5120 5147 941 -557 442 C -ATOM 1516 O LYS A 199 45.724 -11.921 19.071 1.00 39.62 O -ANISOU 1516 O LYS A 199 4612 5238 5203 1046 -521 443 O -ATOM 1517 CB LYS A 199 44.530 -9.435 20.826 1.00 36.66 C -ANISOU 1517 CB LYS A 199 4267 4863 4801 694 -574 456 C -ATOM 1518 CG LYS A 199 45.684 -8.778 20.047 1.00 37.68 C -ANISOU 1518 CG LYS A 199 4239 5125 4951 726 -561 497 C -ATOM 1519 CD LYS A 199 46.351 -7.642 20.822 1.00 39.25 C -ANISOU 1519 CD LYS A 199 4360 5400 5152 620 -626 556 C -ATOM 1520 CE LYS A 199 45.481 -6.405 20.877 1.00 38.23 C -ANISOU 1520 CE LYS A 199 4274 5246 5006 485 -618 519 C -ATOM 1521 NZ LYS A 199 46.051 -5.299 21.702 1.00 38.92 N -ANISOU 1521 NZ LYS A 199 4316 5383 5090 376 -698 569 N -ATOM 1522 N THR A 200 45.068 -12.592 21.114 1.00 38.58 N -ANISOU 1522 N THR A 200 4627 4973 5058 957 -615 472 N -ATOM 1523 CA THR A 200 46.024 -13.691 21.182 1.00 39.14 C -ANISOU 1523 CA THR A 200 4681 5049 5140 1100 -647 507 C -ATOM 1524 C THR A 200 45.753 -14.733 20.105 1.00 39.45 C -ANISOU 1524 C THR A 200 4787 5017 5184 1230 -608 451 C -ATOM 1525 O THR A 200 46.666 -15.154 19.379 1.00 40.65 O -ANISOU 1525 O THR A 200 4873 5231 5342 1375 -589 459 O -ATOM 1526 CB THR A 200 45.989 -14.378 22.560 1.00 40.31 C -ANISOU 1526 CB THR A 200 4910 5126 5279 1082 -722 550 C -ATOM 1527 OG1 THR A 200 46.450 -13.461 23.558 1.00 40.15 O -ANISOU 1527 OG1 THR A 200 4828 5181 5246 984 -771 604 O -ATOM 1528 CG2 THR A 200 46.879 -15.620 22.562 1.00 41.87 C -ANISOU 1528 CG2 THR A 200 5109 5310 5491 1243 -756 580 C -ATOM 1529 N ILE A 201 44.493 -15.151 20.023 1.00 36.92 N -ANISOU 1529 N ILE A 201 4600 4569 4861 1181 -600 398 N -ATOM 1530 CA ILE A 201 44.042 -16.099 19.009 1.00 39.05 C -ANISOU 1530 CA ILE A 201 4960 4746 5133 1282 -578 335 C -ATOM 1531 C ILE A 201 44.312 -15.564 17.598 1.00 36.81 C -ANISOU 1531 C ILE A 201 4599 4547 4840 1344 -508 293 C -ATOM 1532 O ILE A 201 44.768 -16.299 16.716 1.00 37.41 O -ANISOU 1532 O ILE A 201 4689 4617 4907 1499 -491 264 O -ATOM 1533 CB ILE A 201 42.531 -16.407 19.184 1.00 40.64 C -ANISOU 1533 CB ILE A 201 5299 4805 5338 1178 -587 297 C -ATOM 1534 CG1 ILE A 201 42.327 -17.324 20.393 1.00 41.63 C -ANISOU 1534 CG1 ILE A 201 5519 4831 5469 1159 -655 343 C -ATOM 1535 CG2 ILE A 201 41.948 -17.019 17.911 1.00 41.34 C -ANISOU 1535 CG2 ILE A 201 5468 4811 5429 1249 -564 221 C -ATOM 1536 CD1 ILE A 201 40.904 -17.348 20.938 1.00 41.29 C -ANISOU 1536 CD1 ILE A 201 5573 4686 5428 1019 -662 341 C -ATOM 1537 N LEU A 202 44.055 -14.273 17.412 1.00 33.60 N -ANISOU 1537 N LEU A 202 4117 4219 4431 1230 -469 292 N -ATOM 1538 CA LEU A 202 44.208 -13.601 16.121 1.00 35.31 C -ANISOU 1538 CA LEU A 202 4259 4520 4636 1263 -401 261 C -ATOM 1539 C LEU A 202 45.665 -13.453 15.671 1.00 40.63 C -ANISOU 1539 C LEU A 202 4789 5343 5307 1383 -376 312 C -ATOM 1540 O LEU A 202 45.980 -13.679 14.503 1.00 39.46 O -ANISOU 1540 O LEU A 202 4617 5237 5139 1505 -323 283 O -ATOM 1541 CB LEU A 202 43.545 -12.222 16.177 1.00 33.61 C -ANISOU 1541 CB LEU A 202 4006 4343 4421 1100 -376 256 C -ATOM 1542 CG LEU A 202 42.012 -12.279 16.223 1.00 33.15 C -ANISOU 1542 CG LEU A 202 4072 4160 4362 1002 -376 199 C -ATOM 1543 CD1 LEU A 202 41.406 -10.927 16.487 1.00 35.34 C -ANISOU 1543 CD1 LEU A 202 4315 4474 4638 851 -358 201 C -ATOM 1544 CD2 LEU A 202 41.507 -12.836 14.901 1.00 32.86 C -ANISOU 1544 CD2 LEU A 202 4100 4068 4317 1084 -341 129 C -ATOM 1545 N LYS A 203 46.541 -13.055 16.592 1.00 44.37 N -ANISOU 1545 N LYS A 203 5162 5900 5796 1347 -415 391 N -ATOM 1546 CA LYS A 203 47.964 -12.907 16.284 1.00 50.82 C -ANISOU 1546 CA LYS A 203 5821 6870 6620 1450 -399 460 C -ATOM 1547 C LYS A 203 48.556 -14.237 15.828 1.00 53.96 C -ANISOU 1547 C LYS A 203 6249 7250 7005 1660 -390 449 C -ATOM 1548 O LYS A 203 49.414 -14.284 14.944 1.00 54.92 O -ANISOU 1548 O LYS A 203 6269 7484 7113 1794 -336 470 O -ATOM 1549 CB LYS A 203 48.733 -12.386 17.504 1.00 52.34 C -ANISOU 1549 CB LYS A 203 5919 7133 6836 1367 -467 549 C -ATOM 1550 CG LYS A 203 48.293 -11.002 17.972 1.00 53.83 C -ANISOU 1550 CG LYS A 203 6079 7344 7030 1172 -485 561 C -ATOM 1551 CD LYS A 203 48.710 -10.748 19.419 1.00 58.10 C -ANISOU 1551 CD LYS A 203 6601 7891 7581 1084 -577 624 C -ATOM 1552 CE LYS A 203 50.152 -10.257 19.523 1.00 61.69 C -ANISOU 1552 CE LYS A 203 6875 8502 8063 1102 -609 724 C -ATOM 1553 NZ LYS A 203 50.212 -8.773 19.707 1.00 61.38 N -ANISOU 1553 NZ LYS A 203 6761 8527 8033 938 -635 757 N -ATOM 1554 N ALA A 204 48.085 -15.317 16.442 1.00 54.14 N -ANISOU 1554 N ALA A 204 6414 7129 7029 1691 -444 419 N -ATOM 1555 CA ALA A 204 48.583 -16.654 16.154 1.00 54.76 C -ANISOU 1555 CA ALA A 204 6550 7160 7096 1890 -454 405 C -ATOM 1556 C ALA A 204 48.008 -17.227 14.865 1.00 57.51 C -ANISOU 1556 C ALA A 204 7005 7435 7412 1998 -406 312 C -ATOM 1557 O ALA A 204 48.370 -18.330 14.464 1.00 58.16 O -ANISOU 1557 O ALA A 204 7155 7467 7475 2178 -414 286 O -ATOM 1558 CB ALA A 204 48.279 -17.577 17.309 1.00 54.05 C -ANISOU 1558 CB ALA A 204 6581 6934 7021 1873 -540 415 C -ATOM 1559 N LEU A 205 47.106 -16.490 14.224 1.00 58.48 N -ANISOU 1559 N LEU A 205 7152 7544 7525 1892 -365 261 N -ATOM 1560 CA LEU A 205 46.571 -16.907 12.933 1.00 62.01 C -ANISOU 1560 CA LEU A 205 7693 7932 7935 1985 -323 174 C -ATOM 1561 C LEU A 205 47.539 -16.532 11.824 1.00 67.29 C -ANISOU 1561 C LEU A 205 8233 8765 8567 2125 -239 189 C -ATOM 1562 O LEU A 205 47.548 -17.146 10.758 1.00 70.77 O -ANISOU 1562 O LEU A 205 8744 9184 8963 2281 -205 128 O -ATOM 1563 CB LEU A 205 45.204 -16.269 12.672 1.00 61.08 C -ANISOU 1563 CB LEU A 205 7647 7739 7821 1819 -314 118 C -ATOM 1564 CG LEU A 205 43.957 -16.972 13.207 1.00 60.26 C -ANISOU 1564 CG LEU A 205 7716 7443 7738 1731 -381 74 C -ATOM 1565 CD1 LEU A 205 42.785 -16.004 13.211 1.00 58.52 C -ANISOU 1565 CD1 LEU A 205 7503 7202 7529 1543 -365 52 C -ATOM 1566 CD2 LEU A 205 43.632 -18.204 12.367 1.00 61.26 C -ANISOU 1566 CD2 LEU A 205 7997 7439 7840 1873 -404 -4 C -ATOM 1567 N GLY A 206 48.355 -15.517 12.089 1.00 68.87 N -ANISOU 1567 N GLY A 206 8249 9134 8786 2066 -210 276 N -ATOM 1568 CA GLY A 206 49.280 -14.996 11.100 1.00 70.10 C -ANISOU 1568 CA GLY A 206 8254 9469 8913 2170 -126 316 C -ATOM 1569 C GLY A 206 48.610 -13.943 10.239 1.00 70.39 C -ANISOU 1569 C GLY A 206 8273 9542 8932 2063 -68 285 C -ATOM 1570 O GLY A 206 47.390 -13.779 10.294 1.00 70.43 O -ANISOU 1570 O GLY A 206 8398 9420 8943 1939 -92 219 O -ATOM 1571 N PRO A 207 49.403 -13.215 9.440 1.00 70.25 N -ANISOU 1571 N PRO A 207 8098 9701 8893 2111 9 342 N -ATOM 1572 CA PRO A 207 48.844 -12.224 8.517 1.00 67.65 C -ANISOU 1572 CA PRO A 207 7748 9413 8541 2026 68 319 C -ATOM 1573 C PRO A 207 48.013 -12.888 7.423 1.00 64.14 C -ANISOU 1573 C PRO A 207 7468 8865 8036 2130 98 204 C -ATOM 1574 O PRO A 207 48.211 -14.071 7.133 1.00 65.03 O -ANISOU 1574 O PRO A 207 7675 8920 8114 2311 93 157 O -ATOM 1575 CB PRO A 207 50.088 -11.546 7.920 1.00 69.82 C -ANISOU 1575 CB PRO A 207 7813 9910 8804 2093 144 423 C -ATOM 1576 CG PRO A 207 51.214 -11.905 8.833 1.00 71.44 C -ANISOU 1576 CG PRO A 207 7912 10184 9047 2134 104 511 C -ATOM 1577 CD PRO A 207 50.872 -13.260 9.374 1.00 71.76 C -ANISOU 1577 CD PRO A 207 8116 10066 9083 2235 45 440 C -ATOM 1578 N GLY A 208 47.085 -12.138 6.838 1.00 60.38 N -ANISOU 1578 N GLY A 208 7034 8359 7549 2016 119 159 N -ATOM 1579 CA GLY A 208 46.331 -12.619 5.693 1.00 57.88 C -ANISOU 1579 CA GLY A 208 6858 7961 7171 2104 145 58 C -ATOM 1580 C GLY A 208 45.145 -13.521 5.993 1.00 53.08 C -ANISOU 1580 C GLY A 208 6458 7137 6575 2073 66 -41 C -ATOM 1581 O GLY A 208 44.554 -14.098 5.071 1.00 50.58 O -ANISOU 1581 O GLY A 208 6276 6734 6208 2159 68 -129 O -ATOM 1582 N ALA A 209 44.804 -13.665 7.273 1.00 49.06 N -ANISOU 1582 N ALA A 209 5975 6537 6127 1951 -7 -21 N -ATOM 1583 CA ALA A 209 43.557 -14.319 7.647 1.00 44.71 C -ANISOU 1583 CA ALA A 209 5598 5790 5598 1874 -81 -93 C -ATOM 1584 C ALA A 209 42.405 -13.518 7.071 1.00 41.68 C -ANISOU 1584 C ALA A 209 5252 5374 5212 1741 -66 -138 C -ATOM 1585 O ALA A 209 42.416 -12.292 7.119 1.00 42.01 O -ANISOU 1585 O ALA A 209 5181 5513 5267 1625 -29 -94 O -ATOM 1586 CB ALA A 209 43.420 -14.431 9.163 1.00 43.41 C -ANISOU 1586 CB ALA A 209 5434 5565 5495 1754 -148 -45 C -ATOM 1587 N THR A 210 41.416 -14.204 6.518 1.00 40.02 N -ANISOU 1587 N THR A 210 5200 5020 4985 1758 -103 -224 N -ATOM 1588 CA THR A 210 40.197 -13.529 6.079 1.00 38.19 C -ANISOU 1588 CA THR A 210 5010 4740 4759 1622 -104 -265 C -ATOM 1589 C THR A 210 39.367 -13.168 7.315 1.00 37.69 C -ANISOU 1589 C THR A 210 4949 4609 4763 1429 -152 -234 C -ATOM 1590 O THR A 210 39.590 -13.733 8.390 1.00 40.37 O -ANISOU 1590 O THR A 210 5302 4901 5136 1417 -196 -200 O -ATOM 1591 CB THR A 210 39.371 -14.413 5.156 1.00 34.93 C -ANISOU 1591 CB THR A 210 4767 4191 4312 1690 -146 -361 C -ATOM 1592 OG1 THR A 210 38.810 -15.472 5.936 1.00 37.31 O -ANISOU 1592 OG1 THR A 210 5192 4329 4656 1661 -235 -377 O -ATOM 1593 CG2 THR A 210 40.257 -15.010 4.052 1.00 36.89 C -ANISOU 1593 CG2 THR A 210 5044 4490 4481 1916 -107 -398 C -ATOM 1594 N LEU A 211 38.408 -12.254 7.170 1.00 34.12 N -ANISOU 1594 N LEU A 211 4487 4153 4326 1288 -141 -245 N -ATOM 1595 CA LEU A 211 37.565 -11.877 8.312 1.00 30.64 C -ANISOU 1595 CA LEU A 211 4048 3655 3937 1119 -176 -217 C -ATOM 1596 C LEU A 211 36.790 -13.103 8.766 1.00 30.47 C -ANISOU 1596 C LEU A 211 4164 3470 3942 1111 -250 -244 C -ATOM 1597 O LEU A 211 36.680 -13.373 9.973 1.00 28.48 O -ANISOU 1597 O LEU A 211 3919 3176 3726 1045 -286 -200 O -ATOM 1598 CB LEU A 211 36.611 -10.726 7.973 1.00 26.76 C -ANISOU 1598 CB LEU A 211 3531 3184 3452 990 -150 -229 C -ATOM 1599 CG LEU A 211 35.625 -10.300 9.088 1.00 25.12 C -ANISOU 1599 CG LEU A 211 3332 2923 3289 828 -177 -204 C -ATOM 1600 CD1 LEU A 211 36.348 -9.936 10.414 1.00 24.45 C -ANISOU 1600 CD1 LEU A 211 3172 2896 3222 784 -180 -135 C -ATOM 1601 CD2 LEU A 211 34.713 -9.167 8.664 1.00 26.37 C -ANISOU 1601 CD2 LEU A 211 3465 3104 3450 723 -149 -219 C -ATOM 1602 N GLU A 212 36.289 -13.862 7.792 1.00 27.69 N -ANISOU 1602 N GLU A 212 3925 3027 3570 1179 -279 -312 N -ATOM 1603 CA GLU A 212 35.612 -15.116 8.092 1.00 34.13 C -ANISOU 1603 CA GLU A 212 4880 3675 4412 1177 -364 -336 C -ATOM 1604 C GLU A 212 36.433 -15.994 9.040 1.00 35.48 C -ANISOU 1604 C GLU A 212 5067 3818 4597 1246 -398 -295 C -ATOM 1605 O GLU A 212 35.914 -16.503 10.033 1.00 36.55 O -ANISOU 1605 O GLU A 212 5251 3862 4776 1163 -452 -260 O -ATOM 1606 CB GLU A 212 35.311 -15.892 6.809 1.00 39.57 C -ANISOU 1606 CB GLU A 212 5696 4275 5064 1282 -400 -419 C -ATOM 1607 CG GLU A 212 34.691 -17.254 7.074 1.00 45.54 C -ANISOU 1607 CG GLU A 212 6608 4843 5850 1283 -505 -441 C -ATOM 1608 CD GLU A 212 34.307 -17.978 5.800 1.00 51.28 C -ANISOU 1608 CD GLU A 212 7478 5467 6538 1376 -558 -531 C -ATOM 1609 OE1 GLU A 212 35.056 -17.868 4.802 1.00 51.76 O -ANISOU 1609 OE1 GLU A 212 7535 5601 6528 1526 -511 -577 O -ATOM 1610 OE2 GLU A 212 33.252 -18.649 5.800 1.00 53.58 O -ANISOU 1610 OE2 GLU A 212 7885 5604 6867 1297 -650 -550 O -ATOM 1611 N GLU A 213 37.715 -16.152 8.740 1.00 34.27 N -ANISOU 1611 N GLU A 213 4865 3750 4405 1400 -364 -290 N -ATOM 1612 CA GLU A 213 38.576 -16.994 9.561 1.00 36.53 C -ANISOU 1612 CA GLU A 213 5162 4016 4701 1485 -397 -251 C -ATOM 1613 C GLU A 213 38.780 -16.380 10.949 1.00 33.71 C -ANISOU 1613 C GLU A 213 4705 3722 4383 1365 -391 -167 C -ATOM 1614 O GLU A 213 38.833 -17.098 11.950 1.00 35.38 O -ANISOU 1614 O GLU A 213 4962 3861 4621 1353 -445 -130 O -ATOM 1615 CB GLU A 213 39.916 -17.217 8.861 1.00 38.75 C -ANISOU 1615 CB GLU A 213 5395 4397 4930 1686 -352 -259 C -ATOM 1616 CG GLU A 213 39.780 -17.966 7.545 1.00 44.18 C -ANISOU 1616 CG GLU A 213 6208 5014 5566 1834 -364 -348 C -ATOM 1617 CD GLU A 213 41.027 -17.883 6.679 1.00 48.29 C -ANISOU 1617 CD GLU A 213 6655 5674 6019 2031 -289 -352 C -ATOM 1618 OE1 GLU A 213 41.888 -17.017 6.940 1.00 46.87 O -ANISOU 1618 OE1 GLU A 213 6306 5663 5841 2023 -221 -282 O -ATOM 1619 OE2 GLU A 213 41.133 -18.678 5.719 1.00 52.11 O -ANISOU 1619 OE2 GLU A 213 7254 6100 6446 2195 -301 -424 O -ATOM 1620 N MET A 214 38.890 -15.056 11.002 1.00 31.12 N -ANISOU 1620 N MET A 214 4250 3522 4052 1279 -332 -138 N -ATOM 1621 CA MET A 214 39.051 -14.348 12.276 1.00 30.28 C -ANISOU 1621 CA MET A 214 4059 3474 3972 1162 -332 -67 C -ATOM 1622 C MET A 214 37.825 -14.481 13.177 1.00 30.12 C -ANISOU 1622 C MET A 214 4114 3347 3985 1018 -374 -55 C -ATOM 1623 O MET A 214 37.950 -14.714 14.384 1.00 28.97 O -ANISOU 1623 O MET A 214 3971 3182 3855 974 -407 -2 O -ATOM 1624 CB MET A 214 39.353 -12.865 12.036 1.00 28.85 C -ANISOU 1624 CB MET A 214 3745 3437 3781 1097 -270 -44 C -ATOM 1625 CG MET A 214 40.791 -12.577 11.597 1.00 33.29 C -ANISOU 1625 CG MET A 214 4188 4140 4319 1211 -229 -11 C -ATOM 1626 SD MET A 214 41.120 -10.802 11.408 1.00 47.84 S -ANISOU 1626 SD MET A 214 5878 6140 6161 1107 -174 32 S -ATOM 1627 CE MET A 214 40.873 -10.234 13.081 1.00 42.30 C -ANISOU 1627 CE MET A 214 5161 5420 5491 949 -224 86 C -ATOM 1628 N MET A 215 36.644 -14.316 12.594 1.00 29.33 N -ANISOU 1628 N MET A 215 4068 3184 3892 946 -371 -99 N -ATOM 1629 CA MET A 215 35.405 -14.438 13.352 1.00 31.40 C -ANISOU 1629 CA MET A 215 4389 3356 4186 812 -403 -80 C -ATOM 1630 C MET A 215 35.154 -15.880 13.790 1.00 32.14 C -ANISOU 1630 C MET A 215 4600 3308 4303 840 -477 -69 C -ATOM 1631 O MET A 215 34.724 -16.125 14.923 1.00 34.47 O -ANISOU 1631 O MET A 215 4917 3560 4620 756 -505 -14 O -ATOM 1632 CB MET A 215 34.232 -13.910 12.536 1.00 30.14 C -ANISOU 1632 CB MET A 215 4246 3173 4032 734 -385 -124 C -ATOM 1633 CG MET A 215 34.296 -12.395 12.351 1.00 31.99 C -ANISOU 1633 CG MET A 215 4371 3533 4250 676 -319 -121 C -ATOM 1634 SD MET A 215 32.969 -11.778 11.328 1.00 42.87 S -ANISOU 1634 SD MET A 215 5767 4887 5633 601 -301 -172 S -ATOM 1635 CE MET A 215 31.579 -11.967 12.442 1.00 50.43 C -ANISOU 1635 CE MET A 215 6766 5763 6632 459 -330 -128 C -ATOM 1636 N THR A 216 35.450 -16.831 12.911 1.00 33.63 N -ANISOU 1636 N THR A 216 4871 3426 4483 963 -512 -119 N -ATOM 1637 CA THR A 216 35.466 -18.238 13.297 1.00 37.47 C -ANISOU 1637 CA THR A 216 5474 3774 4988 1015 -591 -109 C -ATOM 1638 C THR A 216 36.413 -18.499 14.470 1.00 37.08 C -ANISOU 1638 C THR A 216 5388 3762 4939 1050 -602 -42 C -ATOM 1639 O THR A 216 36.064 -19.207 15.414 1.00 39.30 O -ANISOU 1639 O THR A 216 5733 3953 5247 998 -656 7 O -ATOM 1640 CB THR A 216 35.881 -19.139 12.117 1.00 42.12 C -ANISOU 1640 CB THR A 216 6160 4294 5552 1177 -624 -182 C -ATOM 1641 OG1 THR A 216 34.820 -19.179 11.154 1.00 43.23 O -ANISOU 1641 OG1 THR A 216 6373 4356 5696 1130 -647 -241 O -ATOM 1642 CG2 THR A 216 36.185 -20.550 12.597 1.00 42.57 C -ANISOU 1642 CG2 THR A 216 6333 4217 5623 1256 -708 -167 C -ATOM 1643 N ALA A 217 37.612 -17.929 14.414 1.00 34.42 N -ANISOU 1643 N ALA A 217 4944 3560 4574 1135 -553 -32 N -ATOM 1644 CA ALA A 217 38.631 -18.246 15.413 1.00 36.96 C -ANISOU 1644 CA ALA A 217 5229 3919 4895 1189 -573 29 C -ATOM 1645 C ALA A 217 38.307 -17.634 16.779 1.00 37.12 C -ANISOU 1645 C ALA A 217 5203 3974 4927 1043 -574 100 C -ATOM 1646 O ALA A 217 38.785 -18.110 17.800 1.00 40.66 O -ANISOU 1646 O ALA A 217 5661 4408 5379 1056 -613 156 O -ATOM 1647 CB ALA A 217 40.002 -17.785 14.938 1.00 35.82 C -ANISOU 1647 CB ALA A 217 4970 3920 4721 1315 -525 31 C -ATOM 1648 N CYS A 218 37.514 -16.569 16.794 1.00 35.26 N -ANISOU 1648 N CYS A 218 4921 3785 4691 915 -531 95 N -ATOM 1649 CA CYS A 218 37.162 -15.892 18.044 1.00 36.10 C -ANISOU 1649 CA CYS A 218 4991 3929 4795 789 -525 154 C -ATOM 1650 C CYS A 218 35.708 -16.114 18.475 1.00 39.09 C -ANISOU 1650 C CYS A 218 5445 4214 5193 666 -537 168 C -ATOM 1651 O CYS A 218 35.236 -15.478 19.413 1.00 40.65 O -ANISOU 1651 O CYS A 218 5618 4447 5379 564 -519 210 O -ATOM 1652 CB CYS A 218 37.434 -14.387 17.921 1.00 34.58 C -ANISOU 1652 CB CYS A 218 4683 3874 4583 737 -467 149 C -ATOM 1653 SG CYS A 218 39.205 -13.984 17.847 1.00 41.23 S -ANISOU 1653 SG CYS A 218 5405 4852 5408 843 -460 173 S -ATOM 1654 N GLN A 219 35.004 -17.020 17.803 1.00 40.99 N -ANISOU 1654 N GLN A 219 5778 4335 5460 678 -571 138 N -ATOM 1655 CA GLN A 219 33.584 -17.247 18.091 1.00 45.47 C -ANISOU 1655 CA GLN A 219 6403 4818 6055 556 -586 162 C -ATOM 1656 C GLN A 219 33.384 -17.767 19.514 1.00 46.79 C -ANISOU 1656 C GLN A 219 6606 4947 6227 496 -617 249 C -ATOM 1657 O GLN A 219 34.302 -18.352 20.104 1.00 48.28 O -ANISOU 1657 O GLN A 219 6814 5127 6406 568 -652 280 O -ATOM 1658 CB GLN A 219 32.982 -18.230 17.074 1.00 49.44 C -ANISOU 1658 CB GLN A 219 7007 5188 6591 583 -639 117 C -ATOM 1659 CG GLN A 219 31.494 -18.035 16.806 1.00 52.27 C -ANISOU 1659 CG GLN A 219 7381 5499 6979 456 -638 119 C -ATOM 1660 CD GLN A 219 31.044 -18.642 15.482 1.00 54.94 C -ANISOU 1660 CD GLN A 219 7800 5736 7339 492 -686 51 C -ATOM 1661 OE1 GLN A 219 31.749 -19.457 14.889 1.00 57.99 O -ANISOU 1661 OE1 GLN A 219 8259 6058 7718 613 -733 6 O -ATOM 1662 NE2 GLN A 219 29.867 -18.237 15.013 1.00 53.57 N -ANISOU 1662 NE2 GLN A 219 7616 5549 7189 392 -679 41 N -TER 1663 GLN A 219 -HETATM 1664 O24 1B0 A 301 16.149 26.725 -0.227 1.00 26.22 O -ANISOU 1664 O24 1B0 A 301 3954 2645 3363 89 -391 -234 O -HETATM 1665 C23 1B0 A 301 15.304 25.902 -0.020 1.00 26.40 C -ANISOU 1665 C23 1B0 A 301 3908 2729 3392 147 -333 -263 C -HETATM 1666 N4 1B0 A 301 15.225 24.695 -0.783 1.00 25.14 N -ANISOU 1666 N4 1B0 A 301 3640 2662 3252 118 -289 -249 N -HETATM 1667 C5 1B0 A 301 16.121 24.407 -1.852 1.00 23.37 C -ANISOU 1667 C5 1B0 A 301 3384 2470 3028 36 -300 -206 C -HETATM 1668 C13 1B0 A 301 15.485 24.900 -3.135 1.00 25.73 C -ANISOU 1668 C13 1B0 A 301 3681 2768 3327 55 -325 -180 C -HETATM 1669 N15 1B0 A 301 16.277 25.489 -4.212 1.00 27.10 N -ANISOU 1669 N15 1B0 A 301 3880 2931 3487 -8 -363 -124 N -HETATM 1670 C17 1B0 A 301 17.723 25.617 -4.002 1.00 28.59 C -ANISOU 1670 C17 1B0 A 301 4084 3112 3667 -96 -377 -86 C -HETATM 1671 C22 1B0 A 301 18.578 24.624 -4.466 1.00 26.51 C -ANISOU 1671 C22 1B0 A 301 3749 2929 3394 -146 -338 -63 C -HETATM 1672 C21 1B0 A 301 19.956 24.733 -4.238 1.00 27.91 C -ANISOU 1672 C21 1B0 A 301 3925 3112 3568 -226 -349 -18 C -HETATM 1673 C20 1B0 A 301 20.456 25.831 -3.557 1.00 29.99 C -ANISOU 1673 C20 1B0 A 301 4264 3291 3841 -267 -408 3 C -HETATM 1674 C19 1B0 A 301 19.598 26.823 -3.086 1.00 30.00 C -ANISOU 1674 C19 1B0 A 301 4355 3198 3847 -217 -454 -28 C -HETATM 1675 C18 1B0 A 301 18.227 26.721 -3.306 1.00 29.20 C -ANISOU 1675 C18 1B0 A 301 4250 3100 3746 -124 -433 -73 C -HETATM 1676 C16 1B0 A 301 15.615 25.929 -5.460 1.00 29.84 C -ANISOU 1676 C16 1B0 A 301 4230 3281 3828 16 -388 -97 C -HETATM 1677 O14 1B0 A 301 14.308 24.778 -3.276 1.00 27.63 O -ANISOU 1677 O14 1B0 A 301 3895 3025 3580 123 -313 -200 O -HETATM 1678 C6 1B0 A 301 16.314 22.898 -2.033 1.00 22.29 C -ANISOU 1678 C6 1B0 A 301 3153 2419 2898 12 -248 -213 C -HETATM 1679 C7 1B0 A 301 17.248 22.447 -0.920 1.00 22.61 C -ANISOU 1679 C7 1B0 A 301 3197 2461 2935 -25 -231 -224 C -HETATM 1680 C12 1B0 A 301 18.627 22.477 -1.112 1.00 24.28 C -ANISOU 1680 C12 1B0 A 301 3411 2678 3137 -103 -248 -187 C -HETATM 1681 C11 1B0 A 301 19.468 22.087 -0.071 1.00 24.90 C -ANISOU 1681 C11 1B0 A 301 3490 2757 3214 -135 -241 -194 C -HETATM 1682 C10 1B0 A 301 18.929 21.696 1.150 1.00 23.07 C -ANISOU 1682 C10 1B0 A 301 3268 2517 2982 -87 -216 -240 C -HETATM 1683 C9 1B0 A 301 17.547 21.687 1.334 1.00 21.29 C -ANISOU 1683 C9 1B0 A 301 3039 2290 2761 -8 -192 -273 C -HETATM 1684 C8 1B0 A 301 16.716 22.073 0.300 1.00 21.02 C -ANISOU 1684 C8 1B0 A 301 2995 2257 2736 23 -201 -264 C -HETATM 1685 C25 1B0 A 301 14.247 26.154 1.097 1.00 27.82 C -ANISOU 1685 C25 1B0 A 301 4122 2889 3558 261 -308 -311 C -HETATM 1686 C1 1B0 A 301 14.863 26.302 2.484 1.00 26.30 C -ANISOU 1686 C1 1B0 A 301 4003 2653 3336 262 -315 -343 C -HETATM 1687 C26 1B0 A 301 15.178 27.479 3.176 1.00 24.80 C -ANISOU 1687 C26 1B0 A 301 3950 2357 3115 285 -379 -363 C -HETATM 1688 C31 1B0 A 301 15.051 28.832 2.830 1.00 27.08 C -ANISOU 1688 C31 1B0 A 301 4349 2546 3396 309 -453 -359 C -HETATM 1689 C30 1B0 A 301 15.436 29.809 3.726 1.00 30.53 C -ANISOU 1689 C30 1B0 A 301 4931 2872 3797 329 -521 -388 C -HETATM 1690 C29 1B0 A 301 15.945 29.455 4.975 1.00 28.76 C -ANISOU 1690 C29 1B0 A 301 4743 2642 3541 325 -514 -423 C -HETATM 1691 C28 1B0 A 301 16.079 28.125 5.306 1.00 25.23 C -ANISOU 1691 C28 1B0 A 301 4182 2303 3103 300 -436 -422 C -HETATM 1692 C27 1B0 A 301 15.674 27.132 4.399 1.00 24.35 C -ANISOU 1692 C27 1B0 A 301 3925 2296 3032 281 -368 -392 C -HETATM 1693 N3 1B0 A 301 15.682 25.735 4.474 1.00 23.13 N -ANISOU 1693 N3 1B0 A 301 3649 2246 2895 255 -294 -386 N -HETATM 1694 C2 1B0 A 301 15.177 25.236 3.276 1.00 25.46 C -ANISOU 1694 C2 1B0 A 301 3844 2602 3226 243 -266 -357 C -HETATM 1695 C32 1B0 A 301 15.218 23.723 3.428 1.00 25.52 C -ANISOU 1695 C32 1B0 A 301 3739 2705 3251 215 -199 -354 C -HETATM 1696 H4 1B0 A 301 14.555 24.109 -0.604 1.00 30.17 H -HETATM 1697 H251 1B0 A 301 13.752 26.980 0.888 1.00 33.38 H -HETATM 1698 H252 1B0 A 301 13.623 25.411 1.105 1.00 33.38 H -HETATM 1699 H5 1B0 A 301 17.006 24.860 -1.703 1.00 28.05 H -HETATM 1700 H61C 1B0 A 301 16.718 22.724 -2.897 1.00 26.75 H -HETATM 1701 H62C 1B0 A 301 15.442 22.436 -1.958 1.00 26.75 H -HETATM 1702 H161 1B0 A 301 15.018 26.701 -5.264 1.00 35.81 H -HETATM 1703 H162 1B0 A 301 15.076 25.180 -5.835 1.00 35.81 H -HETATM 1704 H163 1B0 A 301 16.305 26.203 -6.122 1.00 35.81 H -HETATM 1705 H22 1B0 A 301 18.215 23.839 -4.949 1.00 31.81 H -HETATM 1706 H18 1B0 A 301 17.624 27.414 -2.974 1.00 35.04 H -HETATM 1707 H21 1B0 A 301 20.575 24.031 -4.575 1.00 33.49 H -HETATM 1708 H20 1B0 A 301 21.434 25.913 -3.403 1.00 35.99 H -HETATM 1709 H19 1B0 A 301 19.960 27.596 -2.608 1.00 36.01 H -HETATM 1710 H12 1B0 A 301 19.022 22.770 -2.022 1.00 29.14 H -HETATM 1711 H8 1B0 A 301 15.746 22.069 0.427 1.00 25.23 H -HETATM 1712 H11 1B0 A 301 20.446 22.090 -0.199 1.00 29.88 H -HETATM 1713 H10 1B0 A 301 19.540 21.409 1.904 1.00 27.69 H -HETATM 1714 H9 1B0 A 301 17.152 21.398 2.224 1.00 25.55 H -HETATM 1715 H31 1B0 A 301 14.681 29.080 1.972 1.00 32.50 H -HETATM 1716 H30 1B0 A 301 15.347 30.764 3.482 1.00 36.64 H -HETATM 1717 H29 1B0 A 301 16.235 30.150 5.604 1.00 34.51 H -HETATM 1718 H28 1B0 A 301 16.447 27.869 6.188 1.00 30.28 H -HETATM 1719 H3 1B0 A 301 15.984 25.231 5.192 1.00 27.76 H -HETATM 1720 H321 1B0 A 301 15.538 23.326 2.608 1.00 30.62 H -HETATM 1721 H322 1B0 A 301 15.836 23.478 4.184 1.00 30.62 H -HETATM 1722 H323 1B0 A 301 14.311 23.386 3.623 1.00 30.62 H -HETATM 1723 O HOH A 401 14.623 20.538 4.162 1.00 21.99 O -ANISOU 1723 O HOH A 401 3076 2436 2842 203 -60 -353 O -HETATM 1724 O HOH A 402 12.264 22.853 8.665 1.00 26.38 O -ANISOU 1724 O HOH A 402 3880 2927 3217 599 33 -456 O -HETATM 1725 O HOH A 403 27.462 19.309 2.851 1.00 28.86 O -ANISOU 1725 O HOH A 403 3769 3460 3734 -476 -273 0 O -HETATM 1726 O HOH A 404 27.073 -3.083 12.037 1.00 18.27 O -ANISOU 1726 O HOH A 404 2376 2055 2511 4 -57 -152 O -HETATM 1727 O HOH A 405 32.433 -6.069 27.640 1.00 31.68 O -ANISOU 1727 O HOH A 405 4443 3830 3763 18 -322 346 O -HETATM 1728 O HOH A 406 34.711 1.038 22.042 1.00 28.78 O -ANISOU 1728 O HOH A 406 3771 3629 3536 -114 -376 86 O -HETATM 1729 O HOH A 407 27.133 -9.101 11.145 1.00 25.60 O -ANISOU 1729 O HOH A 407 3541 2650 3537 136 -252 -163 O -HETATM 1730 O HOH A 408 27.469 -4.472 17.659 1.00 22.60 O -ANISOU 1730 O HOH A 408 3011 2587 2990 -52 -75 29 O -HETATM 1731 O HOH A 409 31.659 -13.639 18.172 1.00 33.07 O -ANISOU 1731 O HOH A 409 4636 3480 4448 297 -412 147 O -HETATM 1732 O HOH A 410 26.661 9.634 10.155 1.00 24.50 O -ANISOU 1732 O HOH A 410 3135 3014 3158 -203 -45 -216 O -HETATM 1733 O HOH A 411 33.238 -13.972 20.460 1.00 35.30 O -ANISOU 1733 O HOH A 411 4914 3817 4682 336 -449 250 O -HETATM 1734 O HOH A 412 11.929 13.917 6.968 1.00 37.18 O -ANISOU 1734 O HOH A 412 4590 4657 4878 184 187 -254 O -HETATM 1735 O HOH A 413 10.423 21.995 -3.864 1.00 24.65 O -ANISOU 1735 O HOH A 413 3237 2839 3291 264 -237 -236 O -HETATM 1736 O HOH A 414 33.054 -14.299 15.904 1.00 33.94 O -ANISOU 1736 O HOH A 414 4762 3573 4561 503 -436 34 O -HETATM 1737 O HOH A 415 27.593 10.451 -6.909 1.00 29.10 O -ANISOU 1737 O HOH A 415 3553 4050 3454 99 153 -109 O -HETATM 1738 O HOH A 416 26.743 7.675 11.781 1.00 28.80 O -ANISOU 1738 O HOH A 416 3684 3561 3696 -172 -25 -208 O -HETATM 1739 O HOH A 417 19.582 13.772 -15.646 1.00 27.33 O -ANISOU 1739 O HOH A 417 3748 3682 2956 207 -169 -220 O -HETATM 1740 O HOH A 418 39.838 -4.283 23.645 1.00 26.82 O -ANISOU 1740 O HOH A 418 3339 3469 3380 124 -573 321 O -HETATM 1741 O HOH A 419 26.652 3.174 0.980 1.00 33.39 O -ANISOU 1741 O HOH A 419 4177 4238 4270 119 44 -336 O -HETATM 1742 O HOH A 420 15.007 20.390 13.890 1.00 31.48 O -ANISOU 1742 O HOH A 420 4675 3620 3667 540 99 -499 O -HETATM 1743 O HOH A 421 27.770 28.303 -16.568 1.00 39.84 O -ANISOU 1743 O HOH A 421 5136 5349 4651 -669 -197 1121 O -HETATM 1744 O HOH A 422 28.911 12.558 -5.698 1.00 31.17 O -ANISOU 1744 O HOH A 422 3721 4340 3783 -54 142 34 O -HETATM 1745 O HOH A 423 16.608 18.234 13.744 1.00 35.72 O -ANISOU 1745 O HOH A 423 5080 4214 4276 347 93 -445 O -HETATM 1746 O HOH A 424 23.210 29.644 -23.913 1.00 32.97 O -ANISOU 1746 O HOH A 424 4647 4566 3315 -314 -255 1180 O -HETATM 1747 O HOH A 425 24.463 11.281 -10.512 1.00 30.76 O -ANISOU 1747 O HOH A 425 3940 4202 3544 165 68 -189 O -HETATM 1748 O HOH A 426 29.266 27.760 -0.886 1.00 32.67 O -ANISOU 1748 O HOH A 426 4510 3609 4294 -943 -721 457 O -HETATM 1749 O HOH A 427 25.198 29.645 -11.600 1.00 27.76 O -ANISOU 1749 O HOH A 427 3877 3258 3411 -695 -484 748 O -HETATM 1750 O HOH A 428 35.843 9.113 19.076 1.00 37.13 O -ANISOU 1750 O HOH A 428 4804 4668 4636 -434 -594 38 O -HETATM 1751 O HOH A 429 13.385 23.560 -10.504 1.00 22.22 O -ANISOU 1751 O HOH A 429 3098 2545 2799 78 -403 -71 O -HETATM 1752 O HOH A 430 13.196 23.238 -7.605 1.00 27.35 O -ANISOU 1752 O HOH A 430 3718 3150 3524 103 -342 -141 O -HETATM 1753 O HOH A 431 27.526 29.054 -0.022 1.00 45.28 O -ANISOU 1753 O HOH A 431 6342 4986 5875 -854 -812 324 O -HETATM 1754 O HOH A 432 9.813 17.230 -12.093 1.00 29.80 O -ANISOU 1754 O HOH A 432 3825 3670 3826 108 -502 -235 O -HETATM 1755 O HOH A 433 21.699 29.941 -20.620 1.00 31.92 O -ANISOU 1755 O HOH A 433 4550 4112 3465 -353 -398 933 O -HETATM 1756 O HOH A 434 11.205 21.728 -6.401 1.00 22.86 O -ANISOU 1756 O HOH A 434 3025 2634 3028 180 -302 -202 O -HETATM 1757 O HOH A 435 9.764 15.743 6.851 1.00 35.17 O -ANISOU 1757 O HOH A 435 4307 4439 4617 341 221 -238 O -HETATM 1758 O HOH A 436 49.351 -15.408 19.707 1.00 42.36 O -ANISOU 1758 O HOH A 436 4848 5668 5580 1571 -630 596 O -HETATM 1759 O HOH A 437 39.567 -19.994 11.440 1.00 49.72 O -ANISOU 1759 O HOH A 437 7034 5443 6416 1667 -568 -194 O -HETATM 1760 O HOH A 438 43.336 -16.152 23.938 1.00 42.46 O -ANISOU 1760 O HOH A 438 5533 5071 5527 972 -759 521 O -HETATM 1761 O HOH A 439 6.283 4.891 0.967 1.00 40.80 O -ANISOU 1761 O HOH A 439 4546 5107 5849 -319 -266 2 O -HETATM 1762 O HOH A 440 16.462 23.314 -22.310 1.00 29.53 O -ANISOU 1762 O HOH A 440 4289 3932 2999 138 -442 279 O -HETATM 1763 O HOH A 441 16.526 25.728 -23.049 1.00 31.10 O -ANISOU 1763 O HOH A 441 4544 4085 3187 82 -487 448 O -HETATM 1764 O HOH A 442 39.972 -21.171 14.191 1.00 45.13 O -ANISOU 1764 O HOH A 442 6491 4753 5904 1595 -681 -50 O -HETATM 1765 O HOH A 443 18.542 25.112 6.369 1.00 25.95 O -ANISOU 1765 O HOH A 443 4076 2566 3218 82 -360 -385 O -HETATM 1766 O HOH A 444 8.831 25.329 -13.942 1.00 35.01 O -ANISOU 1766 O HOH A 444 4728 4146 4426 272 -627 -15 O -HETATM 1767 O HOH A 445 8.171 8.788 -7.963 1.00 26.72 O -ANISOU 1767 O HOH A 445 3193 3221 3739 -125 -569 -314 O -HETATM 1768 O HOH A 446 34.458 15.864 4.125 1.00 49.68 O -ANISOU 1768 O HOH A 446 5941 6502 6434 -613 -258 301 O -HETATM 1769 O HOH A 447 40.508 -20.439 17.947 1.00 42.17 O -ANISOU 1769 O HOH A 447 5961 4490 5573 1351 -716 177 O -HETATM 1770 O HOH A 448 2.654 11.872 -14.504 1.00 39.39 O -ANISOU 1770 O HOH A 448 4750 4878 5338 -65 -1089 -214 O -HETATM 1771 O HOH A 449 25.963 12.326 -15.507 1.00 52.65 O -ANISOU 1771 O HOH A 449 6781 7264 5958 356 180 -38 O -HETATM 1772 O HOH A 450 27.799 31.787 -16.957 1.00 49.46 O -ANISOU 1772 O HOH A 450 6500 6340 5954 -905 -408 1374 O -HETATM 1773 O HOH A 451 32.207 30.608 -10.890 1.00 41.53 O -ANISOU 1773 O HOH A 451 5208 5297 5273 -1253 -519 1382 O -HETATM 1774 O HOH A 452 22.027 29.226 -1.233 1.00 43.39 O -ANISOU 1774 O HOH A 452 6258 4668 5562 -409 -661 53 O -HETATM 1775 O HOH A 453 7.546 15.433 -10.595 1.00 30.78 O -ANISOU 1775 O HOH A 453 3779 3805 4111 82 -542 -244 O -HETATM 1776 O HOH A 454 30.379 16.861 -9.752 1.00 39.64 O -ANISOU 1776 O HOH A 454 4717 5622 4722 -187 177 399 O -HETATM 1777 O HOH A 455 15.568 9.095 -16.964 1.00 43.91 O -ANISOU 1777 O HOH A 455 6058 5550 5074 283 -525 -524 O -HETATM 1778 O HOH A 456 19.268 12.567 -18.250 1.00 39.61 O -ANISOU 1778 O HOH A 456 5452 5287 4311 347 -226 -285 O -HETATM 1779 O HOH A 457 10.060 13.413 -0.123 1.00 32.46 O -ANISOU 1779 O HOH A 457 3855 4044 4435 62 -62 -244 O -HETATM 1780 O HOH A 458 20.506 31.171 -15.793 1.00 35.73 O -ANISOU 1780 O HOH A 458 5122 4179 4275 -413 -569 699 O -HETATM 1781 O HOH A 459 7.701 15.152 -21.175 1.00 37.52 O -ANISOU 1781 O HOH A 459 5172 4697 4388 204 -1035 -307 O -HETATM 1782 O HOH A 460 39.375 -5.203 26.701 1.00 41.03 O -ANISOU 1782 O HOH A 460 5331 5195 5062 108 -655 378 O -HETATM 1783 O HOH A 461 22.887 11.259 11.908 1.00 38.82 O -ANISOU 1783 O HOH A 461 5091 4751 4908 -113 18 -286 O -HETATM 1784 O HOH A 462 21.694 3.519 -4.325 1.00 25.37 O -ANISOU 1784 O HOH A 462 3340 3100 3200 133 -113 -483 O -HETATM 1785 O HOH A 463 18.114 12.036 -13.553 1.00 37.98 O -ANISOU 1785 O HOH A 463 5058 4898 4472 163 -237 -338 O -HETATM 1786 O HOH A 464 8.941 17.570 -7.900 1.00 31.82 O -ANISOU 1786 O HOH A 464 3942 3908 4242 134 -363 -230 O -HETATM 1787 O HOH A 465 6.986 17.410 3.866 1.00 31.53 O -ANISOU 1787 O HOH A 465 3720 4009 4250 439 141 -195 O -HETATM 1788 O HOH A 466 6.075 11.822 8.679 1.00 42.77 O -ANISOU 1788 O HOH A 466 4834 5683 5734 296 383 29 O -HETATM 1789 O HOH A 467 5.246 13.135 6.100 1.00 40.13 O -ANISOU 1789 O HOH A 467 4475 5310 5462 312 270 -7 O -HETATM 1790 O HOH A 468 6.074 15.839 5.898 1.00 44.17 O -ANISOU 1790 O HOH A 468 5187 5731 5865 457 260 -119 O -HETATM 1791 O HOH A 469 18.837 16.360 14.070 1.00 51.86 O -ANISOU 1791 O HOH A 469 7062 6283 6360 174 51 -407 O -HETATM 1792 O HOH A 470 21.079 16.721 11.705 1.00 42.24 O -ANISOU 1792 O HOH A 470 5785 5018 5245 -14 -74 -374 O -HETATM 1793 O HOH A 471 19.360 26.734 4.653 1.00 38.27 O -ANISOU 1793 O HOH A 471 5697 4030 4815 -27 -481 -312 O -HETATM 1794 O HOH A 472 21.014 29.814 2.948 1.00 45.92 O -ANISOU 1794 O HOH A 472 6851 4776 5822 -229 -733 -173 O -HETATM 1795 O HOH A 473 29.197 22.458 3.463 1.00 33.41 O -ANISOU 1795 O HOH A 473 4463 3886 4344 -691 -502 136 O -HETATM 1796 O HOH A 474 21.754 30.124 -4.027 1.00 56.17 O -ANISOU 1796 O HOH A 474 7845 6321 7176 -446 -672 184 O -HETATM 1797 O HOH A 475 33.526 26.270 -5.737 1.00 41.14 O -ANISOU 1797 O HOH A 475 4985 5324 5322 -1107 -440 995 O -HETATM 1798 O HOH A 476 34.605 21.908 -5.498 1.00 54.32 O -ANISOU 1798 O HOH A 476 6391 7340 6910 -829 -154 865 O -HETATM 1799 O HOH A 477 34.248 17.861 -6.918 1.00 50.47 O -ANISOU 1799 O HOH A 477 5819 7098 6259 -443 124 673 O -HETATM 1800 O HOH A 478 40.018 25.653 -16.048 1.00 64.56 O -ANISOU 1800 O HOH A 478 7018 9704 7809 -954 308 2139 O -HETATM 1801 O HOH A 479 18.751 24.277 -30.227 1.00 40.11 O -ANISOU 1801 O HOH A 479 5939 5763 3538 372 -329 675 O -HETATM 1802 O HOH A 480 22.112 31.713 -18.224 1.00 44.51 O -ANISOU 1802 O HOH A 480 6193 5462 5258 -510 -520 959 O -HETATM 1803 O HOH A 481 10.861 24.107 -11.051 1.00 44.56 O -ANISOU 1803 O HOH A 481 5903 5355 5673 187 -475 -83 O -HETATM 1804 O HOH A 482 8.769 22.690 -7.558 1.00 36.94 O -ANISOU 1804 O HOH A 482 4768 4421 4847 290 -377 -174 O -HETATM 1805 O HOH A 483 13.486 27.549 -8.588 1.00 44.14 O -ANISOU 1805 O HOH A 483 6084 5068 5619 111 -490 -24 O -HETATM 1806 O HOH A 484 14.157 29.529 -7.336 1.00 55.74 O -ANISOU 1806 O HOH A 484 7713 6370 7098 99 -560 -8 O -HETATM 1807 O HOH A 485 10.374 27.035 -19.853 1.00 42.70 O -ANISOU 1807 O HOH A 485 5948 5193 5083 218 -770 207 O -HETATM 1808 O HOH A 486 8.076 24.726 -16.955 1.00 33.35 O -ANISOU 1808 O HOH A 486 4542 4013 4118 278 -745 20 O -HETATM 1809 O HOH A 487 15.055 18.114 -25.917 1.00 47.78 O -ANISOU 1809 O HOH A 487 6830 6381 4943 429 -580 -40 O -HETATM 1810 O HOH A 488 16.855 10.426 -21.030 1.00 39.11 O -ANISOU 1810 O HOH A 488 5654 5124 4084 477 -490 -474 O -HETATM 1811 O HOH A 489 19.371 9.221 -21.187 1.00 48.52 O -ANISOU 1811 O HOH A 489 6883 6432 5122 625 -327 -487 O -HETATM 1812 O HOH A 490 30.255 11.565 -3.865 1.00 38.76 O -ANISOU 1812 O HOH A 490 4612 5320 4795 -64 148 45 O -HETATM 1813 O HOH A 491 27.697 13.447 16.185 1.00 49.58 O -ANISOU 1813 O HOH A 491 6710 6009 6117 -247 -287 -262 O -HETATM 1814 O HOH A 492 29.994 14.145 15.207 1.00 39.15 O -ANISOU 1814 O HOH A 492 5309 4701 4866 -384 -411 -183 O -HETATM 1815 O HOH A 493 37.745 7.403 12.357 1.00 35.96 O -ANISOU 1815 O HOH A 493 4127 4844 4692 -320 -316 195 O -HETATM 1816 O HOH A 494 30.372 5.017 15.173 1.00 37.91 O -ANISOU 1816 O HOH A 494 4825 4760 4820 -168 -126 -110 O -HETATM 1817 O HOH A 495 46.573 -1.987 21.481 1.00 52.02 O -ANISOU 1817 O HOH A 495 5855 7144 6766 114 -783 617 O -HETATM 1818 O HOH A 496 42.673 -3.596 22.529 1.00 44.50 O -ANISOU 1818 O HOH A 496 5321 5887 5700 155 -650 410 O -HETATM 1819 O HOH A 497 44.469 -18.911 16.648 1.00 45.01 O -ANISOU 1819 O HOH A 497 5905 5325 5871 1701 -577 212 O -HETATM 1820 O HOH A 498 38.658 -19.896 4.429 1.00 51.27 O -ANISOU 1820 O HOH A 498 7504 5650 6325 2077 -458 -588 O -HETATM 1821 O HOH A 499 13.185 15.489 9.316 1.00 37.63 O -ANISOU 1821 O HOH A 499 4837 4658 4802 270 212 -309 O -HETATM 1822 O HOH A 500 35.627 26.594 -8.640 1.00 34.66 O -ANISOU 1822 O HOH A 500 3890 4843 4435 -1191 -302 1371 O -CONECT 1664 1665 -CONECT 1665 1664 1666 1685 -CONECT 1666 1665 1667 1696 -CONECT 1667 1666 1668 1678 1699 -CONECT 1668 1667 1669 1677 -CONECT 1669 1668 1670 1676 -CONECT 1670 1669 1671 1675 -CONECT 1671 1670 1672 1705 -CONECT 1672 1671 1673 1707 -CONECT 1673 1672 1674 1708 -CONECT 1674 1673 1675 1709 -CONECT 1675 1670 1674 1706 -CONECT 1676 1669 1702 1703 1704 -CONECT 1677 1668 -CONECT 1678 1667 1679 1700 1701 -CONECT 1679 1678 1680 1684 -CONECT 1680 1679 1681 1710 -CONECT 1681 1680 1682 1712 -CONECT 1682 1681 1683 1713 -CONECT 1683 1682 1684 1714 -CONECT 1684 1679 1683 1711 -CONECT 1685 1665 1686 1697 1698 -CONECT 1686 1685 1687 1694 -CONECT 1687 1686 1688 1692 -CONECT 1688 1687 1689 1715 -CONECT 1689 1688 1690 1716 -CONECT 1690 1689 1691 1717 -CONECT 1691 1690 1692 1718 -CONECT 1692 1687 1691 1693 -CONECT 1693 1692 1694 1719 -CONECT 1694 1686 1693 1695 -CONECT 1695 1694 1720 1721 1722 -CONECT 1696 1666 -CONECT 1697 1685 -CONECT 1698 1685 -CONECT 1699 1667 -CONECT 1700 1678 -CONECT 1701 1678 -CONECT 1702 1676 -CONECT 1703 1676 -CONECT 1704 1676 -CONECT 1705 1671 -CONECT 1706 1675 -CONECT 1707 1672 -CONECT 1708 1673 -CONECT 1709 1674 -CONECT 1710 1680 -CONECT 1711 1684 -CONECT 1712 1681 -CONECT 1713 1682 -CONECT 1714 1683 -CONECT 1715 1688 -CONECT 1716 1689 -CONECT 1717 1690 -CONECT 1718 1691 -CONECT 1719 1693 -CONECT 1720 1695 -CONECT 1721 1695 -CONECT 1722 1695 -MASTER 305 0 1 12 2 0 3 6 1794 1 59 18 -END |