diff options
Diffstat (limited to 'plip/test/pdb/4dst.pdb')
| -rw-r--r-- | plip/test/pdb/4dst.pdb | 3743 |
1 files changed, 0 insertions, 3743 deletions
diff --git a/plip/test/pdb/4dst.pdb b/plip/test/pdb/4dst.pdb deleted file mode 100644 index e9add49..0000000 --- a/plip/test/pdb/4dst.pdb +++ /dev/null @@ -1,3743 +0,0 @@ -HEADER HYDROLASE 19-FEB-12 4DST -TITLE SMALL-MOLECULE LIGANDS BIND TO A DISTINCT POCKET IN RAS AND INHIBIT -TITLE 2 SOS-MEDIATED NUCLEOTIDE EXCHANGE ACTIVITY -COMPND MOL_ID: 1; -COMPND 2 MOLECULE: GTPASE KRAS, ISOFORM 2B; -COMPND 3 CHAIN: A; -COMPND 4 SYNONYM: KRAS 4B, K-RAS 2, KI-RAS, C-K-RAS, C-KI-RAS, GTPASE KRAS, N- -COMPND 5 TERMINALLY PROCESSED; -COMPND 6 EC: 3.6.-.-; -COMPND 7 ENGINEERED: YES; -COMPND 8 MUTATION: YES -SOURCE MOL_ID: 1; -SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; -SOURCE 3 ORGANISM_COMMON: HUMAN; -SOURCE 4 ORGANISM_TAXID: 9606; -SOURCE 5 GENE: KRAS, KRAS2, RASK2; -SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI; -SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562 -KEYWDS SMALL G-PROTEIN, SIGNALING, HYDROLASE -EXPDTA X-RAY DIFFRACTION -AUTHOR A.OH,T.MAURER,L.S.GARRENTON,K.PITTS,D.J.ANDERSON,N.J.SKELTON, -AUTHOR 2 B.P.FAUBER,B.PAN,S.MALEK,D.STOKOE,M.LUDLAM,K.K.BOWMAN,J.WU, -AUTHOR 3 A.M.GIANNETTI,M.A.STAROVASNIK,I.MELLMAN,P.K.JACKSON,J.RULDOLPH, -AUTHOR 4 G.FANG,W.WANG -REVDAT 3 06-JUN-12 4DST 1 COMPND DBREF SEQADV REMARK -REVDAT 2 18-APR-12 4DST 1 JRNL -REVDAT 1 04-APR-12 4DST 0 -JRNL AUTH T.MAURER,L.S.GARRENTON,A.OH,K.PITTS,D.J.ANDERSON, -JRNL AUTH 2 N.J.SKELTON,B.P.FAUBER,B.PAN,S.MALEK,D.STOKOE,M.J.LUDLAM, -JRNL AUTH 3 K.K.BOWMAN,J.WU,A.M.GIANNETTI,M.A.STAROVASNIK,I.MELLMAN, -JRNL AUTH 4 P.K.JACKSON,J.RUDOLPH,W.WANG,G.FANG -JRNL TITL SMALL-MOLECULE LIGANDS BIND TO A DISTINCT POCKET IN RAS AND -JRNL TITL 2 INHIBIT SOS-MEDIATED NUCLEOTIDE EXCHANGE ACTIVITY. -JRNL REF PROC.NATL.ACAD.SCI.USA V. 109 5299 2012 -JRNL REFN ISSN 0027-8424 -JRNL PMID 22431598 -JRNL DOI 10.1073/PNAS.1116510109 -REMARK 2 -REMARK 2 RESOLUTION. 2.30 ANGSTROMS. -REMARK 3 -REMARK 3 REFINEMENT. -REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.6.4_486) -REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN -REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE- -REMARK 3 : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO, -REMARK 3 : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL -REMARK 3 : MORIARTY,REETAL PAI,RANDY READ,JANE -REMARK 3 : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM -REMARK 3 : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH, -REMARK 3 : LAURENT STORONI,TOM TERWILLIGER,PETER -REMARK 3 : ZWART -REMARK 3 -REMARK 3 REFINEMENT TARGET : ML -REMARK 3 -REMARK 3 DATA USED IN REFINEMENT. -REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30 -REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 25.79 -REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.970 -REMARK 3 COMPLETENESS FOR RANGE (%) : 94.4 -REMARK 3 NUMBER OF REFLECTIONS : 7716 -REMARK 3 -REMARK 3 FIT TO DATA USED IN REFINEMENT. -REMARK 3 R VALUE (WORKING + TEST SET) : 0.162 -REMARK 3 R VALUE (WORKING SET) : 0.159 -REMARK 3 FREE R VALUE : 0.209 -REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.090 -REMARK 3 FREE R VALUE TEST SET COUNT : 393 -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 25.7941 - 3.3102 1.00 2570 147 0.1597 0.2015 -REMARK 3 2 3.3102 - 2.6282 1.00 2567 134 0.1530 0.2053 -REMARK 3 3 2.3800 - 2.3000 0.84 2186 112 0.1691 0.2472 -REMARK 3 -REMARK 3 BULK SOLVENT MODELLING. -REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL -REMARK 3 SOLVENT RADIUS : 1.11 -REMARK 3 SHRINKAGE RADIUS : 0.90 -REMARK 3 K_SOL : 0.34 -REMARK 3 B_SOL : 46.26 -REMARK 3 -REMARK 3 ERROR ESTIMATES. -REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.220 -REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 19.950 -REMARK 3 -REMARK 3 B VALUES. -REMARK 3 FROM WILSON PLOT (A**2) : 35.70 -REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL -REMARK 3 OVERALL ANISOTROPIC B VALUE. -REMARK 3 B11 (A**2) : -3.55140 -REMARK 3 B22 (A**2) : -3.55140 -REMARK 3 B33 (A**2) : 7.10290 -REMARK 3 B12 (A**2) : -0.00000 -REMARK 3 B13 (A**2) : 0.00000 -REMARK 3 B23 (A**2) : -0.00000 -REMARK 3 -REMARK 3 TWINNING INFORMATION. -REMARK 3 FRACTION: NULL -REMARK 3 OPERATOR: NULL -REMARK 3 -REMARK 3 DEVIATIONS FROM IDEAL VALUES. -REMARK 3 RMSD COUNT -REMARK 3 BOND : 0.005 1520 -REMARK 3 ANGLE : 1.005 2058 -REMARK 3 CHIRALITY : 0.059 227 -REMARK 3 PLANARITY : 0.003 263 -REMARK 3 DIHEDRAL : 14.818 567 -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): 18.7262 9.8187 0.2962 -REMARK 3 T TENSOR -REMARK 3 T11: 0.1244 T22: 0.1504 -REMARK 3 T33: 0.1346 T12: -0.0101 -REMARK 3 T13: -0.0095 T23: -0.0133 -REMARK 3 L TENSOR -REMARK 3 L11: 1.2115 L22: 0.9535 -REMARK 3 L33: 1.1451 L12: 0.1333 -REMARK 3 L13: 0.2607 L23: -0.5664 -REMARK 3 S TENSOR -REMARK 3 S11: -0.0648 S12: -0.0179 S13: 0.1087 -REMARK 3 S21: 0.0390 S22: -0.0849 S23: -0.0407 -REMARK 3 S31: -0.0642 S32: 0.1230 S33: 0.0000 -REMARK 3 -REMARK 3 NCS DETAILS -REMARK 3 NUMBER OF NCS GROUPS : NULL -REMARK 3 -REMARK 3 OTHER REFINEMENT REMARKS: NULL -REMARK 4 -REMARK 4 4DST COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 -REMARK 100 -REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-FEB-12. -REMARK 100 THE RCSB ID CODE IS RCSB070737. -REMARK 200 -REMARK 200 EXPERIMENTAL DETAILS -REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION -REMARK 200 DATE OF DATA COLLECTION : 03-SEP-10 -REMARK 200 TEMPERATURE (KELVIN) : 93 -REMARK 200 PH : 8.5 -REMARK 200 NUMBER OF CRYSTALS USED : 1 -REMARK 200 -REMARK 200 SYNCHROTRON (Y/N) : Y -REMARK 200 RADIATION SOURCE : ALS -REMARK 200 BEAMLINE : 5.0.2 -REMARK 200 X-RAY GENERATOR MODEL : NULL -REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M -REMARK 200 WAVELENGTH OR RANGE (A) : 0.97740 -REMARK 200 MONOCHROMATOR : LIQUID NITROGEN COOLED DUAL -REMARK 200 CRYSTAL -REMARK 200 OPTICS : NULL -REMARK 200 -REMARK 200 DETECTOR TYPE : CCD -REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315 -REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000 -REMARK 200 DATA SCALING SOFTWARE : SCALEPACK -REMARK 200 -REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 8242 -REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300 -REMARK 200 RESOLUTION RANGE LOW (A) : 30.000 -REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000 -REMARK 200 -REMARK 200 OVERALL. -REMARK 200 COMPLETENESS FOR RANGE (%) : 94.5 -REMARK 200 DATA REDUNDANCY : 5.200 -REMARK 200 R MERGE (I) : NULL -REMARK 200 R SYM (I) : 0.09200 -REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 18.0000 -REMARK 200 -REMARK 200 IN THE HIGHEST RESOLUTION SHELL. -REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30 -REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.38 -REMARK 200 COMPLETENESS FOR SHELL (%) : 70.8 -REMARK 200 DATA REDUNDANCY IN SHELL : 3.30 -REMARK 200 R MERGE FOR SHELL (I) : NULL -REMARK 200 R SYM FOR SHELL (I) : 0.33200 -REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.000 -REMARK 200 -REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH -REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT -REMARK 200 SOFTWARE USED: PHASER -REMARK 200 STARTING MODEL: NULL -REMARK 200 -REMARK 200 REMARK: NULL -REMARK 280 -REMARK 280 CRYSTAL -REMARK 280 SOLVENT CONTENT, VS (%): 43.81 -REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.19 -REMARK 280 -REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 UL + 0.2 UL DROPS CONTAINING 40 -REMARK 280 MG/ML KRAS, 0.1 M TRISCL, 25% POLYETHYLENE GLYCOL 4000, 0.2 M -REMARK 280 NAOAC, 2% BENZAMIDINE-HCL, PH 8.5, VAPOR DIFFUSION, SITTING DROP, -REMARK 280 TEMPERATURE 277K -REMARK 290 -REMARK 290 CRYSTALLOGRAPHIC SYMMETRY -REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: H 3 -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+2/3,Y+1/3,Z+1/3 -REMARK 290 5555 -Y+2/3,X-Y+1/3,Z+1/3 -REMARK 290 6555 -X+Y+2/3,-X+1/3,Z+1/3 -REMARK 290 7555 X+1/3,Y+2/3,Z+2/3 -REMARK 290 8555 -Y+1/3,X-Y+2/3,Z+2/3 -REMARK 290 9555 -X+Y+1/3,-X+2/3,Z+2/3 -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 39.46150 -REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 22.78311 -REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 26.21033 -REMARK 290 SMTRY1 5 -0.500000 -0.866025 0.000000 39.46150 -REMARK 290 SMTRY2 5 0.866025 -0.500000 0.000000 22.78311 -REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 26.21033 -REMARK 290 SMTRY1 6 -0.500000 0.866025 0.000000 39.46150 -REMARK 290 SMTRY2 6 -0.866025 -0.500000 0.000000 22.78311 -REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 26.21033 -REMARK 290 SMTRY1 7 1.000000 0.000000 0.000000 0.00000 -REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 45.56622 -REMARK 290 SMTRY3 7 0.000000 0.000000 1.000000 52.42067 -REMARK 290 SMTRY1 8 -0.500000 -0.866025 0.000000 0.00000 -REMARK 290 SMTRY2 8 0.866025 -0.500000 0.000000 45.56622 -REMARK 290 SMTRY3 8 0.000000 0.000000 1.000000 52.42067 -REMARK 290 SMTRY1 9 -0.500000 0.866025 0.000000 0.00000 -REMARK 290 SMTRY2 9 -0.866025 -0.500000 0.000000 45.56622 -REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 52.42067 -REMARK 290 -REMARK 290 REMARK: NULL -REMARK 300 -REMARK 300 BIOMOLECULE: 1 -REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM -REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN -REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON -REMARK 300 BURIED SURFACE AREA. -REMARK 350 -REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN -REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE -REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS -REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND -REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. -REMARK 350 -REMARK 350 BIOMOLECULE: 1 -REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC -REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC -REMARK 350 SOFTWARE USED: PISA -REMARK 350 APPLY THE FOLLOWING TO CHAINS: A -REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 -REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 -REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 -REMARK 465 -REMARK 465 MISSING RESIDUES -REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE -REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN -REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) -REMARK 465 -REMARK 465 M RES C SSSEQI -REMARK 465 GLY A 0 -REMARK 465 SER A 181 -REMARK 465 LYS A 182 -REMARK 465 THR A 183 -REMARK 465 LYS A 184 -REMARK 465 CYS A 185 -REMARK 465 VAL A 186 -REMARK 465 ILE A 187 -REMARK 465 MET A 188 -REMARK 470 -REMARK 470 MISSING ATOM -REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; -REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; -REMARK 470 I=INSERTION CODE): -REMARK 470 M RES CSSEQI ATOMS -REMARK 470 LYS A 175 CG CD CE NZ -REMARK 470 LYS A 176 CG CD CE NZ -REMARK 470 LYS A 177 CG CD CE NZ -REMARK 470 LYS A 178 CG CD CE NZ -REMARK 470 LYS A 179 CG CD CE NZ -REMARK 470 LYS A 180 CG CD CE NZ -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 ILE A 36 -62.88 -92.11 -REMARK 500 GLU A 37 136.96 -171.00 -REMARK 500 SER A 122 33.71 -85.85 -REMARK 500 ARG A 149 7.62 80.40 -REMARK 500 LYS A 176 47.69 -100.90 -REMARK 500 LYS A 177 -110.27 166.72 -REMARK 500 LYS A 178 -20.90 -146.48 -REMARK 500 LYS A 179 111.62 127.22 -REMARK 500 -REMARK 500 REMARK: NULL -REMARK 620 -REMARK 620 METAL COORDINATION -REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; -REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE): -REMARK 620 -REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL -REMARK 620 MG A 203 MG -REMARK 620 N RES CSSEQI ATOM -REMARK 620 1 GCP A 202 O2B -REMARK 620 2 GCP A 202 O1G 92.5 -REMARK 620 3 SER A 17 OG 93.8 173.1 -REMARK 620 4 HOH A 302 O 86.3 98.2 79.5 -REMARK 620 5 HOH A 301 O 101.7 85.6 95.8 171.0 -REMARK 620 6 THR A 35 OG1 168.2 95.8 77.6 84.2 87.4 -REMARK 620 N 1 2 3 4 5 -REMARK 620 -REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL -REMARK 620 MG A 208 MG -REMARK 620 N RES CSSEQI ATOM -REMARK 620 1 TYR A 96 OH -REMARK 620 2 HOH A 305 O 104.8 -REMARK 620 3 HOH A 308 O 89.9 89.5 -REMARK 620 4 GLY A 60 O 92.2 163.0 91.2 -REMARK 620 5 GLY A 10 O 76.3 93.5 166.2 89.9 -REMARK 620 6 ALA A 59 O 175.4 79.2 92.3 83.8 101.5 -REMARK 620 N 1 2 3 4 5 -REMARK 800 -REMARK 800 SITE -REMARK 800 SITE_IDENTIFIER: AC1 -REMARK 800 EVIDENCE_CODE: SOFTWARE -REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 9LI A 201 -REMARK 800 -REMARK 800 SITE_IDENTIFIER: AC2 -REMARK 800 EVIDENCE_CODE: SOFTWARE -REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GCP A 202 -REMARK 800 -REMARK 800 SITE_IDENTIFIER: AC3 -REMARK 800 EVIDENCE_CODE: SOFTWARE -REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 203 -REMARK 800 -REMARK 800 SITE_IDENTIFIER: AC4 -REMARK 800 EVIDENCE_CODE: SOFTWARE -REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 204 -REMARK 800 -REMARK 800 SITE_IDENTIFIER: AC5 -REMARK 800 EVIDENCE_CODE: SOFTWARE -REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 205 -REMARK 800 -REMARK 800 SITE_IDENTIFIER: AC6 -REMARK 800 EVIDENCE_CODE: SOFTWARE -REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS A 206 -REMARK 800 -REMARK 800 SITE_IDENTIFIER: AC7 -REMARK 800 EVIDENCE_CODE: SOFTWARE -REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A 207 -REMARK 800 -REMARK 800 SITE_IDENTIFIER: AC8 -REMARK 800 EVIDENCE_CODE: SOFTWARE -REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 208 -REMARK 900 -REMARK 900 RELATED ENTRIES -REMARK 900 RELATED ID: 4DSN RELATED DB: PDB -REMARK 900 RELATED ID: 4DSO RELATED DB: PDB -REMARK 900 RELATED ID: 4DSU RELATED DB: PDB -REMARK 999 -REMARK 999 SEQUENCE -REMARK 999 THE SEQUENCE MATCHES UNIPROT ENTRY P01116, ISOFORM 2B WITH -REMARK 999 IDENTIFIER P01116-2. -DBREF 4DST A 2 188 UNP P01116 RASK_HUMAN 2 188 -SEQADV 4DST GLY A 0 UNP P01116 EXPRESSION TAG -SEQADV 4DST SER A 1 UNP P01116 EXPRESSION TAG -SEQADV 4DST ASP A 12 UNP P01116 GLY 12 ENGINEERED MUTATION -SEQRES 1 A 189 GLY SER THR GLU TYR LYS LEU VAL VAL VAL GLY ALA ASP -SEQRES 2 A 189 GLY VAL GLY LYS SER ALA LEU THR ILE GLN LEU ILE GLN -SEQRES 3 A 189 ASN HIS PHE VAL ASP GLU TYR ASP PRO THR ILE GLU ASP -SEQRES 4 A 189 SER TYR ARG LYS GLN VAL VAL ILE ASP GLY GLU THR CYS -SEQRES 5 A 189 LEU LEU ASP ILE LEU ASP THR ALA GLY GLN GLU GLU TYR -SEQRES 6 A 189 SER ALA MET ARG ASP GLN TYR MET ARG THR GLY GLU GLY -SEQRES 7 A 189 PHE LEU CYS VAL PHE ALA ILE ASN ASN THR LYS SER PHE -SEQRES 8 A 189 GLU ASP ILE HIS HIS TYR ARG GLU GLN ILE LYS ARG VAL -SEQRES 9 A 189 LYS ASP SER GLU ASP VAL PRO MET VAL LEU VAL GLY ASN -SEQRES 10 A 189 LYS CYS ASP LEU PRO SER ARG THR VAL ASP THR LYS GLN -SEQRES 11 A 189 ALA GLN ASP LEU ALA ARG SER TYR GLY ILE PRO PHE ILE -SEQRES 12 A 189 GLU THR SER ALA LYS THR ARG GLN GLY VAL ASP ASP ALA -SEQRES 13 A 189 PHE TYR THR LEU VAL ARG GLU ILE ARG LYS HIS LYS GLU -SEQRES 14 A 189 LYS MET SER LYS ASP GLY LYS LYS LYS LYS LYS LYS SER -SEQRES 15 A 189 LYS THR LYS CYS VAL ILE MET -HET 9LI A 201 15 -HET GCP A 202 32 -HET MG A 203 1 -HET GOL A 204 6 -HET EDO A 205 4 -HET DMS A 206 4 -HET ACT A 207 4 -HET MG A 208 1 -HETNAM 9LI 2-(4,6-DICHLORO-2-METHYL-1H-INDOL-3-YL)ETHANAMINE -HETNAM GCP PHOSPHOMETHYLPHOSPHONIC ACID GUANYLATE ESTER -HETNAM MG MAGNESIUM ION -HETNAM GOL GLYCEROL -HETNAM EDO 1,2-ETHANEDIOL -HETNAM DMS DIMETHYL SULFOXIDE -HETNAM ACT ACETATE ION -HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL -HETSYN EDO ETHYLENE GLYCOL -FORMUL 2 9LI C11 H12 CL2 N2 -FORMUL 3 GCP C11 H18 N5 O13 P3 -FORMUL 4 MG 2(MG 2+) -FORMUL 5 GOL C3 H8 O3 -FORMUL 6 EDO C2 H6 O2 -FORMUL 7 DMS C2 H6 O S -FORMUL 8 ACT C2 H3 O2 1- -FORMUL 10 HOH *90(H2 O) -HELIX 1 1 GLY A 15 ASN A 26 1 12 -HELIX 2 2 TYR A 64 GLY A 75 1 12 -HELIX 3 3 ASN A 86 ASP A 105 1 20 -HELIX 4 4 ASP A 126 GLY A 138 1 13 -HELIX 5 5 GLY A 151 ASP A 173 1 23 -SHEET 1 A 6 GLU A 37 ILE A 46 0 -SHEET 2 A 6 GLU A 49 THR A 58 -1 O CYS A 51 N VAL A 44 -SHEET 3 A 6 THR A 2 GLY A 10 1 N TYR A 4 O ASP A 54 -SHEET 4 A 6 GLY A 77 ALA A 83 1 O VAL A 81 N VAL A 9 -SHEET 5 A 6 MET A 111 ASN A 116 1 O ASN A 116 N PHE A 82 -SHEET 6 A 6 PHE A 141 GLU A 143 1 O ILE A 142 N LEU A 113 -LINK O2B GCP A 202 MG MG A 203 1555 1555 2.17 -LINK O1G GCP A 202 MG MG A 203 1555 1555 2.19 -LINK OG SER A 17 MG MG A 203 1555 1555 2.28 -LINK MG MG A 203 O HOH A 302 1555 1555 2.32 -LINK MG MG A 203 O HOH A 301 1555 1555 2.34 -LINK OH TYR A 96 MG MG A 208 1555 1555 2.44 -LINK OG1 THR A 35 MG MG A 203 1555 1555 2.45 -LINK MG MG A 208 O HOH A 305 1555 1555 2.53 -LINK MG MG A 208 O HOH A 308 1555 1555 2.54 -LINK O GLY A 60 MG MG A 208 1555 1555 2.60 -LINK O GLY A 10 MG MG A 208 1555 1555 2.62 -LINK O ALA A 59 MG MG A 208 1555 1555 2.67 -CISPEP 1 ASP A 173 GLY A 174 0 -0.44 -CISPEP 2 LYS A 177 LYS A 178 0 1.72 -SITE 1 AC1 11 LYS A 5 VAL A 7 SER A 39 LEU A 56 -SITE 2 AC1 11 THR A 74 GLY A 75 CYS A 118 ASP A 119 -SITE 3 AC1 11 LEU A 120 ARG A 123 HOH A 376 -SITE 1 AC2 27 ASP A 12 GLY A 13 VAL A 14 GLY A 15 -SITE 2 AC2 27 LYS A 16 SER A 17 ALA A 18 PHE A 28 -SITE 3 AC2 27 VAL A 29 ASP A 30 GLU A 31 TYR A 32 -SITE 4 AC2 27 PRO A 34 THR A 35 GLY A 60 ASN A 116 -SITE 5 AC2 27 LYS A 117 ASP A 119 LEU A 120 SER A 145 -SITE 6 AC2 27 ALA A 146 MG A 203 HOH A 301 HOH A 302 -SITE 7 AC2 27 HOH A 303 HOH A 310 HOH A 342 -SITE 1 AC3 5 SER A 17 THR A 35 GCP A 202 HOH A 301 -SITE 2 AC3 5 HOH A 302 -SITE 1 AC4 3 ASP A 92 TYR A 96 GLN A 99 -SITE 1 AC5 4 LYS A 101 ARG A 102 ASP A 105 SER A 106 -SITE 1 AC6 5 ASP A 33 ILE A 36 GLU A 37 ASP A 38 -SITE 2 AC6 5 HOH A 339 -SITE 1 AC7 3 ARG A 97 VAL A 109 GLY A 138 -SITE 1 AC8 6 GLY A 10 ALA A 59 GLY A 60 TYR A 96 -SITE 2 AC8 6 HOH A 305 HOH A 308 -CRYST1 78.923 78.923 78.631 90.00 90.00 120.00 H 3 9 -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 0.012671 0.007315 0.000000 0.00000 -SCALE2 0.000000 0.014631 0.000000 0.00000 -SCALE3 0.000000 0.000000 0.012718 0.00000 -ATOM 1 N SER A 1 38.831 18.260 0.753 1.00 95.57 N -ANISOU 1 N SER A 1 10900 12964 12449 -1114 -926 1477 N -ATOM 2 CA SER A 1 38.659 19.544 1.423 1.00 95.43 C -ANISOU 2 CA SER A 1 10964 12837 12459 -1244 -1073 1440 C -ATOM 3 C SER A 1 37.224 19.770 1.888 1.00 88.42 C -ANISOU 3 C SER A 1 10243 11811 11543 -1209 -1080 1253 C -ATOM 4 O SER A 1 36.966 19.896 3.085 1.00 93.99 O -ANISOU 4 O SER A 1 11027 12459 12225 -1241 -1151 1167 O -ATOM 5 CB SER A 1 39.080 20.695 0.506 1.00100.74 C -ANISOU 5 CB SER A 1 11592 13498 13189 -1341 -1130 1547 C -ATOM 6 OG SER A 1 40.426 20.558 0.091 1.00106.40 O -ANISOU 6 OG SER A 1 12143 14351 13933 -1381 -1125 1730 O -ATOM 7 N THR A 2 36.294 19.824 0.939 1.00 72.50 N -ANISOU 7 N THR A 2 8275 9747 9524 -1142 -1007 1196 N -ATOM 8 CA THR A 2 34.925 20.234 1.245 1.00 58.63 C -ANISOU 8 CA THR A 2 6663 7857 7755 -1117 -1020 1036 C -ATOM 9 C THR A 2 34.093 19.155 1.936 1.00 48.59 C -ANISOU 9 C THR A 2 5455 6582 6424 -1012 -945 911 C -ATOM 10 O THR A 2 34.149 17.973 1.586 1.00 39.37 O -ANISOU 10 O THR A 2 4236 5497 5227 -919 -838 928 O -ATOM 11 CB THR A 2 34.173 20.737 -0.011 1.00 53.78 C -ANISOU 11 CB THR A 2 6077 7193 7164 -1090 -980 1027 C -ATOM 12 OG1 THR A 2 34.938 21.764 -0.654 1.00 54.72 O -ANISOU 12 OG1 THR A 2 6137 7316 7339 -1194 -1053 1155 O -ATOM 13 CG2 THR A 2 32.806 21.296 0.373 1.00 46.56 C -ANISOU 13 CG2 THR A 2 5303 6137 6251 -1070 -1008 874 C -ATOM 14 N GLU A 3 33.311 19.589 2.915 1.00 50.17 N -ANISOU 14 N GLU A 3 5770 6683 6608 -1029 -1001 785 N -ATOM 15 CA GLU A 3 32.459 18.699 3.682 1.00 51.17 C -ANISOU 15 CA GLU A 3 5962 6801 6678 -944 -941 668 C -ATOM 16 C GLU A 3 31.001 18.772 3.209 1.00 49.57 C -ANISOU 16 C GLU A 3 5846 6517 6472 -869 -881 552 C -ATOM 17 O GLU A 3 30.443 19.860 3.038 1.00 50.36 O -ANISOU 17 O GLU A 3 6012 6517 6606 -904 -936 505 O -ATOM 18 CB GLU A 3 32.561 19.059 5.162 1.00 57.37 C -ANISOU 18 CB GLU A 3 6813 7550 7434 -1007 -1036 606 C -ATOM 19 CG GLU A 3 31.520 18.398 6.036 1.00 67.09 C -ANISOU 19 CG GLU A 3 8130 8758 8604 -932 -985 473 C -ATOM 20 CD GLU A 3 31.422 19.047 7.400 1.00 74.96 C -ANISOU 20 CD GLU A 3 9218 9699 9565 -999 -1083 389 C -ATOM 21 OE1 GLU A 3 32.404 19.704 7.815 1.00 77.04 O -ANISOU 21 OE1 GLU A 3 9462 9968 9842 -1106 -1191 451 O -ATOM 22 OE2 GLU A 3 30.362 18.908 8.050 1.00 75.86 O -ANISOU 22 OE2 GLU A 3 9424 9768 9634 -947 -1051 262 O -ATOM 23 N TYR A 4 30.395 17.607 2.995 1.00 44.05 N -ANISOU 23 N TYR A 4 5144 5857 5737 -766 -773 512 N -ATOM 24 CA TYR A 4 28.989 17.527 2.608 1.00 36.48 C -ANISOU 24 CA TYR A 4 4258 4834 4771 -694 -716 408 C -ATOM 25 C TYR A 4 28.191 16.737 3.630 1.00 33.87 C -ANISOU 25 C TYR A 4 3985 4497 4389 -636 -676 304 C -ATOM 26 O TYR A 4 28.604 15.656 4.050 1.00 35.06 O -ANISOU 26 O TYR A 4 4096 4719 4505 -603 -633 330 O -ATOM 27 CB TYR A 4 28.839 16.860 1.241 1.00 33.00 C -ANISOU 27 CB TYR A 4 3765 4441 4331 -629 -622 454 C -ATOM 28 CG TYR A 4 29.495 17.619 0.124 1.00 32.23 C -ANISOU 28 CG TYR A 4 3611 4360 4275 -679 -648 558 C -ATOM 29 CD1 TYR A 4 28.779 18.537 -0.627 1.00 33.99 C -ANISOU 29 CD1 TYR A 4 3875 4508 4531 -694 -671 539 C -ATOM 30 CD2 TYR A 4 30.837 17.424 -0.178 1.00 34.08 C -ANISOU 30 CD2 TYR A 4 3744 4688 4517 -712 -649 685 C -ATOM 31 CE1 TYR A 4 29.381 19.246 -1.655 1.00 35.83 C -ANISOU 31 CE1 TYR A 4 4054 4760 4799 -746 -698 646 C -ATOM 32 CE2 TYR A 4 31.445 18.120 -1.202 1.00 36.42 C -ANISOU 32 CE2 TYR A 4 3980 5010 4847 -762 -669 791 C -ATOM 33 CZ TYR A 4 30.714 19.032 -1.938 1.00 36.43 C -ANISOU 33 CZ TYR A 4 4029 4937 4877 -782 -694 772 C -ATOM 34 OH TYR A 4 31.320 19.729 -2.957 1.00 38.99 O -ANISOU 34 OH TYR A 4 4293 5291 5232 -838 -716 889 O -ATOM 35 N LYS A 5 27.040 17.275 4.015 1.00 32.82 N -ANISOU 35 N LYS A 5 3940 4276 4252 -620 -687 192 N -ATOM 36 CA LYS A 5 26.147 16.598 4.949 1.00 32.77 C -ANISOU 36 CA LYS A 5 3989 4266 4195 -565 -643 94 C -ATOM 37 C LYS A 5 25.021 15.889 4.195 1.00 32.17 C -ANISOU 37 C LYS A 5 3919 4186 4118 -478 -550 53 C -ATOM 38 O LYS A 5 24.096 16.530 3.701 1.00 32.30 O -ANISOU 38 O LYS A 5 3975 4135 4162 -461 -549 3 O -ATOM 39 CB LYS A 5 25.555 17.600 5.940 1.00 35.07 C -ANISOU 39 CB LYS A 5 4373 4474 4477 -594 -707 -9 C -ATOM 40 CG LYS A 5 26.579 18.406 6.718 1.00 40.19 C -ANISOU 40 CG LYS A 5 5035 5112 5124 -691 -815 17 C -ATOM 41 CD LYS A 5 25.889 19.427 7.614 1.00 47.77 C -ANISOU 41 CD LYS A 5 6104 5976 6071 -710 -872 -104 C -ATOM 42 CE LYS A 5 26.893 20.266 8.393 1.00 54.69 C -ANISOU 42 CE LYS A 5 7008 6831 6942 -816 -991 -87 C -ATOM 43 NZ LYS A 5 27.742 19.434 9.293 1.00 56.98 N -ANISOU 43 NZ LYS A 5 7259 7222 7167 -846 -1004 -42 N -ATOM 44 N LEU A 6 25.103 14.565 4.102 1.00 30.48 N -ANISOU 44 N LEU A 6 3667 4040 3875 -427 -477 78 N -ATOM 45 CA LEU A 6 24.076 13.795 3.409 1.00 25.08 C -ANISOU 45 CA LEU A 6 2991 3351 3186 -354 -395 42 C -ATOM 46 C LEU A 6 23.176 13.093 4.416 1.00 25.65 C -ANISOU 46 C LEU A 6 3106 3423 3218 -314 -359 -36 C -ATOM 47 O LEU A 6 23.654 12.517 5.396 1.00 28.24 O -ANISOU 47 O LEU A 6 3427 3792 3509 -321 -362 -25 O -ATOM 48 CB LEU A 6 24.707 12.767 2.460 1.00 22.65 C -ANISOU 48 CB LEU A 6 2619 3109 2878 -319 -334 119 C -ATOM 49 CG LEU A 6 25.958 13.175 1.676 1.00 26.40 C -ANISOU 49 CG LEU A 6 3028 3626 3379 -358 -358 223 C -ATOM 50 CD1 LEU A 6 26.251 12.171 0.574 1.00 28.39 C -ANISOU 50 CD1 LEU A 6 3232 3933 3623 -301 -277 273 C -ATOM 51 CD2 LEU A 6 25.830 14.565 1.090 1.00 24.75 C -ANISOU 51 CD2 LEU A 6 2834 3362 3208 -410 -418 230 C -ATOM 52 N VAL A 7 21.870 13.156 4.176 1.00 25.07 N -ANISOU 52 N VAL A 7 3070 3305 3150 -275 -326 -106 N -ATOM 53 CA VAL A 7 20.892 12.476 5.018 1.00 18.48 C -ANISOU 53 CA VAL A 7 2267 2476 2280 -236 -283 -172 C -ATOM 54 C VAL A 7 20.111 11.442 4.200 1.00 18.68 C -ANISOU 54 C VAL A 7 2277 2511 2309 -183 -212 -172 C -ATOM 55 O VAL A 7 19.497 11.775 3.188 1.00 17.15 O -ANISOU 55 O VAL A 7 2085 2285 2147 -170 -204 -180 O -ATOM 56 CB VAL A 7 19.899 13.478 5.646 1.00 18.83 C -ANISOU 56 CB VAL A 7 2369 2461 2324 -233 -307 -262 C -ATOM 57 CG1 VAL A 7 18.858 12.739 6.493 1.00 19.39 C -ANISOU 57 CG1 VAL A 7 2462 2553 2354 -191 -252 -320 C -ATOM 58 CG2 VAL A 7 20.641 14.534 6.490 1.00 13.65 C -ANISOU 58 CG2 VAL A 7 1746 1782 1659 -290 -385 -276 C -ATOM 59 N VAL A 8 20.136 10.188 4.643 1.00 20.54 N -ANISOU 59 N VAL A 8 2501 2787 2515 -159 -168 -159 N -ATOM 60 CA VAL A 8 19.406 9.121 3.962 1.00 21.97 C -ANISOU 60 CA VAL A 8 2677 2970 2700 -116 -108 -162 C -ATOM 61 C VAL A 8 18.045 8.911 4.626 1.00 22.49 C -ANISOU 61 C VAL A 8 2772 3023 2752 -97 -82 -226 C -ATOM 62 O VAL A 8 17.979 8.563 5.811 1.00 20.20 O -ANISOU 62 O VAL A 8 2492 2758 2426 -99 -76 -239 O -ATOM 63 CB VAL A 8 20.221 7.810 3.960 1.00 21.76 C -ANISOU 63 CB VAL A 8 2622 2985 2660 -98 -73 -104 C -ATOM 64 CG1 VAL A 8 19.470 6.708 3.239 1.00 16.80 C -ANISOU 64 CG1 VAL A 8 2002 2345 2038 -59 -19 -115 C -ATOM 65 CG2 VAL A 8 21.618 8.049 3.328 1.00 11.62 C -ANISOU 65 CG2 VAL A 8 1296 1728 1392 -111 -92 -33 C -ATOM 66 N VAL A 9 16.966 9.140 3.868 1.00 15.68 N -ANISOU 66 N VAL A 9 1917 2128 1914 -79 -69 -258 N -ATOM 67 CA VAL A 9 15.614 9.065 4.418 1.00 13.34 C -ANISOU 67 CA VAL A 9 1634 1823 1612 -60 -44 -312 C -ATOM 68 C VAL A 9 14.721 8.104 3.625 1.00 14.65 C -ANISOU 68 C VAL A 9 1789 1986 1792 -41 -5 -306 C -ATOM 69 O VAL A 9 15.015 7.774 2.480 1.00 15.61 O -ANISOU 69 O VAL A 9 1904 2100 1928 -41 -4 -277 O -ATOM 70 CB VAL A 9 14.937 10.467 4.493 1.00 22.91 C -ANISOU 70 CB VAL A 9 2863 2993 2848 -56 -72 -364 C -ATOM 71 CG1 VAL A 9 15.799 11.447 5.278 1.00 23.59 C -ANISOU 71 CG1 VAL A 9 2973 3069 2920 -82 -120 -377 C -ATOM 72 CG2 VAL A 9 14.658 11.015 3.095 1.00 19.26 C -ANISOU 72 CG2 VAL A 9 2391 2494 2433 -55 -91 -349 C -ATOM 73 N GLY A 10 13.631 7.657 4.245 1.00 16.29 N -ANISOU 73 N GLY A 10 1996 2205 1990 -28 24 -333 N -ATOM 74 CA GLY A 10 12.708 6.729 3.608 1.00 19.03 C -ANISOU 74 CA GLY A 10 2333 2548 2352 -22 52 -326 C -ATOM 75 C GLY A 10 11.985 5.838 4.604 1.00 21.09 C -ANISOU 75 C GLY A 10 2586 2837 2591 -20 87 -327 C -ATOM 76 O GLY A 10 12.353 5.782 5.776 1.00 23.83 O -ANISOU 76 O GLY A 10 2939 3215 2902 -21 95 -328 O -ATOM 77 N ALA A 11 10.958 5.133 4.135 1.00 23.45 N -ANISOU 77 N ALA A 11 2873 3131 2909 -22 105 -322 N -ATOM 78 CA ALA A 11 10.139 4.276 4.993 1.00 22.92 C -ANISOU 78 CA ALA A 11 2790 3092 2827 -28 137 -312 C -ATOM 79 C ALA A 11 10.923 3.107 5.598 1.00 23.32 C -ANISOU 79 C ALA A 11 2853 3155 2853 -39 151 -271 C -ATOM 80 O ALA A 11 12.104 2.912 5.306 1.00 22.99 O -ANISOU 80 O ALA A 11 2829 3100 2807 -36 138 -252 O -ATOM 81 CB ALA A 11 8.919 3.750 4.211 1.00 21.73 C -ANISOU 81 CB ALA A 11 2619 2927 2710 -41 141 -305 C -ATOM 82 N ASP A 12 10.246 2.339 6.446 1.00 21.34 N -ANISOU 82 N ASP A 12 2588 2933 2587 -50 178 -251 N -ATOM 83 CA ASP A 12 10.799 1.133 7.044 1.00 22.87 C -ANISOU 83 CA ASP A 12 2791 3134 2765 -62 189 -201 C -ATOM 84 C ASP A 12 11.186 0.138 5.974 1.00 22.77 C -ANISOU 84 C ASP A 12 2800 3065 2788 -66 180 -178 C -ATOM 85 O ASP A 12 10.371 -0.210 5.124 1.00 24.12 O -ANISOU 85 O ASP A 12 2972 3205 2988 -79 176 -186 O -ATOM 86 CB ASP A 12 9.738 0.441 7.913 1.00 28.37 C -ANISOU 86 CB ASP A 12 3463 3867 3450 -82 217 -174 C -ATOM 87 CG ASP A 12 9.490 1.149 9.225 1.00 34.34 C -ANISOU 87 CG ASP A 12 4204 4692 4152 -73 239 -191 C -ATOM 88 OD1 ASP A 12 8.313 1.439 9.520 1.00 37.62 O -ANISOU 88 OD1 ASP A 12 4588 5140 4564 -71 265 -206 O -ATOM 89 OD2 ASP A 12 10.462 1.391 9.974 1.00 37.25 O -ANISOU 89 OD2 ASP A 12 4590 5086 4478 -69 230 -187 O -ATOM 90 N GLY A 13 12.414 -0.354 6.036 1.00 23.21 N -ANISOU 90 N GLY A 13 2871 3109 2838 -53 176 -148 N -ATOM 91 CA GLY A 13 12.780 -1.539 5.287 1.00 24.50 C -ANISOU 91 CA GLY A 13 3060 3218 3030 -47 179 -124 C -ATOM 92 C GLY A 13 13.174 -1.346 3.839 1.00 25.68 C -ANISOU 92 C GLY A 13 3232 3328 3198 -30 170 -152 C -ATOM 93 O GLY A 13 13.409 -2.329 3.129 1.00 27.48 O -ANISOU 93 O GLY A 13 3490 3506 3444 -20 177 -146 O -ATOM 94 N VAL A 14 13.250 -0.097 3.389 1.00 19.33 N -ANISOU 94 N VAL A 14 2417 2543 2386 -26 156 -184 N -ATOM 95 CA VAL A 14 13.580 0.166 1.988 1.00 21.58 C -ANISOU 95 CA VAL A 14 2719 2802 2678 -14 148 -204 C -ATOM 96 C VAL A 14 15.059 -0.096 1.655 1.00 20.61 C -ANISOU 96 C VAL A 14 2603 2677 2551 19 159 -178 C -ATOM 97 O VAL A 14 15.416 -0.249 0.488 1.00 21.80 O -ANISOU 97 O VAL A 14 2774 2808 2701 35 166 -189 O -ATOM 98 CB VAL A 14 13.151 1.587 1.546 1.00 20.31 C -ANISOU 98 CB VAL A 14 2542 2658 2518 -23 125 -234 C -ATOM 99 CG1 VAL A 14 11.657 1.770 1.747 1.00 17.89 C -ANISOU 99 CG1 VAL A 14 2221 2354 2224 -45 119 -255 C -ATOM 100 CG2 VAL A 14 13.933 2.655 2.305 1.00 14.57 C -ANISOU 100 CG2 VAL A 14 1795 1964 1778 -17 113 -229 C -ATOM 101 N GLY A 15 15.913 -0.153 2.676 1.00 21.87 N -ANISOU 101 N GLY A 15 2742 2865 2702 29 163 -141 N -ATOM 102 CA GLY A 15 17.321 -0.466 2.472 1.00 20.67 C -ANISOU 102 CA GLY A 15 2582 2720 2553 63 175 -104 C -ATOM 103 C GLY A 15 18.256 0.711 2.691 1.00 20.78 C -ANISOU 103 C GLY A 15 2561 2780 2555 59 153 -85 C -ATOM 104 O GLY A 15 19.348 0.768 2.118 1.00 20.77 O -ANISOU 104 O GLY A 15 2542 2792 2557 83 161 -56 O -ATOM 105 N LYS A 16 17.831 1.658 3.518 1.00 18.30 N -ANISOU 105 N LYS A 16 2237 2491 2226 28 126 -102 N -ATOM 106 CA LYS A 16 18.648 2.826 3.802 1.00 22.47 C -ANISOU 106 CA LYS A 16 2741 3053 2744 12 93 -90 C -ATOM 107 C LYS A 16 20.021 2.422 4.353 1.00 28.69 C -ANISOU 107 C LYS A 16 3499 3874 3529 23 90 -26 C -ATOM 108 O LYS A 16 21.057 2.918 3.907 1.00 26.36 O -ANISOU 108 O LYS A 16 3175 3599 3241 25 77 7 O -ATOM 109 CB LYS A 16 17.924 3.744 4.787 1.00 19.71 C -ANISOU 109 CB LYS A 16 2399 2717 2375 -18 67 -128 C -ATOM 110 CG LYS A 16 16.588 4.276 4.270 1.00 19.73 C -ANISOU 110 CG LYS A 16 2417 2691 2389 -22 69 -184 C -ATOM 111 CD LYS A 16 15.963 5.284 5.234 1.00 17.35 C -ANISOU 111 CD LYS A 16 2121 2401 2069 -38 51 -226 C -ATOM 112 CE LYS A 16 15.573 4.633 6.556 1.00 18.06 C -ANISOU 112 CE LYS A 16 2214 2524 2125 -41 70 -223 C -ATOM 113 NZ LYS A 16 14.474 3.654 6.414 1.00 16.15 N -ANISOU 113 NZ LYS A 16 1970 2272 1893 -34 106 -223 N -ATOM 114 N SER A 17 20.025 1.508 5.315 1.00 27.57 N -ANISOU 114 N SER A 17 3357 3740 3379 28 99 2 N -ATOM 115 CA SER A 17 21.271 1.080 5.938 1.00 26.21 C -ANISOU 115 CA SER A 17 3151 3603 3206 39 90 73 C -ATOM 116 C SER A 17 22.150 0.274 4.995 1.00 26.05 C -ANISOU 116 C SER A 17 3111 3567 3219 91 124 114 C -ATOM 117 O SER A 17 23.362 0.470 4.948 1.00 34.37 O -ANISOU 117 O SER A 17 4119 4657 4281 102 115 170 O -ATOM 118 CB SER A 17 20.984 0.265 7.198 1.00 26.25 C -ANISOU 118 CB SER A 17 3161 3621 3193 31 91 100 C -ATOM 119 OG SER A 17 20.533 1.102 8.245 1.00 24.36 O -ANISOU 119 OG SER A 17 2931 3418 2908 -12 59 72 O -ATOM 120 N ALA A 18 21.538 -0.640 4.252 1.00 24.93 N -ANISOU 120 N ALA A 18 3003 3373 3095 122 164 87 N -ATOM 121 CA ALA A 18 22.277 -1.499 3.339 1.00 24.76 C -ANISOU 121 CA ALA A 18 2979 3329 3101 182 205 111 C -ATOM 122 C ALA A 18 23.021 -0.680 2.284 1.00 23.07 C -ANISOU 122 C ALA A 18 2738 3144 2884 194 211 114 C -ATOM 123 O ALA A 18 24.157 -0.987 1.939 1.00 24.07 O -ANISOU 123 O ALA A 18 2826 3294 3026 239 236 165 O -ATOM 124 CB ALA A 18 21.336 -2.507 2.680 1.00 23.69 C -ANISOU 124 CB ALA A 18 2901 3122 2978 202 236 64 C -ATOM 125 N LEU A 19 22.370 0.364 1.777 1.00 20.25 N -ANISOU 125 N LEU A 19 2395 2789 2509 155 190 67 N -ATOM 126 CA LEU A 19 22.978 1.249 0.789 1.00 20.96 C -ANISOU 126 CA LEU A 19 2460 2909 2593 154 190 77 C -ATOM 127 C LEU A 19 24.180 1.957 1.385 1.00 24.27 C -ANISOU 127 C LEU A 19 2816 3387 3018 135 158 145 C -ATOM 128 O LEU A 19 25.264 1.988 0.802 1.00 27.49 O -ANISOU 128 O LEU A 19 3178 3834 3435 162 178 199 O -ATOM 129 CB LEU A 19 21.970 2.311 0.333 1.00 19.75 C -ANISOU 129 CB LEU A 19 2334 2742 2428 108 160 22 C -ATOM 130 CG LEU A 19 20.835 1.886 -0.601 1.00 24.91 C -ANISOU 130 CG LEU A 19 3040 3350 3073 116 181 -38 C -ATOM 131 CD1 LEU A 19 19.820 3.006 -0.701 1.00 23.13 C -ANISOU 131 CD1 LEU A 19 2828 3116 2846 70 141 -77 C -ATOM 132 CD2 LEU A 19 21.394 1.530 -1.983 1.00 24.39 C -ANISOU 132 CD2 LEU A 19 2981 3291 2995 156 222 -32 C -ATOM 133 N THR A 20 23.955 2.561 2.544 1.00 22.26 N -ANISOU 133 N THR A 20 2559 3143 2755 86 108 143 N -ATOM 134 CA THR A 20 24.984 3.311 3.229 1.00 24.35 C -ANISOU 134 CA THR A 20 2773 3459 3020 50 60 201 C -ATOM 135 C THR A 20 26.173 2.405 3.514 1.00 25.64 C -ANISOU 135 C THR A 20 2883 3659 3201 92 81 284 C -ATOM 136 O THR A 20 27.301 2.765 3.229 1.00 24.14 O -ANISOU 136 O THR A 20 2631 3516 3024 92 73 350 O -ATOM 137 CB THR A 20 24.445 3.875 4.550 1.00 27.75 C -ANISOU 137 CB THR A 20 3228 3889 3426 -3 8 172 C -ATOM 138 OG1 THR A 20 23.258 4.638 4.292 1.00 25.07 O -ANISOU 138 OG1 THR A 20 2936 3511 3077 -27 -2 93 O -ATOM 139 CG2 THR A 20 25.483 4.754 5.222 1.00 27.65 C -ANISOU 139 CG2 THR A 20 3175 3924 3408 -53 -55 223 C -ATOM 140 N AILE A 21 25.911 1.226 4.069 0.57 25.59 N -ANISOU 140 N AILE A 21 2895 3630 3199 127 107 287 N -ATOM 141 N BILE A 21 25.906 1.224 4.064 0.43 25.63 N -ANISOU 141 N BILE A 21 2899 3634 3204 127 107 287 N -ATOM 142 CA AILE A 21 26.983 0.301 4.428 0.57 26.57 C -ANISOU 142 CA AILE A 21 2967 3781 3348 174 124 371 C -ATOM 143 CA BILE A 21 26.967 0.288 4.431 0.43 26.63 C -ANISOU 143 CA BILE A 21 2975 3787 3355 174 124 370 C -ATOM 144 C AILE A 21 27.720 -0.257 3.208 0.57 28.92 C -ANISOU 144 C AILE A 21 3235 4079 3674 249 188 398 C -ATOM 145 C BILE A 21 27.712 -0.272 3.215 0.43 28.77 C -ANISOU 145 C BILE A 21 3217 4060 3656 249 188 398 C -ATOM 146 O AILE A 21 28.914 -0.554 3.281 0.57 29.81 O -ANISOU 146 O AILE A 21 3277 4237 3812 285 198 482 O -ATOM 147 O BILE A 21 28.899 -0.588 3.300 0.43 29.80 O -ANISOU 147 O BILE A 21 3277 4235 3811 286 199 481 O -ATOM 148 CB AILE A 21 26.468 -0.850 5.321 0.57 26.45 C -ANISOU 148 CB AILE A 21 2982 3732 3336 192 133 373 C -ATOM 149 CB BILE A 21 26.427 -0.872 5.294 0.43 26.27 C -ANISOU 149 CB BILE A 21 2962 3706 3313 193 135 371 C -ATOM 150 CG1AILE A 21 26.050 -0.301 6.684 0.57 25.77 C -ANISOU 150 CG1AILE A 21 2908 3673 3211 122 73 369 C -ATOM 151 CG1BILE A 21 25.762 -0.326 6.559 0.43 25.09 C -ANISOU 151 CG1BILE A 21 2836 3574 3123 123 80 349 C -ATOM 152 CG2AILE A 21 27.533 -1.916 5.501 0.57 25.53 C -ANISOU 152 CG2AILE A 21 2815 3628 3259 256 158 461 C -ATOM 153 CG2BILE A 21 27.541 -1.835 5.663 0.43 25.67 C -ANISOU 153 CG2BILE A 21 2830 3651 3272 247 149 465 C -ATOM 154 CD1AILE A 21 27.144 0.497 7.371 0.57 24.66 C -ANISOU 154 CD1AILE A 21 2708 3603 3058 78 13 434 C -ATOM 155 CD1BILE A 21 25.236 -1.398 7.478 0.43 23.05 C -ANISOU 155 CD1BILE A 21 2603 3294 2862 131 87 364 C -ATOM 156 N GLN A 22 27.018 -0.401 2.088 1.00 28.18 N -ANISOU 156 N GLN A 22 3192 3941 3572 274 231 329 N -ATOM 157 CA GLN A 22 27.684 -0.787 0.845 1.00 29.23 C -ANISOU 157 CA GLN A 22 3307 4085 3716 343 295 343 C -ATOM 158 C GLN A 22 28.681 0.304 0.472 1.00 32.38 C -ANISOU 158 C GLN A 22 3629 4561 4111 317 278 404 C -ATOM 159 O GLN A 22 29.820 0.023 0.100 1.00 36.75 O -ANISOU 159 O GLN A 22 4115 5164 4684 370 316 474 O -ATOM 160 CB GLN A 22 26.691 -0.996 -0.304 1.00 28.93 C -ANISOU 160 CB GLN A 22 3346 3993 3655 358 332 253 C -ATOM 161 CG GLN A 22 26.225 -2.433 -0.499 1.00 25.50 C -ANISOU 161 CG GLN A 22 2971 3483 3233 419 379 213 C -ATOM 162 CD GLN A 22 27.300 -3.349 -1.088 1.00 28.79 C -ANISOU 162 CD GLN A 22 3363 3905 3673 519 448 251 C -ATOM 163 OE1 GLN A 22 28.454 -2.955 -1.253 1.00 31.48 O -ANISOU 163 OE1 GLN A 22 3623 4317 4020 544 464 320 O -ATOM 164 NE2 GLN A 22 26.914 -4.582 -1.410 1.00 22.17 N -ANISOU 164 NE2 GLN A 22 2590 2987 2847 576 489 205 N -ATOM 165 N LEU A 23 28.255 1.556 0.579 1.00 32.72 N -ANISOU 165 N LEU A 23 3680 4615 4135 237 220 381 N -ATOM 166 CA LEU A 23 29.132 2.668 0.234 1.00 31.34 C -ANISOU 166 CA LEU A 23 3440 4506 3963 197 192 442 C -ATOM 167 C LEU A 23 30.360 2.712 1.144 1.00 34.99 C -ANISOU 167 C LEU A 23 3815 5029 4449 185 157 544 C -ATOM 168 O LEU A 23 31.488 2.875 0.678 1.00 39.14 O -ANISOU 168 O LEU A 23 4259 5621 4993 203 174 626 O -ATOM 169 CB LEU A 23 28.380 3.997 0.312 1.00 28.67 C -ANISOU 169 CB LEU A 23 3137 4149 3609 112 126 397 C -ATOM 170 CG LEU A 23 29.206 5.219 -0.108 1.00 30.40 C -ANISOU 170 CG LEU A 23 3295 4421 3835 59 88 461 C -ATOM 171 CD1 LEU A 23 29.200 5.389 -1.625 1.00 29.92 C -ANISOU 171 CD1 LEU A 23 3233 4375 3761 86 139 459 C -ATOM 172 CD2 LEU A 23 28.706 6.485 0.579 1.00 29.76 C -ANISOU 172 CD2 LEU A 23 3243 4312 3753 -32 0 431 C -ATOM 173 N ILE A 24 30.133 2.563 2.446 1.00 34.62 N -ANISOU 173 N ILE A 24 3784 4969 4402 152 107 542 N -ATOM 174 CA ILE A 24 31.191 2.718 3.436 1.00 34.63 C -ANISOU 174 CA ILE A 24 3710 5030 4418 120 53 636 C -ATOM 175 C ILE A 24 32.061 1.471 3.588 1.00 42.68 C -ANISOU 175 C ILE A 24 4669 6076 5471 204 101 714 C -ATOM 176 O ILE A 24 33.283 1.559 3.544 1.00 47.77 O -ANISOU 176 O ILE A 24 5218 6791 6143 214 97 816 O -ATOM 177 CB ILE A 24 30.611 3.097 4.811 1.00 32.95 C -ANISOU 177 CB ILE A 24 3543 4801 4177 48 -23 603 C -ATOM 178 CG1 ILE A 24 29.621 4.255 4.673 1.00 31.43 C -ANISOU 178 CG1 ILE A 24 3417 4567 3957 -17 -61 513 C -ATOM 179 CG2 ILE A 24 31.726 3.490 5.770 1.00 33.27 C -ANISOU 179 CG2 ILE A 24 3509 4909 4222 -5 -96 698 C -ATOM 180 CD1 ILE A 24 30.280 5.566 4.265 1.00 34.00 C -ANISOU 180 CD1 ILE A 24 3702 4925 4292 -80 -113 550 C -ATOM 181 N GLN A 25 31.433 0.311 3.757 1.00 46.20 N -ANISOU 181 N GLN A 25 5170 6464 5922 263 145 673 N -ATOM 182 CA GLN A 25 32.162 -0.913 4.093 1.00 46.73 C -ANISOU 182 CA GLN A 25 5190 6538 6028 342 181 747 C -ATOM 183 C GLN A 25 32.265 -1.940 2.958 1.00 46.05 C -ANISOU 183 C GLN A 25 5115 6414 5968 456 281 728 C -ATOM 184 O GLN A 25 32.893 -2.987 3.122 1.00 47.86 O -ANISOU 184 O GLN A 25 5308 6638 6239 537 319 786 O -ATOM 185 CB GLN A 25 31.562 -1.567 5.342 1.00 47.03 C -ANISOU 185 CB GLN A 25 5271 6538 6058 324 145 739 C -ATOM 186 CG GLN A 25 31.637 -0.698 6.587 1.00 51.78 C -ANISOU 186 CG GLN A 25 5859 7189 6626 223 49 766 C -ATOM 187 CD GLN A 25 30.963 -1.331 7.794 1.00 57.25 C -ANISOU 187 CD GLN A 25 6600 7856 7297 203 22 756 C -ATOM 188 OE1 GLN A 25 30.583 -2.504 7.771 1.00 59.49 O -ANISOU 188 OE1 GLN A 25 6913 8085 7604 266 69 752 O -ATOM 189 NE2 GLN A 25 30.808 -0.550 8.857 1.00 57.61 N -ANISOU 189 NE2 GLN A 25 6657 7939 7294 115 -56 754 N -ATOM 190 N ASN A 26 31.652 -1.645 1.816 1.00 40.84 N -ANISOU 190 N ASN A 26 4510 5726 5282 463 322 646 N -ATOM 191 CA ASN A 26 31.779 -2.506 0.641 1.00 42.99 C -ANISOU 191 CA ASN A 26 4802 5968 5564 566 417 617 C -ATOM 192 C ASN A 26 31.240 -3.914 0.832 1.00 42.32 C -ANISOU 192 C ASN A 26 4786 5790 5502 634 454 576 C -ATOM 193 O ASN A 26 31.706 -4.849 0.181 1.00 46.56 O -ANISOU 193 O ASN A 26 5323 6304 6065 737 529 579 O -ATOM 194 CB ASN A 26 33.241 -2.596 0.191 1.00 49.84 C -ANISOU 194 CB ASN A 26 5559 6917 6461 636 465 717 C -ATOM 195 CG ASN A 26 33.844 -1.238 -0.108 1.00 55.63 C -ANISOU 195 CG ASN A 26 6218 7743 7177 566 429 771 C -ATOM 196 OD1 ASN A 26 33.165 -0.336 -0.603 1.00 56.22 O -ANISOU 196 OD1 ASN A 26 6339 7810 7212 499 405 711 O -ATOM 197 ND2 ASN A 26 35.130 -1.085 0.191 1.00 57.59 N -ANISOU 197 ND2 ASN A 26 6345 8077 7459 578 422 892 N -ATOM 198 N HIS A 27 30.270 -4.076 1.722 1.00 41.38 N -ANISOU 198 N HIS A 27 4728 5619 5377 578 404 538 N -ATOM 199 CA HIS A 27 29.612 -5.368 1.873 1.00 41.01 C -ANISOU 199 CA HIS A 27 4753 5475 5353 625 430 499 C -ATOM 200 C HIS A 27 28.109 -5.214 2.090 1.00 39.79 C -ANISOU 200 C HIS A 27 4689 5263 5166 551 395 410 C -ATOM 201 O HIS A 27 27.636 -4.190 2.586 1.00 38.40 O -ANISOU 201 O HIS A 27 4510 5124 4957 465 339 397 O -ATOM 202 CB HIS A 27 30.246 -6.186 3.002 1.00 44.09 C -ANISOU 202 CB HIS A 27 5096 5864 5791 656 413 592 C -ATOM 203 CG HIS A 27 29.940 -5.663 4.370 1.00 48.63 C -ANISOU 203 CG HIS A 27 5657 6476 6346 562 330 628 C -ATOM 204 ND1 HIS A 27 28.828 -6.059 5.084 1.00 49.19 N -ANISOU 204 ND1 HIS A 27 5796 6490 6403 516 301 588 N -ATOM 205 CD2 HIS A 27 30.590 -4.768 5.146 1.00 50.71 C -ANISOU 205 CD2 HIS A 27 5847 6828 6594 501 269 696 C -ATOM 206 CE1 HIS A 27 28.812 -5.431 6.246 1.00 50.49 C -ANISOU 206 CE1 HIS A 27 5933 6713 6538 439 234 627 C -ATOM 207 NE2 HIS A 27 29.868 -4.641 6.312 1.00 51.58 N -ANISOU 207 NE2 HIS A 27 5991 6934 6673 426 209 689 N -ATOM 208 N PHE A 28 27.369 -6.245 1.705 1.00 37.98 N -ANISOU 208 N PHE A 28 4539 4941 4950 587 427 351 N -ATOM 209 CA PHE A 28 25.923 -6.237 1.795 1.00 35.47 C -ANISOU 209 CA PHE A 28 4301 4567 4608 522 400 274 C -ATOM 210 C PHE A 28 25.446 -6.828 3.115 1.00 40.18 C -ANISOU 210 C PHE A 28 4907 5137 5224 488 361 311 C -ATOM 211 O PHE A 28 25.779 -7.963 3.455 1.00 45.72 O -ANISOU 211 O PHE A 28 5613 5788 5971 541 378 354 O -ATOM 212 CB PHE A 28 25.327 -7.023 0.628 1.00 33.08 C -ANISOU 212 CB PHE A 28 4083 4180 4306 565 446 192 C -ATOM 213 CG PHE A 28 23.834 -7.192 0.707 1.00 32.34 C -ANISOU 213 CG PHE A 28 4065 4025 4198 500 415 124 C -ATOM 214 CD1 PHE A 28 22.995 -6.084 0.739 1.00 29.97 C -ANISOU 214 CD1 PHE A 28 3765 3764 3857 419 376 87 C -ATOM 215 CD2 PHE A 28 23.268 -8.454 0.733 1.00 29.19 C -ANISOU 215 CD2 PHE A 28 3733 3526 3831 519 424 102 C -ATOM 216 CE1 PHE A 28 21.619 -6.236 0.806 1.00 26.30 C -ANISOU 216 CE1 PHE A 28 3355 3252 3384 363 350 34 C -ATOM 217 CE2 PHE A 28 21.896 -8.610 0.797 1.00 29.50 C -ANISOU 217 CE2 PHE A 28 3831 3516 3861 451 392 50 C -ATOM 218 CZ PHE A 28 21.070 -7.497 0.833 1.00 28.01 C -ANISOU 218 CZ PHE A 28 3632 3380 3632 375 358 19 C -ATOM 219 N AVAL A 29 24.669 -6.046 3.857 0.52 38.38 N -ANISOU 219 N AVAL A 29 4680 4941 4960 403 311 295 N -ATOM 220 N BVAL A 29 24.662 -6.053 3.856 0.48 38.41 N -ANISOU 220 N BVAL A 29 4685 4945 4964 403 311 295 N -ATOM 221 CA AVAL A 29 24.080 -6.510 5.106 0.52 38.83 C -ANISOU 221 CA AVAL A 29 4749 4987 5019 362 278 326 C -ATOM 222 CA BVAL A 29 24.098 -6.519 5.117 0.48 38.82 C -ANISOU 222 CA BVAL A 29 4746 4986 5019 362 278 328 C -ATOM 223 C AVAL A 29 22.769 -7.244 4.838 0.52 38.28 C -ANISOU 223 C AVAL A 29 4755 4833 4957 343 287 266 C -ATOM 224 C BVAL A 29 22.769 -7.235 4.886 0.48 38.26 C -ANISOU 224 C BVAL A 29 4751 4833 4954 342 285 268 C -ATOM 225 O AVAL A 29 21.768 -6.642 4.443 0.52 36.07 O -ANISOU 225 O AVAL A 29 4507 4552 4648 296 278 197 O -ATOM 226 O BVAL A 29 21.755 -6.609 4.566 0.48 36.17 O -ANISOU 226 O BVAL A 29 4516 4569 4658 291 274 202 O -ATOM 227 CB AVAL A 29 23.832 -5.349 6.094 0.52 39.00 C -ANISOU 227 CB AVAL A 29 4740 5087 4990 283 226 333 C -ATOM 228 CB BVAL A 29 23.895 -5.356 6.109 0.48 38.44 C -ANISOU 228 CB BVAL A 29 4666 5018 4921 285 226 337 C -ATOM 229 CG1AVAL A 29 23.019 -4.244 5.434 0.52 38.31 C -ANISOU 229 CG1AVAL A 29 4679 5010 4869 239 219 249 C -ATOM 230 CG1BVAL A 29 23.125 -5.829 7.333 0.48 38.65 C -ANISOU 230 CG1BVAL A 29 4711 5041 4934 240 200 360 C -ATOM 231 CG2AVAL A 29 23.133 -5.857 7.346 0.52 38.66 C -ANISOU 231 CG2AVAL A 29 4712 5042 4936 241 200 362 C -ATOM 232 CG2BVAL A 29 25.237 -4.760 6.508 0.48 35.40 C -ANISOU 232 CG2BVAL A 29 4206 4712 4533 291 203 410 C -ATOM 233 N ASP A 30 22.787 -8.553 5.050 1.00 39.69 N -ANISOU 233 N ASP A 30 4960 4940 5182 380 300 300 N -ATOM 234 CA ASP A 30 21.620 -9.386 4.808 1.00 40.91 C -ANISOU 234 CA ASP A 30 5186 5004 5353 358 302 255 C -ATOM 235 C ASP A 30 20.611 -9.288 5.953 1.00 38.66 C -ANISOU 235 C ASP A 30 4898 4746 5047 277 264 277 C -ATOM 236 O ASP A 30 19.409 -9.470 5.754 1.00 37.77 O -ANISOU 236 O ASP A 30 4828 4594 4929 230 257 232 O -ATOM 237 CB ASP A 30 22.077 -10.836 4.604 1.00 48.92 C -ANISOU 237 CB ASP A 30 6234 5919 6433 428 327 286 C -ATOM 238 CG ASP A 30 20.927 -11.818 4.576 1.00 55.74 C -ANISOU 238 CG ASP A 30 7172 6683 7325 393 315 259 C -ATOM 239 OD1 ASP A 30 20.163 -11.808 3.586 1.00 56.06 O -ANISOU 239 OD1 ASP A 30 7271 6676 7353 375 321 174 O -ATOM 240 OD2 ASP A 30 20.801 -12.611 5.536 1.00 60.78 O -ANISOU 240 OD2 ASP A 30 7807 7290 7997 378 294 331 O -ATOM 241 N GLU A 31 21.103 -8.996 7.152 1.00 40.11 N -ANISOU 241 N GLU A 31 5028 5002 5211 259 240 350 N -ATOM 242 CA GLU A 31 20.239 -8.900 8.323 1.00 42.45 C -ANISOU 242 CA GLU A 31 5318 5339 5473 188 212 376 C -ATOM 243 C GLU A 31 19.368 -7.644 8.250 1.00 40.95 C -ANISOU 243 C GLU A 31 5127 5206 5226 133 203 303 C -ATOM 244 O GLU A 31 19.757 -6.642 7.653 1.00 39.93 O -ANISOU 244 O GLU A 31 4984 5110 5078 143 204 259 O -ATOM 245 CB GLU A 31 21.079 -8.879 9.602 1.00 49.76 C -ANISOU 245 CB GLU A 31 6190 6335 6380 184 186 471 C -ATOM 246 CG GLU A 31 22.427 -9.596 9.488 1.00 60.72 C -ANISOU 246 CG GLU A 31 7550 7697 7822 258 194 544 C -ATOM 247 CD GLU A 31 22.303 -11.114 9.422 1.00 69.48 C -ANISOU 247 CD GLU A 31 8696 8700 9003 296 208 586 C -ATOM 248 OE1 GLU A 31 23.350 -11.789 9.286 1.00 71.48 O -ANISOU 248 OE1 GLU A 31 8929 8919 9312 369 220 644 O -ATOM 249 OE2 GLU A 31 21.166 -11.633 9.509 1.00 71.04 O -ANISOU 249 OE2 GLU A 31 8940 8846 9206 252 205 566 O -ATOM 250 N TYR A 32 18.183 -7.710 8.847 1.00 35.82 N -ANISOU 250 N TYR A 32 4488 4566 4554 78 196 296 N -ATOM 251 CA TYR A 32 17.322 -6.544 8.988 1.00 35.47 C -ANISOU 251 CA TYR A 32 4436 4581 4458 33 190 237 C -ATOM 252 C TYR A 32 17.395 -6.051 10.433 1.00 34.85 C -ANISOU 252 C TYR A 32 4327 4596 4321 -1 173 278 C -ATOM 253 O TYR A 32 16.724 -6.586 11.316 1.00 31.76 O -ANISOU 253 O TYR A 32 3933 4223 3912 -34 174 318 O -ATOM 254 CB TYR A 32 15.882 -6.912 8.623 1.00 36.23 C -ANISOU 254 CB TYR A 32 4560 4636 4569 -3 199 201 C -ATOM 255 CG TYR A 32 14.894 -5.758 8.588 1.00 34.22 C -ANISOU 255 CG TYR A 32 4294 4432 4276 -36 199 138 C -ATOM 256 CD1 TYR A 32 15.115 -4.587 9.308 1.00 33.11 C -ANISOU 256 CD1 TYR A 32 4126 4373 4080 -44 192 123 C -ATOM 257 CD2 TYR A 32 13.734 -5.848 7.832 1.00 33.59 C -ANISOU 257 CD2 TYR A 32 4231 4315 4217 -60 203 94 C -ATOM 258 CE1 TYR A 32 14.199 -3.543 9.277 1.00 30.77 C -ANISOU 258 CE1 TYR A 32 3822 4112 3756 -64 195 63 C -ATOM 259 CE2 TYR A 32 12.824 -4.814 7.788 1.00 34.30 C -ANISOU 259 CE2 TYR A 32 4302 4449 4280 -82 204 44 C -ATOM 260 CZ TYR A 32 13.057 -3.665 8.511 1.00 31.97 C -ANISOU 260 CZ TYR A 32 3982 4228 3937 -78 204 27 C -ATOM 261 OH TYR A 32 12.131 -2.650 8.457 1.00 30.56 O -ANISOU 261 OH TYR A 32 3788 4083 3740 -90 208 -25 O -ATOM 262 N ASP A 33 18.224 -5.042 10.675 1.00 33.27 N -ANISOU 262 N ASP A 33 4102 4453 4084 4 155 269 N -ATOM 263 CA ASP A 33 18.353 -4.476 12.013 1.00 33.48 C -ANISOU 263 CA ASP A 33 4111 4569 4043 -31 132 295 C -ATOM 264 C ASP A 33 17.859 -3.027 12.020 1.00 30.14 C -ANISOU 264 C ASP A 33 3694 4189 3571 -53 126 211 C -ATOM 265 O ASP A 33 18.564 -2.124 11.572 1.00 26.46 O -ANISOU 265 O ASP A 33 3221 3729 3105 -44 107 181 O -ATOM 266 CB ASP A 33 19.805 -4.566 12.491 1.00 35.97 C -ANISOU 266 CB ASP A 33 4395 4918 4355 -15 102 367 C -ATOM 267 CG ASP A 33 20.025 -3.875 13.819 1.00 41.97 C -ANISOU 267 CG ASP A 33 5143 5773 5032 -59 68 386 C -ATOM 268 OD1 ASP A 33 21.136 -3.343 14.036 1.00 43.18 O -ANISOU 268 OD1 ASP A 33 5271 5964 5169 -60 31 412 O -ATOM 269 OD2 ASP A 33 19.085 -3.861 14.644 1.00 45.11 O -ANISOU 269 OD2 ASP A 33 5555 6210 5376 -93 78 375 O -ATOM 270 N PRO A 34 16.636 -2.808 12.527 1.00 30.39 N -ANISOU 270 N PRO A 34 3734 4248 3566 -81 144 177 N -ATOM 271 CA PRO A 34 15.974 -1.498 12.505 1.00 28.21 C -ANISOU 271 CA PRO A 34 3466 3998 3253 -91 146 92 C -ATOM 272 C PRO A 34 16.877 -0.393 13.045 1.00 31.57 C -ANISOU 272 C PRO A 34 3893 4471 3630 -100 109 73 C -ATOM 273 O PRO A 34 17.510 -0.557 14.087 1.00 28.21 O -ANISOU 273 O PRO A 34 3462 4101 3155 -119 87 122 O -ATOM 274 CB PRO A 34 14.774 -1.698 13.435 1.00 26.22 C -ANISOU 274 CB PRO A 34 3212 3796 2956 -115 175 92 C -ATOM 275 CG PRO A 34 14.484 -3.160 13.367 1.00 27.28 C -ANISOU 275 CG PRO A 34 3340 3895 3133 -121 190 164 C -ATOM 276 CD PRO A 34 15.830 -3.825 13.229 1.00 30.11 C -ANISOU 276 CD PRO A 34 3696 4222 3522 -102 164 227 C -ATOM 277 N THR A 35 16.929 0.729 12.336 1.00 31.46 N -ANISOU 277 N THR A 35 3888 4435 3629 -93 96 7 N -ATOM 278 CA THR A 35 17.792 1.831 12.726 1.00 26.17 C -ANISOU 278 CA THR A 35 3225 3796 2924 -110 52 -13 C -ATOM 279 C THR A 35 17.121 2.806 13.682 1.00 28.66 C -ANISOU 279 C THR A 35 3568 4153 3167 -129 49 -80 C -ATOM 280 O THR A 35 15.937 3.131 13.553 1.00 30.98 O -ANISOU 280 O THR A 35 3871 4438 3461 -116 83 -138 O -ATOM 281 CB THR A 35 18.316 2.587 11.492 1.00 26.78 C -ANISOU 281 CB THR A 35 3298 3823 3053 -98 32 -40 C -ATOM 282 OG1 THR A 35 19.335 1.802 10.867 1.00 30.94 O -ANISOU 282 OG1 THR A 35 3797 4333 3626 -79 30 28 O -ATOM 283 CG2 THR A 35 18.912 3.934 11.879 1.00 25.17 C -ANISOU 283 CG2 THR A 35 3108 3639 2817 -126 -18 -75 C -ATOM 284 N ILE A 36 17.894 3.251 14.662 1.00 29.19 N -ANISOU 284 N ILE A 36 3647 4272 3172 -158 7 -70 N -ATOM 285 CA ILE A 36 17.512 4.377 15.486 1.00 28.52 C -ANISOU 285 CA ILE A 36 3603 4219 3017 -174 -6 -149 C -ATOM 286 C ILE A 36 18.115 5.593 14.806 1.00 29.04 C -ANISOU 286 C ILE A 36 3683 4235 3116 -182 -54 -195 C -ATOM 287 O ILE A 36 17.399 6.472 14.321 1.00 27.04 O -ANISOU 287 O ILE A 36 3450 3938 2885 -164 -42 -271 O -ATOM 288 CB ILE A 36 18.063 4.222 16.916 1.00 30.04 C -ANISOU 288 CB ILE A 36 3810 4492 3112 -212 -36 -116 C -ATOM 289 CG1 ILE A 36 17.403 3.020 17.606 1.00 28.31 C -ANISOU 289 CG1 ILE A 36 3573 4324 2858 -208 12 -59 C -ATOM 290 CG2 ILE A 36 17.865 5.509 17.727 1.00 21.64 C -ANISOU 290 CG2 ILE A 36 2802 3453 1967 -230 -60 -210 C -ATOM 291 CD1 ILE A 36 17.944 2.724 19.006 1.00 29.50 C -ANISOU 291 CD1 ILE A 36 3735 4566 2910 -247 -18 -9 C -ATOM 292 N GLU A 37 19.443 5.605 14.739 1.00 31.89 N -ANISOU 292 N GLU A 37 4027 4603 3489 -210 -109 -137 N -ATOM 293 CA GLU A 37 20.190 6.627 14.025 1.00 33.57 C -ANISOU 293 CA GLU A 37 4241 4773 3743 -227 -160 -154 C -ATOM 294 C GLU A 37 21.657 6.213 13.964 1.00 33.52 C -ANISOU 294 C GLU A 37 4188 4792 3754 -252 -206 -57 C -ATOM 295 O GLU A 37 22.213 5.719 14.951 1.00 35.91 O -ANISOU 295 O GLU A 37 4484 5156 4006 -277 -231 -3 O -ATOM 296 CB GLU A 37 20.038 7.975 14.727 1.00 42.57 C -ANISOU 296 CB GLU A 37 5438 5909 4829 -257 -202 -241 C -ATOM 297 CG GLU A 37 20.763 9.128 14.054 1.00 52.14 C -ANISOU 297 CG GLU A 37 6656 7068 6086 -285 -264 -256 C -ATOM 298 CD GLU A 37 20.436 10.469 14.693 1.00 56.51 C -ANISOU 298 CD GLU A 37 7281 7595 6595 -308 -304 -357 C -ATOM 299 OE1 GLU A 37 19.624 11.215 14.101 1.00 59.45 O -ANISOU 299 OE1 GLU A 37 7678 7903 7008 -277 -284 -426 O -ATOM 300 OE2 GLU A 37 20.982 10.771 15.780 1.00 53.20 O -ANISOU 300 OE2 GLU A 37 6897 7215 6101 -354 -356 -367 O -ATOM 301 N ASP A 38 22.278 6.390 12.802 1.00 29.12 N -ANISOU 301 N ASP A 38 3597 4198 3269 -243 -215 -26 N -ATOM 302 CA ASP A 38 23.681 6.026 12.631 1.00 31.86 C -ANISOU 302 CA ASP A 38 3888 4575 3643 -257 -250 73 C -ATOM 303 C ASP A 38 24.440 7.080 11.828 1.00 35.82 C -ANISOU 303 C ASP A 38 4371 5050 4187 -285 -297 78 C -ATOM 304 O ASP A 38 23.933 7.587 10.829 1.00 39.44 O -ANISOU 304 O ASP A 38 4842 5456 4688 -266 -275 34 O -ATOM 305 CB ASP A 38 23.808 4.649 11.980 1.00 31.84 C -ANISOU 305 CB ASP A 38 3841 4567 3690 -202 -192 140 C -ATOM 306 CG ASP A 38 23.384 3.527 12.905 1.00 37.29 C -ANISOU 306 CG ASP A 38 4537 5288 4343 -189 -165 169 C -ATOM 307 OD1 ASP A 38 23.941 3.428 14.018 1.00 42.04 O -ANISOU 307 OD1 ASP A 38 5133 5948 4893 -224 -207 213 O -ATOM 308 OD2 ASP A 38 22.486 2.748 12.526 1.00 39.54 O -ANISOU 308 OD2 ASP A 38 4834 5541 4650 -150 -106 152 O -ATOM 309 N SER A 39 25.649 7.409 12.280 1.00 36.12 N -ANISOU 309 N SER A 39 4379 5130 4215 -335 -366 140 N -ATOM 310 CA SER A 39 26.453 8.463 11.660 1.00 38.90 C -ANISOU 310 CA SER A 39 4709 5465 4606 -378 -423 159 C -ATOM 311 C SER A 39 27.694 7.892 11.011 1.00 38.76 C -ANISOU 311 C SER A 39 4601 5487 4641 -366 -421 277 C -ATOM 312 O SER A 39 28.457 7.168 11.646 1.00 44.40 O -ANISOU 312 O SER A 39 5270 6259 5342 -370 -437 357 O -ATOM 313 CB SER A 39 26.870 9.505 12.693 1.00 41.47 C -ANISOU 313 CB SER A 39 5073 5803 4879 -460 -518 134 C -ATOM 314 OG SER A 39 25.735 10.054 13.329 1.00 46.00 O -ANISOU 314 OG SER A 39 5735 6343 5400 -460 -511 18 O -ATOM 315 N TYR A 40 27.902 8.225 9.744 1.00 32.58 N -ANISOU 315 N TYR A 40 3787 4677 3916 -349 -400 293 N -ATOM 316 CA TYR A 40 29.044 7.688 9.021 1.00 35.11 C -ANISOU 316 CA TYR A 40 4016 5039 4284 -326 -382 402 C -ATOM 317 C TYR A 40 29.882 8.773 8.392 1.00 39.56 C -ANISOU 317 C TYR A 40 4539 5609 4883 -380 -436 447 C -ATOM 318 O TYR A 40 29.407 9.884 8.143 1.00 35.14 O -ANISOU 318 O TYR A 40 4028 4999 4326 -421 -471 385 O -ATOM 319 CB TYR A 40 28.598 6.702 7.941 1.00 31.74 C -ANISOU 319 CB TYR A 40 3578 4590 3891 -237 -284 398 C -ATOM 320 CG TYR A 40 27.881 5.500 8.491 1.00 32.45 C -ANISOU 320 CG TYR A 40 3699 4671 3958 -186 -233 374 C -ATOM 321 CD1 TYR A 40 26.495 5.452 8.526 1.00 28.47 C -ANISOU 321 CD1 TYR A 40 3267 4117 3434 -171 -200 278 C -ATOM 322 CD2 TYR A 40 28.589 4.411 8.979 1.00 34.13 C -ANISOU 322 CD2 TYR A 40 3864 4927 4179 -155 -221 457 C -ATOM 323 CE1 TYR A 40 25.829 4.345 9.031 1.00 28.75 C -ANISOU 323 CE1 TYR A 40 3325 4146 3452 -134 -157 267 C -ATOM 324 CE2 TYR A 40 27.933 3.296 9.484 1.00 33.08 C -ANISOU 324 CE2 TYR A 40 3759 4779 4031 -115 -179 444 C -ATOM 325 CZ TYR A 40 26.555 3.272 9.514 1.00 34.45 C -ANISOU 325 CZ TYR A 40 4005 4904 4181 -109 -149 350 C -ATOM 326 OH TYR A 40 25.905 2.163 10.017 1.00 38.48 O -ANISOU 326 OH TYR A 40 4538 5402 4679 -77 -111 349 O -ATOM 327 N ARG A 41 31.134 8.423 8.124 1.00 46.77 N -ANISOU 327 N ARG A 41 5357 6585 5829 -378 -441 563 N -ATOM 328 CA ARG A 41 32.085 9.323 7.504 1.00 49.05 C -ANISOU 328 CA ARG A 41 5584 6898 6155 -432 -489 634 C -ATOM 329 C ARG A 41 32.772 8.597 6.359 1.00 49.00 C -ANISOU 329 C ARG A 41 5488 6936 6194 -361 -410 720 C -ATOM 330 O ARG A 41 33.351 7.528 6.553 1.00 49.04 O -ANISOU 330 O ARG A 41 5434 6990 6208 -306 -371 787 O -ATOM 331 CB ARG A 41 33.129 9.750 8.530 1.00 53.55 C -ANISOU 331 CB ARG A 41 6112 7521 6714 -519 -592 708 C -ATOM 332 CG ARG A 41 33.367 11.233 8.570 1.00 59.06 C -ANISOU 332 CG ARG A 41 6832 8189 7418 -624 -691 697 C -ATOM 333 CD ARG A 41 33.952 11.724 7.263 1.00 62.47 C -ANISOU 333 CD ARG A 41 7193 8633 7910 -630 -675 769 C -ATOM 334 NE ARG A 41 33.864 13.175 7.186 1.00 64.90 N -ANISOU 334 NE ARG A 41 7546 8881 8230 -725 -763 738 N -ATOM 335 CZ ARG A 41 34.695 14.004 7.805 1.00 66.87 C -ANISOU 335 CZ ARG A 41 7775 9146 8485 -834 -879 791 C -ATOM 336 NH1 ARG A 41 35.688 13.523 8.544 1.00 65.79 N -ANISOU 336 NH1 ARG A 41 7566 9092 8339 -863 -921 884 N -ATOM 337 NH2 ARG A 41 34.532 15.314 7.683 1.00 68.92 N -ANISOU 337 NH2 ARG A 41 8090 9334 8764 -916 -958 755 N -ATOM 338 N LYS A 42 32.702 9.165 5.162 1.00 47.36 N -ANISOU 338 N LYS A 42 5271 6711 6012 -358 -384 718 N -ATOM 339 CA LYS A 42 33.470 8.626 4.050 1.00 47.73 C -ANISOU 339 CA LYS A 42 5230 6814 6092 -297 -311 803 C -ATOM 340 C LYS A 42 34.194 9.726 3.286 1.00 47.42 C -ANISOU 340 C LYS A 42 5131 6805 6082 -361 -350 875 C -ATOM 341 O LYS A 42 33.613 10.759 2.948 1.00 42.93 O -ANISOU 341 O LYS A 42 4618 6181 5513 -415 -389 824 O -ATOM 342 CB LYS A 42 32.593 7.817 3.095 1.00 48.34 C -ANISOU 342 CB LYS A 42 5353 6854 6162 -201 -205 734 C -ATOM 343 CG LYS A 42 33.402 7.124 2.008 1.00 50.75 C -ANISOU 343 CG LYS A 42 5577 7219 6489 -124 -119 811 C -ATOM 344 CD LYS A 42 32.542 6.260 1.114 1.00 53.96 C -ANISOU 344 CD LYS A 42 6042 7583 6878 -33 -21 734 C -ATOM 345 CE LYS A 42 33.402 5.433 0.169 1.00 56.41 C -ANISOU 345 CE LYS A 42 6278 7953 7202 58 71 802 C -ATOM 346 NZ LYS A 42 34.380 4.593 0.919 1.00 59.15 N -ANISOU 346 NZ LYS A 42 6549 8349 7578 100 79 886 N -ATOM 347 N GLN A 43 35.473 9.498 3.023 1.00 50.99 N -ANISOU 347 N GLN A 43 5465 7345 6563 -355 -340 1003 N -ATOM 348 CA GLN A 43 36.238 10.413 2.197 1.00 53.90 C -ANISOU 348 CA GLN A 43 5760 7759 6962 -411 -365 1093 C -ATOM 349 C GLN A 43 36.380 9.819 0.808 1.00 54.50 C -ANISOU 349 C GLN A 43 5790 7878 7041 -316 -245 1122 C -ATOM 350 O GLN A 43 36.971 8.751 0.636 1.00 56.09 O -ANISOU 350 O GLN A 43 5925 8139 7249 -227 -167 1174 O -ATOM 351 CB GLN A 43 37.612 10.686 2.804 1.00 57.80 C -ANISOU 351 CB GLN A 43 6140 8336 7487 -479 -440 1230 C -ATOM 352 CG GLN A 43 38.426 11.703 2.019 1.00 65.17 C -ANISOU 352 CG GLN A 43 6989 9318 8454 -555 -476 1336 C -ATOM 353 CD GLN A 43 39.848 11.849 2.536 1.00 71.55 C -ANISOU 353 CD GLN A 43 7664 10224 9299 -619 -544 1489 C -ATOM 354 OE1 GLN A 43 40.807 11.790 1.765 1.00 73.39 O -ANISOU 354 OE1 GLN A 43 7771 10552 9563 -602 -501 1616 O -ATOM 355 NE2 GLN A 43 39.989 12.047 3.843 1.00 72.91 N -ANISOU 355 NE2 GLN A 43 7860 10379 9463 -694 -650 1483 N -ATOM 356 N VAL A 44 35.813 10.504 -0.178 1.00 52.90 N -ANISOU 356 N VAL A 44 5628 7641 6829 -333 -231 1085 N -ATOM 357 CA VAL A 44 35.946 10.087 -1.564 1.00 54.21 C -ANISOU 357 CA VAL A 44 5759 7855 6984 -256 -125 1111 C -ATOM 358 C VAL A 44 36.425 11.245 -2.421 1.00 53.50 C -ANISOU 358 C VAL A 44 5615 7803 6909 -331 -157 1194 C -ATOM 359 O VAL A 44 36.427 12.398 -1.989 1.00 53.42 O -ANISOU 359 O VAL A 44 5619 7756 6923 -443 -265 1209 O -ATOM 360 CB VAL A 44 34.619 9.566 -2.141 1.00 55.10 C -ANISOU 360 CB VAL A 44 5983 7894 7057 -186 -57 980 C -ATOM 361 CG1 VAL A 44 34.266 8.223 -1.534 1.00 57.39 C -ANISOU 361 CG1 VAL A 44 6311 8158 7336 -98 -4 918 C -ATOM 362 CG2 VAL A 44 33.506 10.578 -1.914 1.00 55.54 C -ANISOU 362 CG2 VAL A 44 6139 7854 7110 -261 -134 891 C -ATOM 363 N VAL A 45 36.844 10.925 -3.637 1.00 51.97 N -ANISOU 363 N VAL A 45 5361 7684 6699 -270 -62 1250 N -ATOM 364 CA VAL A 45 37.190 11.946 -4.604 1.00 50.35 C -ANISOU 364 CA VAL A 45 5109 7522 6499 -335 -79 1331 C -ATOM 365 C VAL A 45 36.135 11.929 -5.694 1.00 45.49 C -ANISOU 365 C VAL A 45 4582 6865 5836 -293 -19 1243 C -ATOM 366 O VAL A 45 35.830 10.881 -6.266 1.00 41.82 O -ANISOU 366 O VAL A 45 4144 6415 5329 -185 86 1188 O -ATOM 367 CB VAL A 45 38.585 11.721 -5.202 1.00 53.03 C -ANISOU 367 CB VAL A 45 5296 8003 6849 -309 -18 1483 C -ATOM 368 CG1 VAL A 45 38.934 12.854 -6.152 1.00 53.68 C -ANISOU 368 CG1 VAL A 45 5327 8133 6936 -391 -43 1580 C -ATOM 369 CG2 VAL A 45 39.618 11.615 -4.090 1.00 53.32 C -ANISOU 369 CG2 VAL A 45 5238 8086 6934 -345 -78 1575 C -ATOM 370 N ILE A 46 35.564 13.097 -5.956 1.00 45.02 N -ANISOU 370 N ILE A 46 4572 6747 5787 -381 -95 1231 N -ATOM 371 CA ILE A 46 34.495 13.236 -6.928 1.00 42.62 C -ANISOU 371 CA ILE A 46 4352 6399 5444 -358 -61 1156 C -ATOM 372 C ILE A 46 34.830 14.393 -7.859 1.00 44.68 C -ANISOU 372 C ILE A 46 4566 6696 5712 -438 -96 1257 C -ATOM 373 O ILE A 46 34.954 15.539 -7.420 1.00 47.20 O -ANISOU 373 O ILE A 46 4882 6970 6084 -545 -205 1300 O -ATOM 374 CB ILE A 46 33.149 13.497 -6.225 1.00 40.43 C -ANISOU 374 CB ILE A 46 4199 5988 5175 -378 -124 1021 C -ATOM 375 CG1 ILE A 46 32.875 12.398 -5.189 1.00 38.48 C -ANISOU 375 CG1 ILE A 46 3989 5710 4922 -312 -98 938 C -ATOM 376 CG2 ILE A 46 32.019 13.597 -7.242 1.00 37.99 C -ANISOU 376 CG2 ILE A 46 3968 5638 4829 -352 -92 952 C -ATOM 377 CD1 ILE A 46 31.721 12.699 -4.248 1.00 35.65 C -ANISOU 377 CD1 ILE A 46 3734 5236 4574 -340 -164 822 C -ATOM 378 N ASP A 47 34.998 14.089 -9.141 1.00 44.55 N -ANISOU 378 N ASP A 47 4519 6764 5644 -387 -4 1298 N -ATOM 379 CA ASP A 47 35.330 15.114 -10.122 1.00 49.95 C -ANISOU 379 CA ASP A 47 5153 7498 6326 -460 -26 1407 C -ATOM 380 C ASP A 47 36.581 15.892 -9.718 1.00 53.47 C -ANISOU 380 C ASP A 47 5482 8002 6832 -555 -95 1557 C -ATOM 381 O ASP A 47 36.648 17.113 -9.881 1.00 53.91 O -ANISOU 381 O ASP A 47 5527 8030 6928 -665 -186 1629 O -ATOM 382 CB ASP A 47 34.153 16.075 -10.299 1.00 51.63 C -ANISOU 382 CB ASP A 47 5466 7597 6552 -524 -109 1346 C -ATOM 383 CG ASP A 47 32.893 15.373 -10.758 1.00 52.46 C -ANISOU 383 CG ASP A 47 5678 7652 6600 -443 -51 1211 C -ATOM 384 OD1 ASP A 47 32.999 14.399 -11.536 1.00 53.45 O -ANISOU 384 OD1 ASP A 47 5796 7856 6656 -354 59 1197 O -ATOM 385 OD2 ASP A 47 31.797 15.796 -10.336 1.00 51.99 O -ANISOU 385 OD2 ASP A 47 5711 7477 6567 -467 -118 1120 O -ATOM 386 N GLY A 48 37.569 15.184 -9.182 1.00 54.39 N -ANISOU 386 N GLY A 48 5509 8196 6961 -515 -56 1610 N -ATOM 387 CA GLY A 48 38.822 15.806 -8.796 1.00 56.57 C -ANISOU 387 CA GLY A 48 5659 8541 7294 -604 -119 1763 C -ATOM 388 C GLY A 48 38.733 16.679 -7.558 1.00 57.52 C -ANISOU 388 C GLY A 48 5816 8555 7483 -720 -272 1749 C -ATOM 389 O GLY A 48 39.556 17.573 -7.365 1.00 60.09 O -ANISOU 389 O GLY A 48 6063 8908 7861 -833 -360 1873 O -ATOM 390 N GLU A 49 37.729 16.431 -6.723 1.00 55.05 N -ANISOU 390 N GLU A 49 5626 8123 7169 -696 -305 1598 N -ATOM 391 CA GLU A 49 37.635 17.099 -5.430 1.00 54.67 C -ANISOU 391 CA GLU A 49 5624 7978 7171 -789 -438 1563 C -ATOM 392 C GLU A 49 37.560 16.078 -4.302 1.00 54.16 C -ANISOU 392 C GLU A 49 5584 7901 7094 -723 -420 1483 C -ATOM 393 O GLU A 49 36.786 15.121 -4.368 1.00 51.60 O -ANISOU 393 O GLU A 49 5325 7552 6727 -618 -336 1374 O -ATOM 394 CB GLU A 49 36.412 18.013 -5.365 1.00 58.11 C -ANISOU 394 CB GLU A 49 6190 8269 7619 -838 -514 1459 C -ATOM 395 CG GLU A 49 36.254 18.698 -4.009 1.00 63.23 C -ANISOU 395 CG GLU A 49 6902 8810 8310 -923 -644 1403 C -ATOM 396 CD GLU A 49 34.958 19.487 -3.879 1.00 66.52 C -ANISOU 396 CD GLU A 49 7455 9080 8741 -945 -703 1282 C -ATOM 397 OE1 GLU A 49 34.969 20.537 -3.201 1.00 69.56 O -ANISOU 397 OE1 GLU A 49 7883 9374 9172 -1045 -824 1274 O -ATOM 398 OE2 GLU A 49 33.927 19.056 -4.439 1.00 64.30 O -ANISOU 398 OE2 GLU A 49 7238 8769 8424 -862 -630 1193 O -ATOM 399 N THR A 50 38.364 16.280 -3.266 1.00 53.84 N -ANISOU 399 N THR A 50 5492 7876 7090 -792 -504 1541 N -ATOM 400 CA THR A 50 38.298 15.411 -2.100 1.00 51.01 C -ANISOU 400 CA THR A 50 5159 7504 6718 -746 -504 1475 C -ATOM 401 C THR A 50 37.098 15.809 -1.255 1.00 47.39 C -ANISOU 401 C THR A 50 4850 6907 6250 -773 -573 1323 C -ATOM 402 O THR A 50 37.022 16.931 -0.753 1.00 47.84 O -ANISOU 402 O THR A 50 4950 6892 6336 -882 -691 1315 O -ATOM 403 CB THR A 50 39.577 15.483 -1.240 1.00 52.54 C -ANISOU 403 CB THR A 50 5244 7771 6947 -815 -578 1595 C -ATOM 404 OG1 THR A 50 40.731 15.368 -2.081 1.00 53.52 O -ANISOU 404 OG1 THR A 50 5216 8029 7092 -807 -524 1756 O -ATOM 405 CG2 THR A 50 39.589 14.357 -0.212 1.00 49.35 C -ANISOU 405 CG2 THR A 50 4849 7378 6524 -744 -553 1547 C -ATOM 406 N CYS A 51 36.156 14.888 -1.106 1.00 42.96 N -ANISOU 406 N CYS A 51 4367 6307 5649 -672 -499 1202 N -ATOM 407 CA CYS A 51 34.932 15.187 -0.383 1.00 41.67 C -ANISOU 407 CA CYS A 51 4338 6024 5472 -683 -544 1058 C -ATOM 408 C CYS A 51 34.861 14.432 0.928 1.00 41.32 C -ANISOU 408 C CYS A 51 4321 5974 5404 -658 -556 1003 C -ATOM 409 O CYS A 51 35.015 13.209 0.967 1.00 42.09 O -ANISOU 409 O CYS A 51 4386 6125 5482 -568 -473 1008 O -ATOM 410 CB CYS A 51 33.708 14.852 -1.236 1.00 39.52 C -ANISOU 410 CB CYS A 51 4141 5702 5171 -602 -461 960 C -ATOM 411 SG CYS A 51 33.669 15.710 -2.814 1.00 45.34 S -ANISOU 411 SG CYS A 51 4855 6450 5923 -629 -447 1024 S -ATOM 412 N LEU A 52 34.629 15.172 2.002 1.00 39.69 N -ANISOU 412 N LEU A 52 4180 5700 5199 -738 -661 950 N -ATOM 413 CA LEU A 52 34.368 14.557 3.288 1.00 45.23 C -ANISOU 413 CA LEU A 52 4929 6391 5866 -720 -676 884 C -ATOM 414 C LEU A 52 32.853 14.435 3.461 1.00 41.33 C -ANISOU 414 C LEU A 52 4558 5806 5341 -666 -640 731 C -ATOM 415 O LEU A 52 32.158 15.429 3.681 1.00 40.74 O -ANISOU 415 O LEU A 52 4567 5643 5271 -715 -700 655 O -ATOM 416 CB LEU A 52 35.014 15.374 4.408 1.00 53.63 C -ANISOU 416 CB LEU A 52 5996 7446 6935 -837 -809 911 C -ATOM 417 CG LEU A 52 36.502 15.676 4.161 1.00 61.23 C -ANISOU 417 CG LEU A 52 6828 8498 7940 -909 -860 1076 C -ATOM 418 CD1 LEU A 52 37.106 16.530 5.270 1.00 63.37 C -ANISOU 418 CD1 LEU A 52 7111 8753 8214 -1040 -1008 1099 C -ATOM 419 CD2 LEU A 52 37.313 14.392 3.972 1.00 62.76 C -ANISOU 419 CD2 LEU A 52 6904 8809 8133 -827 -774 1173 C -ATOM 420 N LEU A 53 32.344 13.213 3.325 1.00 37.26 N -ANISOU 420 N LEU A 53 4050 5309 4798 -565 -541 692 N -ATOM 421 CA LEU A 53 30.905 12.966 3.401 1.00 36.68 C -ANISOU 421 CA LEU A 53 4077 5163 4699 -511 -498 563 C -ATOM 422 C LEU A 53 30.462 12.651 4.825 1.00 33.92 C -ANISOU 422 C LEU A 53 3786 4793 4308 -515 -526 491 C -ATOM 423 O LEU A 53 30.913 11.673 5.416 1.00 35.10 O -ANISOU 423 O LEU A 53 3900 4999 4439 -485 -503 528 O -ATOM 424 CB LEU A 53 30.491 11.823 2.461 1.00 32.42 C -ANISOU 424 CB LEU A 53 3523 4645 4149 -408 -382 553 C -ATOM 425 CG LEU A 53 30.837 11.972 0.974 1.00 31.11 C -ANISOU 425 CG LEU A 53 3306 4511 4004 -389 -335 615 C -ATOM 426 CD1 LEU A 53 30.299 10.807 0.160 1.00 28.74 C -ANISOU 426 CD1 LEU A 53 3018 4220 3682 -288 -226 580 C -ATOM 427 CD2 LEU A 53 30.315 13.287 0.431 1.00 30.14 C -ANISOU 427 CD2 LEU A 53 3224 4325 3901 -448 -388 591 C -ATOM 428 N ASP A 54 29.586 13.489 5.370 1.00 32.95 N -ANISOU 428 N ASP A 54 3753 4593 4172 -549 -575 393 N -ATOM 429 CA ASP A 54 28.970 13.229 6.665 1.00 36.14 C -ANISOU 429 CA ASP A 54 4226 4981 4526 -545 -588 310 C -ATOM 430 C ASP A 54 27.590 12.661 6.414 1.00 32.28 C -ANISOU 430 C ASP A 54 3791 4452 4021 -465 -506 218 C -ATOM 431 O ASP A 54 26.653 13.408 6.123 1.00 32.22 O -ANISOU 431 O ASP A 54 3842 4375 4025 -463 -510 142 O -ATOM 432 CB ASP A 54 28.842 14.514 7.483 1.00 45.52 C -ANISOU 432 CB ASP A 54 5484 6109 5702 -625 -688 250 C -ATOM 433 CG ASP A 54 30.161 14.969 8.064 1.00 56.76 C -ANISOU 433 CG ASP A 54 6864 7574 7127 -718 -786 333 C -ATOM 434 OD1 ASP A 54 30.464 16.181 7.991 1.00 59.84 O -ANISOU 434 OD1 ASP A 54 7276 7914 7546 -797 -871 335 O -ATOM 435 OD2 ASP A 54 30.894 14.111 8.600 1.00 62.82 O -ANISOU 435 OD2 ASP A 54 7575 8423 7872 -715 -782 401 O -ATOM 436 N ILE A 55 27.461 11.344 6.525 1.00 27.46 N -ANISOU 436 N ILE A 55 3160 3884 3391 -402 -435 231 N -ATOM 437 CA ILE A 55 26.210 10.680 6.177 1.00 27.96 C -ANISOU 437 CA ILE A 55 3264 3915 3445 -332 -358 160 C -ATOM 438 C ILE A 55 25.386 10.273 7.393 1.00 30.14 C -ANISOU 438 C ILE A 55 3594 4185 3671 -320 -349 90 C -ATOM 439 O ILE A 55 25.843 9.511 8.244 1.00 31.96 O -ANISOU 439 O ILE A 55 3807 4465 3871 -319 -350 126 O -ATOM 440 CB ILE A 55 26.458 9.451 5.285 1.00 23.97 C -ANISOU 440 CB ILE A 55 2707 3443 2956 -265 -278 213 C -ATOM 441 CG1 ILE A 55 27.237 9.867 4.030 1.00 24.95 C -ANISOU 441 CG1 ILE A 55 2777 3586 3119 -272 -274 282 C -ATOM 442 CG2 ILE A 55 25.134 8.789 4.910 1.00 23.78 C -ANISOU 442 CG2 ILE A 55 2730 3380 2924 -207 -210 140 C -ATOM 443 CD1 ILE A 55 27.993 8.723 3.356 1.00 22.41 C -ANISOU 443 CD1 ILE A 55 2389 3318 2806 -212 -206 356 C -ATOM 444 N LEU A 56 24.163 10.788 7.468 1.00 27.86 N -ANISOU 444 N LEU A 56 3369 3842 3374 -309 -340 -4 N -ATOM 445 CA LEU A 56 23.248 10.396 8.528 1.00 25.88 C -ANISOU 445 CA LEU A 56 3166 3594 3073 -290 -317 -71 C -ATOM 446 C LEU A 56 22.252 9.355 8.013 1.00 24.14 C -ANISOU 446 C LEU A 56 2943 3367 2860 -226 -235 -89 C -ATOM 447 O LEU A 56 21.543 9.578 7.035 1.00 23.86 O -ANISOU 447 O LEU A 56 2916 3291 2860 -201 -208 -118 O -ATOM 448 CB LEU A 56 22.511 11.616 9.080 1.00 25.48 C -ANISOU 448 CB LEU A 56 3183 3493 3006 -313 -355 -165 C -ATOM 449 CG LEU A 56 21.631 11.402 10.315 1.00 26.50 C -ANISOU 449 CG LEU A 56 3363 3637 3069 -297 -334 -238 C -ATOM 450 CD1 LEU A 56 22.473 10.977 11.509 1.00 25.82 C -ANISOU 450 CD1 LEU A 56 3273 3617 2921 -335 -369 -199 C -ATOM 451 CD2 LEU A 56 20.855 12.669 10.642 1.00 28.04 C -ANISOU 451 CD2 LEU A 56 3624 3771 3257 -301 -359 -338 C -ATOM 452 N ASP A 57 22.220 8.206 8.674 1.00 22.78 N -ANISOU 452 N ASP A 57 2763 3236 2659 -205 -201 -66 N -ATOM 453 CA ASP A 57 21.299 7.140 8.324 1.00 19.73 C -ANISOU 453 CA ASP A 57 2377 2839 2278 -155 -132 -78 C -ATOM 454 C ASP A 57 20.175 7.147 9.360 1.00 26.07 C -ANISOU 454 C ASP A 57 3222 3647 3036 -153 -117 -142 C -ATOM 455 O ASP A 57 20.420 6.985 10.554 1.00 25.33 O -ANISOU 455 O ASP A 57 3139 3597 2890 -174 -134 -134 O -ATOM 456 CB ASP A 57 22.042 5.806 8.298 1.00 21.83 C -ANISOU 456 CB ASP A 57 2604 3138 2553 -131 -104 1 C -ATOM 457 CG ASP A 57 21.155 4.646 7.916 1.00 28.82 C -ANISOU 457 CG ASP A 57 3498 4002 3451 -87 -42 -9 C -ATOM 458 OD1 ASP A 57 20.096 4.885 7.304 1.00 31.73 O -ANISOU 458 OD1 ASP A 57 3890 4332 3832 -75 -19 -65 O -ATOM 459 OD2 ASP A 57 21.523 3.490 8.227 1.00 31.78 O -ANISOU 459 OD2 ASP A 57 3855 4393 3826 -66 -20 44 O -ATOM 460 N THR A 58 18.946 7.351 8.890 1.00 26.42 N -ANISOU 460 N THR A 58 3286 3655 3097 -129 -84 -201 N -ATOM 461 CA THR A 58 17.826 7.654 9.767 1.00 25.52 C -ANISOU 461 CA THR A 58 3205 3546 2944 -122 -66 -268 C -ATOM 462 C THR A 58 16.886 6.466 9.944 1.00 26.85 C -ANISOU 462 C THR A 58 3364 3734 3104 -97 -7 -258 C -ATOM 463 O THR A 58 16.987 5.478 9.225 1.00 28.90 O -ANISOU 463 O THR A 58 3601 3984 3398 -82 17 -212 O -ATOM 464 CB THR A 58 17.032 8.857 9.230 1.00 21.78 C -ANISOU 464 CB THR A 58 2754 3021 2501 -111 -74 -337 C -ATOM 465 OG1 THR A 58 16.397 8.504 7.993 1.00 18.84 O -ANISOU 465 OG1 THR A 58 2361 2617 2181 -85 -44 -329 O -ATOM 466 CG2 THR A 58 17.963 10.052 9.017 1.00 19.87 C -ANISOU 466 CG2 THR A 58 2525 2748 2275 -145 -140 -340 C -ATOM 467 N ALA A 59 15.971 6.574 10.907 1.00 21.14 N -ANISOU 467 N ALA A 59 2659 3038 2335 -91 17 -302 N -ATOM 468 CA ALA A 59 15.008 5.513 11.173 1.00 23.96 C -ANISOU 468 CA ALA A 59 3000 3419 2683 -76 70 -285 C -ATOM 469 C ALA A 59 13.878 5.524 10.148 1.00 23.22 C -ANISOU 469 C ALA A 59 2894 3285 2645 -52 99 -311 C -ATOM 470 O ALA A 59 13.520 6.576 9.621 1.00 21.29 O -ANISOU 470 O ALA A 59 2657 3005 2426 -40 86 -361 O -ATOM 471 CB ALA A 59 14.442 5.653 12.587 1.00 24.66 C -ANISOU 471 CB ALA A 59 3106 3568 2696 -80 90 -315 C -ATOM 472 N GLY A 60 13.315 4.354 9.870 1.00 26.88 N -ANISOU 472 N GLY A 60 3336 3749 3128 -49 132 -273 N -ATOM 473 CA GLY A 60 12.179 4.256 8.966 1.00 23.49 C -ANISOU 473 CA GLY A 60 2891 3288 2745 -36 154 -291 C -ATOM 474 C GLY A 60 11.011 5.043 9.525 1.00 25.70 C -ANISOU 474 C GLY A 60 3165 3593 3009 -20 178 -344 C -ATOM 475 O GLY A 60 10.228 5.646 8.794 1.00 29.66 O -ANISOU 475 O GLY A 60 3654 4065 3552 -2 179 -375 O -ATOM 476 N GLN A 61 10.913 5.053 10.844 1.00 29.92 N -ANISOU 476 N GLN A 61 3705 4184 3480 -21 198 -351 N -ATOM 477 CA GLN A 61 9.816 5.708 11.532 1.00 41.56 C -ANISOU 477 CA GLN A 61 5171 5693 4926 5 235 -403 C -ATOM 478 C GLN A 61 10.341 6.371 12.795 1.00 44.11 C -ANISOU 478 C GLN A 61 5531 6058 5169 6 230 -442 C -ATOM 479 O GLN A 61 10.928 5.714 13.652 1.00 45.94 O -ANISOU 479 O GLN A 61 5773 6340 5344 -20 228 -403 O -ATOM 480 CB GLN A 61 8.758 4.671 11.892 1.00 47.65 C -ANISOU 480 CB GLN A 61 5901 6512 5691 -1 285 -360 C -ATOM 481 CG GLN A 61 7.377 5.222 12.116 1.00 54.28 C -ANISOU 481 CG GLN A 61 6708 7383 6534 33 331 -398 C -ATOM 482 CD GLN A 61 6.323 4.129 12.090 1.00 60.45 C -ANISOU 482 CD GLN A 61 7434 8199 7334 15 368 -337 C -ATOM 483 OE1 GLN A 61 6.733 2.913 11.730 1.00 65.68 O -ANISOU 483 OE1 GLN A 61 8054 8905 7997 39 414 -349 O -ATOM 484 NE2 GLN A 61 5.155 4.375 12.384 1.00 59.01 N -ANISOU 484 NE2 GLN A 61 7251 7995 7173 -26 349 -270 N -ATOM 485 N GLU A 62 10.141 7.677 12.900 1.00 44.59 N -ANISOU 485 N GLU A 62 5619 6096 5226 34 222 -520 N -ATOM 486 CA GLU A 62 10.572 8.416 14.074 1.00 47.70 C -ANISOU 486 CA GLU A 62 6063 6522 5539 34 212 -575 C -ATOM 487 C GLU A 62 9.409 8.531 15.059 1.00 53.47 C -ANISOU 487 C GLU A 62 6787 7320 6211 71 281 -617 C -ATOM 488 O GLU A 62 8.277 8.823 14.669 1.00 53.86 O -ANISOU 488 O GLU A 62 6802 7358 6303 115 322 -642 O -ATOM 489 CB GLU A 62 11.063 9.803 13.661 1.00 49.00 C -ANISOU 489 CB GLU A 62 6271 6613 5735 42 160 -640 C -ATOM 490 CG GLU A 62 12.171 10.369 14.527 1.00 51.39 C -ANISOU 490 CG GLU A 62 6633 6924 5970 8 108 -669 C -ATOM 491 CD GLU A 62 13.490 9.638 14.353 1.00 49.52 C -ANISOU 491 CD GLU A 62 6385 6698 5733 -46 58 -586 C -ATOM 492 OE1 GLU A 62 13.947 9.011 15.333 1.00 51.75 O -ANISOU 492 OE1 GLU A 62 6675 7048 5941 -74 57 -554 O -ATOM 493 OE2 GLU A 62 14.075 9.701 13.246 1.00 43.23 O -ANISOU 493 OE2 GLU A 62 5570 5846 5008 -59 22 -550 O -ATOM 494 N GLU A 63 9.684 8.285 16.335 1.00 60.01 N -ANISOU 494 N GLU A 63 7641 8223 6937 55 295 -619 N -ATOM 495 CA GLU A 63 8.650 8.386 17.359 1.00 66.97 C -ANISOU 495 CA GLU A 63 8517 9184 7744 91 368 -658 C -ATOM 496 C GLU A 63 8.380 9.847 17.698 1.00 67.72 C -ANISOU 496 C GLU A 63 8666 9249 7815 142 374 -778 C -ATOM 497 O GLU A 63 7.252 10.219 18.021 1.00 68.24 O -ANISOU 497 O GLU A 63 8715 9347 7868 202 443 -826 O -ATOM 498 CB GLU A 63 9.051 7.615 18.618 1.00 71.68 C -ANISOU 498 CB GLU A 63 9127 9881 8228 54 381 -615 C -ATOM 499 CG GLU A 63 10.268 8.183 19.324 1.00 75.77 C -ANISOU 499 CG GLU A 63 9719 10400 8669 20 317 -652 C -ATOM 500 CD GLU A 63 11.309 7.128 19.631 1.00 79.86 C -ANISOU 500 CD GLU A 63 10228 10955 9159 -43 274 -551 C -ATOM 501 OE1 GLU A 63 12.507 7.477 19.703 1.00 82.27 O -ANISOU 501 OE1 GLU A 63 10573 11236 9451 -81 199 -552 O -ATOM 502 OE2 GLU A 63 10.929 5.950 19.800 1.00 80.89 O -ANISOU 502 OE2 GLU A 63 10309 11138 9286 -56 311 -465 O -ATOM 503 N TYR A 64 9.421 10.671 17.620 1.00 66.28 N -ANISOU 503 N TYR A 64 8549 9003 7632 120 300 -822 N -ATOM 504 CA TYR A 64 9.286 12.098 17.887 1.00 65.41 C -ANISOU 504 CA TYR A 64 8505 8840 7509 162 290 -939 C -ATOM 505 C TYR A 64 9.540 12.935 16.640 1.00 57.86 C -ANISOU 505 C TYR A 64 7553 7762 6670 169 233 -955 C -ATOM 506 O TYR A 64 10.604 12.849 16.025 1.00 52.56 O -ANISOU 506 O TYR A 64 6887 7046 6038 113 160 -907 O -ATOM 507 CB TYR A 64 10.222 12.532 19.018 1.00 72.69 C -ANISOU 507 CB TYR A 64 9512 9788 8318 124 245 -991 C -ATOM 508 CG TYR A 64 9.857 11.943 20.361 1.00 80.79 C -ANISOU 508 CG TYR A 64 10545 10940 9210 125 306 -992 C -ATOM 509 CD1 TYR A 64 8.673 12.297 20.997 1.00 85.86 C -ANISOU 509 CD1 TYR A 64 11190 11632 9800 199 397 -1065 C -ATOM 510 CD2 TYR A 64 10.696 11.035 20.995 1.00 84.13 C -ANISOU 510 CD2 TYR A 64 10969 11439 9559 57 275 -915 C -ATOM 511 CE1 TYR A 64 8.331 11.761 22.228 1.00 90.04 C -ANISOU 511 CE1 TYR A 64 11724 12289 10197 199 458 -1060 C -ATOM 512 CE2 TYR A 64 10.365 10.493 22.225 1.00 88.33 C -ANISOU 512 CE2 TYR A 64 11507 12091 9962 54 328 -907 C -ATOM 513 CZ TYR A 64 9.182 10.860 22.838 1.00 91.92 C -ANISOU 513 CZ TYR A 64 11966 12601 10358 123 421 -980 C -ATOM 514 OH TYR A 64 8.849 10.324 24.062 1.00 95.58 O -ANISOU 514 OH TYR A 64 12433 13197 10685 118 479 -965 O -ATOM 515 N SER A 65 8.552 13.743 16.275 1.00 58.49 N -ANISOU 515 N SER A 65 7626 7794 6806 239 268 -1016 N -ATOM 516 CA SER A 65 8.671 14.643 15.132 1.00 62.16 C -ANISOU 516 CA SER A 65 8096 8142 7380 250 215 -1030 C -ATOM 517 C SER A 65 9.914 15.530 15.204 1.00 61.55 C -ANISOU 517 C SER A 65 8100 7991 7297 202 122 -1068 C -ATOM 518 O SER A 65 10.551 15.798 14.185 1.00 60.19 O -ANISOU 518 O SER A 65 7920 7747 7204 168 57 -1026 O -ATOM 519 CB SER A 65 7.415 15.508 14.994 1.00 64.47 C -ANISOU 519 CB SER A 65 8378 8395 7722 342 266 -1100 C -ATOM 520 OG SER A 65 6.307 14.731 14.571 1.00 65.72 O -ANISOU 520 OG SER A 65 8443 8608 7919 374 333 -1041 O -ATOM 521 N ALA A 66 10.257 15.981 16.407 1.00 61.14 N -ANISOU 521 N ALA A 66 8125 7961 7146 196 114 -1144 N -ATOM 522 CA ALA A 66 11.380 16.896 16.590 1.00 60.28 C -ANISOU 522 CA ALA A 66 8099 7779 7025 144 18 -1188 C -ATOM 523 C ALA A 66 12.703 16.277 16.141 1.00 61.22 C -ANISOU 523 C ALA A 66 8193 7909 7157 52 -56 -1085 C -ATOM 524 O ALA A 66 13.625 16.981 15.726 1.00 62.41 O -ANISOU 524 O ALA A 66 8376 7986 7350 3 -143 -1081 O -ATOM 525 CB ALA A 66 11.465 17.356 18.043 1.00 58.62 C -ANISOU 525 CB ALA A 66 7981 7606 6688 148 24 -1289 C -ATOM 526 N MET A 67 12.795 14.957 16.220 1.00 60.21 N -ANISOU 526 N MET A 67 8004 7875 6999 31 -21 -998 N -ATOM 527 CA MET A 67 14.004 14.274 15.790 1.00 57.66 C -ANISOU 527 CA MET A 67 7649 7567 6693 -41 -79 -897 C -ATOM 528 C MET A 67 14.109 14.273 14.262 1.00 52.52 C -ANISOU 528 C MET A 67 6944 6849 6161 -41 -98 -836 C -ATOM 529 O MET A 67 15.203 14.385 13.712 1.00 51.27 O -ANISOU 529 O MET A 67 6779 6662 6039 -93 -164 -783 O -ATOM 530 CB MET A 67 14.044 12.853 16.349 1.00 60.35 C -ANISOU 530 CB MET A 67 7945 8016 6970 -57 -36 -823 C -ATOM 531 CG MET A 67 15.437 12.248 16.420 1.00 60.78 C -ANISOU 531 CG MET A 67 7985 8101 7008 -128 -99 -735 C -ATOM 532 SD MET A 67 15.444 10.696 17.337 1.00 95.77 S -ANISOU 532 SD MET A 67 12380 12654 11356 -142 -54 -655 S -ATOM 533 CE MET A 67 17.141 10.173 17.110 1.00 62.27 C -ANISOU 533 CE MET A 67 8109 8421 7131 -212 -137 -547 C -ATOM 534 N ARG A 68 12.970 14.153 13.582 1.00 50.99 N -ANISOU 534 N ARG A 68 6710 6639 6026 17 -39 -841 N -ATOM 535 CA ARG A 68 12.935 14.258 12.124 1.00 52.41 C -ANISOU 535 CA ARG A 68 6847 6758 6310 20 -57 -793 C -ATOM 536 C ARG A 68 13.284 15.679 11.689 1.00 46.45 C -ANISOU 536 C ARG A 68 6137 5902 5610 13 -124 -836 C -ATOM 537 O ARG A 68 14.052 15.886 10.748 1.00 42.35 O -ANISOU 537 O ARG A 68 5603 5341 5148 -26 -178 -780 O -ATOM 538 CB ARG A 68 11.549 13.911 11.576 1.00 58.93 C -ANISOU 538 CB ARG A 68 7621 7589 7180 79 11 -792 C -ATOM 539 CG ARG A 68 10.903 12.679 12.170 1.00 66.43 C -ANISOU 539 CG ARG A 68 8532 8631 8077 92 82 -763 C -ATOM 540 CD ARG A 68 9.431 12.945 12.490 1.00 74.35 C -ANISOU 540 CD ARG A 68 9517 9650 9082 160 151 -816 C -ATOM 541 NE ARG A 68 8.506 12.061 11.782 1.00 76.97 N -ANISOU 541 NE ARG A 68 9774 10009 9461 175 196 -757 N -ATOM 542 CZ ARG A 68 7.312 11.702 12.249 1.00 79.28 C -ANISOU 542 CZ ARG A 68 10027 10360 9737 215 266 -764 C -ATOM 543 NH1 ARG A 68 6.901 12.139 13.433 1.00 79.63 N -ANISOU 543 NH1 ARG A 68 10097 10446 9711 253 311 -830 N -ATOM 544 NH2 ARG A 68 6.532 10.896 11.540 1.00 81.09 N -ANISOU 544 NH2 ARG A 68 10188 10608 10015 214 292 -704 N -ATOM 545 N ASP A 69 12.701 16.658 12.371 1.00 43.89 N -ANISOU 545 N ASP A 69 5870 5538 5269 53 -117 -935 N -ATOM 546 CA ASP A 69 12.924 18.053 12.021 1.00 43.60 C -ANISOU 546 CA ASP A 69 5886 5389 5292 51 -182 -983 C -ATOM 547 C ASP A 69 14.403 18.412 12.138 1.00 40.09 C -ANISOU 547 C ASP A 69 5479 4921 4833 -37 -276 -955 C -ATOM 548 O ASP A 69 14.918 19.212 11.355 1.00 43.82 O -ANISOU 548 O ASP A 69 5959 5311 5378 -68 -344 -932 O -ATOM 549 CB ASP A 69 12.074 18.988 12.893 1.00 47.30 C -ANISOU 549 CB ASP A 69 6420 5816 5734 117 -154 -1106 C -ATOM 550 CG ASP A 69 10.577 18.860 12.616 1.00 49.19 C -ANISOU 550 CG ASP A 69 6610 6068 6014 210 -67 -1125 C -ATOM 551 OD1 ASP A 69 10.197 18.126 11.680 1.00 46.71 O -ANISOU 551 OD1 ASP A 69 6215 5782 5751 214 -41 -1044 O -ATOM 552 OD2 ASP A 69 9.778 19.504 13.332 1.00 51.12 O -ANISOU 552 OD2 ASP A 69 6894 6292 6235 280 -25 -1221 O -ATOM 553 N GLN A 70 15.085 17.812 13.108 1.00 32.52 N -ANISOU 553 N GLN A 70 4536 4039 3781 -80 -284 -947 N -ATOM 554 CA GLN A 70 16.486 18.136 13.345 1.00 35.64 C -ANISOU 554 CA GLN A 70 4961 4424 4158 -168 -378 -917 C -ATOM 555 C GLN A 70 17.393 17.776 12.169 1.00 38.87 C -ANISOU 555 C GLN A 70 5300 4832 4636 -216 -416 -798 C -ATOM 556 O GLN A 70 18.242 18.575 11.775 1.00 44.55 O -ANISOU 556 O GLN A 70 6035 5493 5400 -273 -498 -774 O -ATOM 557 CB GLN A 70 17.002 17.490 14.630 1.00 38.14 C -ANISOU 557 CB GLN A 70 5300 4835 4357 -204 -380 -921 C -ATOM 558 CG GLN A 70 18.488 17.712 14.840 1.00 43.31 C -ANISOU 558 CG GLN A 70 5968 5492 4995 -301 -482 -870 C -ATOM 559 CD GLN A 70 18.927 17.513 16.275 1.00 51.21 C -ANISOU 559 CD GLN A 70 7020 6564 5872 -341 -507 -903 C -ATOM 560 OE1 GLN A 70 18.786 18.409 17.111 1.00 57.02 O -ANISOU 560 OE1 GLN A 70 7851 7262 6553 -349 -541 -1009 O -ATOM 561 NE2 GLN A 70 19.476 16.341 16.568 1.00 52.34 N -ANISOU 561 NE2 GLN A 70 7107 6809 5971 -368 -495 -813 N -ATOM 562 N TYR A 71 17.233 16.581 11.608 1.00 31.94 N -ANISOU 562 N TYR A 71 4348 4021 3768 -196 -358 -723 N -ATOM 563 CA TYR A 71 18.070 16.220 10.470 1.00 30.01 C -ANISOU 563 CA TYR A 71 4041 3780 3583 -231 -382 -619 C -ATOM 564 C TYR A 71 17.626 16.902 9.168 1.00 30.14 C -ANISOU 564 C TYR A 71 4041 3719 3691 -210 -389 -609 C -ATOM 565 O TYR A 71 18.440 17.173 8.289 1.00 31.53 O -ANISOU 565 O TYR A 71 4188 3875 3916 -252 -434 -539 O -ATOM 566 CB TYR A 71 18.254 14.699 10.327 1.00 28.71 C -ANISOU 566 CB TYR A 71 3812 3704 3393 -221 -327 -542 C -ATOM 567 CG TYR A 71 17.036 13.862 9.980 1.00 29.11 C -ANISOU 567 CG TYR A 71 3833 3776 3452 -158 -242 -550 C -ATOM 568 CD1 TYR A 71 16.545 12.911 10.875 1.00 29.55 C -ANISOU 568 CD1 TYR A 71 3885 3899 3443 -136 -187 -560 C -ATOM 569 CD2 TYR A 71 16.412 13.977 8.741 1.00 26.84 C -ANISOU 569 CD2 TYR A 71 3517 3447 3235 -128 -221 -537 C -ATOM 570 CE1 TYR A 71 15.453 12.120 10.555 1.00 29.58 C -ANISOU 570 CE1 TYR A 71 3856 3922 3459 -89 -116 -557 C -ATOM 571 CE2 TYR A 71 15.315 13.189 8.411 1.00 26.51 C -ANISOU 571 CE2 TYR A 71 3446 3426 3201 -81 -154 -538 C -ATOM 572 CZ TYR A 71 14.841 12.261 9.320 1.00 30.67 C -ANISOU 572 CZ TYR A 71 3967 4015 3670 -63 -102 -548 C -ATOM 573 OH TYR A 71 13.750 11.473 8.997 1.00 28.86 O -ANISOU 573 OH TYR A 71 3705 3806 3453 -27 -42 -542 O -ATOM 574 N MET A 72 16.345 17.226 9.064 1.00 27.93 N -ANISOU 574 N MET A 72 3776 3402 3435 -146 -345 -672 N -ATOM 575 CA MET A 72 15.869 17.977 7.912 1.00 29.90 C -ANISOU 575 CA MET A 72 4014 3574 3772 -126 -360 -663 C -ATOM 576 C MET A 72 16.417 19.414 7.877 1.00 31.65 C -ANISOU 576 C MET A 72 4289 3698 4038 -166 -447 -685 C -ATOM 577 O MET A 72 16.532 20.014 6.807 1.00 34.63 O -ANISOU 577 O MET A 72 4648 4019 4490 -180 -484 -639 O -ATOM 578 CB MET A 72 14.341 17.972 7.873 1.00 30.35 C -ANISOU 578 CB MET A 72 4066 3619 3848 -46 -294 -719 C -ATOM 579 CG MET A 72 13.752 16.582 7.664 1.00 28.49 C -ANISOU 579 CG MET A 72 3772 3468 3587 -18 -219 -681 C -ATOM 580 SD MET A 72 11.971 16.593 7.403 1.00 32.43 S -ANISOU 580 SD MET A 72 4242 3957 4123 65 -152 -721 S -ATOM 581 CE MET A 72 11.748 14.980 6.653 1.00 25.81 C -ANISOU 581 CE MET A 72 3334 3198 3276 56 -103 -639 C -ATOM 582 N ARG A 73 16.745 19.966 9.042 1.00 25.79 N -ANISOU 582 N ARG A 73 3616 2935 3249 -188 -485 -756 N -ATOM 583 CA ARG A 73 17.337 21.300 9.107 1.00 28.48 C -ANISOU 583 CA ARG A 73 4018 3174 3629 -237 -579 -781 C -ATOM 584 C ARG A 73 18.815 21.275 8.742 1.00 28.69 C -ANISOU 584 C ARG A 73 4014 3222 3665 -334 -654 -681 C -ATOM 585 O ARG A 73 19.307 22.150 8.033 1.00 29.08 O -ANISOU 585 O ARG A 73 4065 3198 3785 -381 -723 -639 O -ATOM 586 CB ARG A 73 17.197 21.887 10.508 1.00 29.96 C -ANISOU 586 CB ARG A 73 4301 3331 3753 -232 -598 -899 C -ATOM 587 CG ARG A 73 15.802 22.329 10.866 1.00 33.97 C -ANISOU 587 CG ARG A 73 4849 3790 4266 -133 -537 -1007 C -ATOM 588 CD ARG A 73 15.827 23.192 12.111 1.00 37.96 C -ANISOU 588 CD ARG A 73 5467 4240 4716 -134 -572 -1131 C -ATOM 589 NE ARG A 73 16.160 22.409 13.292 1.00 35.95 N -ANISOU 589 NE ARG A 73 5230 4093 4336 -157 -549 -1156 N -ATOM 590 CZ ARG A 73 15.254 21.848 14.081 1.00 33.81 C -ANISOU 590 CZ ARG A 73 4963 3894 3990 -86 -457 -1218 C -ATOM 591 NH1 ARG A 73 15.636 21.150 15.142 1.00 32.19 N -ANISOU 591 NH1 ARG A 73 4774 3790 3668 -116 -444 -1228 N -ATOM 592 NH2 ARG A 73 13.963 21.994 13.806 1.00 32.34 N -ANISOU 592 NH2 ARG A 73 4760 3683 3845 13 -379 -1263 N -ATOM 593 N THR A 74 19.520 20.267 9.242 1.00 26.36 N -ANISOU 593 N THR A 74 3684 3029 3301 -365 -639 -637 N -ATOM 594 CA THR A 74 20.973 20.205 9.126 1.00 29.01 C -ANISOU 594 CA THR A 74 3986 3399 3636 -454 -709 -544 C -ATOM 595 C THR A 74 21.456 19.643 7.788 1.00 29.27 C -ANISOU 595 C THR A 74 3926 3475 3720 -462 -687 -423 C -ATOM 596 O THR A 74 22.466 20.093 7.246 1.00 28.31 O -ANISOU 596 O THR A 74 3774 3344 3638 -530 -751 -342 O -ATOM 597 CB THR A 74 21.574 19.380 10.283 1.00 30.18 C -ANISOU 597 CB THR A 74 4135 3642 3691 -482 -707 -541 C -ATOM 598 OG1 THR A 74 20.980 18.076 10.301 1.00 31.28 O -ANISOU 598 OG1 THR A 74 4228 3864 3792 -417 -609 -529 O -ATOM 599 CG2 THR A 74 21.286 20.061 11.611 1.00 32.03 C -ANISOU 599 CG2 THR A 74 4470 3838 3861 -491 -742 -659 C -ATOM 600 N GLY A 75 20.738 18.660 7.256 1.00 26.64 N -ANISOU 600 N GLY A 75 3549 3191 3382 -395 -598 -411 N -ATOM 601 CA GLY A 75 21.147 18.032 6.013 1.00 25.46 C -ANISOU 601 CA GLY A 75 3322 3087 3266 -394 -569 -310 C -ATOM 602 C GLY A 75 21.281 19.019 4.869 1.00 24.13 C -ANISOU 602 C GLY A 75 3142 2852 3172 -420 -614 -265 C -ATOM 603 O GLY A 75 20.392 19.837 4.639 1.00 20.61 O -ANISOU 603 O GLY A 75 2737 2325 2770 -394 -624 -318 O -ATOM 604 N GLU A 76 22.389 18.945 4.141 1.00 25.20 N -ANISOU 604 N GLU A 76 3219 3028 3327 -470 -640 -159 N -ATOM 605 CA GLU A 76 22.548 19.769 2.944 1.00 27.74 C -ANISOU 605 CA GLU A 76 3519 3305 3715 -499 -676 -96 C -ATOM 606 C GLU A 76 21.934 19.072 1.737 1.00 25.75 C -ANISOU 606 C GLU A 76 3225 3090 3468 -442 -601 -64 C -ATOM 607 O GLU A 76 21.407 19.716 0.836 1.00 27.24 O -ANISOU 607 O GLU A 76 3417 3229 3703 -436 -614 -50 O -ATOM 608 CB GLU A 76 24.019 20.086 2.693 1.00 31.50 C -ANISOU 608 CB GLU A 76 3946 3815 4208 -583 -737 12 C -ATOM 609 CG GLU A 76 24.652 20.939 3.784 1.00 38.66 C -ANISOU 609 CG GLU A 76 4900 4673 5116 -658 -833 -13 C -ATOM 610 CD GLU A 76 26.139 21.145 3.570 1.00 44.33 C -ANISOU 610 CD GLU A 76 5553 5439 5850 -748 -895 108 C -ATOM 611 OE1 GLU A 76 26.856 20.144 3.362 1.00 42.77 O -ANISOU 611 OE1 GLU A 76 5277 5350 5623 -739 -848 184 O -ATOM 612 OE2 GLU A 76 26.587 22.310 3.605 1.00 50.61 O -ANISOU 612 OE2 GLU A 76 6374 6163 6694 -828 -992 130 O -ATOM 613 N GLY A 77 22.000 17.746 1.731 1.00 28.13 N -ANISOU 613 N GLY A 77 3491 3476 3720 -403 -528 -52 N -ATOM 614 CA GLY A 77 21.417 16.962 0.655 1.00 28.92 C -ANISOU 614 CA GLY A 77 3561 3611 3814 -352 -459 -33 C -ATOM 615 C GLY A 77 20.718 15.731 1.192 1.00 29.44 C -ANISOU 615 C GLY A 77 3637 3715 3835 -293 -388 -90 C -ATOM 616 O GLY A 77 21.140 15.163 2.205 1.00 30.51 O -ANISOU 616 O GLY A 77 3774 3885 3934 -296 -380 -103 O -ATOM 617 N PHE A 78 19.652 15.317 0.513 1.00 21.42 N -ANISOU 617 N PHE A 78 2624 2692 2822 -247 -342 -115 N -ATOM 618 CA PHE A 78 18.851 14.194 0.983 1.00 22.44 C -ANISOU 618 CA PHE A 78 2763 2848 2917 -198 -280 -165 C -ATOM 619 C PHE A 78 18.734 13.087 -0.057 1.00 22.62 C -ANISOU 619 C PHE A 78 2758 2914 2921 -171 -224 -132 C -ATOM 620 O PHE A 78 18.350 13.332 -1.200 1.00 21.07 O -ANISOU 620 O PHE A 78 2555 2708 2743 -168 -225 -112 O -ATOM 621 CB PHE A 78 17.454 14.674 1.394 1.00 23.90 C -ANISOU 621 CB PHE A 78 2982 2979 3119 -167 -278 -244 C -ATOM 622 CG PHE A 78 17.469 15.667 2.526 1.00 26.08 C -ANISOU 622 CG PHE A 78 3300 3208 3403 -181 -323 -298 C -ATOM 623 CD1 PHE A 78 17.366 15.239 3.846 1.00 26.15 C -ANISOU 623 CD1 PHE A 78 3331 3240 3364 -170 -303 -349 C -ATOM 624 CD2 PHE A 78 17.610 17.022 2.275 1.00 22.40 C -ANISOU 624 CD2 PHE A 78 2855 2671 2986 -208 -387 -297 C -ATOM 625 CE1 PHE A 78 17.399 16.148 4.896 1.00 26.63 C -ANISOU 625 CE1 PHE A 78 3440 3259 3417 -184 -344 -408 C -ATOM 626 CE2 PHE A 78 17.637 17.943 3.321 1.00 22.04 C -ANISOU 626 CE2 PHE A 78 2860 2570 2944 -221 -431 -357 C -ATOM 627 CZ PHE A 78 17.532 17.505 4.631 1.00 24.47 C -ANISOU 627 CZ PHE A 78 3195 2907 3195 -208 -408 -418 C -ATOM 628 N LEU A 79 19.068 11.867 0.352 1.00 18.32 N -ANISOU 628 N LEU A 79 2203 2416 2341 -151 -179 -126 N -ATOM 629 CA LEU A 79 18.870 10.697 -0.484 1.00 21.73 C -ANISOU 629 CA LEU A 79 2625 2877 2754 -120 -124 -112 C -ATOM 630 C LEU A 79 17.512 10.115 -0.126 1.00 24.15 C -ANISOU 630 C LEU A 79 2956 3165 3055 -92 -96 -173 C -ATOM 631 O LEU A 79 17.323 9.587 0.975 1.00 23.55 O -ANISOU 631 O LEU A 79 2888 3097 2962 -82 -80 -199 O -ATOM 632 CB LEU A 79 19.984 9.674 -0.236 1.00 23.48 C -ANISOU 632 CB LEU A 79 2822 3150 2951 -108 -92 -69 C -ATOM 633 CG LEU A 79 20.506 8.851 -1.414 1.00 23.33 C -ANISOU 633 CG LEU A 79 2784 3164 2916 -83 -47 -28 C -ATOM 634 CD1 LEU A 79 21.291 9.716 -2.407 1.00 19.19 C -ANISOU 634 CD1 LEU A 79 2230 2661 2401 -108 -69 31 C -ATOM 635 CD2 LEU A 79 21.368 7.697 -0.900 1.00 24.70 C -ANISOU 635 CD2 LEU A 79 2938 3373 3073 -54 -9 1 C -ATOM 636 N CYS A 80 16.564 10.226 -1.053 1.00 21.48 N -ANISOU 636 N CYS A 80 2624 2807 2731 -84 -94 -187 N -ATOM 637 CA CYS A 80 15.186 9.834 -0.788 1.00 19.45 C -ANISOU 637 CA CYS A 80 2379 2533 2479 -65 -75 -234 C -ATOM 638 C CYS A 80 14.895 8.440 -1.313 1.00 23.65 C -ANISOU 638 C CYS A 80 2915 3082 2987 -51 -34 -231 C -ATOM 639 O CYS A 80 14.609 8.259 -2.497 1.00 20.09 O -ANISOU 639 O CYS A 80 2469 2631 2533 -53 -34 -221 O -ATOM 640 CB CYS A 80 14.232 10.853 -1.394 1.00 19.26 C -ANISOU 640 CB CYS A 80 2353 2472 2491 -66 -107 -248 C -ATOM 641 SG CYS A 80 14.407 12.506 -0.658 1.00 29.63 S -ANISOU 641 SG CYS A 80 3676 3740 3843 -76 -159 -266 S -ATOM 642 N VAL A 81 14.952 7.464 -0.407 1.00 24.20 N -ANISOU 642 N VAL A 81 2990 3166 3039 -40 -3 -240 N -ATOM 643 CA VAL A 81 14.926 6.054 -0.772 1.00 22.15 C -ANISOU 643 CA VAL A 81 2742 2912 2762 -28 33 -234 C -ATOM 644 C VAL A 81 13.540 5.405 -0.662 1.00 23.57 C -ANISOU 644 C VAL A 81 2930 3077 2949 -30 44 -262 C -ATOM 645 O VAL A 81 12.860 5.506 0.365 1.00 19.22 O -ANISOU 645 O VAL A 81 2369 2530 2404 -30 48 -281 O -ATOM 646 CB VAL A 81 15.922 5.250 0.095 1.00 17.27 C -ANISOU 646 CB VAL A 81 2120 2314 2127 -16 56 -209 C -ATOM 647 CG1 VAL A 81 16.041 3.828 -0.421 1.00 16.92 C -ANISOU 647 CG1 VAL A 81 2094 2261 2074 4 92 -201 C -ATOM 648 CG2 VAL A 81 17.293 5.932 0.107 1.00 12.36 C -ANISOU 648 CG2 VAL A 81 1478 1716 1503 -20 39 -171 C -ATOM 649 N PHE A 82 13.125 4.741 -1.734 1.00 20.01 N -ANISOU 649 N PHE A 82 2497 2614 2494 -34 49 -265 N -ATOM 650 CA PHE A 82 11.968 3.869 -1.665 1.00 19.28 C -ANISOU 650 CA PHE A 82 2412 2507 2408 -46 56 -281 C -ATOM 651 C PHE A 82 12.389 2.490 -2.155 1.00 19.90 C -ANISOU 651 C PHE A 82 2527 2568 2469 -41 79 -277 C -ATOM 652 O PHE A 82 13.462 2.340 -2.740 1.00 21.90 O -ANISOU 652 O PHE A 82 2795 2824 2702 -21 92 -266 O -ATOM 653 CB PHE A 82 10.784 4.440 -2.468 1.00 19.02 C -ANISOU 653 CB PHE A 82 2369 2467 2393 -65 25 -292 C -ATOM 654 CG PHE A 82 10.977 4.414 -3.969 1.00 14.87 C -ANISOU 654 CG PHE A 82 1867 1936 1846 -75 8 -287 C -ATOM 655 CD1 PHE A 82 10.528 3.335 -4.726 1.00 15.96 C -ANISOU 655 CD1 PHE A 82 2039 2059 1967 -93 7 -299 C -ATOM 656 CD2 PHE A 82 11.581 5.477 -4.625 1.00 13.95 C -ANISOU 656 CD2 PHE A 82 1743 1832 1726 -72 -11 -271 C -ATOM 657 CE1 PHE A 82 10.696 3.311 -6.118 1.00 16.39 C -ANISOU 657 CE1 PHE A 82 2124 2116 1988 -103 -8 -300 C -ATOM 658 CE2 PHE A 82 11.748 5.463 -6.016 1.00 16.94 C -ANISOU 658 CE2 PHE A 82 2143 2218 2074 -83 -24 -261 C -ATOM 659 CZ PHE A 82 11.306 4.375 -6.762 1.00 12.87 C -ANISOU 659 CZ PHE A 82 1667 1694 1530 -97 -21 -279 C -ATOM 660 N ALA A 83 11.571 1.477 -1.902 1.00 16.72 N -ANISOU 660 N ALA A 83 2136 2143 2073 -57 85 -284 N -ATOM 661 CA ALA A 83 11.858 0.161 -2.451 1.00 16.33 C -ANISOU 661 CA ALA A 83 2133 2058 2013 -53 100 -288 C -ATOM 662 C ALA A 83 10.911 -0.074 -3.615 1.00 18.57 C -ANISOU 662 C ALA A 83 2444 2320 2291 -85 72 -312 C -ATOM 663 O ALA A 83 9.727 0.248 -3.524 1.00 18.55 O -ANISOU 663 O ALA A 83 2415 2325 2307 -118 45 -312 O -ATOM 664 CB ALA A 83 11.701 -0.918 -1.392 1.00 16.37 C -ANISOU 664 CB ALA A 83 2141 2043 2034 -56 118 -272 C -ATOM 665 N ILE A 84 11.432 -0.614 -4.715 1.00 14.94 N -ANISOU 665 N ILE A 84 2035 1840 1801 -75 78 -330 N -ATOM 666 CA ILE A 84 10.624 -0.796 -5.920 1.00 19.02 C -ANISOU 666 CA ILE A 84 2587 2342 2297 -110 44 -355 C -ATOM 667 C ILE A 84 9.502 -1.812 -5.746 1.00 20.99 C -ANISOU 667 C ILE A 84 2858 2550 2569 -156 20 -365 C -ATOM 668 O ILE A 84 8.613 -1.909 -6.594 1.00 22.83 O -ANISOU 668 O ILE A 84 3110 2773 2791 -200 -22 -379 O -ATOM 669 CB ILE A 84 11.475 -1.211 -7.128 1.00 22.45 C -ANISOU 669 CB ILE A 84 3082 2767 2680 -86 62 -381 C -ATOM 670 CG1 ILE A 84 12.126 -2.573 -6.865 1.00 25.70 C -ANISOU 670 CG1 ILE A 84 3545 3127 3094 -53 100 -397 C -ATOM 671 CG2 ILE A 84 12.501 -0.136 -7.441 1.00 20.76 C -ANISOU 671 CG2 ILE A 84 2838 2605 2445 -52 80 -359 C -ATOM 672 CD1 ILE A 84 12.623 -3.271 -8.108 1.00 28.46 C -ANISOU 672 CD1 ILE A 84 3972 3451 3391 -30 118 -440 C -ATOM 673 N ASN A 85 9.544 -2.569 -4.653 1.00 23.06 N -ANISOU 673 N ASN A 85 3113 2787 2860 -151 41 -349 N -ATOM 674 CA ASN A 85 8.482 -3.525 -4.336 1.00 21.17 C -ANISOU 674 CA ASN A 85 2884 2510 2650 -202 17 -342 C -ATOM 675 C ASN A 85 7.676 -3.056 -3.127 1.00 23.62 C -ANISOU 675 C ASN A 85 3117 2861 2995 -220 17 -304 C -ATOM 676 O ASN A 85 7.082 -3.859 -2.408 1.00 29.12 O -ANISOU 676 O ASN A 85 3805 3539 3719 -251 15 -279 O -ATOM 677 CB ASN A 85 9.075 -4.908 -4.061 1.00 20.69 C -ANISOU 677 CB ASN A 85 2881 2383 2598 -186 39 -346 C -ATOM 678 CG ASN A 85 9.850 -4.961 -2.755 1.00 26.35 C -ANISOU 678 CG ASN A 85 3562 3116 3334 -146 80 -308 C -ATOM 679 OD1 ASN A 85 10.396 -3.956 -2.300 1.00 27.57 O -ANISOU 679 OD1 ASN A 85 3669 3327 3478 -114 98 -294 O -ATOM 680 ND2 ASN A 85 9.894 -6.138 -2.140 1.00 31.38 N -ANISOU 680 ND2 ASN A 85 4225 3701 3999 -151 87 -287 N -ATOM 681 N ASN A 86 7.679 -1.749 -2.901 1.00 19.66 N -ANISOU 681 N ASN A 86 2563 2415 2492 -199 21 -299 N -ATOM 682 CA ASN A 86 6.988 -1.155 -1.770 1.00 18.21 C -ANISOU 682 CA ASN A 86 2311 2275 2333 -201 31 -274 C -ATOM 683 C ASN A 86 6.336 0.150 -2.207 1.00 18.22 C -ANISOU 683 C ASN A 86 2267 2312 2343 -200 7 -280 C -ATOM 684 O ASN A 86 6.946 1.220 -2.129 1.00 14.60 O -ANISOU 684 O ASN A 86 1796 1874 1877 -164 16 -288 O -ATOM 685 CB ASN A 86 7.961 -0.906 -0.609 1.00 17.79 C -ANISOU 685 CB ASN A 86 2246 2245 2270 -159 71 -264 C -ATOM 686 CG ASN A 86 7.253 -0.457 0.661 1.00 20.21 C -ANISOU 686 CG ASN A 86 2493 2598 2588 -160 88 -245 C -ATOM 687 OD1 ASN A 86 6.155 0.087 0.610 1.00 21.20 O -ANISOU 687 OD1 ASN A 86 2575 2749 2732 -174 76 -244 O -ATOM 688 ND2 ASN A 86 7.890 -0.668 1.806 1.00 21.35 N -ANISOU 688 ND2 ASN A 86 2634 2761 2718 -141 118 -228 N -ATOM 689 N THR A 87 5.091 0.047 -2.666 1.00 17.83 N -ANISOU 689 N THR A 87 2193 2267 2316 -243 -27 -269 N -ATOM 690 CA THR A 87 4.328 1.190 -3.160 1.00 18.14 C -ANISOU 690 CA THR A 87 2184 2336 2373 -242 -56 -264 C -ATOM 691 C THR A 87 4.181 2.285 -2.114 1.00 21.83 C -ANISOU 691 C THR A 87 2592 2840 2861 -198 -26 -260 C -ATOM 692 O THR A 87 4.359 3.471 -2.415 1.00 22.69 O -ANISOU 692 O THR A 87 2687 2957 2976 -169 -36 -269 O -ATOM 693 CB THR A 87 2.931 0.748 -3.636 1.00 18.89 C -ANISOU 693 CB THR A 87 2248 2435 2495 -300 -99 -239 C -ATOM 694 OG1 THR A 87 3.077 -0.156 -4.736 1.00 17.25 O -ANISOU 694 OG1 THR A 87 2108 2185 2259 -344 -136 -254 O -ATOM 695 CG2 THR A 87 2.084 1.946 -4.074 1.00 21.22 C -ANISOU 695 CG2 THR A 87 2479 2764 2818 -293 -129 -223 C -ATOM 696 N LYS A 88 3.855 1.890 -0.885 1.00 21.33 N -ANISOU 696 N LYS A 88 2500 2800 2806 -194 10 -247 N -ATOM 697 CA LYS A 88 3.698 2.854 0.198 1.00 22.88 C -ANISOU 697 CA LYS A 88 2649 3034 3009 -150 45 -254 C -ATOM 698 C LYS A 88 4.975 3.679 0.394 1.00 20.86 C -ANISOU 698 C LYS A 88 2429 2768 2729 -108 55 -284 C -ATOM 699 O LYS A 88 4.905 4.898 0.567 1.00 22.20 O -ANISOU 699 O LYS A 88 2578 2945 2912 -73 55 -302 O -ATOM 700 CB LYS A 88 3.288 2.148 1.494 1.00 27.52 C -ANISOU 700 CB LYS A 88 3208 3656 3591 -156 87 -232 C -ATOM 701 CG LYS A 88 3.358 3.002 2.762 1.00 28.29 C -ANISOU 701 CG LYS A 88 3278 3798 3673 -107 132 -251 C -ATOM 702 CD LYS A 88 2.159 3.915 2.908 1.00 36.43 C -ANISOU 702 CD LYS A 88 4240 4864 4737 -79 143 -252 C -ATOM 703 CE LYS A 88 1.976 4.339 4.365 1.00 38.59 C -ANISOU 703 CE LYS A 88 4485 5191 4984 -37 201 -268 C -ATOM 704 NZ LYS A 88 3.252 4.824 4.968 1.00 40.86 N -ANISOU 704 NZ LYS A 88 4832 5466 5228 -9 211 -309 N -ATOM 705 N SER A 89 6.136 3.026 0.351 1.00 17.98 N -ANISOU 705 N SER A 89 2116 2382 2335 -112 62 -286 N -ATOM 706 CA SER A 89 7.403 3.737 0.519 1.00 17.17 C -ANISOU 706 CA SER A 89 2039 2275 2211 -81 66 -302 C -ATOM 707 C SER A 89 7.622 4.761 -0.594 1.00 17.96 C -ANISOU 707 C SER A 89 2145 2358 2322 -74 32 -310 C -ATOM 708 O SER A 89 8.232 5.804 -0.371 1.00 20.02 O -ANISOU 708 O SER A 89 2406 2618 2584 -52 26 -321 O -ATOM 709 CB SER A 89 8.584 2.765 0.589 1.00 15.11 C -ANISOU 709 CB SER A 89 1820 1998 1922 -83 80 -291 C -ATOM 710 OG SER A 89 8.875 2.214 -0.681 1.00 15.95 O -ANISOU 710 OG SER A 89 1963 2074 2025 -96 63 -291 O -ATOM 711 N PHE A 90 7.118 4.460 -1.789 1.00 18.60 N -ANISOU 711 N PHE A 90 2232 2425 2410 -100 3 -302 N -ATOM 712 CA PHE A 90 7.215 5.380 -2.923 1.00 15.99 C -ANISOU 712 CA PHE A 90 1904 2086 2085 -100 -34 -298 C -ATOM 713 C PHE A 90 6.304 6.573 -2.686 1.00 15.43 C -ANISOU 713 C PHE A 90 1784 2021 2058 -82 -50 -298 C -ATOM 714 O PHE A 90 6.687 7.719 -2.906 1.00 18.18 O -ANISOU 714 O PHE A 90 2130 2357 2420 -63 -69 -298 O -ATOM 715 CB PHE A 90 6.830 4.659 -4.225 1.00 19.59 C -ANISOU 715 CB PHE A 90 2384 2533 2525 -137 -63 -290 C -ATOM 716 CG PHE A 90 6.745 5.567 -5.436 1.00 20.98 C -ANISOU 716 CG PHE A 90 2559 2712 2702 -145 -106 -276 C -ATOM 717 CD1 PHE A 90 7.891 6.099 -6.004 1.00 19.39 C -ANISOU 717 CD1 PHE A 90 2384 2511 2474 -133 -107 -270 C -ATOM 718 CD2 PHE A 90 5.518 5.874 -6.010 1.00 19.45 C -ANISOU 718 CD2 PHE A 90 2330 2525 2535 -168 -147 -258 C -ATOM 719 CE1 PHE A 90 7.820 6.920 -7.115 1.00 19.38 C -ANISOU 719 CE1 PHE A 90 2378 2516 2469 -145 -147 -246 C -ATOM 720 CE2 PHE A 90 5.437 6.705 -7.127 1.00 18.68 C -ANISOU 720 CE2 PHE A 90 2229 2432 2437 -177 -192 -234 C -ATOM 721 CZ PHE A 90 6.588 7.226 -7.678 1.00 21.34 C -ANISOU 721 CZ PHE A 90 2597 2767 2742 -167 -192 -229 C -ATOM 722 N GLU A 91 5.089 6.297 -2.235 1.00 15.94 N -ANISOU 722 N GLU A 91 1806 2103 2148 -86 -42 -292 N -ATOM 723 CA GLU A 91 4.137 7.354 -1.914 1.00 20.75 C -ANISOU 723 CA GLU A 91 2360 2720 2804 -55 -47 -292 C -ATOM 724 C GLU A 91 4.640 8.253 -0.778 1.00 22.20 C -ANISOU 724 C GLU A 91 2547 2900 2989 -8 -17 -325 C -ATOM 725 O GLU A 91 4.311 9.438 -0.723 1.00 21.86 O -ANISOU 725 O GLU A 91 2482 2840 2982 28 -28 -336 O -ATOM 726 CB GLU A 91 2.774 6.740 -1.572 1.00 21.08 C -ANISOU 726 CB GLU A 91 2345 2793 2869 -69 -35 -272 C -ATOM 727 CG GLU A 91 2.174 5.950 -2.730 1.00 20.81 C -ANISOU 727 CG GLU A 91 2311 2759 2838 -126 -80 -241 C -ATOM 728 CD GLU A 91 0.968 5.125 -2.336 1.00 24.32 C -ANISOU 728 CD GLU A 91 2702 3236 3305 -156 -72 -212 C -ATOM 729 OE1 GLU A 91 0.795 4.830 -1.132 1.00 26.42 O -ANISOU 729 OE1 GLU A 91 2944 3527 3569 -139 -22 -215 O -ATOM 730 OE2 GLU A 91 0.191 4.770 -3.243 1.00 22.17 O -ANISOU 730 OE2 GLU A 91 2410 2967 3047 -203 -120 -182 O -ATOM 731 N ASP A 92 5.444 7.689 0.121 1.00 21.38 N -ANISOU 731 N ASP A 92 2473 2806 2844 -8 17 -341 N -ATOM 732 CA ASP A 92 6.000 8.448 1.244 1.00 20.71 C -ANISOU 732 CA ASP A 92 2401 2721 2746 26 39 -375 C -ATOM 733 C ASP A 92 6.971 9.539 0.789 1.00 23.88 C -ANISOU 733 C ASP A 92 2834 3084 3157 34 3 -384 C -ATOM 734 O ASP A 92 7.188 10.524 1.491 1.00 26.33 O -ANISOU 734 O ASP A 92 3154 3377 3473 61 2 -416 O -ATOM 735 CB ASP A 92 6.730 7.516 2.213 1.00 22.55 C -ANISOU 735 CB ASP A 92 2659 2979 2930 15 72 -376 C -ATOM 736 CG ASP A 92 5.789 6.789 3.154 1.00 28.97 C -ANISOU 736 CG ASP A 92 3438 3836 3733 16 115 -371 C -ATOM 737 OD1 ASP A 92 4.593 7.139 3.194 1.00 32.08 O -ANISOU 737 OD1 ASP A 92 3784 4246 4158 34 125 -372 O -ATOM 738 OD2 ASP A 92 6.252 5.876 3.867 1.00 33.30 O -ANISOU 738 OD2 ASP A 92 4002 4407 4244 0 138 -358 O -ATOM 739 N ILE A 93 7.572 9.349 -0.379 1.00 22.33 N -ANISOU 739 N ILE A 93 2656 2873 2956 5 -28 -355 N -ATOM 740 CA ILE A 93 8.560 10.292 -0.883 1.00 22.37 C -ANISOU 740 CA ILE A 93 2684 2850 2967 2 -63 -347 C -ATOM 741 C ILE A 93 7.994 11.713 -0.931 1.00 26.14 C -ANISOU 741 C ILE A 93 3145 3289 3497 29 -92 -359 C -ATOM 742 O ILE A 93 8.637 12.666 -0.504 1.00 27.78 O -ANISOU 742 O ILE A 93 3374 3465 3715 38 -109 -375 O -ATOM 743 CB ILE A 93 9.065 9.880 -2.280 1.00 24.76 C -ANISOU 743 CB ILE A 93 2999 3154 3253 -28 -85 -309 C -ATOM 744 CG1 ILE A 93 9.734 8.501 -2.220 1.00 20.66 C -ANISOU 744 CG1 ILE A 93 2504 2659 2688 -43 -53 -304 C -ATOM 745 CG2 ILE A 93 10.045 10.921 -2.818 1.00 24.90 C -ANISOU 745 CG2 ILE A 93 3031 3151 3279 -36 -120 -287 C -ATOM 746 CD1 ILE A 93 10.941 8.456 -1.279 1.00 18.05 C -ANISOU 746 CD1 ILE A 93 2188 2336 2333 -36 -35 -308 C -ATOM 747 N HIS A 94 6.780 11.852 -1.443 1.00 29.69 N -ANISOU 747 N HIS A 94 3558 3737 3984 40 -101 -347 N -ATOM 748 CA HIS A 94 6.147 13.162 -1.498 1.00 31.35 C -ANISOU 748 CA HIS A 94 3749 3907 4256 76 -127 -354 C -ATOM 749 C HIS A 94 6.124 13.841 -0.129 1.00 31.02 C -ANISOU 749 C HIS A 94 3719 3846 4221 122 -99 -411 C -ATOM 750 O HIS A 94 6.423 15.032 -0.005 1.00 29.93 O -ANISOU 750 O HIS A 94 3602 3652 4117 142 -127 -430 O -ATOM 751 CB HIS A 94 4.724 13.062 -2.044 1.00 32.96 C -ANISOU 751 CB HIS A 94 3896 4125 4500 88 -133 -329 C -ATOM 752 CG HIS A 94 4.034 14.386 -2.130 1.00 42.59 C -ANISOU 752 CG HIS A 94 5089 5299 5793 136 -158 -329 C -ATOM 753 ND1 HIS A 94 4.436 15.373 -3.007 1.00 46.99 N -ANISOU 753 ND1 HIS A 94 5661 5808 6386 128 -215 -297 N -ATOM 754 CD2 HIS A 94 3.004 14.903 -1.424 1.00 45.60 C -ANISOU 754 CD2 HIS A 94 5430 5675 6221 196 -131 -354 C -ATOM 755 CE1 HIS A 94 3.671 16.438 -2.844 1.00 46.96 C -ANISOU 755 CE1 HIS A 94 5629 5759 6454 182 -227 -303 C -ATOM 756 NE2 HIS A 94 2.793 16.179 -1.891 1.00 49.50 N -ANISOU 756 NE2 HIS A 94 5917 6107 6783 229 -174 -341 N -ATOM 757 N HIS A 95 5.774 13.076 0.898 1.00 29.48 N -ANISOU 757 N HIS A 95 3515 3695 3991 134 -46 -440 N -ATOM 758 CA HIS A 95 5.673 13.609 2.250 1.00 31.42 C -ANISOU 758 CA HIS A 95 3775 3938 4226 178 -11 -500 C -ATOM 759 C HIS A 95 7.031 14.004 2.829 1.00 32.12 C -ANISOU 759 C HIS A 95 3926 4002 4278 159 -30 -527 C -ATOM 760 O HIS A 95 7.129 14.989 3.556 1.00 31.59 O -ANISOU 760 O HIS A 95 3888 3896 4217 190 -34 -579 O -ATOM 761 CB HIS A 95 4.961 12.611 3.163 1.00 36.69 C -ANISOU 761 CB HIS A 95 4413 4674 4856 189 51 -509 C -ATOM 762 CG HIS A 95 3.640 12.150 2.628 1.00 44.53 C -ANISOU 762 CG HIS A 95 5337 5696 5885 195 64 -472 C -ATOM 763 ND1 HIS A 95 2.499 12.922 2.696 1.00 47.95 N -ANISOU 763 ND1 HIS A 95 5721 6123 6374 252 77 -482 N -ATOM 764 CD2 HIS A 95 3.284 11.006 1.998 1.00 42.97 C -ANISOU 764 CD2 HIS A 95 5111 5533 5681 150 61 -423 C -ATOM 765 CE1 HIS A 95 1.495 12.269 2.139 1.00 47.50 C -ANISOU 765 CE1 HIS A 95 5600 6104 6343 237 79 -432 C -ATOM 766 NE2 HIS A 95 1.944 11.103 1.707 1.00 44.36 N -ANISOU 766 NE2 HIS A 95 5219 5728 5907 171 66 -399 N -ATOM 767 N TYR A 96 8.075 13.242 2.518 1.00 32.86 N -ANISOU 767 N TYR A 96 4037 4117 4332 109 -41 -493 N -ATOM 768 CA TYR A 96 9.416 13.618 2.955 1.00 29.52 C -ANISOU 768 CA TYR A 96 3659 3677 3880 84 -68 -503 C -ATOM 769 C TYR A 96 9.846 14.922 2.296 1.00 25.87 C -ANISOU 769 C TYR A 96 3216 3146 3468 77 -127 -495 C -ATOM 770 O TYR A 96 10.394 15.803 2.958 1.00 24.09 O -ANISOU 770 O TYR A 96 3029 2880 3243 77 -153 -531 O -ATOM 771 CB TYR A 96 10.444 12.528 2.641 1.00 30.14 C -ANISOU 771 CB TYR A 96 3741 3794 3916 40 -65 -456 C -ATOM 772 CG TYR A 96 10.376 11.333 3.558 1.00 29.36 C -ANISOU 772 CG TYR A 96 3638 3751 3765 39 -17 -461 C -ATOM 773 CD1 TYR A 96 10.742 11.433 4.898 1.00 29.69 C -ANISOU 773 CD1 TYR A 96 3703 3813 3763 43 -4 -495 C -ATOM 774 CD2 TYR A 96 9.964 10.100 3.081 1.00 24.88 C -ANISOU 774 CD2 TYR A 96 3048 3214 3192 30 9 -428 C -ATOM 775 CE1 TYR A 96 10.678 10.334 5.737 1.00 25.85 C -ANISOU 775 CE1 TYR A 96 3211 3382 3228 39 37 -487 C -ATOM 776 CE2 TYR A 96 9.905 9.004 3.903 1.00 26.28 C -ANISOU 776 CE2 TYR A 96 3221 3434 3329 25 48 -422 C -ATOM 777 CZ TYR A 96 10.255 9.126 5.230 1.00 25.35 C -ANISOU 777 CZ TYR A 96 3120 3342 3169 31 63 -447 C -ATOM 778 OH TYR A 96 10.179 8.022 6.039 1.00 24.62 O -ANISOU 778 OH TYR A 96 3022 3296 3036 23 99 -430 O -ATOM 779 N ARG A 97 9.607 15.042 0.991 1.00 26.35 N -ANISOU 779 N ARG A 97 3252 3191 3568 67 -153 -446 N -ATOM 780 CA ARG A 97 10.030 16.244 0.276 1.00 33.58 C -ANISOU 780 CA ARG A 97 4182 4044 4534 53 -214 -422 C -ATOM 781 C ARG A 97 9.310 17.488 0.794 1.00 32.25 C -ANISOU 781 C ARG A 97 4027 3806 4422 101 -229 -473 C -ATOM 782 O ARG A 97 9.918 18.553 0.924 1.00 31.44 O -ANISOU 782 O ARG A 97 3960 3636 4348 90 -277 -483 O -ATOM 783 CB ARG A 97 9.861 16.109 -1.241 1.00 36.37 C -ANISOU 783 CB ARG A 97 4505 4405 4908 31 -238 -354 C -ATOM 784 CG ARG A 97 10.237 17.389 -1.977 1.00 41.66 C -ANISOU 784 CG ARG A 97 5185 5012 5633 15 -303 -317 C -ATOM 785 CD ARG A 97 10.552 17.165 -3.449 1.00 45.95 C -ANISOU 785 CD ARG A 97 5709 5583 6168 -25 -328 -238 C -ATOM 786 NE ARG A 97 10.832 18.428 -4.136 1.00 49.48 N -ANISOU 786 NE ARG A 97 6159 5970 6669 -43 -391 -191 N -ATOM 787 CZ ARG A 97 12.047 18.942 -4.318 1.00 50.02 C -ANISOU 787 CZ ARG A 97 6244 6025 6735 -88 -426 -151 C -ATOM 788 NH1 ARG A 97 13.123 18.305 -3.877 1.00 49.30 N -ANISOU 788 NH1 ARG A 97 6162 5979 6589 -115 -403 -153 N -ATOM 789 NH2 ARG A 97 12.188 20.096 -4.954 1.00 53.71 N -ANISOU 789 NH2 ARG A 97 6713 6434 7259 -109 -488 -100 N -ATOM 790 N GLU A 98 8.022 17.335 1.101 1.00 31.83 N -ANISOU 790 N GLU A 98 3943 3765 4385 155 -188 -502 N -ATOM 791 CA GLU A 98 7.201 18.423 1.619 1.00 35.94 C -ANISOU 791 CA GLU A 98 4470 4224 4961 219 -187 -555 C -ATOM 792 C GLU A 98 7.661 18.886 2.991 1.00 32.07 C -ANISOU 792 C GLU A 98 4039 3710 4436 237 -174 -636 C -ATOM 793 O GLU A 98 7.811 20.081 3.219 1.00 27.09 O -ANISOU 793 O GLU A 98 3452 2994 3849 257 -212 -675 O -ATOM 794 CB GLU A 98 5.729 18.010 1.695 1.00 44.15 C -ANISOU 794 CB GLU A 98 5450 5304 6022 275 -136 -560 C -ATOM 795 CG GLU A 98 5.050 17.934 0.350 1.00 53.33 C -ANISOU 795 CG GLU A 98 6557 6470 7236 267 -165 -487 C -ATOM 796 CD GLU A 98 5.061 19.265 -0.369 1.00 63.74 C -ANISOU 796 CD GLU A 98 7885 7699 8634 281 -228 -463 C -ATOM 797 OE1 GLU A 98 5.239 19.275 -1.606 1.00 67.57 O -ANISOU 797 OE1 GLU A 98 8353 8183 9138 239 -277 -390 O -ATOM 798 OE2 GLU A 98 4.891 20.302 0.307 1.00 66.71 O -ANISOU 798 OE2 GLU A 98 8290 8005 9054 335 -230 -518 O -ATOM 799 N GLN A 99 7.865 17.940 3.904 1.00 31.61 N -ANISOU 799 N GLN A 99 3986 3724 4300 227 -126 -662 N -ATOM 800 CA GLN A 99 8.307 18.272 5.252 1.00 33.31 C -ANISOU 800 CA GLN A 99 4259 3932 4463 237 -114 -738 C -ATOM 801 C GLN A 99 9.687 18.918 5.236 1.00 34.00 C -ANISOU 801 C GLN A 99 4404 3966 4547 177 -186 -734 C -ATOM 802 O GLN A 99 9.966 19.812 6.035 1.00 35.23 O -ANISOU 802 O GLN A 99 4622 4067 4697 187 -210 -801 O -ATOM 803 CB GLN A 99 8.303 17.036 6.158 1.00 35.57 C -ANISOU 803 CB GLN A 99 4535 4318 4663 228 -53 -747 C -ATOM 804 CG GLN A 99 7.104 16.951 7.099 1.00 46.20 C -ANISOU 804 CG GLN A 99 5864 5703 5988 298 20 -804 C -ATOM 805 CD GLN A 99 7.006 18.138 8.061 1.00 57.69 C -ANISOU 805 CD GLN A 99 7382 7102 7436 349 22 -902 C -ATOM 806 OE1 GLN A 99 6.101 18.969 7.952 1.00 61.88 O -ANISOU 806 OE1 GLN A 99 7904 7582 8026 419 36 -939 O -ATOM 807 NE2 GLN A 99 7.931 18.210 9.016 1.00 60.50 N -ANISOU 807 NE2 GLN A 99 7804 7466 7717 315 5 -946 N -ATOM 808 N ILE A 100 10.546 18.466 4.324 1.00 32.58 N -ANISOU 808 N ILE A 100 4204 3806 4369 116 -220 -654 N -ATOM 809 CA ILE A 100 11.886 19.031 4.203 1.00 33.05 C -ANISOU 809 CA ILE A 100 4299 3828 4430 53 -288 -629 C -ATOM 810 C ILE A 100 11.795 20.481 3.735 1.00 34.49 C -ANISOU 810 C ILE A 100 4510 3900 4695 59 -351 -636 C -ATOM 811 O ILE A 100 12.431 21.368 4.308 1.00 34.63 O -ANISOU 811 O ILE A 100 4586 3854 4718 35 -402 -674 O -ATOM 812 CB ILE A 100 12.775 18.206 3.245 1.00 29.71 C -ANISOU 812 CB ILE A 100 3837 3459 3991 -4 -299 -536 C -ATOM 813 CG1 ILE A 100 13.149 16.869 3.890 1.00 28.72 C -ANISOU 813 CG1 ILE A 100 3698 3424 3789 -16 -250 -531 C -ATOM 814 CG2 ILE A 100 14.028 18.965 2.897 1.00 25.89 C -ANISOU 814 CG2 ILE A 100 3373 2935 3530 -67 -372 -492 C -ATOM 815 CD1 ILE A 100 13.688 15.830 2.911 1.00 23.72 C -ANISOU 815 CD1 ILE A 100 3022 2847 3142 -45 -237 -451 C -ATOM 816 N LYS A 101 10.979 20.718 2.710 1.00 33.52 N -ANISOU 816 N LYS A 101 4349 3752 4636 89 -352 -598 N -ATOM 817 CA LYS A 101 10.752 22.065 2.192 1.00 37.70 C -ANISOU 817 CA LYS A 101 4897 4172 5254 103 -410 -594 C -ATOM 818 C LYS A 101 10.108 22.996 3.224 1.00 39.90 C -ANISOU 818 C LYS A 101 5231 4371 5560 169 -404 -697 C -ATOM 819 O LYS A 101 10.387 24.195 3.251 1.00 39.71 O -ANISOU 819 O LYS A 101 5258 4237 5594 164 -466 -718 O -ATOM 820 CB LYS A 101 9.905 22.010 0.918 1.00 41.25 C -ANISOU 820 CB LYS A 101 5287 4626 5761 125 -410 -526 C -ATOM 821 CG LYS A 101 10.699 21.673 -0.335 1.00 43.25 C -ANISOU 821 CG LYS A 101 5509 4916 6008 54 -445 -422 C -ATOM 822 CD LYS A 101 9.783 21.270 -1.477 1.00 45.56 C -ANISOU 822 CD LYS A 101 5743 5244 6323 72 -432 -363 C -ATOM 823 CE LYS A 101 8.693 22.303 -1.696 1.00 48.70 C -ANISOU 823 CE LYS A 101 6132 5561 6813 132 -456 -371 C -ATOM 824 NZ LYS A 101 7.665 21.813 -2.653 1.00 50.62 N -ANISOU 824 NZ LYS A 101 6311 5851 7071 151 -443 -318 N -ATOM 825 N ARG A 102 9.239 22.444 4.064 1.00 42.65 N -ANISOU 825 N ARG A 102 5568 4771 5866 233 -327 -762 N -ATOM 826 CA ARG A 102 8.632 23.211 5.147 1.00 45.87 C -ANISOU 826 CA ARG A 102 6028 5121 6279 306 -303 -872 C -ATOM 827 C ARG A 102 9.730 23.658 6.100 1.00 43.39 C -ANISOU 827 C ARG A 102 5803 4770 5914 257 -347 -932 C -ATOM 828 O ARG A 102 9.937 24.847 6.328 1.00 45.00 O -ANISOU 828 O ARG A 102 6075 4858 6163 263 -402 -982 O -ATOM 829 CB ARG A 102 7.636 22.342 5.917 1.00 49.16 C -ANISOU 829 CB ARG A 102 6408 5633 6638 370 -204 -916 C -ATOM 830 CG ARG A 102 6.207 22.830 5.890 1.00 57.92 C -ANISOU 830 CG ARG A 102 7482 6713 7812 475 -158 -949 C -ATOM 831 CD ARG A 102 5.376 22.080 4.855 1.00 64.30 C -ANISOU 831 CD ARG A 102 8189 7585 8658 481 -134 -858 C -ATOM 832 NE ARG A 102 4.872 22.971 3.814 1.00 70.72 N -ANISOU 832 NE ARG A 102 8976 8314 9582 511 -181 -812 N -ATOM 833 CZ ARG A 102 5.177 22.868 2.524 1.00 72.89 C -ANISOU 833 CZ ARG A 102 9216 8583 9895 453 -238 -714 C -ATOM 834 NH1 ARG A 102 4.673 23.729 1.649 1.00 75.97 N -ANISOU 834 NH1 ARG A 102 9583 8899 10385 482 -284 -669 N -ATOM 835 NH2 ARG A 102 5.982 21.901 2.108 1.00 69.79 N -ANISOU 835 NH2 ARG A 102 8814 8264 9439 369 -248 -659 N -ATOM 836 N VAL A 103 10.428 22.669 6.648 1.00 41.13 N -ANISOU 836 N VAL A 103 5514 4581 5533 205 -326 -922 N -ATOM 837 CA VAL A 103 11.505 22.861 7.609 1.00 42.05 C -ANISOU 837 CA VAL A 103 5702 4691 5583 148 -367 -967 C -ATOM 838 C VAL A 103 12.608 23.798 7.103 1.00 48.81 C -ANISOU 838 C VAL A 103 6597 5454 6492 71 -474 -928 C -ATOM 839 O VAL A 103 13.172 24.585 7.867 1.00 52.84 O -ANISOU 839 O VAL A 103 7190 5898 6988 42 -528 -992 O -ATOM 840 CB VAL A 103 12.116 21.495 7.973 1.00 39.74 C -ANISOU 840 CB VAL A 103 5375 4527 5196 100 -333 -923 C -ATOM 841 CG1 VAL A 103 13.455 21.659 8.662 1.00 41.79 C -ANISOU 841 CG1 VAL A 103 5689 4787 5401 19 -398 -930 C -ATOM 842 CG2 VAL A 103 11.142 20.686 8.826 1.00 34.25 C -ANISOU 842 CG2 VAL A 103 4661 3918 4435 164 -237 -974 C -ATOM 843 N LYS A 104 12.912 23.709 5.813 1.00 51.34 N -ANISOU 843 N LYS A 104 6861 5775 6872 32 -505 -821 N -ATOM 844 CA LYS A 104 13.930 24.559 5.206 1.00 51.15 C -ANISOU 844 CA LYS A 104 6858 5674 6902 -46 -602 -762 C -ATOM 845 C LYS A 104 13.359 25.908 4.786 1.00 52.59 C -ANISOU 845 C LYS A 104 7077 5715 7190 -10 -650 -784 C -ATOM 846 O LYS A 104 14.107 26.816 4.426 1.00 54.97 O -ANISOU 846 O LYS A 104 7411 5929 7548 -73 -740 -746 O -ATOM 847 CB LYS A 104 14.524 23.878 3.975 1.00 47.45 C -ANISOU 847 CB LYS A 104 6310 5277 6443 -100 -608 -633 C -ATOM 848 CG LYS A 104 15.254 22.583 4.257 1.00 47.46 C -ANISOU 848 CG LYS A 104 6274 5403 6356 -138 -570 -597 C -ATOM 849 CD LYS A 104 16.606 22.832 4.881 1.00 46.42 C -ANISOU 849 CD LYS A 104 6177 5271 6191 -221 -635 -586 C -ATOM 850 CE LYS A 104 17.519 21.627 4.704 1.00 45.43 C -ANISOU 850 CE LYS A 104 5990 5264 6007 -264 -610 -506 C -ATOM 851 NZ LYS A 104 18.892 21.898 5.214 1.00 46.71 N -ANISOU 851 NZ LYS A 104 6168 5433 6146 -350 -681 -475 N -ATOM 852 N ASP A 105 12.036 26.032 4.825 1.00 49.91 N -ANISOU 852 N ASP A 105 6727 5353 6883 91 -593 -836 N -ATOM 853 CA ASP A 105 11.364 27.202 4.281 1.00 52.96 C -ANISOU 853 CA ASP A 105 7131 5611 7381 140 -630 -840 C -ATOM 854 C ASP A 105 11.975 27.552 2.933 1.00 53.79 C -ANISOU 854 C ASP A 105 7197 5685 7555 67 -705 -711 C -ATOM 855 O ASP A 105 12.392 28.686 2.707 1.00 52.25 O -ANISOU 855 O ASP A 105 7051 5368 7435 34 -790 -697 O -ATOM 856 CB ASP A 105 11.474 28.400 5.225 1.00 55.43 C -ANISOU 856 CB ASP A 105 7553 5788 7720 159 -677 -950 C -ATOM 857 CG ASP A 105 10.605 29.567 4.782 1.00 57.16 C -ANISOU 857 CG ASP A 105 7792 5865 8061 235 -703 -968 C -ATOM 858 OD1 ASP A 105 11.013 30.736 4.969 1.00 54.50 O -ANISOU 858 OD1 ASP A 105 7539 5383 7785 214 -784 -1004 O -ATOM 859 OD2 ASP A 105 9.509 29.307 4.238 1.00 57.01 O -ANISOU 859 OD2 ASP A 105 7702 5877 8082 314 -645 -941 O -ATOM 860 N SER A 106 12.032 26.568 2.044 1.00 54.62 N -ANISOU 860 N SER A 106 7220 5901 7631 42 -673 -617 N -ATOM 861 CA SER A 106 12.718 26.732 0.771 1.00 54.52 C -ANISOU 861 CA SER A 106 7167 5891 7657 -33 -731 -490 C -ATOM 862 C SER A 106 12.144 25.799 -0.289 1.00 58.72 C -ANISOU 862 C SER A 106 7614 6524 8173 -15 -681 -414 C -ATOM 863 O SER A 106 11.662 24.707 0.018 1.00 58.51 O -ANISOU 863 O SER A 106 7556 6594 8083 20 -605 -445 O -ATOM 864 CB SER A 106 14.222 26.485 0.944 1.00 49.68 C -ANISOU 864 CB SER A 106 6564 5322 6990 -135 -772 -448 C -ATOM 865 OG SER A 106 14.888 26.431 -0.306 1.00 46.88 O -ANISOU 865 OG SER A 106 6156 5003 6654 -202 -807 -318 O -ATOM 866 N GLU A 107 12.197 26.243 -1.538 1.00 62.58 N -ANISOU 866 N GLU A 107 8069 6989 8718 -46 -729 -313 N -ATOM 867 CA GLU A 107 11.698 25.458 -2.657 1.00 62.26 C -ANISOU 867 CA GLU A 107 7958 7040 8660 -40 -696 -237 C -ATOM 868 C GLU A 107 12.824 24.611 -3.241 1.00 56.33 C -ANISOU 868 C GLU A 107 7176 6393 7833 -118 -689 -162 C -ATOM 869 O GLU A 107 12.581 23.565 -3.842 1.00 51.96 O -ANISOU 869 O GLU A 107 6578 5939 7226 -114 -640 -131 O -ATOM 870 CB GLU A 107 11.129 26.387 -3.733 1.00 68.48 C -ANISOU 870 CB GLU A 107 8725 7755 9540 -31 -752 -161 C -ATOM 871 CG GLU A 107 10.256 25.686 -4.760 1.00 73.13 C -ANISOU 871 CG GLU A 107 9246 8425 10114 -8 -721 -103 C -ATOM 872 CD GLU A 107 8.962 25.170 -4.160 1.00 75.91 C -ANISOU 872 CD GLU A 107 9578 8800 10465 80 -655 -181 C -ATOM 873 OE1 GLU A 107 8.473 25.785 -3.185 1.00 77.22 O -ANISOU 873 OE1 GLU A 107 9778 8887 10676 144 -645 -266 O -ATOM 874 OE2 GLU A 107 8.440 24.149 -4.658 1.00 76.14 O -ANISOU 874 OE2 GLU A 107 9557 8927 10446 84 -612 -157 O -ATOM 875 N ASP A 108 14.056 25.079 -3.059 1.00 57.06 N -ANISOU 875 N ASP A 108 7294 6460 7925 -188 -739 -132 N -ATOM 876 CA ASP A 108 15.233 24.404 -3.595 1.00 55.84 C -ANISOU 876 CA ASP A 108 7105 6403 7708 -258 -734 -52 C -ATOM 877 C ASP A 108 15.977 23.643 -2.518 1.00 51.24 C -ANISOU 877 C ASP A 108 6537 5878 7056 -272 -699 -106 C -ATOM 878 O ASP A 108 16.637 24.238 -1.667 1.00 54.47 O -ANISOU 878 O ASP A 108 6987 6232 7475 -306 -744 -137 O -ATOM 879 CB ASP A 108 16.190 25.410 -4.225 1.00 59.30 C -ANISOU 879 CB ASP A 108 7542 6792 8195 -337 -816 45 C -ATOM 880 CG ASP A 108 15.697 25.920 -5.551 1.00 66.44 C -ANISOU 880 CG ASP A 108 8416 7680 9150 -341 -847 135 C -ATOM 881 OD1 ASP A 108 15.118 25.115 -6.314 1.00 67.73 O -ANISOU 881 OD1 ASP A 108 8539 7925 9270 -312 -798 158 O -ATOM 882 OD2 ASP A 108 15.885 27.125 -5.825 1.00 70.72 O -ANISOU 882 OD2 ASP A 108 8977 8123 9772 -377 -927 186 O -ATOM 883 N VAL A 109 15.870 22.323 -2.558 1.00 41.69 N -ANISOU 883 N VAL A 109 5295 4772 5773 -248 -625 -114 N -ATOM 884 CA VAL A 109 16.630 21.489 -1.642 1.00 36.03 C -ANISOU 884 CA VAL A 109 4581 4119 4989 -262 -591 -145 C -ATOM 885 C VAL A 109 17.246 20.337 -2.424 1.00 29.01 C -ANISOU 885 C VAL A 109 3640 3341 4041 -279 -544 -76 C -ATOM 886 O VAL A 109 16.539 19.599 -3.106 1.00 26.95 O -ANISOU 886 O VAL A 109 3358 3125 3759 -244 -497 -72 O -ATOM 887 CB VAL A 109 15.752 20.963 -0.502 1.00 34.01 C -ANISOU 887 CB VAL A 109 4353 3866 4703 -200 -539 -252 C -ATOM 888 CG1 VAL A 109 16.622 20.345 0.587 1.00 35.63 C -ANISOU 888 CG1 VAL A 109 4571 4122 4845 -224 -524 -279 C -ATOM 889 CG2 VAL A 109 14.905 22.094 0.070 1.00 29.52 C -ANISOU 889 CG2 VAL A 109 3833 3189 4195 -161 -570 -325 C -ATOM 890 N PRO A 110 18.577 20.195 -2.357 1.00 26.64 N -ANISOU 890 N PRO A 110 3320 3085 3715 -333 -559 -21 N -ATOM 891 CA PRO A 110 19.197 19.148 -3.174 1.00 27.49 C -ANISOU 891 CA PRO A 110 3378 3296 3771 -337 -508 46 C -ATOM 892 C PRO A 110 18.755 17.760 -2.708 1.00 26.82 C -ANISOU 892 C PRO A 110 3293 3268 3629 -284 -431 -11 C -ATOM 893 O PRO A 110 18.836 17.448 -1.518 1.00 23.46 O -ANISOU 893 O PRO A 110 2888 2843 3184 -274 -422 -66 O -ATOM 894 CB PRO A 110 20.699 19.360 -2.947 1.00 22.24 C -ANISOU 894 CB PRO A 110 2687 2663 3100 -400 -542 113 C -ATOM 895 CG PRO A 110 20.817 20.744 -2.386 1.00 25.88 C -ANISOU 895 CG PRO A 110 3186 3025 3623 -446 -629 101 C -ATOM 896 CD PRO A 110 19.572 20.964 -1.595 1.00 26.24 C -ANISOU 896 CD PRO A 110 3290 2997 3685 -391 -624 -11 C -ATOM 897 N MET A 111 18.270 16.958 -3.651 1.00 29.29 N -ANISOU 897 N MET A 111 3588 3627 3914 -256 -383 3 N -ATOM 898 CA MET A 111 17.768 15.617 -3.375 1.00 28.02 C -ANISOU 898 CA MET A 111 3430 3510 3707 -211 -316 -44 C -ATOM 899 C MET A 111 18.047 14.717 -4.557 1.00 23.07 C -ANISOU 899 C MET A 111 2780 2950 3037 -204 -272 3 C -ATOM 900 O MET A 111 18.166 15.186 -5.687 1.00 23.07 O -ANISOU 900 O MET A 111 2766 2960 3041 -224 -290 59 O -ATOM 901 CB MET A 111 16.259 15.633 -3.154 1.00 28.18 C -ANISOU 901 CB MET A 111 3471 3489 3747 -171 -307 -110 C -ATOM 902 CG MET A 111 15.782 16.558 -2.063 1.00 35.80 C -ANISOU 902 CG MET A 111 4466 4386 4752 -162 -339 -169 C -ATOM 903 SD MET A 111 14.014 16.339 -1.729 1.00 46.08 S -ANISOU 903 SD MET A 111 5774 5663 6070 -102 -307 -241 S -ATOM 904 CE MET A 111 13.804 17.475 -0.361 1.00 44.80 C -ANISOU 904 CE MET A 111 5653 5427 5942 -86 -337 -314 C -ATOM 905 N VAL A 112 18.150 13.422 -4.284 1.00 20.42 N -ANISOU 905 N VAL A 112 2445 2658 2658 -175 -215 -20 N -ATOM 906 CA VAL A 112 18.193 12.401 -5.323 1.00 18.39 C -ANISOU 906 CA VAL A 112 2182 2451 2355 -155 -166 -2 C -ATOM 907 C VAL A 112 17.149 11.357 -4.954 1.00 20.67 C -ANISOU 907 C VAL A 112 2496 2729 2628 -121 -130 -67 C -ATOM 908 O VAL A 112 17.088 10.923 -3.803 1.00 20.08 O -ANISOU 908 O VAL A 112 2427 2645 2555 -107 -116 -103 O -ATOM 909 CB VAL A 112 19.586 11.730 -5.425 1.00 19.14 C -ANISOU 909 CB VAL A 112 2249 2607 2415 -151 -128 46 C -ATOM 910 CG1 VAL A 112 19.545 10.533 -6.369 1.00 18.63 C -ANISOU 910 CG1 VAL A 112 2195 2583 2299 -116 -68 42 C -ATOM 911 CG2 VAL A 112 20.632 12.740 -5.888 1.00 18.27 C -ANISOU 911 CG2 VAL A 112 2103 2519 2321 -192 -163 126 C -ATOM 912 N LEU A 113 16.318 10.981 -5.922 1.00 21.55 N -ANISOU 912 N LEU A 113 2620 2844 2723 -114 -121 -77 N -ATOM 913 CA LEU A 113 15.323 9.932 -5.725 1.00 19.73 C -ANISOU 913 CA LEU A 113 2411 2605 2480 -93 -93 -128 C -ATOM 914 C LEU A 113 15.957 8.587 -6.024 1.00 22.85 C -ANISOU 914 C LEU A 113 2821 3035 2828 -73 -40 -128 C -ATOM 915 O LEU A 113 16.538 8.379 -7.095 1.00 21.68 O -ANISOU 915 O LEU A 113 2677 2919 2642 -72 -24 -100 O -ATOM 916 CB LEU A 113 14.121 10.146 -6.641 1.00 17.90 C -ANISOU 916 CB LEU A 113 2187 2361 2254 -103 -118 -134 C -ATOM 917 CG LEU A 113 12.978 9.131 -6.529 1.00 20.34 C -ANISOU 917 CG LEU A 113 2511 2661 2555 -94 -101 -178 C -ATOM 918 CD1 LEU A 113 12.306 9.212 -5.165 1.00 18.44 C -ANISOU 918 CD1 LEU A 113 2259 2396 2353 -80 -98 -214 C -ATOM 919 CD2 LEU A 113 11.958 9.364 -7.627 1.00 18.84 C -ANISOU 919 CD2 LEU A 113 2322 2471 2365 -113 -136 -169 C -ATOM 920 N VAL A 114 15.846 7.673 -5.071 1.00 22.60 N -ANISOU 920 N VAL A 114 2798 2993 2795 -54 -12 -159 N -ATOM 921 CA VAL A 114 16.517 6.389 -5.179 1.00 19.08 C -ANISOU 921 CA VAL A 114 2367 2565 2317 -28 37 -159 C -ATOM 922 C VAL A 114 15.513 5.257 -5.057 1.00 19.29 C -ANISOU 922 C VAL A 114 2426 2564 2339 -21 53 -203 C -ATOM 923 O VAL A 114 14.824 5.146 -4.043 1.00 17.10 O -ANISOU 923 O VAL A 114 2144 2268 2086 -26 47 -223 O -ATOM 924 CB VAL A 114 17.579 6.244 -4.072 1.00 16.28 C -ANISOU 924 CB VAL A 114 1989 2225 1972 -14 52 -136 C -ATOM 925 CG1 VAL A 114 18.218 4.855 -4.095 1.00 14.82 C -ANISOU 925 CG1 VAL A 114 1816 2049 1766 24 104 -132 C -ATOM 926 CG2 VAL A 114 18.634 7.321 -4.225 1.00 20.00 C -ANISOU 926 CG2 VAL A 114 2425 2724 2451 -31 29 -85 C -ATOM 927 N GLY A 115 15.436 4.420 -6.090 1.00 16.73 N -ANISOU 927 N GLY A 115 2137 2240 1981 -13 74 -216 N -ATOM 928 CA GLY A 115 14.572 3.250 -6.071 1.00 14.09 C -ANISOU 928 CA GLY A 115 1841 1871 1643 -15 83 -254 C -ATOM 929 C GLY A 115 15.417 2.014 -5.827 1.00 17.27 C -ANISOU 929 C GLY A 115 2267 2263 2033 23 130 -257 C -ATOM 930 O GLY A 115 16.101 1.512 -6.730 1.00 18.38 O -ANISOU 930 O GLY A 115 2435 2412 2138 50 161 -260 O -ATOM 931 N ASN A 116 15.378 1.524 -4.596 1.00 14.83 N -ANISOU 931 N ASN A 116 1946 1935 1752 29 139 -253 N -ATOM 932 CA ASN A 116 16.283 0.465 -4.178 1.00 18.64 C -ANISOU 932 CA ASN A 116 2439 2406 2236 70 180 -241 C -ATOM 933 C ASN A 116 15.686 -0.935 -4.327 1.00 21.05 C -ANISOU 933 C ASN A 116 2799 2655 2544 73 192 -272 C -ATOM 934 O ASN A 116 14.490 -1.089 -4.550 1.00 21.71 O -ANISOU 934 O ASN A 116 2904 2713 2631 34 164 -300 O -ATOM 935 CB ASN A 116 16.756 0.702 -2.739 1.00 14.91 C -ANISOU 935 CB ASN A 116 1925 1952 1789 73 178 -206 C -ATOM 936 CG ASN A 116 17.958 -0.147 -2.375 1.00 19.34 C -ANISOU 936 CG ASN A 116 2479 2515 2354 119 215 -173 C -ATOM 937 OD1 ASN A 116 18.887 -0.278 -3.163 1.00 21.77 O -ANISOU 937 OD1 ASN A 116 2786 2838 2647 156 244 -160 O -ATOM 938 ND2 ASN A 116 17.939 -0.735 -1.178 1.00 18.89 N -ANISOU 938 ND2 ASN A 116 2413 2446 2318 120 216 -154 N -ATOM 939 N LYS A 117 16.543 -1.946 -4.202 1.00 20.14 N -ANISOU 939 N LYS A 117 2703 2517 2432 119 231 -263 N -ATOM 940 CA LYS A 117 16.157 -3.337 -4.387 1.00 19.66 C -ANISOU 940 CA LYS A 117 2704 2388 2379 128 242 -293 C -ATOM 941 C LYS A 117 15.775 -3.631 -5.835 1.00 23.38 C -ANISOU 941 C LYS A 117 3240 2835 2810 123 241 -346 C -ATOM 942 O LYS A 117 14.853 -4.412 -6.088 1.00 29.18 O -ANISOU 942 O LYS A 117 4028 3512 3548 91 218 -382 O -ATOM 943 CB LYS A 117 14.999 -3.719 -3.457 1.00 18.04 C -ANISOU 943 CB LYS A 117 2497 2151 2207 79 211 -290 C -ATOM 944 CG LYS A 117 15.181 -3.311 -2.001 1.00 19.45 C -ANISOU 944 CG LYS A 117 2616 2364 2409 74 208 -243 C -ATOM 945 CD LYS A 117 14.279 -4.152 -1.096 1.00 19.45 C -ANISOU 945 CD LYS A 117 2624 2329 2438 41 195 -231 C -ATOM 946 CE LYS A 117 14.419 -3.762 0.369 1.00 23.27 C -ANISOU 946 CE LYS A 117 3054 2858 2930 35 195 -186 C -ATOM 947 NZ LYS A 117 13.562 -4.588 1.274 1.00 24.84 N -ANISOU 947 NZ LYS A 117 3254 3034 3150 1 188 -163 N -ATOM 948 N CYS A 118 16.478 -3.028 -6.792 1.00 21.15 N -ANISOU 948 N CYS A 118 2954 2599 2485 149 261 -348 N -ATOM 949 CA CYS A 118 16.150 -3.266 -8.205 1.00 25.81 C -ANISOU 949 CA CYS A 118 3609 3178 3019 143 260 -400 C -ATOM 950 C CYS A 118 16.538 -4.675 -8.658 1.00 27.10 C -ANISOU 950 C CYS A 118 3851 3276 3168 193 300 -445 C -ATOM 951 O CYS A 118 16.283 -5.071 -9.796 1.00 27.95 O -ANISOU 951 O CYS A 118 4032 3364 3223 190 301 -500 O -ATOM 952 CB CYS A 118 16.741 -2.193 -9.129 1.00 29.16 C -ANISOU 952 CB CYS A 118 4006 3679 3394 151 271 -382 C -ATOM 953 SG CYS A 118 18.531 -2.202 -9.260 1.00 34.74 S -ANISOU 953 SG CYS A 118 4677 4437 4085 236 346 -343 S -ATOM 954 N ASP A 119 17.134 -5.437 -7.748 1.00 28.30 N -ANISOU 954 N ASP A 119 3994 3390 3369 237 330 -422 N -ATOM 955 CA ASP A 119 17.468 -6.833 -8.004 1.00 27.29 C -ANISOU 955 CA ASP A 119 3942 3181 3247 291 365 -462 C -ATOM 956 C ASP A 119 16.269 -7.776 -7.836 1.00 30.80 C -ANISOU 956 C ASP A 119 4454 3530 3717 235 317 -500 C -ATOM 957 O ASP A 119 16.313 -8.916 -8.292 1.00 35.78 O -ANISOU 957 O ASP A 119 5172 4077 4347 263 332 -550 O -ATOM 958 CB ASP A 119 18.603 -7.276 -7.077 1.00 30.64 C -ANISOU 958 CB ASP A 119 4321 3600 3721 363 411 -408 C -ATOM 959 CG ASP A 119 18.263 -7.088 -5.599 1.00 29.93 C -ANISOU 959 CG ASP A 119 4169 3514 3689 321 375 -347 C -ATOM 960 OD1 ASP A 119 18.409 -5.958 -5.094 1.00 24.43 O -ANISOU 960 OD1 ASP A 119 3396 2895 2991 296 359 -303 O -ATOM 961 OD2 ASP A 119 17.852 -8.067 -4.940 1.00 33.00 O -ANISOU 961 OD2 ASP A 119 4588 3828 4122 312 361 -344 O -ATOM 962 N LEU A 120 15.210 -7.308 -7.177 1.00 31.00 N -ANISOU 962 N LEU A 120 4440 3568 3770 156 262 -474 N -ATOM 963 CA LEU A 120 14.034 -8.144 -6.910 1.00 32.48 C -ANISOU 963 CA LEU A 120 4673 3679 3990 92 213 -491 C -ATOM 964 C LEU A 120 13.110 -8.270 -8.122 1.00 33.99 C -ANISOU 964 C LEU A 120 4935 3845 4135 36 169 -554 C -ATOM 965 O LEU A 120 13.019 -7.352 -8.940 1.00 35.46 O -ANISOU 965 O LEU A 120 5109 4097 4268 23 160 -568 O -ATOM 966 CB LEU A 120 13.234 -7.608 -5.711 1.00 32.96 C -ANISOU 966 CB LEU A 120 4654 3774 4094 34 177 -434 C -ATOM 967 CG LEU A 120 13.898 -7.558 -4.330 1.00 32.87 C -ANISOU 967 CG LEU A 120 4578 3786 4125 67 204 -369 C -ATOM 968 CD1 LEU A 120 12.917 -7.027 -3.296 1.00 26.12 C -ANISOU 968 CD1 LEU A 120 3659 2969 3295 4 170 -329 C -ATOM 969 CD2 LEU A 120 14.423 -8.938 -3.916 1.00 32.67 C -ANISOU 969 CD2 LEU A 120 4599 3675 4140 108 227 -359 C -ATOM 970 N PRO A 121 12.420 -9.418 -8.237 1.00 36.79 N -ANISOU 970 N PRO A 121 5366 4102 4509 -2 135 -588 N -ATOM 971 CA PRO A 121 11.395 -9.662 -9.262 1.00 39.28 C -ANISOU 971 CA PRO A 121 5752 4385 4786 -75 76 -644 C -ATOM 972 C PRO A 121 10.013 -9.155 -8.836 1.00 42.41 C -ANISOU 972 C PRO A 121 6087 4815 5213 -174 7 -602 C -ATOM 973 O PRO A 121 9.085 -9.114 -9.647 1.00 46.94 O -ANISOU 973 O PRO A 121 6693 5386 5756 -244 -52 -631 O -ATOM 974 CB PRO A 121 11.379 -11.186 -9.366 1.00 36.70 C -ANISOU 974 CB PRO A 121 5532 3928 4484 -71 69 -689 C -ATOM 975 CG PRO A 121 11.734 -11.648 -7.995 1.00 33.96 C -ANISOU 975 CG PRO A 121 5136 3549 4217 -42 94 -625 C -ATOM 976 CD PRO A 121 12.694 -10.625 -7.435 1.00 35.61 C -ANISOU 976 CD PRO A 121 5248 3861 4423 24 150 -573 C -ATOM 977 N SER A 122 9.901 -8.764 -7.570 1.00 41.94 N -ANISOU 977 N SER A 122 5935 4791 5208 -176 17 -534 N -ATOM 978 CA SER A 122 8.643 -8.334 -6.960 1.00 44.14 C -ANISOU 978 CA SER A 122 6142 5105 5523 -254 -32 -487 C -ATOM 979 C SER A 122 8.310 -6.841 -7.166 1.00 48.53 C -ANISOU 979 C SER A 122 6620 5762 6056 -263 -43 -468 C -ATOM 980 O SER A 122 7.701 -6.217 -6.299 1.00 55.90 O -ANISOU 980 O SER A 122 7470 6745 7026 -286 -51 -420 O -ATOM 981 CB SER A 122 8.676 -8.665 -5.458 1.00 39.22 C -ANISOU 981 CB SER A 122 5463 4476 4962 -248 -11 -425 C -ATOM 982 OG SER A 122 7.538 -8.162 -4.781 1.00 37.24 O -ANISOU 982 OG SER A 122 5133 4277 4741 -309 -42 -377 O -ATOM 983 N ARG A 123 8.687 -6.272 -8.308 1.00 42.63 N -ANISOU 983 N ARG A 123 5902 5046 5249 -245 -43 -504 N -ATOM 984 CA ARG A 123 8.442 -4.849 -8.567 1.00 38.75 C -ANISOU 984 CA ARG A 123 5342 4641 4742 -252 -56 -481 C -ATOM 985 C ARG A 123 6.958 -4.466 -8.625 1.00 39.99 C -ANISOU 985 C ARG A 123 5452 4820 4922 -329 -122 -456 C -ATOM 986 O ARG A 123 6.175 -5.115 -9.319 1.00 44.10 O -ANISOU 986 O ARG A 123 6022 5305 5431 -391 -175 -478 O -ATOM 987 CB ARG A 123 9.116 -4.416 -9.869 1.00 35.42 C -ANISOU 987 CB ARG A 123 4965 4248 4246 -224 -47 -516 C -ATOM 988 CG ARG A 123 8.840 -2.970 -10.252 1.00 33.37 C -ANISOU 988 CG ARG A 123 4641 4067 3972 -237 -71 -484 C -ATOM 989 CD ARG A 123 9.477 -2.620 -11.590 1.00 31.74 C -ANISOU 989 CD ARG A 123 4481 3895 3686 -219 -63 -509 C -ATOM 990 NE ARG A 123 10.932 -2.715 -11.526 1.00 32.70 N -ANISOU 990 NE ARG A 123 4616 4025 3785 -142 10 -516 N -ATOM 991 CZ ARG A 123 11.751 -1.683 -11.325 1.00 35.76 C -ANISOU 991 CZ ARG A 123 4943 4471 4174 -103 41 -475 C -ATOM 992 NH1 ARG A 123 11.263 -0.456 -11.173 1.00 32.42 N -ANISOU 992 NH1 ARG A 123 4451 4092 3775 -131 5 -432 N -ATOM 993 NH2 ARG A 123 13.064 -1.879 -11.278 1.00 35.69 N -ANISOU 993 NH2 ARG A 123 4940 4472 4148 -36 105 -474 N -ATOM 994 N THR A 124 6.586 -3.406 -7.902 1.00 29.81 N -ANISOU 994 N THR A 124 4069 3589 3668 -325 -120 -411 N -ATOM 995 CA THR A 124 5.244 -2.834 -7.997 1.00 25.93 C -ANISOU 995 CA THR A 124 3517 3132 3203 -381 -175 -381 C -ATOM 996 C THR A 124 5.295 -1.349 -8.329 1.00 28.14 C -ANISOU 996 C THR A 124 3742 3475 3476 -357 -180 -363 C -ATOM 997 O THR A 124 4.265 -0.721 -8.552 1.00 28.43 O -ANISOU 997 O THR A 124 3725 3544 3535 -391 -225 -335 O -ATOM 998 CB THR A 124 4.437 -3.011 -6.701 1.00 24.99 C -ANISOU 998 CB THR A 124 3328 3021 3148 -401 -169 -338 C -ATOM 999 OG1 THR A 124 5.174 -2.472 -5.603 1.00 27.72 O -ANISOU 999 OG1 THR A 124 3631 3392 3507 -340 -111 -324 O -ATOM 1000 CG2 THR A 124 4.162 -4.473 -6.438 1.00 30.79 C -ANISOU 1000 CG2 THR A 124 4110 3689 3899 -444 -181 -341 C -ATOM 1001 N VAL A 125 6.500 -0.788 -8.338 1.00 29.35 N -ANISOU 1001 N VAL A 125 3904 3644 3604 -298 -136 -371 N -ATOM 1002 CA VAL A 125 6.692 0.606 -8.711 1.00 25.95 C -ANISOU 1002 CA VAL A 125 3431 3261 3167 -277 -144 -351 C -ATOM 1003 C VAL A 125 7.517 0.664 -9.990 1.00 28.20 C -ANISOU 1003 C VAL A 125 3776 3556 3382 -267 -144 -371 C -ATOM 1004 O VAL A 125 8.670 0.245 -10.011 1.00 32.40 O -ANISOU 1004 O VAL A 125 4349 4078 3884 -226 -95 -391 O -ATOM 1005 CB VAL A 125 7.389 1.414 -7.593 1.00 21.37 C -ANISOU 1005 CB VAL A 125 2801 2700 2619 -225 -101 -332 C -ATOM 1006 CG1 VAL A 125 7.459 2.896 -7.974 1.00 20.27 C -ANISOU 1006 CG1 VAL A 125 2620 2595 2485 -212 -121 -308 C -ATOM 1007 CG2 VAL A 125 6.642 1.251 -6.276 1.00 16.50 C -ANISOU 1007 CG2 VAL A 125 2133 2081 2054 -229 -90 -318 C -ATOM 1008 N ASP A 126 6.919 1.177 -11.058 1.00 27.65 N -ANISOU 1008 N ASP A 126 3707 3513 3286 -305 -196 -360 N -ATOM 1009 CA ASP A 126 7.571 1.199 -12.360 1.00 33.51 C -ANISOU 1009 CA ASP A 126 4508 4275 3947 -304 -198 -377 C -ATOM 1010 C ASP A 126 8.626 2.289 -12.455 1.00 28.62 C -ANISOU 1010 C ASP A 126 3860 3698 3317 -258 -166 -347 C -ATOM 1011 O ASP A 126 8.450 3.391 -11.935 1.00 25.11 O -ANISOU 1011 O ASP A 126 3347 3270 2925 -250 -178 -306 O -ATOM 1012 CB ASP A 126 6.539 1.408 -13.469 1.00 45.19 C -ANISOU 1012 CB ASP A 126 5997 5778 5395 -367 -273 -366 C -ATOM 1013 CG ASP A 126 5.497 0.315 -13.505 1.00 59.90 C -ANISOU 1013 CG ASP A 126 7892 7601 7265 -427 -317 -391 C -ATOM 1014 OD1 ASP A 126 5.858 -0.858 -13.266 1.00 67.30 O -ANISOU 1014 OD1 ASP A 126 8893 8487 8189 -420 -288 -438 O -ATOM 1015 OD2 ASP A 126 4.316 0.628 -13.768 1.00 64.40 O -ANISOU 1015 OD2 ASP A 126 8421 8189 7859 -482 -385 -359 O -ATOM 1016 N THR A 127 9.714 1.980 -13.145 1.00 26.14 N -ANISOU 1016 N THR A 127 3597 3400 2935 -229 -125 -366 N -ATOM 1017 CA THR A 127 10.759 2.961 -13.402 1.00 29.75 C -ANISOU 1017 CA THR A 127 4026 3905 3374 -197 -98 -327 C -ATOM 1018 C THR A 127 10.182 4.287 -13.892 1.00 30.78 C -ANISOU 1018 C THR A 127 4107 4071 3519 -230 -155 -273 C -ATOM 1019 O THR A 127 10.548 5.352 -13.399 1.00 34.00 O -ANISOU 1019 O THR A 127 4458 4489 3973 -213 -155 -230 O -ATOM 1020 CB THR A 127 11.768 2.433 -14.430 1.00 33.01 C -ANISOU 1020 CB THR A 127 4501 4347 3694 -170 -52 -351 C -ATOM 1021 OG1 THR A 127 12.342 1.214 -13.944 1.00 35.59 O -ANISOU 1021 OG1 THR A 127 4872 4631 4020 -128 3 -399 O -ATOM 1022 CG2 THR A 127 12.873 3.453 -14.664 1.00 35.87 C -ANISOU 1022 CG2 THR A 127 4820 4768 4042 -142 -23 -296 C -ATOM 1023 N LYS A 128 9.266 4.213 -14.850 1.00 32.85 N -ANISOU 1023 N LYS A 128 4392 4345 3743 -279 -212 -274 N -ATOM 1024 CA LYS A 128 8.696 5.406 -15.467 1.00 33.65 C -ANISOU 1024 CA LYS A 128 4451 4482 3855 -311 -273 -215 C -ATOM 1025 C LYS A 128 7.971 6.310 -14.472 1.00 27.46 C -ANISOU 1025 C LYS A 128 3585 3671 3176 -306 -301 -180 C -ATOM 1026 O LYS A 128 8.221 7.511 -14.435 1.00 29.46 O -ANISOU 1026 O LYS A 128 3793 3935 3464 -294 -315 -130 O -ATOM 1027 CB LYS A 128 7.759 5.032 -16.620 1.00 40.15 C -ANISOU 1027 CB LYS A 128 5314 5325 4617 -371 -336 -221 C -ATOM 1028 CG LYS A 128 7.498 6.173 -17.600 1.00 46.62 C -ANISOU 1028 CG LYS A 128 6104 6195 5413 -401 -394 -151 C -ATOM 1029 CD LYS A 128 6.003 6.393 -17.817 1.00 56.64 C -ANISOU 1029 CD LYS A 128 7337 7462 6722 -455 -481 -121 C -ATOM 1030 CE LYS A 128 5.723 7.377 -18.958 1.00 61.12 C -ANISOU 1030 CE LYS A 128 7885 8083 7254 -491 -546 -48 C -ATOM 1031 NZ LYS A 128 6.316 8.728 -18.725 1.00 61.62 N -ANISOU 1031 NZ LYS A 128 7889 8151 7371 -456 -537 19 N -ATOM 1032 N GLN A 129 7.068 5.750 -13.673 1.00 26.60 N -ANISOU 1032 N GLN A 129 3459 3527 3119 -314 -309 -204 N -ATOM 1033 CA GLN A 129 6.375 6.570 -12.685 1.00 29.56 C -ANISOU 1033 CA GLN A 129 3758 3883 3588 -298 -324 -178 C -ATOM 1034 C GLN A 129 7.359 7.247 -11.733 1.00 26.01 C -ANISOU 1034 C GLN A 129 3286 3421 3176 -248 -277 -175 C -ATOM 1035 O GLN A 129 7.150 8.387 -11.326 1.00 21.26 O -ANISOU 1035 O GLN A 129 2634 2810 2634 -231 -295 -145 O -ATOM 1036 CB GLN A 129 5.260 5.806 -11.937 1.00 36.45 C -ANISOU 1036 CB GLN A 129 4610 4734 4507 -315 -331 -198 C -ATOM 1037 CG GLN A 129 5.622 4.461 -11.331 1.00 41.30 C -ANISOU 1037 CG GLN A 129 5270 5320 5100 -311 -284 -248 C -ATOM 1038 CD GLN A 129 4.411 3.742 -10.722 1.00 39.72 C -ANISOU 1038 CD GLN A 129 5043 5105 4945 -343 -303 -252 C -ATOM 1039 OE1 GLN A 129 4.394 2.515 -10.602 1.00 36.31 O -ANISOU 1039 OE1 GLN A 129 4657 4646 4492 -365 -291 -283 O -ATOM 1040 NE2 GLN A 129 3.399 4.509 -10.335 1.00 41.48 N -ANISOU 1040 NE2 GLN A 129 5187 5342 5232 -344 -330 -215 N -ATOM 1041 N ALA A 130 8.446 6.558 -11.408 1.00 25.84 N -ANISOU 1041 N ALA A 130 3302 3396 3119 -224 -220 -205 N -ATOM 1042 CA ALA A 130 9.484 7.139 -10.568 1.00 22.01 C -ANISOU 1042 CA ALA A 130 2797 2905 2660 -186 -183 -197 C -ATOM 1043 C ALA A 130 10.287 8.220 -11.304 1.00 22.98 C -ANISOU 1043 C ALA A 130 2911 3055 2767 -187 -198 -149 C -ATOM 1044 O ALA A 130 10.630 9.243 -10.724 1.00 25.54 O -ANISOU 1044 O ALA A 130 3200 3365 3140 -173 -205 -124 O -ATOM 1045 CB ALA A 130 10.396 6.060 -10.049 1.00 23.53 C -ANISOU 1045 CB ALA A 130 3024 3092 2823 -161 -124 -230 C -ATOM 1046 N GLN A 131 10.589 7.990 -12.578 1.00 20.98 N -ANISOU 1046 N GLN A 131 2691 2839 2443 -206 -203 -135 N -ATOM 1047 CA GLN A 131 11.270 8.990 -13.398 1.00 23.72 C -ANISOU 1047 CA GLN A 131 3024 3221 2766 -216 -220 -76 C -ATOM 1048 C GLN A 131 10.429 10.248 -13.517 1.00 25.18 C -ANISOU 1048 C GLN A 131 3165 3388 3013 -236 -286 -28 C -ATOM 1049 O GLN A 131 10.946 11.360 -13.435 1.00 26.20 O -ANISOU 1049 O GLN A 131 3265 3511 3178 -234 -303 20 O -ATOM 1050 CB GLN A 131 11.525 8.454 -14.807 1.00 31.06 C -ANISOU 1050 CB GLN A 131 4002 4204 3595 -236 -214 -72 C -ATOM 1051 CG GLN A 131 12.647 7.449 -14.921 1.00 44.79 C -ANISOU 1051 CG GLN A 131 5782 5966 5268 -203 -141 -106 C -ATOM 1052 CD GLN A 131 12.744 6.843 -16.318 1.00 56.31 C -ANISOU 1052 CD GLN A 131 7301 7476 6617 -218 -132 -120 C -ATOM 1053 OE1 GLN A 131 11.854 7.028 -17.152 1.00 58.22 O -ANISOU 1053 OE1 GLN A 131 7559 7733 6829 -261 -188 -109 O -ATOM 1054 NE2 GLN A 131 13.828 6.114 -16.575 1.00 58.26 N -ANISOU 1054 NE2 GLN A 131 7582 7751 6802 -179 -60 -143 N -ATOM 1055 N ASP A 132 9.132 10.060 -13.738 1.00 26.01 N -ANISOU 1055 N ASP A 132 3264 3484 3134 -256 -328 -36 N -ATOM 1056 CA ASP A 132 8.202 11.174 -13.889 1.00 24.79 C -ANISOU 1056 CA ASP A 132 3063 3312 3045 -267 -392 12 C -ATOM 1057 C ASP A 132 8.092 11.989 -12.602 1.00 24.55 C -ANISOU 1057 C ASP A 132 2990 3227 3112 -229 -386 5 C -ATOM 1058 O ASP A 132 7.964 13.214 -12.641 1.00 23.92 O -ANISOU 1058 O ASP A 132 2878 3120 3089 -223 -426 51 O -ATOM 1059 CB ASP A 132 6.814 10.664 -14.305 1.00 26.50 C -ANISOU 1059 CB ASP A 132 3272 3535 3260 -295 -436 7 C -ATOM 1060 CG ASP A 132 6.808 10.033 -15.697 1.00 33.96 C -ANISOU 1060 CG ASP A 132 4267 4533 4104 -342 -459 15 C -ATOM 1061 OD1 ASP A 132 7.822 10.152 -16.411 1.00 35.45 O -ANISOU 1061 OD1 ASP A 132 4488 4758 4224 -346 -440 33 O -ATOM 1062 OD2 ASP A 132 5.785 9.423 -16.086 1.00 39.48 O -ANISOU 1062 OD2 ASP A 132 4973 5242 4788 -377 -498 4 O -ATOM 1063 N LEU A 133 8.120 11.310 -11.459 1.00 21.72 N -ANISOU 1063 N LEU A 133 2635 2849 2769 -203 -339 -52 N -ATOM 1064 CA LEU A 133 8.091 12.016 -10.185 1.00 26.66 C -ANISOU 1064 CA LEU A 133 3231 3429 3468 -166 -327 -70 C -ATOM 1065 C LEU A 133 9.338 12.883 -10.027 1.00 26.02 C -ANISOU 1065 C LEU A 133 3157 3335 3395 -160 -325 -46 C -ATOM 1066 O LEU A 133 9.244 14.063 -9.706 1.00 30.72 O -ANISOU 1066 O LEU A 133 3731 3888 4054 -148 -356 -27 O -ATOM 1067 CB LEU A 133 7.972 11.042 -9.010 1.00 26.56 C -ANISOU 1067 CB LEU A 133 3225 3411 3454 -145 -276 -129 C -ATOM 1068 CG LEU A 133 7.810 11.758 -7.668 1.00 26.37 C -ANISOU 1068 CG LEU A 133 3176 3350 3494 -106 -262 -154 C -ATOM 1069 CD1 LEU A 133 6.483 12.499 -7.655 1.00 25.85 C -ANISOU 1069 CD1 LEU A 133 3064 3263 3496 -89 -296 -141 C -ATOM 1070 CD2 LEU A 133 7.919 10.798 -6.480 1.00 20.92 C -ANISOU 1070 CD2 LEU A 133 2495 2665 2788 -90 -208 -203 C -ATOM 1071 N ALA A 134 10.505 12.287 -10.253 1.00 24.21 N -ANISOU 1071 N ALA A 134 2956 3139 3104 -169 -289 -45 N -ATOM 1072 CA ALA A 134 11.766 13.015 -10.167 1.00 23.20 C -ANISOU 1072 CA ALA A 134 2825 3010 2978 -174 -288 -11 C -ATOM 1073 C ALA A 134 11.766 14.213 -11.106 1.00 22.88 C -ANISOU 1073 C ALA A 134 2768 2965 2960 -200 -345 61 C -ATOM 1074 O ALA A 134 12.175 15.303 -10.728 1.00 26.04 O -ANISOU 1074 O ALA A 134 3154 3325 3414 -203 -374 89 O -ATOM 1075 CB ALA A 134 12.933 12.095 -10.494 1.00 20.05 C -ANISOU 1075 CB ALA A 134 2448 2663 2506 -175 -237 -9 C -ATOM 1076 N ARG A 135 11.314 14.003 -12.338 1.00 24.86 N -ANISOU 1076 N ARG A 135 3025 3256 3166 -223 -366 93 N -ATOM 1077 CA ARG A 135 11.261 15.079 -13.319 1.00 27.11 C -ANISOU 1077 CA ARG A 135 3293 3544 3464 -253 -423 174 C -ATOM 1078 C ARG A 135 10.404 16.242 -12.807 1.00 24.12 C -ANISOU 1078 C ARG A 135 2884 3089 3190 -238 -478 187 C -ATOM 1079 O ARG A 135 10.734 17.409 -13.007 1.00 22.80 O -ANISOU 1079 O ARG A 135 2703 2888 3071 -251 -522 246 O -ATOM 1080 CB ARG A 135 10.737 14.563 -14.660 1.00 30.71 C -ANISOU 1080 CB ARG A 135 3764 4059 3845 -282 -441 199 C -ATOM 1081 CG ARG A 135 11.012 15.498 -15.824 1.00 40.36 C -ANISOU 1081 CG ARG A 135 4974 5311 5050 -320 -489 295 C -ATOM 1082 CD ARG A 135 11.416 14.723 -17.066 1.00 47.61 C -ANISOU 1082 CD ARG A 135 5925 6321 5843 -347 -466 311 C -ATOM 1083 NE ARG A 135 10.551 13.568 -17.292 1.00 53.75 N -ANISOU 1083 NE ARG A 135 6737 7117 6571 -347 -458 247 N -ATOM 1084 CZ ARG A 135 10.990 12.323 -17.467 1.00 54.26 C -ANISOU 1084 CZ ARG A 135 6848 7220 6549 -338 -399 187 C -ATOM 1085 NH1 ARG A 135 12.292 12.063 -17.449 1.00 53.26 N -ANISOU 1085 NH1 ARG A 135 6733 7128 6376 -321 -336 186 N -ATOM 1086 NH2 ARG A 135 10.126 11.337 -17.665 1.00 52.89 N -ANISOU 1086 NH2 ARG A 135 6708 7048 6338 -347 -405 131 N -ATOM 1087 N SER A 136 9.317 15.918 -12.119 1.00 22.84 N -ANISOU 1087 N SER A 136 2712 2898 3069 -207 -472 132 N -ATOM 1088 CA SER A 136 8.439 16.954 -11.594 1.00 27.06 C -ANISOU 1088 CA SER A 136 3215 3362 3703 -177 -512 136 C -ATOM 1089 C SER A 136 9.143 17.807 -10.553 1.00 26.71 C -ANISOU 1089 C SER A 136 3180 3253 3716 -156 -508 115 C -ATOM 1090 O SER A 136 8.951 19.017 -10.517 1.00 24.46 O -ANISOU 1090 O SER A 136 2884 2903 3508 -146 -556 146 O -ATOM 1091 CB SER A 136 7.175 16.342 -11.001 1.00 27.52 C -ANISOU 1091 CB SER A 136 3253 3418 3786 -144 -494 83 C -ATOM 1092 OG SER A 136 6.596 15.448 -11.931 1.00 38.88 O -ANISOU 1092 OG SER A 136 4691 4915 5166 -176 -503 98 O -ATOM 1093 N TYR A 137 9.946 17.160 -9.709 1.00 25.86 N -ANISOU 1093 N TYR A 137 3094 3160 3572 -151 -456 63 N -ATOM 1094 CA TYR A 137 10.671 17.833 -8.636 1.00 21.52 C -ANISOU 1094 CA TYR A 137 2559 2557 3062 -139 -455 36 C -ATOM 1095 C TYR A 137 11.897 18.548 -9.159 1.00 22.06 C -ANISOU 1095 C TYR A 137 2632 2622 3126 -184 -487 103 C -ATOM 1096 O TYR A 137 12.412 19.447 -8.508 1.00 25.00 O -ANISOU 1096 O TYR A 137 3016 2935 3549 -188 -515 101 O -ATOM 1097 CB TYR A 137 11.159 16.821 -7.604 1.00 20.61 C -ANISOU 1097 CB TYR A 137 2461 2471 2901 -126 -394 -30 C -ATOM 1098 CG TYR A 137 10.080 16.136 -6.804 1.00 24.64 C -ANISOU 1098 CG TYR A 137 2964 2982 3416 -86 -357 -96 C -ATOM 1099 CD1 TYR A 137 8.835 16.723 -6.625 1.00 25.66 C -ANISOU 1099 CD1 TYR A 137 3071 3071 3608 -51 -376 -110 C -ATOM 1100 CD2 TYR A 137 10.317 14.900 -6.210 1.00 25.51 C -ANISOU 1100 CD2 TYR A 137 3085 3135 3471 -82 -301 -138 C -ATOM 1101 CE1 TYR A 137 7.846 16.088 -5.877 1.00 25.88 C -ANISOU 1101 CE1 TYR A 137 3081 3112 3640 -16 -337 -161 C -ATOM 1102 CE2 TYR A 137 9.340 14.261 -5.464 1.00 25.60 C -ANISOU 1102 CE2 TYR A 137 3087 3153 3488 -52 -268 -187 C -ATOM 1103 CZ TYR A 137 8.110 14.859 -5.299 1.00 26.26 C -ANISOU 1103 CZ TYR A 137 3141 3206 3629 -21 -284 -197 C -ATOM 1104 OH TYR A 137 7.145 14.219 -4.556 1.00 31.84 O -ANISOU 1104 OH TYR A 137 3828 3931 4340 6 -246 -237 O -ATOM 1105 N GLY A 138 12.392 18.116 -10.314 1.00 23.78 N -ANISOU 1105 N GLY A 138 2845 2910 3280 -219 -483 163 N -ATOM 1106 CA GLY A 138 13.630 18.651 -10.858 1.00 23.07 C -ANISOU 1106 CA GLY A 138 2749 2840 3174 -264 -502 238 C -ATOM 1107 C GLY A 138 14.855 18.017 -10.219 1.00 26.48 C -ANISOU 1107 C GLY A 138 3187 3312 3564 -269 -453 218 C -ATOM 1108 O GLY A 138 15.890 18.667 -10.037 1.00 26.76 O -ANISOU 1108 O GLY A 138 3213 3337 3618 -302 -475 262 O -ATOM 1109 N ILE A 139 14.745 16.739 -9.870 1.00 25.61 N -ANISOU 1109 N ILE A 139 3087 3243 3399 -241 -392 157 N -ATOM 1110 CA ILE A 139 15.858 16.041 -9.232 1.00 22.68 C -ANISOU 1110 CA ILE A 139 2716 2910 2991 -238 -345 141 C -ATOM 1111 C ILE A 139 16.256 14.792 -10.000 1.00 23.34 C -ANISOU 1111 C ILE A 139 2803 3076 2989 -228 -285 146 C -ATOM 1112 O ILE A 139 15.463 14.257 -10.777 1.00 23.51 O -ANISOU 1112 O ILE A 139 2840 3118 2975 -221 -276 132 O -ATOM 1113 CB ILE A 139 15.542 15.651 -7.764 1.00 23.99 C -ANISOU 1113 CB ILE A 139 2897 3038 3179 -205 -323 58 C -ATOM 1114 CG1 ILE A 139 14.480 14.547 -7.698 1.00 22.54 C -ANISOU 1114 CG1 ILE A 139 2726 2868 2968 -171 -284 -2 C -ATOM 1115 CG2 ILE A 139 15.107 16.872 -6.957 1.00 25.38 C -ANISOU 1115 CG2 ILE A 139 3081 3129 3433 -204 -376 36 C -ATOM 1116 CD1 ILE A 139 14.073 14.167 -6.256 1.00 19.20 C -ANISOU 1116 CD1 ILE A 139 2314 2418 2563 -141 -260 -74 C -ATOM 1117 N PRO A 140 17.492 14.318 -9.781 1.00 23.64 N -ANISOU 1117 N PRO A 140 2828 3159 2994 -227 -245 164 N -ATOM 1118 CA PRO A 140 17.934 13.061 -10.388 1.00 24.82 C -ANISOU 1118 CA PRO A 140 2986 3379 3067 -203 -178 157 C -ATOM 1119 C PRO A 140 17.213 11.840 -9.811 1.00 22.12 C -ANISOU 1119 C PRO A 140 2675 3019 2708 -165 -140 74 C -ATOM 1120 O PRO A 140 16.776 11.841 -8.657 1.00 18.96 O -ANISOU 1120 O PRO A 140 2280 2573 2352 -154 -149 28 O -ATOM 1121 CB PRO A 140 19.434 13.014 -10.050 1.00 28.62 C -ANISOU 1121 CB PRO A 140 3432 3903 3540 -206 -150 204 C -ATOM 1122 CG PRO A 140 19.811 14.441 -9.755 1.00 27.81 C -ANISOU 1122 CG PRO A 140 3303 3766 3499 -253 -217 261 C -ATOM 1123 CD PRO A 140 18.594 15.013 -9.090 1.00 25.51 C -ANISOU 1123 CD PRO A 140 3039 3387 3266 -252 -266 203 C -ATOM 1124 N PHE A 141 17.081 10.812 -10.642 1.00 22.67 N -ANISOU 1124 N PHE A 141 2772 3128 2714 -148 -98 55 N -ATOM 1125 CA PHE A 141 16.530 9.539 -10.224 1.00 22.36 C -ANISOU 1125 CA PHE A 141 2767 3072 2658 -118 -62 -15 C -ATOM 1126 C PHE A 141 17.525 8.430 -10.543 1.00 22.87 C -ANISOU 1126 C PHE A 141 2844 3181 2664 -83 6 -19 C -ATOM 1127 O PHE A 141 18.092 8.376 -11.638 1.00 23.48 O -ANISOU 1127 O PHE A 141 2925 3312 2685 -81 30 13 O -ATOM 1128 CB PHE A 141 15.199 9.271 -10.925 1.00 19.28 C -ANISOU 1128 CB PHE A 141 2408 2668 2251 -131 -87 -46 C -ATOM 1129 CG PHE A 141 14.669 7.886 -10.691 1.00 15.79 C -ANISOU 1129 CG PHE A 141 2004 2209 1786 -112 -55 -110 C -ATOM 1130 CD1 PHE A 141 14.544 7.392 -9.405 1.00 15.76 C -ANISOU 1130 CD1 PHE A 141 1996 2171 1822 -93 -38 -145 C -ATOM 1131 CD2 PHE A 141 14.314 7.074 -11.754 1.00 18.01 C -ANISOU 1131 CD2 PHE A 141 2331 2509 2004 -117 -45 -134 C -ATOM 1132 CE1 PHE A 141 14.066 6.115 -9.180 1.00 21.60 C -ANISOU 1132 CE1 PHE A 141 2770 2889 2547 -81 -12 -193 C -ATOM 1133 CE2 PHE A 141 13.832 5.793 -11.538 1.00 21.32 C -ANISOU 1133 CE2 PHE A 141 2792 2900 2409 -106 -23 -192 C -ATOM 1134 CZ PHE A 141 13.705 5.313 -10.249 1.00 20.61 C -ANISOU 1134 CZ PHE A 141 2692 2772 2368 -88 -7 -217 C -ATOM 1135 N ILE A 142 17.742 7.546 -9.580 1.00 22.20 N -ANISOU 1135 N ILE A 142 2766 3076 2594 -53 39 -54 N -ATOM 1136 CA ILE A 142 18.684 6.450 -9.755 1.00 23.07 C -ANISOU 1136 CA ILE A 142 2886 3216 2663 -8 106 -58 C -ATOM 1137 C ILE A 142 18.145 5.197 -9.084 1.00 22.54 C -ANISOU 1137 C ILE A 142 2857 3102 2605 18 128 -119 C -ATOM 1138 O ILE A 142 17.718 5.233 -7.930 1.00 24.27 O -ANISOU 1138 O ILE A 142 3066 3286 2871 10 108 -134 O -ATOM 1139 CB ILE A 142 20.081 6.812 -9.196 1.00 30.08 C -ANISOU 1139 CB ILE A 142 3717 4140 3571 4 124 1 C -ATOM 1140 CG1 ILE A 142 20.635 8.033 -9.936 1.00 36.22 C -ANISOU 1140 CG1 ILE A 142 4455 4964 4342 -30 99 73 C -ATOM 1141 CG2 ILE A 142 21.045 5.644 -9.324 1.00 30.49 C -ANISOU 1141 CG2 ILE A 142 3771 4222 3592 63 197 2 C -ATOM 1142 CD1 ILE A 142 22.081 8.345 -9.630 1.00 39.82 C -ANISOU 1142 CD1 ILE A 142 4848 5470 4810 -25 117 145 C -ATOM 1143 N GLU A 143 18.137 4.097 -9.828 1.00 23.23 N -ANISOU 1143 N GLU A 143 2994 3189 2643 47 169 -155 N -ATOM 1144 CA GLU A 143 17.744 2.804 -9.284 1.00 26.88 C -ANISOU 1144 CA GLU A 143 3497 3600 3115 70 191 -207 C -ATOM 1145 C GLU A 143 18.978 2.072 -8.775 1.00 25.91 C -ANISOU 1145 C GLU A 143 3359 3487 3000 128 248 -188 C -ATOM 1146 O GLU A 143 20.038 2.123 -9.391 1.00 29.05 O -ANISOU 1146 O GLU A 143 3738 3934 3366 162 290 -157 O -ATOM 1147 CB GLU A 143 16.994 1.976 -10.332 1.00 31.66 C -ANISOU 1147 CB GLU A 143 4176 4183 3671 66 194 -262 C -ATOM 1148 CG GLU A 143 15.496 2.281 -10.361 1.00 42.50 C -ANISOU 1148 CG GLU A 143 5562 5526 5061 8 130 -285 C -ATOM 1149 CD GLU A 143 14.735 1.492 -11.409 1.00 51.73 C -ANISOU 1149 CD GLU A 143 6803 6675 6177 -11 118 -335 C -ATOM 1150 OE1 GLU A 143 13.614 1.027 -11.111 1.00 50.60 O -ANISOU 1150 OE1 GLU A 143 6680 6487 6059 -45 82 -364 O -ATOM 1151 OE2 GLU A 143 15.250 1.354 -12.537 1.00 60.47 O -ANISOU 1151 OE2 GLU A 143 7946 7816 7214 5 143 -344 O -ATOM 1152 N THR A 144 18.844 1.403 -7.638 1.00 21.37 N -ANISOU 1152 N THR A 144 2784 2869 2467 139 251 -199 N -ATOM 1153 CA THR A 144 19.996 0.786 -7.007 1.00 17.24 C -ANISOU 1153 CA THR A 144 2235 2355 1962 191 295 -168 C -ATOM 1154 C THR A 144 19.679 -0.594 -6.466 1.00 19.87 C -ANISOU 1154 C THR A 144 2612 2624 2314 219 314 -202 C -ATOM 1155 O THR A 144 18.524 -0.998 -6.362 1.00 21.41 O -ANISOU 1155 O THR A 144 2850 2769 2516 186 287 -245 O -ATOM 1156 CB THR A 144 20.510 1.635 -5.818 1.00 14.36 C -ANISOU 1156 CB THR A 144 1801 2017 1638 171 266 -114 C -ATOM 1157 OG1 THR A 144 19.494 1.704 -4.817 1.00 17.65 O -ANISOU 1157 OG1 THR A 144 2226 2395 2084 134 226 -138 O -ATOM 1158 CG2 THR A 144 20.850 3.044 -6.251 1.00 14.39 C -ANISOU 1158 CG2 THR A 144 1762 2072 1635 136 237 -74 C -ATOM 1159 N SER A 145 20.735 -1.307 -6.116 1.00 19.63 N -ANISOU 1159 N SER A 145 2564 2596 2299 278 360 -174 N -ATOM 1160 CA SER A 145 20.631 -2.546 -5.384 1.00 21.08 C -ANISOU 1160 CA SER A 145 2777 2717 2515 307 374 -185 C -ATOM 1161 C SER A 145 21.809 -2.557 -4.425 1.00 20.97 C -ANISOU 1161 C SER A 145 2695 2738 2536 343 391 -114 C -ATOM 1162 O SER A 145 22.953 -2.478 -4.852 1.00 19.78 O -ANISOU 1162 O SER A 145 2507 2633 2377 392 431 -77 O -ATOM 1163 CB SER A 145 20.728 -3.729 -6.335 1.00 22.34 C -ANISOU 1163 CB SER A 145 3009 2826 2652 362 421 -234 C -ATOM 1164 OG SER A 145 20.668 -4.943 -5.612 1.00 26.10 O -ANISOU 1164 OG SER A 145 3516 3231 3172 390 431 -238 O -ATOM 1165 N ALA A 146 21.531 -2.607 -3.129 1.00 21.96 N -ANISOU 1165 N ALA A 146 2799 2849 2695 314 358 -89 N -ATOM 1166 CA ALA A 146 22.589 -2.655 -2.135 1.00 21.04 C -ANISOU 1166 CA ALA A 146 2620 2767 2608 338 362 -18 C -ATOM 1167 C ALA A 146 23.146 -4.068 -2.073 1.00 24.31 C -ANISOU 1167 C ALA A 146 3053 3134 3050 412 408 -4 C -ATOM 1168 O ALA A 146 24.210 -4.306 -1.515 1.00 26.33 O -ANISOU 1168 O ALA A 146 3254 3419 3332 454 423 62 O -ATOM 1169 CB ALA A 146 22.065 -2.217 -0.773 1.00 19.34 C -ANISOU 1169 CB ALA A 146 2382 2559 2406 280 310 0 C -ATOM 1170 N LYS A 147 22.418 -5.004 -2.667 1.00 25.47 N -ANISOU 1170 N LYS A 147 3278 3205 3194 428 425 -66 N -ATOM 1171 CA LYS A 147 22.848 -6.387 -2.710 1.00 26.67 C -ANISOU 1171 CA LYS A 147 3466 3290 3378 501 467 -65 C -ATOM 1172 C LYS A 147 23.880 -6.613 -3.813 1.00 30.32 C -ANISOU 1172 C LYS A 147 3927 3771 3821 587 535 -72 C -ATOM 1173 O LYS A 147 24.891 -7.278 -3.583 1.00 33.06 O -ANISOU 1173 O LYS A 147 4244 4114 4203 666 576 -26 O -ATOM 1174 CB LYS A 147 21.647 -7.310 -2.902 1.00 28.10 C -ANISOU 1174 CB LYS A 147 3739 3372 3566 475 451 -130 C -ATOM 1175 CG LYS A 147 22.007 -8.777 -3.102 1.00 26.84 C -ANISOU 1175 CG LYS A 147 3637 3119 3442 551 491 -144 C -ATOM 1176 CD LYS A 147 20.730 -9.598 -3.231 1.00 30.64 C -ANISOU 1176 CD LYS A 147 4210 3500 3933 503 459 -203 C -ATOM 1177 CE LYS A 147 21.015 -11.089 -3.322 1.00 34.91 C -ANISOU 1177 CE LYS A 147 4818 3927 4520 571 488 -217 C -ATOM 1178 NZ LYS A 147 19.746 -11.874 -3.317 1.00 37.05 N -ANISOU 1178 NZ LYS A 147 5172 4097 4809 507 442 -261 N -ATOM 1179 N THR A 148 23.627 -6.059 -5.001 1.00 26.68 N -ANISOU 1179 N THR A 148 3496 3338 3305 575 547 -124 N -ATOM 1180 CA THR A 148 24.551 -6.188 -6.130 1.00 28.22 C -ANISOU 1180 CA THR A 148 3690 3567 3464 655 618 -133 C -ATOM 1181 C THR A 148 25.482 -4.980 -6.177 1.00 29.69 C -ANISOU 1181 C THR A 148 3774 3871 3636 647 623 -59 C -ATOM 1182 O THR A 148 26.555 -5.030 -6.783 1.00 33.09 O -ANISOU 1182 O THR A 148 4165 4355 4052 719 687 -29 O -ATOM 1183 CB THR A 148 23.815 -6.268 -7.496 1.00 29.45 C -ANISOU 1183 CB THR A 148 3937 3699 3552 644 629 -226 C -ATOM 1184 OG1 THR A 148 23.249 -4.994 -7.812 1.00 32.52 O -ANISOU 1184 OG1 THR A 148 4303 4150 3902 561 583 -224 O -ATOM 1185 CG2 THR A 148 22.711 -7.292 -7.475 1.00 26.00 C -ANISOU 1185 CG2 THR A 148 3603 3147 3128 622 602 -299 C -ATOM 1186 N ARG A 149 25.045 -3.899 -5.536 1.00 25.90 N -ANISOU 1186 N ARG A 149 3254 3427 3161 559 556 -31 N -ATOM 1187 CA ARG A 149 25.746 -2.613 -5.510 1.00 25.74 C -ANISOU 1187 CA ARG A 149 3146 3503 3132 526 539 36 C -ATOM 1188 C ARG A 149 25.518 -1.777 -6.771 1.00 26.46 C -ANISOU 1188 C ARG A 149 3251 3639 3163 499 545 11 C -ATOM 1189 O ARG A 149 26.142 -0.726 -6.952 1.00 26.28 O -ANISOU 1189 O ARG A 149 3159 3694 3131 473 534 70 O -ATOM 1190 CB ARG A 149 27.249 -2.760 -5.221 1.00 31.14 C -ANISOU 1190 CB ARG A 149 3739 4248 3844 591 581 125 C -ATOM 1191 CG ARG A 149 27.881 -1.448 -4.732 1.00 38.04 C -ANISOU 1191 CG ARG A 149 4519 5208 4728 530 534 207 C -ATOM 1192 CD ARG A 149 29.404 -1.455 -4.831 1.00 46.47 C -ANISOU 1192 CD ARG A 149 5487 6358 5814 589 580 302 C -ATOM 1193 NE ARG A 149 29.987 -0.171 -4.442 1.00 45.56 N -ANISOU 1193 NE ARG A 149 5285 6320 5707 517 525 382 N -ATOM 1194 CZ ARG A 149 30.539 0.069 -3.257 1.00 43.48 C -ANISOU 1194 CZ ARG A 149 4956 6080 5484 485 474 453 C -ATOM 1195 NH1 ARG A 149 31.045 1.265 -2.987 1.00 44.63 N -ANISOU 1195 NH1 ARG A 149 5033 6288 5635 412 417 519 N -ATOM 1196 NH2 ARG A 149 30.593 -0.890 -2.342 1.00 39.47 N -ANISOU 1196 NH2 ARG A 149 4454 5532 5012 522 474 462 N -ATOM 1197 N GLN A 150 24.619 -2.224 -7.638 1.00 25.22 N -ANISOU 1197 N GLN A 150 3183 3434 2965 498 554 -72 N -ATOM 1198 CA GLN A 150 24.255 -1.403 -8.787 1.00 24.76 C -ANISOU 1198 CA GLN A 150 3143 3419 2846 461 546 -92 C -ATOM 1199 C GLN A 150 23.779 -0.027 -8.339 1.00 24.45 C -ANISOU 1199 C GLN A 150 3061 3407 2823 370 470 -58 C -ATOM 1200 O GLN A 150 22.876 0.084 -7.513 1.00 24.08 O -ANISOU 1200 O GLN A 150 3031 3311 2809 322 416 -81 O -ATOM 1201 CB GLN A 150 23.156 -2.064 -9.618 1.00 25.32 C -ANISOU 1201 CB GLN A 150 3321 3427 2873 453 544 -187 C -ATOM 1202 CG GLN A 150 22.713 -1.212 -10.805 1.00 29.65 C -ANISOU 1202 CG GLN A 150 3889 4025 3353 407 527 -202 C -ATOM 1203 CD GLN A 150 21.638 -1.867 -11.667 1.00 37.86 C -ANISOU 1203 CD GLN A 150 5036 5009 4342 391 516 -293 C -ATOM 1204 OE1 GLN A 150 21.050 -2.884 -11.297 1.00 33.38 O -ANISOU 1204 OE1 GLN A 150 4529 4355 3798 399 508 -347 O -ATOM 1205 NE2 GLN A 150 21.376 -1.272 -12.827 1.00 42.87 N -ANISOU 1205 NE2 GLN A 150 5692 5694 4904 362 508 -303 N -ATOM 1206 N GLY A 151 24.395 1.016 -8.884 1.00 28.13 N -ANISOU 1206 N GLY A 151 3470 3950 3267 351 469 -3 N -ATOM 1207 CA GLY A 151 23.928 2.377 -8.700 1.00 25.38 C -ANISOU 1207 CA GLY A 151 3093 3617 2931 268 398 24 C -ATOM 1208 C GLY A 151 24.272 3.060 -7.390 1.00 22.67 C -ANISOU 1208 C GLY A 151 2689 3278 2648 231 348 75 C -ATOM 1209 O GLY A 151 23.969 4.245 -7.220 1.00 23.65 O -ANISOU 1209 O GLY A 151 2793 3408 2786 167 288 95 O -ATOM 1210 N VAL A 152 24.901 2.332 -6.471 1.00 21.21 N -ANISOU 1210 N VAL A 152 2478 3085 2495 270 368 97 N -ATOM 1211 CA VAL A 152 25.172 2.849 -5.123 1.00 22.05 C -ANISOU 1211 CA VAL A 152 2537 3193 2647 231 316 138 C -ATOM 1212 C VAL A 152 26.105 4.076 -5.102 1.00 27.04 C -ANISOU 1212 C VAL A 152 3092 3892 3291 188 283 219 C -ATOM 1213 O VAL A 152 25.737 5.133 -4.583 1.00 29.69 O -ANISOU 1213 O VAL A 152 3423 4214 3644 121 215 222 O -ATOM 1214 CB VAL A 152 25.725 1.737 -4.185 1.00 28.35 C -ANISOU 1214 CB VAL A 152 3320 3978 3475 282 343 157 C -ATOM 1215 CG1 VAL A 152 26.250 2.324 -2.877 1.00 26.06 C -ANISOU 1215 CG1 VAL A 152 2972 3712 3218 240 288 214 C -ATOM 1216 CG2 VAL A 152 24.654 0.684 -3.912 1.00 27.09 C -ANISOU 1216 CG2 VAL A 152 3237 3739 3317 299 351 84 C -ATOM 1217 N ASP A 153 27.309 3.935 -5.649 1.00 29.34 N -ANISOU 1217 N ASP A 153 3322 4251 3574 228 331 287 N -ATOM 1218 CA ASP A 153 28.246 5.059 -5.727 1.00 31.63 C -ANISOU 1218 CA ASP A 153 3532 4609 3877 181 299 377 C -ATOM 1219 C ASP A 153 27.599 6.232 -6.449 1.00 30.21 C -ANISOU 1219 C ASP A 153 3375 4423 3680 116 255 367 C -ATOM 1220 O ASP A 153 27.710 7.380 -6.022 1.00 31.79 O -ANISOU 1220 O ASP A 153 3548 4623 3910 44 184 404 O -ATOM 1221 CB ASP A 153 29.512 4.662 -6.485 1.00 32.65 C -ANISOU 1221 CB ASP A 153 3590 4823 3992 242 374 451 C -ATOM 1222 CG ASP A 153 30.297 3.577 -5.787 1.00 40.51 C -ANISOU 1222 CG ASP A 153 4547 5829 5016 313 416 481 C -ATOM 1223 OD1 ASP A 153 30.429 3.633 -4.550 1.00 41.32 O -ANISOU 1223 OD1 ASP A 153 4628 5914 5159 283 362 503 O -ATOM 1224 OD2 ASP A 153 30.785 2.664 -6.483 1.00 49.27 O -ANISOU 1224 OD2 ASP A 153 5649 6964 6106 403 504 482 O -ATOM 1225 N ASP A 154 26.930 5.922 -7.552 1.00 27.01 N -ANISOU 1225 N ASP A 154 3024 4008 3229 140 293 316 N -ATOM 1226 CA ASP A 154 26.295 6.923 -8.400 1.00 33.67 C -ANISOU 1226 CA ASP A 154 3890 4851 4052 86 256 313 C -ATOM 1227 C ASP A 154 25.249 7.742 -7.654 1.00 30.56 C -ANISOU 1227 C ASP A 154 3531 4384 3696 23 172 272 C -ATOM 1228 O ASP A 154 25.161 8.955 -7.834 1.00 32.25 O -ANISOU 1228 O ASP A 154 3729 4597 3929 -37 115 307 O -ATOM 1229 CB ASP A 154 25.651 6.243 -9.607 1.00 44.17 C -ANISOU 1229 CB ASP A 154 5284 6181 5319 126 308 254 C -ATOM 1230 CG ASP A 154 26.261 6.684 -10.910 1.00 60.92 C -ANISOU 1230 CG ASP A 154 7374 8386 7387 127 343 313 C -ATOM 1231 OD1 ASP A 154 27.382 6.223 -11.225 1.00 64.49 O -ANISOU 1231 OD1 ASP A 154 7776 8909 7819 180 412 363 O -ATOM 1232 OD2 ASP A 154 25.620 7.495 -11.614 1.00 67.71 O -ANISOU 1232 OD2 ASP A 154 8256 9245 8226 76 302 316 O -ATOM 1233 N ALA A 155 24.451 7.072 -6.827 1.00 27.36 N -ANISOU 1233 N ALA A 155 3173 3918 3306 39 167 200 N -ATOM 1234 CA ALA A 155 23.412 7.747 -6.056 1.00 23.86 C -ANISOU 1234 CA ALA A 155 2761 3410 2893 -7 101 155 C -ATOM 1235 C ALA A 155 24.019 8.781 -5.119 1.00 23.03 C -ANISOU 1235 C ALA A 155 2613 3307 2829 -58 40 201 C -ATOM 1236 O ALA A 155 23.550 9.910 -5.045 1.00 25.45 O -ANISOU 1236 O ALA A 155 2930 3580 3161 -107 -20 197 O -ATOM 1237 CB ALA A 155 22.579 6.741 -5.271 1.00 20.51 C -ANISOU 1237 CB ALA A 155 2383 2936 2473 21 115 84 C -ATOM 1238 N PHE A 156 25.069 8.389 -4.408 1.00 20.33 N -ANISOU 1238 N PHE A 156 2227 3000 2498 -45 52 246 N -ATOM 1239 CA PHE A 156 25.719 9.280 -3.461 1.00 20.66 C -ANISOU 1239 CA PHE A 156 2232 3047 2573 -100 -13 290 C -ATOM 1240 C PHE A 156 26.513 10.402 -4.135 1.00 28.12 C -ANISOU 1240 C PHE A 156 3125 4028 3531 -151 -48 372 C -ATOM 1241 O PHE A 156 26.512 11.537 -3.660 1.00 30.44 O -ANISOU 1241 O PHE A 156 3420 4291 3857 -216 -123 383 O -ATOM 1242 CB PHE A 156 26.634 8.474 -2.538 1.00 21.52 C -ANISOU 1242 CB PHE A 156 2299 3191 2686 -75 5 325 C -ATOM 1243 CG PHE A 156 25.900 7.755 -1.441 1.00 24.98 C -ANISOU 1243 CG PHE A 156 2785 3586 3121 -56 5 259 C -ATOM 1244 CD1 PHE A 156 25.550 8.418 -0.271 1.00 22.50 C -ANISOU 1244 CD1 PHE A 156 2492 3240 2817 -105 -59 230 C -ATOM 1245 CD2 PHE A 156 25.561 6.419 -1.575 1.00 23.95 C -ANISOU 1245 CD2 PHE A 156 2679 3446 2976 9 69 226 C -ATOM 1246 CE1 PHE A 156 24.878 7.756 0.746 1.00 22.49 C -ANISOU 1246 CE1 PHE A 156 2530 3213 2805 -88 -53 177 C -ATOM 1247 CE2 PHE A 156 24.884 5.750 -0.564 1.00 21.48 C -ANISOU 1247 CE2 PHE A 156 2404 3097 2662 20 68 179 C -ATOM 1248 CZ PHE A 156 24.542 6.417 0.594 1.00 22.13 C -ANISOU 1248 CZ PHE A 156 2499 3161 2747 -29 10 157 C -ATOM 1249 N TYR A 157 27.199 10.079 -5.230 1.00 27.82 N -ANISOU 1249 N TYR A 157 3044 4056 3469 -122 8 430 N -ATOM 1250 CA TYR A 157 28.010 11.060 -5.941 1.00 27.83 C -ANISOU 1250 CA TYR A 157 2986 4107 3479 -172 -17 525 C -ATOM 1251 C TYR A 157 27.137 12.105 -6.602 1.00 24.87 C -ANISOU 1251 C TYR A 157 2653 3686 3111 -219 -64 507 C -ATOM 1252 O TYR A 157 27.433 13.299 -6.555 1.00 22.02 O -ANISOU 1252 O TYR A 157 2269 3311 2786 -290 -135 561 O -ATOM 1253 CB TYR A 157 28.869 10.388 -7.008 1.00 32.48 C -ANISOU 1253 CB TYR A 157 3522 4790 4030 -118 70 587 C -ATOM 1254 CG TYR A 157 29.980 9.555 -6.437 1.00 41.33 C -ANISOU 1254 CG TYR A 157 4578 5967 5159 -73 112 635 C -ATOM 1255 CD1 TYR A 157 30.077 9.347 -5.069 1.00 44.79 C -ANISOU 1255 CD1 TYR A 157 5016 6372 5631 -85 70 619 C -ATOM 1256 CD2 TYR A 157 30.940 8.990 -7.260 1.00 46.64 C -ANISOU 1256 CD2 TYR A 157 5185 6732 5805 -17 194 702 C -ATOM 1257 CE1 TYR A 157 31.089 8.587 -4.535 1.00 49.06 C -ANISOU 1257 CE1 TYR A 157 5491 6965 6183 -44 102 674 C -ATOM 1258 CE2 TYR A 157 31.961 8.236 -6.735 1.00 53.05 C -ANISOU 1258 CE2 TYR A 157 5929 7595 6634 32 233 754 C -ATOM 1259 CZ TYR A 157 32.030 8.034 -5.371 1.00 55.23 C -ANISOU 1259 CZ TYR A 157 6204 7833 6950 16 183 743 C -ATOM 1260 OH TYR A 157 33.046 7.279 -4.836 1.00 62.68 O -ANISOU 1260 OH TYR A 157 7073 8827 7914 65 215 806 O -ATOM 1261 N THR A 158 26.068 11.642 -7.235 1.00 19.22 N -ANISOU 1261 N THR A 158 1997 2942 2363 -181 -31 437 N -ATOM 1262 CA THR A 158 25.109 12.542 -7.848 1.00 26.99 C -ANISOU 1262 CA THR A 158 3020 3880 3355 -218 -77 419 C -ATOM 1263 C THR A 158 24.558 13.510 -6.806 1.00 29.55 C -ANISOU 1263 C THR A 158 3372 4119 3739 -265 -161 385 C -ATOM 1264 O THR A 158 24.376 14.700 -7.078 1.00 30.82 O -ANISOU 1264 O THR A 158 3534 4243 3934 -318 -224 416 O -ATOM 1265 CB THR A 158 23.956 11.761 -8.475 1.00 26.23 C -ANISOU 1265 CB THR A 158 2985 3765 3218 -171 -36 341 C -ATOM 1266 OG1 THR A 158 24.478 10.860 -9.461 1.00 25.91 O -ANISOU 1266 OG1 THR A 158 2932 3798 3115 -124 44 361 O -ATOM 1267 CG2 THR A 158 22.971 12.710 -9.123 1.00 23.28 C -ANISOU 1267 CG2 THR A 158 2640 3348 2856 -209 -88 336 C -ATOM 1268 N LEU A 159 24.295 12.999 -5.608 1.00 25.48 N -ANISOU 1268 N LEU A 159 2880 3568 3232 -245 -161 321 N -ATOM 1269 CA LEU A 159 23.783 13.852 -4.545 1.00 23.52 C -ANISOU 1269 CA LEU A 159 2665 3244 3027 -281 -231 276 C -ATOM 1270 C LEU A 159 24.790 14.958 -4.248 1.00 27.41 C -ANISOU 1270 C LEU A 159 3121 3736 3558 -351 -301 349 C -ATOM 1271 O LEU A 159 24.427 16.130 -4.191 1.00 29.45 O -ANISOU 1271 O LEU A 159 3403 3928 3857 -396 -369 345 O -ATOM 1272 CB LEU A 159 23.467 13.046 -3.284 1.00 16.18 C -ANISOU 1272 CB LEU A 159 1761 2298 2087 -249 -213 206 C -ATOM 1273 CG LEU A 159 22.906 13.913 -2.157 1.00 18.77 C -ANISOU 1273 CG LEU A 159 2131 2554 2446 -279 -277 149 C -ATOM 1274 CD1 LEU A 159 21.710 14.707 -2.648 1.00 14.16 C -ANISOU 1274 CD1 LEU A 159 1586 1904 1890 -279 -302 106 C -ATOM 1275 CD2 LEU A 159 22.539 13.059 -0.940 1.00 18.33 C -ANISOU 1275 CD2 LEU A 159 2100 2497 2367 -247 -251 84 C -ATOM 1276 N VAL A 160 26.058 14.584 -4.073 1.00 27.78 N -ANISOU 1276 N VAL A 160 3107 3853 3595 -361 -286 420 N -ATOM 1277 CA VAL A 160 27.124 15.564 -3.885 1.00 24.86 C -ANISOU 1277 CA VAL A 160 2689 3495 3261 -437 -355 507 C -ATOM 1278 C VAL A 160 27.115 16.613 -4.999 1.00 27.09 C -ANISOU 1278 C VAL A 160 2959 3767 3568 -484 -390 571 C -ATOM 1279 O VAL A 160 27.262 17.813 -4.743 1.00 29.28 O -ANISOU 1279 O VAL A 160 3244 3987 3894 -556 -477 598 O -ATOM 1280 CB VAL A 160 28.518 14.908 -3.846 1.00 23.09 C -ANISOU 1280 CB VAL A 160 2380 3371 3022 -433 -320 597 C -ATOM 1281 CG1 VAL A 160 29.607 15.983 -3.850 1.00 23.37 C -ANISOU 1281 CG1 VAL A 160 2354 3427 3098 -524 -396 706 C -ATOM 1282 CG2 VAL A 160 28.659 14.018 -2.628 1.00 21.05 C -ANISOU 1282 CG2 VAL A 160 2128 3119 2750 -401 -306 553 C -ATOM 1283 N ARG A 161 26.933 16.156 -6.234 1.00 22.96 N -ANISOU 1283 N ARG A 161 2421 3296 3007 -445 -325 596 N -ATOM 1284 CA ARG A 161 26.886 17.060 -7.375 1.00 26.83 C -ANISOU 1284 CA ARG A 161 2897 3789 3509 -487 -352 666 C -ATOM 1285 C ARG A 161 25.694 18.005 -7.303 1.00 29.88 C -ANISOU 1285 C ARG A 161 3351 4062 3938 -508 -418 608 C -ATOM 1286 O ARG A 161 25.793 19.159 -7.719 1.00 34.35 O -ANISOU 1286 O ARG A 161 3911 4593 4549 -570 -485 671 O -ATOM 1287 CB ARG A 161 26.877 16.279 -8.690 1.00 29.49 C -ANISOU 1287 CB ARG A 161 3215 4212 3779 -435 -264 692 C -ATOM 1288 CG ARG A 161 28.221 15.642 -9.003 1.00 34.38 C -ANISOU 1288 CG ARG A 161 3751 4948 4365 -418 -200 778 C -ATOM 1289 CD ARG A 161 28.192 14.784 -10.260 1.00 39.04 C -ANISOU 1289 CD ARG A 161 4335 5621 4876 -355 -102 784 C -ATOM 1290 NE ARG A 161 29.469 14.097 -10.444 1.00 43.69 N -ANISOU 1290 NE ARG A 161 4845 6320 5437 -320 -30 856 N -ATOM 1291 CZ ARG A 161 29.613 12.777 -10.526 1.00 43.48 C -ANISOU 1291 CZ ARG A 161 4822 6335 5362 -230 63 809 C -ATOM 1292 NH1 ARG A 161 30.822 12.256 -10.682 1.00 45.75 N -ANISOU 1292 NH1 ARG A 161 5029 6722 5634 -194 128 884 N -ATOM 1293 NH2 ARG A 161 28.554 11.978 -10.461 1.00 41.14 N -ANISOU 1293 NH2 ARG A 161 4610 5982 5039 -176 91 693 N -ATOM 1294 N GLU A 162 24.574 17.519 -6.770 1.00 27.39 N -ANISOU 1294 N GLU A 162 3097 3693 3616 -456 -400 495 N -ATOM 1295 CA GLU A 162 23.376 18.344 -6.618 1.00 26.39 C -ANISOU 1295 CA GLU A 162 3030 3463 3534 -461 -454 435 C -ATOM 1296 C GLU A 162 23.589 19.457 -5.586 1.00 28.07 C -ANISOU 1296 C GLU A 162 3265 3588 3811 -515 -542 423 C -ATOM 1297 O GLU A 162 23.180 20.599 -5.798 1.00 24.28 O -ANISOU 1297 O GLU A 162 2810 3027 3387 -549 -609 435 O -ATOM 1298 CB GLU A 162 22.165 17.481 -6.250 1.00 22.99 C -ANISOU 1298 CB GLU A 162 2647 3010 3080 -391 -406 325 C -ATOM 1299 CG GLU A 162 21.622 16.654 -7.419 1.00 22.04 C -ANISOU 1299 CG GLU A 162 2525 2944 2907 -349 -344 326 C -ATOM 1300 CD GLU A 162 21.116 17.526 -8.563 1.00 28.11 C -ANISOU 1300 CD GLU A 162 3295 3693 3692 -376 -382 377 C -ATOM 1301 OE1 GLU A 162 20.096 18.229 -8.376 1.00 28.46 O -ANISOU 1301 OE1 GLU A 162 3372 3655 3786 -374 -429 338 O -ATOM 1302 OE2 GLU A 162 21.736 17.505 -9.650 1.00 30.42 O -ANISOU 1302 OE2 GLU A 162 3553 4057 3948 -394 -364 459 O -ATOM 1303 N ILE A 163 24.235 19.113 -4.477 1.00 28.94 N -ANISOU 1303 N ILE A 163 3372 3712 3913 -523 -545 400 N -ATOM 1304 CA ILE A 163 24.619 20.093 -3.466 1.00 31.08 C -ANISOU 1304 CA ILE A 163 3669 3911 4230 -584 -633 389 C -ATOM 1305 C ILE A 163 25.507 21.199 -4.059 1.00 36.37 C -ANISOU 1305 C ILE A 163 4301 4570 4948 -671 -707 503 C -ATOM 1306 O ILE A 163 25.245 22.389 -3.870 1.00 34.84 O -ANISOU 1306 O ILE A 163 4150 4273 4815 -717 -790 494 O -ATOM 1307 CB ILE A 163 25.335 19.407 -2.288 1.00 30.12 C -ANISOU 1307 CB ILE A 163 3535 3832 4075 -586 -624 367 C -ATOM 1308 CG1 ILE A 163 24.404 18.366 -1.653 1.00 30.00 C -ANISOU 1308 CG1 ILE A 163 3560 3822 4018 -506 -557 261 C -ATOM 1309 CG2 ILE A 163 25.808 20.441 -1.265 1.00 23.99 C -ANISOU 1309 CG2 ILE A 163 2791 2987 3338 -660 -724 356 C -ATOM 1310 CD1 ILE A 163 25.059 17.503 -0.590 1.00 29.47 C -ANISOU 1310 CD1 ILE A 163 3477 3810 3911 -499 -537 250 C -ATOM 1311 N ARG A 164 26.551 20.802 -4.781 1.00 39.29 N -ANISOU 1311 N ARG A 164 4589 5045 5292 -692 -675 613 N -ATOM 1312 CA ARG A 164 27.413 21.763 -5.468 1.00 39.64 C -ANISOU 1312 CA ARG A 164 4583 5099 5377 -778 -735 741 C -ATOM 1313 C ARG A 164 26.626 22.742 -6.335 1.00 40.22 C -ANISOU 1313 C ARG A 164 4689 5096 5495 -795 -777 760 C -ATOM 1314 O ARG A 164 26.840 23.949 -6.254 1.00 41.51 O -ANISOU 1314 O ARG A 164 4867 5177 5726 -871 -873 804 O -ATOM 1315 CB ARG A 164 28.439 21.045 -6.338 1.00 38.20 C -ANISOU 1315 CB ARG A 164 4304 5062 5149 -773 -666 854 C -ATOM 1316 CG ARG A 164 29.537 20.337 -5.582 1.00 40.50 C -ANISOU 1316 CG ARG A 164 4537 5432 5418 -777 -645 883 C -ATOM 1317 CD ARG A 164 30.415 19.620 -6.587 1.00 45.34 C -ANISOU 1317 CD ARG A 164 5054 6186 5987 -752 -561 989 C -ATOM 1318 NE ARG A 164 31.505 18.861 -5.984 1.00 45.35 N -ANISOU 1318 NE ARG A 164 4984 6275 5972 -742 -530 1032 N -ATOM 1319 CZ ARG A 164 32.136 17.874 -6.610 1.00 45.01 C -ANISOU 1319 CZ ARG A 164 4869 6352 5882 -680 -431 1086 C -ATOM 1320 NH1 ARG A 164 31.763 17.532 -7.836 1.00 43.65 N -ANISOU 1320 NH1 ARG A 164 4697 6225 5663 -628 -353 1093 N -ATOM 1321 NH2 ARG A 164 33.124 17.221 -6.015 1.00 46.66 N -ANISOU 1321 NH2 ARG A 164 5007 6634 6087 -667 -408 1131 N -ATOM 1322 N LYS A 165 25.725 22.223 -7.169 1.00 39.16 N -ANISOU 1322 N LYS A 165 4568 4986 5325 -728 -712 730 N -ATOM 1323 CA LYS A 165 24.926 23.070 -8.055 1.00 36.92 C -ANISOU 1323 CA LYS A 165 4309 4640 5078 -739 -750 757 C -ATOM 1324 C LYS A 165 24.051 24.037 -7.273 1.00 38.28 C -ANISOU 1324 C LYS A 165 4559 4658 5327 -742 -828 674 C -ATOM 1325 O LYS A 165 23.826 25.167 -7.701 1.00 41.50 O -ANISOU 1325 O LYS A 165 4983 4984 5802 -785 -901 723 O -ATOM 1326 CB LYS A 165 24.041 22.232 -8.978 1.00 36.84 C -ANISOU 1326 CB LYS A 165 4304 4686 5007 -666 -670 728 C -ATOM 1327 CG LYS A 165 24.808 21.339 -9.936 1.00 44.58 C -ANISOU 1327 CG LYS A 165 5220 5812 5907 -653 -589 803 C -ATOM 1328 CD LYS A 165 23.944 20.907 -11.117 1.00 48.87 C -ANISOU 1328 CD LYS A 165 5777 6396 6396 -610 -541 798 C -ATOM 1329 CE LYS A 165 22.656 20.256 -10.665 1.00 52.20 C -ANISOU 1329 CE LYS A 165 6259 6766 6808 -539 -514 667 C -ATOM 1330 NZ LYS A 165 21.890 19.700 -11.816 1.00 54.86 N -ANISOU 1330 NZ LYS A 165 6608 7154 7083 -503 -470 664 N -ATOM 1331 N HIS A 166 23.543 23.584 -6.134 1.00 36.16 N -ANISOU 1331 N HIS A 166 4340 4352 5049 -693 -809 550 N -ATOM 1332 CA HIS A 166 22.711 24.427 -5.289 1.00 35.18 C -ANISOU 1332 CA HIS A 166 4291 4089 4986 -682 -868 456 C -ATOM 1333 C HIS A 166 23.546 25.526 -4.628 1.00 39.97 C -ANISOU 1333 C HIS A 166 4919 4614 5653 -769 -970 485 C -ATOM 1334 O HIS A 166 23.086 26.653 -4.492 1.00 43.82 O -ANISOU 1334 O HIS A 166 5461 4973 6216 -788 -1045 464 O -ATOM 1335 CB HIS A 166 21.977 23.579 -4.243 1.00 34.26 C -ANISOU 1335 CB HIS A 166 4216 3972 4829 -605 -810 322 C -ATOM 1336 CG HIS A 166 21.103 24.371 -3.319 1.00 36.11 C -ANISOU 1336 CG HIS A 166 4528 4077 5114 -580 -855 215 C -ATOM 1337 ND1 HIS A 166 21.391 24.534 -1.982 1.00 37.65 N -ANISOU 1337 ND1 HIS A 166 4771 4231 5304 -594 -884 138 N -ATOM 1338 CD2 HIS A 166 19.945 25.040 -3.539 1.00 41.24 C -ANISOU 1338 CD2 HIS A 166 5217 4634 5820 -537 -872 173 C -ATOM 1339 CE1 HIS A 166 20.449 25.270 -1.415 1.00 41.81 C -ANISOU 1339 CE1 HIS A 166 5368 4644 5876 -556 -911 44 C -ATOM 1340 NE2 HIS A 166 19.563 25.592 -2.340 1.00 45.18 N -ANISOU 1340 NE2 HIS A 166 5786 5035 6346 -518 -904 66 N -ATOM 1341 N LYS A 167 24.771 25.203 -4.221 1.00 41.64 N -ANISOU 1341 N LYS A 167 5088 4897 5835 -824 -978 534 N -ATOM 1342 CA LYS A 167 25.672 26.220 -3.681 1.00 48.36 C -ANISOU 1342 CA LYS A 167 5950 5682 6741 -925 -1085 579 C -ATOM 1343 C LYS A 167 25.999 27.243 -4.759 1.00 54.86 C -ANISOU 1343 C LYS A 167 6743 6470 7630 -998 -1150 708 C -ATOM 1344 O LYS A 167 26.024 28.448 -4.505 1.00 53.58 O -ANISOU 1344 O LYS A 167 6631 6179 7548 -1060 -1253 715 O -ATOM 1345 CB LYS A 167 26.969 25.594 -3.171 1.00 46.75 C -ANISOU 1345 CB LYS A 167 5685 5584 6493 -972 -1079 632 C -ATOM 1346 CG LYS A 167 26.853 24.825 -1.865 1.00 45.95 C -ANISOU 1346 CG LYS A 167 5621 5498 6338 -929 -1048 517 C -ATOM 1347 CD LYS A 167 28.213 24.259 -1.488 1.00 46.64 C -ANISOU 1347 CD LYS A 167 5634 5696 6392 -981 -1051 597 C -ATOM 1348 CE LYS A 167 28.255 23.739 -0.064 1.00 47.37 C -ANISOU 1348 CE LYS A 167 5768 5791 6439 -966 -1054 500 C -ATOM 1349 NZ LYS A 167 29.629 23.260 0.277 1.00 49.68 N -ANISOU 1349 NZ LYS A 167 5978 6191 6708 -1023 -1068 594 N -ATOM 1350 N GLU A 168 26.267 26.743 -5.962 1.00 59.62 N -ANISOU 1350 N GLU A 168 7268 7189 8197 -990 -1089 813 N -ATOM 1351 CA GLU A 168 26.526 27.588 -7.118 1.00 63.31 C -ANISOU 1351 CA GLU A 168 7696 7648 8709 -1054 -1136 949 C -ATOM 1352 C GLU A 168 25.337 28.504 -7.335 1.00 64.70 C -ANISOU 1352 C GLU A 168 7947 7680 8957 -1030 -1187 903 C -ATOM 1353 O GLU A 168 25.486 29.721 -7.441 1.00 64.46 O -ANISOU 1353 O GLU A 168 7939 7540 9013 -1102 -1289 961 O -ATOM 1354 CB GLU A 168 26.748 26.725 -8.359 1.00 67.57 C -ANISOU 1354 CB GLU A 168 8155 8345 9173 -1023 -1040 1037 C -ATOM 1355 CG GLU A 168 27.113 27.504 -9.610 1.00 74.95 C -ANISOU 1355 CG GLU A 168 9038 9303 10136 -1093 -1078 1195 C -ATOM 1356 CD GLU A 168 28.569 27.933 -9.626 1.00 80.51 C -ANISOU 1356 CD GLU A 168 9667 10062 10862 -1201 -1128 1334 C -ATOM 1357 OE1 GLU A 168 29.423 27.151 -9.155 1.00 80.92 O -ANISOU 1357 OE1 GLU A 168 9666 10214 10866 -1198 -1081 1338 O -ATOM 1358 OE2 GLU A 168 28.858 29.052 -10.105 1.00 82.74 O -ANISOU 1358 OE2 GLU A 168 9937 10288 11214 -1291 -1216 1447 O -ATOM 1359 N LYS A 169 24.153 27.901 -7.396 1.00 66.12 N -ANISOU 1359 N LYS A 169 8159 7858 9104 -928 -1119 804 N -ATOM 1360 CA LYS A 169 22.906 28.643 -7.520 1.00 69.76 C -ANISOU 1360 CA LYS A 169 8683 8191 9632 -884 -1155 750 C -ATOM 1361 C LYS A 169 22.767 29.625 -6.357 1.00 73.03 C -ANISOU 1361 C LYS A 169 9181 8440 10127 -903 -1242 664 C -ATOM 1362 O LYS A 169 22.772 30.830 -6.570 1.00 74.80 O -ANISOU 1362 O LYS A 169 9435 8544 10443 -955 -1336 714 O -ATOM 1363 CB LYS A 169 21.714 27.683 -7.563 1.00 71.17 C -ANISOU 1363 CB LYS A 169 8876 8410 9757 -772 -1063 649 C -ATOM 1364 CG LYS A 169 20.495 28.213 -8.305 1.00 74.66 C -ANISOU 1364 CG LYS A 169 9336 8782 10248 -728 -1080 654 C -ATOM 1365 CD LYS A 169 19.393 27.164 -8.358 1.00 78.02 C -ANISOU 1365 CD LYS A 169 9763 9264 10615 -630 -991 566 C -ATOM 1366 CE LYS A 169 18.212 27.621 -9.206 1.00 81.73 C -ANISOU 1366 CE LYS A 169 10236 9687 11131 -591 -1010 590 C -ATOM 1367 NZ LYS A 169 17.282 28.513 -8.454 1.00 83.62 N -ANISOU 1367 NZ LYS A 169 10535 9771 11467 -544 -1057 506 N -ATOM 1368 N MET A 170 22.653 29.102 -5.136 1.00 73.73 N -ANISOU 1368 N MET A 170 9313 8524 10178 -862 -1212 535 N -ATOM 1369 CA MET A 170 22.573 29.923 -3.921 1.00 75.42 C -ANISOU 1369 CA MET A 170 9616 8596 10445 -877 -1286 435 C -ATOM 1370 C MET A 170 23.399 31.207 -3.996 1.00 81.37 C -ANISOU 1370 C MET A 170 10388 9244 11285 -992 -1412 521 C -ATOM 1371 O MET A 170 22.899 32.290 -3.693 1.00 81.71 O -ANISOU 1371 O MET A 170 10510 9123 11415 -992 -1488 472 O -ATOM 1372 CB MET A 170 23.006 29.113 -2.696 1.00 73.20 C -ANISOU 1372 CB MET A 170 9350 8375 10088 -868 -1250 344 C -ATOM 1373 CG MET A 170 21.975 28.116 -2.204 1.00 71.69 C -ANISOU 1373 CG MET A 170 9176 8229 9833 -753 -1148 221 C -ATOM 1374 SD MET A 170 20.895 28.815 -0.948 1.00 99.07 S -ANISOU 1374 SD MET A 170 12762 11543 13338 -687 -1172 47 S -ATOM 1375 CE MET A 170 22.074 29.148 0.360 1.00 77.65 C -ANISOU 1375 CE MET A 170 10101 8802 10602 -779 -1251 9 C -ATOM 1376 N SER A 171 24.665 31.081 -4.387 1.00 86.43 N -ANISOU 1376 N SER A 171 10954 9978 11906 -1088 -1435 650 N -ATOM 1377 CA SER A 171 25.537 32.243 -4.533 1.00 92.36 C -ANISOU 1377 CA SER A 171 11708 10646 12740 -1213 -1558 755 C -ATOM 1378 C SER A 171 24.917 33.251 -5.488 1.00100.52 C -ANISOU 1378 C SER A 171 12758 11571 13866 -1218 -1611 824 C -ATOM 1379 O SER A 171 24.727 34.411 -5.138 1.00103.38 O -ANISOU 1379 O SER A 171 13199 11757 14325 -1254 -1713 798 O -ATOM 1380 CB SER A 171 26.918 31.831 -5.047 1.00 90.61 C -ANISOU 1380 CB SER A 171 11376 10575 12478 -1305 -1554 910 C -ATOM 1381 OG SER A 171 27.594 31.016 -4.107 1.00 89.08 O -ANISOU 1381 OG SER A 171 11164 10468 12214 -1310 -1524 861 O -ATOM 1382 N LYS A 172 24.598 32.789 -6.692 1.00106.19 N -ANISOU 1382 N LYS A 172 13404 12390 14551 -1182 -1543 911 N -ATOM 1383 CA LYS A 172 24.037 33.636 -7.738 1.00114.29 C -ANISOU 1383 CA LYS A 172 14430 13342 15654 -1189 -1589 1001 C -ATOM 1384 C LYS A 172 22.527 33.788 -7.590 1.00121.54 C -ANISOU 1384 C LYS A 172 15416 14155 16608 -1072 -1566 880 C -ATOM 1385 O LYS A 172 21.903 34.601 -8.273 1.00121.40 O -ANISOU 1385 O LYS A 172 15413 14044 16671 -1064 -1615 935 O -ATOM 1386 CB LYS A 172 24.344 33.033 -9.107 1.00113.55 C -ANISOU 1386 CB LYS A 172 14232 13419 15494 -1202 -1524 1145 C -ATOM 1387 CG LYS A 172 25.741 32.448 -9.234 1.00113.66 C -ANISOU 1387 CG LYS A 172 14157 13589 15438 -1278 -1497 1244 C -ATOM 1388 CD LYS A 172 25.903 31.653 -10.524 1.00113.13 C -ANISOU 1388 CD LYS A 172 13997 13703 15282 -1260 -1404 1352 C -ATOM 1389 CE LYS A 172 25.520 32.472 -11.749 1.00114.38 C -ANISOU 1389 CE LYS A 172 14140 13830 15488 -1292 -1450 1479 C -ATOM 1390 NZ LYS A 172 24.046 32.527 -11.972 1.00114.81 N -ANISOU 1390 NZ LYS A 172 14253 13806 15563 -1196 -1436 1393 N -ATOM 1391 N ASP A 173 21.948 33.000 -6.690 1.00128.21 N -ANISOU 1391 N ASP A 173 16297 15022 17396 -980 -1492 725 N -ATOM 1392 CA ASP A 173 20.505 32.969 -6.494 1.00134.80 C -ANISOU 1392 CA ASP A 173 17180 15787 18252 -860 -1451 610 C -ATOM 1393 C ASP A 173 20.058 34.067 -5.540 1.00141.78 C -ANISOU 1393 C ASP A 173 18169 16468 19233 -841 -1528 504 C -ATOM 1394 O ASP A 173 20.614 34.227 -4.452 1.00142.74 O -ANISOU 1394 O ASP A 173 18346 16542 19347 -876 -1562 425 O -ATOM 1395 CB ASP A 173 20.065 31.599 -5.969 1.00134.04 C -ANISOU 1395 CB ASP A 173 17070 15812 18049 -773 -1334 499 C -ATOM 1396 CG ASP A 173 19.147 30.871 -6.932 1.00134.04 C -ANISOU 1396 CG ASP A 173 17018 15903 18008 -700 -1255 523 C -ATOM 1397 OD1 ASP A 173 18.662 29.777 -6.574 1.00133.67 O -ANISOU 1397 OD1 ASP A 173 16962 15943 17885 -629 -1164 438 O -ATOM 1398 OD2 ASP A 173 18.912 31.393 -8.044 1.00134.40 O -ANISOU 1398 OD2 ASP A 173 17034 15934 18097 -719 -1290 632 O -ATOM 1399 N GLY A 174 19.050 34.825 -5.956 1.00146.99 N -ANISOU 1399 N GLY A 174 18857 17009 19983 -784 -1558 503 N -ATOM 1400 CA GLY A 174 18.419 34.624 -7.248 1.00150.38 C -ANISOU 1400 CA GLY A 174 19218 17505 20415 -753 -1527 606 C -ATOM 1401 C GLY A 174 17.759 35.908 -7.700 1.00154.92 C -ANISOU 1401 C GLY A 174 19829 17909 21127 -739 -1613 652 C -ATOM 1402 O GLY A 174 17.625 36.174 -8.895 1.00154.82 O -ANISOU 1402 O GLY A 174 19762 17919 21141 -765 -1639 791 O -ATOM 1403 N LYS A 175 17.346 36.706 -6.724 1.00159.61 N -ANISOU 1403 N LYS A 175 20516 18325 21802 -695 -1658 534 N -ATOM 1404 CA LYS A 175 16.773 38.016 -6.983 1.00164.71 C -ANISOU 1404 CA LYS A 175 21212 18777 22595 -676 -1747 563 C -ATOM 1405 C LYS A 175 17.381 39.024 -6.016 1.00169.92 C -ANISOU 1405 C LYS A 175 21976 19255 23329 -731 -1844 496 C -ATOM 1406 O LYS A 175 17.436 40.221 -6.302 1.00172.72 O -ANISOU 1406 O LYS A 175 22375 19441 23810 -771 -1951 560 O -ATOM 1407 CB LYS A 175 15.261 37.973 -6.832 1.00164.33 C -ANISOU 1407 CB LYS A 175 21176 18679 22583 -524 -1690 466 C -ATOM 1408 N LYS A 176 17.847 38.526 -4.874 1.00170.94 N -ANISOU 1408 N LYS A 176 22149 19420 23379 -738 -1812 370 N -ATOM 1409 CA LYS A 176 18.408 39.380 -3.834 1.00172.46 C -ANISOU 1409 CA LYS A 176 22453 19452 23623 -791 -1902 284 C -ATOM 1410 C LYS A 176 19.935 39.385 -3.825 1.00173.54 C -ANISOU 1410 C LYS A 176 22567 19644 23725 -954 -1972 381 C -ATOM 1411 O LYS A 176 20.549 39.223 -2.771 1.00174.31 O -ANISOU 1411 O LYS A 176 22717 19742 23769 -994 -1986 287 O -ATOM 1412 CB LYS A 176 17.866 38.981 -2.464 1.00171.32 C -ANISOU 1412 CB LYS A 176 22386 19292 23417 -691 -1833 72 C -ATOM 1413 N LYS A 177 20.528 39.559 -5.005 1.00173.73 N -ANISOU 1413 N LYS A 177 22508 19725 23777 -1048 -2015 575 N -ATOM 1414 CA LYS A 177 21.967 39.817 -5.151 1.00174.17 C -ANISOU 1414 CA LYS A 177 22532 19812 23832 -1212 -2099 700 C -ATOM 1415 C LYS A 177 22.469 39.658 -6.615 1.00166.20 C -ANISOU 1415 C LYS A 177 21399 18935 22815 -1287 -2097 922 C -ATOM 1416 O LYS A 177 22.104 40.491 -7.446 1.00167.50 O -ANISOU 1416 O LYS A 177 21562 19003 23078 -1299 -2158 1024 O -ATOM 1417 CB LYS A 177 22.792 39.034 -4.124 1.00173.13 C -ANISOU 1417 CB LYS A 177 22404 19787 23592 -1252 -2069 618 C -ATOM 1418 N LYS A 178 23.266 38.643 -6.975 1.00164.39 N -ANISOU 1418 N LYS A 178 21067 18920 22472 -1332 -2029 1000 N -ATOM 1419 CA LYS A 178 23.734 37.566 -6.111 1.00162.60 C -ANISOU 1419 CA LYS A 178 20827 18826 22128 -1317 -1953 904 C -ATOM 1420 C LYS A 178 25.140 37.088 -6.477 1.00161.43 C -ANISOU 1420 C LYS A 178 20576 18842 21917 -1435 -1953 1047 C -ATOM 1421 O LYS A 178 25.815 36.478 -5.644 1.00160.58 O -ANISOU 1421 O LYS A 178 20462 18810 21740 -1458 -1932 991 O -ATOM 1422 CB LYS A 178 22.750 36.412 -6.112 1.00161.40 C -ANISOU 1422 CB LYS A 178 20653 18788 21885 -1175 -1813 802 C -ATOM 1423 N LYS A 179 25.562 37.362 -7.715 1.00161.14 N -ANISOU 1423 N LYS A 179 20455 18866 21903 -1504 -1974 1235 N -ATOM 1424 CA LYS A 179 26.922 37.072 -8.195 1.00160.46 C -ANISOU 1424 CA LYS A 179 20262 18935 21773 -1620 -1978 1398 C -ATOM 1425 C LYS A 179 26.954 36.263 -9.489 1.00159.91 C -ANISOU 1425 C LYS A 179 20077 19063 21617 -1591 -1874 1519 C -ATOM 1426 O LYS A 179 26.610 35.085 -9.493 1.00158.76 O -ANISOU 1426 O LYS A 179 19905 19051 21368 -1494 -1752 1444 O -ATOM 1427 CB LYS A 179 27.730 36.371 -7.146 1.00159.25 C -ANISOU 1427 CB LYS A 179 20099 18861 21548 -1643 -1956 1326 C -ATOM 1428 N LYS A 180 27.399 36.898 -10.572 1.00160.68 N -ANISOU 1428 N LYS A 180 20113 19181 21756 -1679 -1924 1708 N -ATOM 1429 CA LYS A 180 27.535 36.243 -11.875 1.00159.71 C -ANISOU 1429 CA LYS A 180 19885 19252 21546 -1667 -1833 1838 C -ATOM 1430 C LYS A 180 26.196 36.092 -12.593 1.00158.71 C -ANISOU 1430 C LYS A 180 19786 19112 21406 -1558 -1783 1798 C -ATOM 1431 O LYS A 180 26.126 36.176 -13.819 1.00158.63 O -ANISOU 1431 O LYS A 180 19718 19183 21373 -1576 -1768 1935 O -ATOM 1432 CB LYS A 180 28.231 34.890 -11.733 1.00158.45 C -ANISOU 1432 CB LYS A 180 19648 19301 21255 -1635 -1714 1818 C -TER 1433 LYS A 180 -HETATM 1434 C1 9LI A 201 24.262 14.237 15.368 1.00 66.49 C -ANISOU 1434 C1 9LI A 201 8631 8773 7859 -579 -679 -346 C -HETATM 1435 CL1 9LI A 201 26.612 12.662 10.139 1.00 52.34 CL -ANISOU 1435 CL1 9LI A 201 6490 6997 6400 -514 -585 48 CL -HETATM 1436 C2 9LI A 201 24.320 14.376 13.871 1.00 66.16 C -ANISOU 1436 C2 9LI A 201 8533 8679 7927 -555 -656 -299 C -HETATM 1437 CL2 9LI A 201 23.161 16.242 8.077 1.00 49.64 CL -ANISOU 1437 CL2 9LI A 201 6338 6332 6191 -460 -583 -233 CL -HETATM 1438 C3 9LI A 201 25.146 13.702 13.046 1.00 65.80 C -ANISOU 1438 C3 9LI A 201 8396 8669 7936 -556 -648 -183 C -HETATM 1439 C4 9LI A 201 24.857 14.154 11.671 1.00 61.10 C -ANISOU 1439 C4 9LI A 201 7779 8008 7427 -529 -624 -179 C -HETATM 1440 C5 9LI A 201 23.828 15.115 11.812 1.00 58.85 C -ANISOU 1440 C5 9LI A 201 7576 7645 7140 -513 -625 -294 C -HETATM 1441 N6 9LI A 201 23.530 15.224 13.151 1.00 63.82 N -ANISOU 1441 N6 9LI A 201 8273 8294 7684 -525 -641 -368 N -HETATM 1442 C8 9LI A 201 23.319 15.746 10.689 1.00 52.10 C -ANISOU 1442 C8 9LI A 201 6721 6716 6359 -488 -611 -311 C -HETATM 1443 C9 9LI A 201 23.819 15.430 9.450 1.00 46.29 C -ANISOU 1443 C9 9LI A 201 5911 5992 5686 -484 -594 -219 C -HETATM 1444 C10 9LI A 201 24.825 14.489 9.287 1.00 47.22 C -ANISOU 1444 C10 9LI A 201 5952 6189 5801 -494 -584 -114 C -HETATM 1445 C11 9LI A 201 25.355 13.845 10.387 1.00 55.51 C -ANISOU 1445 C11 9LI A 201 6995 7305 6790 -515 -600 -91 C -HETATM 1446 C14 9LI A 201 26.172 12.687 13.479 1.00 66.80 C -ANISOU 1446 C14 9LI A 201 8455 8888 8038 -577 -660 -74 C -HETATM 1447 C15 9LI A 201 27.434 13.399 13.980 1.00 66.97 C -ANISOU 1447 C15 9LI A 201 8468 8930 8048 -675 -776 -24 C -HETATM 1448 N16 9LI A 201 28.434 12.402 14.387 1.00 64.29 N -ANISOU 1448 N16 9LI A 201 8051 8685 7692 -690 -789 93 N -HETATM 1449 PG GCP A 202 14.988 0.822 9.002 1.00 25.43 P -ANISOU 1449 PG GCP A 202 3136 3521 3006 -51 145 -97 P -HETATM 1450 O1G GCP A 202 16.239 1.557 9.373 1.00 27.28 O -ANISOU 1450 O1G GCP A 202 3368 3782 3217 -53 112 -87 O -HETATM 1451 O2G GCP A 202 14.391 0.084 10.167 1.00 27.49 O -ANISOU 1451 O2G GCP A 202 3391 3821 3234 -67 166 -64 O -HETATM 1452 O3G GCP A 202 14.009 1.694 8.258 1.00 30.09 O -ANISOU 1452 O3G GCP A 202 3729 4089 3615 -48 149 -160 O -HETATM 1453 C3B GCP A 202 15.455 -0.509 7.867 1.00 14.31 C -ANISOU 1453 C3B GCP A 202 1734 2049 1655 -30 157 -55 C -HETATM 1454 PB GCP A 202 16.345 0.048 6.384 1.00 23.42 P -ANISOU 1454 PB GCP A 202 2892 3168 2840 -4 145 -74 P -HETATM 1455 O1B GCP A 202 15.449 0.948 5.565 1.00 20.37 O -ANISOU 1455 O1B GCP A 202 2513 2765 2463 -12 140 -132 O -HETATM 1456 O2B GCP A 202 17.690 0.595 6.748 1.00 23.04 O -ANISOU 1456 O2B GCP A 202 2824 3154 2777 0 122 -43 O -HETATM 1457 O3A GCP A 202 16.623 -1.273 5.512 1.00 23.25 O -ANISOU 1457 O3A GCP A 202 2887 3091 2855 23 168 -48 O -HETATM 1458 PA GCP A 202 17.923 -2.210 5.673 1.00 24.57 P -ANISOU 1458 PA GCP A 202 3046 3252 3039 58 177 15 P -HETATM 1459 O1A GCP A 202 19.057 -1.658 4.848 1.00 26.52 O -ANISOU 1459 O1A GCP A 202 3276 3509 3293 87 176 21 O -HETATM 1460 O2A GCP A 202 18.135 -2.514 7.136 1.00 26.04 O -ANISOU 1460 O2A GCP A 202 3213 3478 3203 42 166 67 O -HETATM 1461 O5' GCP A 202 17.428 -3.541 4.923 1.00 24.06 O -ANISOU 1461 O5' GCP A 202 3020 3112 3011 76 201 10 O -HETATM 1462 C5' GCP A 202 16.166 -4.133 5.241 1.00 22.63 C -ANISOU 1462 C5' GCP A 202 2857 2905 2835 43 202 1 C -HETATM 1463 C4' GCP A 202 16.114 -5.543 4.668 1.00 23.09 C -ANISOU 1463 C4' GCP A 202 2957 2882 2934 62 216 12 C -HETATM 1464 O4' GCP A 202 16.076 -5.482 3.238 1.00 23.77 O -ANISOU 1464 O4' GCP A 202 3076 2926 3028 80 223 -42 O -HETATM 1465 C3' GCP A 202 17.382 -6.294 5.027 1.00 24.66 C -ANISOU 1465 C3' GCP A 202 3147 3067 3154 109 227 72 C -HETATM 1466 O3' GCP A 202 17.037 -7.667 5.210 1.00 27.83 O -ANISOU 1466 O3' GCP A 202 3582 3398 3594 109 231 101 O -HETATM 1467 C2' GCP A 202 18.267 -6.140 3.807 1.00 27.41 C -ANISOU 1467 C2' GCP A 202 3507 3397 3511 162 247 44 C -HETATM 1468 O2' GCP A 202 19.145 -7.254 3.634 1.00 34.04 O -ANISOU 1468 O2' GCP A 202 4362 4185 4388 222 271 80 O -HETATM 1469 C1' GCP A 202 17.257 -6.069 2.679 1.00 24.92 C -ANISOU 1469 C1' GCP A 202 3237 3040 3191 141 247 -28 C -HETATM 1470 N9 GCP A 202 17.754 -5.211 1.585 1.00 23.03 N -ANISOU 1470 N9 GCP A 202 2995 2826 2931 163 256 -66 N -HETATM 1471 C8 GCP A 202 18.223 -3.958 1.704 1.00 16.12 C -ANISOU 1471 C8 GCP A 202 2074 2019 2031 157 245 -60 C -HETATM 1472 N7 GCP A 202 18.579 -3.474 0.488 1.00 18.57 N -ANISOU 1472 N7 GCP A 202 2393 2336 2327 177 257 -90 N -HETATM 1473 C5 GCP A 202 18.341 -4.432 -0.432 1.00 19.75 C -ANISOU 1473 C5 GCP A 202 2598 2423 2483 200 279 -124 C -HETATM 1474 C6 GCP A 202 18.483 -4.590 -1.901 1.00 20.33 C -ANISOU 1474 C6 GCP A 202 2715 2473 2535 229 302 -170 C -HETATM 1475 O6 GCP A 202 18.939 -3.672 -2.611 1.00 21.68 O -ANISOU 1475 O6 GCP A 202 2864 2694 2678 236 307 -174 O -HETATM 1476 N1 GCP A 202 18.103 -5.749 -2.455 1.00 19.27 N -ANISOU 1476 N1 GCP A 202 2649 2263 2411 244 314 -207 N -HETATM 1477 C2 GCP A 202 17.612 -6.764 -1.719 1.00 20.57 C -ANISOU 1477 C2 GCP A 202 2838 2366 2611 231 304 -194 C -HETATM 1478 N2 GCP A 202 17.250 -7.912 -2.335 1.00 18.65 N -ANISOU 1478 N2 GCP A 202 2672 2034 2381 242 310 -234 N -HETATM 1479 N3 GCP A 202 17.450 -6.687 -0.378 1.00 21.35 N -ANISOU 1479 N3 GCP A 202 2892 2488 2731 204 285 -142 N -HETATM 1480 C4 GCP A 202 17.794 -5.573 0.302 1.00 20.56 C -ANISOU 1480 C4 GCP A 202 2727 2468 2615 190 274 -110 C -HETATM 1481 MG MG A 203 18.308 1.342 8.691 1.00 32.23 MG -ANISOU 1481 MG MG A 203 3972 4398 3875 -35 83 -19 MG -HETATM 1482 C1 GOL A 204 5.212 10.645 6.656 1.00 63.80 C -ANISOU 1482 C1 GOL A 204 7868 8267 8108 185 191 -558 C -HETATM 1483 O1 GOL A 204 5.115 9.582 5.732 1.00 62.30 O -ANISOU 1483 O1 GOL A 204 7652 8084 7937 141 176 -496 O -HETATM 1484 C2 GOL A 204 6.594 11.290 6.593 1.00 64.31 C -ANISOU 1484 C2 GOL A 204 7996 8282 8158 167 142 -579 C -HETATM 1485 O2 GOL A 204 7.483 10.574 7.424 1.00 63.57 O -ANISOU 1485 O2 GOL A 204 7931 8227 7996 135 151 -572 O -HETATM 1486 C3 GOL A 204 6.487 12.740 7.069 1.00 66.37 C -ANISOU 1486 C3 GOL A 204 8287 8498 8433 215 134 -649 C -HETATM 1487 O3 GOL A 204 7.751 13.371 7.056 1.00 65.74 O -ANISOU 1487 O3 GOL A 204 8264 8371 8342 187 81 -664 O -HETATM 1488 C1 EDO A 205 6.854 26.557 0.905 1.00 61.60 C -ANISOU 1488 C1 EDO A 205 7922 6784 8698 384 -500 -638 C -HETATM 1489 O1 EDO A 205 6.789 25.191 0.486 1.00 62.51 O -ANISOU 1489 O1 EDO A 205 7972 7039 8741 349 -454 -585 O -HETATM 1490 C2 EDO A 205 8.303 26.886 1.229 1.00 59.16 C -ANISOU 1490 C2 EDO A 205 7688 6435 8356 296 -560 -648 C -HETATM 1491 O2 EDO A 205 8.829 25.858 2.072 1.00 56.13 O -ANISOU 1491 O2 EDO A 205 7314 6153 7859 265 -509 -692 O -HETATM 1492 S DMS A 206 22.117 0.734 16.054 1.00 88.65 S -ANISOU 1492 S DMS A 206 11063 11913 10706 -198 -116 281 S -HETATM 1493 O DMS A 206 21.220 2.214 15.552 1.00 36.99 O -ANISOU 1493 O DMS A 206 4569 5337 4150 -205 -107 143 O -HETATM 1494 C1 DMS A 206 21.120 -0.721 15.629 1.00 40.77 C -ANISOU 1494 C1 DMS A 206 4997 5799 4695 -154 -43 308 C -HETATM 1495 C2 DMS A 206 23.559 0.480 14.975 1.00 20.88 C -ANISOU 1495 C2 DMS A 206 2421 3297 2217 -167 -136 355 C -HETATM 1496 C ACT A 207 16.488 20.907 -6.366 1.00 61.01 C -ANISOU 1496 C ACT A 207 7614 7433 8133 -306 -576 135 C -HETATM 1497 O ACT A 207 16.636 20.294 -7.447 1.00 59.76 O -ANISOU 1497 O ACT A 207 7427 7353 7926 -315 -548 192 O -HETATM 1498 OXT ACT A 207 15.320 20.930 -5.908 1.00 59.91 O -ANISOU 1498 OXT ACT A 207 7494 7248 8020 -254 -566 63 O -HETATM 1499 CH3 ACT A 207 17.646 21.569 -5.670 1.00 60.91 C -ANISOU 1499 CH3 ACT A 207 7613 7389 8143 -357 -620 152 C -HETATM 1500 MG MG A 208 11.818 7.424 7.750 1.00 37.97 MG -ANISOU 1500 MG MG A 208 4746 5042 4638 -4 98 -410 MG -HETATM 1501 O HOH A 301 18.246 3.658 8.352 1.00 29.29 O -ANISOU 1501 O HOH A 301 3612 4027 3491 -61 37 -102 O -HETATM 1502 O HOH A 302 18.621 -0.878 9.277 1.00 24.70 O -ANISOU 1502 O HOH A 302 3009 3436 2941 -13 113 81 O -HETATM 1503 O HOH A 303 12.131 -0.798 10.168 1.00 21.53 O -ANISOU 1503 O HOH A 303 2620 3062 2500 -88 213 -66 O -HETATM 1504 O HOH A 304 10.363 5.818 1.362 1.00 16.92 O -ANISOU 1504 O HOH A 304 2044 2245 2141 -30 57 -324 O -HETATM 1505 O HOH A 305 13.822 8.899 7.271 1.00 20.45 O -ANISOU 1505 O HOH A 305 2562 2776 2432 -32 11 -409 O -HETATM 1506 O HOH A 306 27.118 3.193 -9.037 1.00 27.50 O -ANISOU 1506 O HOH A 306 3167 4077 3205 323 476 226 O -HETATM 1507 O HOH A 307 -0.641 2.761 -0.147 1.00 16.43 O -ANISOU 1507 O HOH A 307 1614 2314 2314 -220 5 -148 O -HETATM 1508 O HOH A 308 10.885 9.226 9.269 1.00 39.47 O -ANISOU 1508 O HOH A 308 4968 5245 4786 36 110 -522 O -HETATM 1509 O HOH A 309 25.066 -3.333 2.944 1.00 24.41 O -ANISOU 1509 O HOH A 309 2853 3297 3124 333 279 256 O -HETATM 1510 O HOH A 310 19.797 -3.972 8.479 1.00 26.66 O -ANISOU 1510 O HOH A 310 3255 3579 3296 74 159 209 O -HETATM 1511 O HOH A 311 21.580 -5.196 -9.682 1.00 33.67 O -ANISOU 1511 O HOH A 311 4603 4244 3946 502 557 -364 O -HETATM 1512 O HOH A 312 23.346 2.098 9.633 1.00 42.44 O -ANISOU 1512 O HOH A 312 5143 5821 5162 -62 -44 195 O -HETATM 1513 O HOH A 313 18.694 4.264 -12.940 1.00 32.87 O -ANISOU 1513 O HOH A 313 4265 4521 3704 51 211 -137 O -HETATM 1514 O HOH A 314 11.533 4.489 -19.199 1.00 42.67 O -ANISOU 1514 O HOH A 314 5785 5797 4629 -285 -162 -248 O -HETATM 1515 O HOH A 315 18.427 17.986 -6.363 1.00 32.23 O -ANISOU 1515 O HOH A 315 3919 4019 4308 -305 -428 155 O -HETATM 1516 O HOH A 316 4.236 -1.174 2.199 1.00 30.15 O -ANISOU 1516 O HOH A 316 3631 3930 3896 -235 102 -174 O -HETATM 1517 O HOH A 317 12.324 23.514 12.099 1.00 32.34 O -ANISOU 1517 O HOH A 317 4736 3487 4065 143 -361 -1288 O -HETATM 1518 O HOH A 318 10.923 -4.009 0.369 1.00 31.50 O -ANISOU 1518 O HOH A 318 4092 3876 3999 -93 138 -217 O -HETATM 1519 O HOH A 319 25.970 12.427 -11.390 1.00 46.30 O -ANISOU 1519 O HOH A 319 5412 6516 5663 -196 36 561 O -HETATM 1520 O HOH A 320 17.780 11.273 -13.484 1.00 33.06 O -ANISOU 1520 O HOH A 320 4086 4567 3906 -184 -91 165 O -HETATM 1521 O HOH A 321 14.535 -7.310 1.054 1.00 28.29 O -ANISOU 1521 O HOH A 321 3780 3326 3641 56 216 -132 O -HETATM 1522 O HOH A 322 7.652 0.471 4.562 1.00 29.89 O -ANISOU 1522 O HOH A 322 3643 3956 3759 -110 173 -217 O -HETATM 1523 O HOH A 323 7.918 6.690 5.917 1.00 24.34 O -ANISOU 1523 O HOH A 323 2920 3300 3026 28 158 -404 O -HETATM 1524 O HOH A 324 27.101 37.346 -3.596 1.00 57.20 O -ANISOU 1524 O HOH A 324 7489 5556 8687 -1611 -2104 884 O -HETATM 1525 O HOH A 325 7.386 3.419 7.587 1.00 38.52 O -ANISOU 1525 O HOH A 325 4688 5190 4759 -31 233 -298 O -HETATM 1526 O HOH A 326 16.688 8.881 12.690 1.00 35.58 O -ANISOU 1526 O HOH A 326 4570 4885 4065 -136 -70 -407 O -HETATM 1527 O HOH A 327 5.640 10.142 -3.936 1.00 28.00 O -ANISOU 1527 O HOH A 327 3320 3569 3752 -35 -143 -270 O -HETATM 1528 O HOH A 328 39.408 19.703 -2.130 1.00 52.05 O -ANISOU 1528 O HOH A 328 5256 7519 7000 -1184 -883 1698 O -HETATM 1529 O HOH A 329 20.839 24.006 5.372 1.00 36.45 O -ANISOU 1529 O HOH A 329 4931 3995 4921 -523 -890 -417 O -HETATM 1530 O HOH A 330 0.453 6.335 1.139 1.00 33.14 O -ANISOU 1530 O HOH A 330 3727 4432 4432 -22 77 -255 O -HETATM 1531 O HOH A 331 38.104 20.517 -7.720 1.00 58.33 O -ANISOU 1531 O HOH A 331 6014 8429 7721 -1069 -603 1845 O -HETATM 1532 O HOH A 332 -0.073 9.042 0.952 1.00 37.08 O -ANISOU 1532 O HOH A 332 4181 4898 5010 94 67 -295 O -HETATM 1533 O HOH A 333 2.115 7.794 2.418 1.00 41.29 O -ANISOU 1533 O HOH A 333 4836 5435 5419 60 118 -343 O -HETATM 1534 O HOH A 334 10.190 -2.266 2.251 1.00 47.41 O -ANISOU 1534 O HOH A 334 6005 6010 5999 -104 146 -194 O -HETATM 1535 O HOH A 335 13.390 9.128 10.636 1.00 32.30 O -ANISOU 1535 O HOH A 335 4113 4377 3782 -29 44 -490 O -HETATM 1536 O HOH A 336 28.127 1.257 -7.576 1.00 27.54 O -ANISOU 1536 O HOH A 336 3144 4044 3278 442 540 238 O -HETATM 1537 O HOH A 337 27.713 19.918 -9.885 1.00 50.92 O -ANISOU 1537 O HOH A 337 5861 6863 6622 -665 -476 950 O -HETATM 1538 O HOH A 338 9.695 -4.316 4.429 1.00 46.54 O -ANISOU 1538 O HOH A 338 5880 5900 5903 -145 172 -95 O -HETATM 1539 O HOH A 339 26.546 0.244 -10.697 1.00 51.68 O -ANISOU 1539 O HOH A 339 6409 7062 6165 500 637 48 O -HETATM 1540 O HOH A 340 17.346 -10.270 10.006 1.00 44.62 O -ANISOU 1540 O HOH A 340 5635 5582 5737 45 188 429 O -HETATM 1541 O HOH A 341 3.040 23.736 5.244 1.00 40.51 O -ANISOU 1541 O HOH A 341 5138 4464 5789 699 -69 -947 O -HETATM 1542 O HOH A 342 14.128 2.233 11.873 1.00 22.17 O -ANISOU 1542 O HOH A 342 2730 3244 2450 -81 151 -151 O -HETATM 1543 O HOH A 343 11.268 2.649 12.522 1.00 29.78 O -ANISOU 1543 O HOH A 343 3670 4259 3385 -66 233 -223 O -HETATM 1544 O HOH A 344 7.772 6.140 8.336 1.00 34.82 O -ANISOU 1544 O HOH A 344 4247 4724 4260 34 223 -410 O -HETATM 1545 O HOH A 345 28.202 39.437 -11.112 1.00 51.69 O -ANISOU 1545 O HOH A 345 6336 5116 8186 -1916 -2192 1960 O -HETATM 1546 O HOH A 346 20.799 15.187 18.764 1.00 39.21 O -ANISOU 1546 O HOH A 346 5462 5334 4102 -469 -555 -749 O -HETATM 1547 O HOH A 347 16.791 1.304 -14.857 1.00 62.17 O -ANISOU 1547 O HOH A 347 8215 8143 7264 58 225 -343 O -HETATM 1548 O HOH A 348 12.471 20.569 15.983 1.00 53.85 O -ANISOU 1548 O HOH A 348 7488 6623 6350 121 -189 -1369 O -HETATM 1549 O HOH A 349 8.235 -2.712 5.830 1.00 57.29 O -ANISOU 1549 O HOH A 349 7149 7390 7227 -160 195 -102 O -HETATM 1550 O HOH A 350 24.203 9.462 15.252 1.00 40.54 O -ANISOU 1550 O HOH A 350 5138 5699 4566 -437 -462 -88 O -HETATM 1551 O HOH A 351 14.472 19.628 17.461 1.00 49.87 O -ANISOU 1551 O HOH A 351 7032 6257 5661 -39 -280 -1317 O -HETATM 1552 O HOH A 352 37.756 12.489 -9.521 1.00 58.93 O -ANISOU 1552 O HOH A 352 6077 8868 7447 -252 184 1510 O -HETATM 1553 O HOH A 353 28.823 -8.614 0.818 1.00 33.64 O -ANISOU 1553 O HOH A 353 3994 4292 4495 812 554 394 O -HETATM 1554 O HOH A 354 4.138 19.103 5.775 1.00 53.69 O -ANISOU 1554 O HOH A 354 6717 6519 7165 483 35 -824 O -HETATM 1555 O HOH A 355 19.863 17.591 20.126 1.00 56.65 O -ANISOU 1555 O HOH A 355 7899 7423 6203 -457 -601 -1037 O -HETATM 1556 O HOH A 356 19.846 10.623 18.315 1.00 44.50 O -ANISOU 1556 O HOH A 356 5893 6226 4789 -352 -316 -474 O -HETATM 1557 O HOH A 357 18.345 -9.984 1.858 1.00 39.44 O -ANISOU 1557 O HOH A 357 5209 4627 5150 272 302 4 O -HETATM 1558 O HOH A 358 30.159 18.914 -9.630 1.00 49.46 O -ANISOU 1558 O HOH A 358 5520 6876 6398 -668 -395 1090 O -HETATM 1559 O HOH A 359 22.055 -2.702 9.552 1.00 38.72 O -ANISOU 1559 O HOH A 359 4703 5228 4780 64 96 293 O -HETATM 1560 O HOH A 360 7.662 19.236 -4.065 1.00 45.39 O -ANISOU 1560 O HOH A 360 5582 5386 6277 76 -389 -233 O -HETATM 1561 O HOH A 361 25.943 23.241 6.259 1.00 40.40 O -ANISOU 1561 O HOH A 361 5276 4738 5338 -854 -1092 -104 O -HETATM 1562 O HOH A 362 34.769 11.360 -10.037 1.00 55.67 O -ANISOU 1562 O HOH A 362 5967 8249 6935 -134 242 1170 O -HETATM 1563 O HOH A 363 16.749 5.200 -14.344 1.00 49.85 O -ANISOU 1563 O HOH A 363 6457 6672 5811 -43 106 -146 O -HETATM 1564 O HOH A 364 3.600 -1.853 -12.051 1.00 41.48 O -ANISOU 1564 O HOH A 364 5556 5167 5038 -523 -365 -403 O -HETATM 1565 O HOH A 365 21.372 2.185 -11.841 1.00 51.92 O -ANISOU 1565 O HOH A 365 6646 6948 6133 216 378 -129 O -HETATM 1566 O HOH A 366 17.923 -11.105 -5.592 1.00 46.53 O -ANISOU 1566 O HOH A 366 6491 5299 5888 395 395 -427 O -HETATM 1567 O HOH A 367 16.420 -0.832 -13.240 1.00 53.38 O -ANISOU 1567 O HOH A 367 7163 6881 6239 102 251 -428 O -HETATM 1568 O HOH A 368 13.975 11.882 -14.364 1.00 42.12 O -ANISOU 1568 O HOH A 368 5280 5624 5100 -238 -237 115 O -HETATM 1569 O HOH A 369 2.834 0.441 -11.154 1.00 47.21 O -ANISOU 1569 O HOH A 369 6094 5983 5859 -483 -367 -306 O -HETATM 1570 O HOH A 370 12.192 9.603 17.380 1.00 51.11 O -ANISOU 1570 O HOH A 370 6643 7070 5705 -17 156 -681 O -HETATM 1571 O HOH A 371 18.570 18.849 -10.541 1.00 49.04 O -ANISOU 1571 O HOH A 371 5986 6260 6388 -378 -462 399 O -HETATM 1572 O HOH A 372 14.774 14.340 -13.308 1.00 46.16 O -ANISOU 1572 O HOH A 372 5718 6062 5758 -260 -308 211 O -HETATM 1573 O HOH A 373 12.185 -5.325 3.972 1.00 33.92 O -ANISOU 1573 O HOH A 373 4347 4229 4314 -69 184 -75 O -HETATM 1574 O HOH A 374 14.395 1.101 16.331 1.00 54.28 O -ANISOU 1574 O HOH A 374 6805 7552 6267 -149 166 -38 O -HETATM 1575 O HOH A 375 24.047 15.296 -11.083 1.00 46.95 O -ANISOU 1575 O HOH A 375 5554 6411 5875 -337 -179 561 O -HETATM 1576 O HOH A 376 21.851 17.219 13.696 1.00 69.26 O -ANISOU 1576 O HOH A 376 9125 8830 8361 -489 -654 -596 O -HETATM 1577 O HOH A 377 17.246 19.519 19.131 1.00 47.68 O -ANISOU 1577 O HOH A 377 6850 6063 5202 -260 -477 -1275 O -HETATM 1578 O HOH A 378 2.083 2.043 -7.954 1.00 43.89 O -ANISOU 1578 O HOH A 378 5459 5608 5609 -383 -277 -234 O -HETATM 1579 O HOH A 379 4.472 9.573 -11.571 1.00 34.55 O -ANISOU 1579 O HOH A 379 4207 4488 4432 -253 -401 -80 O -HETATM 1580 O HOH A 380 7.178 13.700 -18.122 1.00 46.25 O -ANISOU 1580 O HOH A 380 5745 6146 5682 -395 -613 276 O -HETATM 1581 O HOH A 381 6.682 7.972 9.859 1.00 56.45 O -ANISOU 1581 O HOH A 381 6985 7508 6956 110 274 -516 O -HETATM 1582 O HOH A 382 5.879 1.990 5.314 1.00 40.45 O -ANISOU 1582 O HOH A 382 4900 5366 5102 -87 198 -247 O -HETATM 1583 O HOH A 383 28.059 -6.985 -2.959 1.00 47.01 O -ANISOU 1583 O HOH A 383 5793 6041 6029 805 650 175 O -HETATM 1584 O HOH A 384 27.989 -3.865 9.323 1.00 54.38 O -ANISOU 1584 O HOH A 384 6428 7329 6906 224 67 655 O -HETATM 1585 O HOH A 385 27.507 -8.332 7.171 1.00 62.37 O -ANISOU 1585 O HOH A 385 7549 8034 8114 500 263 644 O -HETATM 1586 O HOH A 386 25.205 -8.744 8.494 1.00 63.99 O -ANISOU 1586 O HOH A 386 7856 8188 8269 376 215 595 O -HETATM 1587 O HOH A 387 17.271 -10.697 -0.530 1.00 41.16 O -ANISOU 1587 O HOH A 387 5573 4715 5353 266 306 -148 O -HETATM 1588 O HOH A 388 10.995 -2.167 12.699 1.00 45.51 O -ANISOU 1588 O HOH A 388 5621 6220 5452 -139 262 39 O -HETATM 1589 O HOH A 389 34.681 20.006 -8.985 1.00 52.44 O -ANISOU 1589 O HOH A 389 5555 7495 6873 -887 -490 1522 O -HETATM 1590 O HOH A 390 8.783 9.385 10.550 1.00 45.66 O -ANISOU 1590 O HOH A 390 5723 6094 5531 98 202 -585 O -CONECT 76 1500 -CONECT 119 1481 -CONECT 282 1481 -CONECT 470 1500 -CONECT 475 1500 -CONECT 778 1500 -CONECT 1434 1436 -CONECT 1435 1445 -CONECT 1436 1434 1438 1441 -CONECT 1437 1443 -CONECT 1438 1436 1439 1446 -CONECT 1439 1438 1440 1445 -CONECT 1440 1439 1441 1442 -CONECT 1441 1436 1440 -CONECT 1442 1440 1443 -CONECT 1443 1437 1442 1444 -CONECT 1444 1443 1445 -CONECT 1445 1435 1439 1444 -CONECT 1446 1438 1447 -CONECT 1447 1446 1448 -CONECT 1448 1447 -CONECT 1449 1450 1451 1452 1453 -CONECT 1450 1449 1481 -CONECT 1451 1449 -CONECT 1452 1449 -CONECT 1453 1449 1454 -CONECT 1454 1453 1455 1456 1457 -CONECT 1455 1454 -CONECT 1456 1454 1481 -CONECT 1457 1454 1458 -CONECT 1458 1457 1459 1460 1461 -CONECT 1459 1458 -CONECT 1460 1458 -CONECT 1461 1458 1462 -CONECT 1462 1461 1463 -CONECT 1463 1462 1464 1465 -CONECT 1464 1463 1469 -CONECT 1465 1463 1466 1467 -CONECT 1466 1465 -CONECT 1467 1465 1468 1469 -CONECT 1468 1467 -CONECT 1469 1464 1467 1470 -CONECT 1470 1469 1471 1480 -CONECT 1471 1470 1472 -CONECT 1472 1471 1473 -CONECT 1473 1472 1474 1480 -CONECT 1474 1473 1475 1476 -CONECT 1475 1474 -CONECT 1476 1474 1477 -CONECT 1477 1476 1478 1479 -CONECT 1478 1477 -CONECT 1479 1477 1480 -CONECT 1480 1470 1473 1479 -CONECT 1481 119 282 1450 1456 -CONECT 1481 1501 1502 -CONECT 1482 1483 1484 -CONECT 1483 1482 -CONECT 1484 1482 1485 1486 -CONECT 1485 1484 -CONECT 1486 1484 1487 -CONECT 1487 1486 -CONECT 1488 1489 1490 -CONECT 1489 1488 -CONECT 1490 1488 1491 -CONECT 1491 1490 -CONECT 1492 1493 1494 1495 -CONECT 1493 1492 -CONECT 1494 1492 -CONECT 1495 1492 -CONECT 1496 1497 1498 1499 -CONECT 1497 1496 -CONECT 1498 1496 -CONECT 1499 1496 -CONECT 1500 76 470 475 778 -CONECT 1500 1505 1508 -CONECT 1501 1481 -CONECT 1502 1481 -CONECT 1505 1500 -CONECT 1508 1500 -MASTER 351 0 8 5 6 0 19 6 1574 1 79 15 -END |