Browse entries in the PDBbind-CN Database
HEADER TRANSPORT PROTEIN 07-MAR-09 3GJ7 TITLE CRYSTAL STRUCTURE OF HUMAN RANGDP-NUP153ZNF12 COMPLEX COMPND MOL_ID: 1; COMPND 2 MOLECULE: GTP-BINDING NUCLEAR PROTEIN RAN; COMPND 3 CHAIN: A, C; COMPND 4 SYNONYM: GTPASE RAN, RAS-RELATED NUCLEAR PROTEIN, RAS-LIKE COMPND 5 PROTEIN TC4, ANDROGEN RECEPTOR-ASSOCIATED PROTEIN 24; COMPND 6 ENGINEERED: YES; COMPND 7 MUTATION: YES; COMPND 8 MOL_ID: 2; COMPND 9 MOLECULE: NUCLEAR PORE COMPLEX PROTEIN NUP153; COMPND 10 CHAIN: B, D; COMPND 11 FRAGMENT: NUP153 - ZINC FINGER MODULE 12: UNP RESIDUES 658- COMPND 12 750; COMPND 13 SYNONYM: NUCLEOPORIN NUP153, 153 KDA NUCLEOPORIN; COMPND 14 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606; SOURCE 5 GENE: RAN, ARA24, OK/SW-CL.81; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 8 EXPRESSION_SYSTEM_VARIANT: BL21(DE3)-RIL; SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET28A; SOURCE 11 MOL_ID: 2; SOURCE 12 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS; SOURCE 13 ORGANISM_COMMON: RAT; SOURCE 14 ORGANISM_TAXID: 10116; SOURCE 15 GENE: NUP153; SOURCE 16 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 17 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 18 EXPRESSION_SYSTEM_VARIANT: BL21(DE3)-RIL; SOURCE 19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 20 EXPRESSION_SYSTEM_PLASMID: PGEX-6P1 KEYWDS G PROTEIN, GDP, RAN, NUP153, NUCLEAR PORE, ZINC FINGER, KEYWDS 2 ACETYLATION, CYTOPLASM, GTP-BINDING, HOST-VIRUS KEYWDS 3 INTERACTION, ISOPEPTIDE BOND, NUCLEOTIDE-BINDING, NUCLEUS, KEYWDS 4 PHOSPHOPROTEIN, POLYMORPHISM, PROTEIN TRANSPORT, TRANSPORT, KEYWDS 5 UBL CONJUGATION, DNA-BINDING, METAL-BINDING, MRNA KEYWDS 6 TRANSPORT, NUCLEAR PORE COMPLEX, TRANSLOCATION, ZINC, ZINC- KEYWDS 7 FINGER, TRANSPORT PROTEIN EXPDTA X-RAY DIFFRACTION AUTHOR J.R.PARTRIDGE,T.U.SCHWARTZ REVDAT 1 04-AUG-09 3GJ7 0 JRNL AUTH J.R.PARTRIDGE,T.U.SCHWARTZ JRNL TITL CRYSTALLOGRAPHIC AND BIOCHEMICAL ANALYSIS OF THE JRNL TITL 2 RAN-BINDING ZINC FINGER DOMAIN. JRNL REF J.MOL.BIOL. V. 391 375 2009 JRNL REFN ISSN 0022-2836 JRNL PMID 19505478 JRNL DOI 10.1016/J.JMB.2009.06.011 REMARK 1 REMARK 2 REMARK 2 RESOLUTION. 1.93 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE) 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 : MAXIMUM LIKELIHOOD REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.93 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.75 REMARK 3 MIN(FOBS/SIGMA_FOBS) : NULL REMARK 3 COMPLETENESS FOR RANGE (%) : 91.9 REMARK 3 NUMBER OF REFLECTIONS : 36366 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.188 REMARK 3 R VALUE (WORKING SET) : 0.186 REMARK 3 FREE R VALUE : 0.229 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.080 REMARK 3 FREE R VALUE TEST SET COUNT : 1991 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 29.7560 - 4.6464 0.91 2696 165 0.1527 0.1841 REMARK 3 2 4.6464 - 3.6902 0.91 2647 137 0.1511 0.2107 REMARK 3 3 3.6902 - 3.2243 0.92 2666 145 0.1819 0.2204 REMARK 3 4 3.2243 - 2.9298 0.93 2682 153 0.2054 0.2321 REMARK 3 5 2.9298 - 2.7200 0.95 2794 132 0.2178 0.2937 REMARK 3 6 2.7200 - 2.5597 0.95 2728 152 0.2064 0.2504 REMARK 3 7 2.5597 - 2.4316 0.96 2763 141 0.1860 0.2375 REMARK 3 8 2.4316 - 2.3258 0.96 2764 147 0.2022 0.2530 REMARK 3 9 2.3258 - 2.2363 0.93 2671 140 0.2002 0.2489 REMARK 3 10 2.2363 - 2.1591 0.93 2654 172 0.2250 0.2875 REMARK 3 11 2.1591 - 2.0916 0.94 2682 129 0.2216 0.3087 REMARK 3 12 2.0916 - 2.0319 0.94 2721 153 0.2399 0.2983 REMARK 3 13 2.0319 - 1.9784 0.93 2658 135 0.2663 0.3428 REMARK 3 14 1.9784 - 1.9300 0.72 2107 90 0.3049 0.3590 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 : 0.31 REMARK 3 B_SOL : 49.84 REMARK 3 REMARK 3 ERROR ESTIMATES. REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.410 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.810 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 37.56 REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : NULL REMARK 3 B22 (A**2) : NULL REMARK 3 B33 (A**2) : NULL REMARK 3 B12 (A**2) : NULL REMARK 3 B13 (A**2) : NULL REMARK 3 B23 (A**2) : NULL REMARK 3 REMARK 3 TWINNING INFORMATION. REMARK 3 FRACTION: NULL REMARK 3 OPERATOR: NULL REMARK 3 REMARK 3 DEVIATIONS FROM IDEAL VALUES. REMARK 3 RMSD COUNT REMARK 3 BOND : 0.007 3773 REMARK 3 ANGLE : 1.055 5131 REMARK 3 CHIRALITY : 0.070 569 REMARK 3 PLANARITY : 0.004 645 REMARK 3 DIHEDRAL : 15.514 1379 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 1 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: CHAIN D REMARK 3 ORIGIN FOR THE GROUP (A): -14.9267 5.0110 5.5920 REMARK 3 T TENSOR REMARK 3 T11: 0.5623 T22: 0.2161 REMARK 3 T33: 0.0993 T12: 0.0479 REMARK 3 T13: 0.0905 T23: 0.0400 REMARK 3 L TENSOR REMARK 3 L11: 0.5800 L22: 1.2667 REMARK 3 L33: 1.7980 L12: -0.3026 REMARK 3 L13: -0.5482 L23: 0.9293 REMARK 3 S TENSOR REMARK 3 S11: -0.1955 S12: -0.1798 S13: -0.0380 REMARK 3 S21: 0.6117 S22: 0.0214 S23: 0.0902 REMARK 3 S31: 0.5078 S32: 0.4065 S33: 0.1677 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 3GJ7 COMPLIES WITH FORMAT V. 3.20, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-MAR-09. REMARK 100 THE RCSB ID CODE IS RCSB051927. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 04-AUG-08 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 6.5 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : APS REMARK 200 BEAMLINE : 24-ID-C REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.979 REMARK 200 MONOCHROMATOR : NULL 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 : HKL-2000 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 39224 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.930 REMARK 200 RESOLUTION RANGE LOW (A) : 50.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 93.3 REMARK 200 DATA REDUNDANCY : 2.300 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : 0.06000 REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.9000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.93 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.00 REMARK 200 COMPLETENESS FOR SHELL (%) : 88.6 REMARK 200 DATA REDUNDANCY IN SHELL : 1.70 REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : 0.40000 REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.160 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: PDB ENTRY 3GJ3 REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 39.88 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.05 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M BIS-TRIS PH 6.5, 18-20% PEG REMARK 280 3350, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 295K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,Y+1/2,-Z REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 30.56450 REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1, 2 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: DIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 350 REMARK 350 BIOMOLECULE: 2 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D 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 -4 REMARK 465 PRO A -3 REMARK 465 HIS A -2 REMARK 465 MET A -1 REMARK 465 ALA A 0 REMARK 465 SER A 1 REMARK 465 ALA A 2 REMARK 465 ALA A 3 REMARK 465 GLN A 4 REMARK 465 GLY A 5 REMARK 465 GLU A 6 REMARK 465 ALA A 208 REMARK 465 LEU A 209 REMARK 465 PRO A 210 REMARK 465 ASP A 211 REMARK 465 GLU A 212 REMARK 465 ASP A 213 REMARK 465 ASP A 214 REMARK 465 ASP A 215 REMARK 465 LEU A 216 REMARK 465 GLY B 653 REMARK 465 PRO B 654 REMARK 465 LEU B 655 REMARK 465 GLY B 656 REMARK 465 SER B 657 REMARK 465 ALA B 658 REMARK 465 GLY B 659 REMARK 465 SER B 660 REMARK 465 SER B 661 REMARK 465 TRP B 662 REMARK 465 GLN B 663 REMARK 465 CYS B 664 REMARK 465 ASP B 665 REMARK 465 THR B 666 REMARK 465 CYS B 667 REMARK 465 LEU B 668 REMARK 465 LEU B 669 REMARK 465 GLN B 670 REMARK 465 ASN B 671 REMARK 465 LYS B 672 REMARK 465 VAL B 673 REMARK 465 THR B 674 REMARK 465 ASP B 675 REMARK 465 ASN B 676 REMARK 465 LYS B 677 REMARK 465 CYS B 678 REMARK 465 ILE B 679 REMARK 465 ALA B 680 REMARK 465 CYS B 681 REMARK 465 GLN B 682 REMARK 465 ALA B 683 REMARK 465 ALA B 684 REMARK 465 LYS B 685 REMARK 465 LEU B 686 REMARK 465 PRO B 687 REMARK 465 LEU B 688 REMARK 465 LYS B 689 REMARK 465 GLU B 690 REMARK 465 THR B 691 REMARK 465 ALA B 692 REMARK 465 LYS B 693 REMARK 465 GLN B 694 REMARK 465 THR B 695 REMARK 465 GLY B 696 REMARK 465 ILE B 697 REMARK 465 GLY B 698 REMARK 465 THR B 699 REMARK 465 PRO B 700 REMARK 465 SER B 701 REMARK 465 LYS B 702 REMARK 465 SER B 703 REMARK 465 ASP B 704 REMARK 465 LYS B 705 REMARK 465 PRO B 706 REMARK 465 ALA B 707 REMARK 465 SER B 708 REMARK 465 THR B 709 REMARK 465 SER B 710 REMARK 465 GLY B 711 REMARK 465 THR B 712 REMARK 465 GLY B 713 REMARK 465 PHE B 714 REMARK 465 GLY B 715 REMARK 465 ASP B 716 REMARK 465 LYS B 717 REMARK 465 PHE B 718 REMARK 465 LYS B 719 REMARK 465 PRO B 720 REMARK 465 ALA B 721 REMARK 465 ILE B 722 REMARK 465 GLY B 750 REMARK 465 GLY C -4 REMARK 465 PRO C -3 REMARK 465 HIS C -2 REMARK 465 MET C -1 REMARK 465 ALA C 0 REMARK 465 SER C 1 REMARK 465 ALA C 2 REMARK 465 ALA C 3 REMARK 465 GLN C 4 REMARK 465 GLY C 5 REMARK 465 GLU C 6 REMARK 465 LEU C 209 REMARK 465 PRO C 210 REMARK 465 ASP C 211 REMARK 465 GLU C 212 REMARK 465 ASP C 213 REMARK 465 ASP C 214 REMARK 465 ASP C 215 REMARK 465 LEU C 216 REMARK 465 GLY D 653 REMARK 465 PRO D 654 REMARK 465 LEU D 655 REMARK 465 GLY D 656 REMARK 465 SER D 657 REMARK 465 ALA D 658 REMARK 465 GLY D 659 REMARK 465 SER D 660 REMARK 465 SER D 661 REMARK 465 TRP D 662 REMARK 465 GLN D 663 REMARK 465 CYS D 664 REMARK 465 ASP D 665 REMARK 465 THR D 666 REMARK 465 CYS D 667 REMARK 465 LEU D 668 REMARK 465 LEU D 669 REMARK 465 GLN D 670 REMARK 465 ASN D 671 REMARK 465 LYS D 672 REMARK 465 VAL D 673 REMARK 465 THR D 674 REMARK 465 ASP D 675 REMARK 465 ASN D 676 REMARK 465 LYS D 677 REMARK 465 CYS D 678 REMARK 465 ILE D 679 REMARK 465 ALA D 680 REMARK 465 CYS D 681 REMARK 465 GLN D 682 REMARK 465 ALA D 683 REMARK 465 ALA D 684 REMARK 465 LYS D 685 REMARK 465 LEU D 686 REMARK 465 PRO D 687 REMARK 465 LEU D 688 REMARK 465 LYS D 689 REMARK 465 GLU D 690 REMARK 465 THR D 691 REMARK 465 ALA D 692 REMARK 465 LYS D 693 REMARK 465 GLN D 694 REMARK 465 THR D 695 REMARK 465 GLY D 696 REMARK 465 ILE D 697 REMARK 465 GLY D 698 REMARK 465 THR D 699 REMARK 465 PRO D 700 REMARK 465 SER D 701 REMARK 465 LYS D 702 REMARK 465 SER D 703 REMARK 465 ASP D 704 REMARK 465 LYS D 705 REMARK 465 PRO D 706 REMARK 465 ALA D 707 REMARK 465 SER D 708 REMARK 465 THR D 709 REMARK 465 SER D 710 REMARK 465 GLY D 711 REMARK 465 THR D 712 REMARK 465 GLY D 713 REMARK 465 PHE D 714 REMARK 465 GLY D 715 REMARK 465 ASP D 716 REMARK 465 LYS D 717 REMARK 465 PHE D 718 REMARK 465 LYS D 719 REMARK 465 PRO D 720 REMARK 465 ALA D 721 REMARK 465 ILE D 722 REMARK 465 GLY D 750 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 GLU A 113 -129.97 80.38 REMARK 500 LYS A 142 50.76 -141.25 REMARK 500 THR A 206 60.56 -105.19 REMARK 500 GLU C 113 -121.50 63.48 REMARK 500 GLU D 745 -3.28 82.16 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 301 MG REMARK 620 N RES CSSEQI ATOM REMARK 620 1 THR A 24 OG1 REMARK 620 2 GDP A 302 O1B 86.6 REMARK 620 3 HOH A 242 O 86.3 87.9 REMARK 620 4 HOH A 240 O 94.5 178.9 92.0 REMARK 620 5 HOH A 241 O 171.3 86.0 88.9 92.9 REMARK 620 6 HOH A 239 O 90.3 83.8 171.2 96.4 93.5 REMARK 620 N 1 2 3 4 5 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 ZN B 300 ZN REMARK 620 N RES CSSEQI ATOM REMARK 620 1 CYS B 727 SG REMARK 620 2 CYS B 730 SG 114.8 REMARK 620 3 CYS B 741 SG 110.2 99.8 REMARK 620 4 CYS B 744 SG 103.6 115.4 113.4 REMARK 620 N 1 2 3 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 MG C 301 MG REMARK 620 N RES CSSEQI ATOM REMARK 620 1 THR C 24 OG1 REMARK 620 2 GDP C 302 O1B 90.8 REMARK 620 3 HOH C 236 O 92.1 91.5 REMARK 620 4 HOH C 238 O 175.1 92.9 84.7 REMARK 620 5 HOH C 237 O 85.6 176.3 89.8 90.7 REMARK 620 6 HOH C 235 O 86.5 88.2 178.5 96.9 90.5 REMARK 620 N 1 2 3 4 5 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 ZN D 300 ZN REMARK 620 N RES CSSEQI ATOM REMARK 620 1 CYS D 727 SG REMARK 620 2 CYS D 730 SG 117.3 REMARK 620 3 CYS D 741 SG 108.9 103.7 REMARK 620 4 CYS D 744 SG 96.4 117.0 113.8 REMARK 620 N 1 2 3 REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 301 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GDP A 302 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 304 REMARK 800 SITE_IDENTIFIER: AC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 306 REMARK 800 SITE_IDENTIFIER: AC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 300 REMARK 800 SITE_IDENTIFIER: AC6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG C 301 REMARK 800 SITE_IDENTIFIER: AC7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GDP C 302 REMARK 800 SITE_IDENTIFIER: AC8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG C 303 REMARK 800 SITE_IDENTIFIER: AC9 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG C 305 REMARK 800 SITE_IDENTIFIER: BC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN D 300 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 3CH5 RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF THE RANGDP-NUP153ZNF2 COMPLEX REMARK 900 RELATED ID: 2GQE RELATED DB: PDB REMARK 900 MOLECULAR CHARACTERIZATION OF THE RAN BINDING ZINC FINGER REMARK 900 DOMAIN REMARK 900 RELATED ID: 1BYU RELATED DB: PDB REMARK 900 CANINE GDP-RAN REMARK 900 RELATED ID: 3GJ0 RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF HUMAN NUCLEOPORIN REMARK 900 RELATED ID: 3GJ3 RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF HUMAN NUCLEOPORIN IN COMPLEX WITH REMARK 900 NUP153 - ZINC FINGER MODULE 2 REMARK 900 RELATED ID: 3GJ4 RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF HUMAN NUCLEOPORIN IN COMPLEX WITH REMARK 900 NUP153 - ZINC FINGER MODULE 3 REMARK 900 RELATED ID: 3GJ5 RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF HUMAN NUCLEOPORIN F35S MUTANT IN REMARK 900 COMPLEX WITH NUP153 - ZINC FINGER MODULE 4 REMARK 900 RELATED ID: 3GJ6 RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF HUMAN NUCLEOPORIN F35S MUTANT IN REMARK 900 COMPLEX WITH NUP153 - ZINC FINGER MODULE 1 REMARK 900 RELATED ID: 3GJ8 RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF HUMAN NUCLEOPORIN F35S MUTANT IN REMARK 900 COMPLEX WITH NUP153 - ZINC FINGER MODULE 34 DBREF 3GJ7 A 2 216 UNP P62826 RAN_HUMAN 2 216 DBREF 3GJ7 B 658 750 UNP P49791 NU153_RAT 658 750 DBREF 3GJ7 C 2 216 UNP P62826 RAN_HUMAN 2 216 DBREF 3GJ7 D 658 750 UNP P49791 NU153_RAT 658 750 SEQADV 3GJ7 GLY A -4 UNP P62826 EXPRESSION TAG SEQADV 3GJ7 PRO A -3 UNP P62826 EXPRESSION TAG SEQADV 3GJ7 HIS A -2 UNP P62826 EXPRESSION TAG SEQADV 3GJ7 MET A -1 UNP P62826 EXPRESSION TAG SEQADV 3GJ7 ALA A 0 UNP P62826 EXPRESSION TAG SEQADV 3GJ7 SER A 1 UNP P62826 EXPRESSION TAG SEQADV 3GJ7 SER A 35 UNP P62826 PHE 35 ENGINEERED SEQADV 3GJ7 GLY B 653 UNP P49791 EXPRESSION TAG SEQADV 3GJ7 PRO B 654 UNP P49791 EXPRESSION TAG SEQADV 3GJ7 LEU B 655 UNP P49791 EXPRESSION TAG SEQADV 3GJ7 GLY B 656 UNP P49791 EXPRESSION TAG SEQADV 3GJ7 SER B 657 UNP P49791 EXPRESSION TAG SEQADV 3GJ7 GLY C -4 UNP P62826 EXPRESSION TAG SEQADV 3GJ7 PRO C -3 UNP P62826 EXPRESSION TAG SEQADV 3GJ7 HIS C -2 UNP P62826 EXPRESSION TAG SEQADV 3GJ7 MET C -1 UNP P62826 EXPRESSION TAG SEQADV 3GJ7 ALA C 0 UNP P62826 EXPRESSION TAG SEQADV 3GJ7 SER C 1 UNP P62826 EXPRESSION TAG SEQADV 3GJ7 SER C 35 UNP P62826 PHE 35 ENGINEERED SEQADV 3GJ7 GLY D 653 UNP P49791 EXPRESSION TAG SEQADV 3GJ7 PRO D 654 UNP P49791 EXPRESSION TAG SEQADV 3GJ7 LEU D 655 UNP P49791 EXPRESSION TAG SEQADV 3GJ7 GLY D 656 UNP P49791 EXPRESSION TAG SEQADV 3GJ7 SER D 657 UNP P49791 EXPRESSION TAG SEQRES 1 A 221 GLY PRO HIS MET ALA SER ALA ALA GLN GLY GLU PRO GLN SEQRES 2 A 221 VAL GLN PHE LYS LEU VAL LEU VAL GLY ASP GLY GLY THR SEQRES 3 A 221 GLY LYS THR THR PHE VAL LYS ARG HIS LEU THR GLY GLU SEQRES 4 A 221 SER GLU LYS LYS TYR VAL ALA THR LEU GLY VAL GLU VAL SEQRES 5 A 221 HIS PRO LEU VAL PHE HIS THR ASN ARG GLY PRO ILE LYS SEQRES 6 A 221 PHE ASN VAL TRP ASP THR ALA GLY GLN GLU LYS PHE GLY SEQRES 7 A 221 GLY LEU ARG ASP GLY TYR TYR ILE GLN ALA GLN CYS ALA SEQRES 8 A 221 ILE ILE MET PHE ASP VAL THR SER ARG VAL THR TYR LYS SEQRES 9 A 221 ASN VAL PRO ASN TRP HIS ARG ASP LEU VAL ARG VAL CYS SEQRES 10 A 221 GLU ASN ILE PRO ILE VAL LEU CYS GLY ASN LYS VAL ASP SEQRES 11 A 221 ILE LYS ASP ARG LYS VAL LYS ALA LYS SER ILE VAL PHE SEQRES 12 A 221 HIS ARG LYS LYS ASN LEU GLN TYR TYR ASP ILE SER ALA SEQRES 13 A 221 LYS SER ASN TYR ASN PHE GLU LYS PRO PHE LEU TRP LEU SEQRES 14 A 221 ALA ARG LYS LEU ILE GLY ASP PRO ASN LEU GLU PHE VAL SEQRES 15 A 221 ALA MET PRO ALA LEU ALA PRO PRO GLU VAL VAL MET ASP SEQRES 16 A 221 PRO ALA LEU ALA ALA GLN TYR GLU HIS ASP LEU GLU VAL SEQRES 17 A 221 ALA GLN THR THR ALA LEU PRO ASP GLU ASP ASP ASP LEU SEQRES 1 B 98 GLY PRO LEU GLY SER ALA GLY SER SER TRP GLN CYS ASP SEQRES 2 B 98 THR CYS LEU LEU GLN ASN LYS VAL THR ASP ASN LYS CYS SEQRES 3 B 98 ILE ALA CYS GLN ALA ALA LYS LEU PRO LEU LYS GLU THR SEQRES 4 B 98 ALA LYS GLN THR GLY ILE GLY THR PRO SER LYS SER ASP SEQRES 5 B 98 LYS PRO ALA SER THR SER GLY THR GLY PHE GLY ASP LYS SEQRES 6 B 98 PHE LYS PRO ALA ILE GLY THR TRP ASP CYS ASP THR CYS SEQRES 7 B 98 LEU VAL GLN ASN LYS PRO GLU ALA VAL LYS CYS VAL ALA SEQRES 8 B 98 CYS GLU THR PRO LYS PRO GLY SEQRES 1 C 221 GLY PRO HIS MET ALA SER ALA ALA GLN GLY GLU PRO GLN SEQRES 2 C 221 VAL GLN PHE LYS LEU VAL LEU VAL GLY ASP GLY GLY THR SEQRES 3 C 221 GLY LYS THR THR PHE VAL LYS ARG HIS LEU THR GLY GLU SEQRES 4 C 221 SER GLU LYS LYS TYR VAL ALA THR LEU GLY VAL GLU VAL SEQRES 5 C 221 HIS PRO LEU VAL PHE HIS THR ASN ARG GLY PRO ILE LYS SEQRES 6 C 221 PHE ASN VAL TRP ASP THR ALA GLY GLN GLU LYS PHE GLY SEQRES 7 C 221 GLY LEU ARG ASP GLY TYR TYR ILE GLN ALA GLN CYS ALA SEQRES 8 C 221 ILE ILE MET PHE ASP VAL THR SER ARG VAL THR TYR LYS SEQRES 9 C 221 ASN VAL PRO ASN TRP HIS ARG ASP LEU VAL ARG VAL CYS SEQRES 10 C 221 GLU ASN ILE PRO ILE VAL LEU CYS GLY ASN LYS VAL ASP SEQRES 11 C 221 ILE LYS ASP ARG LYS VAL LYS ALA LYS SER ILE VAL PHE SEQRES 12 C 221 HIS ARG LYS LYS ASN LEU GLN TYR TYR ASP ILE SER ALA SEQRES 13 C 221 LYS SER ASN TYR ASN PHE GLU LYS PRO PHE LEU TRP LEU SEQRES 14 C 221 ALA ARG LYS LEU ILE GLY ASP PRO ASN LEU GLU PHE VAL SEQRES 15 C 221 ALA MET PRO ALA LEU ALA PRO PRO GLU VAL VAL MET ASP SEQRES 16 C 221 PRO ALA LEU ALA ALA GLN TYR GLU HIS ASP LEU GLU VAL SEQRES 17 C 221 ALA GLN THR THR ALA LEU PRO ASP GLU ASP ASP ASP LEU SEQRES 1 D 98 GLY PRO LEU GLY SER ALA GLY SER SER TRP GLN CYS ASP SEQRES 2 D 98 THR CYS LEU LEU GLN ASN LYS VAL THR ASP ASN LYS CYS SEQRES 3 D 98 ILE ALA CYS GLN ALA ALA LYS LEU PRO LEU LYS GLU THR SEQRES 4 D 98 ALA LYS GLN THR GLY ILE GLY THR PRO SER LYS SER ASP SEQRES 5 D 98 LYS PRO ALA SER THR SER GLY THR GLY PHE GLY ASP LYS SEQRES 6 D 98 PHE LYS PRO ALA ILE GLY THR TRP ASP CYS ASP THR CYS SEQRES 7 D 98 LEU VAL GLN ASN LYS PRO GLU ALA VAL LYS CYS VAL ALA SEQRES 8 D 98 CYS GLU THR PRO LYS PRO GLY HET MG A 301 1 HET GDP A 302 28 HET MG A 304 1 HET MG A 306 1 HET ZN B 300 1 HET MG C 301 1 HET GDP C 302 28 HET MG C 303 1 HET MG C 305 1 HET ZN D 300 1 HETNAM MG MAGNESIUM ION HETNAM GDP GUANOSINE-5'-DIPHOSPHATE HETNAM ZN ZINC ION FORMUL 5 MG 6(MG 2+) FORMUL 6 GDP 2(C10 H15 N5 O11 P2) FORMUL 9 ZN 2(ZN 2+) FORMUL 15 HOH *294(H2 O) HELIX 1 1 GLY A 22 LYS A 28 1 7 HELIX 2 2 HIS A 30 GLU A 36 1 7 HELIX 3 3 GLY A 68 PHE A 72 5 5 HELIX 4 4 ARG A 76 ILE A 81 1 6 HELIX 5 5 SER A 94 ASN A 100 1 7 HELIX 6 6 ASN A 100 GLU A 113 1 14 HELIX 7 7 LYS A 132 ILE A 136 5 5 HELIX 8 8 VAL A 137 LYS A 142 5 6 HELIX 9 9 SER A 150 ASN A 154 5 5 HELIX 10 10 PHE A 157 GLY A 170 1 14 HELIX 11 11 ASP A 190 THR A 206 1 17 HELIX 12 12 GLY C 22 LYS C 28 1 7 HELIX 13 13 HIS C 30 GLU C 36 1 7 HELIX 14 14 GLY C 68 PHE C 72 5 5 HELIX 15 15 ARG C 76 ILE C 81 1 6 HELIX 16 16 SER C 94 ASN C 100 1 7 HELIX 17 17 ASN C 100 GLU C 113 1 14 HELIX 18 18 LYS C 132 ILE C 136 5 5 HELIX 19 19 VAL C 137 LYS C 142 1 6 HELIX 20 20 SER C 150 ASN C 154 5 5 HELIX 21 21 GLU C 158 GLY C 170 1 13 HELIX 22 22 ASP C 190 GLN C 205 1 16 SHEET 1 A 7 LYS A 38 VAL A 40 0 SHEET 2 A 7 VAL A 45 THR A 54 -1 O VAL A 45 N VAL A 40 SHEET 3 A 7 GLY A 57 THR A 66 -1 O PHE A 61 N LEU A 50 SHEET 4 A 7 GLN A 10 GLY A 17 1 N LEU A 13 O TRP A 64 SHEET 5 A 7 CYS A 85 ASP A 91 1 O MET A 89 N VAL A 16 SHEET 6 A 7 ILE A 117 ASN A 122 1 O CYS A 120 N ILE A 88 SHEET 7 A 7 LEU A 144 ASP A 148 1 O GLN A 145 N LEU A 119 SHEET 1 B 2 TRP B 725 ASP B 726 0 SHEET 2 B 2 GLN B 733 ASN B 734 -1 O ASN B 734 N TRP B 725 SHEET 1 C 7 LYS C 38 VAL C 40 0 SHEET 2 C 7 VAL C 45 THR C 54 -1 O VAL C 45 N VAL C 40 SHEET 3 C 7 GLY C 57 THR C 66 -1 O PHE C 61 N LEU C 50 SHEET 4 C 7 GLN C 10 GLY C 17 1 N PHE C 11 O ASN C 62 SHEET 5 C 7 CYS C 85 ASP C 91 1 O MET C 89 N VAL C 16 SHEET 6 C 7 ILE C 117 ASN C 122 1 O ASN C 122 N PHE C 90 SHEET 7 C 7 GLN C 145 ASP C 148 1 O GLN C 145 N LEU C 119 SHEET 1 D 3 LYS C 38 VAL C 40 0 SHEET 2 D 3 VAL C 45 THR C 54 -1 O VAL C 45 N VAL C 40 SHEET 3 D 3 PHE C 176 ALA C 178 -1 O VAL C 177 N HIS C 53 SHEET 1 E 2 TRP D 725 ASP D 726 0 SHEET 2 E 2 GLN D 733 ASN D 734 -1 O ASN D 734 N TRP D 725 LINK OG1 THR A 24 MG MG A 301 1555 1555 2.25 LINK SG CYS B 727 ZN ZN B 300 1555 1555 2.52 LINK SG CYS B 730 ZN ZN B 300 1555 1555 2.40 LINK SG CYS B 741 ZN ZN B 300 1555 1555 2.50 LINK SG CYS B 744 ZN ZN B 300 1555 1555 2.41 LINK OG1 THR C 24 MG MG C 301 1555 1555 2.27 LINK SG CYS D 727 ZN ZN D 300 1555 1555 2.43 LINK SG CYS D 730 ZN ZN D 300 1555 1555 2.28 LINK SG CYS D 741 ZN ZN D 300 1555 1555 2.24 LINK SG CYS D 744 ZN ZN D 300 1555 1555 2.32 LINK MG MG A 301 O1B GDP A 302 1555 1555 2.19 LINK MG MG C 301 O1B GDP C 302 1555 1555 2.11 LINK MG MG A 301 O HOH A 242 1555 1555 2.32 LINK MG MG A 301 O HOH A 240 1555 1555 2.21 LINK MG MG A 301 O HOH A 241 1555 1555 2.29 LINK MG MG A 301 O HOH A 239 1555 1555 2.35 LINK MG MG C 301 O HOH C 236 1555 1555 2.28 LINK MG MG C 301 O HOH C 238 1555 1555 2.25 LINK MG MG C 301 O HOH C 237 1555 1555 2.35 LINK MG MG C 301 O HOH C 235 1555 1555 2.26 SITE 1 AC1 6 THR A 24 HOH A 239 HOH A 240 HOH A 241 SITE 2 AC1 6 HOH A 242 GDP A 302 SITE 1 AC2 20 GLY A 20 THR A 21 GLY A 22 LYS A 23 SITE 2 AC2 20 THR A 24 THR A 25 ASN A 122 LYS A 123 SITE 3 AC2 20 ASP A 125 ILE A 126 SER A 150 ALA A 151 SITE 4 AC2 20 LYS A 152 HOH A 219 HOH A 239 HOH A 241 SITE 5 AC2 20 HOH A 299 MG A 301 HOH A 310 HOH A 344 SITE 1 AC3 3 LEU A 31 HOH A 279 MG C 303 SITE 1 AC4 4 PRO A 180 ALA A 181 HOH A 221 MG C 305 SITE 1 AC5 4 CYS B 727 CYS B 730 CYS B 741 CYS B 744 SITE 1 AC6 6 THR C 24 HOH C 235 HOH C 236 HOH C 237 SITE 2 AC6 6 HOH C 238 GDP C 302 SITE 1 AC7 23 GLY C 20 THR C 21 GLY C 22 LYS C 23 SITE 2 AC7 23 THR C 24 THR C 25 ASN C 122 LYS C 123 SITE 3 AC7 23 ASP C 125 ILE C 126 SER C 150 ALA C 151 SITE 4 AC7 23 LYS C 152 HOH C 235 HOH C 238 HOH C 275 SITE 5 AC7 23 HOH C 300 MG C 301 HOH C 351 HOH C 362 SITE 6 AC7 23 HOH C 392 HOH C 394 HOH C 395 SITE 1 AC8 4 MG A 304 HIS C 53 PRO C 58 HOH C 358 SITE 1 AC9 3 MG A 306 ALA C 181 HOH C 244 SITE 1 BC1 4 CYS D 727 CYS D 730 CYS D 741 CYS D 744 CRYST1 58.523 61.129 80.215 90.00 93.71 90.00 P 1 21 1 4 ORIGX1 1.000000 0.000000 0.000000 0.00000 ORIGX2 0.000000 1.000000 0.000000 0.00000 ORIGX3 0.000000 0.000000 1.000000 0.00000 SCALE1 0.017087 0.000000 0.001108 0.00000 SCALE2 0.000000 0.016359 0.000000 0.00000 SCALE3 0.000000 0.000000 0.012493 0.00000 ATOM 1 N PRO A 7 -8.002 -12.626 21.009 1.00104.37 N ANISOU 1 N PRO A 7 14639 11785 13232 -990 2426 -1389 N ATOM 2 CA PRO A 7 -8.006 -11.392 21.801 1.00102.97 C ANISOU 2 CA PRO A 7 14422 11656 13047 -953 2337 -1327 C ATOM 3 C PRO A 7 -6.641 -11.108 22.424 1.00 99.60 C ANISOU 3 C PRO A 7 14145 11209 12490 -826 2260 -1101 C ATOM 4 O PRO A 7 -5.927 -12.043 22.794 1.00100.57 O ANISOU 4 O PRO A 7 14459 11226 12528 -794 2352 -1009 O ATOM 5 CB PRO A 7 -9.037 -11.687 22.892 1.00105.16 C ANISOU 5 CB PRO A 7 14759 11821 13376 -1090 2543 -1446 C ATOM 6 CG PRO A 7 -9.981 -12.649 22.253 1.00107.26 C ANISOU 6 CG PRO A 7 14963 12056 13734 -1218 2682 -1646 C ATOM 7 CD PRO A 7 -9.150 -13.494 21.325 1.00106.30 C ANISOU 7 CD PRO A 7 14906 11925 13557 -1155 2650 -1577 C ATOM 8 N GLN A 8 -6.293 -9.828 22.534 1.00 92.83 N ANISOU 8 N GLN A 8 13201 10453 11618 -753 2093 -1022 N ATOM 9 CA GLN A 8 -4.997 -9.411 23.065 1.00 83.85 C ANISOU 9 CA GLN A 8 12168 9325 10365 -637 1998 -827 C ATOM 10 C GLN A 8 -4.793 -9.880 24.499 1.00 67.12 C ANISOU 10 C GLN A 8 10259 7072 8171 -648 2139 -762 C ATOM 11 O GLN A 8 -5.680 -9.724 25.340 1.00 72.84 O ANISOU 11 O GLN A 8 11004 7735 8937 -736 2250 -844 O ATOM 12 CB GLN A 8 -4.861 -7.886 23.016 1.00 90.86 C ANISOU 12 CB GLN A 8 12925 10333 11266 -587 1819 -784 C ATOM 13 CG GLN A 8 -4.784 -7.286 21.620 1.00 98.44 C ANISOU 13 CG GLN A 8 13714 11426 12263 -541 1655 -803 C ATOM 14 CD GLN A 8 -4.583 -5.774 21.645 1.00101.76 C ANISOU 14 CD GLN A 8 14042 11941 12682 -489 1495 -748 C ATOM 15 OE1 GLN A 8 -4.197 -5.203 22.667 1.00 98.29 O ANISOU 15 OE1 GLN A 8 13671 11478 12196 -473 1487 -667 O ATOM 16 NE2 GLN A 8 -4.843 -5.123 20.515 1.00103.95 N ANISOU 16 NE2 GLN A 8 14174 12321 13002 -459 1369 -793 N ATOM 17 N VAL A 9 -3.621 -10.445 24.776 1.00 50.23 N ANISOU 17 N VAL A 9 8278 4892 5915 -549 2134 -619 N ATOM 18 CA VAL A 9 -3.262 -10.853 26.139 1.00 49.83 C ANISOU 18 CA VAL A 9 8447 4721 5763 -523 2244 -536 C ATOM 19 C VAL A 9 -2.868 -9.601 26.946 1.00 44.57 C ANISOU 19 C VAL A 9 7753 4124 5056 -473 2123 -455 C ATOM 20 O VAL A 9 -1.974 -8.854 26.541 1.00 39.70 O ANISOU 20 O VAL A 9 7050 3627 4408 -384 1946 -365 O ATOM 21 CB VAL A 9 -2.106 -11.886 26.112 1.00 44.89 C ANISOU 21 CB VAL A 9 7996 4040 5018 -409 2262 -415 C ATOM 22 CG1 VAL A 9 -1.467 -12.033 27.469 1.00 42.43 C ANISOU 22 CG1 VAL A 9 7896 3648 4576 -330 2307 -300 C ATOM 23 CG2 VAL A 9 -2.596 -13.231 25.576 1.00 50.41 C ANISOU 23 CG2 VAL A 9 8775 4628 5749 -473 2428 -501 C ATOM 24 N GLN A 10 -3.558 -9.351 28.059 1.00 43.52 N ANISOU 24 N GLN A 10 7690 3918 4929 -541 2226 -496 N ATOM 25 CA GLN A 10 -3.284 -8.153 28.864 1.00 37.74 C ANISOU 25 CA GLN A 10 6934 3244 4163 -506 2123 -435 C ATOM 26 C GLN A 10 -3.582 -8.365 30.350 1.00 49.76 C ANISOU 26 C GLN A 10 8646 4641 5619 -536 2269 -426 C ATOM 27 O GLN A 10 -4.454 -9.150 30.709 1.00 44.17 O ANISOU 27 O GLN A 10 8033 3808 4940 -632 2464 -516 O ATOM 28 CB GLN A 10 -4.074 -6.950 28.323 1.00 36.28 C ANISOU 28 CB GLN A 10 6522 3164 4098 -566 2025 -530 C ATOM 29 CG GLN A 10 -5.592 -7.099 28.432 1.00 51.77 C ANISOU 29 CG GLN A 10 8425 5068 6175 -703 2171 -705 C ATOM 30 CD GLN A 10 -6.355 -6.079 27.597 1.00 54.15 C ANISOU 30 CD GLN A 10 8489 5488 6597 -735 2058 -811 C ATOM 31 OE1 GLN A 10 -6.091 -4.879 27.657 1.00 48.76 O ANISOU 31 OE1 GLN A 10 7726 4889 5910 -686 1915 -762 O ATOM 32 NE2 GLN A 10 -7.317 -6.559 26.822 1.00 63.44 N ANISOU 32 NE2 GLN A 10 9558 6670 7877 -813 2124 -962 N ATOM 33 N PHE A 11 -2.857 -7.652 31.209 1.00 50.24 N ANISOU 33 N PHE A 11 8764 4737 5588 -460 2178 -323 N ATOM 34 CA PHE A 11 -3.027 -7.791 32.653 1.00 45.21 C ANISOU 34 CA PHE A 11 8321 3989 4866 -470 2300 -301 C ATOM 35 C PHE A 11 -3.084 -6.430 33.331 1.00 42.04 C ANISOU 35 C PHE A 11 7845 3659 4469 -475 2201 -293 C ATOM 36 O PHE A 11 -2.320 -5.535 32.995 1.00 40.09 O ANISOU 36 O PHE A 11 7484 3539 4210 -407 2015 -229 O ATOM 37 CB PHE A 11 -1.855 -8.561 33.253 1.00 45.06 C ANISOU 37 CB PHE A 11 8522 3919 4679 -334 2301 -164 C ATOM 38 CG PHE A 11 -1.577 -9.868 32.584 1.00 47.02 C ANISOU 38 CG PHE A 11 8860 4100 4904 -299 2378 -150 C ATOM 39 CD1 PHE A 11 -2.219 -11.028 33.009 1.00 40.62 C ANISOU 39 CD1 PHE A 11 8247 3112 4073 -361 2607 -197 C ATOM 40 CD2 PHE A 11 -0.665 -9.946 31.541 1.00 46.45 C ANISOU 40 CD2 PHE A 11 8686 4135 4828 -208 2233 -92 C ATOM 41 CE1 PHE A 11 -1.959 -12.241 32.402 1.00 45.09 C ANISOU 41 CE1 PHE A 11 8912 3605 4616 -329 2685 -185 C ATOM 42 CE2 PHE A 11 -0.398 -11.162 30.933 1.00 51.15 C ANISOU 42 CE2 PHE A 11 9371 4664 5399 -171 2306 -80 C ATOM 43 CZ PHE A 11 -1.045 -12.306 31.357 1.00 41.38 C ANISOU 43 CZ PHE A 11 8334 3247 4142 -230 2530 -126 C ATOM 44 N LYS A 12 -3.981 -6.283 34.297 1.00 41.70 N ANISOU 44 N LYS A 12 7874 3529 4440 -560 2336 -361 N ATOM 45 CA LYS A 12 -3.989 -5.092 35.130 1.00 41.31 C ANISOU 45 CA LYS A 12 7797 3526 4372 -558 2263 -346 C ATOM 46 C LYS A 12 -2.817 -5.186 36.094 1.00 38.94 C ANISOU 46 C LYS A 12 7681 3215 3897 -436 2211 -208 C ATOM 47 O LYS A 12 -2.672 -6.170 36.809 1.00 40.13 O ANISOU 47 O LYS A 12 8057 3249 3943 -404 2342 -168 O ATOM 48 CB LYS A 12 -5.290 -4.995 35.921 1.00 38.00 C ANISOU 48 CB LYS A 12 7413 3012 4012 -683 2439 -465 C ATOM 49 CG LYS A 12 -5.292 -3.837 36.937 1.00 40.53 C ANISOU 49 CG LYS A 12 7740 3361 4297 -676 2383 -447 C ATOM 50 CD LYS A 12 -6.675 -3.591 37.515 1.00 42.95 C ANISOU 50 CD LYS A 12 8029 3599 4693 -807 2544 -586 C ATOM 51 CE LYS A 12 -6.619 -2.507 38.592 1.00 44.81 C ANISOU 51 CE LYS A 12 8297 3851 4878 -794 2497 -562 C ATOM 52 NZ LYS A 12 -7.980 -2.087 39.011 1.00 47.49 N ANISOU 52 NZ LYS A 12 8572 4150 5323 -916 2629 -709 N ATOM 53 N LEU A 13 -1.978 -4.159 36.088 1.00 39.51 N ANISOU 53 N LEU A 13 7661 3414 3937 -365 2020 -141 N ATOM 54 CA LEU A 13 -0.840 -4.067 36.992 1.00 38.47 C ANISOU 54 CA LEU A 13 7664 3307 3646 -248 1941 -28 C ATOM 55 C LEU A 13 -0.998 -2.804 37.837 1.00 40.83 C ANISOU 55 C LEU A 13 7927 3646 3939 -278 1882 -43 C ATOM 56 O LEU A 13 -1.096 -1.704 37.308 1.00 36.47 O ANISOU 56 O LEU A 13 7188 3191 3478 -315 1767 -75 O ATOM 57 CB LEU A 13 0.454 -3.972 36.183 1.00 39.83 C ANISOU 57 CB LEU A 13 7742 3610 3782 -139 1758 56 C ATOM 58 CG LEU A 13 1.797 -3.990 36.910 1.00 39.14 C ANISOU 58 CG LEU A 13 7761 3580 3530 2 1652 163 C ATOM 59 CD1 LEU A 13 2.895 -4.356 35.925 1.00 42.59 C ANISOU 59 CD1 LEU A 13 8117 4118 3948 99 1531 224 C ATOM 60 CD2 LEU A 13 2.081 -2.651 37.580 1.00 36.36 C ANISOU 60 CD2 LEU A 13 7342 3316 3158 -6 1535 167 C ATOM 61 N VAL A 14 -1.025 -2.957 39.153 1.00 43.66 N ANISOU 61 N VAL A 14 8479 3924 4184 -258 1966 -20 N ATOM 62 CA VAL A 14 -1.119 -1.788 40.016 1.00 41.62 C ANISOU 62 CA VAL A 14 8201 3703 3908 -281 1911 -34 C ATOM 63 C VAL A 14 0.279 -1.389 40.463 1.00 41.47 C ANISOU 63 C VAL A 14 8215 3787 3753 -157 1741 64 C ATOM 64 O VAL A 14 1.099 -2.226 40.818 1.00 43.94 O ANISOU 64 O VAL A 14 8679 4087 3930 -42 1736 141 O ATOM 65 CB VAL A 14 -2.047 -2.029 41.231 1.00 47.98 C ANISOU 65 CB VAL A 14 9186 4368 4675 -346 2102 -83 C ATOM 66 CG1 VAL A 14 -3.503 -1.992 40.793 1.00 47.10 C ANISOU 66 CG1 VAL A 14 8970 4196 4730 -493 2242 -215 C ATOM 67 CG2 VAL A 14 -1.714 -3.360 41.899 1.00 49.03 C ANISOU 67 CG2 VAL A 14 9590 4382 4658 -270 2228 -19 C ATOM 68 N LEU A 15 0.555 -0.100 40.410 1.00 39.85 N ANISOU 68 N LEU A 15 7864 3692 3586 -176 1601 53 N ATOM 69 CA LEU A 15 1.868 0.405 40.763 1.00 39.78 C ANISOU 69 CA LEU A 15 7848 3800 3466 -79 1434 122 C ATOM 70 C LEU A 15 1.696 1.250 42.011 1.00 39.81 C ANISOU 70 C LEU A 15 7925 3793 3409 -102 1434 101 C ATOM 71 O LEU A 15 1.180 2.372 41.947 1.00 40.05 O ANISOU 71 O LEU A 15 7836 3848 3534 -191 1405 44 O ATOM 72 CB LEU A 15 2.428 1.240 39.603 1.00 44.87 C ANISOU 72 CB LEU A 15 8264 4581 4204 -94 1274 123 C ATOM 73 CG LEU A 15 3.723 2.041 39.766 1.00 44.31 C ANISOU 73 CG LEU A 15 8123 4654 4060 -34 1095 165 C ATOM 74 CD1 LEU A 15 4.886 1.153 40.199 1.00 38.73 C ANISOU 74 CD1 LEU A 15 7530 3991 3195 111 1046 237 C ATOM 75 CD2 LEU A 15 4.068 2.809 38.471 1.00 45.57 C ANISOU 75 CD2 LEU A 15 8066 4917 4330 -76 980 156 C ATOM 76 N VAL A 16 2.106 0.701 43.149 1.00 39.48 N ANISOU 76 N VAL A 16 8089 3708 3202 -16 1470 146 N ATOM 77 CA VAL A 16 1.927 1.378 44.427 1.00 40.07 C ANISOU 77 CA VAL A 16 8264 3761 3198 -30 1484 126 C ATOM 78 C VAL A 16 3.259 1.669 45.099 1.00 45.87 C ANISOU 78 C VAL A 16 9041 4612 3775 91 1325 181 C ATOM 79 O VAL A 16 4.303 1.155 44.691 1.00 44.75 O ANISOU 79 O VAL A 16 8881 4555 3569 201 1224 237 O ATOM 80 CB VAL A 16 1.066 0.551 45.398 1.00 44.83 C ANISOU 80 CB VAL A 16 9107 4196 3730 -44 1691 115 C ATOM 81 CG1 VAL A 16 -0.339 0.369 44.845 1.00 42.94 C ANISOU 81 CG1 VAL A 16 8807 3851 3655 -184 1858 32 C ATOM 82 CG2 VAL A 16 1.723 -0.789 45.664 1.00 45.50 C ANISOU 82 CG2 VAL A 16 9396 4232 3662 92 1729 196 C ATOM 83 N GLY A 17 3.200 2.487 46.148 1.00 46.04 N ANISOU 83 N GLY A 17 9117 4643 3734 71 1305 154 N ATOM 84 CA GLY A 17 4.382 2.916 46.862 1.00 44.62 C ANISOU 84 CA GLY A 17 8960 4585 3410 170 1149 180 C ATOM 85 C GLY A 17 4.195 4.328 47.375 1.00 45.57 C ANISOU 85 C GLY A 17 9000 4750 3565 80 1094 119 C ATOM 86 O GLY A 17 3.292 5.037 46.935 1.00 42.99 O ANISOU 86 O GLY A 17 8563 4381 3390 -48 1147 63 O ATOM 87 N ASP A 18 5.044 4.738 48.310 1.00 45.25 N ANISOU 87 N ASP A 18 9016 4797 3381 152 985 122 N ATOM 88 CA ASP A 18 4.962 6.086 48.866 1.00 47.10 C ANISOU 88 CA ASP A 18 9186 5074 3634 69 928 60 C ATOM 89 C ASP A 18 4.971 7.161 47.781 1.00 41.95 C ANISOU 89 C ASP A 18 8288 4493 3156 -44 850 19 C ATOM 90 O ASP A 18 5.531 6.962 46.700 1.00 40.63 O ANISOU 90 O ASP A 18 7985 4400 3052 -28 777 45 O ATOM 91 CB ASP A 18 6.112 6.343 49.846 1.00 52.16 C ANISOU 91 CB ASP A 18 9888 5837 4094 173 788 62 C ATOM 92 CG ASP A 18 5.866 5.717 51.217 1.00 57.32 C ANISOU 92 CG ASP A 18 10813 6401 4565 261 875 82 C ATOM 93 OD1 ASP A 18 4.875 4.972 51.365 1.00 50.94 O ANISOU 93 OD1 ASP A 18 10153 5433 3770 241 1055 101 O ATOM 94 OD2 ASP A 18 6.657 5.982 52.149 1.00 56.59 O ANISOU 94 OD2 ASP A 18 10788 6399 4315 346 767 72 O ATOM 95 N GLY A 19 4.351 8.300 48.077 1.00 43.49 N ANISOU 95 N GLY A 19 8441 4660 3423 -153 869 -43 N ATOM 96 CA GLY A 19 4.467 9.469 47.224 1.00 42.77 C ANISOU 96 CA GLY A 19 8150 4633 3467 -248 786 -81 C ATOM 97 C GLY A 19 5.920 9.893 47.099 1.00 48.02 C ANISOU 97 C GLY A 19 8715 5463 4067 -209 612 -77 C ATOM 98 O GLY A 19 6.680 9.852 48.075 1.00 41.97 O ANISOU 98 O GLY A 19 8030 4768 3151 -138 542 -81 O ATOM 99 N GLY A 20 6.318 10.275 45.892 1.00 44.44 N ANISOU 99 N GLY A 20 8088 5076 3722 -253 544 -74 N ATOM 100 CA GLY A 20 7.670 10.741 45.650 1.00 45.13 C ANISOU 100 CA GLY A 20 8056 5322 3770 -240 394 -84 C ATOM 101 C GLY A 20 8.705 9.674 45.326 1.00 43.35 C ANISOU 101 C GLY A 20 7812 5198 3462 -116 323 -35 C ATOM 102 O GLY A 20 9.883 9.992 45.167 1.00 45.84 O ANISOU 102 O GLY A 20 8017 5661 3738 -99 199 -56 O ATOM 103 N THR A 21 8.292 8.413 45.234 1.00 42.24 N ANISOU 103 N THR A 21 7776 4981 3294 -31 405 22 N ATOM 104 CA THR A 21 9.249 7.338 44.949 1.00 41.31 C ANISOU 104 CA THR A 21 7658 4947 3089 104 344 71 C ATOM 105 C THR A 21 9.594 7.214 43.462 1.00 40.57 C ANISOU 105 C THR A 21 7397 4906 3113 78 312 91 C ATOM 106 O THR A 21 10.594 6.584 43.122 1.00 39.74 O ANISOU 106 O THR A 21 7244 4906 2948 177 234 117 O ATOM 107 CB THR A 21 8.797 5.959 45.493 1.00 39.71 C ANISOU 107 CB THR A 21 7665 4636 2788 220 448 128 C ATOM 108 OG1 THR A 21 7.492 5.646 44.990 1.00 39.76 O ANISOU 108 OG1 THR A 21 7707 4486 2914 141 601 137 O ATOM 109 CG2 THR A 21 8.767 5.971 47.016 1.00 38.40 C ANISOU 109 CG2 THR A 21 7682 4446 2463 280 457 116 C ATOM 110 N GLY A 22 8.787 7.829 42.593 1.00 36.58 N ANISOU 110 N GLY A 22 6803 4331 2763 -45 368 76 N ATOM 111 CA GLY A 22 9.079 7.870 41.163 1.00 37.81 C ANISOU 111 CA GLY A 22 6804 4535 3028 -79 337 91 C ATOM 112 C GLY A 22 8.152 7.047 40.287 1.00 33.99 C ANISOU 112 C GLY A 22 6339 3942 2634 -80 442 125 C ATOM 113 O GLY A 22 8.484 6.727 39.146 1.00 34.51 O ANISOU 113 O GLY A 22 6305 4048 2758 -72 418 149 O ATOM 114 N LYS A 23 6.986 6.692 40.823 1.00 32.59 N ANISOU 114 N LYS A 23 6286 3628 2468 -95 563 119 N ATOM 115 CA LYS A 23 6.034 5.830 40.119 1.00 36.80 C ANISOU 115 CA LYS A 23 6845 4055 3081 -101 677 133 C ATOM 116 C LYS A 23 5.575 6.438 38.790 1.00 34.29 C ANISOU 116 C LYS A 23 6373 3737 2918 -187 668 111 C ATOM 117 O LYS A 23 5.471 5.753 37.776 1.00 32.40 O ANISOU 117 O LYS A 23 6086 3490 2733 -170 690 131 O ATOM 118 CB LYS A 23 4.829 5.533 41.027 1.00 34.73 C ANISOU 118 CB LYS A 23 6733 3652 2811 -127 818 107 C ATOM 119 CG LYS A 23 5.208 4.835 42.331 1.00 37.19 C ANISOU 119 CG LYS A 23 7233 3943 2955 -31 843 136 C ATOM 120 CD LYS A 23 4.001 4.470 43.199 1.00 36.02 C ANISOU 120 CD LYS A 23 7249 3643 2795 -65 1007 110 C ATOM 121 CE LYS A 23 3.149 5.677 43.587 1.00 36.44 C ANISOU 121 CE LYS A 23 7260 3659 2928 -179 1036 41 C ATOM 122 NZ LYS A 23 3.907 6.723 44.336 1.00 38.57 N ANISOU 122 NZ LYS A 23 7514 4018 3122 -176 919 29 N ATOM 123 N THR A 24 5.278 7.729 38.800 1.00 32.17 N ANISOU 123 N THR A 24 6038 3472 2713 -274 639 68 N ATOM 124 CA THR A 24 4.806 8.368 37.581 1.00 33.07 C ANISOU 124 CA THR A 24 6030 3577 2959 -341 629 49 C ATOM 125 C THR A 24 5.947 8.462 36.576 1.00 35.12 C ANISOU 125 C THR A 24 6176 3949 3219 -325 529 84 C ATOM 126 O THR A 24 5.785 8.092 35.419 1.00 36.31 O ANISOU 126 O THR A 24 6261 4098 3437 -321 537 100 O ATOM 127 CB THR A 24 4.174 9.728 37.877 1.00 35.90 C ANISOU 127 CB THR A 24 6368 3896 3376 -425 629 -3 C ATOM 128 OG1 THR A 24 3.005 9.492 38.664 1.00 34.67 O ANISOU 128 OG1 THR A 24 6306 3634 3234 -438 739 -42 O ATOM 129 CG2 THR A 24 3.749 10.428 36.580 1.00 33.18 C ANISOU 129 CG2 THR A 24 5912 3542 3151 -472 608 -18 C ATOM 130 N THR A 25 7.107 8.913 37.041 1.00 33.33 N ANISOU 130 N THR A 25 5927 3823 2914 -316 440 89 N ATOM 131 CA THR A 25 8.281 9.013 36.186 1.00 31.81 C ANISOU 131 CA THR A 25 5621 3748 2716 -308 353 110 C ATOM 132 C THR A 25 8.581 7.689 35.503 1.00 31.44 C ANISOU 132 C THR A 25 5567 3724 2654 -220 365 156 C ATOM 133 O THR A 25 8.887 7.655 34.312 1.00 33.12 O ANISOU 133 O THR A 25 5686 3976 2922 -231 343 172 O ATOM 134 CB THR A 25 9.505 9.439 36.979 1.00 31.46 C ANISOU 134 CB THR A 25 5556 3823 2574 -297 263 92 C ATOM 135 OG1 THR A 25 9.240 10.697 37.598 1.00 36.29 O ANISOU 135 OG1 THR A 25 6177 4409 3201 -387 255 43 O ATOM 136 CG2 THR A 25 10.711 9.572 36.045 1.00 36.30 C ANISOU 136 CG2 THR A 25 6034 4564 3193 -302 185 98 C ATOM 137 N PHE A 26 8.501 6.610 36.268 1.00 28.67 N ANISOU 137 N PHE A 26 5331 3342 2222 -131 407 177 N ATOM 138 CA PHE A 26 8.785 5.265 35.771 1.00 28.11 C ANISOU 138 CA PHE A 26 5284 3277 2120 -36 429 221 C ATOM 139 C PHE A 26 7.806 4.835 34.693 1.00 30.88 C ANISOU 139 C PHE A 26 5613 3540 2581 -70 509 223 C ATOM 140 O PHE A 26 8.213 4.531 33.576 1.00 36.80 O ANISOU 140 O PHE A 26 6278 4337 3368 -56 482 243 O ATOM 141 CB PHE A 26 8.763 4.269 36.939 1.00 34.04 C ANISOU 141 CB PHE A 26 6200 3981 2751 65 475 243 C ATOM 142 CG PHE A 26 9.023 2.831 36.536 1.00 40.83 C ANISOU 142 CG PHE A 26 7119 4826 3568 174 511 290 C ATOM 143 CD1 PHE A 26 10.301 2.409 36.189 1.00 39.42 C ANISOU 143 CD1 PHE A 26 6880 4773 3325 269 419 317 C ATOM 144 CD2 PHE A 26 7.997 1.903 36.524 1.00 41.20 C ANISOU 144 CD2 PHE A 26 7282 4733 3638 178 642 298 C ATOM 145 CE1 PHE A 26 10.546 1.108 35.836 1.00 35.74 C ANISOU 145 CE1 PHE A 26 6476 4287 2815 378 453 360 C ATOM 146 CE2 PHE A 26 8.241 0.570 36.157 1.00 35.68 C ANISOU 146 CE2 PHE A 26 6653 4008 2897 275 685 339 C ATOM 147 CZ PHE A 26 9.514 0.180 35.819 1.00 37.43 C ANISOU 147 CZ PHE A 26 6822 4349 3050 380 588 374 C ATOM 148 N VAL A 27 6.512 4.807 35.008 1.00 29.47 N ANISOU 148 N VAL A 27 5504 3239 2454 -117 607 193 N ATOM 149 CA VAL A 27 5.553 4.305 34.033 1.00 26.85 C ANISOU 149 CA VAL A 27 5145 2834 2222 -144 682 177 C ATOM 150 C VAL A 27 5.619 5.091 32.719 1.00 32.08 C ANISOU 150 C VAL A 27 5663 3548 2978 -196 619 169 C ATOM 151 O VAL A 27 5.421 4.529 31.627 1.00 35.39 O ANISOU 151 O VAL A 27 6034 3963 3451 -185 636 173 O ATOM 152 CB VAL A 27 4.110 4.269 34.575 1.00 30.88 C ANISOU 152 CB VAL A 27 5728 3219 2786 -199 799 123 C ATOM 153 CG1 VAL A 27 3.582 5.686 34.868 1.00 33.44 C ANISOU 153 CG1 VAL A 27 6006 3535 3167 -278 774 76 C ATOM 154 CG2 VAL A 27 3.211 3.531 33.581 1.00 34.32 C ANISOU 154 CG2 VAL A 27 6132 3595 3315 -217 877 94 C ATOM 155 N LYS A 28 5.928 6.381 32.830 1.00 31.80 N ANISOU 155 N LYS A 28 5572 3557 2954 -250 551 156 N ATOM 156 CA LYS A 28 5.949 7.270 31.679 1.00 37.17 C ANISOU 156 CA LYS A 28 6145 4267 3711 -301 502 149 C ATOM 157 C LYS A 28 7.136 7.046 30.738 1.00 38.16 C ANISOU 157 C LYS A 28 6190 4494 3813 -273 436 190 C ATOM 158 O LYS A 28 7.161 7.600 29.637 1.00 38.40 O ANISOU 158 O LYS A 28 6148 4543 3900 -307 408 192 O ATOM 159 CB LYS A 28 5.949 8.728 32.142 1.00 33.51 C ANISOU 159 CB LYS A 28 5670 3804 3259 -371 463 122 C ATOM 160 CG LYS A 28 4.625 9.241 32.681 1.00 37.78 C ANISOU 160 CG LYS A 28 6257 4242 3854 -411 523 71 C ATOM 161 CD LYS A 28 4.738 10.763 32.938 1.00 44.73 C ANISOU 161 CD LYS A 28 7124 5124 4748 -477 479 48 C ATOM 162 CE LYS A 28 3.414 11.371 33.403 1.00 54.01 C ANISOU 162 CE LYS A 28 8337 6201 5983 -508 534 -8 C ATOM 163 NZ LYS A 28 2.216 10.761 32.746 1.00 60.58 N ANISOU 163 NZ LYS A 28 9149 6973 6895 -485 595 -39 N ATOM 164 N ARG A 29 8.131 6.268 31.154 1.00 31.39 N ANISOU 164 N ARG A 29 5351 3707 2869 -204 410 221 N ATOM 165 CA ARG A 29 9.253 5.997 30.245 1.00 33.79 C ANISOU 165 CA ARG A 29 5569 4115 3155 -173 355 251 C ATOM 166 C ARG A 29 8.761 5.350 28.940 1.00 39.95 C ANISOU 166 C ARG A 29 6318 4861 4000 -159 392 264 C ATOM 167 O ARG A 29 9.349 5.543 27.866 1.00 34.79 O ANISOU 167 O ARG A 29 5581 4269 3367 -170 356 278 O ATOM 168 CB ARG A 29 10.288 5.072 30.899 1.00 29.55 C ANISOU 168 CB ARG A 29 5060 3656 2512 -72 325 275 C ATOM 169 CG ARG A 29 10.835 5.578 32.243 1.00 37.91 C ANISOU 169 CG ARG A 29 6153 4765 3488 -66 277 256 C ATOM 170 CD ARG A 29 11.248 7.027 32.145 1.00 37.24 C ANISOU 170 CD ARG A 29 5978 4736 3434 -170 221 221 C ATOM 171 NE ARG A 29 12.402 7.220 31.270 1.00 41.13 N ANISOU 171 NE ARG A 29 6347 5351 3929 -181 163 222 N ATOM 172 CZ ARG A 29 12.968 8.399 31.033 1.00 40.32 C ANISOU 172 CZ ARG A 29 6161 5308 3849 -278 124 189 C ATOM 173 NH1 ARG A 29 12.488 9.492 31.606 1.00 39.61 N ANISOU 173 NH1 ARG A 29 6104 5164 3782 -365 130 157 N ATOM 174 NH2 ARG A 29 14.022 8.488 30.227 1.00 44.01 N ANISOU 174 NH2 ARG A 29 6518 5885 4318 -294 88 184 N ATOM 175 N HIS A 30 7.687 4.576 29.047 1.00 35.43 N ANISOU 175 N HIS A 30 5815 4190 3457 -140 471 251 N ATOM 176 CA HIS A 30 7.141 3.828 27.911 1.00 28.01 C ANISOU 176 CA HIS A 30 4854 3216 2575 -125 512 248 C ATOM 177 C HIS A 30 6.307 4.755 27.027 1.00 30.28 C ANISOU 177 C HIS A 30 5080 3473 2954 -191 503 214 C ATOM 178 O HIS A 30 5.151 5.072 27.353 1.00 29.48 O ANISOU 178 O HIS A 30 5005 3293 2905 -227 546 167 O ATOM 179 CB HIS A 30 6.279 2.690 28.428 1.00 32.26 C ANISOU 179 CB HIS A 30 5490 3657 3110 -94 610 230 C ATOM 180 CG HIS A 30 5.928 1.673 27.386 1.00 37.37 C ANISOU 180 CG HIS A 30 6124 4277 3797 -70 657 224 C ATOM 181 ND1 HIS A 30 5.104 1.958 26.321 1.00 38.20 N ANISOU 181 ND1 HIS A 30 6160 4363 3992 -114 662 183 N ATOM 182 CD2 HIS A 30 6.277 0.370 27.256 1.00 31.53 C ANISOU 182 CD2 HIS A 30 5439 3527 3014 0 700 248 C ATOM 183 CE1 HIS A 30 4.951 0.873 25.584 1.00 38.84 C ANISOU 183 CE1 HIS A 30 6245 4426 4087 -82 706 176 C ATOM 184 NE2 HIS A 30 5.648 -0.105 26.131 1.00 29.50 N ANISOU 184 NE2 HIS A 30 5141 3242 2827 -17 735 217 N ATOM 185 N LEU A 31 6.898 5.184 25.912 1.00 27.58 N ANISOU 185 N LEU A 31 4662 3193 2626 -201 449 235 N ATOM 186 CA LEU A 31 6.330 6.251 25.101 1.00 26.43 C ANISOU 186 CA LEU A 31 4475 3025 2542 -250 425 215 C ATOM 187 C LEU A 31 4.923 5.992 24.579 1.00 31.19 C ANISOU 187 C LEU A 31 5078 3553 3218 -246 467 164 C ATOM 188 O LEU A 31 4.087 6.882 24.611 1.00 28.69 O ANISOU 188 O LEU A 31 4761 3192 2948 -276 462 126 O ATOM 189 CB LEU A 31 7.272 6.610 23.942 1.00 32.59 C ANISOU 189 CB LEU A 31 5193 3880 3310 -256 376 251 C ATOM 190 CG LEU A 31 8.652 7.176 24.309 1.00 35.45 C ANISOU 190 CG LEU A 31 5525 4329 3615 -284 331 279 C ATOM 191 CD1 LEU A 31 9.510 7.317 23.056 1.00 33.11 C ANISOU 191 CD1 LEU A 31 5167 4101 3311 -293 307 306 C ATOM 192 CD2 LEU A 31 8.537 8.513 25.028 1.00 33.43 C ANISOU 192 CD2 LEU A 31 5290 4048 3364 -354 314 259 C ATOM 193 N THR A 32 4.668 4.794 24.056 1.00 28.02 N ANISOU 193 N THR A 32 4675 3144 2828 -207 507 155 N ATOM 194 CA THR A 32 3.340 4.487 23.547 1.00 25.53 C ANISOU 194 CA THR A 32 4344 2772 2585 -209 547 87 C ATOM 195 C THR A 32 2.344 4.339 24.705 1.00 29.57 C ANISOU 195 C THR A 32 4904 3207 3124 -235 619 29 C ATOM 196 O THR A 32 1.170 4.674 24.564 1.00 36.56 O ANISOU 196 O THR A 32 5762 4052 4078 -254 638 -44 O ATOM 197 CB THR A 32 3.340 3.207 22.683 1.00 42.32 C ANISOU 197 CB THR A 32 6457 4907 4716 -171 580 81 C ATOM 198 OG1 THR A 32 4.259 3.361 21.588 1.00 43.63 O ANISOU 198 OG1 THR A 32 6578 5144 4854 -148 519 131 O ATOM 199 CG2 THR A 32 1.942 2.927 22.142 1.00 41.30 C ANISOU 199 CG2 THR A 32 6294 4731 4665 -181 617 -11 C ATOM 200 N GLY A 33 2.813 3.836 25.847 1.00 27.96 N ANISOU 200 N GLY A 33 4774 2988 2862 -229 660 58 N ATOM 201 CA GLY A 33 1.958 3.706 27.017 1.00 31.73 C ANISOU 201 CA GLY A 33 5315 3388 3351 -257 740 9 C ATOM 202 C GLY A 33 1.521 5.078 27.482 1.00 38.09 C ANISOU 202 C GLY A 33 6105 4182 4186 -298 705 -17 C ATOM 203 O GLY A 33 0.411 5.264 27.981 1.00 42.62 O ANISOU 203 O GLY A 33 6688 4695 4811 -329 762 -88 O ATOM 204 N GLU A 34 2.400 6.056 27.305 1.00 30.94 N ANISOU 204 N GLU A 34 5174 3333 3249 -301 618 32 N ATOM 205 CA GLU A 34 2.069 7.426 27.680 1.00 33.40 C ANISOU 205 CA GLU A 34 5481 3627 3583 -339 585 11 C ATOM 206 C GLU A 34 1.131 8.076 26.662 1.00 38.04 C ANISOU 206 C GLU A 34 6008 4195 4248 -337 560 -38 C ATOM 207 O GLU A 34 0.196 8.768 27.055 1.00 37.96 O ANISOU 207 O GLU A 34 6000 4138 4284 -353 575 -95 O ATOM 208 CB GLU A 34 3.328 8.266 27.866 1.00 37.24 C ANISOU 208 CB GLU A 34 5968 4173 4008 -356 513 70 C ATOM 209 CG GLU A 34 3.071 9.781 27.892 1.00 40.90 C ANISOU 209 CG GLU A 34 6428 4613 4499 -398 474 52 C ATOM 210 CD GLU A 34 2.418 10.253 29.191 1.00 51.25 C ANISOU 210 CD GLU A 34 7794 5866 5814 -427 513 8 C ATOM 211 OE1 GLU A 34 2.324 9.449 30.146 1.00 44.54 O ANISOU 211 OE1 GLU A 34 6992 4998 4931 -418 568 0 O ATOM 212 OE2 GLU A 34 2.006 11.432 29.258 1.00 59.37 O ANISOU 212 OE2 GLU A 34 8828 6858 6871 -454 494 -17 O ATOM 213 N SER A 35 1.366 7.858 25.362 1.00 36.40 N ANISOU 213 N SER A 35 5751 4028 4051 -308 520 -19 N ATOM 214 CA SER A 35 0.495 8.457 24.338 1.00 35.18 C ANISOU 214 CA SER A 35 5549 3862 3955 -285 485 -65 C ATOM 215 C SER A 35 -0.901 7.830 24.312 1.00 39.37 C ANISOU 215 C SER A 35 6043 4357 4558 -274 541 -166 C ATOM 216 O SER A 35 -1.873 8.465 23.915 1.00 37.08 O ANISOU 216 O SER A 35 5715 4053 4322 -252 518 -232 O ATOM 217 CB SER A 35 1.140 8.431 22.941 1.00 42.24 C ANISOU 217 CB SER A 35 6412 4808 4828 -254 428 -18 C ATOM 218 OG SER A 35 1.301 7.111 22.452 1.00 41.84 O ANISOU 218 OG SER A 35 6338 4785 4774 -232 458 -17 O ATOM 219 N GLU A 36 -1.014 6.594 24.784 1.00 38.40 N ANISOU 219 N GLU A 36 5936 4219 4435 -288 620 -186 N ATOM 220 CA GLU A 36 -2.297 5.905 24.755 1.00 40.73 C ANISOU 220 CA GLU A 36 6193 4480 4802 -297 693 -294 C ATOM 221 C GLU A 36 -2.951 5.769 26.136 1.00 37.62 C ANISOU 221 C GLU A 36 5846 4023 4426 -344 789 -347 C ATOM 222 O GLU A 36 -3.900 5.007 26.310 1.00 35.84 O ANISOU 222 O GLU A 36 5603 3763 4253 -371 880 -439 O ATOM 223 CB GLU A 36 -2.138 4.540 24.077 1.00 43.62 C ANISOU 223 CB GLU A 36 6546 4861 5165 -286 732 -298 C ATOM 224 CG GLU A 36 -1.730 4.682 22.627 1.00 50.79 C ANISOU 224 CG GLU A 36 7401 5831 6066 -240 644 -269 C ATOM 225 CD GLU A 36 -1.662 3.363 21.878 1.00 62.76 C ANISOU 225 CD GLU A 36 8900 7362 7585 -228 682 -285 C ATOM 226 OE1 GLU A 36 -1.984 2.311 22.471 1.00 70.80 O ANISOU 226 OE1 GLU A 36 9952 8333 8614 -260 785 -324 O ATOM 227 OE2 GLU A 36 -1.284 3.389 20.686 1.00 66.47 O ANISOU 227 OE2 GLU A 36 9333 7882 8040 -189 616 -260 O ATOM 228 N LYS A 37 -2.456 6.520 27.115 1.00 36.08 N ANISOU 228 N LYS A 37 5712 3811 4184 -360 776 -297 N ATOM 229 CA LYS A 37 -2.930 6.350 28.482 1.00 32.87 C ANISOU 229 CA LYS A 37 5371 3343 3774 -402 871 -334 C ATOM 230 C LYS A 37 -4.392 6.787 28.600 1.00 40.81 C ANISOU 230 C LYS A 37 6317 4316 4873 -422 914 -458 C ATOM 231 O LYS A 37 -4.864 7.636 27.843 1.00 41.93 O ANISOU 231 O LYS A 37 6383 4485 5063 -391 840 -496 O ATOM 232 CB LYS A 37 -2.070 7.158 29.450 1.00 34.44 C ANISOU 232 CB LYS A 37 5643 3544 3901 -411 833 -262 C ATOM 233 CG LYS A 37 -2.378 8.638 29.439 1.00 41.85 C ANISOU 233 CG LYS A 37 6551 4481 4869 -415 769 -282 C ATOM 234 CD LYS A 37 -1.257 9.422 30.084 1.00 46.16 C ANISOU 234 CD LYS A 37 7156 5045 5337 -428 714 -203 C ATOM 235 CE LYS A 37 -1.533 10.922 30.055 1.00 44.07 C ANISOU 235 CE LYS A 37 6880 4765 5099 -436 659 -222 C ATOM 236 NZ LYS A 37 -0.461 11.628 30.814 1.00 50.84 N ANISOU 236 NZ LYS A 37 7796 5638 5882 -467 621 -162 N ATOM 237 N LYS A 38 -5.108 6.208 29.552 1.00 36.60 N ANISOU 237 N LYS A 38 5824 3723 4359 -470 1037 -525 N ATOM 238 CA LYS A 38 -6.509 6.549 29.744 1.00 38.49 C ANISOU 238 CA LYS A 38 5996 3939 4691 -495 1093 -659 C ATOM 239 C LYS A 38 -6.746 7.106 31.148 1.00 45.39 C ANISOU 239 C LYS A 38 6944 4757 5545 -533 1155 -672 C ATOM 240 O LYS A 38 -6.365 6.484 32.140 1.00 38.43 O ANISOU 240 O LYS A 38 6176 3827 4599 -567 1240 -632 O ATOM 241 CB LYS A 38 -7.371 5.309 29.526 1.00 38.19 C ANISOU 241 CB LYS A 38 5919 3879 4713 -537 1210 -764 C ATOM 242 CG LYS A 38 -7.050 4.583 28.216 1.00 45.71 C ANISOU 242 CG LYS A 38 6815 4880 5672 -505 1161 -749 C ATOM 243 CD LYS A 38 -7.841 3.294 28.068 1.00 56.31 C ANISOU 243 CD LYS A 38 8133 6193 7071 -560 1291 -857 C ATOM 244 CE LYS A 38 -9.280 3.571 27.662 1.00 66.54 C ANISOU 244 CE LYS A 38 9283 7518 8482 -577 1309 -1031 C ATOM 245 NZ LYS A 38 -9.365 4.212 26.317 1.00 70.19 N ANISOU 245 NZ LYS A 38 9626 8070 8974 -496 1157 -1047 N ATOM 246 N TYR A 39 -7.377 8.274 31.231 1.00 44.55 N ANISOU 246 N TYR A 39 6786 4655 5487 -519 1112 -728 N ATOM 247 CA TYR A 39 -7.691 8.862 32.539 1.00 47.29 C ANISOU 247 CA TYR A 39 7199 4949 5821 -555 1174 -752 C ATOM 248 C TYR A 39 -9.003 8.302 33.083 1.00 47.84 C ANISOU 248 C TYR A 39 7237 4975 5966 -610 1321 -893 C ATOM 249 O TYR A 39 -9.995 8.173 32.361 1.00 48.98 O ANISOU 249 O TYR A 39 7256 5148 6205 -603 1332 -1011 O ATOM 250 CB TYR A 39 -7.726 10.388 32.473 1.00 48.28 C ANISOU 250 CB TYR A 39 7300 5086 5957 -516 1072 -747 C ATOM 251 CG TYR A 39 -8.047 11.045 33.809 1.00 57.90 C ANISOU 251 CG TYR A 39 8588 6250 7161 -552 1134 -776 C ATOM 252 CD1 TYR A 39 -7.180 10.931 34.890 1.00 56.04 C ANISOU 252 CD1 TYR A 39 8479 5984 6827 -586 1163 -695 C ATOM 253 CD2 TYR A 39 -9.219 11.772 33.987 1.00 62.57 C ANISOU 253 CD2 TYR A 39 9115 6825 7833 -542 1159 -893 C ATOM 254 CE1 TYR A 39 -7.475 11.525 36.121 1.00 59.69 C ANISOU 254 CE1 TYR A 39 9012 6397 7269 -619 1220 -725 C ATOM 255 CE2 TYR A 39 -9.521 12.368 35.208 1.00 60.70 C ANISOU 255 CE2 TYR A 39 8943 6537 7582 -576 1221 -923 C ATOM 256 CZ TYR A 39 -8.646 12.242 36.268 1.00 57.54 C ANISOU 256 CZ TYR A 39 8678 6104 7082 -617 1252 -837 C ATOM 257 OH TYR A 39 -8.946 12.830 37.477 1.00 61.01 O ANISOU 257 OH TYR A 39 9188 6492 7500 -649 1314 -871 O ATOM 258 N VAL A 40 -8.989 7.933 34.357 1.00 44.74 N ANISOU 258 N VAL A 40 6958 4516 5524 -665 1438 -888 N ATOM 259 CA VAL A 40 -10.167 7.396 35.013 1.00 46.95 C ANISOU 259 CA VAL A 40 7231 4743 5866 -735 1604 -1019 C ATOM 260 C VAL A 40 -10.541 8.333 36.160 1.00 53.13 C ANISOU 260 C VAL A 40 8061 5486 6639 -754 1641 -1051 C ATOM 261 O VAL A 40 -9.995 8.228 37.259 1.00 49.20 O ANISOU 261 O VAL A 40 7710 4935 6047 -779 1694 -982 O ATOM 262 CB VAL A 40 -9.889 6.001 35.554 1.00 40.75 C ANISOU 262 CB VAL A 40 6570 3894 5020 -789 1742 -989 C ATOM 263 CG1 VAL A 40 -11.171 5.358 36.060 1.00 44.32 C ANISOU 263 CG1 VAL A 40 7006 4287 5548 -878 1934 -1142 C ATOM 264 CG2 VAL A 40 -9.239 5.146 34.471 1.00 43.98 C ANISOU 264 CG2 VAL A 40 6957 4340 5415 -757 1688 -929 C ATOM 265 N ALA A 41 -11.464 9.250 35.885 1.00 55.07 N ANISOU 265 N ALA A 41 8186 5760 6977 -732 1606 -1156 N ATOM 266 CA ALA A 41 -11.778 10.345 36.808 1.00 53.61 C ANISOU 266 CA ALA A 41 8035 5546 6790 -732 1614 -1184 C ATOM 267 C ALA A 41 -12.333 9.847 38.133 1.00 55.51 C ANISOU 267 C ALA A 41 8366 5710 7016 -817 1799 -1247 C ATOM 268 O ALA A 41 -11.909 10.289 39.196 1.00 58.93 O ANISOU 268 O ALA A 41 8924 6097 7368 -831 1819 -1191 O ATOM 269 CB ALA A 41 -12.749 11.314 36.165 1.00 53.64 C ANISOU 269 CB ALA A 41 7888 5595 6900 -676 1547 -1297 C ATOM 270 N THR A 42 -13.275 8.917 38.061 1.00 61.49 N ANISOU 270 N THR A 42 9065 6452 7847 -878 1940 -1370 N ATOM 271 CA THR A 42 -13.889 8.352 39.256 1.00 65.50 C ANISOU 271 CA THR A 42 9664 6878 8346 -972 2143 -1443 C ATOM 272 C THR A 42 -12.864 7.936 40.309 1.00 61.24 C ANISOU 272 C THR A 42 9349 6266 7655 -990 2190 -1302 C ATOM 273 O THR A 42 -13.112 8.061 41.507 1.00 66.44 O ANISOU 273 O THR A 42 10118 6857 8267 -1035 2304 -1323 O ATOM 274 CB THR A 42 -14.767 7.151 38.902 1.00 69.44 C ANISOU 274 CB THR A 42 10092 7363 8927 -1050 2296 -1572 C ATOM 275 OG1 THR A 42 -14.116 6.381 37.884 1.00 76.90 O ANISOU 275 OG1 THR A 42 11021 8341 9855 -1022 2224 -1499 O ATOM 276 CG2 THR A 42 -16.117 7.624 38.381 1.00 66.26 C ANISOU 276 CG2 THR A 42 9473 7025 8678 -1053 2306 -1767 C ATOM 277 N LEU A 43 -11.709 7.455 39.865 1.00 55.78 N ANISOU 277 N LEU A 43 8724 5592 6879 -946 2099 -1164 N ATOM 278 CA LEU A 43 -10.696 6.967 40.796 1.00 52.81 C ANISOU 278 CA LEU A 43 8555 5161 6351 -942 2130 -1035 C ATOM 279 C LEU A 43 -9.470 7.874 40.858 1.00 49.10 C ANISOU 279 C LEU A 43 8124 4743 5790 -868 1948 -904 C ATOM 280 O LEU A 43 -8.601 7.696 41.711 1.00 48.31 O ANISOU 280 O LEU A 43 8182 4616 5558 -851 1947 -808 O ATOM 281 CB LEU A 43 -10.288 5.530 40.440 1.00 52.22 C ANISOU 281 CB LEU A 43 8554 5056 6233 -950 2196 -986 C ATOM 282 CG LEU A 43 -11.402 4.483 40.527 1.00 53.63 C ANISOU 282 CG LEU A 43 8732 5162 6482 -1045 2408 -1115 C ATOM 283 CD1 LEU A 43 -11.076 3.224 39.714 1.00 50.56 C ANISOU 283 CD1 LEU A 43 8358 4765 6090 -1045 2436 -1085 C ATOM 284 CD2 LEU A 43 -11.700 4.118 41.972 1.00 57.21 C ANISOU 284 CD2 LEU A 43 9377 5504 6858 -1107 2597 -1131 C ATOM 285 N GLY A 44 -9.413 8.864 39.973 1.00 46.21 N ANISOU 285 N GLY A 44 7618 4449 5490 -824 1799 -907 N ATOM 286 CA GLY A 44 -8.227 9.692 39.847 1.00 45.51 C ANISOU 286 CA GLY A 44 7552 4411 5328 -768 1633 -792 C ATOM 287 C GLY A 44 -7.003 8.845 39.518 1.00 53.40 C ANISOU 287 C GLY A 44 8616 5440 6234 -733 1577 -671 C ATOM 288 O GLY A 44 -6.018 8.833 40.264 1.00 52.16 O ANISOU 288 O GLY A 44 8577 5284 5955 -713 1544 -582 O ATOM 289 N VAL A 45 -7.065 8.130 38.396 1.00 46.81 N ANISOU 289 N VAL A 45 7697 4636 5454 -718 1563 -675 N ATOM 290 CA VAL A 45 -5.991 7.225 37.996 1.00 43.42 C ANISOU 290 CA VAL A 45 7320 4233 4947 -680 1521 -571 C ATOM 291 C VAL A 45 -5.754 7.356 36.501 1.00 45.92 C ANISOU 291 C VAL A 45 7497 4622 5327 -643 1405 -556 C ATOM 292 O VAL A 45 -6.685 7.649 35.752 1.00 46.47 O ANISOU 292 O VAL A 45 7444 4706 5508 -652 1403 -646 O ATOM 293 CB VAL A 45 -6.365 5.751 38.303 1.00 44.70 C ANISOU 293 CB VAL A 45 7574 4322 5089 -710 1682 -594 C ATOM 294 CG1 VAL A 45 -5.482 4.772 37.510 1.00 44.42 C ANISOU 294 CG1 VAL A 45 7552 4318 5010 -662 1637 -511 C ATOM 295 CG2 VAL A 45 -6.289 5.468 39.800 1.00 45.11 C ANISOU 295 CG2 VAL A 45 7810 4295 5034 -729 1793 -575 C ATOM 296 N GLU A 46 -4.510 7.157 36.069 1.00 34.16 N ANISOU 296 N GLU A 46 6027 3187 3765 -595 1305 -448 N ATOM 297 CA GLU A 46 -4.218 7.012 34.645 1.00 34.39 C ANISOU 297 CA GLU A 46 5948 3278 3839 -562 1218 -426 C ATOM 298 C GLU A 46 -3.750 5.587 34.378 1.00 39.34 C ANISOU 298 C GLU A 46 6628 3899 4422 -543 1268 -382 C ATOM 299 O GLU A 46 -2.825 5.106 35.030 1.00 45.08 O ANISOU 299 O GLU A 46 7466 4622 5040 -514 1269 -302 O ATOM 300 CB GLU A 46 -3.141 8.007 34.214 1.00 39.67 C ANISOU 300 CB GLU A 46 6585 4020 4470 -527 1066 -345 C ATOM 301 CG GLU A 46 -3.616 9.462 34.220 1.00 47.02 C ANISOU 301 CG GLU A 46 7464 4950 5452 -539 1012 -387 C ATOM 302 CD GLU A 46 -2.531 10.454 33.839 1.00 65.36 C ANISOU 302 CD GLU A 46 9774 7328 7732 -523 883 -311 C ATOM 303 OE1 GLU A 46 -1.337 10.076 33.836 1.00 69.20 O ANISOU 303 OE1 GLU A 46 10291 7862 8139 -508 838 -230 O ATOM 304 OE2 GLU A 46 -2.875 11.622 33.547 1.00 73.77 O ANISOU 304 OE2 GLU A 46 10799 8387 8842 -524 833 -339 O ATOM 305 N VAL A 47 -4.395 4.912 33.431 1.00 37.72 N ANISOU 305 N VAL A 47 6345 3691 4295 -552 1307 -442 N ATOM 306 CA VAL A 47 -4.027 3.545 33.067 1.00 33.87 C ANISOU 306 CA VAL A 47 5907 3189 3775 -537 1362 -410 C ATOM 307 C VAL A 47 -3.168 3.590 31.793 1.00 32.55 C ANISOU 307 C VAL A 47 5656 3106 3603 -482 1232 -344 C ATOM 308 O VAL A 47 -3.636 4.033 30.742 1.00 37.65 O ANISOU 308 O VAL A 47 6179 3796 4332 -480 1173 -393 O ATOM 309 CB VAL A 47 -5.273 2.688 32.811 1.00 41.04 C ANISOU 309 CB VAL A 47 6783 4039 4772 -595 1501 -530 C ATOM 310 CG1 VAL A 47 -4.881 1.254 32.498 1.00 37.77 C ANISOU 310 CG1 VAL A 47 6443 3590 4317 -584 1572 -496 C ATOM 311 CG2 VAL A 47 -6.206 2.732 34.032 1.00 39.79 C ANISOU 311 CG2 VAL A 47 6695 3797 4628 -662 1643 -609 C ATOM 312 N HIS A 48 -1.907 3.174 31.907 1.00 29.28 N ANISOU 312 N HIS A 48 5313 2722 3090 -430 1185 -238 N ATOM 313 CA HIS A 48 -0.951 3.218 30.791 1.00 29.24 C ANISOU 313 CA HIS A 48 5238 2802 3070 -380 1070 -172 C ATOM 314 C HIS A 48 -0.872 1.838 30.180 1.00 33.30 C ANISOU 314 C HIS A 48 5774 3297 3579 -358 1130 -168 C ATOM 315 O HIS A 48 -0.443 0.871 30.837 1.00 33.61 O ANISOU 315 O HIS A 48 5937 3293 3541 -331 1200 -126 O ATOM 316 CB HIS A 48 0.449 3.631 31.268 1.00 27.99 C ANISOU 316 CB HIS A 48 5123 2703 2807 -336 977 -72 C ATOM 317 CG HIS A 48 0.539 5.040 31.802 1.00 24.27 C ANISOU 317 CG HIS A 48 4631 2255 2334 -363 910 -73 C ATOM 318 ND1 HIS A 48 -0.130 5.456 32.936 1.00 39.63 N ANISOU 318 ND1 HIS A 48 6639 4141 4279 -400 971 -117 N ATOM 319 CD2 HIS A 48 1.261 6.106 31.384 1.00 26.62 C ANISOU 319 CD2 HIS A 48 4866 2624 2626 -362 797 -37 C ATOM 320 CE1 HIS A 48 0.165 6.722 33.184 1.00 30.25 C ANISOU 320 CE1 HIS A 48 5423 2984 3085 -418 893 -109 C ATOM 321 NE2 HIS A 48 1.003 7.144 32.251 1.00 34.70 N ANISOU 321 NE2 HIS A 48 5913 3624 3646 -399 790 -62 N ATOM 322 N PRO A 49 -1.306 1.718 28.922 1.00 37.87 N ANISOU 322 N PRO A 49 6247 3906 4237 -364 1106 -213 N ATOM 323 CA PRO A 49 -1.232 0.418 28.246 1.00 36.84 C ANISOU 323 CA PRO A 49 6133 3759 4106 -347 1162 -217 C ATOM 324 C PRO A 49 0.192 0.167 27.745 1.00 37.16 C ANISOU 324 C PRO A 49 6183 3868 4067 -274 1074 -109 C ATOM 325 O PRO A 49 0.593 0.789 26.761 1.00 30.21 O ANISOU 325 O PRO A 49 5205 3066 3207 -255 968 -87 O ATOM 326 CB PRO A 49 -2.180 0.583 27.049 1.00 43.40 C ANISOU 326 CB PRO A 49 6829 4617 5044 -374 1144 -312 C ATOM 327 CG PRO A 49 -2.894 1.896 27.250 1.00 44.46 C ANISOU 327 CG PRO A 49 6892 4766 5235 -399 1096 -366 C ATOM 328 CD PRO A 49 -2.007 2.732 28.116 1.00 31.64 C ANISOU 328 CD PRO A 49 5330 3156 3536 -381 1036 -275 C ATOM 329 N LEU A 50 0.931 -0.733 28.393 1.00 32.70 N ANISOU 329 N LEU A 50 5739 3274 3410 -227 1119 -46 N ATOM 330 CA LEU A 50 2.319 -0.974 28.011 1.00 31.30 C ANISOU 330 CA LEU A 50 5563 3174 3156 -147 1034 47 C ATOM 331 C LEU A 50 2.501 -2.276 27.246 1.00 36.10 C ANISOU 331 C LEU A 50 6198 3762 3756 -108 1085 53 C ATOM 332 O LEU A 50 2.509 -3.345 27.837 1.00 35.79 O ANISOU 332 O LEU A 50 6290 3645 3665 -81 1184 65 O ATOM 333 CB LEU A 50 3.236 -0.989 29.227 1.00 34.42 C ANISOU 333 CB LEU A 50 6065 3577 3436 -91 1017 117 C ATOM 334 CG LEU A 50 3.261 0.184 30.207 1.00 42.41 C ANISOU 334 CG LEU A 50 7080 4606 4427 -120 971 118 C ATOM 335 CD1 LEU A 50 4.647 0.274 30.829 1.00 36.58 C ANISOU 335 CD1 LEU A 50 6381 3945 3573 -42 888 195 C ATOM 336 CD2 LEU A 50 2.877 1.485 29.540 1.00 45.09 C ANISOU 336 CD2 LEU A 50 7285 4993 4854 -181 895 82 C ATOM 337 N VAL A 51 2.672 -2.196 25.933 1.00 31.14 N ANISOU 337 N VAL A 51 5461 3198 3172 -102 1022 49 N ATOM 338 CA VAL A 51 2.914 -3.418 25.178 1.00 36.74 C ANISOU 338 CA VAL A 51 6195 3892 3870 -63 1066 54 C ATOM 339 C VAL A 51 4.390 -3.795 25.209 1.00 33.55 C ANISOU 339 C VAL A 51 5828 3552 3366 36 1007 152 C ATOM 340 O VAL A 51 5.267 -2.932 25.142 1.00 33.83 O ANISOU 340 O VAL A 51 5796 3686 3373 60 897 200 O ATOM 341 CB VAL A 51 2.433 -3.318 23.718 1.00 41.40 C ANISOU 341 CB VAL A 51 6664 4524 4544 -92 1032 -1 C ATOM 342 CG1 VAL A 51 3.229 -2.264 22.974 1.00 52.56 C ANISOU 342 CG1 VAL A 51 7973 6049 5950 -69 895 50 C ATOM 343 CG2 VAL A 51 2.579 -4.673 23.025 1.00 43.27 C ANISOU 343 CG2 VAL A 51 6941 4730 4770 -60 1097 -8 C ATOM 344 N PHE A 52 4.634 -5.096 25.321 1.00 29.33 N ANISOU 344 N PHE A 52 5403 2959 2781 93 1086 171 N ATOM 345 CA PHE A 52 5.955 -5.694 25.216 1.00 34.84 C ANISOU 345 CA PHE A 52 6138 3713 3388 205 1041 249 C ATOM 346 C PHE A 52 5.840 -6.854 24.223 1.00 31.27 C ANISOU 346 C PHE A 52 5704 3222 2956 226 1105 229 C ATOM 347 O PHE A 52 4.874 -7.617 24.258 1.00 37.99 O ANISOU 347 O PHE A 52 6629 3959 3845 177 1228 170 O ATOM 348 CB PHE A 52 6.406 -6.232 26.591 1.00 37.07 C ANISOU 348 CB PHE A 52 6584 3943 3559 284 1084 298 C ATOM 349 CG PHE A 52 6.695 -5.148 27.605 1.00 35.63 C ANISOU 349 CG PHE A 52 6388 3811 3338 278 1011 319 C ATOM 350 CD1 PHE A 52 5.688 -4.678 28.444 1.00 36.78 C ANISOU 350 CD1 PHE A 52 6581 3877 3515 197 1073 275 C ATOM 351 CD2 PHE A 52 7.974 -4.613 27.727 1.00 29.42 C ANISOU 351 CD2 PHE A 52 5539 3154 2486 349 886 372 C ATOM 352 CE1 PHE A 52 5.944 -3.675 29.379 1.00 41.34 C ANISOU 352 CE1 PHE A 52 7152 4499 4056 189 1008 290 C ATOM 353 CE2 PHE A 52 8.243 -3.622 28.659 1.00 40.11 C ANISOU 353 CE2 PHE A 52 6879 4556 3804 336 820 380 C ATOM 354 CZ PHE A 52 7.226 -3.142 29.487 1.00 39.31 C ANISOU 354 CZ PHE A 52 6835 4370 3732 257 880 342 C ATOM 355 N HIS A 53 6.826 -6.993 23.346 1.00 31.46 N ANISOU 355 N HIS A 53 5659 3339 2955 292 1031 271 N ATOM 356 CA HIS A 53 6.799 -8.013 22.311 1.00 30.45 C ANISOU 356 CA HIS A 53 5539 3186 2845 314 1080 252 C ATOM 357 C HIS A 53 7.660 -9.182 22.740 1.00 34.25 C ANISOU 357 C HIS A 53 6155 3632 3224 439 1123 310 C ATOM 358 O HIS A 53 8.865 -9.035 22.935 1.00 35.50 O ANISOU 358 O HIS A 53 6294 3886 3307 537 1037 375 O ATOM 359 CB HIS A 53 7.302 -7.418 20.990 1.00 34.23 C ANISOU 359 CB HIS A 53 5861 3785 3359 309 978 257 C ATOM 360 CG HIS A 53 6.416 -6.340 20.467 1.00 32.52 C ANISOU 360 CG HIS A 53 5533 3591 3232 206 938 200 C ATOM 361 ND1 HIS A 53 5.207 -6.608 19.863 1.00 35.09 N ANISOU 361 ND1 HIS A 53 5838 3857 3637 136 997 112 N ATOM 362 CD2 HIS A 53 6.525 -4.991 20.509 1.00 31.04 C ANISOU 362 CD2 HIS A 53 5255 3475 3063 168 847 212 C ATOM 363 CE1 HIS A 53 4.624 -5.472 19.531 1.00 33.38 C ANISOU 363 CE1 HIS A 53 5522 3680 3480 74 934 76 C ATOM 364 NE2 HIS A 53 5.401 -4.474 19.914 1.00 35.69 N ANISOU 364 NE2 HIS A 53 5780 4044 3736 91 848 140 N ATOM 365 N THR A 54 7.031 -10.338 22.924 1.00 35.59 N ANISOU 365 N THR A 54 6468 3666 3390 436 1260 281 N ATOM 366 CA THR A 54 7.726 -11.469 23.507 1.00 30.95 C ANISOU 366 CA THR A 54 6052 3014 2693 564 1317 339 C ATOM 367 C THR A 54 7.886 -12.542 22.464 1.00 42.38 C ANISOU 367 C THR A 54 7523 4432 4149 601 1370 325 C ATOM 368 O THR A 54 7.234 -12.498 21.415 1.00 37.71 O ANISOU 368 O THR A 54 6833 3846 3651 508 1385 258 O ATOM 369 CB THR A 54 6.962 -12.077 24.711 1.00 33.80 C ANISOU 369 CB THR A 54 6617 3210 3017 545 1461 326 C ATOM 370 OG1 THR A 54 6.021 -13.053 24.239 1.00 39.37 O ANISOU 370 OG1 THR A 54 7400 3781 3777 470 1612 255 O ATOM 371 CG2 THR A 54 6.235 -10.993 25.505 1.00 42.85 C ANISOU 371 CG2 THR A 54 7721 4357 4204 444 1447 295 C ATOM 372 N ASN A 55 8.740 -13.518 22.756 1.00 41.99 N ANISOU 372 N ASN A 55 7607 4350 3995 745 1396 385 N ATOM 373 CA ASN A 55 8.975 -14.606 21.820 1.00 48.22 C ANISOU 373 CA ASN A 55 8438 5103 4782 795 1452 376 C ATOM 374 C ASN A 55 7.705 -15.415 21.543 1.00 52.20 C ANISOU 374 C ASN A 55 9036 5445 5353 680 1617 292 C ATOM 375 O ASN A 55 7.671 -16.230 20.617 1.00 55.21 O ANISOU 375 O ASN A 55 9430 5791 5756 683 1671 260 O ATOM 376 CB ASN A 55 10.109 -15.518 22.303 1.00 51.01 C ANISOU 376 CB ASN A 55 8938 5442 5001 989 1453 456 C ATOM 377 CG ASN A 55 9.756 -16.275 23.574 1.00 47.18 C ANISOU 377 CG ASN A 55 8708 4788 4430 1038 1577 480 C ATOM 378 OD1 ASN A 55 9.183 -15.714 24.506 1.00 42.42 O ANISOU 378 OD1 ASN A 55 8142 4147 3829 972 1597 473 O ATOM 379 ND2 ASN A 55 10.100 -17.560 23.614 1.00 46.01 N ANISOU 379 ND2 ASN A 55 8749 4532 4200 1158 1669 510 N ATOM 380 N ARG A 56 6.662 -15.174 22.335 1.00 45.69 N ANISOU 380 N ARG A 56 8270 4526 4564 572 1701 245 N ATOM 381 CA ARG A 56 5.370 -15.823 22.126 1.00 56.35 C ANISOU 381 CA ARG A 56 9683 5734 5992 437 1864 141 C ATOM 382 C ARG A 56 4.251 -14.843 21.804 1.00 53.37 C ANISOU 382 C ARG A 56 9133 5404 5743 275 1839 42 C ATOM 383 O ARG A 56 3.077 -15.137 22.035 1.00 60.47 O ANISOU 383 O ARG A 56 10076 6194 6705 151 1972 -54 O ATOM 384 CB ARG A 56 4.981 -16.652 23.349 1.00 62.48 C ANISOU 384 CB ARG A 56 10714 6326 6700 445 2032 151 C ATOM 385 CG ARG A 56 5.578 -18.041 23.348 1.00 65.48 C ANISOU 385 CG ARG A 56 11305 6592 6983 567 2130 199 C ATOM 386 CD ARG A 56 5.244 -18.779 24.622 1.00 62.14 C ANISOU 386 CD ARG A 56 11160 5978 6472 586 2296 221 C ATOM 387 NE ARG A 56 3.807 -18.923 24.818 1.00 64.21 N ANISOU 387 NE ARG A 56 11459 6111 6828 391 2466 105 N ATOM 388 CZ ARG A 56 3.273 -19.591 25.835 1.00 58.94 C ANISOU 388 CZ ARG A 56 11036 5254 6105 360 2652 98 C ATOM 389 NH1 ARG A 56 1.955 -19.692 25.964 1.00 52.39 N ANISOU 389 NH1 ARG A 56 10215 4319 5372 168 2813 -25 N ATOM 390 NH2 ARG A 56 4.069 -20.168 26.721 1.00 57.49 N ANISOU 390 NH2 ARG A 56 11092 4988 5765 528 2680 210 N ATOM 391 N GLY A 57 4.612 -13.680 21.276 1.00 46.79 N ANISOU 391 N GLY A 57 8105 4731 4943 277 1675 61 N ATOM 392 CA GLY A 57 3.625 -12.681 20.918 1.00 43.94 C ANISOU 392 CA GLY A 57 7581 4422 4691 150 1633 -25 C ATOM 393 C GLY A 57 3.602 -11.476 21.845 1.00 46.24 C ANISOU 393 C GLY A 57 7830 4763 4977 135 1558 8 C ATOM 394 O GLY A 57 4.360 -11.404 22.815 1.00 43.51 O ANISOU 394 O GLY A 57 7579 4415 4540 219 1537 95 O ATOM 395 N PRO A 58 2.716 -10.515 21.554 1.00 43.53 N ANISOU 395 N PRO A 58 7346 4466 4728 36 1516 -68 N ATOM 396 CA PRO A 58 2.610 -9.299 22.361 1.00 43.71 C ANISOU 396 CA PRO A 58 7321 4532 4754 13 1447 -47 C ATOM 397 C PRO A 58 1.928 -9.567 23.713 1.00 37.38 C ANISOU 397 C PRO A 58 6659 3606 3938 -33 1577 -72 C ATOM 398 O PRO A 58 1.001 -10.369 23.811 1.00 38.61 O ANISOU 398 O PRO A 58 6885 3649 4135 -108 1724 -158 O ATOM 399 CB PRO A 58 1.706 -8.390 21.513 1.00 42.77 C ANISOU 399 CB PRO A 58 7027 4479 4744 -73 1385 -138 C ATOM 400 CG PRO A 58 1.272 -9.195 20.333 1.00 47.43 C ANISOU 400 CG PRO A 58 7576 5059 5385 -99 1427 -216 C ATOM 401 CD PRO A 58 1.615 -10.623 20.589 1.00 45.17 C ANISOU 401 CD PRO A 58 7451 4669 5041 -63 1552 -194 C ATOM 402 N ILE A 59 2.381 -8.898 24.759 1.00 34.24 N ANISOU 402 N ILE A 59 6305 3227 3479 4 1529 -5 N ATOM 403 CA ILE A 59 1.599 -8.886 25.996 1.00 34.17 C ANISOU 403 CA ILE A 59 6405 3112 3465 -56 1641 -40 C ATOM 404 C ILE A 59 1.466 -7.457 26.506 1.00 34.68 C ANISOU 404 C ILE A 59 6374 3251 3554 -86 1543 -36 C ATOM 405 O ILE A 59 2.419 -6.682 26.465 1.00 40.55 O ANISOU 405 O ILE A 59 7053 4100 4252 -22 1403 39 O ATOM 406 CB ILE A 59 2.177 -9.805 27.090 1.00 48.55 C ANISOU 406 CB ILE A 59 8456 4832 5160 29 1732 37 C ATOM 407 CG1 ILE A 59 3.474 -9.237 27.655 1.00 53.53 C ANISOU 407 CG1 ILE A 59 9097 5558 5682 152 1593 151 C ATOM 408 CG2 ILE A 59 2.393 -11.212 26.559 1.00 58.64 C ANISOU 408 CG2 ILE A 59 9844 6029 6406 73 1828 41 C ATOM 409 CD1 ILE A 59 3.990 -10.023 28.837 1.00 65.29 C ANISOU 409 CD1 ILE A 59 10818 6956 7033 254 1666 222 C ATOM 410 N LYS A 60 0.278 -7.104 26.981 1.00 34.07 N ANISOU 410 N LYS A 60 6282 3115 3547 -189 1622 -127 N ATOM 411 CA LYS A 60 0.022 -5.729 27.379 1.00 38.10 C ANISOU 411 CA LYS A 60 6697 3688 4091 -223 1536 -138 C ATOM 412 C LYS A 60 -0.140 -5.589 28.900 1.00 39.27 C ANISOU 412 C LYS A 60 6983 3759 4178 -233 1611 -120 C ATOM 413 O LYS A 60 -0.988 -6.258 29.506 1.00 39.27 O ANISOU 413 O LYS A 60 7091 3640 4191 -296 1773 -182 O ATOM 414 CB LYS A 60 -1.231 -5.221 26.668 1.00 46.09 C ANISOU 414 CB LYS A 60 7557 4719 5237 -320 1543 -265 C ATOM 415 CG LYS A 60 -1.233 -3.726 26.409 1.00 56.13 C ANISOU 415 CG LYS A 60 8687 6092 6548 -320 1398 -262 C ATOM 416 CD LYS A 60 -2.530 -3.251 25.745 1.00 63.05 C ANISOU 416 CD LYS A 60 9421 6987 7547 -393 1402 -396 C ATOM 417 CE LYS A 60 -3.706 -3.295 26.717 1.00 63.08 C ANISOU 417 CE LYS A 60 9461 6905 7602 -479 1536 -497 C ATOM 418 NZ LYS A 60 -4.832 -2.377 26.360 1.00 60.79 N ANISOU 418 NZ LYS A 60 9019 6660 7420 -527 1500 -616 N ATOM 419 N PHE A 61 0.659 -4.723 29.524 1.00 33.63 N ANISOU 419 N PHE A 61 6271 3112 3396 -178 1501 -42 N ATOM 420 CA PHE A 61 0.423 -4.415 30.941 1.00 33.41 C ANISOU 420 CA PHE A 61 6359 3023 3314 -193 1559 -36 C ATOM 421 C PHE A 61 -0.291 -3.076 31.051 1.00 36.00 C ANISOU 421 C PHE A 61 6560 3392 3726 -269 1507 -98 C ATOM 422 O PHE A 61 0.236 -2.046 30.640 1.00 35.31 O ANISOU 422 O PHE A 61 6356 3410 3650 -248 1363 -66 O ATOM 423 CB PHE A 61 1.729 -4.376 31.747 1.00 34.44 C ANISOU 423 CB PHE A 61 6593 3193 3301 -79 1480 77 C ATOM 424 CG PHE A 61 2.364 -5.730 31.954 1.00 37.58 C ANISOU 424 CG PHE A 61 7160 3527 3592 18 1547 139 C ATOM 425 CD1 PHE A 61 1.900 -6.586 32.936 1.00 40.55 C ANISOU 425 CD1 PHE A 61 7746 3758 3903 16 1708 134 C ATOM 426 CD2 PHE A 61 3.450 -6.125 31.184 1.00 38.65 C ANISOU 426 CD2 PHE A 61 7256 3744 3687 116 1454 202 C ATOM 427 CE1 PHE A 61 2.489 -7.824 33.141 1.00 48.74 C ANISOU 427 CE1 PHE A 61 8964 4723 4831 119 1774 195 C ATOM 428 CE2 PHE A 61 4.050 -7.365 31.376 1.00 44.57 C ANISOU 428 CE2 PHE A 61 8168 4433 4333 222 1512 258 C ATOM 429 CZ PHE A 61 3.566 -8.219 32.353 1.00 48.42 C ANISOU 429 CZ PHE A 61 8878 4767 4752 228 1671 257 C ATOM 430 N ASN A 62 -1.501 -3.103 31.593 1.00 35.41 N ANISOU 430 N ASN A 62 6513 3230 3709 -359 1635 -191 N ATOM 431 CA ASN A 62 -2.266 -1.892 31.826 1.00 34.52 C ANISOU 431 CA ASN A 62 6298 3145 3673 -422 1603 -258 C ATOM 432 C ASN A 62 -1.936 -1.419 33.234 1.00 40.76 C ANISOU 432 C ASN A 62 7210 3907 4371 -404 1610 -208 C ATOM 433 O ASN A 62 -2.483 -1.914 34.229 1.00 37.44 O ANISOU 433 O ASN A 62 6927 3381 3917 -441 1755 -238 O ATOM 434 CB ASN A 62 -3.758 -2.180 31.632 1.00 36.20 C ANISOU 434 CB ASN A 62 6457 3294 4004 -526 1737 -402 C ATOM 435 CG ASN A 62 -4.063 -2.708 30.219 1.00 35.90 C ANISOU 435 CG ASN A 62 6299 3292 4049 -539 1723 -461 C ATOM 436 OD1 ASN A 62 -3.461 -2.260 29.255 1.00 42.41 O ANISOU 436 OD1 ASN A 62 7020 4213 4881 -485 1579 -416 O ATOM 437 ND2 ASN A 62 -4.982 -3.651 30.106 1.00 34.31 N ANISOU 437 ND2 ASN A 62 6118 3012 3906 -614 1877 -566 N ATOM 438 N VAL A 63 -0.990 -0.490 33.304 1.00 40.46 N ANISOU 438 N VAL A 63 7127 3963 4283 -350 1459 -134 N ATOM 439 CA VAL A 63 -0.433 -0.039 34.567 1.00 36.22 C ANISOU 439 CA VAL A 63 6698 3424 3641 -317 1436 -80 C ATOM 440 C VAL A 63 -1.255 1.100 35.157 1.00 34.68 C ANISOU 440 C VAL A 63 6459 3216 3503 -388 1444 -147 C ATOM 441 O VAL A 63 -1.440 2.138 34.515 1.00 31.22 O ANISOU 441 O VAL A 63 5875 2843 3145 -414 1350 -176 O ATOM 442 CB VAL A 63 1.032 0.427 34.381 1.00 36.11 C ANISOU 442 CB VAL A 63 6646 3527 3547 -232 1270 15 C ATOM 443 CG1 VAL A 63 1.613 0.951 35.716 1.00 29.92 C ANISOU 443 CG1 VAL A 63 5962 2755 2651 -198 1234 56 C ATOM 444 CG2 VAL A 63 1.876 -0.709 33.838 1.00 33.71 C ANISOU 444 CG2 VAL A 63 6386 3241 3184 -147 1261 78 C ATOM 445 N TRP A 64 -1.739 0.906 36.383 1.00 37.05 N ANISOU 445 N TRP A 64 6897 3427 3755 -415 1561 -169 N ATOM 446 CA TRP A 64 -2.542 1.920 37.062 1.00 41.95 C ANISOU 446 CA TRP A 64 7491 4027 4422 -481 1586 -237 C ATOM 447 C TRP A 64 -1.672 2.860 37.880 1.00 41.14 C ANISOU 447 C TRP A 64 7427 3979 4225 -440 1477 -174 C ATOM 448 O TRP A 64 -1.079 2.457 38.874 1.00 37.09 O ANISOU 448 O TRP A 64 7068 3440 3583 -390 1499 -118 O ATOM 449 CB TRP A 64 -3.590 1.264 37.969 1.00 36.59 C ANISOU 449 CB TRP A 64 6940 3220 3744 -546 1786 -307 C ATOM 450 CG TRP A 64 -4.695 0.637 37.210 1.00 38.17 C ANISOU 450 CG TRP A 64 7062 3374 4067 -619 1901 -412 C ATOM 451 CD1 TRP A 64 -4.582 -0.178 36.113 1.00 40.63 C ANISOU 451 CD1 TRP A 64 7319 3702 4419 -607 1897 -412 C ATOM 452 CD2 TRP A 64 -6.091 0.755 37.481 1.00 36.92 C ANISOU 452 CD2 TRP A 64 6864 3155 4010 -720 2038 -546 C ATOM 453 NE1 TRP A 64 -5.829 -0.569 35.688 1.00 40.76 N ANISOU 453 NE1 TRP A 64 7260 3672 4554 -697 2020 -543 N ATOM 454 CE2 TRP A 64 -6.772 -0.014 36.516 1.00 41.51 C ANISOU 454 CE2 TRP A 64 7357 3723 4690 -768 2109 -630 C ATOM 455 CE3 TRP A 64 -6.833 1.415 38.467 1.00 46.31 C ANISOU 455 CE3 TRP A 64 8080 4302 5214 -776 2113 -612 C ATOM 456 CZ2 TRP A 64 -8.163 -0.123 36.494 1.00 49.56 C ANISOU 456 CZ2 TRP A 64 8301 4701 5829 -871 2247 -787 C ATOM 457 CZ3 TRP A 64 -8.215 1.302 38.442 1.00 49.88 C ANISOU 457 CZ3 TRP A 64 8461 4708 5785 -875 2255 -762 C ATOM 458 CH2 TRP A 64 -8.864 0.542 37.462 1.00 50.48 C ANISOU 458 CH2 TRP A 64 8436 4782 5963 -923 2319 -851 C ATOM 459 N ASP A 65 -1.600 4.113 37.449 1.00 39.57 N ANISOU 459 N ASP A 65 7094 3855 4088 -458 1359 -188 N ATOM 460 CA ASP A 65 -0.811 5.113 38.140 1.00 38.17 C ANISOU 460 CA ASP A 65 6934 3733 3836 -438 1255 -147 C ATOM 461 C ASP A 65 -1.726 6.086 38.867 1.00 37.40 C ANISOU 461 C ASP A 65 6837 3590 3785 -502 1300 -220 C ATOM 462 O ASP A 65 -2.666 6.614 38.278 1.00 38.89 O ANISOU 462 O ASP A 65 6917 3766 4093 -550 1316 -294 O ATOM 463 CB ASP A 65 0.062 5.891 37.156 1.00 35.30 C ANISOU 463 CB ASP A 65 6437 3479 3497 -417 1096 -106 C ATOM 464 CG ASP A 65 1.087 6.757 37.855 1.00 43.56 C ANISOU 464 CG ASP A 65 7504 4592 4454 -400 992 -65 C ATOM 465 OD1 ASP A 65 1.653 6.282 38.865 1.00 43.76 O ANISOU 465 OD1 ASP A 65 7653 4616 4360 -354 1005 -29 O ATOM 466 OD2 ASP A 65 1.323 7.909 37.412 1.00 36.44 O ANISOU 466 OD2 ASP A 65 6506 3742 3597 -430 900 -72 O ATOM 467 N THR A 66 -1.449 6.315 40.145 1.00 35.04 N ANISOU 467 N THR A 66 6661 3269 3384 -495 1318 -204 N ATOM 468 CA THR A 66 -2.236 7.253 40.941 1.00 36.02 C ANISOU 468 CA THR A 66 6799 3349 3538 -552 1363 -272 C ATOM 469 C THR A 66 -2.073 8.683 40.450 1.00 38.02 C ANISOU 469 C THR A 66 6925 3666 3855 -572 1238 -286 C ATOM 470 O THR A 66 -1.218 8.965 39.608 1.00 35.14 O ANISOU 470 O THR A 66 6478 3382 3493 -545 1117 -236 O ATOM 471 CB THR A 66 -1.785 7.267 42.400 1.00 45.37 C ANISOU 471 CB THR A 66 8148 4509 4580 -530 1386 -243 C ATOM 472 OG1 THR A 66 -0.517 7.931 42.492 1.00 41.28 O ANISOU 472 OG1 THR A 66 7608 4091 3984 -488 1230 -184 O ATOM 473 CG2 THR A 66 -1.687 5.848 42.949 1.00 40.21 C ANISOU 473 CG2 THR A 66 7662 3791 3827 -486 1497 -205 C ATOM 474 N ALA A 67 -2.887 9.577 41.003 1.00 37.88 N ANISOU 474 N ALA A 67 6904 3605 3882 -620 1278 -356 N ATOM 475 CA ALA A 67 -2.736 11.014 40.789 1.00 39.86 C ANISOU 475 CA ALA A 67 7078 3894 4174 -637 1175 -370 C ATOM 476 C ALA A 67 -2.295 11.720 42.072 1.00 47.74 C ANISOU 476 C ALA A 67 8176 4888 5075 -651 1159 -365 C ATOM 477 O ALA A 67 -2.651 12.872 42.321 1.00 49.22 O ANISOU 477 O ALA A 67 8342 5059 5300 -684 1140 -410 O ATOM 478 CB ALA A 67 -4.039 11.610 40.271 1.00 41.75 C ANISOU 478 CB ALA A 67 7221 4093 4551 -668 1218 -462 C ATOM 479 N GLY A 68 -1.531 11.012 42.894 1.00 47.88 N ANISOU 479 N GLY A 68 8311 4919 4961 -616 1165 -313 N ATOM 480 CA GLY A 68 -0.935 11.595 44.081 1.00 40.13 C ANISOU 480 CA GLY A 68 7425 3954 3867 -616 1129 -305 C ATOM 481 C GLY A 68 -1.639 11.301 45.394 1.00 38.73 C ANISOU 481 C GLY A 68 7398 3691 3628 -629 1259 -344 C ATOM 482 O GLY A 68 -1.104 11.609 46.449 1.00 44.23 O ANISOU 482 O GLY A 68 8195 4403 4208 -616 1232 -334 O ATOM 483 N GLN A 69 -2.832 10.715 45.340 1.00 40.64 N ANISOU 483 N GLN A 69 7653 3845 3943 -658 1403 -395 N ATOM 484 CA GLN A 69 -3.639 10.493 46.553 1.00 49.68 C ANISOU 484 CA GLN A 69 8937 4896 5042 -687 1553 -445 C ATOM 485 C GLN A 69 -2.939 9.669 47.643 1.00 51.79 C ANISOU 485 C GLN A 69 9403 5148 5129 -631 1584 -383 C ATOM 486 O GLN A 69 -3.239 9.821 48.836 1.00 48.65 O ANISOU 486 O GLN A 69 9141 4694 4649 -645 1663 -410 O ATOM 487 CB GLN A 69 -4.987 9.849 46.205 1.00 46.30 C ANISOU 487 CB GLN A 69 8478 4386 4730 -736 1715 -520 C ATOM 488 CG GLN A 69 -5.688 10.493 45.002 1.00 53.31 C ANISOU 488 CG GLN A 69 9165 5299 5790 -765 1674 -584 C ATOM 489 CD GLN A 69 -5.284 9.851 43.673 1.00 46.80 C ANISOU 489 CD GLN A 69 8239 4529 5015 -732 1605 -538 C ATOM 490 OE1 GLN A 69 -4.171 9.345 43.529 1.00 43.72 O ANISOU 490 OE1 GLN A 69 7892 4186 4534 -680 1528 -446 O ATOM 491 NE2 GLN A 69 -6.198 9.858 42.706 1.00 44.27 N ANISOU 491 NE2 GLN A 69 7779 4205 4835 -755 1632 -610 N ATOM 492 N GLU A 70 -2.012 8.804 47.234 1.00 43.66 N ANISOU 492 N GLU A 70 8395 4167 4029 -559 1521 -303 N ATOM 493 CA GLU A 70 -1.278 7.956 48.172 1.00 45.68 C ANISOU 493 CA GLU A 70 8842 4414 4101 -477 1535 -238 C ATOM 494 C GLU A 70 -0.539 8.751 49.250 1.00 46.04 C ANISOU 494 C GLU A 70 8963 4516 4016 -448 1441 -232 C ATOM 495 O GLU A 70 -0.081 8.182 50.243 1.00 44.13 O ANISOU 495 O GLU A 70 8902 4259 3606 -375 1459 -194 O ATOM 496 CB GLU A 70 -0.309 7.013 47.440 1.00 47.00 C ANISOU 496 CB GLU A 70 8995 4643 4220 -389 1457 -157 C ATOM 497 CG GLU A 70 0.957 7.667 46.886 1.00 44.02 C ANISOU 497 CG GLU A 70 8484 4414 3829 -348 1253 -119 C ATOM 498 CD GLU A 70 0.756 8.265 45.503 1.00 40.07 C ANISOU 498 CD GLU A 70 7771 3957 3498 -409 1194 -142 C ATOM 499 OE1 GLU A 70 -0.407 8.336 45.049 1.00 40.28 O ANISOU 499 OE1 GLU A 70 7742 3908 3654 -477 1293 -197 O ATOM 500 OE2 GLU A 70 1.760 8.667 44.870 1.00 40.38 O ANISOU 500 OE2 GLU A 70 7699 4107 3537 -385 1049 -110 O ATOM 501 N LYS A 71 -0.423 10.062 49.073 1.00 39.64 N ANISOU 501 N LYS A 71 8024 3764 3272 -500 1342 -272 N ATOM 502 CA LYS A 71 0.202 10.878 50.108 1.00 42.20 C ANISOU 502 CA LYS A 71 8413 4139 3481 -489 1261 -285 C ATOM 503 C LYS A 71 -0.714 11.059 51.318 1.00 44.88 C ANISOU 503 C LYS A 71 8903 4374 3776 -527 1400 -338 C ATOM 504 O LYS A 71 -0.260 11.449 52.400 1.00 51.21 O ANISOU 504 O LYS A 71 9814 5199 4445 -502 1362 -345 O ATOM 505 CB LYS A 71 0.598 12.251 49.547 1.00 57.37 C ANISOU 505 CB LYS A 71 10166 6142 5490 -546 1129 -317 C ATOM 506 CG LYS A 71 1.397 12.179 48.255 1.00 62.56 C ANISOU 506 CG LYS A 71 10666 6893 6209 -528 1011 -274 C ATOM 507 CD LYS A 71 1.965 13.533 47.865 1.00 68.81 C ANISOU 507 CD LYS A 71 11330 7762 7054 -585 888 -303 C ATOM 508 CE LYS A 71 2.241 13.583 46.372 1.00 67.36 C ANISOU 508 CE LYS A 71 10984 7624 6983 -597 825 -276 C ATOM 509 NZ LYS A 71 0.961 13.646 45.623 1.00 68.10 N ANISOU 509 NZ LYS A 71 11023 7625 7227 -639 919 -304 N ATOM 510 N PHE A 72 -2.007 10.797 51.143 1.00 46.29 N ANISOU 510 N PHE A 72 9081 4444 4064 -589 1562 -386 N ATOM 511 CA PHE A 72 -2.984 11.200 52.164 1.00 45.95 C ANISOU 511 CA PHE A 72 9140 4307 4013 -646 1697 -458 C ATOM 512 C PHE A 72 -3.712 10.023 52.782 1.00 53.43 C ANISOU 512 C PHE A 72 10265 5135 4901 -644 1896 -458 C ATOM 513 O PHE A 72 -4.562 10.198 53.658 1.00 53.34 O ANISOU 513 O PHE A 72 10355 5037 4876 -695 2037 -519 O ATOM 514 CB PHE A 72 -3.992 12.206 51.596 1.00 45.98 C ANISOU 514 CB PHE A 72 8983 4287 4203 -735 1727 -546 C ATOM 515 CG PHE A 72 -3.355 13.325 50.827 1.00 45.39 C ANISOU 515 CG PHE A 72 8744 4306 4196 -742 1552 -542 C ATOM 516 CD1 PHE A 72 -2.759 14.382 51.495 1.00 51.52 C ANISOU 516 CD1 PHE A 72 9545 5127 4903 -751 1458 -556 C ATOM 517 CD2 PHE A 72 -3.340 13.311 49.435 1.00 41.57 C ANISOU 517 CD2 PHE A 72 8092 3862 3840 -744 1489 -527 C ATOM 518 CE1 PHE A 72 -2.163 15.411 50.794 1.00 57.47 C ANISOU 518 CE1 PHE A 72 10164 5955 5718 -771 1315 -556 C ATOM 519 CE2 PHE A 72 -2.750 14.329 48.725 1.00 48.76 C ANISOU 519 CE2 PHE A 72 8875 4846 4805 -754 1345 -521 C ATOM 520 CZ PHE A 72 -2.159 15.389 49.405 1.00 55.79 C ANISOU 520 CZ PHE A 72 9796 5772 5631 -772 1263 -536 C ATOM 521 N GLY A 73 -3.376 8.823 52.333 1.00 51.66 N ANISOU 521 N GLY A 73 10088 4901 4640 -589 1918 -394 N ATOM 522 CA GLY A 73 -3.916 7.628 52.947 1.00 51.91 C ANISOU 522 CA GLY A 73 10322 4809 4591 -582 2111 -384 C ATOM 523 C GLY A 73 -3.812 6.418 52.054 1.00 58.66 C ANISOU 523 C GLY A 73 11167 5644 5478 -551 2148 -335 C ATOM 524 O GLY A 73 -3.288 6.506 50.929 1.00 55.85 O ANISOU 524 O GLY A 73 10638 5379 5204 -530 2014 -307 O ATOM 525 N GLY A 74 -4.294 5.282 52.560 1.00 48.56 N ANISOU 525 N GLY A 74 10087 4238 4127 -551 2338 -326 N ATOM 526 CA GLY A 74 -4.435 4.093 51.741 1.00 54.15 C ANISOU 526 CA GLY A 74 10798 4897 4881 -547 2418 -301 C ATOM 527 C GLY A 74 -5.320 4.333 50.523 1.00 58.07 C ANISOU 527 C GLY A 74 11048 5408 5609 -651 2446 -387 C ATOM 528 O GLY A 74 -6.207 5.192 50.543 1.00 55.62 O ANISOU 528 O GLY A 74 10620 5094 5419 -741 2486 -484 O ATOM 529 N LEU A 75 -5.085 3.569 49.455 1.00 54.43 N ANISOU 529 N LEU A 75 10510 4965 5204 -629 2421 -355 N ATOM 530 CA LEU A 75 -5.876 3.698 48.237 1.00 51.79 C ANISOU 530 CA LEU A 75 9949 4652 5076 -712 2436 -436 C ATOM 531 C LEU A 75 -7.171 2.895 48.333 1.00 55.87 C ANISOU 531 C LEU A 75 10519 5039 5670 -819 2687 -533 C ATOM 532 O LEU A 75 -7.209 1.837 48.944 1.00 58.69 O ANISOU 532 O LEU A 75 11097 5283 5919 -812 2842 -503 O ATOM 533 CB LEU A 75 -5.068 3.230 47.017 1.00 54.25 C ANISOU 533 CB LEU A 75 10152 5044 5416 -647 2303 -368 C ATOM 534 CG LEU A 75 -3.702 3.874 46.788 1.00 50.56 C ANISOU 534 CG LEU A 75 9620 4712 4877 -548 2065 -278 C ATOM 535 CD1 LEU A 75 -2.973 3.209 45.615 1.00 50.12 C ANISOU 535 CD1 LEU A 75 9480 4718 4843 -487 1971 -216 C ATOM 536 CD2 LEU A 75 -3.866 5.364 46.555 1.00 50.79 C ANISOU 536 CD2 LEU A 75 9468 4824 5007 -593 1948 -330 C ATOM 537 N ARG A 76 -8.221 3.399 47.697 1.00 56.23 N ANISOU 537 N ARG A 76 10362 5103 5900 -914 2725 -654 N ATOM 538 CA ARG A 76 -9.528 2.747 47.713 1.00 55.29 C ANISOU 538 CA ARG A 76 10245 4882 5880 -1032 2960 -778 C ATOM 539 C ARG A 76 -9.549 1.383 47.013 1.00 50.59 C ANISOU 539 C ARG A 76 9691 4232 5300 -1046 3056 -768 C ATOM 540 O ARG A 76 -8.667 1.065 46.208 1.00 48.71 O ANISOU 540 O ARG A 76 9411 4057 5040 -965 2915 -680 O ATOM 541 CB ARG A 76 -10.572 3.688 47.107 1.00 58.69 C ANISOU 541 CB ARG A 76 10419 5375 6506 -1108 2943 -919 C ATOM 542 CG ARG A 76 -10.838 4.918 47.977 1.00 67.38 C ANISOU 542 CG ARG A 76 11514 6490 7597 -1117 2917 -957 C ATOM 543 CD ARG A 76 -11.587 5.978 47.209 1.00 74.90 C ANISOU 543 CD ARG A 76 12204 7526 8726 -1145 2835 -1067 C ATOM 544 NE ARG A 76 -12.839 5.469 46.658 1.00 84.79 N ANISOU 544 NE ARG A 76 13328 8755 10133 -1237 2986 -1217 N ATOM 545 CZ ARG A 76 -13.319 5.811 45.467 1.00 87.76 C ANISOU 545 CZ ARG A 76 13464 9216 10663 -1236 2898 -1296 C ATOM 546 NH1 ARG A 76 -12.641 6.650 44.691 1.00 82.58 N ANISOU 546 NH1 ARG A 76 12691 8661 10024 -1149 2671 -1227 N ATOM 547 NH2 ARG A 76 -14.470 5.303 45.044 1.00 90.21 N ANISOU 547 NH2 ARG A 76 13656 9513 11108 -1322 3041 -1450 N ATOM 548 N ASP A 77 -10.559 0.579 47.334 1.00 56.23 N ANISOU 548 N ASP A 77 10488 4824 6052 -1155 3306 -866 N ATOM 549 CA ASP A 77 -10.662 -0.783 46.810 1.00 56.14 C ANISOU 549 CA ASP A 77 10550 4732 6047 -1187 3437 -869 C ATOM 550 C ASP A 77 -10.708 -0.841 45.284 1.00 52.98 C ANISOU 550 C ASP A 77 9900 4433 5796 -1189 3319 -908 C ATOM 551 O ASP A 77 -10.151 -1.753 44.681 1.00 52.73 O ANISOU 551 O ASP A 77 9920 4385 5729 -1146 3305 -842 O ATOM 552 CB ASP A 77 -11.897 -1.495 47.375 1.00 61.91 C ANISOU 552 CB ASP A 77 11382 5318 6821 -1336 3744 -1001 C ATOM 553 CG ASP A 77 -11.820 -1.715 48.880 1.00 68.99 C ANISOU 553 CG ASP A 77 12584 6085 7543 -1333 3898 -951 C ATOM 554 OD1 ASP A 77 -10.708 -1.673 49.445 1.00 66.46 O ANISOU 554 OD1 ASP A 77 12440 5769 7044 -1199 3781 -799 O ATOM 555 OD2 ASP A 77 -12.882 -1.940 49.498 1.00 79.71 O ANISOU 555 OD2 ASP A 77 14006 7338 8940 -1464 4141 -1071 O ATOM 556 N GLY A 78 -11.389 0.124 44.673 1.00 48.90 N ANISOU 556 N GLY A 78 9123 4018 5441 -1231 3237 -1016 N ATOM 557 CA GLY A 78 -11.596 0.138 43.238 1.00 52.21 C ANISOU 557 CA GLY A 78 9301 4532 6003 -1235 3133 -1073 C ATOM 558 C GLY A 78 -10.308 0.315 42.463 1.00 57.94 C ANISOU 558 C GLY A 78 9987 5356 6673 -1107 2897 -929 C ATOM 559 O GLY A 78 -10.241 0.011 41.268 1.00 58.58 O ANISOU 559 O GLY A 78 9929 5496 6832 -1095 2824 -943 O ATOM 560 N TYR A 79 -9.283 0.819 43.144 1.00 61.85 N ANISOU 560 N TYR A 79 10598 5873 7030 -1014 2779 -799 N ATOM 561 CA TYR A 79 -7.968 0.965 42.539 1.00 56.38 C ANISOU 561 CA TYR A 79 9880 5273 6269 -896 2567 -664 C ATOM 562 C TYR A 79 -7.335 -0.414 42.417 1.00 56.26 C ANISOU 562 C TYR A 79 10027 5193 6156 -850 2630 -582 C ATOM 563 O TYR A 79 -6.773 -0.784 41.378 1.00 47.85 O ANISOU 563 O TYR A 79 8881 4188 5114 -800 2530 -538 O ATOM 564 CB TYR A 79 -7.069 1.877 43.384 1.00 50.45 C ANISOU 564 CB TYR A 79 9203 4568 5396 -818 2433 -570 C ATOM 565 CG TYR A 79 -5.648 1.876 42.887 1.00 47.27 C ANISOU 565 CG TYR A 79 8794 4258 4909 -702 2240 -439 C ATOM 566 CD1 TYR A 79 -5.207 2.839 41.995 1.00 38.03 C ANISOU 566 CD1 TYR A 79 7429 3212 3808 -674 2048 -424 C ATOM 567 CD2 TYR A 79 -4.757 0.882 43.273 1.00 52.15 C ANISOU 567 CD2 TYR A 79 9601 4837 5377 -619 2257 -336 C ATOM 568 CE1 TYR A 79 -3.909 2.826 41.511 1.00 45.99 C ANISOU 568 CE1 TYR A 79 8420 4308 4745 -580 1885 -317 C ATOM 569 CE2 TYR A 79 -3.460 0.860 42.794 1.00 52.96 C ANISOU 569 CE2 TYR A 79 9678 5036 5407 -510 2081 -231 C ATOM 570 CZ TYR A 79 -3.044 1.829 41.914 1.00 53.28 C ANISOU 570 CZ TYR A 79 9511 5204 5527 -500 1900 -226 C ATOM 571 OH TYR A 79 -1.751 1.809 41.434 1.00 56.13 O ANISOU 571 OH TYR A 79 9840 5666 5822 -403 1739 -132 O ATOM 572 N TYR A 80 -7.433 -1.179 43.495 1.00 59.88 N ANISOU 572 N TYR A 80 10730 5521 6499 -862 2803 -562 N ATOM 573 CA TYR A 80 -6.823 -2.493 43.542 1.00 57.88 C ANISOU 573 CA TYR A 80 10677 5185 6130 -802 2877 -477 C ATOM 574 C TYR A 80 -7.620 -3.533 42.774 1.00 58.36 C ANISOU 574 C TYR A 80 10708 5170 6297 -897 3040 -568 C ATOM 575 O TYR A 80 -7.067 -4.550 42.357 1.00 63.95 O ANISOU 575 O TYR A 80 11514 5838 6948 -843 3059 -503 O ATOM 576 CB TYR A 80 -6.671 -2.960 44.990 1.00 58.04 C ANISOU 576 CB TYR A 80 11001 5077 5973 -773 3015 -421 C ATOM 577 CG TYR A 80 -5.606 -2.226 45.764 1.00 57.43 C ANISOU 577 CG TYR A 80 10998 5074 5747 -649 2844 -312 C ATOM 578 CD1 TYR A 80 -4.262 -2.474 45.536 1.00 54.90 C ANISOU 578 CD1 TYR A 80 10721 4827 5311 -499 2675 -186 C ATOM 579 CD2 TYR A 80 -5.944 -1.290 46.725 1.00 48.65 C ANISOU 579 CD2 TYR A 80 9908 3965 4613 -682 2852 -346 C ATOM 580 CE1 TYR A 80 -3.284 -1.813 46.242 1.00 48.96 C ANISOU 580 CE1 TYR A 80 10021 4157 4426 -390 2517 -105 C ATOM 581 CE2 TYR A 80 -4.976 -0.624 47.435 1.00 53.43 C ANISOU 581 CE2 TYR A 80 10576 4642 5081 -575 2696 -260 C ATOM 582 CZ TYR A 80 -3.648 -0.888 47.193 1.00 53.76 C ANISOU 582 CZ TYR A 80 10650 4764 5011 -432 2527 -143 C ATOM 583 OH TYR A 80 -2.678 -0.216 47.899 1.00 56.51 O ANISOU 583 OH TYR A 80 11045 5200 5227 -330 2368 -76 O ATOM 584 N ILE A 81 -8.913 -3.287 42.592 1.00 56.62 N ANISOU 584 N ILE A 81 10350 4934 6230 -1036 3159 -726 N ATOM 585 CA ILE A 81 -9.818 -4.363 42.180 1.00 63.12 C ANISOU 585 CA ILE A 81 11184 5658 7139 -1154 3372 -839 C ATOM 586 C ILE A 81 -9.438 -5.021 40.847 1.00 62.93 C ANISOU 586 C ILE A 81 11057 5683 7169 -1122 3293 -824 C ATOM 587 O ILE A 81 -9.281 -4.354 39.822 1.00 52.65 O ANISOU 587 O ILE A 81 9521 4522 5962 -1088 3105 -836 O ATOM 588 CB ILE A 81 -11.316 -3.936 42.220 1.00 62.64 C ANISOU 588 CB ILE A 81 10963 5594 7245 -1311 3510 -1038 C ATOM 589 CG1 ILE A 81 -12.234 -5.145 42.023 1.00 69.72 C ANISOU 589 CG1 ILE A 81 11910 6370 8210 -1451 3768 -1166 C ATOM 590 CG2 ILE A 81 -11.614 -2.867 41.195 1.00 59.76 C ANISOU 590 CG2 ILE A 81 10278 5395 7032 -1302 3316 -1111 C ATOM 591 CD1 ILE A 81 -12.024 -6.251 43.031 1.00 70.78 C ANISOU 591 CD1 ILE A 81 12391 6313 8189 -1465 3989 -1099 C ATOM 592 N GLN A 82 -9.259 -6.337 40.899 1.00 64.41 N ANISOU 592 N GLN A 82 11444 5744 7285 -1127 3444 -791 N ATOM 593 CA GLN A 82 -8.968 -7.146 39.718 1.00 58.72 C ANISOU 593 CA GLN A 82 10662 5042 6607 -1108 3412 -786 C ATOM 594 C GLN A 82 -7.543 -6.988 39.197 1.00 53.61 C ANISOU 594 C GLN A 82 10002 4498 5869 -936 3172 -624 C ATOM 595 O GLN A 82 -7.252 -7.350 38.057 1.00 54.67 O ANISOU 595 O GLN A 82 10024 4690 6057 -911 3092 -622 O ATOM 596 CB GLN A 82 -9.981 -6.878 38.604 1.00 64.53 C ANISOU 596 CB GLN A 82 11108 5863 7548 -1221 3404 -957 C ATOM 597 CG GLN A 82 -11.416 -6.982 39.079 1.00 76.18 C ANISOU 597 CG GLN A 82 12558 7260 9128 -1395 3635 -1142 C ATOM 598 CD GLN A 82 -12.264 -7.867 38.195 1.00 84.77 C ANISOU 598 CD GLN A 82 13546 8318 10345 -1521 3776 -1300 C ATOM 599 OE1 GLN A 82 -11.787 -8.413 37.198 1.00 84.11 O ANISOU 599 OE1 GLN A 82 13418 8268 10272 -1476 3698 -1267 O ATOM 600 NE2 GLN A 82 -13.529 -8.022 38.561 1.00 87.17 N ANISOU 600 NE2 GLN A 82 13810 8560 10749 -1686 3990 -1482 N ATOM 601 N ALA A 83 -6.655 -6.456 40.032 1.00 47.00 N ANISOU 601 N ALA A 83 9275 3688 4893 -822 3062 -499 N ATOM 602 CA ALA A 83 -5.238 -6.448 39.696 1.00 47.03 C ANISOU 602 CA ALA A 83 9297 3781 4793 -658 2861 -351 C ATOM 603 C ALA A 83 -4.822 -7.893 39.461 1.00 51.14 C ANISOU 603 C ALA A 83 10004 4194 5233 -607 2966 -296 C ATOM 604 O ALA A 83 -5.327 -8.801 40.121 1.00 49.44 O ANISOU 604 O ALA A 83 10010 3811 4964 -660 3190 -321 O ATOM 605 CB ALA A 83 -4.427 -5.845 40.824 1.00 47.18 C ANISOU 605 CB ALA A 83 9444 3825 4659 -552 2767 -244 C ATOM 606 N GLN A 84 -3.918 -8.126 38.515 1.00 49.55 N ANISOU 606 N GLN A 84 9725 4081 5022 -508 2816 -226 N ATOM 607 CA GLN A 84 -3.431 -9.486 38.314 1.00 52.93 C ANISOU 607 CA GLN A 84 10342 4407 5362 -439 2906 -166 C ATOM 608 C GLN A 84 -1.972 -9.591 38.717 1.00 55.06 C ANISOU 608 C GLN A 84 10742 4726 5454 -239 2758 -8 C ATOM 609 O GLN A 84 -1.437 -10.675 38.933 1.00 54.08 O ANISOU 609 O GLN A 84 10840 4503 5206 -140 2831 66 O ATOM 610 CB GLN A 84 -3.673 -9.928 36.875 1.00 53.58 C ANISOU 610 CB GLN A 84 10253 4529 5577 -492 2894 -232 C ATOM 611 CG GLN A 84 -5.165 -9.999 36.578 1.00 64.43 C ANISOU 611 CG GLN A 84 11522 5845 7113 -687 3063 -408 C ATOM 612 CD GLN A 84 -5.499 -9.912 35.107 1.00 61.63 C ANISOU 612 CD GLN A 84 10909 5593 6913 -741 2983 -496 C ATOM 613 OE1 GLN A 84 -5.368 -8.857 34.485 1.00 59.45 O ANISOU 613 OE1 GLN A 84 10403 5475 6710 -721 2792 -503 O ATOM 614 NE2 GLN A 84 -5.971 -11.020 34.549 1.00 55.18 N ANISOU 614 NE2 GLN A 84 10139 4682 6143 -815 3138 -571 N ATOM 615 N CYS A 85 -1.345 -8.434 38.857 1.00 49.32 N ANISOU 615 N CYS A 85 9876 4151 4711 -177 2553 36 N ATOM 616 CA CYS A 85 0.043 -8.371 39.255 1.00 46.52 C ANISOU 616 CA CYS A 85 9602 3876 4199 6 2393 164 C ATOM 617 C CYS A 85 0.297 -6.974 39.775 1.00 44.89 C ANISOU 617 C CYS A 85 9272 3796 3989 9 2238 169 C ATOM 618 O CYS A 85 -0.542 -6.085 39.624 1.00 42.69 O ANISOU 618 O CYS A 85 8832 3547 3840 -119 2242 83 O ATOM 619 CB CYS A 85 0.952 -8.679 38.063 1.00 38.61 C ANISOU 619 CB CYS A 85 8473 2980 3216 96 2253 211 C ATOM 620 SG CYS A 85 0.758 -7.546 36.657 1.00 43.67 S ANISOU 620 SG CYS A 85 8743 3795 4054 1 2091 143 S ATOM 621 N ALA A 86 1.458 -6.766 40.375 1.00 45.92 N ANISOU 621 N ALA A 86 9472 4005 3971 160 2099 263 N ATOM 622 CA ALA A 86 1.765 -5.456 40.915 1.00 46.30 C ANISOU 622 CA ALA A 86 9415 4171 4007 160 1955 263 C ATOM 623 C ALA A 86 3.252 -5.221 40.982 1.00 39.64 C ANISOU 623 C ALA A 86 8541 3474 3046 322 1751 348 C ATOM 624 O ALA A 86 4.049 -6.152 40.992 1.00 45.63 O ANISOU 624 O ALA A 86 9426 4223 3688 463 1736 418 O ATOM 625 CB ALA A 86 1.147 -5.306 42.333 1.00 43.95 C ANISOU 625 CB ALA A 86 9311 3762 3625 126 2081 246 C ATOM 626 N ILE A 87 3.601 -3.952 41.061 1.00 40.83 N ANISOU 626 N ILE A 87 8526 3761 3228 298 1598 333 N ATOM 627 CA ILE A 87 4.949 -3.516 41.348 1.00 45.55 C ANISOU 627 CA ILE A 87 9084 4509 3714 428 1408 388 C ATOM 628 C ILE A 87 4.835 -2.630 42.574 1.00 46.30 C ANISOU 628 C ILE A 87 9238 4614 3740 409 1385 370 C ATOM 629 O ILE A 87 3.998 -1.732 42.612 1.00 46.22 O ANISOU 629 O ILE A 87 9135 4589 3840 272 1417 305 O ATOM 630 CB ILE A 87 5.521 -2.669 40.183 1.00 47.86 C ANISOU 630 CB ILE A 87 9096 4967 4123 392 1243 373 C ATOM 631 CG1 ILE A 87 5.934 -3.571 39.014 1.00 40.56 C ANISOU 631 CG1 ILE A 87 8120 4060 3233 446 1236 402 C ATOM 632 CG2 ILE A 87 6.690 -1.804 40.660 1.00 41.44 C ANISOU 632 CG2 ILE A 87 8207 4316 3223 467 1058 392 C ATOM 633 CD1 ILE A 87 6.317 -2.781 37.741 1.00 37.94 C ANISOU 633 CD1 ILE A 87 7523 3867 3028 390 1107 381 C ATOM 634 N ILE A 88 5.655 -2.898 43.583 1.00 38.39 N ANISOU 634 N ILE A 88 8398 3638 2552 554 1329 422 N ATOM 635 CA ILE A 88 5.746 -2.021 44.747 1.00 38.27 C ANISOU 635 CA ILE A 88 8430 3659 2452 554 1278 404 C ATOM 636 C ILE A 88 7.039 -1.228 44.695 1.00 42.32 C ANISOU 636 C ILE A 88 8784 4378 2919 629 1052 410 C ATOM 637 O ILE A 88 8.125 -1.793 44.589 1.00 46.34 O ANISOU 637 O ILE A 88 9307 4976 3325 782 950 456 O ATOM 638 CB ILE A 88 5.714 -2.817 46.051 1.00 41.72 C ANISOU 638 CB ILE A 88 9180 3981 2693 666 1376 447 C ATOM 639 CG1 ILE A 88 4.484 -3.724 46.081 1.00 41.60 C ANISOU 639 CG1 ILE A 88 9338 3751 2718 585 1623 437 C ATOM 640 CG2 ILE A 88 5.765 -1.872 47.271 1.00 39.95 C ANISOU 640 CG2 ILE A 88 9006 3795 2378 661 1323 422 C ATOM 641 CD1 ILE A 88 4.210 -4.346 47.496 1.00 48.53 C ANISOU 641 CD1 ILE A 88 10552 4481 3407 658 1762 470 C ATOM 642 N MET A 89 6.924 0.087 44.785 1.00 37.63 N ANISOU 642 N MET A 89 8038 3860 2401 521 978 355 N ATOM 643 CA MET A 89 8.091 0.935 44.600 1.00 34.93 C ANISOU 643 CA MET A 89 7516 3712 2044 554 779 342 C ATOM 644 C MET A 89 8.465 1.695 45.847 1.00 38.49 C ANISOU 644 C MET A 89 8025 4224 2375 581 702 315 C ATOM 645 O MET A 89 7.605 2.166 46.590 1.00 42.60 O ANISOU 645 O MET A 89 8632 4651 2901 499 789 283 O ATOM 646 CB MET A 89 7.875 1.930 43.452 1.00 38.30 C ANISOU 646 CB MET A 89 7691 4200 2662 406 733 297 C ATOM 647 CG MET A 89 9.176 2.441 42.865 1.00 39.40 C ANISOU 647 CG MET A 89 7640 4529 2801 443 554 292 C ATOM 648 SD MET A 89 8.965 3.463 41.394 1.00 49.43 S ANISOU 648 SD MET A 89 8652 5850 4281 284 518 254 S ATOM 649 CE MET A 89 8.531 2.201 40.191 1.00 48.18 C ANISOU 649 CE MET A 89 8500 5609 4198 310 614 297 C ATOM 650 N PHE A 90 9.765 1.799 46.072 1.00 38.97 N ANISOU 650 N PHE A 90 8032 4450 2326 700 536 318 N ATOM 651 CA PHE A 90 10.283 2.722 47.057 1.00 39.02 C ANISOU 651 CA PHE A 90 8027 4558 2240 708 427 271 C ATOM 652 C PHE A 90 11.481 3.459 46.475 1.00 38.82 C ANISOU 652 C PHE A 90 7758 4742 2248 704 245 229 C ATOM 653 O PHE A 90 11.875 3.237 45.330 1.00 43.30 O ANISOU 653 O PHE A 90 8178 5367 2907 698 212 243 O ATOM 654 CB PHE A 90 10.633 2.014 48.377 1.00 39.26 C ANISOU 654 CB PHE A 90 8304 4571 2042 884 420 303 C ATOM 655 CG PHE A 90 11.772 1.048 48.264 1.00 44.69 C ANISOU 655 CG PHE A 90 9022 5359 2599 1091 319 347 C ATOM 656 CD1 PHE A 90 11.556 -0.252 47.835 1.00 46.31 C ANISOU 656 CD1 PHE A 90 9361 5453 2784 1182 420 419 C ATOM 657 CD2 PHE A 90 13.060 1.439 48.582 1.00 50.47 C ANISOU 657 CD2 PHE A 90 9646 6301 3231 1196 124 307 C ATOM 658 CE1 PHE A 90 12.598 -1.146 47.741 1.00 42.92 C ANISOU 658 CE1 PHE A 90 8968 5110 2229 1387 328 459 C ATOM 659 CE2 PHE A 90 14.115 0.546 48.476 1.00 50.08 C ANISOU 659 CE2 PHE A 90 9614 6355 3060 1402 24 338 C ATOM 660 CZ PHE A 90 13.883 -0.747 48.063 1.00 43.31 C ANISOU 660 CZ PHE A 90 8902 5377 2177 1505 125 419 C ATOM 661 N ASP A 91 12.040 4.349 47.280 1.00 46.62 N ANISOU 661 N ASP A 91 8706 5842 3163 699 136 171 N ATOM 662 CA ASP A 91 13.076 5.260 46.841 1.00 47.97 C ANISOU 662 CA ASP A 91 8643 6205 3379 652 -18 106 C ATOM 663 C ASP A 91 14.297 4.985 47.707 1.00 52.32 C ANISOU 663 C ASP A 91 9221 6919 3737 827 -166 80 C ATOM 664 O ASP A 91 14.247 5.149 48.934 1.00 52.81 O ANISOU 664 O ASP A 91 9424 6977 3664 880 -185 58 O ATOM 665 CB ASP A 91 12.572 6.699 47.037 1.00 50.13 C ANISOU 665 CB ASP A 91 8836 6461 3749 466 -7 37 C ATOM 666 CG ASP A 91 13.651 7.744 46.830 1.00 55.10 C ANISOU 666 CG ASP A 91 9254 7280 4402 404 -154 -45 C ATOM 667 OD1 ASP A 91 14.798 7.378 46.504 1.00 59.45 O ANISOU 667 OD1 ASP A 91 9697 7989 4903 499 -266 -57 O ATOM 668 OD2 ASP A 91 13.348 8.946 47.003 1.00 60.59 O ANISOU 668 OD2 ASP A 91 9891 7964 5167 257 -150 -104 O ATOM 669 N VAL A 92 15.388 4.566 47.074 1.00 50.65 N ANISOU 669 N VAL A 92 8876 6859 3509 924 -274 76 N ATOM 670 CA VAL A 92 16.574 4.144 47.814 1.00 57.10 C ANISOU 670 CA VAL A 92 9712 7845 4138 1124 -423 48 C ATOM 671 C VAL A 92 17.304 5.329 48.440 1.00 56.83 C ANISOU 671 C VAL A 92 9540 7985 4069 1064 -560 -67 C ATOM 672 O VAL A 92 18.318 5.158 49.122 1.00 51.82 O ANISOU 672 O VAL A 92 8892 7519 3279 1218 -703 -118 O ATOM 673 CB VAL A 92 17.540 3.302 46.936 1.00 56.16 C ANISOU 673 CB VAL A 92 9480 7845 4014 1256 -497 69 C ATOM 674 CG1 VAL A 92 16.838 2.054 46.438 1.00 57.26 C ANISOU 674 CG1 VAL A 92 9785 7806 4166 1329 -359 178 C ATOM 675 CG2 VAL A 92 18.057 4.115 45.766 1.00 46.72 C ANISOU 675 CG2 VAL A 92 7994 6771 2987 1102 -546 9 C ATOM 676 N THR A 93 16.775 6.529 48.212 1.00 59.61 N ANISOU 676 N THR A 93 9793 8296 4562 844 -515 -114 N ATOM 677 CA THR A 93 17.289 7.732 48.866 1.00 64.06 C ANISOU 677 CA THR A 93 10251 8988 5099 757 -616 -228 C ATOM 678 C THR A 93 16.418 8.155 50.061 1.00 61.43 C ANISOU 678 C THR A 93 10113 8533 4696 721 -552 -233 C ATOM 679 O THR A 93 16.747 9.111 50.773 1.00 61.21 O ANISOU 679 O THR A 93 10037 8593 4627 657 -627 -328 O ATOM 680 CB THR A 93 17.422 8.915 47.883 1.00 60.40 C ANISOU 680 CB THR A 93 9554 8571 4826 535 -616 -291 C ATOM 681 OG1 THR A 93 16.120 9.355 47.468 1.00 59.10 O ANISOU 681 OG1 THR A 93 9450 8203 4803 379 -466 -244 O ATOM 682 CG2 THR A 93 18.235 8.512 46.661 1.00 65.99 C ANISOU 682 CG2 THR A 93 10076 9390 5607 558 -661 -286 C ATOM 683 N SER A 94 15.311 7.445 50.273 1.00 62.15 N ANISOU 683 N SER A 94 10420 8420 4774 754 -407 -141 N ATOM 684 CA SER A 94 14.419 7.721 51.402 1.00 64.96 C ANISOU 684 CA SER A 94 10978 8646 5060 727 -324 -141 C ATOM 685 C SER A 94 14.082 6.455 52.181 1.00 67.95 C ANISOU 685 C SER A 94 11635 8917 5267 914 -257 -58 C ATOM 686 O SER A 94 13.210 5.683 51.784 1.00 69.81 O ANISOU 686 O SER A 94 11989 8980 5556 912 -108 24 O ATOM 687 CB SER A 94 13.130 8.395 50.927 1.00 66.35 C ANISOU 687 CB SER A 94 11144 8646 5419 523 -171 -130 C ATOM 688 OG SER A 94 12.268 8.655 52.024 1.00 63.86 O ANISOU 688 OG SER A 94 11018 8208 5038 497 -84 -138 O ATOM 689 N ARG A 95 14.768 6.251 53.300 1.00 66.09 N ANISOU 689 N ARG A 95 11510 8780 4820 1075 -365 -85 N ATOM 690 CA ARG A 95 14.611 5.030 54.083 1.00 67.95 C ANISOU 690 CA ARG A 95 12032 8923 4861 1281 -315 -5 C ATOM 691 C ARG A 95 13.172 4.791 54.546 1.00 60.28 C ANISOU 691 C ARG A 95 11302 7699 3902 1208 -100 55 C ATOM 692 O ARG A 95 12.731 3.644 54.639 1.00 57.05 O ANISOU 692 O ARG A 95 11109 7148 3422 1314 16 144 O ATOM 693 CB ARG A 95 15.560 5.044 55.283 1.00 83.09 C ANISOU 693 CB ARG A 95 14030 11000 6542 1463 -479 -59 C ATOM 694 CG ARG A 95 17.028 5.186 54.902 1.00 96.01 C ANISOU 694 CG ARG A 95 15424 12905 8151 1555 -694 -135 C ATOM 695 CD ARG A 95 17.861 5.691 56.074 1.00107.32 C ANISOU 695 CD ARG A 95 16861 14520 9396 1657 -867 -237 C ATOM 696 NE ARG A 95 19.263 5.889 55.713 1.00112.13 N ANISOU 696 NE ARG A 95 17211 15404 9991 1729 -1071 -335 N ATOM 697 CZ ARG A 95 20.091 6.704 56.360 1.00116.32 C ANISOU 697 CZ ARG A 95 17611 16142 10442 1730 -1236 -471 C ATOM 698 NH1 ARG A 95 19.657 7.407 57.398 1.00118.69 N ANISOU 698 NH1 ARG A 95 18028 16401 10669 1667 -1224 -518 N ATOM 699 NH2 ARG A 95 21.352 6.824 55.967 1.00117.38 N ANISOU 699 NH2 ARG A 95 17494 16530 10576 1789 -1409 -570 N ATOM 700 N VAL A 96 12.443 5.866 54.838 1.00 51.60 N ANISOU 700 N VAL A 96 10169 6541 2895 1024 -40 0 N ATOM 701 CA VAL A 96 11.052 5.724 55.258 1.00 53.27 C ANISOU 701 CA VAL A 96 10581 6525 3135 939 168 38 C ATOM 702 C VAL A 96 10.171 5.088 54.163 1.00 51.04 C ANISOU 702 C VAL A 96 10282 6089 3024 858 331 102 C ATOM 703 O VAL A 96 9.204 4.389 54.468 1.00 60.69 O ANISOU 703 O VAL A 96 11713 7124 4224 858 510 152 O ATOM 704 CB VAL A 96 10.455 7.061 55.748 1.00 56.16 C ANISOU 704 CB VAL A 96 10897 6868 3574 761 196 -43 C ATOM 705 CG1 VAL A 96 10.295 8.033 54.597 1.00 60.52 C ANISOU 705 CG1 VAL A 96 11174 7454 4367 569 182 -89 C ATOM 706 CG2 VAL A 96 9.121 6.829 56.454 1.00 59.30 C ANISOU 706 CG2 VAL A 96 11531 7046 3952 710 404 -15 C ATOM 707 N THR A 97 10.512 5.302 52.896 1.00 55.42 N ANISOU 707 N THR A 97 10594 6723 3742 789 273 94 N ATOM 708 CA THR A 97 9.727 4.712 51.807 1.00 46.28 C ANISOU 708 CA THR A 97 9405 5436 2743 718 410 145 C ATOM 709 C THR A 97 9.862 3.194 51.787 1.00 51.00 C ANISOU 709 C THR A 97 10187 5962 3227 887 470 231 C ATOM 710 O THR A 97 8.910 2.474 51.465 1.00 45.70 O ANISOU 710 O THR A 97 9626 5120 2620 846 645 274 O ATOM 711 CB THR A 97 10.068 5.312 50.414 1.00 44.29 C ANISOU 711 CB THR A 97 8860 5283 2684 608 334 118 C ATOM 712 OG1 THR A 97 11.380 4.902 49.996 1.00 47.10 O ANISOU 712 OG1 THR A 97 9112 5808 2976 738 181 128 O ATOM 713 CG2 THR A 97 9.977 6.845 50.443 1.00 39.81 C ANISOU 713 CG2 THR A 97 8133 4775 2219 445 280 34 C ATOM 714 N TYR A 98 11.044 2.701 52.131 1.00 51.84 N ANISOU 714 N TYR A 98 10330 6202 3166 1080 326 249 N ATOM 715 CA TYR A 98 11.225 1.268 52.225 1.00 51.23 C ANISOU 715 CA TYR A 98 10459 6051 2956 1266 378 333 C ATOM 716 C TYR A 98 10.543 0.749 53.481 1.00 58.58 C ANISOU 716 C TYR A 98 11723 6815 3719 1331 515 369 C ATOM 717 O TYR A 98 10.035 -0.373 53.497 1.00 58.73 O ANISOU 717 O TYR A 98 11959 6667 3687 1394 667 440 O ATOM 718 CB TYR A 98 12.703 0.884 52.243 1.00 58.52 C ANISOU 718 CB TYR A 98 11325 7172 3739 1476 178 336 C ATOM 719 CG TYR A 98 12.896 -0.599 52.463 1.00 60.52 C ANISOU 719 CG TYR A 98 11830 7337 3828 1695 231 426 C ATOM 720 CD1 TYR A 98 12.727 -1.505 51.418 1.00 51.09 C ANISOU 720 CD1 TYR A 98 10624 6062 2725 1705 316 484 C ATOM 721 CD2 TYR A 98 13.216 -1.097 53.718 1.00 66.44 C ANISOU 721 CD2 TYR A 98 12845 8073 4325 1894 203 453 C ATOM 722 CE1 TYR A 98 12.891 -2.860 51.621 1.00 53.94 C ANISOU 722 CE1 TYR A 98 11233 6327 2935 1903 376 567 C ATOM 723 CE2 TYR A 98 13.380 -2.447 53.933 1.00 67.33 C ANISOU 723 CE2 TYR A 98 13217 8089 4278 2103 260 541 C ATOM 724 CZ TYR A 98 13.214 -3.327 52.886 1.00 63.20 C ANISOU 724 CZ TYR A 98 12680 7480 3854 2105 350 598 C ATOM 725 OH TYR A 98 13.380 -4.675 53.114 1.00 63.27 O ANISOU 725 OH TYR A 98 12965 7378 3698 2316 415 685 O ATOM 726 N LYS A 99 10.541 1.573 54.532 1.00 60.03 N ANISOU 726 N LYS A 99 11956 7040 3815 1312 467 317 N ATOM 727 CA LYS A 99 9.903 1.220 55.788 1.00 54.29 C ANISOU 727 CA LYS A 99 11545 6162 2921 1364 595 343 C ATOM 728 C LYS A 99 8.407 0.992 55.601 1.00 55.93 C ANISOU 728 C LYS A 99 11855 6134 3260 1194 853 360 C ATOM 729 O LYS A 99 7.790 0.222 56.344 1.00 58.19 O ANISOU 729 O LYS A 99 12439 6247 3424 1245 1020 406 O ATOM 730 CB LYS A 99 10.147 2.295 56.858 1.00 61.02 C ANISOU 730 CB LYS A 99 12395 7113 3678 1347 492 269 C ATOM 731 CG LYS A 99 11.530 2.248 57.493 1.00 64.95 C ANISOU 731 CG LYS A 99 12902 7813 3963 1564 265 250 C ATOM 732 CD LYS A 99 11.516 2.826 58.905 1.00 72.06 C ANISOU 732 CD LYS A 99 13959 8731 4687 1600 230 203 C ATOM 733 CE LYS A 99 10.385 2.216 59.732 1.00 77.94 C ANISOU 733 CE LYS A 99 15050 9228 5335 1599 463 264 C ATOM 734 NZ LYS A 99 10.693 2.137 61.192 1.00 79.54 N ANISOU 734 NZ LYS A 99 15518 9445 5259 1764 414 262 N ATOM 735 N ASN A 100 7.839 1.646 54.595 1.00 56.19 N ANISOU 735 N ASN A 100 11646 6167 3539 997 888 316 N ATOM 736 CA ASN A 100 6.408 1.556 54.315 1.00 59.30 C ANISOU 736 CA ASN A 100 12080 6369 4084 825 1115 306 C ATOM 737 C ASN A 100 6.003 0.393 53.400 1.00 59.88 C ANISOU 737 C ASN A 100 12192 6324 4235 827 1247 360 C ATOM 738 O ASN A 100 4.818 0.072 53.275 1.00 54.61 O ANISOU 738 O ASN A 100 11599 5486 3663 706 1455 349 O ATOM 739 CB ASN A 100 5.891 2.895 53.770 1.00 53.62 C ANISOU 739 CB ASN A 100 11096 5697 3578 620 1091 224 C ATOM 740 CG ASN A 100 5.610 3.892 54.882 1.00 58.27 C ANISOU 740 CG ASN A 100 11743 6289 4107 564 1087 164 C ATOM 741 OD1 ASN A 100 5.770 5.103 54.720 1.00 59.97 O ANISOU 741 OD1 ASN A 100 11762 6608 4417 467 982 99 O ATOM 742 ND2 ASN A 100 5.201 3.373 56.032 1.00 46.36 N ANISOU 742 ND2 ASN A 100 10522 4660 2435 625 1209 187 N ATOM 743 N VAL A 101 6.995 -0.243 52.783 1.00 51.93 N ANISOU 743 N VAL A 101 11133 5414 3186 966 1128 409 N ATOM 744 CA VAL A 101 6.755 -1.364 51.875 1.00 50.61 C ANISOU 744 CA VAL A 101 10998 5148 3082 983 1235 459 C ATOM 745 C VAL A 101 5.808 -2.440 52.423 1.00 56.59 C ANISOU 745 C VAL A 101 12069 5668 3765 986 1484 498 C ATOM 746 O VAL A 101 4.837 -2.796 51.750 1.00 60.45 O ANISOU 746 O VAL A 101 12532 6029 4407 848 1653 480 O ATOM 747 CB VAL A 101 8.076 -1.979 51.373 1.00 53.07 C ANISOU 747 CB VAL A 101 11258 5597 3310 1173 1069 511 C ATOM 748 CG1 VAL A 101 7.853 -3.395 50.850 1.00 57.82 C ANISOU 748 CG1 VAL A 101 12016 6056 3896 1243 1206 578 C ATOM 749 CG2 VAL A 101 8.678 -1.095 50.282 1.00 49.37 C ANISOU 749 CG2 VAL A 101 10434 5317 3006 1096 898 464 C ATOM 750 N PRO A 102 6.077 -2.957 53.642 1.00 60.04 N ANISOU 750 N PRO A 102 12808 6043 3963 1140 1514 545 N ATOM 751 CA PRO A 102 5.191 -3.964 54.244 1.00 60.87 C ANISOU 751 CA PRO A 102 13243 5906 3979 1138 1770 583 C ATOM 752 C PRO A 102 3.739 -3.484 54.315 1.00 62.78 C ANISOU 752 C PRO A 102 13459 6013 4383 896 1975 508 C ATOM 753 O PRO A 102 2.828 -4.285 54.097 1.00 58.44 O ANISOU 753 O PRO A 102 13036 5280 3890 810 2203 508 O ATOM 754 CB PRO A 102 5.764 -4.132 55.655 1.00 71.88 C ANISOU 754 CB PRO A 102 14923 7297 5090 1328 1723 627 C ATOM 755 CG PRO A 102 7.198 -3.761 55.519 1.00 74.84 C ANISOU 755 CG PRO A 102 15134 7914 5385 1497 1432 635 C ATOM 756 CD PRO A 102 7.223 -2.647 54.516 1.00 67.00 C ANISOU 756 CD PRO A 102 13744 7076 4637 1326 1313 560 C ATOM 757 N ASN A 103 3.538 -2.198 54.612 1.00 62.98 N ANISOU 757 N ASN A 103 13318 6130 4479 789 1898 438 N ATOM 758 CA ASN A 103 2.207 -1.589 54.585 1.00 62.29 C ANISOU 758 CA ASN A 103 13154 5948 4566 565 2063 353 C ATOM 759 C ASN A 103 1.512 -1.686 53.220 1.00 63.52 C ANISOU 759 C ASN A 103 13083 6081 4973 414 2134 309 C ATOM 760 O ASN A 103 0.320 -1.988 53.146 1.00 61.26 O ANISOU 760 O ASN A 103 12843 5643 4788 273 2354 259 O ATOM 761 CB ASN A 103 2.273 -0.124 55.002 1.00 62.25 C ANISOU 761 CB ASN A 103 12983 6069 4600 496 1932 287 C ATOM 762 CG ASN A 103 2.614 0.060 56.470 1.00 73.72 C ANISOU 762 CG ASN A 103 14673 7517 5821 602 1910 303 C ATOM 763 OD1 ASN A 103 3.135 1.107 56.864 1.00 76.17 O ANISOU 763 OD1 ASN A 103 14871 7968 6103 611 1743 267 O ATOM 764 ND2 ASN A 103 2.317 -0.948 57.289 1.00 72.42 N ANISOU 764 ND2 ASN A 103 14846 7186 5484 679 2082 354 N ATOM 765 N TRP A 104 2.246 -1.416 52.142 1.00 60.47 N ANISOU 765 N TRP A 104 12445 5847 4685 440 1951 318 N ATOM 766 CA TRP A 104 1.665 -1.525 50.805 1.00 53.12 C ANISOU 766 CA TRP A 104 11303 4904 3975 316 2000 280 C ATOM 767 C TRP A 104 1.348 -2.976 50.481 1.00 55.40 C ANISOU 767 C TRP A 104 11767 5042 4241 344 2174 319 C ATOM 768 O TRP A 104 0.272 -3.286 49.973 1.00 55.61 O ANISOU 768 O TRP A 104 11759 4958 4413 201 2348 261 O ATOM 769 CB TRP A 104 2.565 -0.881 49.730 1.00 50.84 C ANISOU 769 CB TRP A 104 10721 4811 3785 339 1769 283 C ATOM 770 CG TRP A 104 2.577 0.606 49.854 1.00 50.40 C ANISOU 770 CG TRP A 104 10473 4870 3805 255 1647 223 C ATOM 771 CD1 TRP A 104 3.564 1.380 50.396 1.00 50.24 C ANISOU 771 CD1 TRP A 104 10412 4993 3683 332 1462 231 C ATOM 772 CD2 TRP A 104 1.522 1.502 49.485 1.00 54.48 C ANISOU 772 CD2 TRP A 104 10827 5363 4511 79 1709 137 C ATOM 773 NE1 TRP A 104 3.196 2.707 50.365 1.00 52.03 N ANISOU 773 NE1 TRP A 104 10468 5274 4025 206 1413 159 N ATOM 774 CE2 TRP A 104 1.948 2.806 49.807 1.00 55.22 C ANISOU 774 CE2 TRP A 104 10799 5576 4606 59 1559 105 C ATOM 775 CE3 TRP A 104 0.263 1.328 48.901 1.00 51.31 C ANISOU 775 CE3 TRP A 104 10366 4855 4276 -58 1873 75 C ATOM 776 CZ2 TRP A 104 1.161 3.927 49.566 1.00 57.13 C ANISOU 776 CZ2 TRP A 104 10881 5821 5004 -83 1572 26 C ATOM 777 CZ3 TRP A 104 -0.514 2.442 48.664 1.00 57.78 C ANISOU 777 CZ3 TRP A 104 11011 5694 5250 -190 1874 -10 C ATOM 778 CH2 TRP A 104 -0.065 3.724 48.995 1.00 57.81 C ANISOU 778 CH2 TRP A 104 10914 5805 5247 -196 1726 -28 C ATOM 779 N HIS A 105 2.283 -3.863 50.792 1.00 55.66 N ANISOU 779 N HIS A 105 11992 5070 4086 533 2127 410 N ATOM 780 CA HIS A 105 2.071 -5.281 50.560 1.00 52.00 C ANISOU 780 CA HIS A 105 11733 4450 3576 578 2294 456 C ATOM 781 C HIS A 105 0.792 -5.743 51.255 1.00 56.46 C ANISOU 781 C HIS A 105 12524 4793 4136 454 2583 415 C ATOM 782 O HIS A 105 -0.073 -6.358 50.633 1.00 61.84 O ANISOU 782 O HIS A 105 13198 5355 4944 329 2764 370 O ATOM 783 CB HIS A 105 3.269 -6.089 51.042 1.00 53.29 C ANISOU 783 CB HIS A 105 12114 4632 3503 827 2200 561 C ATOM 784 CG HIS A 105 3.172 -7.550 50.725 1.00 59.89 C ANISOU 784 CG HIS A 105 13165 5307 4285 892 2359 615 C ATOM 785 ND1 HIS A 105 2.619 -8.464 51.594 1.00 63.90 N ANISOU 785 ND1 HIS A 105 14034 5594 4651 913 2590 646 N ATOM 786 CD2 HIS A 105 3.541 -8.250 49.626 1.00 53.24 C ANISOU 786 CD2 HIS A 105 12236 4482 3509 932 2331 641 C ATOM 787 CE1 HIS A 105 2.662 -9.667 51.049 1.00 62.22 C ANISOU 787 CE1 HIS A 105 13953 5266 4422 965 2698 689 C ATOM 788 NE2 HIS A 105 3.217 -9.563 49.855 1.00 66.41 N ANISOU 788 NE2 HIS A 105 14213 5941 5078 980 2540 686 N ATOM 789 N ARG A 106 0.673 -5.428 52.542 1.00 58.47 N ANISOU 789 N ARG A 106 12973 5000 4244 482 2628 420 N ATOM 790 CA ARG A 106 -0.523 -5.761 53.312 1.00 59.21 C ANISOU 790 CA ARG A 106 13285 4889 4323 357 2908 374 C ATOM 791 C ARG A 106 -1.795 -5.211 52.655 1.00 59.10 C ANISOU 791 C ARG A 106 13031 4854 4570 113 3027 248 C ATOM 792 O ARG A 106 -2.764 -5.945 52.466 1.00 60.40 O ANISOU 792 O ARG A 106 13279 4858 4810 -11 3268 197 O ATOM 793 CB ARG A 106 -0.398 -5.242 54.755 1.00 62.28 C ANISOU 793 CB ARG A 106 13871 5267 4526 420 2900 390 C ATOM 794 CG ARG A 106 -1.678 -5.370 55.570 1.00 67.92 C ANISOU 794 CG ARG A 106 14778 5788 5242 269 3188 327 C ATOM 795 CD ARG A 106 -1.560 -4.712 56.940 1.00 76.60 C ANISOU 795 CD ARG A 106 16042 6894 6168 323 3163 334 C ATOM 796 NE ARG A 106 -1.061 -3.342 56.859 1.00 85.01 N ANISOU 796 NE ARG A 106 16829 8173 7298 324 2911 299 N ATOM 797 CZ ARG A 106 -1.774 -2.309 56.423 1.00 87.04 C ANISOU 797 CZ ARG A 106 16808 8494 7771 148 2901 197 C ATOM 798 NH1 ARG A 106 -3.023 -2.490 56.014 1.00 87.04 N ANISOU 798 NH1 ARG A 106 16748 8378 7947 -38 3117 112 N ATOM 799 NH2 ARG A 106 -1.237 -1.097 56.388 1.00 87.44 N ANISOU 799 NH2 ARG A 106 16640 8723 7858 161 2676 174 N ATOM 800 N ASP A 107 -1.789 -3.923 52.316 1.00 58.07 N ANISOU 800 N ASP A 107 12607 4885 4574 46 2861 191 N ATOM 801 CA ASP A 107 -2.921 -3.304 51.623 1.00 62.66 C ANISOU 801 CA ASP A 107 12936 5472 5401 -157 2937 69 C ATOM 802 C ASP A 107 -3.273 -4.073 50.351 1.00 58.60 C ANISOU 802 C ASP A 107 12302 4925 5037 -222 3004 41 C ATOM 803 O ASP A 107 -4.445 -4.258 50.021 1.00 62.57 O ANISOU 803 O ASP A 107 12745 5340 5689 -384 3189 -61 O ATOM 804 CB ASP A 107 -2.602 -1.856 51.236 1.00 71.45 C ANISOU 804 CB ASP A 107 13751 6776 6622 -178 2707 35 C ATOM 805 CG ASP A 107 -2.712 -0.888 52.400 1.00 80.68 C ANISOU 805 CG ASP A 107 14981 7962 7712 -190 2687 9 C ATOM 806 OD1 ASP A 107 -3.084 -1.319 53.512 1.00 81.90 O ANISOU 806 OD1 ASP A 107 15406 7983 7731 -184 2854 16 O ATOM 807 OD2 ASP A 107 -2.428 0.313 52.192 1.00 82.44 O ANISOU 807 OD2 ASP A 107 14990 8327 8007 -206 2510 -19 O ATOM 808 N LEU A 108 -2.244 -4.521 49.642 1.00 60.60 N ANISOU 808 N LEU A 108 12515 5259 5250 -92 2852 124 N ATOM 809 CA LEU A 108 -2.416 -5.130 48.327 1.00 62.41 C ANISOU 809 CA LEU A 108 12600 5489 5623 -139 2872 101 C ATOM 810 C LEU A 108 -2.979 -6.539 48.459 1.00 63.89 C ANISOU 810 C LEU A 108 13039 5472 5765 -171 3132 100 C ATOM 811 O LEU A 108 -3.976 -6.888 47.827 1.00 62.38 O ANISOU 811 O LEU A 108 12763 5208 5732 -324 3290 4 O ATOM 812 CB LEU A 108 -1.071 -5.158 47.596 1.00 63.68 C ANISOU 812 CB LEU A 108 12652 5801 5741 17 2632 191 C ATOM 813 CG LEU A 108 -0.982 -5.525 46.109 1.00 61.56 C ANISOU 813 CG LEU A 108 12181 5588 5619 -9 2580 177 C ATOM 814 CD1 LEU A 108 -2.072 -4.867 45.284 1.00 51.84 C ANISOU 814 CD1 LEU A 108 10690 4385 4621 -193 2619 55 C ATOM 815 CD2 LEU A 108 0.382 -5.127 45.581 1.00 58.49 C ANISOU 815 CD2 LEU A 108 11650 5384 5188 133 2316 252 C ATOM 816 N VAL A 109 -2.325 -7.343 49.288 1.00 64.32 N ANISOU 816 N VAL A 109 13408 5434 5597 -21 3175 202 N ATOM 817 CA VAL A 109 -2.733 -8.723 49.513 1.00 71.61 C ANISOU 817 CA VAL A 109 14625 6142 6442 -30 3427 219 C ATOM 818 C VAL A 109 -4.122 -8.822 50.144 1.00 71.47 C ANISOU 818 C VAL A 109 14721 5955 6481 -224 3716 113 C ATOM 819 O VAL A 109 -4.853 -9.783 49.899 1.00 74.18 O ANISOU 819 O VAL A 109 15177 6136 6872 -329 3953 63 O ATOM 820 CB VAL A 109 -1.702 -9.471 50.383 1.00 79.02 C ANISOU 820 CB VAL A 109 15904 7016 7103 198 3401 357 C ATOM 821 CG1 VAL A 109 -2.195 -10.867 50.719 1.00 83.14 C ANISOU 821 CG1 VAL A 109 16774 7285 7531 183 3691 375 C ATOM 822 CG2 VAL A 109 -0.361 -9.527 49.663 1.00 79.76 C ANISOU 822 CG2 VAL A 109 15875 7275 7154 386 3137 445 C ATOM 823 N ARG A 110 -4.489 -7.828 50.948 1.00 69.35 N ANISOU 823 N ARG A 110 14417 5725 6209 -277 3702 71 N ATOM 824 CA ARG A 110 -5.816 -7.810 51.552 1.00 73.30 C ANISOU 824 CA ARG A 110 14995 6084 6772 -465 3970 -43 C ATOM 825 C ARG A 110 -6.884 -7.884 50.476 1.00 70.87 C ANISOU 825 C ARG A 110 14433 5773 6721 -665 4081 -186 C ATOM 826 O ARG A 110 -7.935 -8.499 50.655 1.00 74.18 O ANISOU 826 O ARG A 110 14955 6034 7196 -821 4360 -283 O ATOM 827 CB ARG A 110 -6.032 -6.541 52.380 1.00 72.64 C ANISOU 827 CB ARG A 110 14836 6080 6682 -495 3899 -80 C ATOM 828 CG ARG A 110 -7.425 -6.475 52.990 1.00 77.47 C ANISOU 828 CG ARG A 110 15507 6557 7370 -692 4177 -210 C ATOM 829 CD ARG A 110 -7.666 -5.188 53.751 1.00 82.64 C ANISOU 829 CD ARG A 110 16075 7295 8031 -722 4105 -254 C ATOM 830 NE ARG A 110 -7.881 -4.047 52.866 1.00 83.97 N ANISOU 830 NE ARG A 110 15849 7643 8412 -788 3923 -335 N ATOM 831 CZ ARG A 110 -9.020 -3.800 52.224 1.00 84.84 C ANISOU 831 CZ ARG A 110 15731 7759 8745 -961 4027 -483 C ATOM 832 NH1 ARG A 110 -10.051 -4.624 52.352 1.00 85.12 N ANISOU 832 NH1 ARG A 110 15873 7636 8832 -1105 4319 -578 N ATOM 833 NH2 ARG A 110 -9.125 -2.729 51.447 1.00 83.83 N ANISOU 833 NH2 ARG A 110 15271 7796 8786 -989 3842 -543 N ATOM 834 N VAL A 111 -6.590 -7.260 49.346 1.00 68.27 N ANISOU 834 N VAL A 111 13773 5624 6542 -657 3861 -206 N ATOM 835 CA VAL A 111 -7.575 -7.057 48.299 1.00 67.11 C ANISOU 835 CA VAL A 111 13337 5520 6642 -827 3910 -351 C ATOM 836 C VAL A 111 -7.373 -7.979 47.082 1.00 69.15 C ANISOU 836 C VAL A 111 13528 5773 6971 -821 3906 -346 C ATOM 837 O VAL A 111 -8.334 -8.303 46.383 1.00 68.04 O ANISOU 837 O VAL A 111 13255 5598 6998 -976 4042 -477 O ATOM 838 CB VAL A 111 -7.570 -5.575 47.859 1.00 68.27 C ANISOU 838 CB VAL A 111 13151 5867 6921 -839 3679 -395 C ATOM 839 CG1 VAL A 111 -8.231 -5.409 46.516 1.00 65.69 C ANISOU 839 CG1 VAL A 111 12513 5623 6824 -947 3650 -512 C ATOM 840 CG2 VAL A 111 -8.240 -4.701 48.909 1.00 67.06 C ANISOU 840 CG2 VAL A 111 13021 5696 6764 -912 3752 -461 C ATOM 841 N CYS A 112 -6.134 -8.413 46.849 1.00 66.50 N ANISOU 841 N CYS A 112 13284 5477 6507 -642 3753 -205 N ATOM 842 CA CYS A 112 -5.788 -9.136 45.620 1.00 63.28 C ANISOU 842 CA CYS A 112 12782 5094 6166 -614 3704 -191 C ATOM 843 C CYS A 112 -5.291 -10.572 45.811 1.00 72.53 C ANISOU 843 C CYS A 112 14273 6105 7181 -519 3836 -100 C ATOM 844 O CYS A 112 -5.214 -11.347 44.845 1.00 75.26 O ANISOU 844 O CYS A 112 14577 6430 7588 -527 3859 -110 O ATOM 845 CB CYS A 112 -4.747 -8.337 44.833 1.00 60.47 C ANISOU 845 CB CYS A 112 12184 4955 5837 -491 3386 -122 C ATOM 846 SG CYS A 112 -5.334 -6.729 44.277 1.00 56.79 S ANISOU 846 SG CYS A 112 11332 4670 5576 -600 3230 -231 S ATOM 847 N GLU A 113 -4.940 -10.916 47.047 1.00 80.64 N ANISOU 847 N GLU A 113 15627 7016 7998 -421 3918 -12 N ATOM 848 CA GLU A 113 -4.460 -12.256 47.388 1.00 91.55 C ANISOU 848 CA GLU A 113 17361 8224 9199 -307 4051 85 C ATOM 849 C GLU A 113 -2.984 -12.471 47.045 1.00 88.75 C ANISOU 849 C GLU A 113 17027 7979 8716 -63 3808 228 C ATOM 850 O GLU A 113 -2.125 -11.660 47.392 1.00 91.92 O ANISOU 850 O GLU A 113 17356 8535 9036 73 3576 298 O ATOM 851 CB GLU A 113 -5.321 -13.342 46.729 1.00104.66 C ANISOU 851 CB GLU A 113 19072 9724 10969 -463 4305 -8 C ATOM 852 CG GLU A 113 -6.808 -13.234 47.030 1.00113.48 C ANISOU 852 CG GLU A 113 20161 10736 12221 -714 4566 -172 C ATOM 853 CD GLU A 113 -7.113 -13.363 48.507 1.00122.18 C ANISOU 853 CD GLU A 113 21594 11673 13157 -720 4761 -146 C ATOM 854 OE1 GLU A 113 -6.676 -14.359 49.119 1.00126.54 O ANISOU 854 OE1 GLU A 113 22521 12051 13509 -611 4889 -43 O ATOM 855 OE2 GLU A 113 -7.794 -12.471 49.056 1.00125.45 O ANISOU 855 OE2 GLU A 113 21903 12127 13634 -828 4790 -227 O ATOM 856 N ASN A 114 -2.704 -13.567 46.350 1.00 82.54 N ANISOU 856 N ASN A 114 16330 7113 7917 -15 3868 260 N ATOM 857 CA ASN A 114 -1.335 -14.017 46.140 1.00 76.33 C ANISOU 857 CA ASN A 114 15626 6393 6984 230 3685 395 C ATOM 858 C ASN A 114 -0.808 -13.713 44.732 1.00 66.83 C ANISOU 858 C ASN A 114 14084 5381 5929 248 3471 383 C ATOM 859 O ASN A 114 0.003 -14.464 44.186 1.00 63.48 O ANISOU 859 O ASN A 114 13717 4961 5441 389 3407 456 O ATOM 860 CB ASN A 114 -1.241 -15.516 46.458 1.00 81.90 C ANISOU 860 CB ASN A 114 16724 6862 7531 313 3900 460 C ATOM 861 CG ASN A 114 0.155 -16.079 46.262 1.00 89.28 C ANISOU 861 CG ASN A 114 17764 7854 8304 586 3723 595 C ATOM 862 OD1 ASN A 114 1.157 -15.389 46.458 1.00 92.60 O ANISOU 862 OD1 ASN A 114 18079 8460 8643 753 3464 664 O ATOM 863 ND2 ASN A 114 0.225 -17.347 45.873 1.00 88.66 N ANISOU 863 ND2 ASN A 114 17893 7617 8179 631 3869 626 N ATOM 864 N ILE A 115 -1.258 -12.603 44.151 1.00 60.01 N ANISOU 864 N ILE A 115 12876 4671 5255 112 3360 293 N ATOM 865 CA ILE A 115 -0.819 -12.222 42.809 1.00 62.10 C ANISOU 865 CA ILE A 115 12822 5114 5659 118 3164 278 C ATOM 866 C ILE A 115 0.700 -12.035 42.740 1.00 64.86 C ANISOU 866 C ILE A 115 13145 5619 5881 347 2907 400 C ATOM 867 O ILE A 115 1.341 -11.766 43.758 1.00 63.05 O ANISOU 867 O ILE A 115 13056 5415 5486 481 2829 474 O ATOM 868 CB ILE A 115 -1.528 -10.937 42.313 1.00 59.56 C ANISOU 868 CB ILE A 115 12160 4931 5539 -45 3077 168 C ATOM 869 CG1 ILE A 115 -1.334 -9.784 43.309 1.00 53.62 C ANISOU 869 CG1 ILE A 115 11388 4264 4722 -15 2966 190 C ATOM 870 CG2 ILE A 115 -3.010 -11.208 42.074 1.00 64.19 C ANISOU 870 CG2 ILE A 115 12711 5397 6283 -268 3313 24 C ATOM 871 CD1 ILE A 115 -1.684 -8.391 42.746 1.00 49.03 C ANISOU 871 CD1 ILE A 115 10464 3850 4315 -120 2817 111 C ATOM 872 N PRO A 116 1.280 -12.185 41.535 1.00 61.12 N ANISOU 872 N PRO A 116 12485 5254 5483 392 2778 411 N ATOM 873 CA PRO A 116 2.710 -11.927 41.335 1.00 53.69 C ANISOU 873 CA PRO A 116 11465 4486 4449 591 2529 505 C ATOM 874 C PRO A 116 3.032 -10.467 41.611 1.00 51.27 C ANISOU 874 C PRO A 116 10944 4366 4172 580 2331 494 C ATOM 875 O PRO A 116 2.362 -9.584 41.068 1.00 48.01 O ANISOU 875 O PRO A 116 10291 4020 3930 420 2305 411 O ATOM 876 CB PRO A 116 2.916 -12.224 39.848 1.00 49.85 C ANISOU 876 CB PRO A 116 10775 4073 4092 569 2469 483 C ATOM 877 CG PRO A 116 1.795 -13.125 39.482 1.00 58.50 C ANISOU 877 CG PRO A 116 11968 4983 5276 423 2715 409 C ATOM 878 CD PRO A 116 0.633 -12.656 40.299 1.00 58.13 C ANISOU 878 CD PRO A 116 11967 4844 5275 261 2864 330 C ATOM 879 N ILE A 117 4.053 -10.227 42.428 1.00 46.26 N ANISOU 879 N ILE A 117 10397 3812 3367 753 2192 571 N ATOM 880 CA ILE A 117 4.434 -8.879 42.835 1.00 48.02 C ANISOU 880 CA ILE A 117 10449 4202 3595 748 2011 559 C ATOM 881 C ILE A 117 5.944 -8.702 42.735 1.00 48.32 C ANISOU 881 C ILE A 117 10409 4424 3527 941 1777 626 C ATOM 882 O ILE A 117 6.702 -9.576 43.141 1.00 52.19 O ANISOU 882 O ILE A 117 11098 4885 3848 1132 1765 699 O ATOM 883 CB ILE A 117 4.026 -8.602 44.295 1.00 49.78 C ANISOU 883 CB ILE A 117 10879 4337 3697 745 2094 561 C ATOM 884 CG1 ILE A 117 2.517 -8.759 44.483 1.00 49.68 C ANISOU 884 CG1 ILE A 117 10943 4145 3787 547 2340 482 C ATOM 885 CG2 ILE A 117 4.457 -7.201 44.711 1.00 47.36 C ANISOU 885 CG2 ILE A 117 10397 4205 3394 739 1905 543 C ATOM 886 CD1 ILE A 117 2.089 -8.733 45.960 1.00 55.66 C ANISOU 886 CD1 ILE A 117 11962 4781 4404 552 2466 490 C ATOM 887 N VAL A 118 6.378 -7.571 42.192 1.00 47.35 N ANISOU 887 N VAL A 118 9998 4489 3502 895 1596 595 N ATOM 888 CA VAL A 118 7.801 -7.263 42.115 1.00 46.67 C ANISOU 888 CA VAL A 118 9804 4597 3331 1053 1374 635 C ATOM 889 C VAL A 118 8.109 -6.031 42.943 1.00 49.23 C ANISOU 889 C VAL A 118 10048 5041 3614 1040 1246 610 C ATOM 890 O VAL A 118 7.359 -5.052 42.936 1.00 44.52 O ANISOU 890 O VAL A 118 9331 4446 3138 872 1266 550 O ATOM 891 CB VAL A 118 8.262 -6.992 40.664 1.00 50.74 C ANISOU 891 CB VAL A 118 10040 5249 3990 1014 1263 616 C ATOM 892 CG1 VAL A 118 9.734 -6.604 40.641 1.00 48.14 C ANISOU 892 CG1 VAL A 118 9584 5129 3577 1160 1043 641 C ATOM 893 CG2 VAL A 118 8.037 -8.202 39.796 1.00 51.43 C ANISOU 893 CG2 VAL A 118 10195 5231 4115 1032 1377 635 C ATOM 894 N LEU A 119 9.223 -6.086 43.656 1.00 51.90 N ANISOU 894 N LEU A 119 10456 5485 3780 1223 1110 649 N ATOM 895 CA LEU A 119 9.625 -4.994 44.525 1.00 53.55 C ANISOU 895 CA LEU A 119 10606 5815 3927 1228 981 620 C ATOM 896 C LEU A 119 10.725 -4.219 43.830 1.00 53.99 C ANISOU 896 C LEU A 119 10376 6101 4035 1246 771 593 C ATOM 897 O LEU A 119 11.711 -4.801 43.389 1.00 52.91 O ANISOU 897 O LEU A 119 10201 6060 3842 1392 678 623 O ATOM 898 CB LEU A 119 10.112 -5.541 45.871 1.00 55.49 C ANISOU 898 CB LEU A 119 11124 6029 3929 1423 969 668 C ATOM 899 CG LEU A 119 10.576 -4.531 46.921 1.00 54.65 C ANISOU 899 CG LEU A 119 10993 6047 3725 1452 835 634 C ATOM 900 CD1 LEU A 119 9.480 -3.519 47.250 1.00 57.35 C ANISOU 900 CD1 LEU A 119 11290 6321 4181 1237 922 576 C ATOM 901 CD2 LEU A 119 11.044 -5.254 48.176 1.00 55.43 C ANISOU 901 CD2 LEU A 119 11389 6106 3566 1672 828 687 C ATOM 902 N CYS A 120 10.541 -2.909 43.706 1.00 53.05 N ANISOU 902 N CYS A 120 10060 6067 4030 1093 706 532 N ATOM 903 CA CYS A 120 11.506 -2.071 42.995 1.00 46.01 C ANISOU 903 CA CYS A 120 8895 5382 3206 1074 530 496 C ATOM 904 C CYS A 120 12.023 -0.944 43.884 1.00 51.60 C ANISOU 904 C CYS A 120 9538 6217 3850 1064 402 447 C ATOM 905 O CYS A 120 11.244 -0.236 44.533 1.00 50.39 O ANISOU 905 O CYS A 120 9432 5993 3720 953 459 416 O ATOM 906 CB CYS A 120 10.876 -1.488 41.726 1.00 53.99 C ANISOU 906 CB CYS A 120 9702 6379 4432 887 568 464 C ATOM 907 SG CYS A 120 10.536 -2.740 40.452 1.00 51.25 S ANISOU 907 SG CYS A 120 9370 5935 4167 903 677 505 S ATOM 908 N GLY A 121 13.343 -0.800 43.924 1.00 54.37 N ANISOU 908 N GLY A 121 9778 6761 4119 1181 231 430 N ATOM 909 CA GLY A 121 13.976 0.315 44.604 1.00 50.77 C ANISOU 909 CA GLY A 121 9215 6456 3617 1159 94 364 C ATOM 910 C GLY A 121 14.444 1.300 43.550 1.00 46.19 C ANISOU 910 C GLY A 121 8344 6013 3193 1023 9 309 C ATOM 911 O GLY A 121 15.443 1.073 42.882 1.00 47.39 O ANISOU 911 O GLY A 121 8354 6306 3345 1093 -88 300 O ATOM 912 N ASN A 122 13.704 2.391 43.398 1.00 47.02 N ANISOU 912 N ASN A 122 8369 6070 3425 829 52 269 N ATOM 913 CA ASN A 122 13.956 3.379 42.345 1.00 49.07 C ANISOU 913 CA ASN A 122 8385 6418 3839 681 2 224 C ATOM 914 C ASN A 122 15.007 4.426 42.731 1.00 42.67 C ANISOU 914 C ASN A 122 7424 5797 2993 654 -145 144 C ATOM 915 O ASN A 122 15.335 4.565 43.894 1.00 49.98 O ANISOU 915 O ASN A 122 8431 6774 3787 726 -206 114 O ATOM 916 CB ASN A 122 12.634 4.057 41.973 1.00 42.46 C ANISOU 916 CB ASN A 122 7548 5433 3154 499 120 218 C ATOM 917 CG ASN A 122 12.767 5.020 40.827 1.00 40.16 C ANISOU 917 CG ASN A 122 7044 5201 3014 355 87 184 C ATOM 918 OD1 ASN A 122 13.489 4.773 39.863 1.00 44.60 O ANISOU 918 OD1 ASN A 122 7479 5854 3612 379 38 192 O ATOM 919 ND2 ASN A 122 12.046 6.126 40.910 1.00 37.63 N ANISOU 919 ND2 ASN A 122 6695 4821 2780 209 122 146 N ATOM 920 N LYS A 123 15.547 5.125 41.734 1.00 41.26 N ANISOU 920 N LYS A 123 7030 5721 2926 551 -198 104 N ATOM 921 CA LYS A 123 16.503 6.227 41.923 1.00 47.70 C ANISOU 921 CA LYS A 123 7679 6708 3737 482 -316 13 C ATOM 922 C LYS A 123 17.938 5.791 42.211 1.00 51.05 C ANISOU 922 C LYS A 123 8017 7341 4038 635 -457 -30 C ATOM 923 O LYS A 123 18.708 6.540 42.811 1.00 52.43 O ANISOU 923 O LYS A 123 8097 7662 4160 613 -560 -120 O ATOM 924 CB LYS A 123 16.032 7.207 43.011 1.00 44.67 C ANISOU 924 CB LYS A 123 7364 6284 3324 395 -313 -37 C ATOM 925 CG LYS A 123 14.699 7.882 42.710 1.00 42.61 C ANISOU 925 CG LYS A 123 7150 5845 3197 234 -190 -19 C ATOM 926 CD LYS A 123 14.369 8.977 43.707 1.00 44.36 C ANISOU 926 CD LYS A 123 7414 6045 3398 140 -195 -80 C ATOM 927 CE LYS A 123 12.891 9.350 43.636 1.00 46.06 C ANISOU 927 CE LYS A 123 7722 6063 3714 32 -61 -54 C ATOM 928 NZ LYS A 123 12.577 10.533 44.504 1.00 50.48 N ANISOU 928 NZ LYS A 123 8310 6600 4268 -70 -64 -120 N ATOM 929 N VAL A 124 18.309 4.594 41.778 1.00 51.46 N ANISOU 929 N VAL A 124 8095 7413 4046 790 -462 24 N ATOM 930 CA VAL A 124 19.653 4.088 42.059 1.00 55.71 C ANISOU 930 CA VAL A 124 8555 8152 4459 964 -599 -19 C ATOM 931 C VAL A 124 20.710 4.818 41.235 1.00 56.46 C ANISOU 931 C VAL A 124 8375 8439 4638 870 -682 -108 C ATOM 932 O VAL A 124 21.903 4.548 41.366 1.00 58.41 O ANISOU 932 O VAL A 124 8506 8882 4803 992 -802 -169 O ATOM 933 CB VAL A 124 19.756 2.581 41.794 1.00 57.42 C ANISOU 933 CB VAL A 124 8887 8328 4603 1166 -575 64 C ATOM 934 CG1 VAL A 124 18.809 1.824 42.713 1.00 54.04 C ANISOU 934 CG1 VAL A 124 8749 7713 4072 1264 -486 142 C ATOM 935 CG2 VAL A 124 19.451 2.285 40.330 1.00 56.81 C ANISOU 935 CG2 VAL A 124 8728 8183 4676 1085 -489 112 C ATOM 936 N ASP A 125 20.266 5.732 40.377 1.00 57.40 N ANISOU 936 N ASP A 125 8394 8497 4917 656 -612 -118 N ATOM 937 CA ASP A 125 21.181 6.571 39.620 1.00 58.12 C ANISOU 937 CA ASP A 125 8245 8745 5092 532 -663 -205 C ATOM 938 C ASP A 125 21.841 7.589 40.543 1.00 67.10 C ANISOU 938 C ASP A 125 9294 10025 6176 470 -760 -326 C ATOM 939 O ASP A 125 22.939 8.074 40.267 1.00 70.86 O ANISOU 939 O ASP A 125 9566 10690 6667 422 -836 -429 O ATOM 940 CB ASP A 125 20.436 7.307 38.514 1.00 64.78 C ANISOU 940 CB ASP A 125 9047 9461 6106 329 -554 -176 C ATOM 941 CG ASP A 125 19.280 8.137 39.043 1.00 64.00 C ANISOU 941 CG ASP A 125 9070 9199 6049 202 -482 -163 C ATOM 942 OD1 ASP A 125 18.171 7.582 39.210 1.00 61.13 O ANISOU 942 OD1 ASP A 125 8878 8663 5687 242 -398 -81 O ATOM 943 OD2 ASP A 125 19.479 9.347 39.282 1.00 61.80 O ANISOU 943 OD2 ASP A 125 8714 8963 5804 58 -503 -241 O ATOM 944 N ILE A 126 21.163 7.909 41.641 1.00 63.88 N ANISOU 944 N ILE A 126 9037 9527 5705 464 -749 -323 N ATOM 945 CA ILE A 126 21.641 8.938 42.556 1.00 65.49 C ANISOU 945 CA ILE A 126 9179 9844 5862 389 -830 -440 C ATOM 946 C ILE A 126 22.869 8.487 43.352 1.00 74.59 C ANISOU 946 C ILE A 126 10259 11224 6857 568 -987 -525 C ATOM 947 O ILE A 126 22.864 7.436 43.996 1.00 74.05 O ANISOU 947 O ILE A 126 10335 11152 6651 785 -1026 -472 O ATOM 948 CB ILE A 126 20.515 9.434 43.484 1.00 62.22 C ANISOU 948 CB ILE A 126 8952 9261 5428 328 -767 -413 C ATOM 949 CG1 ILE A 126 19.602 10.392 42.716 1.00 54.79 C ANISOU 949 CG1 ILE A 126 8000 8161 4655 108 -647 -390 C ATOM 950 CG2 ILE A 126 21.096 10.126 44.722 1.00 70.56 C ANISOU 950 CG2 ILE A 126 9987 10449 6374 328 -873 -529 C ATOM 951 CD1 ILE A 126 18.247 10.593 43.350 1.00 59.23 C ANISOU 951 CD1 ILE A 126 8762 8521 5224 70 -552 -335 C ATOM 952 N LYS A 127 23.916 9.303 43.290 1.00 79.80 N ANISOU 952 N LYS A 127 10701 12084 7538 475 -1072 -665 N ATOM 953 CA LYS A 127 25.206 8.973 43.880 1.00 89.64 C ANISOU 953 CA LYS A 127 11821 13586 8653 632 -1233 -776 C ATOM 954 C LYS A 127 25.093 8.451 45.313 1.00 88.60 C ANISOU 954 C LYS A 127 11872 13465 8328 833 -1317 -768 C ATOM 955 O LYS A 127 25.443 7.306 45.589 1.00 89.18 O ANISOU 955 O LYS A 127 12019 13593 8274 1079 -1383 -726 O ATOM 956 CB LYS A 127 26.136 10.190 43.823 1.00 99.50 C ANISOU 956 CB LYS A 127 12825 15023 9959 449 -1293 -951 C ATOM 957 CG LYS A 127 27.608 9.864 44.021 1.00109.04 C ANISOU 957 CG LYS A 127 13823 16529 11077 583 -1451 -1089 C ATOM 958 CD LYS A 127 28.487 11.055 43.668 1.00114.64 C ANISOU 958 CD LYS A 127 14268 17408 11883 358 -1471 -1265 C ATOM 959 CE LYS A 127 29.964 10.702 43.753 1.00118.74 C ANISOU 959 CE LYS A 127 14546 18241 12330 485 -1622 -1419 C ATOM 960 NZ LYS A 127 30.353 10.256 45.119 1.00120.90 N ANISOU 960 NZ LYS A 127 14876 18655 12404 714 -1785 -1481 N ATOM 961 N ASP A 128 24.595 9.288 46.216 1.00 88.56 N ANISOU 961 N ASP A 128 11954 13399 8295 734 -1310 -807 N ATOM 962 CA ASP A 128 24.546 8.945 47.635 1.00 94.09 C ANISOU 962 CA ASP A 128 12825 14122 8801 909 -1392 -816 C ATOM 963 C ASP A 128 23.343 8.077 47.998 1.00 89.03 C ANISOU 963 C ASP A 128 12489 13238 8102 1021 -1284 -653 C ATOM 964 O ASP A 128 22.331 8.576 48.487 1.00 87.49 O ANISOU 964 O ASP A 128 12445 12871 7927 915 -1193 -616 O ATOM 965 CB ASP A 128 24.545 10.213 48.488 1.00103.13 C ANISOU 965 CB ASP A 128 13938 15311 9934 754 -1428 -936 C ATOM 966 CG ASP A 128 24.632 9.916 49.972 1.00111.62 C ANISOU 966 CG ASP A 128 15174 16442 10796 938 -1531 -965 C ATOM 967 OD1 ASP A 128 25.172 8.849 50.335 1.00113.23 O ANISOU 967 OD1 ASP A 128 15433 16743 10846 1199 -1628 -944 O ATOM 968 OD2 ASP A 128 24.165 10.753 50.773 1.00115.13 O ANISOU 968 OD2 ASP A 128 15697 16828 11219 830 -1514 -1010 O ATOM 969 N ARG A 129 23.471 6.774 47.776 1.00 85.17 N ANISOU 969 N ARG A 129 12090 12733 7539 1234 -1290 -563 N ATOM 970 CA ARG A 129 22.390 5.830 48.052 1.00 80.09 C ANISOU 970 CA ARG A 129 11736 11855 6837 1341 -1173 -413 C ATOM 971 C ARG A 129 22.258 5.517 49.548 1.00 79.25 C ANISOU 971 C ARG A 129 11859 11734 6517 1511 -1225 -409 C ATOM 972 O ARG A 129 23.260 5.403 50.257 1.00 83.27 O ANISOU 972 O ARG A 129 12321 12446 6871 1674 -1387 -495 O ATOM 973 CB ARG A 129 22.614 4.543 47.257 1.00 74.94 C ANISOU 973 CB ARG A 129 11109 11185 6179 1505 -1151 -323 C ATOM 974 CG ARG A 129 21.669 3.426 47.615 1.00 74.40 C ANISOU 974 CG ARG A 129 11350 10895 6026 1642 -1037 -182 C ATOM 975 CD ARG A 129 21.731 2.329 46.585 1.00 75.30 C ANISOU 975 CD ARG A 129 11468 10958 6186 1736 -982 -96 C ATOM 976 NE ARG A 129 20.748 1.285 46.846 1.00 71.13 N ANISOU 976 NE ARG A 129 11237 10194 5594 1833 -845 33 N ATOM 977 CZ ARG A 129 20.485 0.293 46.006 1.00 65.35 C ANISOU 977 CZ ARG A 129 10566 9355 4910 1890 -754 121 C ATOM 978 NH1 ARG A 129 21.138 0.213 44.853 1.00 54.71 N ANISOU 978 NH1 ARG A 129 9003 8119 3668 1869 -792 100 N ATOM 979 NH2 ARG A 129 19.574 -0.618 46.319 1.00 69.25 N ANISOU 979 NH2 ARG A 129 11340 9630 5344 1961 -617 225 N ATOM 980 N LYS A 130 21.022 5.373 50.023 1.00 71.06 N ANISOU 980 N LYS A 130 11070 10461 5467 1475 -1086 -316 N ATOM 981 CA LYS A 130 20.776 5.163 51.458 1.00 71.33 C ANISOU 981 CA LYS A 130 11347 10455 5301 1611 -1110 -308 C ATOM 982 C LYS A 130 20.288 3.749 51.808 1.00 73.17 C ANISOU 982 C LYS A 130 11880 10527 5396 1827 -1028 -175 C ATOM 983 O LYS A 130 20.703 3.175 52.818 1.00 74.59 O ANISOU 983 O LYS A 130 12226 10759 5354 2053 -1113 -173 O ATOM 984 CB LYS A 130 19.791 6.206 51.998 1.00 68.10 C ANISOU 984 CB LYS A 130 11009 9912 4953 1406 -1015 -329 C ATOM 985 CG LYS A 130 20.267 7.656 51.897 1.00 74.90 C ANISOU 985 CG LYS A 130 11624 10919 5918 1203 -1093 -468 C ATOM 986 CD LYS A 130 21.632 7.849 52.549 1.00 85.10 C ANISOU 986 CD LYS A 130 12783 12487 7063 1328 -1302 -601 C ATOM 987 CE LYS A 130 21.824 9.278 53.050 1.00 90.31 C ANISOU 987 CE LYS A 130 13316 13240 7759 1140 -1356 -742 C ATOM 988 NZ LYS A 130 21.694 10.297 51.972 1.00 93.19 N ANISOU 988 NZ LYS A 130 13468 13582 8356 868 -1286 -783 N ATOM 989 N VAL A 131 19.405 3.198 50.977 1.00 70.27 N ANISOU 989 N VAL A 131 11587 9960 5152 1757 -861 -68 N ATOM 990 CA VAL A 131 18.874 1.852 51.188 1.00 70.74 C ANISOU 990 CA VAL A 131 11932 9842 5103 1929 -753 56 C ATOM 991 C VAL A 131 19.594 0.829 50.302 1.00 73.85 C ANISOU 991 C VAL A 131 12260 10304 5496 2085 -795 98 C ATOM 992 O VAL A 131 19.151 0.533 49.184 1.00 71.05 O ANISOU 992 O VAL A 131 11845 9851 5302 1986 -687 151 O ATOM 993 CB VAL A 131 17.355 1.799 50.930 1.00 69.99 C ANISOU 993 CB VAL A 131 11986 9473 5135 1757 -527 136 C ATOM 994 CG1 VAL A 131 16.822 0.401 51.174 1.00 71.15 C ANISOU 994 CG1 VAL A 131 12435 9431 5168 1919 -399 253 C ATOM 995 CG2 VAL A 131 16.631 2.808 51.822 1.00 71.96 C ANISOU 995 CG2 VAL A 131 12301 9655 5384 1611 -481 91 C ATOM 996 N LYS A 132 20.701 0.288 50.815 1.00 69.14 N ANISOU 996 N LYS A 132 11678 9879 4713 2339 -956 68 N ATOM 997 CA LYS A 132 21.562 -0.606 50.040 1.00 68.41 C ANISOU 997 CA LYS A 132 11497 9891 4607 2509 -1024 87 C ATOM 998 C LYS A 132 21.103 -2.067 50.050 1.00 71.37 C ANISOU 998 C LYS A 132 12171 10067 4879 2696 -905 222 C ATOM 999 O LYS A 132 20.264 -2.470 50.862 1.00 71.39 O ANISOU 999 O LYS A 132 12477 9872 4776 2735 -788 296 O ATOM 1000 CB LYS A 132 23.012 -0.520 50.530 1.00 78.73 C ANISOU 1000 CB LYS A 132 12657 11492 5764 2710 -1260 -23 C ATOM 1001 CG LYS A 132 23.690 0.820 50.281 1.00 86.21 C ANISOU 1001 CG LYS A 132 13260 12666 6830 2525 -1381 -175 C ATOM 1002 CD LYS A 132 25.166 0.759 50.655 1.00 92.09 C ANISOU 1002 CD LYS A 132 13837 13717 7435 2733 -1611 -297 C ATOM 1003 CE LYS A 132 25.886 2.069 50.359 1.00 92.72 C ANISOU 1003 CE LYS A 132 13563 14025 7640 2532 -1716 -464 C ATOM 1004 NZ LYS A 132 25.468 3.166 51.274 1.00 93.47 N ANISOU 1004 NZ LYS A 132 13690 14105 7718 2378 -1722 -531 N ATOM 1005 N ALA A 133 21.681 -2.856 49.148 1.00 70.85 N ANISOU 1005 N ALA A 133 12024 10053 4843 2808 -929 250 N ATOM 1006 CA ALA A 133 21.312 -4.258 48.974 1.00 74.11 C ANISOU 1006 CA ALA A 133 12700 10277 5180 2973 -809 372 C ATOM 1007 C ALA A 133 21.096 -5.012 50.288 1.00 77.68 C ANISOU 1007 C ALA A 133 13527 10610 5377 3199 -784 438 C ATOM 1008 O ALA A 133 20.095 -5.709 50.449 1.00 77.77 O ANISOU 1008 O ALA A 133 13824 10360 5365 3185 -592 540 O ATOM 1009 CB ALA A 133 22.355 -4.978 48.113 1.00 71.91 C ANISOU 1009 CB ALA A 133 12277 10144 4901 3143 -905 365 C ATOM 1010 N LYS A 134 22.029 -4.878 51.224 1.00 79.94 N ANISOU 1010 N LYS A 134 13818 11088 5468 3405 -974 375 N ATOM 1011 CA LYS A 134 21.986 -5.699 52.433 1.00 82.59 C ANISOU 1011 CA LYS A 134 14524 11327 5531 3669 -971 441 C ATOM 1012 C LYS A 134 20.792 -5.384 53.343 1.00 85.14 C ANISOU 1012 C LYS A 134 15106 11430 5814 3537 -813 486 C ATOM 1013 O LYS A 134 20.440 -6.179 54.213 1.00 82.62 O ANISOU 1013 O LYS A 134 15151 10947 5292 3709 -733 569 O ATOM 1014 CB LYS A 134 23.312 -5.621 53.200 1.00 85.18 C ANISOU 1014 CB LYS A 134 14782 11935 5650 3941 -1231 350 C ATOM 1015 CG LYS A 134 23.539 -4.335 53.985 1.00 91.26 C ANISOU 1015 CG LYS A 134 15398 12876 6401 3831 -1361 226 C ATOM 1016 CD LYS A 134 24.844 -4.420 54.776 1.00101.67 C ANISOU 1016 CD LYS A 134 16669 14471 7490 4133 -1620 131 C ATOM 1017 CE LYS A 134 24.841 -3.497 55.991 1.00106.60 C ANISOU 1017 CE LYS A 134 17323 15184 7997 4101 -1714 43 C ATOM 1018 NZ LYS A 134 26.047 -3.692 56.850 1.00108.07 N ANISOU 1018 NZ LYS A 134 17502 15630 7930 4425 -1967 -49 N ATOM 1019 N SER A 135 20.160 -4.236 53.124 1.00 83.62 N ANISOU 1019 N SER A 135 14734 11227 5812 3232 -758 430 N ATOM 1020 CA SER A 135 19.021 -3.821 53.936 1.00 78.36 C ANISOU 1020 CA SER A 135 14273 10369 5131 3085 -610 455 C ATOM 1021 C SER A 135 17.693 -4.224 53.293 1.00 75.69 C ANISOU 1021 C SER A 135 14054 9748 4955 2893 -347 542 C ATOM 1022 O SER A 135 16.647 -4.209 53.944 1.00 71.74 O ANISOU 1022 O SER A 135 13783 9047 4427 2803 -181 580 O ATOM 1023 CB SER A 135 19.054 -2.307 54.152 1.00 77.00 C ANISOU 1023 CB SER A 135 13852 10341 5065 2872 -698 337 C ATOM 1024 OG SER A 135 20.385 -1.844 54.292 1.00 79.07 O ANISOU 1024 OG SER A 135 13883 10903 5257 2990 -946 228 O ATOM 1025 N ILE A 136 17.739 -4.580 52.013 1.00 74.51 N ANISOU 1025 N ILE A 136 13743 9593 4974 2830 -308 563 N ATOM 1026 CA ILE A 136 16.536 -4.928 51.262 1.00 72.84 C ANISOU 1026 CA ILE A 136 13597 9145 4936 2640 -76 624 C ATOM 1027 C ILE A 136 16.168 -6.395 51.459 1.00 73.97 C ANISOU 1027 C ILE A 136 14092 9071 4944 2808 78 734 C ATOM 1028 O ILE A 136 16.746 -7.277 50.820 1.00 75.85 O ANISOU 1028 O ILE A 136 14330 9331 5159 2958 49 774 O ATOM 1029 CB ILE A 136 16.726 -4.656 49.758 1.00 62.89 C ANISOU 1029 CB ILE A 136 12013 7970 3912 2493 -99 594 C ATOM 1030 CG1 ILE A 136 17.267 -3.242 49.547 1.00 59.55 C ANISOU 1030 CG1 ILE A 136 11253 7771 3602 2348 -257 484 C ATOM 1031 CG2 ILE A 136 15.417 -4.860 49.010 1.00 62.34 C ANISOU 1031 CG2 ILE A 136 11985 7674 4028 2279 127 637 C ATOM 1032 CD1 ILE A 136 17.454 -2.858 48.104 1.00 52.94 C ANISOU 1032 CD1 ILE A 136 10108 7016 2989 2194 -276 452 C ATOM 1033 N VAL A 137 15.192 -6.654 52.324 1.00 74.35 N ANISOU 1033 N VAL A 137 14444 8900 4906 2775 253 780 N ATOM 1034 CA VAL A 137 14.903 -8.024 52.742 1.00 80.65 C ANISOU 1034 CA VAL A 137 15628 9483 5533 2951 404 882 C ATOM 1035 C VAL A 137 13.437 -8.438 52.587 1.00 80.20 C ANISOU 1035 C VAL A 137 15756 9132 5583 2750 699 924 C ATOM 1036 O VAL A 137 13.118 -9.626 52.580 1.00 81.88 O ANISOU 1036 O VAL A 137 16249 9148 5714 2844 858 1003 O ATOM 1037 CB VAL A 137 15.338 -8.247 54.207 1.00 82.93 C ANISOU 1037 CB VAL A 137 16209 9781 5522 3195 332 907 C ATOM 1038 CG1 VAL A 137 15.062 -9.675 54.637 1.00 90.38 C ANISOU 1038 CG1 VAL A 137 17582 10485 6273 3387 498 1018 C ATOM 1039 CG2 VAL A 137 16.813 -7.909 54.374 1.00 78.99 C ANISOU 1039 CG2 VAL A 137 15518 9586 4907 3410 33 848 C ATOM 1040 N PHE A 138 12.546 -7.465 52.443 1.00 74.78 N ANISOU 1040 N PHE A 138 14914 8418 5082 2474 775 865 N ATOM 1041 CA PHE A 138 11.118 -7.766 52.477 1.00 76.84 C ANISOU 1041 CA PHE A 138 15349 8417 5432 2284 1052 883 C ATOM 1042 C PHE A 138 10.665 -8.797 51.442 1.00 71.23 C ANISOU 1042 C PHE A 138 14679 7554 4832 2240 1214 925 C ATOM 1043 O PHE A 138 9.722 -9.552 51.685 1.00 66.61 O ANISOU 1043 O PHE A 138 14357 6725 4226 2183 1454 960 O ATOM 1044 CB PHE A 138 10.276 -6.495 52.347 1.00 77.52 C ANISOU 1044 CB PHE A 138 15212 8524 5720 2002 1086 799 C ATOM 1045 CG PHE A 138 8.802 -6.749 52.445 1.00 73.04 C ANISOU 1045 CG PHE A 138 14802 7708 5244 1809 1364 797 C ATOM 1046 CD1 PHE A 138 8.182 -6.823 53.683 1.00 76.78 C ANISOU 1046 CD1 PHE A 138 15565 8034 5573 1811 1502 809 C ATOM 1047 CD2 PHE A 138 8.043 -6.947 51.304 1.00 66.42 C ANISOU 1047 CD2 PHE A 138 13822 6786 4627 1629 1492 776 C ATOM 1048 CE1 PHE A 138 6.825 -7.069 53.781 1.00 76.46 C ANISOU 1048 CE1 PHE A 138 15661 7771 5622 1625 1770 793 C ATOM 1049 CE2 PHE A 138 6.686 -7.194 51.391 1.00 66.47 C ANISOU 1049 CE2 PHE A 138 13955 6579 4722 1448 1748 755 C ATOM 1050 CZ PHE A 138 6.075 -7.254 52.633 1.00 75.51 C ANISOU 1050 CZ PHE A 138 15379 7580 5732 1442 1892 761 C ATOM 1051 N HIS A 139 11.328 -8.827 50.291 1.00 69.77 N ANISOU 1051 N HIS A 139 14236 7510 4765 2257 1091 913 N ATOM 1052 CA HIS A 139 10.904 -9.705 49.207 1.00 71.94 C ANISOU 1052 CA HIS A 139 14511 7658 5164 2196 1232 940 C ATOM 1053 C HIS A 139 11.213 -11.177 49.485 1.00 82.17 C ANISOU 1053 C HIS A 139 16148 8807 6266 2427 1320 1030 C ATOM 1054 O HIS A 139 10.418 -12.060 49.161 1.00 81.67 O ANISOU 1054 O HIS A 139 16261 8524 6245 2356 1542 1059 O ATOM 1055 CB HIS A 139 11.540 -9.279 47.883 1.00 65.58 C ANISOU 1055 CB HIS A 139 13334 7048 4535 2148 1076 901 C ATOM 1056 CG HIS A 139 13.026 -9.448 47.844 1.00 65.45 C ANISOU 1056 CG HIS A 139 13240 7238 4391 2396 848 917 C ATOM 1057 ND1 HIS A 139 13.873 -8.779 48.702 1.00 68.95 N ANISOU 1057 ND1 HIS A 139 13639 7863 4697 2521 655 890 N ATOM 1058 CD2 HIS A 139 13.817 -10.202 47.045 1.00 71.41 C ANISOU 1058 CD2 HIS A 139 13942 8057 5136 2541 782 947 C ATOM 1059 CE1 HIS A 139 15.122 -9.119 48.436 1.00 75.39 C ANISOU 1059 CE1 HIS A 139 14367 8851 5425 2735 478 896 C ATOM 1060 NE2 HIS A 139 15.114 -9.980 47.434 1.00 77.01 N ANISOU 1060 NE2 HIS A 139 14568 8988 5706 2754 552 934 N ATOM 1061 N ARG A 140 12.369 -11.432 50.086 1.00 88.03 N ANISOU 1061 N ARG A 140 16984 9670 6793 2706 1147 1068 N ATOM 1062 CA ARG A 140 12.826 -12.798 50.326 1.00 98.74 C ANISOU 1062 CA ARG A 140 18661 10909 7948 2968 1197 1157 C ATOM 1063 C ARG A 140 11.719 -13.734 50.800 1.00108.34 C ANISOU 1063 C ARG A 140 20270 11797 9098 2914 1500 1213 C ATOM 1064 O ARG A 140 11.719 -14.918 50.469 1.00111.05 O ANISOU 1064 O ARG A 140 20825 11985 9385 3017 1622 1274 O ATOM 1065 CB ARG A 140 13.971 -12.801 51.341 1.00 97.89 C ANISOU 1065 CB ARG A 140 18671 10949 7575 3274 991 1181 C ATOM 1066 CG ARG A 140 15.327 -12.472 50.751 1.00 96.53 C ANISOU 1066 CG ARG A 140 18185 11076 7416 3423 711 1141 C ATOM 1067 CD ARG A 140 16.291 -12.033 51.835 1.00100.40 C ANISOU 1067 CD ARG A 140 18701 11758 7687 3648 489 1119 C ATOM 1068 NE ARG A 140 17.680 -12.247 51.447 1.00106.01 N ANISOU 1068 NE ARG A 140 19241 12707 8329 3891 254 1100 N ATOM 1069 CZ ARG A 140 18.394 -13.317 51.786 1.00110.61 C ANISOU 1069 CZ ARG A 140 20067 13270 8688 4219 206 1163 C ATOM 1070 NH1 ARG A 140 17.852 -14.276 52.526 1.00111.42 N ANISOU 1070 NH1 ARG A 140 20618 13111 8606 4342 384 1259 N ATOM 1071 NH2 ARG A 140 19.653 -13.427 51.388 1.00112.98 N ANISOU 1071 NH2 ARG A 140 20170 13812 8946 4429 -16 1128 N ATOM 1072 N LYS A 141 10.768 -13.196 51.557 1.00116.01 N ANISOU 1072 N LYS A 141 21335 12660 10081 2744 1631 1185 N ATOM 1073 CA LYS A 141 9.825 -14.026 52.303 1.00122.93 C ANISOU 1073 CA LYS A 141 22626 13236 10845 2719 1914 1234 C ATOM 1074 C LYS A 141 8.558 -14.475 51.572 1.00125.65 C ANISOU 1074 C LYS A 141 22986 13364 11391 2454 2193 1204 C ATOM 1075 O LYS A 141 7.907 -15.426 52.009 1.00124.78 O ANISOU 1075 O LYS A 141 23235 12991 11184 2453 2444 1247 O ATOM 1076 CB LYS A 141 9.411 -13.321 53.596 1.00123.95 C ANISOU 1076 CB LYS A 141 22894 13340 10862 2680 1941 1217 C ATOM 1077 CG LYS A 141 10.562 -12.869 54.469 1.00125.42 C ANISOU 1077 CG LYS A 141 23094 13730 10831 2934 1679 1232 C ATOM 1078 CD LYS A 141 11.023 -11.474 54.096 1.00121.55 C ANISOU 1078 CD LYS A 141 22160 13528 10497 2829 1437 1141 C ATOM 1079 CE LYS A 141 11.748 -10.822 55.258 1.00119.82 C ANISOU 1079 CE LYS A 141 21986 13467 10072 2995 1243 1127 C ATOM 1080 NZ LYS A 141 12.866 -11.669 55.757 1.00119.71 N ANISOU 1080 NZ LYS A 141 22195 13504 9783 3359 1109 1197 N ATOM 1081 N LYS A 142 8.187 -13.805 50.484 1.00124.66 N ANISOU 1081 N LYS A 142 22486 13343 11537 2230 2159 1126 N ATOM 1082 CA LYS A 142 6.841 -14.002 49.945 1.00121.77 C ANISOU 1082 CA LYS A 142 22105 12794 11367 1952 2415 1069 C ATOM 1083 C LYS A 142 6.705 -14.036 48.427 1.00121.40 C ANISOU 1083 C LYS A 142 21753 12812 11563 1816 2397 1020 C ATOM 1084 O LYS A 142 5.846 -13.350 47.871 1.00122.22 O ANISOU 1084 O LYS A 142 21618 12935 11886 1568 2450 933 O ATOM 1085 CB LYS A 142 5.902 -12.933 50.506 1.00117.74 C ANISOU 1085 CB LYS A 142 21502 12282 10953 1732 2479 992 C ATOM 1086 CG LYS A 142 5.645 -13.067 51.995 1.00121.41 C ANISOU 1086 CG LYS A 142 22325 12607 11197 1805 2593 1030 C ATOM 1087 CD LYS A 142 4.749 -11.958 52.507 1.00121.06 C ANISOU 1087 CD LYS A 142 22165 12575 11256 1588 2647 946 C ATOM 1088 CE LYS A 142 5.471 -10.625 52.476 1.00121.07 C ANISOU 1088 CE LYS A 142 21842 12856 11305 1610 2356 910 C ATOM 1089 NZ LYS A 142 6.663 -10.627 53.368 1.00121.25 N ANISOU 1089 NZ LYS A 142 22011 12990 11069 1888 2162 977 N ATOM 1090 N ASN A 143 7.515 -14.850 47.758 1.00120.21 N ANISOU 1090 N ASN A 143 21620 12688 11368 1983 2329 1073 N ATOM 1091 CA ASN A 143 7.457 -14.922 46.301 1.00120.97 C ANISOU 1091 CA ASN A 143 21438 12849 11677 1871 2306 1029 C ATOM 1092 C ASN A 143 7.520 -13.526 45.694 1.00114.28 C ANISOU 1092 C ASN A 143 20165 12236 11021 1725 2119 954 C ATOM 1093 O ASN A 143 6.869 -13.233 44.690 1.00114.54 O ANISOU 1093 O ASN A 143 19967 12281 11273 1523 2165 885 O ATOM 1094 CB ASN A 143 6.183 -15.638 45.841 1.00128.03 C ANISOU 1094 CB ASN A 143 22438 13507 12699 1660 2596 984 C ATOM 1095 CG ASN A 143 6.044 -15.676 44.324 1.00131.58 C ANISOU 1095 CG ASN A 143 22597 14028 13371 1534 2572 928 C ATOM 1096 OD1 ASN A 143 6.957 -16.100 43.612 1.00131.40 O ANISOU 1096 OD1 ASN A 143 22503 14096 13328 1682 2447 969 O ATOM 1097 ND2 ASN A 143 4.893 -15.237 43.825 1.00131.47 N ANISOU 1097 ND2 ASN A 143 22412 13974 13565 1266 2690 829 N ATOM 1098 N LEU A 144 8.295 -12.656 46.325 1.00104.64 N ANISOU 1098 N LEU A 144 18852 11196 9710 1829 1912 962 N ATOM 1099 CA LEU A 144 8.496 -11.315 45.804 1.00 95.73 C ANISOU 1099 CA LEU A 144 17343 10290 8741 1710 1728 896 C ATOM 1100 C LEU A 144 9.885 -11.223 45.196 1.00 86.45 C ANISOU 1100 C LEU A 144 15974 9338 7537 1881 1487 917 C ATOM 1101 O LEU A 144 10.883 -11.505 45.864 1.00 89.66 O ANISOU 1101 O LEU A 144 16502 9819 7746 2118 1364 967 O ATOM 1102 CB LEU A 144 8.336 -10.284 46.917 1.00 94.30 C ANISOU 1102 CB LEU A 144 17170 10161 8500 1671 1675 869 C ATOM 1103 CG LEU A 144 7.044 -10.425 47.721 1.00 96.29 C ANISOU 1103 CG LEU A 144 17653 10191 8743 1530 1919 849 C ATOM 1104 CD1 LEU A 144 7.208 -9.871 49.129 1.00 99.14 C ANISOU 1104 CD1 LEU A 144 18166 10572 8931 1606 1871 861 C ATOM 1105 CD2 LEU A 144 5.882 -9.760 47.000 1.00 95.35 C ANISOU 1105 CD2 LEU A 144 17306 10045 8877 1248 2019 757 C ATOM 1106 N GLN A 145 9.946 -10.858 43.919 1.00 67.97 N ANISOU 1106 N GLN A 145 13334 7104 5389 1767 1423 875 N ATOM 1107 CA GLN A 145 11.221 -10.641 43.261 1.00 60.41 C ANISOU 1107 CA GLN A 145 12154 6370 4431 1895 1203 880 C ATOM 1108 C GLN A 145 11.593 -9.170 43.449 1.00 59.09 C ANISOU 1108 C GLN A 145 11725 6407 4318 1817 1024 822 C ATOM 1109 O GLN A 145 10.713 -8.319 43.561 1.00 52.40 O ANISOU 1109 O GLN A 145 10798 5526 3586 1618 1081 773 O ATOM 1110 CB GLN A 145 11.120 -11.015 41.776 1.00 55.00 C ANISOU 1110 CB GLN A 145 11296 5687 3913 1812 1235 864 C ATOM 1111 CG GLN A 145 12.255 -10.501 40.905 1.00 54.77 C ANISOU 1111 CG GLN A 145 10968 5902 3942 1867 1022 846 C ATOM 1112 CD GLN A 145 13.522 -11.311 41.059 1.00 61.71 C ANISOU 1112 CD GLN A 145 11935 6863 4649 2146 912 898 C ATOM 1113 OE1 GLN A 145 13.480 -12.488 41.414 1.00 68.61 O ANISOU 1113 OE1 GLN A 145 13092 7584 5393 2291 1018 957 O ATOM 1114 NE2 GLN A 145 14.662 -10.685 40.778 1.00 62.51 N ANISOU 1114 NE2 GLN A 145 11795 7208 4749 2222 702 869 N ATOM 1115 N TYR A 146 12.887 -8.875 43.528 1.00 56.23 N ANISOU 1115 N TYR A 146 11238 6256 3870 1976 813 822 N ATOM 1116 CA TYR A 146 13.335 -7.496 43.687 1.00 49.46 C ANISOU 1116 CA TYR A 146 10133 5597 3061 1900 645 758 C ATOM 1117 C TYR A 146 14.273 -7.075 42.558 1.00 53.46 C ANISOU 1117 C TYR A 146 10327 6313 3674 1895 488 723 C ATOM 1118 O TYR A 146 15.099 -7.870 42.105 1.00 52.00 O ANISOU 1118 O TYR A 146 10140 6188 3431 2060 432 752 O ATOM 1119 CB TYR A 146 14.032 -7.270 45.040 1.00 55.46 C ANISOU 1119 CB TYR A 146 11013 6445 3612 2070 526 760 C ATOM 1120 CG TYR A 146 14.634 -5.883 45.123 1.00 57.43 C ANISOU 1120 CG TYR A 146 10989 6916 3914 1993 344 683 C ATOM 1121 CD1 TYR A 146 13.832 -4.775 45.371 1.00 53.97 C ANISOU 1121 CD1 TYR A 146 10473 6450 3583 1780 385 633 C ATOM 1122 CD2 TYR A 146 15.992 -5.673 44.904 1.00 56.19 C ANISOU 1122 CD2 TYR A 146 10645 6997 3709 2125 141 649 C ATOM 1123 CE1 TYR A 146 14.364 -3.496 45.418 1.00 52.66 C ANISOU 1123 CE1 TYR A 146 10070 6471 3469 1698 233 559 C ATOM 1124 CE2 TYR A 146 16.534 -4.394 44.959 1.00 50.22 C ANISOU 1124 CE2 TYR A 146 9637 6437 3007 2033 -8 566 C ATOM 1125 CZ TYR A 146 15.713 -3.314 45.216 1.00 50.22 C ANISOU 1125 CZ TYR A 146 9584 6388 3108 1818 42 525 C ATOM 1126 OH TYR A 146 16.235 -2.041 45.263 1.00 48.38 O ANISOU 1126 OH TYR A 146 9118 6334 2930 1719 -93 441 O ATOM 1127 N TYR A 147 14.133 -5.825 42.115 1.00 49.31 N ANISOU 1127 N TYR A 147 9547 5889 3300 1706 427 660 N ATOM 1128 CA TYR A 147 15.075 -5.206 41.176 1.00 48.95 C ANISOU 1128 CA TYR A 147 9201 6053 3344 1682 277 615 C ATOM 1129 C TYR A 147 15.405 -3.786 41.607 1.00 51.71 C ANISOU 1129 C TYR A 147 9373 6553 3719 1583 153 545 C ATOM 1130 O TYR A 147 14.519 -3.042 42.052 1.00 48.13 O ANISOU 1130 O TYR A 147 8950 6018 3322 1433 218 523 O ATOM 1131 CB TYR A 147 14.506 -5.158 39.746 1.00 45.40 C ANISOU 1131 CB TYR A 147 8600 5555 3094 1518 355 609 C ATOM 1132 CG TYR A 147 14.401 -6.514 39.093 1.00 46.53 C ANISOU 1132 CG TYR A 147 8863 5589 3228 1611 453 663 C ATOM 1133 CD1 TYR A 147 15.539 -7.186 38.658 1.00 45.56 C ANISOU 1133 CD1 TYR A 147 8693 5581 3036 1789 360 682 C ATOM 1134 CD2 TYR A 147 13.165 -7.123 38.911 1.00 44.23 C ANISOU 1134 CD2 TYR A 147 8727 5081 2998 1518 643 685 C ATOM 1135 CE1 TYR A 147 15.452 -8.440 38.073 1.00 53.10 C ANISOU 1135 CE1 TYR A 147 9772 6428 3978 1879 454 730 C ATOM 1136 CE2 TYR A 147 13.065 -8.370 38.317 1.00 51.35 C ANISOU 1136 CE2 TYR A 147 9745 5875 3891 1593 742 727 C ATOM 1137 CZ TYR A 147 14.212 -9.025 37.906 1.00 57.39 C ANISOU 1137 CZ TYR A 147 10478 6748 4581 1776 647 753 C ATOM 1138 OH TYR A 147 14.114 -10.265 37.328 1.00 61.29 O ANISOU 1138 OH TYR A 147 11099 7126 5063 1854 749 794 O ATOM 1139 N ASP A 148 16.678 -3.412 41.481 1.00 48.92 N ANISOU 1139 N ASP A 148 8837 6423 3329 1665 -19 501 N ATOM 1140 CA ASP A 148 17.062 -2.003 41.517 1.00 43.82 C ANISOU 1140 CA ASP A 148 7968 5931 2751 1530 -129 419 C ATOM 1141 C ASP A 148 16.595 -1.401 40.199 1.00 53.94 C ANISOU 1141 C ASP A 148 9060 7191 4242 1323 -74 404 C ATOM 1142 O ASP A 148 16.700 -2.054 39.157 1.00 50.86 O ANISOU 1142 O ASP A 148 8621 6788 3914 1344 -40 433 O ATOM 1143 CB ASP A 148 18.582 -1.856 41.573 1.00 50.64 C ANISOU 1143 CB ASP A 148 8662 7045 3532 1663 -314 362 C ATOM 1144 CG ASP A 148 19.156 -2.070 42.963 1.00 62.08 C ANISOU 1144 CG ASP A 148 10249 8567 4772 1856 -413 347 C ATOM 1145 OD1 ASP A 148 18.433 -1.886 43.972 1.00 56.33 O ANISOU 1145 OD1 ASP A 148 9704 7724 3976 1835 -356 363 O ATOM 1146 OD2 ASP A 148 20.356 -2.409 43.036 1.00 65.46 O ANISOU 1146 OD2 ASP A 148 10595 9178 5100 2035 -551 314 O ATOM 1147 N ILE A 149 16.097 -0.167 40.223 1.00 46.13 N ANISOU 1147 N ILE A 149 7974 6199 3356 1132 -68 357 N ATOM 1148 CA ILE A 149 15.783 0.517 38.972 1.00 44.66 C ANISOU 1148 CA ILE A 149 7606 6011 3352 953 -37 338 C ATOM 1149 C ILE A 149 16.159 1.992 39.014 1.00 44.56 C ANISOU 1149 C ILE A 149 7414 6118 3399 811 -122 262 C ATOM 1150 O ILE A 149 16.372 2.557 40.086 1.00 45.71 O ANISOU 1150 O ILE A 149 7592 6314 3463 819 -181 221 O ATOM 1151 CB ILE A 149 14.289 0.376 38.575 1.00 41.70 C ANISOU 1151 CB ILE A 149 7329 5427 3088 832 123 372 C ATOM 1152 CG1 ILE A 149 13.383 0.996 39.626 1.00 43.75 C ANISOU 1152 CG1 ILE A 149 7706 5585 3334 752 179 354 C ATOM 1153 CG2 ILE A 149 13.918 -1.090 38.326 1.00 48.20 C ANISOU 1153 CG2 ILE A 149 8312 6127 3875 943 224 437 C ATOM 1154 CD1 ILE A 149 11.961 1.220 39.136 1.00 46.53 C ANISOU 1154 CD1 ILE A 149 8081 5772 3825 599 315 356 C ATOM 1155 N SER A 150 16.263 2.606 37.839 1.00 47.91 N ANISOU 1155 N SER A 150 7660 6583 3959 682 -124 241 N ATOM 1156 CA SER A 150 16.358 4.060 37.754 1.00 47.48 C ANISOU 1156 CA SER A 150 7467 6590 3983 514 -163 176 C ATOM 1157 C SER A 150 15.471 4.581 36.624 1.00 45.66 C ANISOU 1157 C SER A 150 7184 6252 3914 356 -75 192 C ATOM 1158 O SER A 150 15.845 4.554 35.441 1.00 41.03 O ANISOU 1158 O SER A 150 6475 5713 3401 324 -80 197 O ATOM 1159 CB SER A 150 17.806 4.525 37.561 1.00 51.52 C ANISOU 1159 CB SER A 150 7785 7320 4469 525 -288 107 C ATOM 1160 OG SER A 150 17.842 5.864 37.082 1.00 47.50 O ANISOU 1160 OG SER A 150 7140 6842 4068 336 -293 52 O ATOM 1161 N ALA A 151 14.287 5.053 37.000 1.00 43.04 N ANISOU 1161 N ALA A 151 6948 5777 3630 266 3 196 N ATOM 1162 CA ALA A 151 13.316 5.550 36.031 1.00 43.86 C ANISOU 1162 CA ALA A 151 7016 5773 3876 136 81 205 C ATOM 1163 C ALA A 151 13.929 6.581 35.080 1.00 50.40 C ANISOU 1163 C ALA A 151 7671 6693 4786 24 31 170 C ATOM 1164 O ALA A 151 13.714 6.523 33.874 1.00 46.36 O ANISOU 1164 O ALA A 151 7099 6154 4361 -17 65 192 O ATOM 1165 CB ALA A 151 12.104 6.129 36.751 1.00 40.59 C ANISOU 1165 CB ALA A 151 6706 5224 3492 58 151 191 C ATOM 1166 N LYS A 152 14.715 7.509 35.624 1.00 51.89 N ANISOU 1166 N LYS A 152 7787 6990 4940 -26 -45 112 N ATOM 1167 CA LYS A 152 15.281 8.592 34.825 1.00 51.38 C ANISOU 1167 CA LYS A 152 7576 6997 4949 -153 -73 70 C ATOM 1168 C LYS A 152 16.328 8.147 33.806 1.00 47.95 C ANISOU 1168 C LYS A 152 7010 6686 4522 -120 -109 72 C ATOM 1169 O LYS A 152 16.631 8.888 32.864 1.00 49.86 O ANISOU 1169 O LYS A 152 7150 6955 4839 -229 -101 53 O ATOM 1170 CB LYS A 152 15.894 9.661 35.729 1.00 57.59 C ANISOU 1170 CB LYS A 152 8319 7870 5693 -225 -136 -8 C ATOM 1171 CG LYS A 152 14.893 10.452 36.547 1.00 66.23 C ANISOU 1171 CG LYS A 152 9520 8842 6801 -299 -95 -22 C ATOM 1172 CD LYS A 152 14.105 11.416 35.690 1.00 68.00 C ANISOU 1172 CD LYS A 152 9734 8955 7149 -434 -29 -16 C ATOM 1173 CE LYS A 152 13.715 12.651 36.489 1.00 67.94 C ANISOU 1173 CE LYS A 152 9771 8895 7150 -538 -22 -69 C ATOM 1174 NZ LYS A 152 14.917 13.441 36.883 1.00 70.65 N ANISOU 1174 NZ LYS A 152 10017 9378 7450 -607 -95 -149 N ATOM 1175 N SER A 153 16.890 6.958 33.999 1.00 39.29 N ANISOU 1175 N SER A 153 5925 5659 3345 33 -144 93 N ATOM 1176 CA SER A 153 17.949 6.466 33.122 1.00 46.71 C ANISOU 1176 CA SER A 153 6736 6729 4283 83 -182 87 C ATOM 1177 C SER A 153 17.500 5.244 32.328 1.00 47.88 C ANISOU 1177 C SER A 153 6944 6798 4450 177 -124 162 C ATOM 1178 O SER A 153 18.261 4.704 31.517 1.00 47.05 O ANISOU 1178 O SER A 153 6748 6783 4347 229 -142 165 O ATOM 1179 CB SER A 153 19.206 6.125 33.929 1.00 50.33 C ANISOU 1179 CB SER A 153 7129 7369 4626 198 -287 33 C ATOM 1180 OG SER A 153 18.960 5.062 34.841 1.00 48.87 O ANISOU 1180 OG SER A 153 7091 7144 4334 368 -298 74 O ATOM 1181 N ASN A 154 16.263 4.816 32.563 1.00 41.07 N ANISOU 1181 N ASN A 154 6231 5771 3603 192 -48 211 N ATOM 1182 CA ASN A 154 15.732 3.613 31.924 1.00 45.11 C ANISOU 1182 CA ASN A 154 6817 6194 4130 273 18 271 C ATOM 1183 C ASN A 154 16.410 2.342 32.439 1.00 44.16 C ANISOU 1183 C ASN A 154 6756 6129 3893 459 -14 293 C ATOM 1184 O ASN A 154 16.203 1.256 31.900 1.00 43.66 O ANISOU 1184 O ASN A 154 6751 6009 3830 540 36 338 O ATOM 1185 CB ASN A 154 15.846 3.705 30.392 1.00 40.10 C ANISOU 1185 CB ASN A 154 6073 5574 3588 211 41 281 C ATOM 1186 CG ASN A 154 14.937 4.765 29.798 1.00 41.63 C ANISOU 1186 CG ASN A 154 6254 5675 3889 58 87 274 C ATOM 1187 OD1 ASN A 154 13.908 5.118 30.381 1.00 39.20 O ANISOU 1187 OD1 ASN A 154 6037 5255 3603 14 127 273 O ATOM 1188 ND2 ASN A 154 15.309 5.282 28.626 1.00 37.00 N ANISOU 1188 ND2 ASN A 154 5560 5133 3365 -17 84 268 N ATOM 1189 N TYR A 155 17.212 2.474 33.489 1.00 43.49 N ANISOU 1189 N TYR A 155 6667 6154 3705 532 -98 258 N ATOM 1190 CA TYR A 155 17.980 1.342 33.988 1.00 41.90 C ANISOU 1190 CA TYR A 155 6519 6024 3377 731 -147 274 C ATOM 1191 C TYR A 155 17.105 0.226 34.545 1.00 44.18 C ANISOU 1191 C TYR A 155 7034 6148 3605 836 -62 340 C ATOM 1192 O TYR A 155 16.296 0.449 35.439 1.00 42.84 O ANISOU 1192 O TYR A 155 6994 5871 3410 804 -18 346 O ATOM 1193 CB TYR A 155 18.986 1.795 35.037 1.00 45.52 C ANISOU 1193 CB TYR A 155 6921 6645 3731 792 -267 210 C ATOM 1194 CG TYR A 155 19.694 0.648 35.720 1.00 48.56 C ANISOU 1194 CG TYR A 155 7390 7096 3964 1024 -327 226 C ATOM 1195 CD1 TYR A 155 20.550 -0.190 35.012 1.00 47.29 C ANISOU 1195 CD1 TYR A 155 7155 7033 3782 1149 -361 233 C ATOM 1196 CD2 TYR A 155 19.510 0.404 37.073 1.00 50.78 C ANISOU 1196 CD2 TYR A 155 7837 7341 4116 1129 -349 235 C ATOM 1197 CE1 TYR A 155 21.200 -1.237 35.646 1.00 50.19 C ANISOU 1197 CE1 TYR A 155 7610 7458 4002 1383 -421 248 C ATOM 1198 CE2 TYR A 155 20.146 -0.636 37.704 1.00 55.52 C ANISOU 1198 CE2 TYR A 155 8537 7995 4563 1360 -406 253 C ATOM 1199 CZ TYR A 155 20.993 -1.452 36.992 1.00 54.24 C ANISOU 1199 CZ TYR A 155 8299 7929 4382 1491 -445 260 C ATOM 1200 OH TYR A 155 21.627 -2.494 37.641 1.00 64.53 O ANISOU 1200 OH TYR A 155 9715 9282 5523 1742 -506 279 O ATOM 1201 N ASN A 156 17.284 -0.978 34.007 1.00 41.61 N ANISOU 1201 N ASN A 156 6758 5798 3254 958 -31 384 N ATOM 1202 CA ASN A 156 16.507 -2.150 34.403 1.00 42.04 C ANISOU 1202 CA ASN A 156 7036 5685 3251 1055 70 445 C ATOM 1203 C ASN A 156 15.007 -1.993 34.142 1.00 42.54 C ANISOU 1203 C ASN A 156 7181 5561 3422 907 202 460 C ATOM 1204 O ASN A 156 14.184 -2.699 34.727 1.00 37.32 O ANISOU 1204 O ASN A 156 6713 4747 2720 942 301 491 O ATOM 1205 CB ASN A 156 16.756 -2.505 35.874 1.00 42.43 C ANISOU 1205 CB ASN A 156 7248 5735 3138 1199 33 453 C ATOM 1206 CG ASN A 156 17.892 -3.503 36.055 1.00 46.26 C ANISOU 1206 CG ASN A 156 7763 6324 3488 1429 -44 470 C ATOM 1207 OD1 ASN A 156 18.400 -4.074 35.087 1.00 45.69 O ANISOU 1207 OD1 ASN A 156 7610 6303 3449 1482 -50 480 O ATOM 1208 ND2 ASN A 156 18.287 -3.725 37.301 1.00 46.87 N ANISOU 1208 ND2 ASN A 156 7964 6436 3409 1575 -104 470 N ATOM 1209 N PHE A 157 14.645 -1.082 33.251 1.00 34.74 N ANISOU 1209 N PHE A 157 6050 4582 2569 746 208 432 N ATOM 1210 CA PHE A 157 13.221 -0.828 32.998 1.00 34.27 C ANISOU 1210 CA PHE A 157 6043 4365 2613 613 317 430 C ATOM 1211 C PHE A 157 12.367 -2.066 32.679 1.00 39.74 C ANISOU 1211 C PHE A 157 6874 4905 3320 649 443 463 C ATOM 1212 O PHE A 157 11.264 -2.222 33.215 1.00 39.59 O ANISOU 1212 O PHE A 157 6982 4744 3315 601 544 458 O ATOM 1213 CB PHE A 157 13.007 0.225 31.904 1.00 34.56 C ANISOU 1213 CB PHE A 157 5913 4436 2784 462 300 401 C ATOM 1214 CG PHE A 157 11.552 0.494 31.639 1.00 34.90 C ANISOU 1214 CG PHE A 157 5998 4333 2929 347 397 388 C ATOM 1215 CD1 PHE A 157 10.853 1.393 32.418 1.00 33.26 C ANISOU 1215 CD1 PHE A 157 5823 4073 2741 262 412 358 C ATOM 1216 CD2 PHE A 157 10.872 -0.206 30.662 1.00 33.95 C ANISOU 1216 CD2 PHE A 157 5888 4132 2880 333 474 396 C ATOM 1217 CE1 PHE A 157 9.507 1.616 32.209 1.00 28.81 C ANISOU 1217 CE1 PHE A 157 5290 3386 2271 169 499 335 C ATOM 1218 CE2 PHE A 157 9.522 0.018 30.441 1.00 35.79 C ANISOU 1218 CE2 PHE A 157 6146 4247 3205 235 557 367 C ATOM 1219 CZ PHE A 157 8.839 0.934 31.220 1.00 29.06 C ANISOU 1219 CZ PHE A 157 5316 3349 2375 156 568 336 C ATOM 1220 N GLU A 158 12.861 -2.928 31.788 1.00 39.15 N ANISOU 1220 N GLU A 158 6771 4858 3245 724 445 486 N ATOM 1221 CA GLU A 158 12.123 -4.131 31.397 1.00 41.29 C ANISOU 1221 CA GLU A 158 7169 4987 3533 753 568 509 C ATOM 1222 C GLU A 158 12.088 -5.260 32.447 1.00 42.89 C ANISOU 1222 C GLU A 158 7602 5091 3605 888 635 546 C ATOM 1223 O GLU A 158 11.262 -6.166 32.344 1.00 40.44 O ANISOU 1223 O GLU A 158 7428 4628 3308 881 767 555 O ATOM 1224 CB GLU A 158 12.671 -4.693 30.078 1.00 38.57 C ANISOU 1224 CB GLU A 158 6729 4700 3227 790 552 519 C ATOM 1225 CG GLU A 158 13.861 -5.632 30.237 1.00 45.27 C ANISOU 1225 CG GLU A 158 7620 5623 3957 977 503 555 C ATOM 1226 CD GLU A 158 15.142 -4.920 30.655 1.00 52.56 C ANISOU 1226 CD GLU A 158 8420 6737 4816 1038 357 541 C ATOM 1227 OE1 GLU A 158 15.149 -3.668 30.747 1.00 47.70 O ANISOU 1227 OE1 GLU A 158 7682 6191 4252 921 299 505 O ATOM 1228 OE2 GLU A 158 16.150 -5.622 30.881 1.00 58.46 O ANISOU 1228 OE2 GLU A 158 9189 7564 5458 1207 301 559 O ATOM 1229 N LYS A 159 12.975 -5.213 33.442 1.00 42.59 N ANISOU 1229 N LYS A 159 7611 5135 3436 1012 550 563 N ATOM 1230 CA LYS A 159 13.171 -6.365 34.350 1.00 42.58 C ANISOU 1230 CA LYS A 159 7841 5054 3284 1182 597 609 C ATOM 1231 C LYS A 159 11.924 -6.806 35.128 1.00 48.05 C ANISOU 1231 C LYS A 159 8757 5540 3960 1133 756 617 C ATOM 1232 O LYS A 159 11.581 -7.995 35.137 1.00 51.60 O ANISOU 1232 O LYS A 159 9389 5851 4365 1199 875 649 O ATOM 1233 CB LYS A 159 14.322 -6.114 35.335 1.00 45.80 C ANISOU 1233 CB LYS A 159 8252 5603 3545 1330 460 614 C ATOM 1234 CG LYS A 159 15.713 -6.278 34.742 1.00 52.07 C ANISOU 1234 CG LYS A 159 8895 6583 4304 1455 329 611 C ATOM 1235 CD LYS A 159 15.747 -7.395 33.723 1.00 60.10 C ANISOU 1235 CD LYS A 159 9943 7542 5350 1516 397 642 C ATOM 1236 CE LYS A 159 17.146 -7.978 33.593 1.00 66.01 C ANISOU 1236 CE LYS A 159 10642 8442 5998 1722 287 651 C ATOM 1237 NZ LYS A 159 18.189 -6.918 33.576 1.00 65.74 N ANISOU 1237 NZ LYS A 159 10369 8637 5971 1707 126 595 N ATOM 1238 N PRO A 160 11.257 -5.859 35.808 1.00 41.89 N ANISOU 1238 N PRO A 160 7970 4734 3211 1016 768 585 N ATOM 1239 CA PRO A 160 10.027 -6.203 36.534 1.00 42.57 C ANISOU 1239 CA PRO A 160 8252 4630 3293 950 931 579 C ATOM 1240 C PRO A 160 8.986 -6.786 35.591 1.00 42.90 C ANISOU 1240 C PRO A 160 8296 4542 3461 840 1075 555 C ATOM 1241 O PRO A 160 8.374 -7.794 35.939 1.00 38.79 O ANISOU 1241 O PRO A 160 7981 3859 2900 859 1226 567 O ATOM 1242 CB PRO A 160 9.531 -4.856 37.061 1.00 41.90 C ANISOU 1242 CB PRO A 160 8080 4577 3265 817 897 532 C ATOM 1243 CG PRO A 160 10.705 -3.950 37.015 1.00 45.41 C ANISOU 1243 CG PRO A 160 8348 5221 3684 857 712 526 C ATOM 1244 CD PRO A 160 11.582 -4.425 35.911 1.00 47.39 C ANISOU 1244 CD PRO A 160 8481 5571 3955 930 645 545 C ATOM 1245 N PHE A 161 8.816 -6.177 34.412 1.00 35.12 N ANISOU 1245 N PHE A 161 7095 3629 2622 729 1029 517 N ATOM 1246 CA PHE A 161 7.828 -6.632 33.430 1.00 34.80 C ANISOU 1246 CA PHE A 161 7026 3490 2708 622 1145 478 C ATOM 1247 C PHE A 161 8.104 -8.025 32.906 1.00 33.89 C ANISOU 1247 C PHE A 161 7017 3309 2550 719 1215 510 C ATOM 1248 O PHE A 161 7.187 -8.825 32.742 1.00 42.69 O ANISOU 1248 O PHE A 161 8240 4276 3705 661 1370 483 O ATOM 1249 CB PHE A 161 7.720 -5.628 32.268 1.00 29.13 C ANISOU 1249 CB PHE A 161 6060 2878 2132 511 1058 436 C ATOM 1250 CG PHE A 161 7.319 -4.256 32.719 1.00 34.88 C ANISOU 1250 CG PHE A 161 6697 3646 2911 408 1007 399 C ATOM 1251 CD1 PHE A 161 5.988 -3.971 33.000 1.00 35.24 C ANISOU 1251 CD1 PHE A 161 6771 3582 3034 287 1113 341 C ATOM 1252 CD2 PHE A 161 8.269 -3.266 32.906 1.00 34.04 C ANISOU 1252 CD2 PHE A 161 6480 3684 2770 432 861 415 C ATOM 1253 CE1 PHE A 161 5.606 -2.712 33.437 1.00 38.82 C ANISOU 1253 CE1 PHE A 161 7150 4066 3531 203 1070 306 C ATOM 1254 CE2 PHE A 161 7.897 -1.994 33.333 1.00 35.07 C ANISOU 1254 CE2 PHE A 161 6540 3839 2945 336 822 379 C ATOM 1255 CZ PHE A 161 6.564 -1.716 33.597 1.00 42.15 C ANISOU 1255 CZ PHE A 161 7475 4623 3919 227 924 329 C ATOM 1256 N LEU A 162 9.368 -8.320 32.631 1.00 34.21 N ANISOU 1256 N LEU A 162 7022 3463 2514 862 1105 559 N ATOM 1257 CA LEU A 162 9.740 -9.661 32.186 1.00 36.52 C ANISOU 1257 CA LEU A 162 7428 3695 2751 978 1165 594 C ATOM 1258 C LEU A 162 9.496 -10.733 33.263 1.00 38.45 C ANISOU 1258 C LEU A 162 7972 3772 2864 1075 1296 632 C ATOM 1259 O LEU A 162 9.012 -11.831 32.963 1.00 41.46 O ANISOU 1259 O LEU A 162 8497 4008 3248 1077 1440 632 O ATOM 1260 CB LEU A 162 11.202 -9.680 31.727 1.00 42.99 C ANISOU 1260 CB LEU A 162 8135 4688 3513 1124 1011 632 C ATOM 1261 CG LEU A 162 11.754 -10.962 31.092 1.00 47.24 C ANISOU 1261 CG LEU A 162 8752 5196 4002 1257 1046 666 C ATOM 1262 CD1 LEU A 162 10.951 -11.371 29.858 1.00 40.82 C ANISOU 1262 CD1 LEU A 162 7885 4304 3321 1135 1146 626 C ATOM 1263 CD2 LEU A 162 13.227 -10.791 30.724 1.00 48.37 C ANISOU 1263 CD2 LEU A 162 8751 5537 4091 1395 882 688 C ATOM 1264 N TRP A 163 9.830 -10.430 34.513 1.00 39.14 N ANISOU 1264 N TRP A 163 8168 3875 2830 1155 1253 662 N ATOM 1265 CA TRP A 163 9.605 -11.402 35.597 1.00 44.96 C ANISOU 1265 CA TRP A 163 9217 4445 3423 1256 1382 705 C ATOM 1266 C TRP A 163 8.116 -11.710 35.763 1.00 48.36 C ANISOU 1266 C TRP A 163 9772 4673 3930 1088 1595 658 C ATOM 1267 O TRP A 163 7.722 -12.873 35.878 1.00 48.97 O ANISOU 1267 O TRP A 163 10072 4576 3958 1117 1759 673 O ATOM 1268 CB TRP A 163 10.199 -10.922 36.923 1.00 42.41 C ANISOU 1268 CB TRP A 163 8982 4184 2949 1370 1288 738 C ATOM 1269 CG TRP A 163 10.126 -11.955 38.032 1.00 50.43 C ANISOU 1269 CG TRP A 163 10342 5035 3786 1510 1406 794 C ATOM 1270 CD1 TRP A 163 11.044 -12.930 38.315 1.00 58.38 C ANISOU 1270 CD1 TRP A 163 11523 6033 4626 1745 1376 861 C ATOM 1271 CD2 TRP A 163 9.074 -12.107 38.994 1.00 47.77 C ANISOU 1271 CD2 TRP A 163 10226 4511 3413 1428 1578 786 C ATOM 1272 NE1 TRP A 163 10.628 -13.678 39.392 1.00 54.53 N ANISOU 1272 NE1 TRP A 163 11369 5356 3993 1818 1520 903 N ATOM 1273 CE2 TRP A 163 9.422 -13.195 39.828 1.00 57.84 C ANISOU 1273 CE2 TRP A 163 11824 5663 4491 1618 1653 857 C ATOM 1274 CE3 TRP A 163 7.872 -11.437 39.227 1.00 48.29 C ANISOU 1274 CE3 TRP A 163 10253 4503 3591 1217 1682 723 C ATOM 1275 CZ2 TRP A 163 8.611 -13.619 40.885 1.00 63.32 C ANISOU 1275 CZ2 TRP A 163 12810 6154 5094 1593 1836 869 C ATOM 1276 CZ3 TRP A 163 7.064 -11.860 40.281 1.00 63.42 C ANISOU 1276 CZ3 TRP A 163 12440 6229 5427 1187 1863 727 C ATOM 1277 CH2 TRP A 163 7.441 -12.942 41.095 1.00 65.36 C ANISOU 1277 CH2 TRP A 163 13014 6348 5473 1369 1943 801 C ATOM 1278 N LEU A 164 7.297 -10.664 35.752 1.00 39.55 N ANISOU 1278 N LEU A 164 8509 3581 2937 910 1596 593 N ATOM 1279 CA LEU A 164 5.851 -10.820 35.853 1.00 44.32 C ANISOU 1279 CA LEU A 164 9182 4022 3635 737 1787 525 C ATOM 1280 C LEU A 164 5.273 -11.575 34.663 1.00 41.79 C ANISOU 1280 C LEU A 164 8816 3631 3432 652 1892 477 C ATOM 1281 O LEU A 164 4.333 -12.349 34.832 1.00 42.54 O ANISOU 1281 O LEU A 164 9067 3551 3547 571 2091 436 O ATOM 1282 CB LEU A 164 5.162 -9.456 35.994 1.00 44.38 C ANISOU 1282 CB LEU A 164 9011 4095 3755 582 1742 460 C ATOM 1283 CG LEU A 164 5.361 -8.684 37.306 1.00 44.34 C ANISOU 1283 CG LEU A 164 9076 4120 3652 616 1688 482 C ATOM 1284 CD1 LEU A 164 4.910 -7.218 37.177 1.00 42.14 C ANISOU 1284 CD1 LEU A 164 8574 3940 3496 478 1603 420 C ATOM 1285 CD2 LEU A 164 4.657 -9.371 38.484 1.00 42.22 C ANISOU 1285 CD2 LEU A 164 9097 3659 3285 612 1879 487 C ATOM 1286 N ALA A 165 5.812 -11.323 33.461 1.00 43.93 N ANISOU 1286 N ALA A 165 8873 4039 3782 662 1765 473 N ATOM 1287 CA ALA A 165 5.363 -12.007 32.250 1.00 45.41 C ANISOU 1287 CA ALA A 165 9002 4180 4074 594 1842 425 C ATOM 1288 C ALA A 165 5.599 -13.498 32.405 1.00 43.19 C ANISOU 1288 C ALA A 165 8971 3751 3686 701 1973 469 C ATOM 1289 O ALA A 165 4.708 -14.319 32.182 1.00 42.92 O ANISOU 1289 O ALA A 165 9044 3562 3702 608 2155 414 O ATOM 1290 CB ALA A 165 6.089 -11.455 30.961 1.00 31.79 C ANISOU 1290 CB ALA A 165 7017 2637 2423 611 1669 428 C ATOM 1291 N ARG A 166 6.809 -13.849 32.807 1.00 45.15 N ANISOU 1291 N ARG A 166 9319 4050 3787 902 1882 561 N ATOM 1292 CA ARG A 166 7.152 -15.246 32.995 1.00 42.60 C ANISOU 1292 CA ARG A 166 9254 3589 3343 1039 1992 613 C ATOM 1293 C ARG A 166 6.274 -15.920 34.064 1.00 47.08 C ANISOU 1293 C ARG A 166 10120 3929 3840 997 2210 608 C ATOM 1294 O ARG A 166 5.960 -17.102 33.956 1.00 49.05 O ANISOU 1294 O ARG A 166 10574 4004 4057 1006 2382 607 O ATOM 1295 CB ARG A 166 8.631 -15.382 33.351 1.00 44.96 C ANISOU 1295 CB ARG A 166 9597 4003 3485 1283 1834 707 C ATOM 1296 CG ARG A 166 9.554 -15.112 32.192 1.00 43.34 C ANISOU 1296 CG ARG A 166 9146 3986 3336 1338 1669 710 C ATOM 1297 CD ARG A 166 10.988 -14.977 32.645 1.00 47.31 C ANISOU 1297 CD ARG A 166 9637 4641 3697 1559 1493 778 C ATOM 1298 NE ARG A 166 11.895 -15.015 31.504 1.00 53.17 N ANISOU 1298 NE ARG A 166 10186 5536 4482 1625 1374 779 N ATOM 1299 CZ ARG A 166 13.179 -14.680 31.556 1.00 61.96 C ANISOU 1299 CZ ARG A 166 11184 6837 5521 1779 1197 808 C ATOM 1300 NH1 ARG A 166 13.712 -14.275 32.701 1.00 60.41 N ANISOU 1300 NH1 ARG A 166 11045 6706 5203 1889 1107 835 N ATOM 1301 NH2 ARG A 166 13.928 -14.741 30.457 1.00 60.40 N ANISOU 1301 NH2 ARG A 166 10809 6767 5372 1820 1112 799 N ATOM 1302 N LYS A 167 5.873 -15.164 35.078 1.00 46.52 N ANISOU 1302 N LYS A 167 10077 3854 3745 944 2213 600 N ATOM 1303 CA LYS A 167 5.060 -15.724 36.162 1.00 43.46 C ANISOU 1303 CA LYS A 167 9978 3253 3281 900 2425 595 C ATOM 1304 C LYS A 167 3.609 -15.888 35.715 1.00 48.42 C ANISOU 1304 C LYS A 167 10568 3757 4073 658 2621 478 C ATOM 1305 O LYS A 167 2.997 -16.920 35.952 1.00 45.81 O ANISOU 1305 O LYS A 167 10471 3221 3713 613 2843 457 O ATOM 1306 CB LYS A 167 5.142 -14.853 37.411 1.00 51.15 C ANISOU 1306 CB LYS A 167 10996 4270 4168 928 2360 622 C ATOM 1307 CG LYS A 167 6.518 -14.836 38.053 1.00 58.70 C ANISOU 1307 CG LYS A 167 12036 5332 4937 1178 2190 725 C ATOM 1308 CD LYS A 167 6.784 -16.121 38.839 1.00 68.09 C ANISOU 1308 CD LYS A 167 13607 6337 5929 1349 2323 802 C ATOM 1309 CE LYS A 167 5.785 -16.295 39.971 1.00 70.20 C ANISOU 1309 CE LYS A 167 14132 6404 6137 1257 2532 787 C ATOM 1310 NZ LYS A 167 6.247 -17.309 40.960 1.00 79.89 N ANISOU 1310 NZ LYS A 167 15749 7477 7127 1464 2619 881 N ATOM 1311 N LEU A 168 3.077 -14.885 35.026 1.00 41.85 N ANISOU 1311 N LEU A 168 9439 3050 3412 506 2540 395 N ATOM 1312 CA LEU A 168 1.686 -14.913 34.576 1.00 47.34 C ANISOU 1312 CA LEU A 168 10054 3661 4271 282 2700 264 C ATOM 1313 C LEU A 168 1.420 -15.929 33.451 1.00 50.39 C ANISOU 1313 C LEU A 168 10434 3978 4733 233 2800 211 C ATOM 1314 O LEU A 168 0.417 -16.642 33.489 1.00 50.20 O ANISOU 1314 O LEU A 168 10523 3790 4760 98 3020 125 O ATOM 1315 CB LEU A 168 1.234 -13.506 34.153 1.00 42.81 C ANISOU 1315 CB LEU A 168 9169 3251 3846 162 2565 192 C ATOM 1316 CG LEU A 168 1.173 -12.482 35.292 1.00 47.59 C ANISOU 1316 CG LEU A 168 9781 3896 4404 160 2511 211 C ATOM 1317 CD1 LEU A 168 1.242 -11.083 34.757 1.00 44.18 C ANISOU 1317 CD1 LEU A 168 9051 3656 4082 113 2318 182 C ATOM 1318 CD2 LEU A 168 -0.077 -12.692 36.150 1.00 54.16 C ANISOU 1318 CD2 LEU A 168 10760 4559 5257 16 2738 131 C ATOM 1319 N ILE A 169 2.305 -15.995 32.456 1.00 48.99 N ANISOU 1319 N ILE A 169 10125 3925 4564 334 2647 254 N ATOM 1320 CA ILE A 169 2.122 -16.939 31.342 1.00 46.43 C ANISOU 1320 CA ILE A 169 9790 3546 4307 296 2730 204 C ATOM 1321 C ILE A 169 2.468 -18.374 31.758 1.00 50.97 C ANISOU 1321 C ILE A 169 10695 3929 4742 406 2890 265 C ATOM 1322 O ILE A 169 1.937 -19.345 31.204 1.00 50.54 O ANISOU 1322 O ILE A 169 10725 3745 4735 327 3055 201 O ATOM 1323 CB ILE A 169 2.915 -16.518 30.088 1.00 42.20 C ANISOU 1323 CB ILE A 169 9003 3203 3828 360 2523 223 C ATOM 1324 CG1 ILE A 169 2.505 -15.102 29.656 1.00 49.37 C ANISOU 1324 CG1 ILE A 169 9613 4278 4869 249 2381 162 C ATOM 1325 CG2 ILE A 169 2.694 -17.505 28.939 1.00 42.23 C ANISOU 1325 CG2 ILE A 169 9002 3147 3896 318 2611 166 C ATOM 1326 CD1 ILE A 169 0.995 -14.891 29.619 1.00 49.47 C ANISOU 1326 CD1 ILE A 169 9558 4220 5018 38 2518 22 C ATOM 1327 N GLY A 170 3.331 -18.508 32.761 1.00 44.33 N ANISOU 1327 N GLY A 170 10053 3067 3724 590 2846 384 N ATOM 1328 CA GLY A 170 3.749 -19.825 33.218 1.00 40.88 C ANISOU 1328 CA GLY A 170 9954 2449 3131 731 2983 457 C ATOM 1329 C GLY A 170 4.771 -20.374 32.243 1.00 50.41 C ANISOU 1329 C GLY A 170 11108 3733 4312 883 2872 508 C ATOM 1330 O GLY A 170 4.719 -21.530 31.868 1.00 56.81 O ANISOU 1330 O GLY A 170 12091 4397 5096 906 3014 503 O ATOM 1331 N ASP A 171 5.693 -19.516 31.816 1.00 48.39 N ANISOU 1331 N ASP A 171 10609 3709 4067 980 2624 549 N ATOM 1332 CA ASP A 171 6.747 -19.908 30.887 1.00 44.55 C ANISOU 1332 CA ASP A 171 10041 3326 3558 1128 2501 594 C ATOM 1333 C ASP A 171 8.073 -19.278 31.311 1.00 46.45 C ANISOU 1333 C ASP A 171 10207 3755 3686 1334 2273 687 C ATOM 1334 O ASP A 171 8.303 -18.086 31.093 1.00 45.40 O ANISOU 1334 O ASP A 171 9810 3815 3626 1287 2103 671 O ATOM 1335 CB ASP A 171 6.382 -19.480 29.461 1.00 41.44 C ANISOU 1335 CB ASP A 171 9348 3049 3349 978 2443 505 C ATOM 1336 CG ASP A 171 7.415 -19.909 28.445 1.00 54.56 C ANISOU 1336 CG ASP A 171 10927 4811 4994 1116 2334 543 C ATOM 1337 OD1 ASP A 171 8.472 -20.437 28.857 1.00 56.14 O ANISOU 1337 OD1 ASP A 171 11271 5015 5045 1336 2283 636 O ATOM 1338 OD2 ASP A 171 7.165 -19.727 27.234 1.00 54.02 O ANISOU 1338 OD2 ASP A 171 10650 4820 5057 1011 2301 477 O ATOM 1339 N PRO A 172 8.951 -20.081 31.921 1.00 50.25 N ANISOU 1339 N PRO A 172 10924 4181 3987 1565 2270 777 N ATOM 1340 CA PRO A 172 10.242 -19.583 32.410 1.00 54.33 C ANISOU 1340 CA PRO A 172 11380 4880 4382 1779 2056 852 C ATOM 1341 C PRO A 172 11.146 -19.101 31.269 1.00 50.83 C ANISOU 1341 C PRO A 172 10631 4667 4015 1820 1863 842 C ATOM 1342 O PRO A 172 12.074 -18.332 31.508 1.00 54.40 O ANISOU 1342 O PRO A 172 10932 5315 4422 1923 1671 869 O ATOM 1343 CB PRO A 172 10.870 -20.815 33.082 1.00 57.03 C ANISOU 1343 CB PRO A 172 12063 5084 4520 2025 2124 938 C ATOM 1344 CG PRO A 172 9.770 -21.811 33.217 1.00 60.62 C ANISOU 1344 CG PRO A 172 12792 5258 4983 1911 2398 913 C ATOM 1345 CD PRO A 172 8.788 -21.526 32.137 1.00 54.91 C ANISOU 1345 CD PRO A 172 11851 4536 4478 1645 2470 807 C ATOM 1346 N ASN A 173 10.873 -19.547 30.048 1.00 44.37 N ANISOU 1346 N ASN A 173 9724 3825 3310 1735 1921 797 N ATOM 1347 CA ASN A 173 11.754 -19.255 28.919 1.00 46.18 C ANISOU 1347 CA ASN A 173 9699 4250 3596 1785 1764 791 C ATOM 1348 C ASN A 173 11.285 -18.088 28.055 1.00 40.56 C ANISOU 1348 C ASN A 173 8673 3675 3062 1577 1685 720 C ATOM 1349 O ASN A 173 11.852 -17.822 26.996 1.00 42.95 O ANISOU 1349 O ASN A 173 8768 4123 3430 1582 1581 705 O ATOM 1350 CB ASN A 173 11.960 -20.510 28.069 1.00 48.47 C ANISOU 1350 CB ASN A 173 10095 4445 3875 1862 1856 795 C ATOM 1351 CG ASN A 173 12.378 -21.702 28.903 1.00 60.25 C ANISOU 1351 CG ASN A 173 11928 5779 5185 2077 1947 868 C ATOM 1352 OD1 ASN A 173 13.332 -21.623 29.676 1.00 58.92 O ANISOU 1352 OD1 ASN A 173 11818 5696 4875 2286 1830 933 O ATOM 1353 ND2 ASN A 173 11.655 -22.809 28.765 1.00 59.57 N ANISOU 1353 ND2 ASN A 173 12075 5460 5097 2029 2160 852 N ATOM 1354 N LEU A 174 10.247 -17.397 28.514 1.00 44.20 N ANISOU 1354 N LEU A 174 9112 4085 3596 1401 1740 675 N ATOM 1355 CA LEU A 174 9.736 -16.231 27.811 1.00 44.36 C ANISOU 1355 CA LEU A 174 8858 4224 3771 1217 1665 609 C ATOM 1356 C LEU A 174 10.809 -15.145 27.735 1.00 44.03 C ANISOU 1356 C LEU A 174 8601 4413 3717 1286 1451 639 C ATOM 1357 O LEU A 174 11.512 -14.897 28.713 1.00 42.04 O ANISOU 1357 O LEU A 174 8405 4217 3351 1409 1371 689 O ATOM 1358 CB LEU A 174 8.473 -15.712 28.503 1.00 42.57 C ANISOU 1358 CB LEU A 174 8669 3898 3606 1045 1764 556 C ATOM 1359 CG LEU A 174 7.740 -14.566 27.815 1.00 51.70 C ANISOU 1359 CG LEU A 174 9573 5148 4924 857 1708 479 C ATOM 1360 CD1 LEU A 174 6.234 -14.671 28.037 1.00 57.87 C ANISOU 1360 CD1 LEU A 174 10417 5778 5794 676 1877 393 C ATOM 1361 CD2 LEU A 174 8.264 -13.226 28.325 1.00 55.34 C ANISOU 1361 CD2 LEU A 174 9889 5767 5371 869 1542 506 C ATOM 1362 N GLU A 175 10.956 -14.532 26.560 1.00 42.66 N ANISOU 1362 N GLU A 175 8187 4369 3652 1207 1364 604 N ATOM 1363 CA GLU A 175 11.919 -13.456 26.354 1.00 44.21 C ANISOU 1363 CA GLU A 175 8167 4778 3853 1238 1181 618 C ATOM 1364 C GLU A 175 11.242 -12.263 25.681 1.00 42.32 C ANISOU 1364 C GLU A 175 7720 4605 3756 1048 1139 561 C ATOM 1365 O GLU A 175 10.251 -12.427 24.975 1.00 38.23 O ANISOU 1365 O GLU A 175 7183 4006 3337 923 1226 507 O ATOM 1366 CB GLU A 175 13.060 -13.939 25.450 1.00 47.40 C ANISOU 1366 CB GLU A 175 8489 5292 4228 1366 1109 641 C ATOM 1367 CG GLU A 175 13.809 -15.158 25.968 1.00 60.70 C ANISOU 1367 CG GLU A 175 10372 6921 5770 1582 1140 696 C ATOM 1368 CD GLU A 175 14.752 -14.825 27.109 1.00 73.46 C ANISOU 1368 CD GLU A 175 12016 8638 7257 1736 1026 738 C ATOM 1369 OE1 GLU A 175 15.021 -13.621 27.320 1.00 75.11 O ANISOU 1369 OE1 GLU A 175 12051 8990 7497 1673 909 721 O ATOM 1370 OE2 GLU A 175 15.222 -15.765 27.793 1.00 76.26 O ANISOU 1370 OE2 GLU A 175 12572 8928 7474 1925 1053 786 O ATOM 1371 N PHE A 176 11.778 -11.063 25.886 1.00 29.96 N ANISOU 1371 N PHE A 176 6000 3187 2196 1029 1006 566 N ATOM 1372 CA PHE A 176 11.332 -9.910 25.107 1.00 34.00 C ANISOU 1372 CA PHE A 176 6316 3772 2829 875 953 521 C ATOM 1373 C PHE A 176 12.186 -9.864 23.849 1.00 38.94 C ANISOU 1373 C PHE A 176 6789 4526 3481 905 877 525 C ATOM 1374 O PHE A 176 13.413 -9.858 23.949 1.00 45.67 O ANISOU 1374 O PHE A 176 7591 5499 4261 1021 789 558 O ATOM 1375 CB PHE A 176 11.497 -8.596 25.890 1.00 35.55 C ANISOU 1375 CB PHE A 176 6431 4055 3021 828 859 522 C ATOM 1376 CG PHE A 176 10.534 -8.431 27.038 1.00 40.07 C ANISOU 1376 CG PHE A 176 7131 4508 3584 770 934 508 C ATOM 1377 CD1 PHE A 176 9.368 -9.185 27.106 1.00 42.61 C ANISOU 1377 CD1 PHE A 176 7585 4663 3943 710 1083 476 C ATOM 1378 CD2 PHE A 176 10.791 -7.503 28.050 1.00 36.31 C ANISOU 1378 CD2 PHE A 176 6639 4090 3065 767 861 516 C ATOM 1379 CE1 PHE A 176 8.479 -9.030 28.176 1.00 40.05 C ANISOU 1379 CE1 PHE A 176 7377 4230 3612 650 1165 456 C ATOM 1380 CE2 PHE A 176 9.905 -7.334 29.117 1.00 33.82 C ANISOU 1380 CE2 PHE A 176 6445 3666 2739 713 935 501 C ATOM 1381 CZ PHE A 176 8.744 -8.094 29.178 1.00 37.98 C ANISOU 1381 CZ PHE A 176 7103 4025 3302 654 1089 472 C ATOM 1382 N VAL A 177 11.562 -9.848 22.671 1.00 36.73 N ANISOU 1382 N VAL A 177 6431 4225 3298 808 911 485 N ATOM 1383 CA VAL A 177 12.341 -9.872 21.425 1.00 37.70 C ANISOU 1383 CA VAL A 177 6427 4459 3440 836 854 488 C ATOM 1384 C VAL A 177 13.052 -8.541 21.169 1.00 38.29 C ANISOU 1384 C VAL A 177 6322 4692 3533 793 731 493 C ATOM 1385 O VAL A 177 14.063 -8.491 20.455 1.00 44.67 O ANISOU 1385 O VAL A 177 7027 5619 4326 842 672 505 O ATOM 1386 CB VAL A 177 11.486 -10.215 20.172 1.00 54.81 C ANISOU 1386 CB VAL A 177 8563 6565 5695 749 918 439 C ATOM 1387 CG1 VAL A 177 10.832 -11.589 20.302 1.00 47.66 C ANISOU 1387 CG1 VAL A 177 7829 5502 4776 776 1053 421 C ATOM 1388 CG2 VAL A 177 10.460 -9.135 19.902 1.00 52.57 C ANISOU 1388 CG2 VAL A 177 8191 6275 5507 599 903 391 C ATOM 1389 N ALA A 178 12.512 -7.468 21.743 1.00 32.94 N ANISOU 1389 N ALA A 178 5612 4011 2891 696 704 478 N ATOM 1390 CA ALA A 178 13.064 -6.124 21.572 1.00 34.74 C ANISOU 1390 CA ALA A 178 5692 4366 3141 635 604 476 C ATOM 1391 C ALA A 178 12.598 -5.209 22.712 1.00 38.41 C ANISOU 1391 C ALA A 178 6180 4806 3607 573 585 468 C ATOM 1392 O ALA A 178 11.502 -5.391 23.247 1.00 36.97 O ANISOU 1392 O ALA A 178 6096 4502 3449 530 655 449 O ATOM 1393 CB ALA A 178 12.645 -5.544 20.214 1.00 29.69 C ANISOU 1393 CB ALA A 178 4948 3745 2588 534 598 450 C ATOM 1394 N MET A 179 13.423 -4.231 23.086 1.00 36.43 N ANISOU 1394 N MET A 179 5839 4672 3332 561 496 473 N ATOM 1395 CA MET A 179 13.028 -3.267 24.118 1.00 39.87 C ANISOU 1395 CA MET A 179 6290 5090 3769 496 473 460 C ATOM 1396 C MET A 179 11.941 -2.355 23.558 1.00 43.64 C ANISOU 1396 C MET A 179 6725 5508 4346 359 492 430 C ATOM 1397 O MET A 179 11.944 -2.051 22.370 1.00 37.10 O ANISOU 1397 O MET A 179 5814 4712 3571 313 480 422 O ATOM 1398 CB MET A 179 14.231 -2.420 24.561 1.00 41.72 C ANISOU 1398 CB MET A 179 6424 5472 3956 507 373 459 C ATOM 1399 CG MET A 179 15.224 -3.140 25.461 1.00 54.77 C ANISOU 1399 CG MET A 179 8121 7193 5497 655 334 476 C ATOM 1400 SD MET A 179 14.591 -3.431 27.141 1.00 51.40 S ANISOU 1400 SD MET A 179 7877 6659 4995 705 367 487 S ATOM 1401 CE MET A 179 14.327 -1.762 27.733 1.00 48.19 C ANISOU 1401 CE MET A 179 7395 6286 4630 562 315 451 C ATOM 1402 N PRO A 180 11.001 -1.913 24.407 1.00 40.69 N ANISOU 1402 N PRO A 180 6416 5051 3995 302 522 409 N ATOM 1403 CA PRO A 180 10.011 -0.959 23.889 1.00 40.97 C ANISOU 1403 CA PRO A 180 6403 5044 4121 189 528 374 C ATOM 1404 C PRO A 180 10.674 0.394 23.627 1.00 36.37 C ANISOU 1404 C PRO A 180 5715 4557 3549 129 445 377 C ATOM 1405 O PRO A 180 11.741 0.645 24.182 1.00 34.45 O ANISOU 1405 O PRO A 180 5441 4404 3245 158 392 393 O ATOM 1406 CB PRO A 180 8.994 -0.838 25.038 1.00 44.14 C ANISOU 1406 CB PRO A 180 6897 5342 4530 155 581 348 C ATOM 1407 CG PRO A 180 9.353 -1.927 26.029 1.00 41.87 C ANISOU 1407 CG PRO A 180 6732 5023 4155 251 623 375 C ATOM 1408 CD PRO A 180 10.804 -2.210 25.839 1.00 42.93 C ANISOU 1408 CD PRO A 180 6820 5277 4216 343 552 415 C ATOM 1409 N ALA A 181 10.085 1.225 22.768 1.00 32.01 N ANISOU 1409 N ALA A 181 5110 3987 3065 51 437 358 N ATOM 1410 CA ALA A 181 10.571 2.587 22.566 1.00 33.52 C ANISOU 1410 CA ALA A 181 5231 4239 3267 -19 379 359 C ATOM 1411 C ALA A 181 10.377 3.378 23.868 1.00 31.09 C ANISOU 1411 C ALA A 181 4958 3908 2945 -58 365 344 C ATOM 1412 O ALA A 181 9.249 3.553 24.322 1.00 28.66 O ANISOU 1412 O ALA A 181 4705 3508 2675 -86 401 318 O ATOM 1413 CB ALA A 181 9.812 3.255 21.444 1.00 32.25 C ANISOU 1413 CB ALA A 181 5044 4039 3172 -75 380 344 C ATOM 1414 N LEU A 182 11.472 3.833 24.465 1.00 35.29 N ANISOU 1414 N LEU A 182 5454 4531 3424 -61 315 351 N ATOM 1415 CA LEU A 182 11.411 4.563 25.729 1.00 32.53 C ANISOU 1415 CA LEU A 182 5137 4173 3051 -95 297 332 C ATOM 1416 C LEU A 182 11.948 5.973 25.587 1.00 32.93 C ANISOU 1416 C LEU A 182 5121 4276 3114 -189 253 316 C ATOM 1417 O LEU A 182 12.805 6.232 24.738 1.00 31.45 O ANISOU 1417 O LEU A 182 4855 4168 2928 -213 231 322 O ATOM 1418 CB LEU A 182 12.266 3.862 26.782 1.00 32.94 C ANISOU 1418 CB LEU A 182 5214 4291 3012 -9 271 340 C ATOM 1419 CG LEU A 182 11.978 2.403 27.096 1.00 38.19 C ANISOU 1419 CG LEU A 182 5971 4903 3636 98 319 362 C ATOM 1420 CD1 LEU A 182 13.063 1.853 28.011 1.00 40.69 C ANISOU 1420 CD1 LEU A 182 6306 5309 3846 202 272 372 C ATOM 1421 CD2 LEU A 182 10.595 2.288 27.732 1.00 38.11 C ANISOU 1421 CD2 LEU A 182 6070 4754 3657 72 391 347 C ATOM 1422 N ALA A 183 11.491 6.869 26.458 1.00 30.30 N ANISOU 1422 N ALA A 183 4826 3897 2788 -246 249 291 N ATOM 1423 CA ALA A 183 12.065 8.209 26.547 1.00 35.13 C ANISOU 1423 CA ALA A 183 5392 4552 3402 -340 215 269 C ATOM 1424 C ALA A 183 13.562 8.096 26.791 1.00 42.45 C ANISOU 1424 C ALA A 183 6236 5624 4267 -328 166 256 C ATOM 1425 O ALA A 183 13.999 7.283 27.609 1.00 41.70 O ANISOU 1425 O ALA A 183 6152 5583 4108 -243 142 255 O ATOM 1426 CB ALA A 183 11.406 8.999 27.659 1.00 32.54 C ANISOU 1426 CB ALA A 183 5128 4157 3077 -386 219 240 C ATOM 1427 N PRO A 184 14.357 8.904 26.069 1.00 47.60 N ANISOU 1427 N PRO A 184 6810 6342 4934 -409 154 241 N ATOM 1428 CA PRO A 184 15.816 8.912 26.220 1.00 51.25 C ANISOU 1428 CA PRO A 184 7166 6959 5348 -415 111 208 C ATOM 1429 C PRO A 184 16.206 9.241 27.656 1.00 43.96 C ANISOU 1429 C PRO A 184 6242 6090 4369 -417 63 161 C ATOM 1430 O PRO A 184 15.564 10.081 28.282 1.00 43.02 O ANISOU 1430 O PRO A 184 6186 5894 4267 -483 73 145 O ATOM 1431 CB PRO A 184 16.269 10.056 25.299 1.00 51.06 C ANISOU 1431 CB PRO A 184 7088 6949 5364 -544 134 190 C ATOM 1432 CG PRO A 184 15.127 10.332 24.397 1.00 48.51 C ANISOU 1432 CG PRO A 184 6845 6487 5098 -564 182 233 C ATOM 1433 CD PRO A 184 13.883 9.931 25.123 1.00 50.41 C ANISOU 1433 CD PRO A 184 7180 6623 5350 -503 186 248 C ATOM 1434 N PRO A 185 17.255 8.592 28.174 1.00 47.29 N ANISOU 1434 N PRO A 185 6595 6651 4722 -338 9 135 N ATOM 1435 CA PRO A 185 17.630 8.823 29.574 1.00 46.98 C ANISOU 1435 CA PRO A 185 6561 6674 4615 -321 -48 85 C ATOM 1436 C PRO A 185 17.877 10.306 29.844 1.00 52.30 C ANISOU 1436 C PRO A 185 7195 7362 5315 -476 -52 22 C ATOM 1437 O PRO A 185 18.439 11.006 28.992 1.00 45.86 O ANISOU 1437 O PRO A 185 6296 6587 4542 -583 -31 -4 O ATOM 1438 CB PRO A 185 18.932 8.036 29.729 1.00 45.11 C ANISOU 1438 CB PRO A 185 6220 6614 4307 -217 -114 54 C ATOM 1439 CG PRO A 185 18.912 7.026 28.635 1.00 50.24 C ANISOU 1439 CG PRO A 185 6861 7251 4978 -139 -81 109 C ATOM 1440 CD PRO A 185 18.147 7.633 27.499 1.00 48.96 C ANISOU 1440 CD PRO A 185 6722 6971 4909 -252 -8 143 C ATOM 1441 N GLU A 186 17.449 10.775 31.015 1.00 49.05 N ANISOU 1441 N GLU A 186 6854 6909 4873 -492 -70 -3 N ATOM 1442 CA GLU A 186 17.688 12.152 31.427 1.00 60.62 C ANISOU 1442 CA GLU A 186 8294 8385 6354 -635 -74 -71 C ATOM 1443 C GLU A 186 18.936 12.231 32.307 1.00 62.13 C ANISOU 1443 C GLU A 186 8381 8757 6468 -625 -155 -160 C ATOM 1444 O GLU A 186 19.505 13.303 32.503 1.00 65.28 O ANISOU 1444 O GLU A 186 8714 9211 6878 -756 -163 -240 O ATOM 1445 CB GLU A 186 16.466 12.708 32.158 1.00 67.75 C ANISOU 1445 CB GLU A 186 9332 9137 7273 -666 -42 -57 C ATOM 1446 CG GLU A 186 15.167 12.505 31.391 1.00 78.03 C ANISOU 1446 CG GLU A 186 10726 10276 8645 -651 28 17 C ATOM 1447 CD GLU A 186 13.962 13.086 32.101 1.00 88.36 C ANISOU 1447 CD GLU A 186 12152 11446 9976 -680 62 18 C ATOM 1448 OE1 GLU A 186 14.145 13.758 33.142 1.00 93.50 O ANISOU 1448 OE1 GLU A 186 12821 12115 10590 -726 38 -35 O ATOM 1449 OE2 GLU A 186 12.832 12.872 31.615 1.00 90.56 O ANISOU 1449 OE2 GLU A 186 12498 11601 10308 -655 113 62 O ATOM 1450 N VAL A 187 19.349 11.085 32.839 1.00 57.71 N ANISOU 1450 N VAL A 187 7811 8288 5827 -466 -216 -152 N ATOM 1451 CA VAL A 187 20.626 10.968 33.528 1.00 56.84 C ANISOU 1451 CA VAL A 187 7583 8378 5637 -419 -310 -241 C ATOM 1452 C VAL A 187 21.303 9.702 33.035 1.00 61.10 C ANISOU 1452 C VAL A 187 8056 9022 6137 -267 -344 -216 C ATOM 1453 O VAL A 187 20.664 8.860 32.410 1.00 51.47 O ANISOU 1453 O VAL A 187 6914 7702 4941 -190 -296 -126 O ATOM 1454 CB VAL A 187 20.461 10.899 35.064 1.00 56.25 C ANISOU 1454 CB VAL A 187 7593 8316 5464 -343 -372 -269 C ATOM 1455 CG1 VAL A 187 19.680 12.105 35.575 1.00 59.01 C ANISOU 1455 CG1 VAL A 187 8023 8546 5852 -485 -330 -290 C ATOM 1456 CG2 VAL A 187 19.780 9.605 35.477 1.00 54.41 C ANISOU 1456 CG2 VAL A 187 7504 8001 5167 -161 -368 -180 C ATOM 1457 N VAL A 188 22.592 9.563 33.317 1.00 73.67 N ANISOU 1457 N VAL A 188 9501 10819 7670 -220 -428 -304 N ATOM 1458 CA VAL A 188 23.321 8.366 32.916 1.00 76.28 C ANISOU 1458 CA VAL A 188 9763 11264 7957 -58 -470 -290 C ATOM 1459 C VAL A 188 23.506 7.412 34.092 1.00 74.52 C ANISOU 1459 C VAL A 188 9611 11101 7600 154 -560 -287 C ATOM 1460 O VAL A 188 23.887 7.823 35.185 1.00 81.84 O ANISOU 1460 O VAL A 188 10521 12119 8454 167 -637 -363 O ATOM 1461 CB VAL A 188 24.697 8.717 32.318 1.00 84.07 C ANISOU 1461 CB VAL A 188 10524 12454 8965 -123 -501 -397 C ATOM 1462 CG1 VAL A 188 25.438 7.456 31.909 1.00 86.12 C ANISOU 1462 CG1 VAL A 188 10710 12833 9177 61 -545 -386 C ATOM 1463 CG2 VAL A 188 24.528 9.645 31.128 1.00 85.57 C ANISOU 1463 CG2 VAL A 188 10670 12569 9275 -329 -398 -393 C ATOM 1464 N MET A 189 23.215 6.136 33.865 1.00 68.93 N ANISOU 1464 N MET A 189 8999 10336 6855 321 -545 -199 N ATOM 1465 CA MET A 189 23.485 5.112 34.862 1.00 66.87 C ANISOU 1465 CA MET A 189 8822 10129 6455 545 -623 -188 C ATOM 1466 C MET A 189 24.911 4.599 34.699 1.00 67.72 C ANISOU 1466 C MET A 189 8757 10468 6504 672 -721 -263 C ATOM 1467 O MET A 189 25.223 3.924 33.719 1.00 67.66 O ANISOU 1467 O MET A 189 8693 10484 6531 725 -694 -233 O ATOM 1468 CB MET A 189 22.496 3.953 34.726 1.00 62.83 C ANISOU 1468 CB MET A 189 8513 9434 5926 665 -548 -63 C ATOM 1469 CG MET A 189 22.598 2.939 35.850 1.00 58.29 C ANISOU 1469 CG MET A 189 8083 8867 5196 891 -606 -37 C ATOM 1470 SD MET A 189 22.267 3.708 37.448 1.00 65.71 S ANISOU 1470 SD MET A 189 9124 9794 6049 866 -654 -81 S ATOM 1471 CE MET A 189 22.731 2.393 38.573 1.00 59.09 C ANISOU 1471 CE MET A 189 8438 9009 5005 1170 -739 -56 C ATOM 1472 N ASP A 190 25.773 4.921 35.658 1.00 73.57 N ANISOU 1472 N ASP A 190 9409 11387 7156 725 -837 -370 N ATOM 1473 CA ASP A 190 27.167 4.489 35.611 1.00 80.02 C ANISOU 1473 CA ASP A 190 10041 12452 7912 856 -945 -466 C ATOM 1474 C ASP A 190 27.276 2.970 35.523 1.00 80.96 C ANISOU 1474 C ASP A 190 10259 12559 7944 1116 -966 -386 C ATOM 1475 O ASP A 190 26.850 2.256 36.432 1.00 78.00 O ANISOU 1475 O ASP A 190 10078 12106 7451 1287 -993 -324 O ATOM 1476 CB ASP A 190 27.930 4.994 36.838 1.00 87.38 C ANISOU 1476 CB ASP A 190 10890 13569 8741 899 -1079 -595 C ATOM 1477 CG ASP A 190 29.386 4.558 36.839 1.00 95.21 C ANISOU 1477 CG ASP A 190 11671 14838 9666 1047 -1204 -715 C ATOM 1478 OD1 ASP A 190 29.992 4.509 35.749 1.00 98.37 O ANISOU 1478 OD1 ASP A 190 11901 15324 10152 993 -1171 -749 O ATOM 1479 OD2 ASP A 190 29.926 4.267 37.928 1.00 99.22 O ANISOU 1479 OD2 ASP A 190 12182 15484 10033 1225 -1335 -780 O ATOM 1480 N PRO A 191 27.848 2.471 34.418 1.00 85.12 N ANISOU 1480 N PRO A 191 10662 13155 8523 1145 -944 -387 N ATOM 1481 CA PRO A 191 28.007 1.031 34.198 1.00 85.94 C ANISOU 1481 CA PRO A 191 10854 13247 8554 1387 -954 -316 C ATOM 1482 C PRO A 191 28.718 0.344 35.358 1.00 89.01 C ANISOU 1482 C PRO A 191 11277 13775 8767 1652 -1094 -359 C ATOM 1483 O PRO A 191 28.521 -0.851 35.576 1.00 88.98 O ANISOU 1483 O PRO A 191 11448 13693 8667 1872 -1094 -273 O ATOM 1484 CB PRO A 191 28.869 0.968 32.936 1.00 84.49 C ANISOU 1484 CB PRO A 191 10451 13195 8455 1345 -938 -368 C ATOM 1485 CG PRO A 191 28.540 2.223 32.203 1.00 83.64 C ANISOU 1485 CG PRO A 191 10249 13036 8493 1049 -850 -394 C ATOM 1486 CD PRO A 191 28.326 3.263 33.270 1.00 85.37 C ANISOU 1486 CD PRO A 191 10485 13263 8690 941 -892 -453 C ATOM 1487 N ALA A 192 29.535 1.095 36.089 1.00 91.47 N ANISOU 1487 N ALA A 192 11431 14290 9032 1634 -1211 -495 N ATOM 1488 CA ALA A 192 30.276 0.543 37.219 1.00 93.52 C ANISOU 1488 CA ALA A 192 11708 14711 9115 1894 -1365 -555 C ATOM 1489 C ALA A 192 29.372 0.377 38.435 1.00 91.75 C ANISOU 1489 C ALA A 192 11762 14323 8776 1974 -1366 -474 C ATOM 1490 O ALA A 192 29.431 -0.638 39.131 1.00 85.15 O ANISOU 1490 O ALA A 192 11099 13472 7784 2238 -1422 -423 O ATOM 1491 CB ALA A 192 31.471 1.425 37.557 1.00 95.68 C ANISOU 1491 CB ALA A 192 11698 15274 9382 1838 -1492 -749 C ATOM 1492 N LEU A 193 28.538 1.383 38.686 1.00 94.84 N ANISOU 1492 N LEU A 193 12207 14589 9240 1748 -1297 -463 N ATOM 1493 CA LEU A 193 27.567 1.318 39.771 1.00 90.55 C ANISOU 1493 CA LEU A 193 11927 13873 8606 1787 -1272 -387 C ATOM 1494 C LEU A 193 26.579 0.192 39.517 1.00 81.49 C ANISOU 1494 C LEU A 193 11041 12479 7442 1888 -1153 -224 C ATOM 1495 O LEU A 193 26.236 -0.559 40.426 1.00 83.89 O ANISOU 1495 O LEU A 193 11578 12694 7601 2073 -1163 -159 O ATOM 1496 CB LEU A 193 26.818 2.642 39.919 1.00 93.12 C ANISOU 1496 CB LEU A 193 12244 14100 9035 1510 -1204 -408 C ATOM 1497 CG LEU A 193 27.590 3.818 40.517 1.00 97.30 C ANISOU 1497 CG LEU A 193 12582 14832 9556 1401 -1311 -569 C ATOM 1498 CD1 LEU A 193 26.667 5.009 40.702 1.00 96.02 C ANISOU 1498 CD1 LEU A 193 12472 14523 9487 1147 -1224 -565 C ATOM 1499 CD2 LEU A 193 28.226 3.420 41.838 1.00102.54 C ANISOU 1499 CD2 LEU A 193 13296 15646 10021 1636 -1467 -633 C ATOM 1500 N ALA A 194 26.124 0.078 38.274 1.00 72.68 N ANISOU 1500 N ALA A 194 9893 11252 6472 1763 -1034 -163 N ATOM 1501 CA ALA A 194 25.194 -0.978 37.907 1.00 73.98 C ANISOU 1501 CA ALA A 194 10281 11189 6638 1835 -912 -24 C ATOM 1502 C ALA A 194 25.824 -2.328 38.210 1.00 77.96 C ANISOU 1502 C ALA A 194 10886 11745 6988 2141 -975 7 C ATOM 1503 O ALA A 194 25.176 -3.222 38.754 1.00 77.24 O ANISOU 1503 O ALA A 194 11063 11485 6799 2279 -917 103 O ATOM 1504 CB ALA A 194 24.822 -0.875 36.436 1.00 69.10 C ANISOU 1504 CB ALA A 194 9569 10492 6193 1668 -800 12 C ATOM 1505 N ALA A 195 27.101 -2.461 37.869 1.00 80.44 N ANISOU 1505 N ALA A 195 10990 12295 7280 2249 -1088 -81 N ATOM 1506 CA ALA A 195 27.838 -3.698 38.104 1.00 80.66 C ANISOU 1506 CA ALA A 195 11087 12400 7160 2559 -1165 -66 C ATOM 1507 C ALA A 195 27.986 -4.001 39.595 1.00 80.16 C ANISOU 1507 C ALA A 195 11201 12365 6891 2776 -1267 -71 C ATOM 1508 O ALA A 195 27.794 -5.140 40.027 1.00 79.22 O ANISOU 1508 O ALA A 195 11329 12134 6635 3008 -1250 18 O ATOM 1509 CB ALA A 195 29.201 -3.637 37.435 1.00 80.81 C ANISOU 1509 CB ALA A 195 10806 12689 7208 2614 -1271 -182 C ATOM 1510 N GLN A 196 28.327 -2.982 40.379 1.00 76.39 N ANISOU 1510 N GLN A 196 10609 12031 6386 2702 -1369 -176 N ATOM 1511 CA GLN A 196 28.518 -3.169 41.809 1.00 77.80 C ANISOU 1511 CA GLN A 196 10943 12257 6361 2904 -1479 -194 C ATOM 1512 C GLN A 196 27.198 -3.425 42.527 1.00 77.95 C ANISOU 1512 C GLN A 196 11302 11993 6324 2885 -1355 -67 C ATOM 1513 O GLN A 196 27.125 -4.285 43.402 1.00 78.71 O ANISOU 1513 O GLN A 196 11650 12020 6234 3126 -1378 -6 O ATOM 1514 CB GLN A 196 29.241 -1.970 42.428 1.00 86.66 C ANISOU 1514 CB GLN A 196 11839 13616 7474 2813 -1620 -355 C ATOM 1515 CG GLN A 196 29.629 -2.175 43.887 1.00 95.98 C ANISOU 1515 CG GLN A 196 13148 14893 8427 3050 -1765 -397 C ATOM 1516 CD GLN A 196 30.543 -3.377 44.092 1.00104.84 C ANISOU 1516 CD GLN A 196 14314 16145 9376 3416 -1886 -400 C ATOM 1517 OE1 GLN A 196 31.426 -3.650 43.278 1.00105.87 O ANISOU 1517 OE1 GLN A 196 14225 16442 9559 3477 -1939 -463 O ATOM 1518 NE2 GLN A 196 30.335 -4.097 45.189 1.00109.95 N ANISOU 1518 NE2 GLN A 196 15254 16711 9810 3667 -1926 -333 N ATOM 1519 N TYR A 197 26.156 -2.679 42.163 1.00 74.22 N ANISOU 1519 N TYR A 197 10842 11354 6007 2603 -1220 -30 N ATOM 1520 CA TYR A 197 24.847 -2.878 42.775 1.00 70.68 C ANISOU 1520 CA TYR A 197 10692 10638 5526 2559 -1086 77 C ATOM 1521 C TYR A 197 24.304 -4.255 42.428 1.00 73.91 C ANISOU 1521 C TYR A 197 11343 10845 5895 2700 -965 207 C ATOM 1522 O TYR A 197 23.637 -4.892 43.244 1.00 79.02 O ANISOU 1522 O TYR A 197 12289 11315 6419 2807 -894 289 O ATOM 1523 CB TYR A 197 23.846 -1.816 42.327 1.00 68.66 C ANISOU 1523 CB TYR A 197 10376 10254 5457 2237 -967 81 C ATOM 1524 CG TYR A 197 24.044 -0.450 42.944 1.00 71.72 C ANISOU 1524 CG TYR A 197 10624 10764 5864 2084 -1047 -27 C ATOM 1525 CD1 TYR A 197 24.567 -0.310 44.220 1.00 78.17 C ANISOU 1525 CD1 TYR A 197 11492 11700 6507 2227 -1176 -89 C ATOM 1526 CD2 TYR A 197 23.677 0.700 42.254 1.00 72.99 C ANISOU 1526 CD2 TYR A 197 10614 10909 6211 1801 -990 -68 C ATOM 1527 CE1 TYR A 197 24.738 0.942 44.785 1.00 82.89 C ANISOU 1527 CE1 TYR A 197 11964 12406 7123 2079 -1245 -196 C ATOM 1528 CE2 TYR A 197 23.841 1.954 42.809 1.00 74.98 C ANISOU 1528 CE2 TYR A 197 10752 11255 6480 1655 -1052 -167 C ATOM 1529 CZ TYR A 197 24.372 2.070 44.073 1.00 81.48 C ANISOU 1529 CZ TYR A 197 11619 12202 7138 1788 -1178 -234 C ATOM 1530 OH TYR A 197 24.538 3.318 44.629 1.00 86.24 O ANISOU 1530 OH TYR A 197 12110 12899 7760 1636 -1236 -343 O ATOM 1531 N GLU A 198 24.591 -4.705 41.210 1.00 71.99 N ANISOU 1531 N GLU A 198 10976 10622 5756 2692 -931 222 N ATOM 1532 CA GLU A 198 24.133 -6.008 40.743 1.00 73.78 C ANISOU 1532 CA GLU A 198 11409 10663 5961 2810 -812 333 C ATOM 1533 C GLU A 198 24.829 -7.125 41.505 1.00 80.77 C ANISOU 1533 C GLU A 198 12477 11590 6622 3156 -895 360 C ATOM 1534 O GLU A 198 24.201 -8.104 41.899 1.00 82.53 O ANISOU 1534 O GLU A 198 13009 11603 6744 3278 -790 462 O ATOM 1535 CB GLU A 198 24.349 -6.153 39.227 1.00 75.59 C ANISOU 1535 CB GLU A 198 11444 10923 6353 2717 -767 330 C ATOM 1536 CG GLU A 198 23.197 -5.583 38.396 1.00 77.50 C ANISOU 1536 CG GLU A 198 11656 10997 6792 2423 -614 363 C ATOM 1537 CD GLU A 198 23.596 -5.198 36.979 1.00 81.92 C ANISOU 1537 CD GLU A 198 11950 11657 7519 2283 -613 322 C ATOM 1538 OE1 GLU A 198 24.695 -5.597 36.535 1.00 83.59 O ANISOU 1538 OE1 GLU A 198 12021 12039 7700 2421 -701 280 O ATOM 1539 OE2 GLU A 198 22.804 -4.493 36.309 1.00 78.11 O ANISOU 1539 OE2 GLU A 198 11404 11083 7193 2042 -521 328 O ATOM 1540 N HIS A 199 26.130 -6.967 41.716 1.00 87.36 N ANISOU 1540 N HIS A 199 13121 12695 7375 3314 -1083 262 N ATOM 1541 CA HIS A 199 26.909 -7.951 42.454 1.00 93.36 C ANISOU 1541 CA HIS A 199 14031 13531 7910 3669 -1193 272 C ATOM 1542 C HIS A 199 26.530 -7.927 43.927 1.00 87.03 C ANISOU 1542 C HIS A 199 13492 12653 6924 3776 -1217 299 C ATOM 1543 O HIS A 199 26.512 -8.963 44.589 1.00 91.31 O ANISOU 1543 O HIS A 199 14327 13091 7274 4037 -1208 376 O ATOM 1544 CB HIS A 199 28.404 -7.680 42.291 1.00105.18 C ANISOU 1544 CB HIS A 199 15217 15366 9379 3799 -1398 135 C ATOM 1545 CG HIS A 199 29.269 -8.505 43.193 1.00116.77 C ANISOU 1545 CG HIS A 199 16812 16953 10602 4178 -1548 120 C ATOM 1546 ND1 HIS A 199 29.471 -9.854 42.999 1.00121.01 N ANISOU 1546 ND1 HIS A 199 17542 17406 11030 4449 -1521 204 N ATOM 1547 CD2 HIS A 199 29.989 -8.169 44.289 1.00119.28 C ANISOU 1547 CD2 HIS A 199 17097 17469 10755 4343 -1730 28 C ATOM 1548 CE1 HIS A 199 30.276 -10.316 43.939 1.00122.98 C ANISOU 1548 CE1 HIS A 199 17879 17794 11053 4776 -1683 168 C ATOM 1549 NE2 HIS A 199 30.606 -9.313 44.734 1.00122.02 N ANISOU 1549 NE2 HIS A 199 17617 17851 10892 4720 -1816 59 N ATOM 1550 N ASP A 200 26.225 -6.735 44.429 1.00 80.42 N ANISOU 1550 N ASP A 200 12558 11858 6138 3573 -1241 237 N ATOM 1551 CA ASP A 200 25.814 -6.556 45.816 1.00 79.48 C ANISOU 1551 CA ASP A 200 12672 11671 5857 3637 -1258 252 C ATOM 1552 C ASP A 200 24.553 -7.363 46.132 1.00 76.11 C ANISOU 1552 C ASP A 200 12630 10909 5381 3642 -1054 399 C ATOM 1553 O ASP A 200 24.435 -7.944 47.213 1.00 75.79 O ANISOU 1553 O ASP A 200 12885 10782 5129 3846 -1057 451 O ATOM 1554 CB ASP A 200 25.586 -5.071 46.119 1.00 81.80 C ANISOU 1554 CB ASP A 200 12781 12045 6254 3371 -1291 159 C ATOM 1555 CG ASP A 200 26.886 -4.302 46.312 1.00 87.29 C ANISOU 1555 CG ASP A 200 13166 13077 6922 3414 -1509 -3 C ATOM 1556 OD1 ASP A 200 27.941 -4.948 46.481 1.00 89.17 O ANISOU 1556 OD1 ASP A 200 13364 13493 7022 3690 -1654 -46 O ATOM 1557 OD2 ASP A 200 26.852 -3.051 46.304 1.00 90.09 O ANISOU 1557 OD2 ASP A 200 13318 13519 7393 3174 -1534 -96 O ATOM 1558 N LEU A 201 23.618 -7.399 45.183 1.00 71.37 N ANISOU 1558 N LEU A 201 12026 10122 4970 3417 -873 458 N ATOM 1559 CA LEU A 201 22.359 -8.125 45.362 1.00 69.87 C ANISOU 1559 CA LEU A 201 12167 9615 4766 3379 -659 578 C ATOM 1560 C LEU A 201 22.538 -9.653 45.357 1.00 76.36 C ANISOU 1560 C LEU A 201 13257 10316 5440 3653 -605 672 C ATOM 1561 O LEU A 201 21.855 -10.375 46.091 1.00 73.89 O ANISOU 1561 O LEU A 201 13296 9782 4995 3742 -480 759 O ATOM 1562 CB LEU A 201 21.339 -7.701 44.302 1.00 62.67 C ANISOU 1562 CB LEU A 201 11146 8563 4102 3065 -495 595 C ATOM 1563 CG LEU A 201 20.767 -6.288 44.470 1.00 67.90 C ANISOU 1563 CG LEU A 201 11655 9247 4894 2788 -489 532 C ATOM 1564 CD1 LEU A 201 20.017 -5.807 43.214 1.00 60.19 C ANISOU 1564 CD1 LEU A 201 10508 8192 4169 2508 -372 531 C ATOM 1565 CD2 LEU A 201 19.879 -6.217 45.708 1.00 63.04 C ANISOU 1565 CD2 LEU A 201 11318 8464 4170 2775 -401 569 C ATOM 1566 N GLU A 202 23.455 -10.138 44.528 1.00 79.78 N ANISOU 1566 N GLU A 202 13531 10887 5893 3784 -689 651 N ATOM 1567 CA GLU A 202 23.757 -11.563 44.475 1.00 85.60 C ANISOU 1567 CA GLU A 202 14506 11531 6489 4063 -655 731 C ATOM 1568 C GLU A 202 24.497 -11.988 45.732 1.00 88.12 C ANISOU 1568 C GLU A 202 15018 11934 6529 4397 -796 732 C ATOM 1569 O GLU A 202 24.190 -13.019 46.326 1.00 92.22 O ANISOU 1569 O GLU A 202 15907 12259 6874 4593 -706 829 O ATOM 1570 CB GLU A 202 24.587 -11.886 43.235 1.00 87.68 C ANISOU 1570 CB GLU A 202 14521 11940 6854 4112 -716 696 C ATOM 1571 CG GLU A 202 23.863 -11.583 41.936 1.00 93.12 C ANISOU 1571 CG GLU A 202 15046 12534 7799 3809 -575 703 C ATOM 1572 CD GLU A 202 24.760 -11.694 40.717 1.00 99.49 C ANISOU 1572 CD GLU A 202 15570 13519 8712 3833 -650 651 C ATOM 1573 OE1 GLU A 202 25.994 -11.791 40.888 1.00104.14 O ANISOU 1573 OE1 GLU A 202 16027 14342 9200 4052 -828 587 O ATOM 1574 OE2 GLU A 202 24.226 -11.678 39.586 1.00 97.95 O ANISOU 1574 OE2 GLU A 202 15281 13236 8701 3634 -532 668 O ATOM 1575 N VAL A 203 25.479 -11.186 46.132 1.00 86.63 N ANISOU 1575 N VAL A 203 14583 12038 6295 4461 -1016 617 N ATOM 1576 CA VAL A 203 26.197 -11.433 47.371 1.00 94.25 C ANISOU 1576 CA VAL A 203 15700 13117 6994 4772 -1177 596 C ATOM 1577 C VAL A 203 25.203 -11.543 48.515 1.00 95.51 C ANISOU 1577 C VAL A 203 16234 13037 7017 4765 -1054 680 C ATOM 1578 O VAL A 203 25.282 -12.451 49.338 1.00100.73 O ANISOU 1578 O VAL A 203 17237 13595 7440 5047 -1049 753 O ATOM 1579 CB VAL A 203 27.198 -10.304 47.678 1.00 97.68 C ANISOU 1579 CB VAL A 203 15785 13897 7432 4760 -1413 437 C ATOM 1580 CG1 VAL A 203 27.761 -10.458 49.081 1.00101.81 C ANISOU 1580 CG1 VAL A 203 16487 14524 7673 5059 -1574 410 C ATOM 1581 CG2 VAL A 203 28.316 -10.290 46.654 1.00100.04 C ANISOU 1581 CG2 VAL A 203 15728 14450 7832 4809 -1541 343 C ATOM 1582 N ALA A 204 24.256 -10.612 48.548 1.00 92.36 N ANISOU 1582 N ALA A 204 15778 12546 6769 4443 -947 669 N ATOM 1583 CA ALA A 204 23.266 -10.560 49.616 1.00 90.70 C ANISOU 1583 CA ALA A 204 15887 12121 6454 4394 -821 731 C ATOM 1584 C ALA A 204 22.297 -11.735 49.559 1.00 93.68 C ANISOU 1584 C ALA A 204 16647 12159 6789 4422 -576 870 C ATOM 1585 O ALA A 204 21.950 -12.308 50.591 1.00 97.01 O ANISOU 1585 O ALA A 204 17440 12417 7003 4578 -506 941 O ATOM 1586 CB ALA A 204 22.508 -9.232 49.580 1.00 86.03 C ANISOU 1586 CB ALA A 204 15110 11526 6052 4037 -769 672 C ATOM 1587 N GLN A 205 21.875 -12.098 48.351 1.00 96.04 N ANISOU 1587 N GLN A 205 16860 12350 7280 4272 -441 902 N ATOM 1588 CA GLN A 205 20.949 -13.212 48.174 1.00105.17 C ANISOU 1588 CA GLN A 205 18351 13187 8421 4270 -196 1016 C ATOM 1589 C GLN A 205 21.515 -14.519 48.736 1.00112.60 C ANISOU 1589 C GLN A 205 19632 14053 9096 4647 -212 1096 C ATOM 1590 O GLN A 205 20.780 -15.487 48.947 1.00117.08 O ANISOU 1590 O GLN A 205 20566 14335 9585 4688 -5 1195 O ATOM 1591 CB GLN A 205 20.585 -13.399 46.701 1.00106.43 C ANISOU 1591 CB GLN A 205 18324 13288 8825 4073 -84 1019 C ATOM 1592 CG GLN A 205 19.519 -14.456 46.456 1.00110.11 C ANISOU 1592 CG GLN A 205 19105 13423 9307 4017 185 1116 C ATOM 1593 CD GLN A 205 18.211 -14.108 47.141 1.00111.22 C ANISOU 1593 CD GLN A 205 19436 13351 9473 3802 371 1136 C ATOM 1594 OE1 GLN A 205 17.639 -13.041 46.901 1.00110.38 O ANISOU 1594 OE1 GLN A 205 19105 13288 9547 3527 384 1075 O ATOM 1595 NE2 GLN A 205 17.728 -15.005 47.993 1.00111.69 N ANISOU 1595 NE2 GLN A 205 19917 13172 9348 3930 524 1219 N ATOM 1596 N THR A 206 22.820 -14.545 48.990 1.00115.01 N ANISOU 1596 N THR A 206 19823 14615 9260 4926 -454 1046 N ATOM 1597 CA THR A 206 23.445 -15.698 49.631 1.00115.32 C ANISOU 1597 CA THR A 206 20185 14610 9020 5324 -502 1113 C ATOM 1598 C THR A 206 23.777 -15.387 51.086 1.00117.27 C ANISOU 1598 C THR A 206 20601 14940 9017 5519 -637 1096 C ATOM 1599 O THR A 206 24.935 -15.431 51.498 1.00117.74 O ANISOU 1599 O THR A 206 20586 15238 8910 5812 -872 1042 O ATOM 1600 CB THR A 206 24.736 -16.129 48.888 1.00 96.73 C ANISOU 1600 CB THR A 206 17610 12488 6656 5560 -685 1067 C ATOM 1601 OG1 THR A 206 25.832 -15.298 49.295 1.00100.58 O ANISOU 1601 OG1 THR A 206 17806 13324 7085 5673 -963 944 O ATOM 1602 CG2 THR A 206 24.550 -16.034 47.377 1.00 86.95 C ANISOU 1602 CG2 THR A 206 16082 11254 5701 5315 -603 1045 C ATOM 1603 N THR A 207 22.748 -15.076 51.865 1.00120.44 N ANISOU 1603 N THR A 207 21226 15147 9389 5359 -487 1136 N ATOM 1604 CA THR A 207 22.937 -14.771 53.274 1.00123.20 C ANISOU 1604 CA THR A 207 21765 15547 9497 5524 -591 1125 C ATOM 1605 C THR A 207 21.664 -15.042 54.071 1.00124.51 C ANISOU 1605 C THR A 207 22344 15380 9583 5415 -336 1221 C ATOM 1606 O THR A 207 21.690 -15.150 55.297 1.00125.60 O ANISOU 1606 O THR A 207 22777 15475 9473 5597 -363 1250 O ATOM 1607 CB THR A 207 23.362 -13.303 53.478 1.00121.83 C ANISOU 1607 CB THR A 207 21202 15670 9419 5370 -792 984 C ATOM 1608 OG1 THR A 207 24.440 -12.981 52.589 1.00117.55 O ANISOU 1608 OG1 THR A 207 20242 15424 8996 5403 -991 884 O ATOM 1609 CG2 THR A 207 23.803 -13.066 54.914 1.00124.78 C ANISOU 1609 CG2 THR A 207 21750 16146 9515 5600 -947 957 C TER 1610 THR A 207 ATOM 1611 N GLY B 723 -20.536 -13.903 27.576 1.00165.81 N ANISOU 1611 N GLY B 723 19099 22115 21787 -3502 3241 -5292 N ATOM 1612 CA GLY B 723 -19.115 -13.610 27.615 1.00162.41 C ANISOU 1612 CA GLY B 723 18929 21486 21292 -3374 3176 -4942 C ATOM 1613 C GLY B 723 -18.804 -12.299 28.313 1.00159.47 C ANISOU 1613 C GLY B 723 18484 21048 21059 -3269 3195 -4929 C ATOM 1614 O GLY B 723 -19.611 -11.369 28.300 1.00164.25 O ANISOU 1614 O GLY B 723 18800 21752 21855 -3152 3172 -5141 O ATOM 1615 N THR B 724 -17.625 -12.224 28.922 1.00147.81 N ANISOU 1615 N THR B 724 17272 19399 19490 -3307 3230 -4680 N ATOM 1616 CA THR B 724 -17.204 -11.031 29.649 1.00135.44 C ANISOU 1616 CA THR B 724 15678 17750 18034 -3220 3253 -4632 C ATOM 1617 C THR B 724 -16.969 -9.848 28.708 1.00123.17 C ANISOU 1617 C THR B 724 13983 16174 16641 -2822 3047 -4513 C ATOM 1618 O THR B 724 -17.047 -9.995 27.490 1.00120.05 O ANISOU 1618 O THR B 724 13540 15809 16263 -2622 2888 -4448 O ATOM 1619 CB THR B 724 -15.931 -11.305 30.471 1.00133.13 C ANISOU 1619 CB THR B 724 15727 17261 17596 -3353 3326 -4374 C ATOM 1620 OG1 THR B 724 -14.823 -11.506 29.587 1.00132.40 O ANISOU 1620 OG1 THR B 724 15832 17042 17433 -3147 3172 -4048 O ATOM 1621 CG2 THR B 724 -16.113 -12.546 31.336 1.00132.83 C ANISOU 1621 CG2 THR B 724 15867 17224 17377 -3754 3502 -4479 C ATOM 1622 N TRP B 725 -16.688 -8.676 29.274 1.00116.28 N ANISOU 1622 N TRP B 725 13055 15243 15882 -2714 3046 -4483 N ATOM 1623 CA TRP B 725 -16.497 -7.466 28.472 1.00111.79 C ANISOU 1623 CA TRP B 725 12358 14653 15463 -2350 2846 -4386 C ATOM 1624 C TRP B 725 -15.448 -6.513 29.058 1.00100.96 C ANISOU 1624 C TRP B 725 11123 13128 14111 -2244 2833 -4160 C ATOM 1625 O TRP B 725 -15.247 -6.466 30.270 1.00101.88 O ANISOU 1625 O TRP B 725 11324 13192 14194 -2447 2996 -4183 O ATOM 1626 CB TRP B 725 -17.829 -6.732 28.282 1.00116.09 C ANISOU 1626 CB TRP B 725 12535 15362 16210 -2256 2800 -4717 C ATOM 1627 CG TRP B 725 -18.465 -6.287 29.565 1.00122.05 C ANISOU 1627 CG TRP B 725 13146 16182 17046 -2450 2977 -4973 C ATOM 1628 CD1 TRP B 725 -19.176 -7.059 30.438 1.00125.12 C ANISOU 1628 CD1 TRP B 725 13499 16663 17376 -2790 3190 -5218 C ATOM 1629 CD2 TRP B 725 -18.452 -4.964 30.119 1.00124.55 C ANISOU 1629 CD2 TRP B 725 13337 16475 17510 -2321 2956 -5014 C ATOM 1630 NE1 TRP B 725 -19.604 -6.300 31.502 1.00127.89 N ANISOU 1630 NE1 TRP B 725 13709 17050 17834 -2887 3313 -5414 N ATOM 1631 CE2 TRP B 725 -19.173 -5.011 31.330 1.00127.64 C ANISOU 1631 CE2 TRP B 725 13617 16948 17932 -2598 3170 -5291 C ATOM 1632 CE3 TRP B 725 -17.901 -3.747 29.709 1.00123.39 C ANISOU 1632 CE3 TRP B 725 13170 16247 17465 -2006 2774 -4844 C ATOM 1633 CZ2 TRP B 725 -19.356 -3.888 32.134 1.00128.73 C ANISOU 1633 CZ2 TRP B 725 13616 17089 18205 -2560 3210 -5402 C ATOM 1634 CZ3 TRP B 725 -18.084 -2.632 30.510 1.00125.74 C ANISOU 1634 CZ3 TRP B 725 13335 16548 17893 -1966 2805 -4950 C ATOM 1635 CH2 TRP B 725 -18.805 -2.711 31.708 1.00128.08 C ANISOU 1635 CH2 TRP B 725 13514 16926 18223 -2237 3022 -5225 C ATOM 1636 N ASP B 726 -14.789 -5.759 28.182 1.00 90.15 N ANISOU 1636 N ASP B 726 9779 11684 12788 -1932 2638 -3942 N ATOM 1637 CA ASP B 726 -13.768 -4.793 28.589 1.00 89.78 C ANISOU 1637 CA ASP B 726 9858 11495 12760 -1797 2600 -3711 C ATOM 1638 C ASP B 726 -14.351 -3.410 28.855 1.00 81.24 C ANISOU 1638 C ASP B 726 8531 10470 11865 -1641 2540 -3867 C ATOM 1639 O ASP B 726 -15.114 -2.890 28.042 1.00 79.73 O ANISOU 1639 O ASP B 726 8113 10379 11803 -1450 2390 -4014 O ATOM 1640 CB ASP B 726 -12.696 -4.665 27.504 1.00 96.23 C ANISOU 1640 CB ASP B 726 10844 12201 13519 -1548 2418 -3391 C ATOM 1641 CG ASP B 726 -11.469 -5.495 27.795 1.00107.30 C ANISOU 1641 CG ASP B 726 12571 13451 14745 -1673 2493 -3122 C ATOM 1642 OD1 ASP B 726 -11.581 -6.476 28.561 1.00113.24 O ANISOU 1642 OD1 ASP B 726 13427 14201 15399 -1961 2660 -3197 O ATOM 1643 OD2 ASP B 726 -10.389 -5.161 27.258 1.00109.00 O ANISOU 1643 OD2 ASP B 726 12944 13548 14922 -1487 2379 -2844 O ATOM 1644 N CYS B 727 -13.983 -2.805 29.981 1.00 77.69 N ANISOU 1644 N CYS B 727 8135 9949 11435 -1716 2646 -3833 N ATOM 1645 CA CYS B 727 -14.392 -1.428 30.242 1.00 69.84 C ANISOU 1645 CA CYS B 727 6934 8991 10612 -1548 2574 -3946 C ATOM 1646 C CYS B 727 -13.619 -0.459 29.355 1.00 65.64 C ANISOU 1646 C CYS B 727 6454 8373 10114 -1206 2340 -3695 C ATOM 1647 O CYS B 727 -12.393 -0.502 29.284 1.00 59.72 O ANISOU 1647 O CYS B 727 5960 7476 9255 -1154 2315 -3380 O ATOM 1648 CB CYS B 727 -14.203 -1.037 31.708 1.00 65.48 C ANISOU 1648 CB CYS B 727 6432 8381 10066 -1727 2754 -3973 C ATOM 1649 SG CYS B 727 -14.475 0.738 31.959 1.00 67.73 S ANISOU 1649 SG CYS B 727 6501 8686 10548 -1476 2635 -4048 S ATOM 1650 N ASP B 728 -14.350 0.426 28.690 1.00 67.96 N ANISOU 1650 N ASP B 728 6506 8754 10560 -980 2163 -3847 N ATOM 1651 CA ASP B 728 -13.747 1.392 27.786 1.00 72.88 C ANISOU 1651 CA ASP B 728 7170 9306 11217 -660 1920 -3642 C ATOM 1652 C ASP B 728 -13.025 2.502 28.549 1.00 65.48 C ANISOU 1652 C ASP B 728 6309 8266 10304 -574 1914 -3487 C ATOM 1653 O ASP B 728 -12.252 3.258 27.974 1.00 63.64 O ANISOU 1653 O ASP B 728 6178 7944 10056 -343 1740 -3256 O ATOM 1654 CB ASP B 728 -14.824 1.993 26.881 1.00 89.79 C ANISOU 1654 CB ASP B 728 9034 11563 13518 -458 1717 -3877 C ATOM 1655 CG ASP B 728 -14.315 2.288 25.485 1.00 97.45 C ANISOU 1655 CG ASP B 728 10095 12472 14461 -193 1464 -3674 C ATOM 1656 OD1 ASP B 728 -13.090 2.471 25.321 1.00 94.34 O ANISOU 1656 OD1 ASP B 728 9943 11945 13955 -112 1424 -3353 O ATOM 1657 OD2 ASP B 728 -15.143 2.332 24.549 1.00103.99 O ANISOU 1657 OD2 ASP B 728 10755 13379 15378 -74 1307 -3842 O ATOM 1658 N THR B 729 -13.276 2.601 29.848 1.00 63.97 N ANISOU 1658 N THR B 729 6076 8087 10144 -766 2104 -3613 N ATOM 1659 CA THR B 729 -12.688 3.684 30.632 1.00 60.36 C ANISOU 1659 CA THR B 729 5675 7538 9721 -690 2102 -3485 C ATOM 1660 C THR B 729 -11.367 3.291 31.283 1.00 56.98 C ANISOU 1660 C THR B 729 5571 6940 9140 -811 2228 -3171 C ATOM 1661 O THR B 729 -10.380 4.024 31.181 1.00 54.72 O ANISOU 1661 O THR B 729 5433 6535 8824 -639 2126 -2902 O ATOM 1662 CB THR B 729 -13.670 4.233 31.702 1.00 61.18 C ANISOU 1662 CB THR B 729 5546 7738 9963 -802 2220 -3793 C ATOM 1663 OG1 THR B 729 -14.736 4.937 31.053 1.00 60.46 O ANISOU 1663 OG1 THR B 729 5154 7779 10041 -613 2046 -4053 O ATOM 1664 CG2 THR B 729 -12.954 5.186 32.645 1.00 57.02 C ANISOU 1664 CG2 THR B 729 5123 7099 9444 -766 2254 -3631 C ATOM 1665 N CYS B 730 -11.350 2.137 31.946 1.00 59.22 N ANISOU 1665 N CYS B 730 5968 7207 9326 -1108 2440 -3210 N ATOM 1666 CA CYS B 730 -10.170 1.710 32.696 1.00 56.18 C ANISOU 1666 CA CYS B 730 5891 6650 8807 -1253 2565 -2946 C ATOM 1667 C CYS B 730 -9.590 0.381 32.212 1.00 55.75 C ANISOU 1667 C CYS B 730 6047 6537 8598 -1368 2599 -2803 C ATOM 1668 O CYS B 730 -8.595 -0.096 32.755 1.00 51.71 O ANISOU 1668 O CYS B 730 5799 5874 7973 -1491 2687 -2592 O ATOM 1669 CB CYS B 730 -10.488 1.615 34.191 1.00 51.28 C ANISOU 1669 CB CYS B 730 5275 6012 8196 -1533 2793 -3092 C ATOM 1670 SG CYS B 730 -11.382 0.125 34.646 1.00 57.62 S ANISOU 1670 SG CYS B 730 6052 6912 8927 -1912 3008 -3368 S ATOM 1671 N LEU B 731 -10.228 -0.218 31.212 1.00 57.66 N ANISOU 1671 N LEU B 731 6174 6896 8839 -1330 2525 -2927 N ATOM 1672 CA LEU B 731 -9.729 -1.449 30.591 1.00 54.30 C ANISOU 1672 CA LEU B 731 5930 6430 8272 -1407 2529 -2798 C ATOM 1673 C LEU B 731 -9.863 -2.720 31.437 1.00 58.43 C ANISOU 1673 C LEU B 731 6579 6938 8684 -1759 2739 -2888 C ATOM 1674 O LEU B 731 -9.325 -3.762 31.071 1.00 59.77 O ANISOU 1674 O LEU B 731 6934 7050 8724 -1840 2748 -2761 O ATOM 1675 CB LEU B 731 -8.269 -1.277 30.166 1.00 50.31 C ANISOU 1675 CB LEU B 731 5677 5759 7681 -1250 2431 -2432 C ATOM 1676 CG LEU B 731 -7.999 -0.131 29.206 1.00 53.39 C ANISOU 1676 CG LEU B 731 5994 6150 8143 -914 2210 -2310 C ATOM 1677 CD1 LEU B 731 -6.558 -0.182 28.738 1.00 53.46 C ANISOU 1677 CD1 LEU B 731 6262 6005 8045 -799 2136 -1964 C ATOM 1678 CD2 LEU B 731 -8.960 -0.196 28.034 1.00 58.49 C ANISOU 1678 CD2 LEU B 731 6431 6943 8851 -786 2072 -2488 C ATOM 1679 N VAL B 732 -10.562 -2.643 32.567 1.00 61.58 N ANISOU 1679 N VAL B 732 6887 7383 9128 -1975 2904 -3108 N ATOM 1680 CA VAL B 732 -10.772 -3.829 33.396 1.00 63.20 C ANISOU 1680 CA VAL B 732 7216 7578 9220 -2333 3101 -3218 C ATOM 1681 C VAL B 732 -11.788 -4.763 32.739 1.00 72.30 C ANISOU 1681 C VAL B 732 8224 8895 10350 -2427 3108 -3448 C ATOM 1682 O VAL B 732 -12.726 -4.308 32.084 1.00 72.15 O ANISOU 1682 O VAL B 732 7931 9028 10453 -2280 3022 -3640 O ATOM 1683 CB VAL B 732 -11.230 -3.461 34.838 1.00 56.06 C ANISOU 1683 CB VAL B 732 6268 6671 8362 -2561 3287 -3396 C ATOM 1684 CG1 VAL B 732 -11.886 -4.645 35.519 1.00 59.10 C ANISOU 1684 CG1 VAL B 732 6696 7110 8650 -2936 3478 -3615 C ATOM 1685 CG2 VAL B 732 -10.044 -2.978 35.660 1.00 64.38 C ANISOU 1685 CG2 VAL B 732 7565 7517 9379 -2563 3318 -3131 C ATOM 1686 N GLN B 733 -11.591 -6.068 32.902 1.00 81.28 N ANISOU 1686 N GLN B 733 9555 9995 11333 -2667 3200 -3425 N ATOM 1687 CA GLN B 733 -12.531 -7.049 32.367 1.00 92.18 C ANISOU 1687 CA GLN B 733 10826 11527 12672 -2788 3221 -3636 C ATOM 1688 C GLN B 733 -13.628 -7.369 33.374 1.00 98.31 C ANISOU 1688 C GLN B 733 11480 12417 13459 -3101 3418 -3967 C ATOM 1689 O GLN B 733 -13.347 -7.791 34.494 1.00 99.25 O ANISOU 1689 O GLN B 733 11784 12443 13482 -3380 3576 -3967 O ATOM 1690 CB GLN B 733 -11.812 -8.341 31.974 1.00 98.77 C ANISOU 1690 CB GLN B 733 11929 12276 13325 -2890 3208 -3457 C ATOM 1691 CG GLN B 733 -12.758 -9.507 31.715 1.00107.93 C ANISOU 1691 CG GLN B 733 13024 13576 14407 -3094 3269 -3679 C ATOM 1692 CD GLN B 733 -12.061 -10.856 31.755 1.00114.30 C ANISOU 1692 CD GLN B 733 14135 14279 15013 -3285 3298 -3532 C ATOM 1693 OE1 GLN B 733 -12.673 -11.875 32.082 1.00114.89 O ANISOU 1693 OE1 GLN B 733 14244 14424 14984 -3561 3403 -3704 O ATOM 1694 NE2 GLN B 733 -10.774 -10.868 31.427 1.00116.27 N ANISOU 1694 NE2 GLN B 733 14610 14363 15206 -3142 3200 -3220 N ATOM 1695 N ASN B 734 -14.876 -7.167 32.966 1.00104.63 N ANISOU 1695 N ASN B 734 11970 13410 14373 -3061 3405 -4256 N ATOM 1696 CA ASN B 734 -16.024 -7.490 33.803 1.00113.57 C ANISOU 1696 CA ASN B 734 12950 14678 15524 -3356 3591 -4606 C ATOM 1697 C ASN B 734 -16.757 -8.711 33.265 1.00125.35 C ANISOU 1697 C ASN B 734 14406 16296 16924 -3512 3617 -4766 C ATOM 1698 O ASN B 734 -16.759 -8.953 32.061 1.00125.33 O ANISOU 1698 O ASN B 734 14360 16333 16925 -3310 3460 -4686 O ATOM 1699 CB ASN B 734 -16.986 -6.303 33.864 1.00112.94 C ANISOU 1699 CB ASN B 734 12518 14733 15661 -3213 3570 -4860 C ATOM 1700 CG ASN B 734 -16.395 -5.110 34.586 1.00110.33 C ANISOU 1700 CG ASN B 734 12214 14290 15414 -3106 3572 -4743 C ATOM 1701 OD1 ASN B 734 -16.040 -4.107 33.965 1.00111.73 O ANISOU 1701 OD1 ASN B 734 12317 14436 15700 -2780 3395 -4606 O ATOM 1702 ND2 ASN B 734 -16.280 -5.214 35.904 1.00106.91 N ANISOU 1702 ND2 ASN B 734 11903 13792 14925 -3388 3769 -4794 N ATOM 1703 N LYS B 735 -17.378 -9.481 34.153 1.00135.38 N ANISOU 1703 N LYS B 735 15702 17629 18107 -3878 3814 -4990 N ATOM 1704 CA LYS B 735 -18.173 -10.625 33.718 1.00142.19 C ANISOU 1704 CA LYS B 735 16518 18628 18880 -4049 3850 -5169 C ATOM 1705 C LYS B 735 -19.498 -10.162 33.104 1.00146.22 C ANISOU 1705 C LYS B 735 16633 19353 19572 -3920 3804 -5478 C ATOM 1706 O LYS B 735 -20.046 -9.137 33.508 1.00146.60 O ANISOU 1706 O LYS B 735 16444 19465 19792 -3852 3833 -5662 O ATOM 1707 CB LYS B 735 -18.383 -11.623 34.864 1.00146.50 C ANISOU 1707 CB LYS B 735 17244 19165 19254 -4499 4069 -5306 C ATOM 1708 CG LYS B 735 -18.753 -11.007 36.201 1.00150.79 C ANISOU 1708 CG LYS B 735 17722 19714 19859 -4711 4255 -5503 C ATOM 1709 CD LYS B 735 -18.508 -11.996 37.335 1.00154.18 C ANISOU 1709 CD LYS B 735 18453 20050 20078 -5144 4439 -5521 C ATOM 1710 CE LYS B 735 -18.909 -13.410 36.933 1.00156.81 C ANISOU 1710 CE LYS B 735 18881 20464 20236 -5354 4456 -5601 C ATOM 1711 NZ LYS B 735 -18.835 -14.368 38.072 1.00157.25 N ANISOU 1711 NZ LYS B 735 19218 20446 20084 -5807 4634 -5669 N ATOM 1712 N PRO B 736 -20.008 -10.921 32.117 1.00149.38 N ANISOU 1712 N PRO B 736 16964 19856 19937 -3882 3724 -5537 N ATOM 1713 CA PRO B 736 -21.140 -10.566 31.249 1.00148.79 C ANISOU 1713 CA PRO B 736 16541 19959 20033 -3704 3625 -5779 C ATOM 1714 C PRO B 736 -22.371 -10.051 31.989 1.00145.40 C ANISOU 1714 C PRO B 736 15800 19690 19753 -3844 3763 -6182 C ATOM 1715 O PRO B 736 -23.194 -9.358 31.393 1.00145.69 O ANISOU 1715 O PRO B 736 15523 19844 19988 -3636 3657 -6377 O ATOM 1716 CB PRO B 736 -21.472 -11.898 30.555 1.00151.28 C ANISOU 1716 CB PRO B 736 16927 20346 20205 -3821 3612 -5799 C ATOM 1717 CG PRO B 736 -20.798 -12.949 31.404 1.00152.25 C ANISOU 1717 CG PRO B 736 17394 20367 20088 -4152 3761 -5676 C ATOM 1718 CD PRO B 736 -19.536 -12.282 31.820 1.00150.46 C ANISOU 1718 CD PRO B 736 17375 19941 19854 -4036 3726 -5381 C ATOM 1719 N GLU B 737 -22.490 -10.391 33.267 1.00141.95 N ANISOU 1719 N GLU B 737 15454 19254 19225 -4196 3991 -6314 N ATOM 1720 CA GLU B 737 -23.657 -10.025 34.062 1.00140.81 C ANISOU 1720 CA GLU B 737 15031 19268 19201 -4383 4155 -6717 C ATOM 1721 C GLU B 737 -23.657 -8.565 34.521 1.00139.78 C ANISOU 1721 C GLU B 737 14719 19116 19274 -4201 4135 -6773 C ATOM 1722 O GLU B 737 -24.694 -7.901 34.493 1.00141.34 O ANISOU 1722 O GLU B 737 14570 19464 19669 -4132 4134 -7089 O ATOM 1723 CB GLU B 737 -23.762 -10.952 35.273 1.00139.65 C ANISOU 1723 CB GLU B 737 15076 19122 18863 -4852 4411 -6836 C ATOM 1724 CG GLU B 737 -22.419 -11.498 35.724 1.00137.86 C ANISOU 1724 CG GLU B 737 15282 18674 18423 -4968 4431 -6481 C ATOM 1725 CD GLU B 737 -22.461 -12.070 37.122 1.00141.02 C ANISOU 1725 CD GLU B 737 15874 19039 18669 -5418 4676 -6602 C ATOM 1726 OE1 GLU B 737 -23.191 -11.514 37.968 1.00145.91 O ANISOU 1726 OE1 GLU B 737 16303 19748 19389 -5571 4832 -6887 O ATOM 1727 OE2 GLU B 737 -21.759 -13.070 37.375 1.00139.06 O ANISOU 1727 OE2 GLU B 737 15972 18666 18197 -5623 4707 -6417 O ATOM 1728 N ALA B 738 -22.493 -8.073 34.939 1.00135.61 N ANISOU 1728 N ALA B 738 14426 18400 18701 -4123 4111 -6471 N ATOM 1729 CA ALA B 738 -22.370 -6.733 35.517 1.00130.89 C ANISOU 1729 CA ALA B 738 13707 17760 18264 -3982 4106 -6491 C ATOM 1730 C ALA B 738 -22.958 -5.630 34.637 1.00127.87 C ANISOU 1730 C ALA B 738 12985 17472 18127 -3609 3903 -6610 C ATOM 1731 O ALA B 738 -22.906 -5.704 33.410 1.00128.76 O ANISOU 1731 O ALA B 738 13062 17594 18268 -3356 3700 -6501 O ATOM 1732 CB ALA B 738 -20.912 -6.431 35.843 1.00126.19 C ANISOU 1732 CB ALA B 738 13439 16935 17574 -3901 4065 -6091 C ATOM 1733 N VAL B 739 -23.515 -4.605 35.276 1.00124.92 N ANISOU 1733 N VAL B 739 12373 17161 17928 -3582 3952 -6838 N ATOM 1734 CA VAL B 739 -24.087 -3.469 34.560 1.00122.54 C ANISOU 1734 CA VAL B 739 11752 16938 17870 -3235 3749 -6974 C ATOM 1735 C VAL B 739 -23.069 -2.335 34.432 1.00116.15 C ANISOU 1735 C VAL B 739 11051 15970 17113 -2930 3581 -6665 C ATOM 1736 O VAL B 739 -22.980 -1.682 33.392 1.00116.40 O ANISOU 1736 O VAL B 739 10989 15987 17252 -2584 3331 -6571 O ATOM 1737 CB VAL B 739 -25.383 -2.951 35.239 1.00138.35 C ANISOU 1737 CB VAL B 739 13390 19118 20059 -3354 3873 -7439 C ATOM 1738 CG1 VAL B 739 -25.095 -2.451 36.650 1.00137.43 C ANISOU 1738 CG1 VAL B 739 13347 18941 19929 -3549 4070 -7464 C ATOM 1739 CG2 VAL B 739 -26.031 -1.858 34.399 1.00138.50 C ANISOU 1739 CG2 VAL B 739 13074 19216 20336 -2987 3632 -7599 C ATOM 1740 N LYS B 740 -22.299 -2.113 35.494 1.00108.88 N ANISOU 1740 N LYS B 740 10338 14924 16108 -3069 3717 -6508 N ATOM 1741 CA LYS B 740 -21.251 -1.100 35.491 1.00101.96 C ANISOU 1741 CA LYS B 740 9598 13887 15257 -2813 3582 -6196 C ATOM 1742 C LYS B 740 -19.911 -1.744 35.835 1.00 98.45 C ANISOU 1742 C LYS B 740 9568 13246 14590 -2935 3649 -5815 C ATOM 1743 O LYS B 740 -19.871 -2.862 36.353 1.00 98.96 O ANISOU 1743 O LYS B 740 9806 13299 14495 -3256 3828 -5835 O ATOM 1744 CB LYS B 740 -21.577 0.011 36.488 1.00 98.36 C ANISOU 1744 CB LYS B 740 8977 13452 14946 -2822 3659 -6370 C ATOM 1745 CG LYS B 740 -21.762 -0.477 37.913 1.00102.04 C ANISOU 1745 CG LYS B 740 9526 13919 15324 -3233 3964 -6521 C ATOM 1746 CD LYS B 740 -21.905 0.685 38.883 1.00106.67 C ANISOU 1746 CD LYS B 740 9987 14498 16044 -3219 4029 -6636 C ATOM 1747 CE LYS B 740 -22.254 0.196 40.280 1.00107.19 C ANISOU 1747 CE LYS B 740 10108 14583 16034 -3651 4342 -6840 C ATOM 1748 NZ LYS B 740 -21.318 -0.860 40.756 1.00103.82 N ANISOU 1748 NZ LYS B 740 10090 13996 15360 -3917 4472 -6573 N ATOM 1749 N CYS B 741 -18.817 -1.045 35.547 1.00 92.92 N ANISOU 1749 N CYS B 741 9033 12392 13881 -2682 3497 -5476 N ATOM 1750 CA CYS B 741 -17.491 -1.586 35.821 1.00 87.21 C ANISOU 1750 CA CYS B 741 8695 11473 12967 -2767 3538 -5110 C ATOM 1751 C CYS B 741 -17.249 -1.727 37.319 1.00 85.88 C ANISOU 1751 C CYS B 741 8686 11220 12725 -3085 3777 -5131 C ATOM 1752 O CYS B 741 -17.398 -0.762 38.075 1.00 85.52 O ANISOU 1752 O CYS B 741 8538 11169 12787 -3067 3826 -5214 O ATOM 1753 CB CYS B 741 -16.394 -0.727 35.183 1.00 80.86 C ANISOU 1753 CB CYS B 741 8014 10530 12180 -2421 3324 -4759 C ATOM 1754 SG CYS B 741 -14.721 -1.353 35.489 1.00 70.45 S ANISOU 1754 SG CYS B 741 7155 8966 10648 -2505 3363 -4317 S ATOM 1755 N VAL B 742 -16.869 -2.934 37.732 1.00 83.74 N ANISOU 1755 N VAL B 742 8676 10876 12266 -3379 3916 -5055 N ATOM 1756 CA VAL B 742 -16.620 -3.236 39.134 1.00 88.97 C ANISOU 1756 CA VAL B 742 9536 11437 12831 -3721 4140 -5071 C ATOM 1757 C VAL B 742 -15.487 -2.389 39.693 1.00 87.00 C ANISOU 1757 C VAL B 742 9483 10988 12587 -3602 4107 -4774 C ATOM 1758 O VAL B 742 -15.311 -2.297 40.917 1.00 89.94 O ANISOU 1758 O VAL B 742 9984 11267 12923 -3838 4276 -4792 O ATOM 1759 CB VAL B 742 -16.269 -4.730 39.336 1.00 90.97 C ANISOU 1759 CB VAL B 742 10082 11619 12865 -4030 4246 -4998 C ATOM 1760 CG1 VAL B 742 -14.946 -5.050 38.666 1.00 87.57 C ANISOU 1760 CG1 VAL B 742 9936 11012 12326 -3854 4092 -4596 C ATOM 1761 CG2 VAL B 742 -16.216 -5.067 40.817 1.00 96.85 C ANISOU 1761 CG2 VAL B 742 11014 12272 13513 -4423 4482 -5077 C ATOM 1762 N ALA B 743 -14.717 -1.768 38.807 1.00 78.58 N ANISOU 1762 N ALA B 743 8447 9850 11559 -3247 3892 -4501 N ATOM 1763 CA ALA B 743 -13.576 -0.983 39.254 1.00 75.45 C ANISOU 1763 CA ALA B 743 8246 9261 11158 -3120 3847 -4197 C ATOM 1764 C ALA B 743 -13.881 0.503 39.328 1.00 77.01 C ANISOU 1764 C ALA B 743 8210 9512 11539 -2874 3761 -4263 C ATOM 1765 O ALA B 743 -13.763 1.114 40.391 1.00 69.64 O ANISOU 1765 O ALA B 743 7310 8509 10640 -2967 3869 -4273 O ATOM 1766 CB ALA B 743 -12.401 -1.214 38.337 1.00 73.34 C ANISOU 1766 CB ALA B 743 8198 8865 10803 -2905 3674 -3834 C ATOM 1767 N CYS B 744 -14.275 1.075 38.192 1.00 79.78 N ANISOU 1767 N CYS B 744 8332 9978 12003 -2561 3558 -4308 N ATOM 1768 CA CYS B 744 -14.463 2.517 38.094 1.00 82.43 C ANISOU 1768 CA CYS B 744 8464 10349 12504 -2283 3423 -4338 C ATOM 1769 C CYS B 744 -15.926 2.942 38.008 1.00 79.40 C ANISOU 1769 C CYS B 744 7693 10181 12296 -2263 3422 -4753 C ATOM 1770 O CYS B 744 -16.219 4.109 37.737 1.00 75.92 O ANISOU 1770 O CYS B 744 7049 9790 12007 -2004 3270 -4815 O ATOM 1771 CB CYS B 744 -13.688 3.071 36.898 1.00 80.93 C ANISOU 1771 CB CYS B 744 8331 10098 12320 -1913 3157 -4053 C ATOM 1772 SG CYS B 744 -14.438 2.734 35.277 1.00 70.55 S ANISOU 1772 SG CYS B 744 6803 8943 11059 -1712 2957 -4189 S ATOM 1773 N GLU B 745 -16.833 1.990 38.202 1.00 82.49 N ANISOU 1773 N GLU B 745 7982 10698 12665 -2532 3579 -5038 N ATOM 1774 CA GLU B 745 -18.270 2.269 38.242 1.00 93.72 C ANISOU 1774 CA GLU B 745 9030 12327 14251 -2564 3613 -5469 C ATOM 1775 C GLU B 745 -18.826 2.829 36.935 1.00 97.23 C ANISOU 1775 C GLU B 745 9216 12884 14842 -2221 3352 -5561 C ATOM 1776 O GLU B 745 -19.941 3.351 36.901 1.00100.14 O ANISOU 1776 O GLU B 745 9254 13409 15386 -2169 3325 -5902 O ATOM 1777 CB GLU B 745 -18.601 3.210 39.402 1.00 95.97 C ANISOU 1777 CB GLU B 745 9193 12624 14649 -2636 3730 -5633 C ATOM 1778 CG GLU B 745 -17.932 2.841 40.718 1.00100.61 C ANISOU 1778 CG GLU B 745 10067 13063 15098 -2947 3963 -5504 C ATOM 1779 CD GLU B 745 -18.446 1.539 41.303 1.00110.86 C ANISOU 1779 CD GLU B 745 11432 14414 16275 -3366 4207 -5705 C ATOM 1780 OE1 GLU B 745 -18.991 0.707 40.544 1.00110.27 O ANISOU 1780 OE1 GLU B 745 11273 14454 16171 -3402 4180 -5832 O ATOM 1781 OE2 GLU B 745 -18.301 1.348 42.529 1.00116.56 O ANISOU 1781 OE2 GLU B 745 12305 15058 16925 -3667 4423 -5734 O ATOM 1782 N THR B 746 -18.047 2.721 35.864 1.00 94.13 N ANISOU 1782 N THR B 746 8978 12408 14380 -1994 3156 -5265 N ATOM 1783 CA THR B 746 -18.493 3.180 34.555 1.00 94.51 C ANISOU 1783 CA THR B 746 8827 12537 14545 -1680 2895 -5323 C ATOM 1784 C THR B 746 -19.459 2.179 33.923 1.00 98.44 C ANISOU 1784 C THR B 746 9173 13182 15049 -1790 2919 -5573 C ATOM 1785 O THR B 746 -19.168 0.986 33.842 1.00 95.13 O ANISOU 1785 O THR B 746 8940 12737 14468 -1984 3026 -5477 O ATOM 1786 CB THR B 746 -17.303 3.435 33.609 1.00 91.06 C ANISOU 1786 CB THR B 746 8619 11954 14023 -1408 2679 -4919 C ATOM 1787 OG1 THR B 746 -16.554 4.563 34.078 1.00 85.16 O ANISOU 1787 OG1 THR B 746 7960 11094 13305 -1257 2616 -4723 O ATOM 1788 CG2 THR B 746 -17.792 3.715 32.196 1.00 94.26 C ANISOU 1788 CG2 THR B 746 8854 12436 14526 -1126 2415 -4984 C ATOM 1789 N PRO B 747 -20.624 2.672 33.480 1.00106.53 N ANISOU 1789 N PRO B 747 9855 14359 16263 -1665 2812 -5900 N ATOM 1790 CA PRO B 747 -21.680 1.856 32.869 1.00112.24 C ANISOU 1790 CA PRO B 747 10386 15233 17025 -1747 2819 -6177 C ATOM 1791 C PRO B 747 -21.242 1.208 31.558 1.00118.52 C ANISOU 1791 C PRO B 747 11327 15982 17723 -1603 2651 -5952 C ATOM 1792 O PRO B 747 -20.399 1.756 30.848 1.00117.97 O ANISOU 1792 O PRO B 747 11395 15795 17631 -1340 2449 -5661 O ATOM 1793 CB PRO B 747 -22.794 2.873 32.597 1.00111.04 C ANISOU 1793 CB PRO B 747 9852 15210 17127 -1549 2670 -6516 C ATOM 1794 CG PRO B 747 -22.508 4.019 33.517 1.00107.74 C ANISOU 1794 CG PRO B 747 9410 14739 16786 -1494 2693 -6500 C ATOM 1795 CD PRO B 747 -21.023 4.082 33.620 1.00104.53 C ANISOU 1795 CD PRO B 747 9371 14138 16208 -1442 2677 -6041 C ATOM 1796 N LYS B 748 -21.824 0.053 31.246 1.00126.70 N ANISOU 1796 N LYS B 748 12331 17111 18696 -1782 2738 -6093 N ATOM 1797 CA LYS B 748 -21.514 -0.669 30.016 1.00133.06 C ANISOU 1797 CA LYS B 748 13263 17885 19408 -1672 2596 -5909 C ATOM 1798 C LYS B 748 -22.160 -0.010 28.802 1.00137.70 C ANISOU 1798 C LYS B 748 13620 18528 20169 -1357 2317 -6027 C ATOM 1799 O LYS B 748 -23.352 0.295 28.818 1.00140.67 O ANISOU 1799 O LYS B 748 13681 19043 20723 -1348 2298 -6389 O ATOM 1800 CB LYS B 748 -21.981 -2.123 30.116 1.00138.20 C ANISOU 1800 CB LYS B 748 13954 18622 19934 -1975 2777 -6034 C ATOM 1801 CG LYS B 748 -21.752 -2.929 28.847 1.00143.28 C ANISOU 1801 CG LYS B 748 14713 19243 20483 -1873 2638 -5867 C ATOM 1802 CD LYS B 748 -22.569 -4.213 28.833 1.00148.96 C ANISOU 1802 CD LYS B 748 15378 20090 21130 -2137 2780 -6082 C ATOM 1803 CE LYS B 748 -22.185 -5.136 29.977 1.00150.60 C ANISOU 1803 CE LYS B 748 15805 20270 21148 -2508 3051 -6041 C ATOM 1804 NZ LYS B 748 -22.850 -6.465 29.861 1.00152.44 N ANISOU 1804 NZ LYS B 748 16035 20613 21273 -2762 3168 -6203 N ATOM 1805 N PRO B 749 -21.372 0.202 27.737 1.00139.69 N ANISOU 1805 N PRO B 749 14036 18668 20371 -1104 2096 -5727 N ATOM 1806 CA PRO B 749 -21.869 0.817 26.502 1.00143.20 C ANISOU 1806 CA PRO B 749 14315 19134 20960 -803 1806 -5800 C ATOM 1807 C PRO B 749 -23.036 0.033 25.903 1.00146.34 C ANISOU 1807 C PRO B 749 14510 19669 21423 -874 1799 -6086 C ATOM 1808 O PRO B 749 -24.190 0.407 26.119 1.00147.68 O ANISOU 1808 O PRO B 749 14369 19965 21779 -879 1794 -6452 O ATOM 1809 CB PRO B 749 -20.656 0.751 25.568 1.00140.76 C ANISOU 1809 CB PRO B 749 14302 18672 20509 -625 1648 -5388 C ATOM 1810 CG PRO B 749 -19.478 0.676 26.478 1.00138.13 C ANISOU 1810 CG PRO B 749 14237 18225 20022 -751 1813 -5112 C ATOM 1811 CD PRO B 749 -19.939 -0.124 27.656 1.00137.78 C ANISOU 1811 CD PRO B 749 14155 18264 19932 -1098 2108 -5306 C TER 1812 PRO B 749 ATOM 1813 N PRO C 7 -7.768 13.541 18.498 1.00129.36 N ANISOU 1813 N PRO C 7 17258 15509 16384 449 745 -722 N ATOM 1814 CA PRO C 7 -7.353 13.648 17.095 1.00126.66 C ANISOU 1814 CA PRO C 7 16917 15152 16056 465 661 -646 C ATOM 1815 C PRO C 7 -5.933 13.130 16.897 1.00117.73 C ANISOU 1815 C PRO C 7 15828 14070 14835 394 629 -584 C ATOM 1816 O PRO C 7 -4.975 13.880 17.084 1.00119.62 O ANISOU 1816 O PRO C 7 16133 14279 15040 354 614 -575 O ATOM 1817 CB PRO C 7 -7.392 15.159 16.827 1.00130.32 C ANISOU 1817 CB PRO C 7 17426 15514 16576 499 636 -657 C ATOM 1818 CG PRO C 7 -8.180 15.749 17.956 1.00132.04 C ANISOU 1818 CG PRO C 7 17643 15692 16836 522 709 -750 C ATOM 1819 CD PRO C 7 -7.927 14.862 19.126 1.00131.24 C ANISOU 1819 CD PRO C 7 17542 15667 16654 463 773 -785 C ATOM 1820 N GLN C 8 -5.800 11.862 16.524 1.00104.17 N ANISOU 1820 N GLN C 8 14068 12424 13086 379 621 -545 N ATOM 1821 CA GLN C 8 -4.487 11.270 16.311 1.00 91.36 C ANISOU 1821 CA GLN C 8 12474 10851 11387 319 594 -487 C ATOM 1822 C GLN C 8 -3.950 11.615 14.928 1.00 72.63 C ANISOU 1822 C GLN C 8 10116 8458 9023 326 524 -423 C ATOM 1823 O GLN C 8 -4.641 11.434 13.927 1.00 78.60 O ANISOU 1823 O GLN C 8 10831 9212 9823 374 491 -404 O ATOM 1824 CB GLN C 8 -4.553 9.752 16.479 1.00 97.06 C ANISOU 1824 CB GLN C 8 13148 11651 12081 301 620 -471 C ATOM 1825 CG GLN C 8 -3.194 9.071 16.436 1.00103.56 C ANISOU 1825 CG GLN C 8 13995 12524 12830 243 602 -416 C ATOM 1826 CD GLN C 8 -3.279 7.569 16.631 1.00104.98 C ANISOU 1826 CD GLN C 8 14129 12768 12991 230 632 -399 C ATOM 1827 OE1 GLN C 8 -4.363 6.985 16.584 1.00104.02 O ANISOU 1827 OE1 GLN C 8 13954 12654 12916 262 661 -425 O ATOM 1828 NE2 GLN C 8 -2.131 6.934 16.849 1.00104.02 N ANISOU 1828 NE2 GLN C 8 14024 12690 12808 183 626 -356 N ATOM 1829 N VAL C 9 -2.720 12.115 14.874 1.00 51.11 N ANISOU 1829 N VAL C 9 7448 5722 6251 277 500 -390 N ATOM 1830 CA VAL C 9 -2.080 12.410 13.590 1.00 44.08 C ANISOU 1830 CA VAL C 9 6576 4816 5356 273 442 -325 C ATOM 1831 C VAL C 9 -1.685 11.113 12.850 1.00 36.24 C ANISOU 1831 C VAL C 9 5543 3898 4327 258 426 -277 C ATOM 1832 O VAL C 9 -0.802 10.369 13.283 1.00 33.39 O ANISOU 1832 O VAL C 9 5183 3590 3914 208 442 -263 O ATOM 1833 CB VAL C 9 -0.848 13.341 13.761 1.00 41.95 C ANISOU 1833 CB VAL C 9 6374 4510 5053 217 429 -307 C ATOM 1834 CG1 VAL C 9 -0.165 13.591 12.423 1.00 38.75 C ANISOU 1834 CG1 VAL C 9 5989 4095 4639 208 379 -235 C ATOM 1835 CG2 VAL C 9 -1.252 14.665 14.396 1.00 45.42 C ANISOU 1835 CG2 VAL C 9 6858 4865 5537 232 446 -359 C ATOM 1836 N GLN C 10 -2.363 10.829 11.748 1.00 30.05 N ANISOU 1836 N GLN C 10 4723 3120 3574 303 394 -256 N ATOM 1837 CA GLN C 10 -1.997 9.665 10.938 1.00 29.54 C ANISOU 1837 CA GLN C 10 4625 3120 3479 288 379 -219 C ATOM 1838 C GLN C 10 -2.035 9.903 9.421 1.00 32.85 C ANISOU 1838 C GLN C 10 5047 3535 3900 312 322 -172 C ATOM 1839 O GLN C 10 -2.764 10.759 8.933 1.00 33.30 O ANISOU 1839 O GLN C 10 5111 3544 3996 360 290 -169 O ATOM 1840 CB GLN C 10 -2.885 8.485 11.303 1.00 32.22 C ANISOU 1840 CB GLN C 10 4898 3504 3840 307 413 -256 C ATOM 1841 CG GLN C 10 -4.362 8.781 11.208 1.00 34.49 C ANISOU 1841 CG GLN C 10 5144 3764 4196 370 410 -297 C ATOM 1842 CD GLN C 10 -5.191 7.712 11.890 1.00 48.64 C ANISOU 1842 CD GLN C 10 6874 5593 6014 376 462 -342 C ATOM 1843 OE1 GLN C 10 -4.949 6.516 11.708 1.00 42.15 O ANISOU 1843 OE1 GLN C 10 6022 4822 5172 352 474 -330 O ATOM 1844 NE2 GLN C 10 -6.176 8.134 12.679 1.00 48.76 N ANISOU 1844 NE2 GLN C 10 6870 5580 6078 408 497 -396 N ATOM 1845 N PHE C 11 -1.248 9.117 8.689 1.00 34.55 N ANISOU 1845 N PHE C 11 5257 3802 4071 280 311 -134 N ATOM 1846 CA PHE C 11 -1.149 9.241 7.233 1.00 32.41 C ANISOU 1846 CA PHE C 11 4993 3539 3781 292 262 -88 C ATOM 1847 C PHE C 11 -1.242 7.880 6.565 1.00 29.58 C ANISOU 1847 C PHE C 11 4584 3250 3405 288 262 -91 C ATOM 1848 O PHE C 11 -0.595 6.923 7.007 1.00 30.83 O ANISOU 1848 O PHE C 11 4724 3447 3541 250 299 -97 O ATOM 1849 CB PHE C 11 0.195 9.866 6.858 1.00 30.97 C ANISOU 1849 CB PHE C 11 4870 3342 3553 243 252 -35 C ATOM 1850 CG PHE C 11 0.430 11.196 7.488 1.00 30.17 C ANISOU 1850 CG PHE C 11 4823 3168 3470 235 254 -35 C ATOM 1851 CD1 PHE C 11 -0.216 12.330 6.994 1.00 29.86 C ANISOU 1851 CD1 PHE C 11 4815 3063 3467 279 220 -19 C ATOM 1852 CD2 PHE C 11 1.287 11.323 8.564 1.00 33.08 C ANISOU 1852 CD2 PHE C 11 5213 3533 3823 184 288 -52 C ATOM 1853 CE1 PHE C 11 -0.001 13.572 7.563 1.00 30.48 C ANISOU 1853 CE1 PHE C 11 4946 3063 3571 271 227 -23 C ATOM 1854 CE2 PHE C 11 1.497 12.578 9.153 1.00 36.89 C ANISOU 1854 CE2 PHE C 11 5747 3944 4324 170 291 -62 C ATOM 1855 CZ PHE C 11 0.855 13.690 8.646 1.00 35.60 C ANISOU 1855 CZ PHE C 11 5617 3708 4203 213 264 -49 C ATOM 1856 N LYS C 12 -2.040 7.781 5.504 1.00 31.93 N ANISOU 1856 N LYS C 12 4858 3563 3712 327 220 -87 N ATOM 1857 CA LYS C 12 -1.965 6.597 4.645 1.00 34.11 C ANISOU 1857 CA LYS C 12 5097 3904 3961 315 215 -89 C ATOM 1858 C LYS C 12 -0.688 6.632 3.801 1.00 31.97 C ANISOU 1858 C LYS C 12 4869 3654 3625 272 207 -37 C ATOM 1859 O LYS C 12 -0.443 7.570 3.049 1.00 35.06 O ANISOU 1859 O LYS C 12 5308 4023 3990 276 170 8 O ATOM 1860 CB LYS C 12 -3.171 6.478 3.718 1.00 35.87 C ANISOU 1860 CB LYS C 12 5278 4145 4204 364 167 -105 C ATOM 1861 CG LYS C 12 -3.014 5.332 2.717 1.00 32.86 C ANISOU 1861 CG LYS C 12 4868 3831 3786 344 159 -112 C ATOM 1862 CD LYS C 12 -4.323 4.982 2.022 1.00 33.48 C ANISOU 1862 CD LYS C 12 4889 3939 3892 387 114 -148 C ATOM 1863 CE LYS C 12 -4.069 4.083 0.797 1.00 29.06 C ANISOU 1863 CE LYS C 12 4316 3444 3279 364 95 -152 C ATOM 1864 NZ LYS C 12 -5.357 3.511 0.305 1.00 38.72 N ANISOU 1864 NZ LYS C 12 5470 4705 4536 395 59 -205 N ATOM 1865 N LEU C 13 0.124 5.599 3.941 1.00 26.91 N ANISOU 1865 N LEU C 13 4210 3053 2961 231 246 -42 N ATOM 1866 CA LEU C 13 1.353 5.474 3.178 1.00 30.11 C ANISOU 1866 CA LEU C 13 4644 3485 3312 188 250 -2 C ATOM 1867 C LEU C 13 1.241 4.228 2.300 1.00 31.85 C ANISOU 1867 C LEU C 13 4823 3763 3514 185 255 -24 C ATOM 1868 O LEU C 13 1.034 3.122 2.809 1.00 30.75 O ANISOU 1868 O LEU C 13 4636 3644 3405 182 290 -64 O ATOM 1869 CB LEU C 13 2.544 5.347 4.132 1.00 24.55 C ANISOU 1869 CB LEU C 13 3950 2777 2602 143 293 9 C ATOM 1870 CG LEU C 13 3.959 5.323 3.533 1.00 28.79 C ANISOU 1870 CG LEU C 13 4510 3338 3092 94 305 50 C ATOM 1871 CD1 LEU C 13 4.967 5.728 4.602 1.00 25.41 C ANISOU 1871 CD1 LEU C 13 4098 2889 2666 56 329 65 C ATOM 1872 CD2 LEU C 13 4.308 3.959 2.903 1.00 31.04 C ANISOU 1872 CD2 LEU C 13 4754 3679 3363 82 331 36 C ATOM 1873 N VAL C 14 1.367 4.398 0.987 1.00 27.08 N ANISOU 1873 N VAL C 14 4241 3187 2862 183 223 0 N ATOM 1874 CA VAL C 14 1.392 3.221 0.088 1.00 27.71 C ANISOU 1874 CA VAL C 14 4287 3324 2916 172 232 -28 C ATOM 1875 C VAL C 14 2.819 2.767 -0.207 1.00 28.69 C ANISOU 1875 C VAL C 14 4425 3474 3001 122 275 -7 C ATOM 1876 O VAL C 14 3.682 3.570 -0.525 1.00 31.67 O ANISOU 1876 O VAL C 14 4850 3843 3340 98 273 42 O ATOM 1877 CB VAL C 14 0.597 3.424 -1.215 1.00 30.92 C ANISOU 1877 CB VAL C 14 4701 3763 3286 198 174 -29 C ATOM 1878 CG1 VAL C 14 -0.906 3.533 -0.911 1.00 30.37 C ANISOU 1878 CG1 VAL C 14 4590 3680 3270 249 135 -66 C ATOM 1879 CG2 VAL C 14 1.103 4.643 -1.999 1.00 31.30 C ANISOU 1879 CG2 VAL C 14 4819 3800 3274 192 139 41 C ATOM 1880 N LEU C 15 3.061 1.472 -0.065 1.00 28.70 N ANISOU 1880 N LEU C 15 4380 3502 3021 108 319 -46 N ATOM 1881 CA LEU C 15 4.390 0.910 -0.235 1.00 26.93 C ANISOU 1881 CA LEU C 15 4155 3300 2778 69 366 -32 C ATOM 1882 C LEU C 15 4.377 0.076 -1.519 1.00 33.51 C ANISOU 1882 C LEU C 15 4975 4184 3574 60 373 -64 C ATOM 1883 O LEU C 15 3.795 -1.005 -1.553 1.00 29.60 O ANISOU 1883 O LEU C 15 4435 3702 3111 69 388 -119 O ATOM 1884 CB LEU C 15 4.739 0.052 0.987 1.00 31.19 C ANISOU 1884 CB LEU C 15 4653 3824 3372 63 413 -48 C ATOM 1885 CG LEU C 15 5.970 -0.864 0.966 1.00 38.03 C ANISOU 1885 CG LEU C 15 5496 4711 4243 34 466 -45 C ATOM 1886 CD1 LEU C 15 7.252 -0.096 0.612 1.00 31.75 C ANISOU 1886 CD1 LEU C 15 4734 3924 3404 -1 471 4 C ATOM 1887 CD2 LEU C 15 6.120 -1.618 2.305 1.00 36.52 C ANISOU 1887 CD2 LEU C 15 5268 4499 4109 39 501 -50 C ATOM 1888 N VAL C 16 4.993 0.594 -2.578 1.00 31.78 N ANISOU 1888 N VAL C 16 4797 3991 3286 38 364 -32 N ATOM 1889 CA VAL C 16 4.925 -0.066 -3.886 1.00 30.98 C ANISOU 1889 CA VAL C 16 4694 3945 3134 28 366 -65 C ATOM 1890 C VAL C 16 6.304 -0.378 -4.443 1.00 35.85 C ANISOU 1890 C VAL C 16 5319 4589 3713 -14 421 -52 C ATOM 1891 O VAL C 16 7.313 0.178 -3.993 1.00 34.46 O ANISOU 1891 O VAL C 16 5160 4394 3541 -37 445 -4 O ATOM 1892 CB VAL C 16 4.128 0.761 -4.938 1.00 37.31 C ANISOU 1892 CB VAL C 16 5537 4770 3870 46 298 -46 C ATOM 1893 CG1 VAL C 16 2.706 1.026 -4.442 1.00 39.24 C ANISOU 1893 CG1 VAL C 16 5760 4990 4161 93 243 -65 C ATOM 1894 CG2 VAL C 16 4.841 2.069 -5.261 1.00 32.53 C ANISOU 1894 CG2 VAL C 16 4998 4149 3211 29 285 33 C ATOM 1895 N GLY C 17 6.323 -1.261 -5.439 1.00 31.80 N ANISOU 1895 N GLY C 17 4793 4124 3166 -26 443 -99 N ATOM 1896 CA GLY C 17 7.544 -1.701 -6.091 1.00 29.51 C ANISOU 1896 CA GLY C 17 4504 3866 2842 -63 504 -102 C ATOM 1897 C GLY C 17 7.339 -3.141 -6.566 1.00 32.70 C ANISOU 1897 C GLY C 17 4864 4299 3263 -65 542 -185 C ATOM 1898 O GLY C 17 6.353 -3.785 -6.198 1.00 30.83 O ANISOU 1898 O GLY C 17 4592 4048 3075 -41 525 -234 O ATOM 1899 N ASP C 18 8.275 -3.652 -7.357 1.00 29.82 N ANISOU 1899 N ASP C 18 4498 3969 2862 -95 599 -205 N ATOM 1900 CA ASP C 18 8.134 -4.969 -7.984 1.00 30.34 C ANISOU 1900 CA ASP C 18 4529 4062 2937 -101 641 -291 C ATOM 1901 C ASP C 18 8.037 -6.077 -6.931 1.00 37.84 C ANISOU 1901 C ASP C 18 5415 4962 4001 -82 678 -329 C ATOM 1902 O ASP C 18 8.520 -5.915 -5.807 1.00 36.55 O ANISOU 1902 O ASP C 18 5233 4755 3898 -71 690 -283 O ATOM 1903 CB ASP C 18 9.351 -5.264 -8.876 1.00 34.33 C ANISOU 1903 CB ASP C 18 5043 4607 3394 -137 711 -303 C ATOM 1904 CG ASP C 18 9.246 -4.640 -10.267 1.00 44.02 C ANISOU 1904 CG ASP C 18 6331 5900 4493 -161 687 -297 C ATOM 1905 OD1 ASP C 18 8.265 -3.912 -10.554 1.00 38.10 O ANISOU 1905 OD1 ASP C 18 5621 5165 3692 -147 608 -275 O ATOM 1906 OD2 ASP C 18 10.163 -4.895 -11.083 1.00 47.23 O ANISOU 1906 OD2 ASP C 18 6748 6346 4851 -194 749 -313 O ATOM 1907 N GLY C 19 7.453 -7.216 -7.299 1.00 36.58 N ANISOU 1907 N GLY C 19 5223 4808 3868 -80 698 -413 N ATOM 1908 CA GLY C 19 7.443 -8.365 -6.405 1.00 34.57 C ANISOU 1908 CA GLY C 19 4912 4501 3723 -65 745 -447 C ATOM 1909 C GLY C 19 8.868 -8.795 -6.118 1.00 40.35 C ANISOU 1909 C GLY C 19 5620 5215 4494 -72 818 -425 C ATOM 1910 O GLY C 19 9.736 -8.653 -6.972 1.00 38.78 O ANISOU 1910 O GLY C 19 5438 5055 4241 -95 852 -426 O ATOM 1911 N GLY C 20 9.131 -9.299 -4.917 1.00 39.84 N ANISOU 1911 N GLY C 20 5516 5097 4524 -51 844 -400 N ATOM 1912 CA GLY C 20 10.472 -9.751 -4.582 1.00 35.86 C ANISOU 1912 CA GLY C 20 4980 4577 4068 -50 906 -376 C ATOM 1913 C GLY C 20 11.451 -8.667 -4.140 1.00 32.12 C ANISOU 1913 C GLY C 20 4522 4114 3567 -59 891 -292 C ATOM 1914 O GLY C 20 12.589 -8.982 -3.808 1.00 37.14 O ANISOU 1914 O GLY C 20 5124 4742 4247 -58 936 -268 O ATOM 1915 N THR C 21 11.029 -7.404 -4.125 1.00 30.09 N ANISOU 1915 N THR C 21 4313 3874 3246 -67 828 -249 N ATOM 1916 CA THR C 21 11.935 -6.311 -3.697 1.00 29.10 C ANISOU 1916 CA THR C 21 4205 3753 3097 -83 813 -174 C ATOM 1917 C THR C 21 12.125 -6.163 -2.176 1.00 34.42 C ANISOU 1917 C THR C 21 4857 4387 3835 -65 796 -124 C ATOM 1918 O THR C 21 13.106 -5.560 -1.735 1.00 31.96 O ANISOU 1918 O THR C 21 4540 4079 3523 -80 797 -72 O ATOM 1919 CB THR C 21 11.570 -4.915 -4.298 1.00 27.82 C ANISOU 1919 CB THR C 21 4109 3617 2844 -102 759 -139 C ATOM 1920 OG1 THR C 21 10.189 -4.604 -4.053 1.00 30.82 O ANISOU 1920 OG1 THR C 21 4511 3981 3218 -79 698 -149 O ATOM 1921 CG2 THR C 21 11.823 -4.886 -5.801 1.00 24.87 C ANISOU 1921 CG2 THR C 21 3764 3296 2390 -129 783 -167 C ATOM 1922 N GLY C 22 11.193 -6.708 -1.393 1.00 28.61 N ANISOU 1922 N GLY C 22 4106 3617 3149 -37 781 -141 N ATOM 1923 CA GLY C 22 11.328 -6.765 0.064 1.00 27.83 C ANISOU 1923 CA GLY C 22 3985 3483 3104 -19 772 -99 C ATOM 1924 C GLY C 22 10.344 -5.873 0.808 1.00 31.34 C ANISOU 1924 C GLY C 22 4465 3911 3532 -11 714 -78 C ATOM 1925 O GLY C 22 10.565 -5.524 1.970 1.00 30.47 O ANISOU 1925 O GLY C 22 4353 3784 3440 -6 699 -36 O ATOM 1926 N LYS C 23 9.247 -5.506 0.153 1.00 32.09 N ANISOU 1926 N LYS C 23 4589 4013 3590 -8 682 -110 N ATOM 1927 CA LYS C 23 8.287 -4.587 0.763 1.00 31.22 C ANISOU 1927 CA LYS C 23 4509 3885 3468 5 630 -94 C ATOM 1928 C LYS C 23 7.689 -5.158 2.053 1.00 34.56 C ANISOU 1928 C LYS C 23 4906 4273 3952 27 638 -97 C ATOM 1929 O LYS C 23 7.573 -4.447 3.052 1.00 28.84 O ANISOU 1929 O LYS C 23 4198 3532 3227 31 614 -65 O ATOM 1930 CB LYS C 23 7.185 -4.236 -0.233 1.00 26.23 C ANISOU 1930 CB LYS C 23 3902 3270 2795 11 593 -130 C ATOM 1931 CG LYS C 23 7.730 -3.716 -1.585 1.00 25.57 C ANISOU 1931 CG LYS C 23 3851 3226 2637 -13 586 -123 C ATOM 1932 CD LYS C 23 6.598 -3.266 -2.509 1.00 24.59 C ANISOU 1932 CD LYS C 23 3755 3124 2465 -2 535 -148 C ATOM 1933 CE LYS C 23 5.794 -4.464 -3.002 1.00 26.76 C ANISOU 1933 CE LYS C 23 3993 3413 2763 6 549 -223 C ATOM 1934 NZ LYS C 23 6.691 -5.435 -3.693 1.00 25.14 N ANISOU 1934 NZ LYS C 23 3769 3231 2554 -16 609 -255 N ATOM 1935 N THR C 24 7.312 -6.432 2.025 1.00 32.66 N ANISOU 1935 N THR C 24 4628 4020 3763 39 676 -138 N ATOM 1936 CA THR C 24 6.697 -7.082 3.188 1.00 30.35 C ANISOU 1936 CA THR C 24 4311 3692 3529 57 693 -139 C ATOM 1937 C THR C 24 7.700 -7.216 4.317 1.00 31.83 C ANISOU 1937 C THR C 24 4489 3868 3737 58 710 -82 C ATOM 1938 O THR C 24 7.423 -6.875 5.471 1.00 35.44 O ANISOU 1938 O THR C 24 4956 4311 4199 65 697 -53 O ATOM 1939 CB THR C 24 6.183 -8.481 2.824 1.00 38.58 C ANISOU 1939 CB THR C 24 5315 4717 4628 63 737 -194 C ATOM 1940 OG1 THR C 24 5.067 -8.333 1.958 1.00 31.68 O ANISOU 1940 OG1 THR C 24 4446 3857 3735 61 710 -250 O ATOM 1941 CG2 THR C 24 5.721 -9.256 4.085 1.00 40.27 C ANISOU 1941 CG2 THR C 24 5505 4888 4907 78 767 -182 C ATOM 1942 N THR C 25 8.872 -7.727 3.975 1.00 28.18 N ANISOU 1942 N THR C 25 4004 3415 3287 52 740 -67 N ATOM 1943 CA THR C 25 9.944 -7.878 4.939 1.00 29.15 C ANISOU 1943 CA THR C 25 4109 3536 3430 55 750 -11 C ATOM 1944 C THR C 25 10.181 -6.529 5.627 1.00 28.08 C ANISOU 1944 C THR C 25 4008 3416 3244 40 701 31 C ATOM 1945 O THR C 25 10.265 -6.443 6.865 1.00 27.96 O ANISOU 1945 O THR C 25 3995 3394 3236 46 691 67 O ATOM 1946 CB THR C 25 11.211 -8.384 4.241 1.00 26.76 C ANISOU 1946 CB THR C 25 3774 3250 3144 50 784 -7 C ATOM 1947 OG1 THR C 25 10.921 -9.650 3.635 1.00 37.53 O ANISOU 1947 OG1 THR C 25 5109 4591 4559 63 834 -54 O ATOM 1948 CG2 THR C 25 12.370 -8.543 5.233 1.00 29.39 C ANISOU 1948 CG2 THR C 25 4079 3586 3503 56 787 55 C ATOM 1949 N PHE C 26 10.259 -5.470 4.823 1.00 28.17 N ANISOU 1949 N PHE C 26 4052 3448 3204 20 673 24 N ATOM 1950 CA PHE C 26 10.454 -4.117 5.345 1.00 24.54 C ANISOU 1950 CA PHE C 26 3630 2994 2701 1 630 56 C ATOM 1951 C PHE C 26 9.370 -3.647 6.344 1.00 26.51 C ANISOU 1951 C PHE C 26 3905 3220 2949 15 604 52 C ATOM 1952 O PHE C 26 9.685 -3.229 7.470 1.00 28.25 O ANISOU 1952 O PHE C 26 4134 3439 3161 8 590 81 O ATOM 1953 CB PHE C 26 10.561 -3.115 4.178 1.00 22.94 C ANISOU 1953 CB PHE C 26 3463 2807 2448 -21 609 51 C ATOM 1954 CG PHE C 26 10.816 -1.685 4.619 1.00 25.68 C ANISOU 1954 CG PHE C 26 3850 3148 2758 -44 570 82 C ATOM 1955 CD1 PHE C 26 12.054 -1.319 5.151 1.00 30.51 C ANISOU 1955 CD1 PHE C 26 4451 3773 3367 -72 568 119 C ATOM 1956 CD2 PHE C 26 9.839 -0.715 4.481 1.00 30.04 C ANISOU 1956 CD2 PHE C 26 4448 3680 3285 -38 534 72 C ATOM 1957 CE1 PHE C 26 12.306 -0.018 5.554 1.00 27.72 C ANISOU 1957 CE1 PHE C 26 4135 3411 2986 -99 535 140 C ATOM 1958 CE2 PHE C 26 10.086 0.621 4.892 1.00 32.97 C ANISOU 1958 CE2 PHE C 26 4860 4035 3631 -59 503 98 C ATOM 1959 CZ PHE C 26 11.322 0.954 5.425 1.00 29.37 C ANISOU 1959 CZ PHE C 26 4396 3591 3172 -93 505 129 C ATOM 1960 N VAL C 27 8.099 -3.693 5.940 1.00 23.04 N ANISOU 1960 N VAL C 27 3475 2767 2514 32 599 12 N ATOM 1961 CA VAL C 27 7.037 -3.156 6.798 1.00 25.09 C ANISOU 1961 CA VAL C 27 3756 3005 2774 46 580 2 C ATOM 1962 C VAL C 27 6.959 -3.934 8.109 1.00 31.29 C ANISOU 1962 C VAL C 27 4520 3778 3591 56 608 16 C ATOM 1963 O VAL C 27 6.685 -3.373 9.174 1.00 28.01 O ANISOU 1963 O VAL C 27 4125 3354 3161 55 596 27 O ATOM 1964 CB VAL C 27 5.653 -3.144 6.093 1.00 33.55 C ANISOU 1964 CB VAL C 27 4827 4066 3855 65 569 -45 C ATOM 1965 CG1 VAL C 27 5.141 -4.587 5.807 1.00 34.37 C ANISOU 1965 CG1 VAL C 27 4887 4166 4006 77 608 -82 C ATOM 1966 CG2 VAL C 27 4.653 -2.388 6.933 1.00 25.83 C ANISOU 1966 CG2 VAL C 27 3868 3066 2879 80 550 -55 C ATOM 1967 N LYS C 28 7.202 -5.234 8.013 1.00 28.95 N ANISOU 1967 N LYS C 28 4185 3478 3335 64 647 16 N ATOM 1968 CA LYS C 28 7.149 -6.128 9.166 1.00 30.33 C ANISOU 1968 CA LYS C 28 4341 3639 3542 76 678 38 C ATOM 1969 C LYS C 28 8.225 -5.896 10.236 1.00 33.35 C ANISOU 1969 C LYS C 28 4730 4039 3902 67 665 96 C ATOM 1970 O LYS C 28 8.136 -6.466 11.328 1.00 32.05 O ANISOU 1970 O LYS C 28 4561 3868 3750 76 683 123 O ATOM 1971 CB LYS C 28 7.223 -7.581 8.699 1.00 32.97 C ANISOU 1971 CB LYS C 28 4635 3957 3936 88 725 26 C ATOM 1972 CG LYS C 28 5.935 -8.150 8.127 1.00 39.67 C ANISOU 1972 CG LYS C 28 5470 4783 4820 96 747 -33 C ATOM 1973 CD LYS C 28 6.107 -9.668 7.882 1.00 46.45 C ANISOU 1973 CD LYS C 28 6290 5615 5746 104 801 -43 C ATOM 1974 CE LYS C 28 4.877 -10.314 7.236 1.00 46.23 C ANISOU 1974 CE LYS C 28 6241 5565 5758 104 824 -112 C ATOM 1975 NZ LYS C 28 3.589 -10.025 7.934 1.00 53.84 N ANISOU 1975 NZ LYS C 28 7211 6517 6728 106 820 -128 N ATOM 1976 N ARG C 29 9.250 -5.102 9.943 1.00 27.04 N ANISOU 1976 N ARG C 29 3940 3265 3070 46 635 115 N ATOM 1977 CA ARG C 29 10.271 -4.832 10.962 1.00 28.16 C ANISOU 1977 CA ARG C 29 4081 3430 3189 33 615 164 C ATOM 1978 C ARG C 29 9.667 -4.184 12.222 1.00 30.20 C ANISOU 1978 C ARG C 29 4376 3687 3412 28 597 167 C ATOM 1979 O ARG C 29 10.123 -4.427 13.336 1.00 33.02 O ANISOU 1979 O ARG C 29 4730 4061 3754 27 592 204 O ATOM 1980 CB ARG C 29 11.385 -3.935 10.431 1.00 25.55 C ANISOU 1980 CB ARG C 29 3752 3125 2830 3 586 176 C ATOM 1981 CG ARG C 29 12.096 -4.491 9.155 1.00 28.68 C ANISOU 1981 CG ARG C 29 4113 3529 3254 4 610 171 C ATOM 1982 CD ARG C 29 12.399 -5.970 9.300 1.00 33.27 C ANISOU 1982 CD ARG C 29 4646 4104 3892 32 650 187 C ATOM 1983 NE ARG C 29 13.485 -6.232 10.239 1.00 31.69 N ANISOU 1983 NE ARG C 29 4416 3926 3700 34 637 241 N ATOM 1984 CZ ARG C 29 13.951 -7.443 10.521 1.00 32.62 C ANISOU 1984 CZ ARG C 29 4489 4036 3869 62 665 270 C ATOM 1985 NH1 ARG C 29 13.421 -8.512 9.943 1.00 33.33 N ANISOU 1985 NH1 ARG C 29 4563 4091 4011 88 713 245 N ATOM 1986 NH2 ARG C 29 14.948 -7.587 11.376 1.00 33.42 N ANISOU 1986 NH2 ARG C 29 4562 4164 3974 66 643 324 N ATOM 1987 N HIS C 30 8.651 -3.358 12.016 1.00 30.57 N ANISOU 1987 N HIS C 30 4455 3715 3443 27 587 126 N ATOM 1988 CA HIS C 30 7.979 -2.617 13.074 1.00 35.66 C ANISOU 1988 CA HIS C 30 5137 4355 4057 23 577 115 C ATOM 1989 C HIS C 30 7.050 -3.545 13.875 1.00 31.15 C ANISOU 1989 C HIS C 30 4557 3771 3507 45 617 112 C ATOM 1990 O HIS C 30 5.975 -3.943 13.406 1.00 28.48 O ANISOU 1990 O HIS C 30 4208 3408 3206 63 643 76 O ATOM 1991 CB HIS C 30 7.186 -1.474 12.435 1.00 30.74 C ANISOU 1991 CB HIS C 30 4545 3709 3425 22 556 72 C ATOM 1992 CG HIS C 30 6.779 -0.403 13.402 1.00 32.39 C ANISOU 1992 CG HIS C 30 4796 3910 3602 12 541 55 C ATOM 1993 ND1 HIS C 30 5.803 -0.596 14.357 1.00 25.52 N ANISOU 1993 ND1 HIS C 30 3933 3030 2732 27 567 35 N ATOM 1994 CD2 HIS C 30 7.193 0.879 13.542 1.00 28.37 C ANISOU 1994 CD2 HIS C 30 4323 3396 3060 -12 508 50 C ATOM 1995 CE1 HIS C 30 5.644 0.515 15.052 1.00 33.42 C ANISOU 1995 CE1 HIS C 30 4974 4024 3701 13 552 15 C ATOM 1996 NE2 HIS C 30 6.471 1.427 14.575 1.00 27.71 N ANISOU 1996 NE2 HIS C 30 4269 3300 2959 -11 514 22 N ATOM 1997 N LEU C 31 7.468 -3.906 15.084 1.00 31.15 N ANISOU 1997 N LEU C 31 4561 3789 3484 40 622 150 N ATOM 1998 CA LEU C 31 6.767 -4.950 15.843 1.00 25.06 C ANISOU 1998 CA LEU C 31 3781 3007 2733 58 668 163 C ATOM 1999 C LEU C 31 5.289 -4.651 16.156 1.00 30.30 C ANISOU 1999 C LEU C 31 4463 3647 3402 64 696 115 C ATOM 2000 O LEU C 31 4.425 -5.507 15.991 1.00 28.49 O ANISOU 2000 O LEU C 31 4211 3393 3220 79 739 99 O ATOM 2001 CB LEU C 31 7.535 -5.278 17.138 1.00 33.34 C ANISOU 2001 CB LEU C 31 4839 4087 3741 51 661 223 C ATOM 2002 CG LEU C 31 8.909 -5.927 16.923 1.00 35.04 C ANISOU 2002 CG LEU C 31 5020 4323 3972 55 643 278 C ATOM 2003 CD1 LEU C 31 9.650 -6.152 18.242 1.00 36.06 C ANISOU 2003 CD1 LEU C 31 5157 4491 4053 51 623 341 C ATOM 2004 CD2 LEU C 31 8.771 -7.244 16.150 1.00 35.31 C ANISOU 2004 CD2 LEU C 31 5012 4322 4083 82 686 286 C ATOM 2005 N THR C 32 5.002 -3.443 16.617 1.00 23.55 N ANISOU 2005 N THR C 32 3645 2798 2503 52 674 87 N ATOM 2006 CA THR C 32 3.631 -3.080 16.966 1.00 27.56 C ANISOU 2006 CA THR C 32 4166 3286 3021 61 703 37 C ATOM 2007 C THR C 32 2.769 -2.995 15.719 1.00 32.23 C ANISOU 2007 C THR C 32 4731 3848 3666 80 702 -9 C ATOM 2008 O THR C 32 1.607 -3.417 15.723 1.00 34.05 O ANISOU 2008 O THR C 32 4941 4060 3938 95 739 -42 O ATOM 2009 CB THR C 32 3.588 -1.763 17.797 1.00 40.67 C ANISOU 2009 CB THR C 32 5873 4955 4624 45 683 14 C ATOM 2010 OG1 THR C 32 4.346 -1.954 19.001 1.00 36.67 O ANISOU 2010 OG1 THR C 32 5389 4486 4059 24 681 55 O ATOM 2011 CG2 THR C 32 2.144 -1.376 18.168 1.00 37.30 C ANISOU 2011 CG2 THR C 32 5453 4505 4215 59 719 -43 C ATOM 2012 N GLY C 33 3.357 -2.469 14.645 1.00 33.13 N ANISOU 2012 N GLY C 33 4845 3962 3780 77 660 -11 N ATOM 2013 CA GLY C 33 2.683 -2.372 13.367 1.00 35.41 C ANISOU 2013 CA GLY C 33 5113 4233 4107 94 649 -47 C ATOM 2014 C GLY C 33 2.305 -3.746 12.864 1.00 36.88 C ANISOU 2014 C GLY C 33 5255 4414 4345 105 684 -53 C ATOM 2015 O GLY C 33 1.270 -3.919 12.228 1.00 35.21 O ANISOU 2015 O GLY C 33 5018 4188 4172 119 691 -97 O ATOM 2016 N GLU C 34 3.138 -4.739 13.156 1.00 29.93 N ANISOU 2016 N GLU C 34 4362 3542 3470 97 706 -12 N ATOM 2017 CA GLU C 34 2.809 -6.099 12.738 1.00 34.41 C ANISOU 2017 CA GLU C 34 4888 4092 4094 105 748 -19 C ATOM 2018 C GLU C 34 1.737 -6.699 13.648 1.00 38.69 C ANISOU 2018 C GLU C 34 5419 4615 4666 109 799 -31 C ATOM 2019 O GLU C 34 0.814 -7.354 13.156 1.00 35.87 O ANISOU 2019 O GLU C 34 5029 4238 4364 115 827 -71 O ATOM 2020 CB GLU C 34 4.037 -7.001 12.705 1.00 39.15 C ANISOU 2020 CB GLU C 34 5474 4698 4703 102 759 30 C ATOM 2021 CG GLU C 34 3.700 -8.497 12.656 1.00 47.54 C ANISOU 2021 CG GLU C 34 6502 5731 5832 111 814 30 C ATOM 2022 CD GLU C 34 3.129 -8.943 11.316 1.00 53.52 C ANISOU 2022 CD GLU C 34 7226 6472 6635 113 822 -29 C ATOM 2023 OE1 GLU C 34 3.174 -8.155 10.341 1.00 44.18 O ANISOU 2023 OE1 GLU C 34 6051 5309 5426 110 781 -59 O ATOM 2024 OE2 GLU C 34 2.636 -10.091 11.241 1.00 53.87 O ANISOU 2024 OE2 GLU C 34 7242 6486 6740 114 870 -46 O ATOM 2025 N SER C 35 1.844 -6.464 14.961 1.00 35.23 N ANISOU 2025 N SER C 35 5011 4186 4189 103 812 1 N ATOM 2026 CA SER C 35 0.874 -7.040 15.915 1.00 34.64 C ANISOU 2026 CA SER C 35 4931 4097 4135 103 871 -4 C ATOM 2027 C SER C 35 -0.516 -6.410 15.798 1.00 39.95 C ANISOU 2027 C SER C 35 5593 4758 4829 109 880 -71 C ATOM 2028 O SER C 35 -1.525 -7.041 16.117 1.00 40.32 O ANISOU 2028 O SER C 35 5614 4787 4920 108 933 -94 O ATOM 2029 CB SER C 35 1.388 -6.980 17.363 1.00 37.05 C ANISOU 2029 CB SER C 35 5274 4423 4380 92 883 50 C ATOM 2030 OG SER C 35 1.438 -5.663 17.876 1.00 36.97 O ANISOU 2030 OG SER C 35 5303 4436 4308 85 850 33 O ATOM 2031 N GLU C 36 -0.565 -5.173 15.310 1.00 41.66 N ANISOU 2031 N GLU C 36 5825 4984 5022 116 830 -101 N ATOM 2032 CA GLU C 36 -1.823 -4.450 15.192 1.00 39.58 C ANISOU 2032 CA GLU C 36 5549 4709 4782 131 831 -162 C ATOM 2033 C GLU C 36 -2.304 -4.313 13.747 1.00 32.99 C ANISOU 2033 C GLU C 36 4680 3868 3989 147 793 -203 C ATOM 2034 O GLU C 36 -3.190 -3.515 13.463 1.00 32.94 O ANISOU 2034 O GLU C 36 4662 3854 3999 166 773 -246 O ATOM 2035 CB GLU C 36 -1.697 -3.064 15.831 1.00 44.92 C ANISOU 2035 CB GLU C 36 6271 5392 5406 132 805 -168 C ATOM 2036 CG GLU C 36 -1.379 -3.113 17.322 1.00 52.98 C ANISOU 2036 CG GLU C 36 7327 6427 6374 114 841 -139 C ATOM 2037 CD GLU C 36 -1.421 -1.741 17.994 1.00 65.66 C ANISOU 2037 CD GLU C 36 8978 8037 7933 111 824 -164 C ATOM 2038 OE1 GLU C 36 -1.778 -0.743 17.328 1.00 68.47 O ANISOU 2038 OE1 GLU C 36 9334 8373 8307 128 788 -202 O ATOM 2039 OE2 GLU C 36 -1.098 -1.667 19.200 1.00 69.36 O ANISOU 2039 OE2 GLU C 36 9482 8525 8345 92 847 -146 O ATOM 2040 N LYS C 37 -1.732 -5.091 12.833 1.00 31.77 N ANISOU 2040 N LYS C 37 4507 3716 3850 141 782 -190 N ATOM 2041 CA LYS C 37 -2.069 -4.936 11.423 1.00 34.96 C ANISOU 2041 CA LYS C 37 4886 4124 4275 152 741 -227 C ATOM 2042 C LYS C 37 -3.526 -5.324 11.146 1.00 46.00 C ANISOU 2042 C LYS C 37 6230 5513 5736 163 760 -288 C ATOM 2043 O LYS C 37 -4.098 -6.184 11.814 1.00 40.06 O ANISOU 2043 O LYS C 37 5450 4745 5025 153 819 -298 O ATOM 2044 CB LYS C 37 -1.120 -5.753 10.538 1.00 33.22 C ANISOU 2044 CB LYS C 37 4657 3911 4054 140 735 -208 C ATOM 2045 CG LYS C 37 -1.327 -7.226 10.642 1.00 34.57 C ANISOU 2045 CG LYS C 37 4791 4065 4280 130 792 -216 C ATOM 2046 CD LYS C 37 -0.245 -7.993 9.905 1.00 36.39 C ANISOU 2046 CD LYS C 37 5018 4298 4511 121 794 -195 C ATOM 2047 CE LYS C 37 -0.496 -9.508 10.051 1.00 42.95 C ANISOU 2047 CE LYS C 37 5813 5098 5410 112 857 -205 C ATOM 2048 NZ LYS C 37 0.510 -10.326 9.323 1.00 51.96 N ANISOU 2048 NZ LYS C 37 6945 6233 6564 107 867 -194 N ATOM 2049 N LYS C 38 -4.124 -4.672 10.157 1.00 38.94 N ANISOU 2049 N LYS C 38 5319 4627 4848 181 708 -325 N ATOM 2050 CA LYS C 38 -5.501 -4.948 9.767 1.00 35.84 C ANISOU 2050 CA LYS C 38 4867 4234 4517 193 711 -386 C ATOM 2051 C LYS C 38 -5.566 -5.573 8.379 1.00 45.04 C ANISOU 2051 C LYS C 38 6000 5417 5697 187 680 -417 C ATOM 2052 O LYS C 38 -4.943 -5.068 7.446 1.00 37.20 O ANISOU 2052 O LYS C 38 5035 4443 4658 192 626 -401 O ATOM 2053 CB LYS C 38 -6.281 -3.645 9.767 1.00 35.42 C ANISOU 2053 CB LYS C 38 4814 4179 4464 226 670 -408 C ATOM 2054 CG LYS C 38 -6.269 -2.950 11.120 1.00 47.84 C ANISOU 2054 CG LYS C 38 6421 5735 6020 230 704 -391 C ATOM 2055 CD LYS C 38 -7.539 -2.157 11.334 1.00 58.60 C ANISOU 2055 CD LYS C 38 7752 7087 7425 263 699 -438 C ATOM 2056 CE LYS C 38 -7.980 -2.245 12.782 1.00 61.31 C ANISOU 2056 CE LYS C 38 8095 7418 7782 255 774 -448 C ATOM 2057 NZ LYS C 38 -9.450 -2.105 12.906 1.00 60.39 N ANISOU 2057 NZ LYS C 38 7913 7295 7737 279 795 -509 N ATOM 2058 N TYR C 39 -6.315 -6.661 8.227 1.00 41.91 N ANISOU 2058 N TYR C 39 5547 5015 5363 172 717 -463 N ATOM 2059 CA TYR C 39 -6.460 -7.256 6.892 1.00 39.66 C ANISOU 2059 CA TYR C 39 5229 4751 5090 163 686 -506 C ATOM 2060 C TYR C 39 -7.671 -6.679 6.161 1.00 37.39 C ANISOU 2060 C TYR C 39 4896 4489 4823 185 627 -561 C ATOM 2061 O TYR C 39 -8.778 -6.671 6.690 1.00 43.26 O ANISOU 2061 O TYR C 39 5590 5223 5623 193 648 -597 O ATOM 2062 CB TYR C 39 -6.532 -8.789 6.942 1.00 38.92 C ANISOU 2062 CB TYR C 39 5098 4635 5054 130 751 -534 C ATOM 2063 CG TYR C 39 -6.633 -9.415 5.554 1.00 46.04 C ANISOU 2063 CG TYR C 39 5970 5560 5964 115 721 -589 C ATOM 2064 CD1 TYR C 39 -5.582 -9.311 4.639 1.00 42.52 C ANISOU 2064 CD1 TYR C 39 5562 5135 5457 112 687 -570 C ATOM 2065 CD2 TYR C 39 -7.778 -10.095 5.155 1.00 48.83 C ANISOU 2065 CD2 TYR C 39 6255 5916 6384 99 728 -666 C ATOM 2066 CE1 TYR C 39 -5.677 -9.868 3.366 1.00 48.68 C ANISOU 2066 CE1 TYR C 39 6319 5942 6234 96 663 -627 C ATOM 2067 CE2 TYR C 39 -7.881 -10.663 3.884 1.00 47.96 C ANISOU 2067 CE2 TYR C 39 6118 5831 6274 81 699 -725 C ATOM 2068 CZ TYR C 39 -6.829 -10.546 2.996 1.00 56.71 C ANISOU 2068 CZ TYR C 39 7271 6963 7312 80 667 -706 C ATOM 2069 OH TYR C 39 -6.936 -11.103 1.738 1.00 60.57 O ANISOU 2069 OH TYR C 39 7738 7483 7792 59 640 -771 O ATOM 2070 N VAL C 40 -7.442 -6.166 4.957 1.00 35.08 N ANISOU 2070 N VAL C 40 4618 4229 4482 197 555 -563 N ATOM 2071 CA VAL C 40 -8.511 -5.648 4.113 1.00 34.42 C ANISOU 2071 CA VAL C 40 4491 4177 4409 222 486 -607 C ATOM 2072 C VAL C 40 -8.792 -6.646 2.981 1.00 36.45 C ANISOU 2072 C VAL C 40 4705 4466 4679 196 469 -668 C ATOM 2073 O VAL C 40 -8.085 -6.675 1.966 1.00 37.71 O ANISOU 2073 O VAL C 40 4898 4655 4776 187 433 -660 O ATOM 2074 CB VAL C 40 -8.123 -4.286 3.503 1.00 39.43 C ANISOU 2074 CB VAL C 40 5179 4829 4974 255 408 -562 C ATOM 2075 CG1 VAL C 40 -9.327 -3.636 2.829 1.00 36.38 C ANISOU 2075 CG1 VAL C 40 4746 4469 4606 293 333 -596 C ATOM 2076 CG2 VAL C 40 -7.551 -3.367 4.587 1.00 37.53 C ANISOU 2076 CG2 VAL C 40 4994 4552 4714 270 430 -503 C ATOM 2077 N ALA C 41 -9.830 -7.451 3.161 1.00 37.52 N ANISOU 2077 N ALA C 41 4767 4598 4893 180 499 -733 N ATOM 2078 CA ALA C 41 -10.092 -8.588 2.284 1.00 51.66 C ANISOU 2078 CA ALA C 41 6512 6408 6708 143 502 -802 C ATOM 2079 C ALA C 41 -10.505 -8.178 0.883 1.00 51.69 C ANISOU 2079 C ALA C 41 6499 6475 6666 156 404 -838 C ATOM 2080 O ALA C 41 -10.122 -8.829 -0.089 1.00 51.99 O ANISOU 2080 O ALA C 41 6543 6540 6671 127 392 -872 O ATOM 2081 CB ALA C 41 -11.141 -9.511 2.896 1.00 58.06 C ANISOU 2081 CB ALA C 41 7244 7194 7622 118 562 -863 C ATOM 2082 N THR C 42 -11.280 -7.103 0.775 1.00 49.41 N ANISOU 2082 N THR C 42 6191 6209 6373 200 335 -831 N ATOM 2083 CA THR C 42 -11.726 -6.640 -0.534 1.00 49.52 C ANISOU 2083 CA THR C 42 6190 6287 6339 218 232 -854 C ATOM 2084 C THR C 42 -10.553 -6.301 -1.460 1.00 50.09 C ANISOU 2084 C THR C 42 6345 6386 6300 214 195 -807 C ATOM 2085 O THR C 42 -10.616 -6.531 -2.667 1.00 55.45 O ANISOU 2085 O THR C 42 7019 7121 6927 201 140 -842 O ATOM 2086 CB THR C 42 -12.703 -5.449 -0.426 1.00 51.19 C ANISOU 2086 CB THR C 42 6369 6510 6570 277 163 -840 C ATOM 2087 OG1 THR C 42 -12.153 -4.435 0.428 1.00 48.94 O ANISOU 2087 OG1 THR C 42 6147 6180 6268 310 182 -763 O ATOM 2088 CG2 THR C 42 -14.047 -5.918 0.150 1.00 50.80 C ANISOU 2088 CG2 THR C 42 6215 6454 6632 275 188 -910 C ATOM 2089 N LEU C 43 -9.472 -5.794 -0.884 1.00 39.80 N ANISOU 2089 N LEU C 43 5116 5046 4959 221 231 -731 N ATOM 2090 CA LEU C 43 -8.347 -5.289 -1.667 1.00 38.96 C ANISOU 2090 CA LEU C 43 5089 4962 4753 219 201 -678 C ATOM 2091 C LEU C 43 -7.117 -6.187 -1.605 1.00 46.43 C ANISOU 2091 C LEU C 43 6071 5891 5681 176 275 -671 C ATOM 2092 O LEU C 43 -6.144 -5.964 -2.331 1.00 49.76 O ANISOU 2092 O LEU C 43 6548 6335 6022 166 262 -639 O ATOM 2093 CB LEU C 43 -7.979 -3.865 -1.213 1.00 46.16 C ANISOU 2093 CB LEU C 43 6059 5848 5632 259 174 -594 C ATOM 2094 CG LEU C 43 -9.046 -2.776 -1.396 1.00 46.64 C ANISOU 2094 CG LEU C 43 6096 5920 5704 313 93 -585 C ATOM 2095 CD1 LEU C 43 -8.689 -1.479 -0.651 1.00 39.74 C ANISOU 2095 CD1 LEU C 43 5277 4998 4824 349 91 -511 C ATOM 2096 CD2 LEU C 43 -9.318 -2.497 -2.878 1.00 41.09 C ANISOU 2096 CD2 LEU C 43 5398 5283 4931 324 -1 -591 C ATOM 2097 N GLY C 44 -7.160 -7.211 -0.757 1.00 42.34 N ANISOU 2097 N GLY C 44 5518 5331 5238 152 354 -701 N ATOM 2098 CA GLY C 44 -5.992 -8.045 -0.542 1.00 38.90 C ANISOU 2098 CA GLY C 44 5112 4869 4799 121 427 -686 C ATOM 2099 C GLY C 44 -4.818 -7.204 -0.076 1.00 43.51 C ANISOU 2099 C GLY C 44 5765 5435 5330 134 435 -598 C ATOM 2100 O GLY C 44 -3.792 -7.099 -0.759 1.00 49.07 O ANISOU 2100 O GLY C 44 6515 6160 5970 122 430 -572 O ATOM 2101 N VAL C 45 -4.985 -6.585 1.089 1.00 37.03 N ANISOU 2101 N VAL C 45 4952 4579 4539 155 448 -556 N ATOM 2102 CA VAL C 45 -3.992 -5.673 1.643 1.00 36.85 C ANISOU 2102 CA VAL C 45 4991 4539 4471 166 449 -478 C ATOM 2103 C VAL C 45 -3.887 -5.871 3.145 1.00 35.63 C ANISOU 2103 C VAL C 45 4834 4339 4365 166 510 -453 C ATOM 2104 O VAL C 45 -4.887 -6.162 3.810 1.00 36.56 O ANISOU 2104 O VAL C 45 4908 4439 4544 172 533 -485 O ATOM 2105 CB VAL C 45 -4.399 -4.207 1.420 1.00 34.69 C ANISOU 2105 CB VAL C 45 4744 4276 4160 201 378 -448 C ATOM 2106 CG1 VAL C 45 -3.665 -3.309 2.386 1.00 35.68 C ANISOU 2106 CG1 VAL C 45 4920 4367 4268 208 392 -383 C ATOM 2107 CG2 VAL C 45 -4.129 -3.780 -0.013 1.00 39.11 C ANISOU 2107 CG2 VAL C 45 5333 4881 4644 201 316 -441 C ATOM 2108 N GLU C 46 -2.684 -5.714 3.685 1.00 33.92 N ANISOU 2108 N GLU C 46 4661 4107 4119 156 536 -395 N ATOM 2109 CA GLU C 46 -2.533 -5.622 5.135 1.00 31.96 C ANISOU 2109 CA GLU C 46 4423 3825 3894 159 579 -361 C ATOM 2110 C GLU C 46 -2.094 -4.212 5.468 1.00 32.01 C ANISOU 2110 C GLU C 46 4481 3829 3851 173 541 -313 C ATOM 2111 O GLU C 46 -1.099 -3.737 4.931 1.00 30.54 O ANISOU 2111 O GLU C 46 4334 3656 3612 164 518 -277 O ATOM 2112 CB GLU C 46 -1.509 -6.643 5.654 1.00 35.03 C ANISOU 2112 CB GLU C 46 4816 4197 4296 137 638 -333 C ATOM 2113 CG GLU C 46 -2.002 -8.091 5.553 1.00 42.01 C ANISOU 2113 CG GLU C 46 5651 5066 5247 122 689 -380 C ATOM 2114 CD GLU C 46 -1.026 -9.111 6.107 1.00 49.87 C ANISOU 2114 CD GLU C 46 6649 6035 6265 108 749 -345 C ATOM 2115 OE1 GLU C 46 0.184 -8.819 6.194 1.00 54.20 O ANISOU 2115 OE1 GLU C 46 7230 6590 6772 108 743 -293 O ATOM 2116 OE2 GLU C 46 -1.474 -10.222 6.446 1.00 61.57 O ANISOU 2116 OE2 GLU C 46 8096 7486 7810 98 802 -368 O ATOM 2117 N VAL C 47 -2.838 -3.539 6.349 1.00 28.51 N ANISOU 2117 N VAL C 47 4038 3367 3428 192 540 -315 N ATOM 2118 CA VAL C 47 -2.492 -2.182 6.764 1.00 29.63 C ANISOU 2118 CA VAL C 47 4230 3497 3532 204 511 -278 C ATOM 2119 C VAL C 47 -1.790 -2.224 8.121 1.00 39.20 C ANISOU 2119 C VAL C 47 5467 4692 4735 188 555 -244 C ATOM 2120 O VAL C 47 -2.316 -2.785 9.086 1.00 36.12 O ANISOU 2120 O VAL C 47 5054 4290 4380 187 602 -259 O ATOM 2121 CB VAL C 47 -3.741 -1.291 6.847 1.00 34.88 C ANISOU 2121 CB VAL C 47 4881 4149 4225 240 480 -307 C ATOM 2122 CG1 VAL C 47 -3.373 0.114 7.301 1.00 32.98 C ANISOU 2122 CG1 VAL C 47 4694 3883 3953 252 455 -274 C ATOM 2123 CG2 VAL C 47 -4.452 -1.260 5.489 1.00 34.28 C ANISOU 2123 CG2 VAL C 47 4776 4098 4153 259 425 -337 C ATOM 2124 N HIS C 48 -0.591 -1.658 8.177 1.00 32.98 N ANISOU 2124 N HIS C 48 4725 3906 3898 172 540 -198 N ATOM 2125 CA HIS C 48 0.263 -1.745 9.356 1.00 29.04 C ANISOU 2125 CA HIS C 48 4250 3404 3381 152 571 -163 C ATOM 2126 C HIS C 48 0.313 -0.371 9.984 1.00 34.02 C ANISOU 2126 C HIS C 48 4925 4018 3985 155 548 -154 C ATOM 2127 O HIS C 48 0.883 0.538 9.412 1.00 29.52 O ANISOU 2127 O HIS C 48 4387 3445 3383 150 509 -133 O ATOM 2128 CB HIS C 48 1.698 -2.156 8.979 1.00 30.85 C ANISOU 2128 CB HIS C 48 4489 3651 3580 128 571 -122 C ATOM 2129 CG HIS C 48 1.851 -3.595 8.562 1.00 28.60 C ANISOU 2129 CG HIS C 48 4163 3375 3327 123 607 -129 C ATOM 2130 ND1 HIS C 48 1.358 -4.086 7.371 1.00 35.53 N ANISOU 2130 ND1 HIS C 48 5015 4262 4225 128 599 -167 N ATOM 2131 CD2 HIS C 48 2.486 -4.636 9.160 1.00 29.88 C ANISOU 2131 CD2 HIS C 48 4310 3537 3507 113 648 -105 C ATOM 2132 CE1 HIS C 48 1.659 -5.372 7.263 1.00 31.76 C ANISOU 2132 CE1 HIS C 48 4507 3783 3779 120 641 -172 C ATOM 2133 NE2 HIS C 48 2.337 -5.732 8.339 1.00 35.52 N ANISOU 2133 NE2 HIS C 48 4988 4250 4258 113 671 -131 N ATOM 2134 N PRO C 49 -0.288 -0.210 11.171 1.00 33.93 N ANISOU 2134 N PRO C 49 4915 3993 3985 161 577 -170 N ATOM 2135 CA PRO C 49 -0.232 1.109 11.810 1.00 36.96 C ANISOU 2135 CA PRO C 49 5343 4356 4343 162 560 -171 C ATOM 2136 C PRO C 49 1.107 1.275 12.516 1.00 38.11 C ANISOU 2136 C PRO C 49 5525 4516 4439 127 560 -131 C ATOM 2137 O PRO C 49 1.296 0.650 13.567 1.00 34.16 O ANISOU 2137 O PRO C 49 5022 4031 3927 113 596 -121 O ATOM 2138 CB PRO C 49 -1.359 1.055 12.850 1.00 37.64 C ANISOU 2138 CB PRO C 49 5413 4429 4457 178 602 -211 C ATOM 2139 CG PRO C 49 -1.830 -0.390 12.890 1.00 35.79 C ANISOU 2139 CG PRO C 49 5129 4210 4259 177 646 -219 C ATOM 2140 CD PRO C 49 -0.974 -1.216 11.993 1.00 33.43 C ANISOU 2140 CD PRO C 49 4818 3930 3954 163 632 -189 C ATOM 2141 N LEU C 50 2.011 2.080 11.948 1.00 27.80 N ANISOU 2141 N LEU C 50 4250 3207 3104 110 521 -106 N ATOM 2142 CA LEU C 50 3.359 2.250 12.502 1.00 21.86 C ANISOU 2142 CA LEU C 50 3523 2473 2309 72 515 -70 C ATOM 2143 C LEU C 50 3.468 3.575 13.205 1.00 28.58 C ANISOU 2143 C LEU C 50 4421 3300 3137 58 499 -84 C ATOM 2144 O LEU C 50 3.511 4.628 12.559 1.00 31.41 O ANISOU 2144 O LEU C 50 4808 3628 3498 59 468 -85 O ATOM 2145 CB LEU C 50 4.463 2.212 11.432 1.00 26.61 C ANISOU 2145 CB LEU C 50 4124 3090 2897 52 490 -34 C ATOM 2146 CG LEU C 50 4.601 1.247 10.253 1.00 35.02 C ANISOU 2146 CG LEU C 50 5153 4174 3979 60 495 -25 C ATOM 2147 CD1 LEU C 50 6.100 1.107 9.901 1.00 36.20 C ANISOU 2147 CD1 LEU C 50 5301 4350 4105 28 488 16 C ATOM 2148 CD2 LEU C 50 3.993 -0.089 10.468 1.00 26.90 C ANISOU 2148 CD2 LEU C 50 4081 3154 2983 79 532 -40 C ATOM 2149 N VAL C 51 3.538 3.524 14.530 1.00 26.77 N ANISOU 2149 N VAL C 51 4204 3082 2883 44 521 -93 N ATOM 2150 CA VAL C 51 3.711 4.737 15.324 1.00 26.40 C ANISOU 2150 CA VAL C 51 4205 3016 2810 23 510 -115 C ATOM 2151 C VAL C 51 5.184 5.124 15.434 1.00 24.85 C ANISOU 2151 C VAL C 51 4028 2840 2573 -25 480 -83 C ATOM 2152 O VAL C 51 6.049 4.279 15.658 1.00 25.94 O ANISOU 2152 O VAL C 51 4143 3023 2690 -43 480 -47 O ATOM 2153 CB VAL C 51 3.101 4.575 16.753 1.00 31.36 C ANISOU 2153 CB VAL C 51 4843 3655 3419 24 550 -147 C ATOM 2154 CG1 VAL C 51 3.371 5.819 17.605 1.00 31.28 C ANISOU 2154 CG1 VAL C 51 4884 3627 3373 -4 540 -180 C ATOM 2155 CG2 VAL C 51 1.609 4.327 16.657 1.00 43.17 C ANISOU 2155 CG2 VAL C 51 6313 5127 4962 68 584 -186 C ATOM 2156 N PHE C 52 5.469 6.407 15.265 1.00 25.54 N ANISOU 2156 N PHE C 52 4155 2891 2657 -44 455 -97 N ATOM 2157 CA PHE C 52 6.799 6.914 15.542 1.00 27.36 C ANISOU 2157 CA PHE C 52 4404 3139 2853 -98 429 -78 C ATOM 2158 C PHE C 52 6.610 8.038 16.543 1.00 28.10 C ANISOU 2158 C PHE C 52 4546 3204 2929 -119 429 -127 C ATOM 2159 O PHE C 52 5.693 8.847 16.393 1.00 30.89 O ANISOU 2159 O PHE C 52 4925 3500 3313 -93 437 -164 O ATOM 2160 CB PHE C 52 7.467 7.449 14.269 1.00 27.93 C ANISOU 2160 CB PHE C 52 4482 3190 2942 -114 402 -48 C ATOM 2161 CG PHE C 52 7.801 6.379 13.263 1.00 28.81 C ANISOU 2161 CG PHE C 52 4548 3334 3064 -100 405 -7 C ATOM 2162 CD1 PHE C 52 6.826 5.894 12.397 1.00 32.54 C ANISOU 2162 CD1 PHE C 52 5003 3794 3567 -54 415 -10 C ATOM 2163 CD2 PHE C 52 9.083 5.832 13.205 1.00 26.93 C ANISOU 2163 CD2 PHE C 52 4281 3142 2809 -134 398 30 C ATOM 2164 CE1 PHE C 52 7.135 4.884 11.465 1.00 34.10 C ANISOU 2164 CE1 PHE C 52 5162 4023 3772 -45 422 18 C ATOM 2165 CE2 PHE C 52 9.394 4.827 12.284 1.00 32.14 C ANISOU 2165 CE2 PHE C 52 4900 3830 3484 -120 409 61 C ATOM 2166 CZ PHE C 52 8.421 4.355 11.417 1.00 29.45 C ANISOU 2166 CZ PHE C 52 4549 3474 3168 -77 422 52 C ATOM 2167 N HIS C 53 7.478 8.119 17.538 1.00 32.13 N ANISOU 2167 N HIS C 53 5066 3752 3390 -165 418 -130 N ATOM 2168 CA HIS C 53 7.363 9.187 18.551 1.00 30.64 C ANISOU 2168 CA HIS C 53 4926 3540 3177 -194 420 -187 C ATOM 2169 C HIS C 53 8.275 10.352 18.214 1.00 32.51 C ANISOU 2169 C HIS C 53 5192 3743 3419 -244 388 -192 C ATOM 2170 O HIS C 53 9.496 10.176 18.129 1.00 33.13 O ANISOU 2170 O HIS C 53 5250 3862 3475 -288 360 -159 O ATOM 2171 CB HIS C 53 7.656 8.633 19.949 1.00 36.76 C ANISOU 2171 CB HIS C 53 5701 4381 3885 -218 426 -197 C ATOM 2172 CG HIS C 53 6.697 7.565 20.361 1.00 32.86 C ANISOU 2172 CG HIS C 53 5186 3911 3388 -173 467 -192 C ATOM 2173 ND1 HIS C 53 5.432 7.849 20.836 1.00 35.72 N ANISOU 2173 ND1 HIS C 53 5568 4241 3762 -143 510 -246 N ATOM 2174 CD2 HIS C 53 6.792 6.215 20.323 1.00 31.58 C ANISOU 2174 CD2 HIS C 53 4982 3796 3221 -154 478 -141 C ATOM 2175 CE1 HIS C 53 4.795 6.717 21.087 1.00 39.07 C ANISOU 2175 CE1 HIS C 53 5964 4695 4186 -112 545 -227 C ATOM 2176 NE2 HIS C 53 5.596 5.712 20.778 1.00 39.03 N ANISOU 2176 NE2 HIS C 53 5923 4734 4172 -118 526 -163 N ATOM 2177 N THR C 54 7.684 11.530 17.987 1.00 28.47 N ANISOU 2177 N THR C 54 4722 3152 2942 -236 393 -232 N ATOM 2178 CA THR C 54 8.458 12.681 17.529 1.00 27.97 C ANISOU 2178 CA THR C 54 4691 3039 2897 -283 369 -233 C ATOM 2179 C THR C 54 8.504 13.760 18.599 1.00 34.72 C ANISOU 2179 C THR C 54 5595 3861 3736 -324 373 -304 C ATOM 2180 O THR C 54 7.830 13.662 19.633 1.00 35.24 O ANISOU 2180 O THR C 54 5674 3940 3775 -310 398 -356 O ATOM 2181 CB THR C 54 7.871 13.298 16.230 1.00 37.76 C ANISOU 2181 CB THR C 54 5947 4201 4199 -245 369 -211 C ATOM 2182 OG1 THR C 54 6.843 14.249 16.567 1.00 38.82 O ANISOU 2182 OG1 THR C 54 6124 4258 4369 -215 387 -267 O ATOM 2183 CG2 THR C 54 7.299 12.203 15.309 1.00 32.58 C ANISOU 2183 CG2 THR C 54 5248 3575 3558 -187 374 -165 C ATOM 2184 N ASN C 55 9.289 14.803 18.358 1.00 30.97 N ANISOU 2184 N ASN C 55 5150 3341 3277 -379 354 -312 N ATOM 2185 CA ASN C 55 9.375 15.882 19.337 1.00 39.18 C ANISOU 2185 CA ASN C 55 6239 4341 4306 -425 358 -389 C ATOM 2186 C ASN C 55 8.106 16.723 19.340 1.00 48.20 C ANISOU 2186 C ASN C 55 7425 5388 5501 -374 391 -440 C ATOM 2187 O ASN C 55 7.928 17.574 20.203 1.00 56.16 O ANISOU 2187 O ASN C 55 8476 6355 6507 -400 407 -517 O ATOM 2188 CB ASN C 55 10.615 16.758 19.116 1.00 47.04 C ANISOU 2188 CB ASN C 55 7251 5312 5311 -506 331 -387 C ATOM 2189 CG ASN C 55 10.612 17.451 17.760 1.00 47.83 C ANISOU 2189 CG ASN C 55 7369 5325 5479 -495 331 -342 C ATOM 2190 OD1 ASN C 55 10.179 16.882 16.769 1.00 38.54 O ANISOU 2190 OD1 ASN C 55 6170 4150 4324 -440 334 -283 O ATOM 2191 ND2 ASN C 55 11.094 18.687 17.721 1.00 46.18 N ANISOU 2191 ND2 ASN C 55 7204 5040 5302 -551 329 -370 N ATOM 2192 N ARG C 56 7.227 16.475 18.372 1.00 48.68 N ANISOU 2192 N ARG C 56 7471 5413 5612 -303 401 -400 N ATOM 2193 CA ARG C 56 5.903 17.095 18.349 1.00 55.70 C ANISOU 2193 CA ARG C 56 8385 6221 6557 -239 430 -442 C ATOM 2194 C ARG C 56 4.835 16.101 18.820 1.00 54.24 C ANISOU 2194 C ARG C 56 8164 6087 6359 -180 459 -459 C ATOM 2195 O ARG C 56 3.643 16.374 18.721 1.00 58.06 O ANISOU 2195 O ARG C 56 8648 6518 6894 -117 485 -487 O ATOM 2196 CB ARG C 56 5.543 17.564 16.934 1.00 51.86 C ANISOU 2196 CB ARG C 56 7905 5659 6139 -195 415 -387 C ATOM 2197 CG ARG C 56 6.597 18.418 16.221 1.00 57.14 C ANISOU 2197 CG ARG C 56 8606 6278 6825 -252 390 -349 C ATOM 2198 CD ARG C 56 6.276 19.902 16.292 1.00 53.38 C ANISOU 2198 CD ARG C 56 8193 5677 6412 -253 402 -391 C ATOM 2199 NE ARG C 56 4.908 20.189 15.867 1.00 53.90 N ANISOU 2199 NE ARG C 56 8263 5675 6542 -161 414 -394 N ATOM 2200 CZ ARG C 56 4.579 20.835 14.749 1.00 52.48 C ANISOU 2200 CZ ARG C 56 8105 5413 6421 -121 398 -340 C ATOM 2201 NH1 ARG C 56 3.299 21.044 14.461 1.00 53.39 N ANISOU 2201 NH1 ARG C 56 8215 5477 6595 -33 403 -346 N ATOM 2202 NH2 ARG C 56 5.523 21.280 13.925 1.00 41.83 N ANISOU 2202 NH2 ARG C 56 6783 4038 5074 -169 377 -278 N ATOM 2203 N GLY C 57 5.263 14.943 19.315 1.00 40.46 N ANISOU 2203 N GLY C 57 6382 4441 4549 -199 458 -438 N ATOM 2204 CA GLY C 57 4.331 13.904 19.725 1.00 41.87 C ANISOU 2204 CA GLY C 57 6525 4669 4714 -150 490 -444 C ATOM 2205 C GLY C 57 4.276 12.742 18.741 1.00 40.59 C ANISOU 2205 C GLY C 57 6309 4549 4564 -116 477 -371 C ATOM 2206 O GLY C 57 5.072 12.671 17.803 1.00 35.34 O ANISOU 2206 O GLY C 57 5634 3888 3905 -133 443 -315 O ATOM 2207 N PRO C 58 3.310 11.832 18.933 1.00 38.12 N ANISOU 2207 N PRO C 58 5961 4266 4257 -69 508 -375 N ATOM 2208 CA PRO C 58 3.214 10.615 18.115 1.00 35.86 C ANISOU 2208 CA PRO C 58 5622 4023 3982 -40 502 -317 C ATOM 2209 C PRO C 58 2.720 10.900 16.699 1.00 32.18 C ANISOU 2209 C PRO C 58 5142 3506 3577 3 480 -290 C ATOM 2210 O PRO C 58 1.842 11.732 16.483 1.00 30.64 O ANISOU 2210 O PRO C 58 4963 3247 3433 42 484 -322 O ATOM 2211 CB PRO C 58 2.147 9.783 18.841 1.00 41.81 C ANISOU 2211 CB PRO C 58 6348 4805 4734 -6 550 -346 C ATOM 2212 CG PRO C 58 1.742 10.557 20.048 1.00 45.69 C ANISOU 2212 CG PRO C 58 6878 5276 5206 -18 584 -417 C ATOM 2213 CD PRO C 58 2.165 11.972 19.843 1.00 46.73 C ANISOU 2213 CD PRO C 58 7057 5341 5356 -39 558 -442 C ATOM 2214 N ILE C 59 3.268 10.196 15.722 1.00 35.29 N ANISOU 2214 N ILE C 59 5508 3932 3968 1 455 -232 N ATOM 2215 CA ILE C 59 2.649 10.204 14.410 1.00 37.96 C ANISOU 2215 CA ILE C 59 5829 4243 4353 46 436 -207 C ATOM 2216 C ILE C 59 2.559 8.783 13.879 1.00 31.06 C ANISOU 2216 C ILE C 59 4900 3427 3473 62 442 -177 C ATOM 2217 O ILE C 59 3.473 7.983 14.033 1.00 35.51 O ANISOU 2217 O ILE C 59 5448 4043 4002 29 444 -147 O ATOM 2218 CB ILE C 59 3.364 11.139 13.424 1.00 44.80 C ANISOU 2218 CB ILE C 59 6730 5067 5225 27 399 -170 C ATOM 2219 CG1 ILE C 59 4.700 10.549 12.986 1.00 47.66 C ANISOU 2219 CG1 ILE C 59 7079 5481 5546 -22 385 -119 C ATOM 2220 CG2 ILE C 59 3.544 12.533 14.046 1.00 48.91 C ANISOU 2220 CG2 ILE C 59 7307 5522 5755 3 399 -204 C ATOM 2221 CD1 ILE C 59 5.482 11.485 12.094 1.00 50.36 C ANISOU 2221 CD1 ILE C 59 7459 5786 5892 -52 357 -82 C ATOM 2222 N LYS C 60 1.433 8.482 13.263 1.00 29.64 N ANISOU 2222 N LYS C 60 4689 3237 3336 114 443 -187 N ATOM 2223 CA LYS C 60 1.151 7.134 12.790 1.00 33.95 C ANISOU 2223 CA LYS C 60 5182 3830 3887 130 453 -173 C ATOM 2224 C LYS C 60 1.152 7.044 11.244 1.00 35.38 C ANISOU 2224 C LYS C 60 5350 4012 4080 147 416 -139 C ATOM 2225 O LYS C 60 0.422 7.763 10.568 1.00 36.32 O ANISOU 2225 O LYS C 60 5477 4093 4228 184 389 -144 O ATOM 2226 CB LYS C 60 -0.195 6.711 13.377 1.00 32.98 C ANISOU 2226 CB LYS C 60 5024 3705 3801 168 489 -220 C ATOM 2227 CG LYS C 60 -0.639 5.299 13.150 1.00 46.02 C ANISOU 2227 CG LYS C 60 6619 5398 5468 180 512 -218 C ATOM 2228 CD LYS C 60 -2.029 5.121 13.790 1.00 56.70 C ANISOU 2228 CD LYS C 60 7938 6740 6865 213 552 -270 C ATOM 2229 CE LYS C 60 -2.850 4.044 13.093 1.00 50.94 C ANISOU 2229 CE LYS C 60 7146 6033 6178 237 559 -279 C ATOM 2230 NZ LYS C 60 -4.294 4.355 13.011 1.00 52.86 N ANISOU 2230 NZ LYS C 60 7351 6253 6483 283 566 -328 N ATOM 2231 N PHE C 61 1.988 6.166 10.697 1.00 30.87 N ANISOU 2231 N PHE C 61 4761 3485 3483 122 414 -105 N ATOM 2232 CA PHE C 61 1.945 5.846 9.269 1.00 26.93 C ANISOU 2232 CA PHE C 61 4247 3000 2985 136 388 -82 C ATOM 2233 C PHE C 61 1.186 4.549 9.064 1.00 33.01 C ANISOU 2233 C PHE C 61 4960 3804 3779 159 408 -105 C ATOM 2234 O PHE C 61 1.635 3.487 9.470 1.00 27.85 O ANISOU 2234 O PHE C 61 4281 3183 3120 140 439 -101 O ATOM 2235 CB PHE C 61 3.358 5.699 8.686 1.00 31.17 C ANISOU 2235 CB PHE C 61 4797 3563 3482 92 381 -37 C ATOM 2236 CG PHE C 61 4.088 7.005 8.533 1.00 31.60 C ANISOU 2236 CG PHE C 61 4906 3583 3519 65 358 -10 C ATOM 2237 CD1 PHE C 61 3.805 7.857 7.464 1.00 29.42 C ANISOU 2237 CD1 PHE C 61 4660 3274 3243 82 325 11 C ATOM 2238 CD2 PHE C 61 5.058 7.382 9.458 1.00 30.06 C ANISOU 2238 CD2 PHE C 61 4731 3386 3305 20 368 -5 C ATOM 2239 CE1 PHE C 61 4.468 9.039 7.318 1.00 35.55 C ANISOU 2239 CE1 PHE C 61 5489 4010 4009 54 310 39 C ATOM 2240 CE2 PHE C 61 5.729 8.572 9.318 1.00 37.04 C ANISOU 2240 CE2 PHE C 61 5661 4232 4178 -12 350 14 C ATOM 2241 CZ PHE C 61 5.437 9.407 8.248 1.00 35.22 C ANISOU 2241 CZ PHE C 61 5464 3962 3956 4 325 37 C ATOM 2242 N ASN C 62 0.018 4.634 8.447 1.00 29.01 N ANISOU 2242 N ASN C 62 4430 3287 3304 201 389 -129 N ATOM 2243 CA ASN C 62 -0.728 3.437 8.114 1.00 26.71 C ANISOU 2243 CA ASN C 62 4082 3026 3040 217 404 -156 C ATOM 2244 C ASN C 62 -0.252 2.885 6.764 1.00 32.17 C ANISOU 2244 C ASN C 62 4765 3751 3706 206 381 -136 C ATOM 2245 O ASN C 62 -0.663 3.360 5.699 1.00 29.81 O ANISOU 2245 O ASN C 62 4473 3454 3401 228 337 -131 O ATOM 2246 CB ASN C 62 -2.226 3.753 8.130 1.00 26.93 C ANISOU 2246 CB ASN C 62 4079 3034 3119 264 393 -199 C ATOM 2247 CG ASN C 62 -2.698 4.213 9.509 1.00 31.36 C ANISOU 2247 CG ASN C 62 4646 3565 3705 273 429 -227 C ATOM 2248 OD1 ASN C 62 -2.227 3.713 10.536 1.00 30.18 O ANISOU 2248 OD1 ASN C 62 4502 3426 3541 244 474 -227 O ATOM 2249 ND2 ASN C 62 -3.616 5.161 9.537 1.00 30.64 N ANISOU 2249 ND2 ASN C 62 4555 3437 3650 313 410 -250 N ATOM 2250 N VAL C 63 0.633 1.893 6.825 1.00 27.86 N ANISOU 2250 N VAL C 63 4207 3234 3145 175 413 -124 N ATOM 2251 CA VAL C 63 1.326 1.422 5.642 1.00 28.83 C ANISOU 2251 CA VAL C 63 4329 3389 3238 158 402 -106 C ATOM 2252 C VAL C 63 0.541 0.324 4.956 1.00 31.17 C ANISOU 2252 C VAL C 63 4575 3709 3558 171 408 -147 C ATOM 2253 O VAL C 63 0.231 -0.700 5.560 1.00 29.90 O ANISOU 2253 O VAL C 63 4375 3550 3436 169 449 -173 O ATOM 2254 CB VAL C 63 2.743 0.911 5.957 1.00 25.13 C ANISOU 2254 CB VAL C 63 3865 2936 2747 119 434 -75 C ATOM 2255 CG1 VAL C 63 3.434 0.421 4.654 1.00 22.70 C ANISOU 2255 CG1 VAL C 63 3553 2661 2411 103 432 -65 C ATOM 2256 CG2 VAL C 63 3.557 2.008 6.603 1.00 27.77 C ANISOU 2256 CG2 VAL C 63 4244 3250 3056 98 423 -41 C ATOM 2257 N TRP C 64 0.213 0.555 3.692 1.00 26.95 N ANISOU 2257 N TRP C 64 4045 3194 3002 182 367 -152 N ATOM 2258 CA TRP C 64 -0.504 -0.439 2.895 1.00 30.35 C ANISOU 2258 CA TRP C 64 4429 3656 3448 189 364 -198 C ATOM 2259 C TRP C 64 0.438 -1.408 2.179 1.00 36.92 C ANISOU 2259 C TRP C 64 5255 4519 4254 157 392 -199 C ATOM 2260 O TRP C 64 1.128 -1.032 1.218 1.00 33.73 O ANISOU 2260 O TRP C 64 4884 4138 3794 143 372 -174 O ATOM 2261 CB TRP C 64 -1.437 0.256 1.901 1.00 26.71 C ANISOU 2261 CB TRP C 64 3970 3207 2971 220 299 -208 C ATOM 2262 CG TRP C 64 -2.622 0.882 2.564 1.00 32.18 C ANISOU 2262 CG TRP C 64 4643 3870 3714 259 279 -226 C ATOM 2263 CD1 TRP C 64 -2.623 1.674 3.693 1.00 31.39 C ANISOU 2263 CD1 TRP C 64 4565 3726 3636 270 294 -209 C ATOM 2264 CD2 TRP C 64 -3.985 0.796 2.138 1.00 33.88 C ANISOU 2264 CD2 TRP C 64 4809 4099 3964 293 242 -270 C ATOM 2265 NE1 TRP C 64 -3.909 2.069 3.990 1.00 32.72 N ANISOU 2265 NE1 TRP C 64 4700 3877 3855 311 275 -241 N ATOM 2266 CE2 TRP C 64 -4.763 1.536 3.059 1.00 38.43 C ANISOU 2266 CE2 TRP C 64 5375 4635 4590 327 241 -276 C ATOM 2267 CE3 TRP C 64 -4.627 0.163 1.069 1.00 35.71 C ANISOU 2267 CE3 TRP C 64 5001 4376 4191 297 208 -309 C ATOM 2268 CZ2 TRP C 64 -6.145 1.651 2.941 1.00 39.15 C ANISOU 2268 CZ2 TRP C 64 5412 4729 4733 368 210 -317 C ATOM 2269 CZ3 TRP C 64 -6.000 0.283 0.954 1.00 40.99 C ANISOU 2269 CZ3 TRP C 64 5616 5052 4907 335 169 -349 C ATOM 2270 CH2 TRP C 64 -6.743 1.020 1.886 1.00 39.35 C ANISOU 2270 CH2 TRP C 64 5393 4802 4756 371 171 -351 C ATOM 2271 N ASP C 65 0.466 -2.650 2.654 1.00 36.25 N ANISOU 2271 N ASP C 65 5129 4431 4211 146 444 -228 N ATOM 2272 CA ASP C 65 1.249 -3.708 2.021 1.00 39.08 C ANISOU 2272 CA ASP C 65 5474 4812 4563 121 479 -241 C ATOM 2273 C ASP C 65 0.385 -4.689 1.222 1.00 36.40 C ANISOU 2273 C ASP C 65 5091 4492 4247 122 481 -308 C ATOM 2274 O ASP C 65 -0.614 -5.190 1.729 1.00 38.39 O ANISOU 2274 O ASP C 65 5303 4728 4556 132 493 -347 O ATOM 2275 CB ASP C 65 2.035 -4.489 3.076 1.00 37.74 C ANISOU 2275 CB ASP C 65 5290 4620 4430 109 538 -221 C ATOM 2276 CG ASP C 65 3.041 -5.463 2.456 1.00 36.13 C ANISOU 2276 CG ASP C 65 5073 4430 4224 88 577 -226 C ATOM 2277 OD1 ASP C 65 3.755 -5.077 1.494 1.00 35.60 O ANISOU 2277 OD1 ASP C 65 5030 4392 4105 74 563 -214 O ATOM 2278 OD2 ASP C 65 3.129 -6.613 2.941 1.00 32.76 O ANISOU 2278 OD2 ASP C 65 4613 3984 3851 86 627 -240 O ATOM 2279 N THR C 66 0.791 -4.976 -0.016 1.00 33.83 N ANISOU 2279 N THR C 66 4773 4203 3878 106 473 -327 N ATOM 2280 CA THR C 66 0.089 -5.929 -0.881 1.00 36.12 C ANISOU 2280 CA THR C 66 5025 4518 4182 98 474 -400 C ATOM 2281 C THR C 66 0.155 -7.365 -0.374 1.00 35.19 C ANISOU 2281 C THR C 66 4862 4371 4137 84 544 -439 C ATOM 2282 O THR C 66 0.935 -7.690 0.512 1.00 36.26 O ANISOU 2282 O THR C 66 5001 4475 4303 81 592 -402 O ATOM 2283 CB THR C 66 0.730 -5.989 -2.277 1.00 32.86 C ANISOU 2283 CB THR C 66 4637 4152 3694 78 463 -411 C ATOM 2284 OG1 THR C 66 2.060 -6.511 -2.150 1.00 33.28 O ANISOU 2284 OG1 THR C 66 4699 4197 3751 57 524 -390 O ATOM 2285 CG2 THR C 66 0.788 -4.603 -2.908 1.00 34.67 C ANISOU 2285 CG2 THR C 66 4919 4409 3844 88 398 -362 C ATOM 2286 N ALA C 67 -0.652 -8.228 -0.980 1.00 37.80 N ANISOU 2286 N ALA C 67 5153 4714 4496 74 547 -514 N ATOM 2287 CA ALA C 67 -0.506 -9.673 -0.816 1.00 38.64 C ANISOU 2287 CA ALA C 67 5222 4790 4669 54 617 -560 C ATOM 2288 C ALA C 67 0.082 -10.341 -2.083 1.00 42.84 C ANISOU 2288 C ALA C 67 5757 5353 5166 30 633 -609 C ATOM 2289 O ALA C 67 -0.307 -11.447 -2.446 1.00 42.32 O ANISOU 2289 O ALA C 67 5654 5278 5146 11 667 -683 O ATOM 2290 CB ALA C 67 -1.844 -10.295 -0.447 1.00 38.29 C ANISOU 2290 CB ALA C 67 5124 4726 4699 53 623 -618 C ATOM 2291 N GLY C 68 1.002 -9.648 -2.750 1.00 36.27 N ANISOU 2291 N GLY C 68 4970 4558 4254 27 615 -572 N ATOM 2292 CA GLY C 68 1.749 -10.170 -3.888 1.00 32.55 C ANISOU 2292 CA GLY C 68 4510 4119 3740 3 641 -610 C ATOM 2293 C GLY C 68 1.169 -9.899 -5.270 1.00 37.96 C ANISOU 2293 C GLY C 68 5209 4872 4343 -11 586 -663 C ATOM 2294 O GLY C 68 1.770 -10.289 -6.280 1.00 39.68 O ANISOU 2294 O GLY C 68 5441 5125 4512 -34 609 -700 O ATOM 2295 N GLN C 69 0.013 -9.237 -5.332 1.00 36.07 N ANISOU 2295 N GLN C 69 4963 4653 4087 5 513 -667 N ATOM 2296 CA GLN C 69 -0.680 -9.019 -6.616 1.00 37.97 C ANISOU 2296 CA GLN C 69 5211 4964 4252 -4 448 -717 C ATOM 2297 C GLN C 69 0.116 -8.187 -7.615 1.00 39.40 C ANISOU 2297 C GLN C 69 5456 5199 4314 -11 421 -673 C ATOM 2298 O GLN C 69 -0.146 -8.227 -8.819 1.00 42.11 O ANISOU 2298 O GLN C 69 5813 5608 4577 -27 384 -717 O ATOM 2299 CB GLN C 69 -2.061 -8.384 -6.397 1.00 39.52 C ANISOU 2299 CB GLN C 69 5383 5171 4464 24 369 -718 C ATOM 2300 CG GLN C 69 -2.961 -9.137 -5.392 1.00 39.79 C ANISOU 2300 CG GLN C 69 5350 5154 4615 28 399 -762 C ATOM 2301 CD GLN C 69 -2.920 -8.540 -3.976 1.00 45.54 C ANISOU 2301 CD GLN C 69 6081 5823 5398 56 415 -688 C ATOM 2302 OE1 GLN C 69 -1.892 -8.046 -3.530 1.00 37.39 O ANISOU 2302 OE1 GLN C 69 5092 4770 4343 62 439 -617 O ATOM 2303 NE2 GLN C 69 -4.049 -8.590 -3.276 1.00 50.25 N ANISOU 2303 NE2 GLN C 69 6629 6398 6066 71 404 -711 N ATOM 2304 N GLU C 70 1.091 -7.437 -7.116 1.00 35.28 N ANISOU 2304 N GLU C 70 4973 4654 3777 -2 439 -587 N ATOM 2305 CA GLU C 70 1.935 -6.611 -7.964 1.00 36.95 C ANISOU 2305 CA GLU C 70 5246 4908 3884 -14 426 -536 C ATOM 2306 C GLU C 70 2.757 -7.443 -8.953 1.00 41.42 C ANISOU 2306 C GLU C 70 5821 5514 4405 -51 483 -589 C ATOM 2307 O GLU C 70 3.255 -6.921 -9.954 1.00 41.23 O ANISOU 2307 O GLU C 70 5846 5543 4278 -68 472 -569 O ATOM 2308 CB GLU C 70 2.840 -5.713 -7.110 1.00 39.65 C ANISOU 2308 CB GLU C 70 5619 5209 4237 -5 442 -440 C ATOM 2309 CG GLU C 70 3.998 -6.414 -6.427 1.00 36.64 C ANISOU 2309 CG GLU C 70 5218 4790 3915 -18 527 -433 C ATOM 2310 CD GLU C 70 3.647 -6.988 -5.057 1.00 35.48 C ANISOU 2310 CD GLU C 70 5024 4580 3877 1 553 -438 C ATOM 2311 OE1 GLU C 70 2.445 -7.062 -4.707 1.00 36.03 O ANISOU 2311 OE1 GLU C 70 5068 4637 3984 19 517 -466 O ATOM 2312 OE2 GLU C 70 4.585 -7.379 -4.332 1.00 31.33 O ANISOU 2312 OE2 GLU C 70 4485 4020 3399 -2 609 -412 O ATOM 2313 N LYS C 71 2.893 -8.738 -8.684 1.00 41.25 N ANISOU 2313 N LYS C 71 5751 5461 4460 -63 551 -658 N ATOM 2314 CA LYS C 71 3.627 -9.622 -9.589 1.00 43.97 C ANISOU 2314 CA LYS C 71 6097 5834 4776 -96 615 -723 C ATOM 2315 C LYS C 71 2.876 -9.834 -10.904 1.00 43.64 C ANISOU 2315 C LYS C 71 6066 5866 4648 -118 571 -802 C ATOM 2316 O LYS C 71 3.465 -10.250 -11.912 1.00 42.57 O ANISOU 2316 O LYS C 71 5950 5776 4447 -148 610 -851 O ATOM 2317 CB LYS C 71 3.861 -10.981 -8.925 1.00 55.27 C ANISOU 2317 CB LYS C 71 7473 7202 6326 -98 696 -777 C ATOM 2318 CG LYS C 71 4.495 -10.896 -7.553 1.00 67.56 C ANISOU 2318 CG LYS C 71 9013 8689 7968 -74 732 -701 C ATOM 2319 CD LYS C 71 4.305 -12.184 -6.766 1.00 70.20 C ANISOU 2319 CD LYS C 71 9293 8954 8426 -68 791 -746 C ATOM 2320 CE LYS C 71 4.892 -12.047 -5.376 1.00 66.65 C ANISOU 2320 CE LYS C 71 8832 8445 8048 -43 816 -662 C ATOM 2321 NZ LYS C 71 6.266 -11.464 -5.442 1.00 64.07 N ANISOU 2321 NZ LYS C 71 8530 8134 7679 -44 837 -597 N ATOM 2322 N PHE C 72 1.573 -9.571 -10.892 1.00 40.78 N ANISOU 2322 N PHE C 72 5687 5521 4288 -103 491 -820 N ATOM 2323 CA PHE C 72 0.724 -9.961 -12.018 1.00 43.79 C ANISOU 2323 CA PHE C 72 6061 5971 4604 -124 444 -910 C ATOM 2324 C PHE C 72 0.117 -8.777 -12.761 1.00 45.32 C ANISOU 2324 C PHE C 72 6299 6237 4684 -110 338 -862 C ATOM 2325 O PHE C 72 -0.570 -8.956 -13.759 1.00 49.10 O ANISOU 2325 O PHE C 72 6778 6788 5090 -126 283 -926 O ATOM 2326 CB PHE C 72 -0.360 -10.957 -11.567 1.00 40.68 C ANISOU 2326 CB PHE C 72 5596 5545 4316 -127 444 -999 C ATOM 2327 CG PHE C 72 0.172 -12.067 -10.698 1.00 42.58 C ANISOU 2327 CG PHE C 72 5796 5700 4680 -134 546 -1028 C ATOM 2328 CD1 PHE C 72 0.969 -13.065 -11.240 1.00 48.74 C ANISOU 2328 CD1 PHE C 72 6577 6477 5465 -165 628 -1097 C ATOM 2329 CD2 PHE C 72 -0.097 -12.093 -9.334 1.00 38.87 C ANISOU 2329 CD2 PHE C 72 5292 5153 4322 -108 562 -983 C ATOM 2330 CE1 PHE C 72 1.480 -14.081 -10.440 1.00 46.72 C ANISOU 2330 CE1 PHE C 72 6286 6137 5331 -165 721 -1115 C ATOM 2331 CE2 PHE C 72 0.406 -13.102 -8.525 1.00 38.46 C ANISOU 2331 CE2 PHE C 72 5209 5024 4380 -111 652 -997 C ATOM 2332 CZ PHE C 72 1.200 -14.095 -9.078 1.00 45.43 C ANISOU 2332 CZ PHE C 72 6090 5898 5273 -137 729 -1060 C ATOM 2333 N GLY C 73 0.379 -7.566 -12.284 1.00 40.04 N ANISOU 2333 N GLY C 73 5667 5547 3998 -80 306 -750 N ATOM 2334 CA GLY C 73 -0.093 -6.375 -12.969 1.00 43.31 C ANISOU 2334 CA GLY C 73 6129 6017 4308 -62 210 -688 C ATOM 2335 C GLY C 73 -0.045 -5.168 -12.059 1.00 49.24 C ANISOU 2335 C GLY C 73 6902 6714 5094 -22 181 -577 C ATOM 2336 O GLY C 73 0.459 -5.251 -10.933 1.00 42.35 O ANISOU 2336 O GLY C 73 6011 5769 4312 -15 238 -549 O ATOM 2337 N GLY C 74 -0.571 -4.045 -12.539 1.00 51.16 N ANISOU 2337 N GLY C 74 7184 6990 5264 4 91 -514 N ATOM 2338 CA GLY C 74 -0.716 -2.866 -11.702 1.00 53.18 C ANISOU 2338 CA GLY C 74 7457 7188 5560 46 56 -419 C ATOM 2339 C GLY C 74 -1.733 -3.065 -10.582 1.00 50.49 C ANISOU 2339 C GLY C 74 7046 6794 5343 80 39 -448 C ATOM 2340 O GLY C 74 -2.597 -3.942 -10.646 1.00 46.58 O ANISOU 2340 O GLY C 74 6489 6319 4890 77 26 -535 O ATOM 2341 N LEU C 75 -1.635 -2.242 -9.548 1.00 37.71 N ANISOU 2341 N LEU C 75 5437 5108 3783 109 42 -379 N ATOM 2342 CA LEU C 75 -2.569 -2.330 -8.430 1.00 38.48 C ANISOU 2342 CA LEU C 75 5473 5155 3993 142 33 -402 C ATOM 2343 C LEU C 75 -3.862 -1.567 -8.710 1.00 41.84 C ANISOU 2343 C LEU C 75 5882 5600 4416 190 -69 -390 C ATOM 2344 O LEU C 75 -3.853 -0.591 -9.444 1.00 42.40 O ANISOU 2344 O LEU C 75 6006 5697 4407 208 -131 -327 O ATOM 2345 CB LEU C 75 -1.892 -1.832 -7.161 1.00 36.19 C ANISOU 2345 CB LEU C 75 5200 4788 3764 150 84 -343 C ATOM 2346 CG LEU C 75 -0.629 -2.633 -6.816 1.00 36.78 C ANISOU 2346 CG LEU C 75 5278 4843 3852 108 179 -353 C ATOM 2347 CD1 LEU C 75 0.185 -1.942 -5.718 1.00 32.64 C ANISOU 2347 CD1 LEU C 75 4781 4258 3363 112 216 -283 C ATOM 2348 CD2 LEU C 75 -0.990 -4.074 -6.434 1.00 39.02 C ANISOU 2348 CD2 LEU C 75 5494 5120 4212 93 229 -441 C ATOM 2349 N ARG C 76 -4.968 -2.022 -8.124 1.00 43.94 N ANISOU 2349 N ARG C 76 6071 5852 4771 210 -83 -449 N ATOM 2350 CA ARG C 76 -6.283 -1.397 -8.314 1.00 46.82 C ANISOU 2350 CA ARG C 76 6401 6236 5153 259 -177 -449 C ATOM 2351 C ARG C 76 -6.372 -0.025 -7.656 1.00 46.78 C ANISOU 2351 C ARG C 76 6428 6172 5174 310 -205 -361 C ATOM 2352 O ARG C 76 -5.610 0.266 -6.736 1.00 41.33 O ANISOU 2352 O ARG C 76 5768 5418 4517 303 -142 -322 O ATOM 2353 CB ARG C 76 -7.386 -2.306 -7.761 1.00 49.37 C ANISOU 2353 CB ARG C 76 6624 6555 5578 261 -169 -541 C ATOM 2354 CG ARG C 76 -7.793 -3.432 -8.709 1.00 59.91 C ANISOU 2354 CG ARG C 76 7916 7962 6885 224 -185 -637 C ATOM 2355 CD ARG C 76 -8.743 -4.404 -8.033 1.00 67.39 C ANISOU 2355 CD ARG C 76 8766 8891 7948 214 -156 -727 C ATOM 2356 NE ARG C 76 -8.033 -5.248 -7.074 1.00 77.52 N ANISOU 2356 NE ARG C 76 10046 10109 9298 180 -42 -745 N ATOM 2357 CZ ARG C 76 -8.572 -5.751 -5.967 1.00 76.34 C ANISOU 2357 CZ ARG C 76 9836 9908 9262 180 9 -778 C ATOM 2358 NH1 ARG C 76 -9.837 -5.486 -5.663 1.00 68.23 N ANISOU 2358 NH1 ARG C 76 8742 8884 8300 211 -37 -804 N ATOM 2359 NH2 ARG C 76 -7.842 -6.512 -5.159 1.00 75.06 N ANISOU 2359 NH2 ARG C 76 9680 9690 9148 151 109 -782 N ATOM 2360 N ASP C 77 -7.308 0.805 -8.126 1.00 45.03 N ANISOU 2360 N ASP C 77 6199 5971 4941 361 -301 -334 N ATOM 2361 CA ASP C 77 -7.468 2.177 -7.632 1.00 47.05 C ANISOU 2361 CA ASP C 77 6487 6166 5223 415 -333 -252 C ATOM 2362 C ASP C 77 -7.659 2.261 -6.119 1.00 48.48 C ANISOU 2362 C ASP C 77 6632 6267 5520 430 -272 -266 C ATOM 2363 O ASP C 77 -7.093 3.131 -5.459 1.00 47.22 O ANISOU 2363 O ASP C 77 6524 6042 5374 441 -245 -205 O ATOM 2364 CB ASP C 77 -8.641 2.881 -8.329 1.00 54.92 C ANISOU 2364 CB ASP C 77 7459 7197 6210 476 -449 -232 C ATOM 2365 CG ASP C 77 -8.364 3.173 -9.797 1.00 60.60 C ANISOU 2365 CG ASP C 77 8239 7990 6796 470 -520 -186 C ATOM 2366 OD1 ASP C 77 -7.199 3.043 -10.229 1.00 58.94 O ANISOU 2366 OD1 ASP C 77 8100 7792 6501 421 -473 -158 O ATOM 2367 OD2 ASP C 77 -9.315 3.533 -10.520 1.00 65.43 O ANISOU 2367 OD2 ASP C 77 8825 8650 7384 514 -622 -177 O ATOM 2368 N GLY C 78 -8.474 1.361 -5.577 1.00 42.90 N ANISOU 2368 N GLY C 78 5838 5566 4894 427 -249 -349 N ATOM 2369 CA GLY C 78 -8.745 1.336 -4.156 1.00 35.77 C ANISOU 2369 CA GLY C 78 4898 4596 4095 438 -187 -369 C ATOM 2370 C GLY C 78 -7.480 1.254 -3.324 1.00 42.40 C ANISOU 2370 C GLY C 78 5794 5387 4930 399 -98 -337 C ATOM 2371 O GLY C 78 -7.432 1.726 -2.186 1.00 37.75 O ANISOU 2371 O GLY C 78 5210 4737 4396 414 -58 -320 O ATOM 2372 N TYR C 79 -6.444 0.641 -3.882 1.00 39.71 N ANISOU 2372 N TYR C 79 5490 5075 4521 350 -66 -334 N ATOM 2373 CA TYR C 79 -5.182 0.533 -3.154 1.00 38.34 C ANISOU 2373 CA TYR C 79 5362 4862 4343 314 13 -303 C ATOM 2374 C TYR C 79 -4.559 1.922 -2.942 1.00 39.48 C ANISOU 2374 C TYR C 79 5580 4962 4458 331 -2 -218 C ATOM 2375 O TYR C 79 -4.053 2.245 -1.867 1.00 36.80 O ANISOU 2375 O TYR C 79 5260 4570 4154 325 46 -196 O ATOM 2376 CB TYR C 79 -4.204 -0.392 -3.897 1.00 34.69 C ANISOU 2376 CB TYR C 79 4919 4441 3819 262 50 -318 C ATOM 2377 CG TYR C 79 -2.849 -0.397 -3.248 1.00 35.84 C ANISOU 2377 CG TYR C 79 5108 4552 3958 231 120 -278 C ATOM 2378 CD1 TYR C 79 -2.564 -1.272 -2.203 1.00 31.77 C ANISOU 2378 CD1 TYR C 79 4559 4006 3506 211 193 -307 C ATOM 2379 CD2 TYR C 79 -1.871 0.514 -3.634 1.00 31.73 C ANISOU 2379 CD2 TYR C 79 4658 4026 3370 221 111 -207 C ATOM 2380 CE1 TYR C 79 -1.327 -1.265 -1.577 1.00 32.40 C ANISOU 2380 CE1 TYR C 79 4672 4058 3580 186 249 -267 C ATOM 2381 CE2 TYR C 79 -0.618 0.536 -3.000 1.00 34.44 C ANISOU 2381 CE2 TYR C 79 5032 4339 3713 189 172 -172 C ATOM 2382 CZ TYR C 79 -0.363 -0.355 -1.977 1.00 39.73 C ANISOU 2382 CZ TYR C 79 5664 4987 4445 174 236 -203 C ATOM 2383 OH TYR C 79 0.858 -0.348 -1.354 1.00 38.91 O ANISOU 2383 OH TYR C 79 5583 4861 4340 147 287 -168 O ATOM 2384 N TYR C 80 -4.609 2.747 -3.980 1.00 38.59 N ANISOU 2384 N TYR C 80 5511 4872 4280 351 -71 -170 N ATOM 2385 CA TYR C 80 -3.934 4.034 -3.964 1.00 37.14 C ANISOU 2385 CA TYR C 80 5404 4644 4064 359 -83 -86 C ATOM 2386 C TYR C 80 -4.760 5.118 -3.291 1.00 37.80 C ANISOU 2386 C TYR C 80 5484 4667 4212 416 -117 -65 C ATOM 2387 O TYR C 80 -4.214 6.104 -2.795 1.00 48.22 O ANISOU 2387 O TYR C 80 6858 5926 5538 418 -103 -12 O ATOM 2388 CB TYR C 80 -3.603 4.470 -5.410 1.00 34.61 C ANISOU 2388 CB TYR C 80 5140 4370 3639 353 -137 -34 C ATOM 2389 CG TYR C 80 -2.509 3.653 -6.067 1.00 31.54 C ANISOU 2389 CG TYR C 80 4775 4032 3177 293 -90 -43 C ATOM 2390 CD1 TYR C 80 -1.189 3.801 -5.680 1.00 29.35 C ANISOU 2390 CD1 TYR C 80 4541 3725 2884 250 -25 -7 C ATOM 2391 CD2 TYR C 80 -2.799 2.742 -7.077 1.00 38.01 C ANISOU 2391 CD2 TYR C 80 5568 4928 3944 277 -110 -93 C ATOM 2392 CE1 TYR C 80 -0.185 3.057 -6.267 1.00 31.91 C ANISOU 2392 CE1 TYR C 80 4880 4094 3152 199 23 -19 C ATOM 2393 CE2 TYR C 80 -1.806 2.004 -7.673 1.00 36.04 C ANISOU 2393 CE2 TYR C 80 5340 4722 3633 224 -60 -109 C ATOM 2394 CZ TYR C 80 -0.493 2.165 -7.259 1.00 42.50 C ANISOU 2394 CZ TYR C 80 6197 5506 4443 187 9 -70 C ATOM 2395 OH TYR C 80 0.520 1.429 -7.841 1.00 37.99 O ANISOU 2395 OH TYR C 80 5640 4976 3818 137 65 -87 O ATOM 2396 N ILE C 81 -6.078 4.948 -3.279 1.00 37.32 N ANISOU 2396 N ILE C 81 5355 4620 4205 461 -160 -110 N ATOM 2397 CA ILE C 81 -6.971 6.062 -2.982 1.00 36.71 C ANISOU 2397 CA ILE C 81 5272 4493 4183 527 -209 -85 C ATOM 2398 C ILE C 81 -6.745 6.699 -1.609 1.00 41.80 C ANISOU 2398 C ILE C 81 5933 5055 4894 533 -152 -80 C ATOM 2399 O ILE C 81 -6.637 6.003 -0.584 1.00 36.36 O ANISOU 2399 O ILE C 81 5212 4356 4249 506 -82 -129 O ATOM 2400 CB ILE C 81 -8.469 5.700 -3.199 1.00 41.93 C ANISOU 2400 CB ILE C 81 5841 5190 4900 575 -263 -143 C ATOM 2401 CG1 ILE C 81 -9.289 6.960 -3.481 1.00 49.20 C ANISOU 2401 CG1 ILE C 81 6767 6079 5850 651 -343 -95 C ATOM 2402 CG2 ILE C 81 -9.032 4.949 -2.016 1.00 40.26 C ANISOU 2402 CG2 ILE C 81 5554 4962 4781 569 -199 -220 C ATOM 2403 CD1 ILE C 81 -8.846 7.719 -4.717 1.00 57.08 C ANISOU 2403 CD1 ILE C 81 7842 7095 6753 661 -413 -8 C ATOM 2404 N GLN C 82 -6.661 8.032 -1.609 1.00 34.81 N ANISOU 2404 N GLN C 82 5104 4109 4013 566 -182 -17 N ATOM 2405 CA GLN C 82 -6.425 8.816 -0.396 1.00 34.59 C ANISOU 2405 CA GLN C 82 5103 3998 4041 572 -134 -12 C ATOM 2406 C GLN C 82 -5.045 8.580 0.209 1.00 36.14 C ANISOU 2406 C GLN C 82 5348 4182 4202 502 -62 -3 C ATOM 2407 O GLN C 82 -4.827 8.858 1.381 1.00 38.09 O ANISOU 2407 O GLN C 82 5602 4379 4490 492 -11 -21 O ATOM 2408 CB GLN C 82 -7.497 8.545 0.662 1.00 39.78 C ANISOU 2408 CB GLN C 82 5684 4637 4794 605 -106 -85 C ATOM 2409 CG GLN C 82 -8.918 8.809 0.195 1.00 52.84 C ANISOU 2409 CG GLN C 82 7275 6301 6502 679 -175 -101 C ATOM 2410 CD GLN C 82 -9.253 10.281 0.138 1.00 63.87 C ANISOU 2410 CD GLN C 82 8709 7623 7934 742 -220 -49 C ATOM 2411 OE1 GLN C 82 -8.453 11.126 0.536 1.00 65.38 O ANISOU 2411 OE1 GLN C 82 8976 7749 8116 726 -192 -8 O ATOM 2412 NE2 GLN C 82 -10.445 10.598 -0.354 1.00 71.36 N ANISOU 2412 NE2 GLN C 82 9603 8579 8930 814 -290 -53 N ATOM 2413 N ALA C 83 -4.111 8.060 -0.576 1.00 31.60 N ANISOU 2413 N ALA C 83 4802 3656 3549 453 -57 23 N ATOM 2414 CA ALA C 83 -2.745 7.936 -0.069 1.00 30.59 C ANISOU 2414 CA ALA C 83 4715 3516 3390 390 5 40 C ATOM 2415 C ALA C 83 -2.205 9.345 0.162 1.00 32.81 C ANISOU 2415 C ALA C 83 5070 3723 3673 390 0 98 C ATOM 2416 O ALA C 83 -2.488 10.263 -0.612 1.00 38.83 O ANISOU 2416 O ALA C 83 5872 4462 4422 423 -54 150 O ATOM 2417 CB ALA C 83 -1.876 7.181 -1.056 1.00 34.37 C ANISOU 2417 CB ALA C 83 5209 4060 3791 343 12 56 C ATOM 2418 N GLN C 84 -1.455 9.536 1.238 1.00 34.87 N ANISOU 2418 N GLN C 84 5350 3947 3953 354 54 90 N ATOM 2419 CA GLN C 84 -0.933 10.866 1.544 1.00 36.11 C ANISOU 2419 CA GLN C 84 5574 4027 4119 346 54 133 C ATOM 2420 C GLN C 84 0.585 10.898 1.325 1.00 35.15 C ANISOU 2420 C GLN C 84 5499 3917 3940 274 85 174 C ATOM 2421 O GLN C 84 1.196 11.958 1.282 1.00 29.34 O ANISOU 2421 O GLN C 84 4823 3125 3198 254 84 220 O ATOM 2422 CB GLN C 84 -1.308 11.256 2.980 1.00 39.28 C ANISOU 2422 CB GLN C 84 5963 4372 4588 359 87 86 C ATOM 2423 CG GLN C 84 -2.799 11.607 3.138 1.00 40.48 C ANISOU 2423 CG GLN C 84 6077 4494 4808 436 57 54 C ATOM 2424 CD GLN C 84 -3.324 11.374 4.548 1.00 46.96 C ANISOU 2424 CD GLN C 84 6858 5297 5687 445 106 -17 C ATOM 2425 OE1 GLN C 84 -3.432 10.233 5.004 1.00 40.04 O ANISOU 2425 OE1 GLN C 84 5931 4474 4809 427 140 -60 O ATOM 2426 NE2 GLN C 84 -3.668 12.455 5.235 1.00 49.80 N ANISOU 2426 NE2 GLN C 84 7244 5579 6099 472 113 -29 N ATOM 2427 N CYS C 85 1.179 9.720 1.163 1.00 29.77 N ANISOU 2427 N CYS C 85 4786 3305 3222 236 115 156 N ATOM 2428 CA CYS C 85 2.623 9.595 0.936 1.00 32.59 C ANISOU 2428 CA CYS C 85 5170 3682 3529 170 149 188 C ATOM 2429 C CYS C 85 2.915 8.188 0.444 1.00 35.04 C ANISOU 2429 C CYS C 85 5434 4073 3806 150 170 163 C ATOM 2430 O CYS C 85 2.031 7.320 0.464 1.00 32.75 O ANISOU 2430 O CYS C 85 5093 3815 3536 182 164 116 O ATOM 2431 CB CYS C 85 3.415 9.895 2.214 1.00 30.47 C ANISOU 2431 CB CYS C 85 4911 3379 3289 130 190 175 C ATOM 2432 SG CYS C 85 2.951 8.884 3.656 1.00 32.86 S ANISOU 2432 SG CYS C 85 5149 3700 3638 141 225 101 S ATOM 2433 N ALA C 86 4.145 7.954 -0.004 1.00 30.93 N ANISOU 2433 N ALA C 86 4930 3582 3240 97 200 190 N ATOM 2434 CA ALA C 86 4.495 6.654 -0.568 1.00 28.95 C ANISOU 2434 CA ALA C 86 4639 3401 2959 79 226 165 C ATOM 2435 C ALA C 86 5.969 6.337 -0.411 1.00 28.72 C ANISOU 2435 C ALA C 86 4608 3392 2913 21 277 180 C ATOM 2436 O ALA C 86 6.794 7.229 -0.277 1.00 31.16 O ANISOU 2436 O ALA C 86 4957 3671 3214 -14 285 221 O ATOM 2437 CB ALA C 86 4.122 6.600 -2.056 1.00 30.52 C ANISOU 2437 CB ALA C 86 4857 3642 3098 92 192 184 C ATOM 2438 N ILE C 87 6.283 5.049 -0.437 1.00 26.42 N ANISOU 2438 N ILE C 87 4267 3149 2623 10 312 144 N ATOM 2439 CA ILE C 87 7.643 4.606 -0.659 1.00 28.32 C ANISOU 2439 CA ILE C 87 4497 3420 2843 -38 359 158 C ATOM 2440 C ILE C 87 7.639 3.743 -1.929 1.00 29.85 C ANISOU 2440 C ILE C 87 4678 3672 2992 -40 372 140 C ATOM 2441 O ILE C 87 6.815 2.837 -2.064 1.00 32.04 O ANISOU 2441 O ILE C 87 4920 3971 3283 -11 367 92 O ATOM 2442 CB ILE C 87 8.172 3.802 0.546 1.00 30.05 C ANISOU 2442 CB ILE C 87 4665 3641 3111 -48 396 133 C ATOM 2443 CG1 ILE C 87 8.358 4.735 1.763 1.00 32.69 C ANISOU 2443 CG1 ILE C 87 5020 3928 3475 -58 385 149 C ATOM 2444 CG2 ILE C 87 9.471 3.081 0.166 1.00 28.68 C ANISOU 2444 CG2 ILE C 87 4464 3508 2925 -86 444 139 C ATOM 2445 CD1 ILE C 87 8.467 4.009 3.115 1.00 33.63 C ANISOU 2445 CD1 ILE C 87 5095 4048 3637 -54 406 123 C ATOM 2446 N ILE C 88 8.520 4.059 -2.872 1.00 33.40 N ANISOU 2446 N ILE C 88 5159 4146 3386 -77 390 175 N ATOM 2447 CA ILE C 88 8.783 3.165 -4.001 1.00 32.00 C ANISOU 2447 CA ILE C 88 4967 4028 3162 -90 419 150 C ATOM 2448 C ILE C 88 10.049 2.369 -3.704 1.00 31.12 C ANISOU 2448 C ILE C 88 4812 3938 3076 -124 485 137 C ATOM 2449 O ILE C 88 11.101 2.938 -3.422 1.00 30.73 O ANISOU 2449 O ILE C 88 4771 3876 3030 -161 508 176 O ATOM 2450 CB ILE C 88 8.982 3.931 -5.306 1.00 29.81 C ANISOU 2450 CB ILE C 88 4752 3774 2799 -111 406 196 C ATOM 2451 CG1 ILE C 88 7.777 4.837 -5.584 1.00 30.20 C ANISOU 2451 CG1 ILE C 88 4847 3799 2829 -71 333 223 C ATOM 2452 CG2 ILE C 88 9.202 2.945 -6.476 1.00 31.50 C ANISOU 2452 CG2 ILE C 88 4953 4058 2956 -126 439 159 C ATOM 2453 CD1 ILE C 88 7.872 5.613 -6.932 1.00 34.70 C ANISOU 2453 CD1 ILE C 88 5487 4392 3304 -86 313 280 C ATOM 2454 N MET C 89 9.936 1.049 -3.734 1.00 27.89 N ANISOU 2454 N MET C 89 4350 3554 2691 -111 515 82 N ATOM 2455 CA MET C 89 11.068 0.197 -3.417 1.00 30.75 C ANISOU 2455 CA MET C 89 4662 3931 3090 -132 577 69 C ATOM 2456 C MET C 89 11.559 -0.542 -4.651 1.00 33.47 C ANISOU 2456 C MET C 89 4998 4326 3392 -152 624 39 C ATOM 2457 O MET C 89 10.764 -0.963 -5.482 1.00 32.15 O ANISOU 2457 O MET C 89 4841 4185 3188 -138 611 0 O ATOM 2458 CB MET C 89 10.666 -0.840 -2.355 1.00 34.69 C ANISOU 2458 CB MET C 89 5105 4409 3665 -101 586 30 C ATOM 2459 CG MET C 89 11.857 -1.513 -1.686 1.00 28.69 C ANISOU 2459 CG MET C 89 4294 3651 2957 -115 636 36 C ATOM 2460 SD MET C 89 11.445 -2.378 -0.151 1.00 45.69 S ANISOU 2460 SD MET C 89 6397 5769 5193 -80 636 21 S ATOM 2461 CE MET C 89 11.098 -0.984 0.911 1.00 43.20 C ANISOU 2461 CE MET C 89 6123 5419 4871 -82 580 63 C ATOM 2462 N PHE C 90 12.877 -0.683 -4.760 1.00 30.91 N ANISOU 2462 N PHE C 90 4652 4019 3074 -185 679 53 N ATOM 2463 CA PHE C 90 13.475 -1.648 -5.662 1.00 32.04 C ANISOU 2463 CA PHE C 90 4767 4205 3202 -199 742 11 C ATOM 2464 C PHE C 90 14.551 -2.448 -4.935 1.00 35.24 C ANISOU 2464 C PHE C 90 5101 4603 3686 -201 797 3 C ATOM 2465 O PHE C 90 14.799 -2.251 -3.734 1.00 30.12 O ANISOU 2465 O PHE C 90 4428 3922 3095 -193 779 33 O ATOM 2466 CB PHE C 90 14.030 -0.981 -6.944 1.00 22.54 C ANISOU 2466 CB PHE C 90 3612 3044 1907 -241 765 35 C ATOM 2467 CG PHE C 90 15.182 -0.048 -6.702 1.00 28.67 C ANISOU 2467 CG PHE C 90 4397 3812 2685 -283 786 97 C ATOM 2468 CD1 PHE C 90 14.955 1.253 -6.261 1.00 31.50 C ANISOU 2468 CD1 PHE C 90 4803 4133 3031 -292 734 157 C ATOM 2469 CD2 PHE C 90 16.491 -0.469 -6.899 1.00 30.95 C ANISOU 2469 CD2 PHE C 90 4639 4126 2993 -314 859 91 C ATOM 2470 CE1 PHE C 90 16.014 2.127 -6.027 1.00 29.05 C ANISOU 2470 CE1 PHE C 90 4498 3811 2727 -337 753 209 C ATOM 2471 CE2 PHE C 90 17.561 0.390 -6.662 1.00 33.32 C ANISOU 2471 CE2 PHE C 90 4938 4421 3302 -358 878 144 C ATOM 2472 CZ PHE C 90 17.325 1.695 -6.228 1.00 34.70 C ANISOU 2472 CZ PHE C 90 5164 4558 3462 -373 825 202 C ATOM 2473 N ASP C 91 15.174 -3.360 -5.679 1.00 30.93 N ANISOU 2473 N ASP C 91 4522 4088 3141 -210 863 -39 N ATOM 2474 CA ASP C 91 16.129 -4.301 -5.145 1.00 28.45 C ANISOU 2474 CA ASP C 91 4133 3767 2909 -202 918 -53 C ATOM 2475 C ASP C 91 17.488 -4.022 -5.791 1.00 34.69 C ANISOU 2475 C ASP C 91 4908 4593 3678 -243 978 -37 C ATOM 2476 O ASP C 91 17.625 -4.104 -7.009 1.00 40.62 O ANISOU 2476 O ASP C 91 5683 5384 4367 -266 1019 -65 O ATOM 2477 CB ASP C 91 15.612 -5.717 -5.466 1.00 34.49 C ANISOU 2477 CB ASP C 91 4867 4529 3710 -171 952 -129 C ATOM 2478 CG ASP C 91 16.544 -6.826 -5.015 1.00 42.45 C ANISOU 2478 CG ASP C 91 5797 5522 4811 -154 1015 -146 C ATOM 2479 OD1 ASP C 91 17.729 -6.569 -4.698 1.00 46.85 O ANISOU 2479 OD1 ASP C 91 6318 6087 5395 -168 1040 -108 O ATOM 2480 OD2 ASP C 91 16.080 -7.983 -4.996 1.00 49.06 O ANISOU 2480 OD2 ASP C 91 6606 6338 5698 -125 1039 -201 O ATOM 2481 N VAL C 92 18.487 -3.675 -4.989 1.00 37.18 N ANISOU 2481 N VAL C 92 5184 4900 4044 -256 983 8 N ATOM 2482 CA VAL C 92 19.793 -3.316 -5.554 1.00 36.21 C ANISOU 2482 CA VAL C 92 5039 4812 3908 -301 1041 26 C ATOM 2483 C VAL C 92 20.577 -4.507 -6.135 1.00 37.38 C ANISOU 2483 C VAL C 92 5121 4984 4097 -293 1128 -27 C ATOM 2484 O VAL C 92 21.655 -4.319 -6.695 1.00 39.65 O ANISOU 2484 O VAL C 92 5383 5305 4377 -330 1187 -21 O ATOM 2485 CB VAL C 92 20.690 -2.546 -4.552 1.00 35.81 C ANISOU 2485 CB VAL C 92 4955 4749 3901 -325 1019 85 C ATOM 2486 CG1 VAL C 92 19.927 -1.372 -3.918 1.00 39.34 C ANISOU 2486 CG1 VAL C 92 5468 5164 4316 -332 938 128 C ATOM 2487 CG2 VAL C 92 21.233 -3.492 -3.491 1.00 36.26 C ANISOU 2487 CG2 VAL C 92 4925 4792 4060 -288 1026 79 C ATOM 2488 N THR C 93 20.043 -5.718 -6.000 1.00 36.60 N ANISOU 2488 N THR C 93 4994 4867 4047 -247 1140 -79 N ATOM 2489 CA THR C 93 20.648 -6.877 -6.640 1.00 47.31 C ANISOU 2489 CA THR C 93 6296 6237 5443 -236 1226 -140 C ATOM 2490 C THR C 93 19.903 -7.263 -7.918 1.00 48.84 C ANISOU 2490 C THR C 93 6540 6456 5560 -244 1253 -209 C ATOM 2491 O THR C 93 20.247 -8.249 -8.567 1.00 51.06 O ANISOU 2491 O THR C 93 6787 6748 5864 -237 1328 -275 O ATOM 2492 CB THR C 93 20.684 -8.096 -5.703 1.00 49.60 C ANISOU 2492 CB THR C 93 6515 6481 5849 -181 1234 -158 C ATOM 2493 OG1 THR C 93 19.366 -8.644 -5.573 1.00 51.15 O ANISOU 2493 OG1 THR C 93 6744 6646 6045 -151 1200 -194 O ATOM 2494 CG2 THR C 93 21.219 -7.701 -4.334 1.00 51.10 C ANISOU 2494 CG2 THR C 93 6663 6650 6101 -169 1188 -87 C ATOM 2495 N SER C 94 18.876 -6.490 -8.268 1.00 44.25 N ANISOU 2495 N SER C 94 6039 5886 4889 -258 1191 -196 N ATOM 2496 CA SER C 94 18.056 -6.793 -9.438 1.00 42.43 C ANISOU 2496 CA SER C 94 5859 5687 4575 -266 1199 -258 C ATOM 2497 C SER C 94 17.769 -5.540 -10.269 1.00 43.21 C ANISOU 2497 C SER C 94 6044 5828 4547 -306 1164 -217 C ATOM 2498 O SER C 94 16.846 -4.772 -9.990 1.00 40.38 O ANISOU 2498 O SER C 94 5736 5455 4153 -298 1082 -178 O ATOM 2499 CB SER C 94 16.762 -7.501 -9.040 1.00 45.77 C ANISOU 2499 CB SER C 94 6285 6075 5031 -226 1152 -302 C ATOM 2500 OG SER C 94 15.982 -7.795 -10.185 1.00 49.97 O ANISOU 2500 OG SER C 94 6860 6644 5481 -237 1153 -368 O ATOM 2501 N ARG C 95 18.576 -5.358 -11.306 1.00 34.77 N ANISOU 2501 N ARG C 95 4989 4810 3412 -348 1231 -225 N ATOM 2502 CA ARG C 95 18.543 -4.153 -12.123 1.00 40.89 C ANISOU 2502 CA ARG C 95 5845 5625 4068 -392 1212 -172 C ATOM 2503 C ARG C 95 17.167 -3.875 -12.740 1.00 34.31 C ANISOU 2503 C ARG C 95 5088 4810 3138 -382 1139 -182 C ATOM 2504 O ARG C 95 16.779 -2.722 -12.891 1.00 38.78 O ANISOU 2504 O ARG C 95 5720 5378 3635 -396 1081 -113 O ATOM 2505 CB ARG C 95 19.626 -4.237 -13.213 1.00 50.04 C ANISOU 2505 CB ARG C 95 7001 6840 5170 -440 1314 -192 C ATOM 2506 CG ARG C 95 19.943 -2.910 -13.874 1.00 62.35 C ANISOU 2506 CG ARG C 95 8634 8431 6624 -493 1311 -116 C ATOM 2507 CD ARG C 95 21.137 -3.028 -14.806 1.00 69.19 C ANISOU 2507 CD ARG C 95 9487 9353 7451 -543 1425 -134 C ATOM 2508 NE ARG C 95 22.399 -3.215 -14.093 1.00 71.24 N ANISOU 2508 NE ARG C 95 9653 9590 7824 -550 1486 -125 N ATOM 2509 CZ ARG C 95 23.079 -2.234 -13.505 1.00 74.01 C ANISOU 2509 CZ ARG C 95 9994 9919 8207 -580 1474 -46 C ATOM 2510 NH1 ARG C 95 22.614 -0.991 -13.522 1.00 72.75 N ANISOU 2510 NH1 ARG C 95 9915 9746 7981 -604 1410 31 N ATOM 2511 NH2 ARG C 95 24.223 -2.498 -12.892 1.00 78.66 N ANISOU 2511 NH2 ARG C 95 10488 10497 8901 -585 1526 -46 N ATOM 2512 N VAL C 96 16.430 -4.919 -13.091 1.00 34.62 N ANISOU 2512 N VAL C 96 5115 4861 3177 -358 1140 -267 N ATOM 2513 CA VAL C 96 15.097 -4.718 -13.666 1.00 40.10 C ANISOU 2513 CA VAL C 96 5871 5580 3786 -348 1064 -283 C ATOM 2514 C VAL C 96 14.085 -4.097 -12.680 1.00 39.98 C ANISOU 2514 C VAL C 96 5867 5513 3812 -311 962 -233 C ATOM 2515 O VAL C 96 13.176 -3.374 -13.085 1.00 36.76 O ANISOU 2515 O VAL C 96 5519 5122 3327 -307 888 -204 O ATOM 2516 CB VAL C 96 14.518 -6.014 -14.270 1.00 42.72 C ANISOU 2516 CB VAL C 96 6182 5937 4114 -337 1088 -398 C ATOM 2517 CG1 VAL C 96 14.036 -6.956 -13.173 1.00 42.54 C ANISOU 2517 CG1 VAL C 96 6091 5849 4224 -293 1075 -440 C ATOM 2518 CG2 VAL C 96 13.376 -5.680 -15.220 1.00 50.04 C ANISOU 2518 CG2 VAL C 96 7178 6918 4917 -343 1018 -414 C ATOM 2519 N THR C 97 14.242 -4.358 -11.386 1.00 35.01 N ANISOU 2519 N THR C 97 5180 4821 3301 -284 958 -220 N ATOM 2520 CA THR C 97 13.346 -3.722 -10.414 1.00 34.07 C ANISOU 2520 CA THR C 97 5072 4654 3218 -252 871 -174 C ATOM 2521 C THR C 97 13.569 -2.217 -10.382 1.00 33.96 C ANISOU 2521 C THR C 97 5117 4634 3154 -273 832 -80 C ATOM 2522 O THR C 97 12.625 -1.443 -10.164 1.00 30.40 O ANISOU 2522 O THR C 97 4705 4162 2682 -252 754 -44 O ATOM 2523 CB THR C 97 13.476 -4.322 -8.996 1.00 30.73 C ANISOU 2523 CB THR C 97 4581 4171 2924 -221 877 -179 C ATOM 2524 OG1 THR C 97 14.762 -4.004 -8.449 1.00 33.95 O ANISOU 2524 OG1 THR C 97 4960 4565 3374 -240 919 -130 O ATOM 2525 CG2 THR C 97 13.299 -5.833 -9.056 1.00 33.21 C ANISOU 2525 CG2 THR C 97 4841 4480 3297 -202 924 -267 C ATOM 2526 N TYR C 98 14.811 -1.797 -10.608 1.00 32.81 N ANISOU 2526 N TYR C 98 4972 4501 2993 -313 890 -42 N ATOM 2527 CA TYR C 98 15.085 -0.369 -10.736 1.00 32.15 C ANISOU 2527 CA TYR C 98 4949 4409 2856 -342 864 45 C ATOM 2528 C TYR C 98 14.542 0.188 -12.053 1.00 36.17 C ANISOU 2528 C TYR C 98 5540 4966 3235 -358 839 63 C ATOM 2529 O TYR C 98 14.102 1.339 -12.118 1.00 34.61 O ANISOU 2529 O TYR C 98 5406 4750 2996 -358 780 133 O ATOM 2530 CB TYR C 98 16.582 -0.076 -10.615 1.00 39.13 C ANISOU 2530 CB TYR C 98 5807 5296 3766 -388 936 79 C ATOM 2531 CG TYR C 98 16.902 1.393 -10.795 1.00 42.41 C ANISOU 2531 CG TYR C 98 6286 5697 4131 -427 917 167 C ATOM 2532 CD1 TYR C 98 16.625 2.314 -9.788 1.00 36.19 C ANISOU 2532 CD1 TYR C 98 5513 4847 3389 -417 856 220 C ATOM 2533 CD2 TYR C 98 17.459 1.863 -11.979 1.00 41.20 C ANISOU 2533 CD2 TYR C 98 6184 5589 3881 -476 965 196 C ATOM 2534 CE1 TYR C 98 16.898 3.663 -9.951 1.00 32.78 C ANISOU 2534 CE1 TYR C 98 5143 4391 2921 -454 842 298 C ATOM 2535 CE2 TYR C 98 17.738 3.210 -12.155 1.00 39.28 C ANISOU 2535 CE2 TYR C 98 6004 5324 3597 -514 952 282 C ATOM 2536 CZ TYR C 98 17.462 4.106 -11.138 1.00 43.23 C ANISOU 2536 CZ TYR C 98 6516 5755 4155 -503 891 332 C ATOM 2537 OH TYR C 98 17.736 5.444 -11.312 1.00 40.18 O ANISOU 2537 OH TYR C 98 6194 5336 3735 -542 882 415 O ATOM 2538 N LYS C 99 14.620 -0.619 -13.112 1.00 43.07 N ANISOU 2538 N LYS C 99 6416 5904 4046 -372 886 2 N ATOM 2539 CA LYS C 99 14.080 -0.234 -14.413 1.00 41.66 C ANISOU 2539 CA LYS C 99 6315 5785 3731 -387 860 12 C ATOM 2540 C LYS C 99 12.580 0.033 -14.322 1.00 44.02 C ANISOU 2540 C LYS C 99 6642 6071 4011 -341 751 16 C ATOM 2541 O LYS C 99 12.057 0.912 -15.003 1.00 38.47 O ANISOU 2541 O LYS C 99 6013 5390 3215 -342 696 72 O ATOM 2542 CB LYS C 99 14.370 -1.309 -15.468 1.00 46.61 C ANISOU 2542 CB LYS C 99 6930 6483 4298 -409 931 -75 C ATOM 2543 CG LYS C 99 15.792 -1.247 -16.028 1.00 57.56 C ANISOU 2543 CG LYS C 99 8315 7902 5653 -463 1038 -63 C ATOM 2544 CD LYS C 99 16.041 -2.340 -17.055 1.00 67.58 C ANISOU 2544 CD LYS C 99 9572 9241 6865 -482 1114 -161 C ATOM 2545 CE LYS C 99 17.443 -2.236 -17.633 1.00 75.38 C ANISOU 2545 CE LYS C 99 10557 10264 7822 -537 1228 -151 C ATOM 2546 NZ LYS C 99 18.482 -2.594 -16.632 1.00 78.49 N ANISOU 2546 NZ LYS C 99 10858 10606 8358 -533 1288 -154 N ATOM 2547 N ASN C 100 11.895 -0.716 -13.462 1.00 41.85 N ANISOU 2547 N ASN C 100 6309 5762 3831 -299 722 -40 N ATOM 2548 CA ASN C 100 10.446 -0.561 -13.311 1.00 45.88 C ANISOU 2548 CA ASN C 100 6831 6262 4340 -254 625 -47 C ATOM 2549 C ASN C 100 10.019 0.590 -12.399 1.00 40.01 C ANISOU 2549 C ASN C 100 6107 5452 3643 -227 558 33 C ATOM 2550 O ASN C 100 8.834 0.883 -12.282 1.00 39.38 O ANISOU 2550 O ASN C 100 6038 5361 3564 -187 477 37 O ATOM 2551 CB ASN C 100 9.811 -1.879 -12.853 1.00 45.15 C ANISOU 2551 CB ASN C 100 6667 6162 4326 -226 628 -145 C ATOM 2552 CG ASN C 100 9.807 -2.926 -13.959 1.00 47.96 C ANISOU 2552 CG ASN C 100 7017 6587 4619 -247 669 -235 C ATOM 2553 OD1 ASN C 100 10.018 -4.117 -13.719 1.00 46.43 O ANISOU 2553 OD1 ASN C 100 6764 6384 4494 -246 726 -316 O ATOM 2554 ND2 ASN C 100 9.581 -2.474 -15.187 1.00 34.88 N ANISOU 2554 ND2 ASN C 100 5425 4999 2830 -267 643 -222 N ATOM 2555 N VAL C 101 10.983 1.250 -11.772 1.00 40.55 N ANISOU 2555 N VAL C 101 6178 5477 3752 -249 593 92 N ATOM 2556 CA VAL C 101 10.666 2.365 -10.871 1.00 36.03 C ANISOU 2556 CA VAL C 101 5628 4836 3227 -229 539 161 C ATOM 2557 C VAL C 101 9.832 3.471 -11.550 1.00 37.72 C ANISOU 2557 C VAL C 101 5919 5051 3363 -212 462 224 C ATOM 2558 O VAL C 101 8.811 3.871 -10.997 1.00 40.58 O ANISOU 2558 O VAL C 101 6280 5373 3765 -166 391 234 O ATOM 2559 CB VAL C 101 11.923 2.903 -10.127 1.00 31.27 C ANISOU 2559 CB VAL C 101 5014 4190 2677 -265 590 207 C ATOM 2560 CG1 VAL C 101 11.727 4.345 -9.662 1.00 34.49 C ANISOU 2560 CG1 VAL C 101 5475 4537 3094 -262 540 288 C ATOM 2561 CG2 VAL C 101 12.257 1.997 -8.905 1.00 29.68 C ANISOU 2561 CG2 VAL C 101 4728 3961 2586 -252 621 157 C ATOM 2562 N PRO C 102 10.230 3.935 -12.759 1.00 40.23 N ANISOU 2562 N PRO C 102 6301 5416 3570 -246 476 268 N ATOM 2563 CA PRO C 102 9.414 4.931 -13.471 1.00 38.57 C ANISOU 2563 CA PRO C 102 6166 5210 3279 -225 398 336 C ATOM 2564 C PRO C 102 7.951 4.513 -13.627 1.00 41.44 C ANISOU 2564 C PRO C 102 6511 5597 3636 -168 313 290 C ATOM 2565 O PRO C 102 7.064 5.355 -13.470 1.00 38.70 O ANISOU 2565 O PRO C 102 6192 5214 3297 -125 233 340 O ATOM 2566 CB PRO C 102 10.078 5.004 -14.859 1.00 40.07 C ANISOU 2566 CB PRO C 102 6416 5473 3337 -274 442 364 C ATOM 2567 CG PRO C 102 11.503 4.664 -14.600 1.00 41.51 C ANISOU 2567 CG PRO C 102 6566 5653 3555 -329 548 349 C ATOM 2568 CD PRO C 102 11.469 3.617 -13.498 1.00 39.39 C ANISOU 2568 CD PRO C 102 6202 5359 3407 -305 567 264 C ATOM 2569 N ASN C 103 7.712 3.240 -13.947 1.00 40.46 N ANISOU 2569 N ASN C 103 6338 5532 3502 -168 331 195 N ATOM 2570 CA ASN C 103 6.356 2.703 -14.054 1.00 40.31 C ANISOU 2570 CA ASN C 103 6287 5540 3489 -123 257 135 C ATOM 2571 C ASN C 103 5.556 2.843 -12.753 1.00 46.86 C ANISOU 2571 C ASN C 103 7067 6295 4443 -73 213 127 C ATOM 2572 O ASN C 103 4.373 3.210 -12.765 1.00 39.08 O ANISOU 2572 O ASN C 103 6081 5305 3462 -26 128 134 O ATOM 2573 CB ASN C 103 6.397 1.222 -14.445 1.00 41.75 C ANISOU 2573 CB ASN C 103 6417 5782 3664 -142 303 22 C ATOM 2574 CG ASN C 103 7.026 0.986 -15.810 1.00 52.82 C ANISOU 2574 CG ASN C 103 7867 7268 4934 -189 345 12 C ATOM 2575 OD1 ASN C 103 7.739 -0.001 -16.012 1.00 58.19 O ANISOU 2575 OD1 ASN C 103 8515 7976 5618 -222 428 -59 O ATOM 2576 ND2 ASN C 103 6.765 1.886 -16.753 1.00 43.66 N ANISOU 2576 ND2 ASN C 103 6784 6148 3656 -190 291 84 N ATOM 2577 N TRP C 104 6.195 2.525 -11.633 1.00 41.00 N ANISOU 2577 N TRP C 104 6280 5499 3799 -83 273 109 N ATOM 2578 CA TRP C 104 5.515 2.584 -10.348 1.00 40.98 C ANISOU 2578 CA TRP C 104 6232 5431 3909 -42 244 96 C ATOM 2579 C TRP C 104 5.171 4.024 -10.028 1.00 40.33 C ANISOU 2579 C TRP C 104 6198 5291 3833 -15 188 181 C ATOM 2580 O TRP C 104 4.070 4.334 -9.564 1.00 41.28 O ANISOU 2580 O TRP C 104 6303 5382 4002 34 126 177 O ATOM 2581 CB TRP C 104 6.369 1.970 -9.236 1.00 35.03 C ANISOU 2581 CB TRP C 104 5426 4638 3245 -61 318 68 C ATOM 2582 CG TRP C 104 6.324 0.484 -9.268 1.00 39.29 C ANISOU 2582 CG TRP C 104 5904 5210 3813 -66 361 -24 C ATOM 2583 CD1 TRP C 104 7.355 -0.364 -9.539 1.00 43.50 C ANISOU 2583 CD1 TRP C 104 6416 5769 4342 -103 440 -58 C ATOM 2584 CD2 TRP C 104 5.169 -0.334 -9.067 1.00 33.88 C ANISOU 2584 CD2 TRP C 104 5168 4531 3172 -35 330 -95 C ATOM 2585 NE1 TRP C 104 6.914 -1.666 -9.504 1.00 40.05 N ANISOU 2585 NE1 TRP C 104 5923 5348 3946 -94 460 -146 N ATOM 2586 CE2 TRP C 104 5.576 -1.673 -9.209 1.00 39.82 C ANISOU 2586 CE2 TRP C 104 5876 5308 3948 -56 394 -170 C ATOM 2587 CE3 TRP C 104 3.830 -0.064 -8.752 1.00 38.25 C ANISOU 2587 CE3 TRP C 104 5706 5068 3757 9 257 -105 C ATOM 2588 CZ2 TRP C 104 4.690 -2.741 -9.069 1.00 48.80 C ANISOU 2588 CZ2 TRP C 104 6958 6450 5135 -40 389 -253 C ATOM 2589 CZ3 TRP C 104 2.954 -1.118 -8.614 1.00 43.34 C ANISOU 2589 CZ3 TRP C 104 6291 5726 4450 24 252 -188 C ATOM 2590 CH2 TRP C 104 3.387 -2.444 -8.770 1.00 52.52 C ANISOU 2590 CH2 TRP C 104 7414 6909 5633 -3 318 -260 C ATOM 2591 N HIS C 105 6.119 4.909 -10.290 1.00 36.50 N ANISOU 2591 N HIS C 105 5772 4788 3307 -49 214 256 N ATOM 2592 CA HIS C 105 5.907 6.315 -10.015 1.00 36.79 C ANISOU 2592 CA HIS C 105 5863 4760 3357 -30 170 339 C ATOM 2593 C HIS C 105 4.740 6.807 -10.868 1.00 41.76 C ANISOU 2593 C HIS C 105 6527 5412 3927 17 80 369 C ATOM 2594 O HIS C 105 3.837 7.471 -10.370 1.00 39.89 O ANISOU 2594 O HIS C 105 6290 5124 3744 68 19 390 O ATOM 2595 CB HIS C 105 7.192 7.094 -10.273 1.00 36.65 C ANISOU 2595 CB HIS C 105 5902 4722 3301 -85 222 410 C ATOM 2596 CG HIS C 105 7.056 8.571 -10.083 1.00 42.15 C ANISOU 2596 CG HIS C 105 6661 5343 4010 -73 184 499 C ATOM 2597 ND1 HIS C 105 6.666 9.416 -11.101 1.00 45.01 N ANISOU 2597 ND1 HIS C 105 7097 5711 4292 -59 134 574 N ATOM 2598 CD2 HIS C 105 7.270 9.358 -9.002 1.00 38.55 C ANISOU 2598 CD2 HIS C 105 6210 4802 3638 -72 190 523 C ATOM 2599 CE1 HIS C 105 6.638 10.659 -10.651 1.00 48.77 C ANISOU 2599 CE1 HIS C 105 7619 6099 4811 -48 113 643 C ATOM 2600 NE2 HIS C 105 7.005 10.652 -9.382 1.00 44.46 N ANISOU 2600 NE2 HIS C 105 7032 5497 4364 -58 148 608 N ATOM 2601 N ARG C 106 4.752 6.439 -12.149 1.00 50.15 N ANISOU 2601 N ARG C 106 7617 6557 4881 0 71 367 N ATOM 2602 CA ARG C 106 3.679 6.791 -13.075 1.00 52.63 C ANISOU 2602 CA ARG C 106 7962 6912 5123 42 -21 394 C ATOM 2603 C ARG C 106 2.294 6.373 -12.566 1.00 52.53 C ANISOU 2603 C ARG C 106 7881 6896 5183 103 -89 332 C ATOM 2604 O ARG C 106 1.366 7.185 -12.555 1.00 49.18 O ANISOU 2604 O ARG C 106 7469 6441 4775 159 -169 377 O ATOM 2605 CB ARG C 106 3.949 6.172 -14.452 1.00 56.22 C ANISOU 2605 CB ARG C 106 8444 7471 5445 6 -10 375 C ATOM 2606 CG ARG C 106 2.774 6.245 -15.420 1.00 65.78 C ANISOU 2606 CG ARG C 106 9670 8747 6574 47 -112 381 C ATOM 2607 CD ARG C 106 3.123 5.623 -16.771 1.00 71.26 C ANISOU 2607 CD ARG C 106 10399 9553 7126 3 -95 355 C ATOM 2608 NE ARG C 106 3.659 4.269 -16.638 1.00 74.09 N ANISOU 2608 NE ARG C 106 10698 9948 7506 -40 -13 243 N ATOM 2609 CZ ARG C 106 2.912 3.184 -16.456 1.00 74.20 C ANISOU 2609 CZ ARG C 106 10636 9992 7564 -24 -30 136 C ATOM 2610 NH1 ARG C 106 1.591 3.291 -16.384 1.00 76.45 N ANISOU 2610 NH1 ARG C 106 10889 10283 7874 31 -129 122 N ATOM 2611 NH2 ARG C 106 3.484 1.991 -16.344 1.00 70.21 N ANISOU 2611 NH2 ARG C 106 10084 9508 7084 -63 52 42 N ATOM 2612 N ASP C 107 2.161 5.109 -12.161 1.00 45.32 N ANISOU 2612 N ASP C 107 6892 6011 4318 94 -54 229 N ATOM 2613 CA ASP C 107 0.902 4.576 -11.619 1.00 46.00 C ANISOU 2613 CA ASP C 107 6902 6094 4481 142 -103 160 C ATOM 2614 C ASP C 107 0.443 5.360 -10.393 1.00 46.20 C ANISOU 2614 C ASP C 107 6911 6026 4616 186 -121 189 C ATOM 2615 O ASP C 107 -0.723 5.755 -10.283 1.00 43.49 O ANISOU 2615 O ASP C 107 6546 5670 4309 243 -195 191 O ATOM 2616 CB ASP C 107 1.065 3.102 -11.221 1.00 46.59 C ANISOU 2616 CB ASP C 107 6905 6193 4604 114 -40 53 C ATOM 2617 CG ASP C 107 1.375 2.207 -12.400 1.00 58.99 C ANISOU 2617 CG ASP C 107 8482 7854 6077 74 -20 3 C ATOM 2618 OD1 ASP C 107 1.242 2.678 -13.553 1.00 57.53 O ANISOU 2618 OD1 ASP C 107 8352 7726 5780 72 -70 43 O ATOM 2619 OD2 ASP C 107 1.750 1.033 -12.171 1.00 63.52 O ANISOU 2619 OD2 ASP C 107 9008 8441 6687 44 47 -77 O ATOM 2620 N LEU C 108 1.373 5.570 -9.468 1.00 46.65 N ANISOU 2620 N LEU C 108 6976 6022 4727 158 -52 206 N ATOM 2621 CA LEU C 108 1.098 6.280 -8.225 1.00 48.05 C ANISOU 2621 CA LEU C 108 7142 6111 5002 189 -55 224 C ATOM 2622 C LEU C 108 0.603 7.704 -8.495 1.00 52.22 C ANISOU 2622 C LEU C 108 7728 6593 5521 232 -122 308 C ATOM 2623 O LEU C 108 -0.448 8.119 -8.010 1.00 51.76 O ANISOU 2623 O LEU C 108 7642 6496 5527 290 -173 302 O ATOM 2624 CB LEU C 108 2.373 6.306 -7.370 1.00 41.38 C ANISOU 2624 CB LEU C 108 6307 5223 4192 141 28 234 C ATOM 2625 CG LEU C 108 2.402 7.126 -6.090 1.00 48.91 C ANISOU 2625 CG LEU C 108 7265 6088 5231 155 37 255 C ATOM 2626 CD1 LEU C 108 1.397 6.573 -5.086 1.00 40.25 C ANISOU 2626 CD1 LEU C 108 6098 4974 4222 195 29 186 C ATOM 2627 CD2 LEU C 108 3.815 7.115 -5.510 1.00 52.89 C ANISOU 2627 CD2 LEU C 108 7781 6570 5744 97 111 268 C ATOM 2628 N VAL C 109 1.369 8.441 -9.288 1.00 45.48 N ANISOU 2628 N VAL C 109 6952 5740 4588 204 -119 388 N ATOM 2629 CA VAL C 109 1.105 9.854 -9.543 1.00 51.78 C ANISOU 2629 CA VAL C 109 7818 6480 5378 237 -171 482 C ATOM 2630 C VAL C 109 -0.168 10.092 -10.377 1.00 52.91 C ANISOU 2630 C VAL C 109 7960 6658 5486 303 -273 503 C ATOM 2631 O VAL C 109 -0.775 11.162 -10.314 1.00 55.34 O ANISOU 2631 O VAL C 109 8295 6904 5826 356 -330 564 O ATOM 2632 CB VAL C 109 2.341 10.509 -10.197 1.00 55.20 C ANISOU 2632 CB VAL C 109 8336 6904 5733 180 -130 565 C ATOM 2633 CG1 VAL C 109 1.968 11.736 -11.011 1.00 56.97 C ANISOU 2633 CG1 VAL C 109 8639 7100 5908 214 -196 671 C ATOM 2634 CG2 VAL C 109 3.380 10.835 -9.126 1.00 56.74 C ANISOU 2634 CG2 VAL C 109 8535 7028 5997 135 -54 566 C ATOM 2635 N ARG C 110 -0.575 9.087 -11.141 1.00 56.73 N ANISOU 2635 N ARG C 110 8407 7240 5909 299 -298 448 N ATOM 2636 CA ARG C 110 -1.842 9.147 -11.863 1.00 60.24 C ANISOU 2636 CA ARG C 110 8831 7732 6324 359 -401 450 C ATOM 2637 C ARG C 110 -3.032 9.270 -10.896 1.00 60.25 C ANISOU 2637 C ARG C 110 8758 7682 6451 427 -442 408 C ATOM 2638 O ARG C 110 -3.962 10.033 -11.145 1.00 63.96 O ANISOU 2638 O ARG C 110 9231 8134 6938 494 -526 454 O ATOM 2639 CB ARG C 110 -2.006 7.911 -12.755 1.00 57.31 C ANISOU 2639 CB ARG C 110 8426 7479 5871 331 -411 377 C ATOM 2640 CG ARG C 110 -3.229 7.950 -13.656 1.00 60.35 C ANISOU 2640 CG ARG C 110 8793 7932 6205 384 -525 380 C ATOM 2641 CD ARG C 110 -3.345 6.685 -14.489 1.00 63.59 C ANISOU 2641 CD ARG C 110 9169 8458 6535 346 -529 292 C ATOM 2642 NE ARG C 110 -3.626 5.513 -13.663 1.00 71.92 N ANISOU 2642 NE ARG C 110 10129 9513 7685 332 -482 173 N ATOM 2643 CZ ARG C 110 -4.841 5.179 -13.238 1.00 74.58 C ANISOU 2643 CZ ARG C 110 10380 9853 8105 377 -534 111 C ATOM 2644 NH1 ARG C 110 -5.889 5.928 -13.562 1.00 75.48 N ANISOU 2644 NH1 ARG C 110 10485 9973 8222 444 -640 155 N ATOM 2645 NH2 ARG C 110 -5.011 4.100 -12.489 1.00 75.79 N ANISOU 2645 NH2 ARG C 110 10454 10000 8342 356 -479 8 N ATOM 2646 N VAL C 111 -2.987 8.533 -9.788 1.00 46.79 N ANISOU 2646 N VAL C 111 6988 5954 4836 411 -379 325 N ATOM 2647 CA VAL C 111 -4.096 8.497 -8.832 1.00 50.54 C ANISOU 2647 CA VAL C 111 7386 6389 5427 466 -402 273 C ATOM 2648 C VAL C 111 -3.960 9.490 -7.673 1.00 54.30 C ANISOU 2648 C VAL C 111 7882 6753 5997 488 -372 305 C ATOM 2649 O VAL C 111 -4.957 10.025 -7.187 1.00 54.42 O ANISOU 2649 O VAL C 111 7863 6723 6092 553 -413 301 O ATOM 2650 CB VAL C 111 -4.284 7.083 -8.225 1.00 65.84 C ANISOU 2650 CB VAL C 111 9237 8364 7414 438 -351 160 C ATOM 2651 CG1 VAL C 111 -5.464 7.071 -7.251 1.00 71.15 C ANISOU 2651 CG1 VAL C 111 9831 8998 8206 492 -368 108 C ATOM 2652 CG2 VAL C 111 -4.489 6.044 -9.315 1.00 62.04 C ANISOU 2652 CG2 VAL C 111 8730 7988 6854 414 -378 110 C ATOM 2653 N CYS C 112 -2.731 9.730 -7.225 1.00 55.38 N ANISOU 2653 N CYS C 112 8070 6847 6124 434 -298 332 N ATOM 2654 CA CYS C 112 -2.508 10.527 -6.022 1.00 53.24 C ANISOU 2654 CA CYS C 112 7813 6476 5939 442 -259 344 C ATOM 2655 C CYS C 112 -1.992 11.946 -6.269 1.00 62.80 C ANISOU 2655 C CYS C 112 9116 7612 7135 445 -271 443 C ATOM 2656 O CYS C 112 -2.153 12.817 -5.418 1.00 66.88 O ANISOU 2656 O CYS C 112 9645 8038 7729 470 -263 455 O ATOM 2657 CB CYS C 112 -1.570 9.788 -5.063 1.00 45.40 C ANISOU 2657 CB CYS C 112 6800 5480 4971 380 -168 291 C ATOM 2658 SG CYS C 112 -2.085 8.093 -4.740 1.00 48.41 S ANISOU 2658 SG CYS C 112 7082 5933 5377 371 -142 183 S ATOM 2659 N GLU C 113 -1.363 12.171 -7.417 1.00 71.06 N ANISOU 2659 N GLU C 113 10226 8693 8080 415 -285 512 N ATOM 2660 CA GLU C 113 -0.798 13.484 -7.734 1.00 77.98 C ANISOU 2660 CA GLU C 113 11194 9497 8937 409 -289 614 C ATOM 2661 C GLU C 113 0.325 13.911 -6.785 1.00 78.96 C ANISOU 2661 C GLU C 113 11348 9548 9104 351 -208 616 C ATOM 2662 O GLU C 113 1.333 13.220 -6.626 1.00 74.34 O ANISOU 2662 O GLU C 113 10755 9002 8490 282 -143 586 O ATOM 2663 CB GLU C 113 -1.891 14.562 -7.734 1.00 85.68 C ANISOU 2663 CB GLU C 113 12182 10402 9971 495 -364 662 C ATOM 2664 CG GLU C 113 -3.025 14.324 -8.718 1.00 95.91 C ANISOU 2664 CG GLU C 113 13449 11767 11224 559 -459 674 C ATOM 2665 CD GLU C 113 -4.059 15.437 -8.701 1.00102.31 C ANISOU 2665 CD GLU C 113 14268 12502 12103 651 -535 729 C ATOM 2666 OE1 GLU C 113 -3.958 16.339 -7.842 1.00101.14 O ANISOU 2666 OE1 GLU C 113 14143 12241 12043 666 -505 744 O ATOM 2667 OE2 GLU C 113 -4.977 15.409 -9.549 1.00106.62 O ANISOU 2667 OE2 GLU C 113 14794 13101 12615 709 -625 754 O ATOM 2668 N ASN C 114 0.105 15.053 -6.142 1.00 85.29 N ANISOU 2668 N ASN C 114 12182 10244 9983 381 -215 647 N ATOM 2669 CA ASN C 114 1.121 15.772 -5.376 1.00 92.30 C ANISOU 2669 CA ASN C 114 13114 11049 10908 328 -152 663 C ATOM 2670 C ASN C 114 1.416 15.257 -3.960 1.00 80.05 C ANISOU 2670 C ASN C 114 11508 9485 9424 299 -93 573 C ATOM 2671 O ASN C 114 1.243 15.991 -2.982 1.00 90.83 O ANISOU 2671 O ASN C 114 12879 10762 10869 314 -81 556 O ATOM 2672 CB ASN C 114 0.719 17.250 -5.284 1.00107.61 C ANISOU 2672 CB ASN C 114 15112 12869 12905 373 -184 730 C ATOM 2673 CG ASN C 114 -0.734 17.437 -4.855 1.00120.61 C ANISOU 2673 CG ASN C 114 16710 14483 14633 469 -239 695 C ATOM 2674 OD1 ASN C 114 -1.473 16.467 -4.676 1.00124.71 O ANISOU 2674 OD1 ASN C 114 17151 15073 15162 498 -256 624 O ATOM 2675 ND2 ASN C 114 -1.146 18.689 -4.689 1.00125.15 N ANISOU 2675 ND2 ASN C 114 17328 14947 15274 517 -264 744 N ATOM 2676 N ILE C 115 1.876 14.016 -3.836 1.00 51.07 N ANISOU 2676 N ILE C 115 7786 5898 5722 258 -55 517 N ATOM 2677 CA ILE C 115 2.230 13.508 -2.513 1.00 40.38 C ANISOU 2677 CA ILE C 115 6385 4535 4421 229 -1 444 C ATOM 2678 C ILE C 115 3.734 13.290 -2.415 1.00 36.41 C ANISOU 2678 C ILE C 115 5899 4052 3882 144 60 454 C ATOM 2679 O ILE C 115 4.392 12.965 -3.408 1.00 37.28 O ANISOU 2679 O ILE C 115 6029 4217 3920 107 70 489 O ATOM 2680 CB ILE C 115 1.470 12.202 -2.151 1.00 40.01 C ANISOU 2680 CB ILE C 115 6253 4556 4393 257 -2 362 C ATOM 2681 CG1 ILE C 115 1.809 11.082 -3.142 1.00 38.41 C ANISOU 2681 CG1 ILE C 115 6029 4452 4114 230 3 356 C ATOM 2682 CG2 ILE C 115 -0.032 12.438 -2.135 1.00 41.63 C ANISOU 2682 CG2 ILE C 115 6427 4741 4647 339 -59 344 C ATOM 2683 CD1 ILE C 115 1.488 9.701 -2.610 1.00 38.99 C ANISOU 2683 CD1 ILE C 115 6022 4581 4210 231 28 273 C ATOM 2684 N PRO C 116 4.288 13.471 -1.213 1.00 36.98 N ANISOU 2684 N PRO C 116 5963 4083 4004 110 101 420 N ATOM 2685 CA PRO C 116 5.717 13.212 -0.997 1.00 40.58 C ANISOU 2685 CA PRO C 116 6420 4562 4435 31 155 423 C ATOM 2686 C PRO C 116 6.039 11.723 -1.167 1.00 38.02 C ANISOU 2686 C PRO C 116 6034 4335 4078 14 181 382 C ATOM 2687 O PRO C 116 5.284 10.862 -0.715 1.00 30.06 O ANISOU 2687 O PRO C 116 4971 3357 3095 51 175 326 O ATOM 2688 CB PRO C 116 5.940 13.653 0.457 1.00 42.92 C ANISOU 2688 CB PRO C 116 6709 4801 4796 14 178 382 C ATOM 2689 CG PRO C 116 4.593 13.603 1.092 1.00 36.16 C ANISOU 2689 CG PRO C 116 5826 3922 3993 84 151 335 C ATOM 2690 CD PRO C 116 3.587 13.878 0.021 1.00 34.67 C ANISOU 2690 CD PRO C 116 5654 3728 3790 146 98 372 C ATOM 2691 N ILE C 117 7.161 11.429 -1.814 1.00 35.48 N ANISOU 2691 N ILE C 117 5719 4056 3705 -42 216 409 N ATOM 2692 CA ILE C 117 7.527 10.053 -2.133 1.00 34.53 C ANISOU 2692 CA ILE C 117 5545 4020 3554 -56 245 373 C ATOM 2693 C ILE C 117 9.004 9.839 -1.831 1.00 36.14 C ANISOU 2693 C ILE C 117 5733 4243 3755 -126 301 377 C ATOM 2694 O ILE C 117 9.838 10.685 -2.145 1.00 33.20 O ANISOU 2694 O ILE C 117 5404 3844 3365 -173 318 426 O ATOM 2695 CB ILE C 117 7.288 9.763 -3.634 1.00 36.91 C ANISOU 2695 CB ILE C 117 5867 4377 3780 -47 229 400 C ATOM 2696 CG1 ILE C 117 5.828 10.009 -4.010 1.00 35.78 C ANISOU 2696 CG1 ILE C 117 5733 4223 3638 23 162 401 C ATOM 2697 CG2 ILE C 117 7.712 8.336 -3.992 1.00 35.68 C ANISOU 2697 CG2 ILE C 117 5656 4303 3596 -65 267 354 C ATOM 2698 CD1 ILE C 117 5.564 10.021 -5.514 1.00 40.31 C ANISOU 2698 CD1 ILE C 117 6344 4846 4127 32 131 441 C ATOM 2699 N VAL C 118 9.333 8.715 -1.212 1.00 32.01 N ANISOU 2699 N VAL C 118 5146 3762 3254 -132 331 328 N ATOM 2700 CA VAL C 118 10.733 8.355 -1.014 1.00 32.38 C ANISOU 2700 CA VAL C 118 5164 3838 3300 -190 381 331 C ATOM 2701 C VAL C 118 11.054 7.145 -1.869 1.00 31.56 C ANISOU 2701 C VAL C 118 5022 3807 3162 -193 413 312 C ATOM 2702 O VAL C 118 10.257 6.217 -1.959 1.00 31.38 O ANISOU 2702 O VAL C 118 4968 3812 3143 -152 404 271 O ATOM 2703 CB VAL C 118 11.043 7.986 0.450 1.00 34.35 C ANISOU 2703 CB VAL C 118 5367 4080 3605 -196 392 294 C ATOM 2704 CG1 VAL C 118 12.500 7.562 0.579 1.00 35.50 C ANISOU 2704 CG1 VAL C 118 5473 4263 3753 -251 436 300 C ATOM 2705 CG2 VAL C 118 10.710 9.147 1.410 1.00 32.94 C ANISOU 2705 CG2 VAL C 118 5224 3829 3461 -195 364 297 C ATOM 2706 N LEU C 119 12.219 7.166 -2.507 1.00 30.22 N ANISOU 2706 N LEU C 119 4854 3666 2961 -245 456 338 N ATOM 2707 CA LEU C 119 12.705 6.017 -3.247 1.00 28.54 C ANISOU 2707 CA LEU C 119 4601 3520 2722 -254 499 313 C ATOM 2708 C LEU C 119 13.690 5.268 -2.367 1.00 33.33 C ANISOU 2708 C LEU C 119 5138 4144 3382 -275 539 288 C ATOM 2709 O LEU C 119 14.598 5.862 -1.773 1.00 31.19 O ANISOU 2709 O LEU C 119 4861 3854 3135 -316 551 312 O ATOM 2710 CB LEU C 119 13.383 6.455 -4.554 1.00 32.64 C ANISOU 2710 CB LEU C 119 5163 4067 3173 -297 530 356 C ATOM 2711 CG LEU C 119 13.896 5.355 -5.487 1.00 33.22 C ANISOU 2711 CG LEU C 119 5203 4212 3208 -310 583 326 C ATOM 2712 CD1 LEU C 119 12.758 4.521 -6.060 1.00 31.51 C ANISOU 2712 CD1 LEU C 119 4983 4027 2963 -261 558 281 C ATOM 2713 CD2 LEU C 119 14.733 5.958 -6.610 1.00 34.97 C ANISOU 2713 CD2 LEU C 119 5469 4457 3362 -364 623 373 C ATOM 2714 N CYS C 120 13.503 3.958 -2.280 1.00 31.10 N ANISOU 2714 N CYS C 120 4800 3895 3120 -246 558 241 N ATOM 2715 CA CYS C 120 14.329 3.119 -1.414 1.00 28.80 C ANISOU 2715 CA CYS C 120 4440 3619 2885 -253 590 222 C ATOM 2716 C CYS C 120 14.934 1.969 -2.187 1.00 35.60 C ANISOU 2716 C CYS C 120 5255 4529 3741 -257 646 194 C ATOM 2717 O CYS C 120 14.211 1.200 -2.818 1.00 29.86 O ANISOU 2717 O CYS C 120 4527 3821 2998 -228 651 157 O ATOM 2718 CB CYS C 120 13.484 2.553 -0.277 1.00 33.29 C ANISOU 2718 CB CYS C 120 4981 4165 3501 -207 563 191 C ATOM 2719 SG CYS C 120 13.118 3.793 0.986 1.00 37.25 S ANISOU 2719 SG CYS C 120 5519 4611 4023 -210 514 213 S ATOM 2720 N GLY C 121 16.257 1.845 -2.127 1.00 31.14 N ANISOU 2720 N GLY C 121 4649 3985 3196 -293 690 207 N ATOM 2721 CA GLY C 121 16.922 0.697 -2.720 1.00 29.70 C ANISOU 2721 CA GLY C 121 4413 3846 3027 -293 751 176 C ATOM 2722 C GLY C 121 17.233 -0.324 -1.640 1.00 32.25 C ANISOU 2722 C GLY C 121 4661 4164 3427 -264 760 157 C ATOM 2723 O GLY C 121 18.104 -0.097 -0.799 1.00 33.25 O ANISOU 2723 O GLY C 121 4751 4289 3594 -282 757 183 O ATOM 2724 N ASN C 122 16.534 -1.454 -1.686 1.00 34.66 N ANISOU 2724 N ASN C 122 4945 4468 3755 -221 769 114 N ATOM 2725 CA ASN C 122 16.625 -2.496 -0.660 1.00 33.90 C ANISOU 2725 CA ASN C 122 4788 4358 3733 -186 776 101 C ATOM 2726 C ASN C 122 17.706 -3.553 -0.928 1.00 34.64 C ANISOU 2726 C ASN C 122 4811 4475 3875 -183 840 85 C ATOM 2727 O ASN C 122 18.243 -3.641 -2.037 1.00 36.36 O ANISOU 2727 O ASN C 122 5026 4722 4066 -206 889 68 O ATOM 2728 CB ASN C 122 15.244 -3.158 -0.453 1.00 29.18 C ANISOU 2728 CB ASN C 122 4204 3736 3148 -142 756 65 C ATOM 2729 CG ASN C 122 15.153 -3.977 0.855 1.00 35.94 C ANISOU 2729 CG ASN C 122 5015 4567 4074 -108 751 69 C ATOM 2730 OD1 ASN C 122 15.788 -3.647 1.863 1.00 33.93 O ANISOU 2730 OD1 ASN C 122 4742 4310 3842 -115 733 107 O ATOM 2731 ND2 ASN C 122 14.358 -5.045 0.833 1.00 32.16 N ANISOU 2731 ND2 ASN C 122 4521 4072 3628 -74 768 29 N ATOM 2732 N LYS C 123 18.014 -4.338 0.107 1.00 33.79 N ANISOU 2732 N LYS C 123 4647 4353 3839 -153 842 93 N ATOM 2733 CA LYS C 123 18.977 -5.452 0.080 1.00 30.99 C ANISOU 2733 CA LYS C 123 4215 4008 3551 -136 897 83 C ATOM 2734 C LYS C 123 20.451 -5.048 0.030 1.00 34.68 C ANISOU 2734 C LYS C 123 4634 4508 4034 -169 920 112 C ATOM 2735 O LYS C 123 21.298 -5.817 -0.419 1.00 36.30 O ANISOU 2735 O LYS C 123 4779 4730 4284 -161 978 95 O ATOM 2736 CB LYS C 123 18.642 -6.496 -1.013 1.00 30.58 C ANISOU 2736 CB LYS C 123 4157 3957 3506 -118 956 21 C ATOM 2737 CG LYS C 123 17.169 -6.900 -1.011 1.00 27.66 C ANISOU 2737 CG LYS C 123 3827 3558 3124 -91 932 -15 C ATOM 2738 CD LYS C 123 16.890 -8.115 -1.852 1.00 36.56 C ANISOU 2738 CD LYS C 123 4936 4679 4277 -73 989 -82 C ATOM 2739 CE LYS C 123 15.387 -8.311 -2.015 1.00 31.80 C ANISOU 2739 CE LYS C 123 4375 4057 3650 -59 960 -123 C ATOM 2740 NZ LYS C 123 15.079 -9.541 -2.820 1.00 33.55 N ANISOU 2740 NZ LYS C 123 4577 4270 3899 -47 1015 -199 N ATOM 2741 N VAL C 124 20.775 -3.857 0.519 1.00 42.06 N ANISOU 2741 N VAL C 124 5589 5451 4940 -207 876 153 N ATOM 2742 CA VAL C 124 22.169 -3.427 0.477 1.00 39.89 C ANISOU 2742 CA VAL C 124 5263 5208 4684 -246 897 178 C ATOM 2743 C VAL C 124 23.099 -4.242 1.395 1.00 45.30 C ANISOU 2743 C VAL C 124 5855 5904 5455 -217 899 197 C ATOM 2744 O VAL C 124 24.315 -4.048 1.364 1.00 47.83 O ANISOU 2744 O VAL C 124 6112 6255 5804 -244 918 213 O ATOM 2745 CB VAL C 124 22.322 -1.898 0.692 1.00 37.89 C ANISOU 2745 CB VAL C 124 5056 4957 4382 -303 854 212 C ATOM 2746 CG1 VAL C 124 21.459 -1.155 -0.311 1.00 30.37 C ANISOU 2746 CG1 VAL C 124 4194 3993 3351 -324 854 202 C ATOM 2747 CG2 VAL C 124 21.939 -1.502 2.129 1.00 35.25 C ANISOU 2747 CG2 VAL C 124 4734 4601 4057 -292 781 237 C ATOM 2748 N ASP C 125 22.540 -5.163 2.187 1.00 40.71 N ANISOU 2748 N ASP C 125 5259 5295 4913 -162 880 197 N ATOM 2749 CA ASP C 125 23.363 -6.083 2.983 1.00 43.19 C ANISOU 2749 CA ASP C 125 5485 5615 5310 -123 884 221 C ATOM 2750 C ASP C 125 24.124 -7.075 2.101 1.00 47.76 C ANISOU 2750 C ASP C 125 5996 6202 5948 -102 963 192 C ATOM 2751 O ASP C 125 25.157 -7.615 2.494 1.00 49.83 O ANISOU 2751 O ASP C 125 6171 6478 6282 -81 976 213 O ATOM 2752 CB ASP C 125 22.510 -6.857 4.002 1.00 41.27 C ANISOU 2752 CB ASP C 125 5253 5335 5092 -70 851 235 C ATOM 2753 CG ASP C 125 21.334 -7.582 3.356 1.00 42.57 C ANISOU 2753 CG ASP C 125 5462 5462 5252 -42 886 188 C ATOM 2754 OD1 ASP C 125 20.346 -6.913 2.987 1.00 41.83 O ANISOU 2754 OD1 ASP C 125 5443 5359 5093 -63 867 166 O ATOM 2755 OD2 ASP C 125 21.388 -8.823 3.229 1.00 48.81 O ANISOU 2755 OD2 ASP C 125 6210 6227 6107 2 930 171 O ATOM 2756 N ILE C 126 23.594 -7.313 0.910 1.00 42.16 N ANISOU 2756 N ILE C 126 5326 5485 5208 -107 1016 140 N ATOM 2757 CA ILE C 126 24.189 -8.240 -0.046 1.00 43.44 C ANISOU 2757 CA ILE C 126 5436 5653 5417 -91 1102 96 C ATOM 2758 C ILE C 126 25.416 -7.650 -0.750 1.00 53.43 C ANISOU 2758 C ILE C 126 6659 6966 6676 -139 1146 97 C ATOM 2759 O ILE C 126 25.329 -6.615 -1.406 1.00 55.06 O ANISOU 2759 O ILE C 126 6920 7196 6803 -195 1146 95 O ATOM 2760 CB ILE C 126 23.148 -8.645 -1.093 1.00 50.26 C ANISOU 2760 CB ILE C 126 6362 6499 6236 -88 1140 33 C ATOM 2761 CG1 ILE C 126 22.031 -9.445 -0.416 1.00 51.44 C ANISOU 2761 CG1 ILE C 126 6533 6596 6415 -39 1111 26 C ATOM 2762 CG2 ILE C 126 23.805 -9.419 -2.237 1.00 58.70 C ANISOU 2762 CG2 ILE C 126 7387 7582 7335 -85 1235 -24 C ATOM 2763 CD1 ILE C 126 20.785 -9.601 -1.257 1.00 59.74 C ANISOU 2763 CD1 ILE C 126 7654 7633 7410 -44 1122 -33 C ATOM 2764 N LYS C 127 26.557 -8.319 -0.615 1.00 56.64 N ANISOU 2764 N LYS C 127 6964 7385 7170 -115 1186 101 N ATOM 2765 CA LYS C 127 27.823 -7.801 -1.147 1.00 59.54 C ANISOU 2765 CA LYS C 127 7274 7802 7548 -160 1230 104 C ATOM 2766 C LYS C 127 27.835 -7.598 -2.666 1.00 53.87 C ANISOU 2766 C LYS C 127 6593 7106 6768 -202 1313 51 C ATOM 2767 O LYS C 127 28.302 -6.568 -3.152 1.00 57.39 O ANISOU 2767 O LYS C 127 7057 7588 7160 -267 1324 63 O ATOM 2768 CB LYS C 127 28.997 -8.697 -0.732 1.00 71.27 C ANISOU 2768 CB LYS C 127 8633 9294 9153 -115 1261 114 C ATOM 2769 CG LYS C 127 30.340 -8.234 -1.286 1.00 81.59 C ANISOU 2769 CG LYS C 127 9863 10654 10483 -161 1315 111 C ATOM 2770 CD LYS C 127 31.450 -9.231 -0.998 1.00 90.31 C ANISOU 2770 CD LYS C 127 10835 11764 11716 -107 1352 113 C ATOM 2771 CE LYS C 127 32.774 -8.743 -1.565 1.00 97.61 C ANISOU 2771 CE LYS C 127 11675 12743 12667 -156 1410 106 C ATOM 2772 NZ LYS C 127 33.883 -9.705 -1.314 1.00102.35 N ANISOU 2772 NZ LYS C 127 12136 13351 13403 -98 1448 107 N ATOM 2773 N ASP C 128 27.337 -8.585 -3.409 1.00 51.93 N ANISOU 2773 N ASP C 128 6362 6840 6530 -168 1371 -9 N ATOM 2774 CA ASP C 128 27.300 -8.511 -4.870 1.00 56.71 C ANISOU 2774 CA ASP C 128 7007 7473 7066 -206 1451 -67 C ATOM 2775 C ASP C 128 26.176 -7.592 -5.355 1.00 50.57 C ANISOU 2775 C ASP C 128 6352 6701 6164 -246 1407 -64 C ATOM 2776 O ASP C 128 25.188 -8.034 -5.947 1.00 45.43 O ANISOU 2776 O ASP C 128 5760 6036 5467 -232 1415 -112 O ATOM 2777 CB ASP C 128 27.148 -9.906 -5.478 1.00 63.58 C ANISOU 2777 CB ASP C 128 7850 8319 7987 -158 1527 -142 C ATOM 2778 CG ASP C 128 27.476 -9.935 -6.958 1.00 75.85 C ANISOU 2778 CG ASP C 128 9421 9915 9485 -197 1626 -206 C ATOM 2779 OD1 ASP C 128 27.862 -8.879 -7.500 1.00 78.56 O ANISOU 2779 OD1 ASP C 128 9795 10306 9751 -261 1637 -184 O ATOM 2780 OD2 ASP C 128 27.350 -11.013 -7.579 1.00 77.85 O ANISOU 2780 OD2 ASP C 128 9659 10152 9769 -167 1696 -280 O ATOM 2781 N ARG C 129 26.343 -6.306 -5.087 1.00 52.02 N ANISOU 2781 N ARG C 129 6568 6901 6296 -296 1359 -9 N ATOM 2782 CA ARG C 129 25.347 -5.304 -5.426 1.00 48.91 C ANISOU 2782 CA ARG C 129 6285 6505 5794 -331 1309 7 C ATOM 2783 C ARG C 129 25.414 -4.992 -6.915 1.00 44.77 C ANISOU 2783 C ARG C 129 5811 6021 5179 -377 1376 -23 C ATOM 2784 O ARG C 129 26.502 -4.792 -7.459 1.00 43.27 O ANISOU 2784 O ARG C 129 5580 5868 4994 -416 1446 -23 O ATOM 2785 CB ARG C 129 25.606 -4.041 -4.609 1.00 48.31 C ANISOU 2785 CB ARG C 129 6222 6426 5707 -369 1242 75 C ATOM 2786 CG ARG C 129 24.721 -2.867 -4.954 1.00 48.00 C ANISOU 2786 CG ARG C 129 6294 6378 5566 -406 1194 101 C ATOM 2787 CD ARG C 129 24.881 -1.759 -3.925 1.00 41.01 C ANISOU 2787 CD ARG C 129 5418 5474 4690 -434 1124 158 C ATOM 2788 NE ARG C 129 23.934 -0.676 -4.166 1.00 41.71 N ANISOU 2788 NE ARG C 129 5612 5541 4695 -458 1075 183 N ATOM 2789 CZ ARG C 129 23.692 0.317 -3.317 1.00 40.61 C ANISOU 2789 CZ ARG C 129 5507 5372 4553 -475 1007 223 C ATOM 2790 NH1 ARG C 129 24.326 0.371 -2.146 1.00 39.08 N ANISOU 2790 NH1 ARG C 129 5251 5174 4425 -477 975 240 N ATOM 2791 NH2 ARG C 129 22.813 1.252 -3.643 1.00 41.26 N ANISOU 2791 NH2 ARG C 129 5684 5429 4566 -490 969 243 N ATOM 2792 N LYS C 130 24.257 -4.946 -7.571 1.00 42.18 N ANISOU 2792 N LYS C 130 5571 5690 4766 -374 1356 -48 N ATOM 2793 CA LYS C 130 24.212 -4.686 -9.009 1.00 52.08 C ANISOU 2793 CA LYS C 130 6884 6989 5917 -416 1413 -76 C ATOM 2794 C LYS C 130 23.877 -3.242 -9.349 1.00 50.65 C ANISOU 2794 C LYS C 130 6793 6816 5634 -467 1369 -15 C ATOM 2795 O LYS C 130 24.476 -2.662 -10.248 1.00 48.41 O ANISOU 2795 O LYS C 130 6535 6572 5286 -521 1424 -1 O ATOM 2796 CB LYS C 130 23.240 -5.640 -9.709 1.00 54.35 C ANISOU 2796 CB LYS C 130 7205 7278 6168 -383 1427 -150 C ATOM 2797 CG LYS C 130 23.691 -7.083 -9.688 1.00 57.18 C ANISOU 2797 CG LYS C 130 7479 7626 6621 -342 1497 -219 C ATOM 2798 CD LYS C 130 25.145 -7.205 -10.134 1.00 66.14 C ANISOU 2798 CD LYS C 130 8543 8795 7791 -369 1595 -229 C ATOM 2799 CE LYS C 130 25.496 -8.638 -10.509 1.00 72.71 C ANISOU 2799 CE LYS C 130 9308 9621 8696 -330 1683 -315 C ATOM 2800 NZ LYS C 130 25.110 -9.607 -9.447 1.00 72.98 N ANISOU 2800 NZ LYS C 130 9293 9592 8845 -262 1644 -323 N ATOM 2801 N VAL C 131 22.918 -2.662 -8.634 1.00 46.61 N ANISOU 2801 N VAL C 131 6332 6266 5110 -449 1274 22 N ATOM 2802 CA VAL C 131 22.540 -1.270 -8.863 1.00 40.18 C ANISOU 2802 CA VAL C 131 5605 5447 4214 -489 1226 83 C ATOM 2803 C VAL C 131 23.230 -0.372 -7.847 1.00 43.03 C ANISOU 2803 C VAL C 131 5939 5781 4631 -517 1195 143 C ATOM 2804 O VAL C 131 22.847 -0.322 -6.673 1.00 38.44 O ANISOU 2804 O VAL C 131 5342 5160 4105 -486 1128 157 O ATOM 2805 CB VAL C 131 21.012 -1.069 -8.787 1.00 42.36 C ANISOU 2805 CB VAL C 131 5957 5697 4442 -454 1142 83 C ATOM 2806 CG1 VAL C 131 20.650 0.371 -9.116 1.00 41.44 C ANISOU 2806 CG1 VAL C 131 5931 5570 4244 -490 1098 149 C ATOM 2807 CG2 VAL C 131 20.302 -2.048 -9.729 1.00 41.46 C ANISOU 2807 CG2 VAL C 131 5860 5613 4279 -428 1166 13 C ATOM 2808 N LYS C 132 24.250 0.340 -8.308 1.00 42.64 N ANISOU 2808 N LYS C 132 5885 5754 4563 -579 1246 175 N ATOM 2809 CA LYS C 132 25.116 1.109 -7.429 1.00 40.63 C ANISOU 2809 CA LYS C 132 5588 5482 4368 -617 1230 220 C ATOM 2810 C LYS C 132 24.746 2.575 -7.463 1.00 40.72 C ANISOU 2810 C LYS C 132 5690 5461 4321 -661 1184 282 C ATOM 2811 O LYS C 132 23.986 3.009 -8.330 1.00 42.04 O ANISOU 2811 O LYS C 132 5948 5627 4397 -666 1176 297 O ATOM 2812 CB LYS C 132 26.586 0.910 -7.823 1.00 51.40 C ANISOU 2812 CB LYS C 132 6870 6888 5771 -661 1323 212 C ATOM 2813 CG LYS C 132 27.004 -0.552 -7.834 1.00 60.59 C ANISOU 2813 CG LYS C 132 7941 8078 7003 -612 1377 150 C ATOM 2814 CD LYS C 132 28.472 -0.706 -8.143 1.00 72.82 C ANISOU 2814 CD LYS C 132 9396 9667 8603 -652 1467 141 C ATOM 2815 CE LYS C 132 28.910 -2.150 -8.026 1.00 74.51 C ANISOU 2815 CE LYS C 132 9510 9895 8904 -595 1515 83 C ATOM 2816 NZ LYS C 132 30.390 -2.256 -8.119 1.00 76.62 N ANISOU 2816 NZ LYS C 132 9669 10199 9243 -627 1593 79 N ATOM 2817 N ALA C 133 25.293 3.330 -6.515 1.00 43.36 N ANISOU 2817 N ALA C 133 5997 5767 4710 -692 1151 316 N ATOM 2818 CA ALA C 133 24.987 4.749 -6.359 1.00 50.02 C ANISOU 2818 CA ALA C 133 6921 6564 5519 -734 1106 371 C ATOM 2819 C ALA C 133 24.996 5.490 -7.691 1.00 50.19 C ANISOU 2819 C ALA C 133 7025 6596 5448 -783 1153 408 C ATOM 2820 O ALA C 133 24.005 6.108 -8.070 1.00 45.78 O ANISOU 2820 O ALA C 133 6564 6007 4822 -771 1110 438 O ATOM 2821 CB ALA C 133 25.964 5.395 -5.388 1.00 55.20 C ANISOU 2821 CB ALA C 133 7520 7205 6249 -783 1093 392 C ATOM 2822 N LYS C 134 26.123 5.417 -8.394 1.00 53.31 N ANISOU 2822 N LYS C 134 7379 7035 5840 -838 1243 408 N ATOM 2823 CA LYS C 134 26.278 6.062 -9.694 1.00 56.05 C ANISOU 2823 CA LYS C 134 7802 7401 6094 -892 1303 447 C ATOM 2824 C LYS C 134 25.068 5.847 -10.610 1.00 55.92 C ANISOU 2824 C LYS C 134 7879 7396 5972 -850 1280 444 C ATOM 2825 O LYS C 134 24.652 6.763 -11.324 1.00 53.68 O ANISOU 2825 O LYS C 134 7695 7096 5604 -877 1271 501 O ATOM 2826 CB LYS C 134 27.548 5.549 -10.382 1.00 65.77 C ANISOU 2826 CB LYS C 134 8958 8695 7336 -938 1416 422 C ATOM 2827 CG LYS C 134 27.677 4.034 -10.350 1.00 77.25 C ANISOU 2827 CG LYS C 134 10325 10193 8832 -879 1448 345 C ATOM 2828 CD LYS C 134 28.884 3.545 -11.128 1.00 90.71 C ANISOU 2828 CD LYS C 134 11959 11959 10547 -920 1568 316 C ATOM 2829 CE LYS C 134 28.979 2.027 -11.072 1.00 96.95 C ANISOU 2829 CE LYS C 134 12664 12782 11392 -855 1600 237 C ATOM 2830 NZ LYS C 134 30.089 1.503 -11.911 1.00100.38 N ANISOU 2830 NZ LYS C 134 13031 13275 11835 -889 1726 200 N ATOM 2831 N SER C 135 24.510 4.639 -10.589 1.00 46.34 N ANISOU 2831 N SER C 135 6632 6209 4765 -784 1269 380 N ATOM 2832 CA SER C 135 23.383 4.298 -11.457 1.00 50.94 C ANISOU 2832 CA SER C 135 7290 6812 5252 -744 1246 364 C ATOM 2833 C SER C 135 22.025 4.777 -10.941 1.00 49.85 C ANISOU 2833 C SER C 135 7217 6622 5103 -695 1137 387 C ATOM 2834 O SER C 135 21.043 4.758 -11.683 1.00 47.89 O ANISOU 2834 O SER C 135 7039 6388 4769 -669 1105 388 O ATOM 2835 CB SER C 135 23.316 2.786 -11.693 1.00 55.25 C ANISOU 2835 CB SER C 135 7773 7405 5815 -699 1283 278 C ATOM 2836 OG SER C 135 24.448 2.325 -12.402 1.00 59.23 O ANISOU 2836 OG SER C 135 8228 7963 6315 -740 1392 250 O ATOM 2837 N ILE C 136 21.954 5.182 -9.674 1.00 44.15 N ANISOU 2837 N ILE C 136 6469 5843 4464 -682 1080 402 N ATOM 2838 CA ILE C 136 20.667 5.572 -9.101 1.00 37.37 C ANISOU 2838 CA ILE C 136 5662 4933 3606 -632 983 415 C ATOM 2839 C ILE C 136 20.370 7.048 -9.348 1.00 48.67 C ANISOU 2839 C ILE C 136 7187 6315 4990 -662 949 492 C ATOM 2840 O ILE C 136 20.887 7.934 -8.662 1.00 45.47 O ANISOU 2840 O ILE C 136 6781 5862 4636 -700 942 529 O ATOM 2841 CB ILE C 136 20.549 5.213 -7.599 1.00 37.92 C ANISOU 2841 CB ILE C 136 5665 4966 3778 -595 937 386 C ATOM 2842 CG1 ILE C 136 20.788 3.708 -7.398 1.00 35.36 C ANISOU 2842 CG1 ILE C 136 5252 4683 3501 -558 971 317 C ATOM 2843 CG2 ILE C 136 19.168 5.592 -7.084 1.00 34.60 C ANISOU 2843 CG2 ILE C 136 5297 4497 3354 -543 848 392 C ATOM 2844 CD1 ILE C 136 20.933 3.271 -5.945 1.00 39.11 C ANISOU 2844 CD1 ILE C 136 5655 5132 4075 -529 938 297 C ATOM 2845 N VAL C 137 19.505 7.291 -10.328 1.00 43.66 N ANISOU 2845 N VAL C 137 6634 5693 4263 -644 925 517 N ATOM 2846 CA VAL C 137 19.332 8.620 -10.896 1.00 49.61 C ANISOU 2846 CA VAL C 137 7485 6409 4957 -676 908 601 C ATOM 2847 C VAL C 137 17.881 9.103 -10.979 1.00 49.03 C ANISOU 2847 C VAL C 137 7484 6298 4846 -616 816 628 C ATOM 2848 O VAL C 137 17.628 10.297 -11.170 1.00 52.43 O ANISOU 2848 O VAL C 137 7994 6675 5254 -629 786 703 O ATOM 2849 CB VAL C 137 20.005 8.676 -12.292 1.00 54.22 C ANISOU 2849 CB VAL C 137 8108 7053 5441 -731 987 631 C ATOM 2850 CG1 VAL C 137 19.142 9.415 -13.305 1.00 61.52 C ANISOU 2850 CG1 VAL C 137 9145 7974 6254 -720 947 698 C ATOM 2851 CG2 VAL C 137 21.391 9.278 -12.165 1.00 56.57 C ANISOU 2851 CG2 VAL C 137 8381 7336 5777 -813 1062 665 C ATOM 2852 N PHE C 138 16.933 8.187 -10.801 1.00 45.71 N ANISOU 2852 N PHE C 138 7034 5901 4431 -550 771 568 N ATOM 2853 CA PHE C 138 15.523 8.524 -10.977 1.00 45.71 C ANISOU 2853 CA PHE C 138 7091 5880 4397 -490 684 585 C ATOM 2854 C PHE C 138 15.013 9.610 -10.043 1.00 47.53 C ANISOU 2854 C PHE C 138 7351 6017 4691 -470 622 627 C ATOM 2855 O PHE C 138 14.204 10.442 -10.447 1.00 51.82 O ANISOU 2855 O PHE C 138 7967 6526 5197 -443 567 682 O ATOM 2856 CB PHE C 138 14.622 7.293 -10.858 1.00 48.02 C ANISOU 2856 CB PHE C 138 7333 6213 4698 -429 651 504 C ATOM 2857 CG PHE C 138 13.179 7.590 -11.148 1.00 44.66 C ANISOU 2857 CG PHE C 138 6956 5777 4236 -370 563 517 C ATOM 2858 CD1 PHE C 138 12.752 7.799 -12.453 1.00 46.45 C ANISOU 2858 CD1 PHE C 138 7249 6051 4348 -369 544 552 C ATOM 2859 CD2 PHE C 138 12.260 7.701 -10.119 1.00 41.21 C ANISOU 2859 CD2 PHE C 138 6496 5285 3876 -316 499 498 C ATOM 2860 CE1 PHE C 138 11.425 8.086 -12.725 1.00 49.23 C ANISOU 2860 CE1 PHE C 138 7637 6398 4669 -311 454 567 C ATOM 2861 CE2 PHE C 138 10.933 7.991 -10.382 1.00 46.26 C ANISOU 2861 CE2 PHE C 138 7170 5916 4491 -259 418 510 C ATOM 2862 CZ PHE C 138 10.516 8.181 -11.687 1.00 49.10 C ANISOU 2862 CZ PHE C 138 7589 6325 4742 -255 392 545 C ATOM 2863 N HIS C 139 15.476 9.598 -8.796 1.00 42.50 N ANISOU 2863 N HIS C 139 6657 5339 4151 -479 630 599 N ATOM 2864 CA HIS C 139 14.960 10.519 -7.783 1.00 45.22 C ANISOU 2864 CA HIS C 139 7023 5596 4561 -458 575 619 C ATOM 2865 C HIS C 139 15.412 11.949 -8.055 1.00 48.27 C ANISOU 2865 C HIS C 139 7484 5920 4937 -507 584 702 C ATOM 2866 O HIS C 139 14.648 12.895 -7.881 1.00 47.71 O ANISOU 2866 O HIS C 139 7471 5778 4880 -478 531 741 O ATOM 2867 CB HIS C 139 15.411 10.087 -6.389 1.00 42.95 C ANISOU 2867 CB HIS C 139 6657 5293 4368 -462 584 565 C ATOM 2868 CG HIS C 139 16.894 10.106 -6.216 1.00 40.77 C ANISOU 2868 CG HIS C 139 6340 5032 4116 -535 650 569 C ATOM 2869 ND1 HIS C 139 17.527 10.914 -5.295 1.00 48.22 N ANISOU 2869 ND1 HIS C 139 7278 5922 5123 -578 651 582 N ATOM 2870 CD2 HIS C 139 17.872 9.436 -6.867 1.00 42.63 C ANISOU 2870 CD2 HIS C 139 6537 5334 4326 -575 719 558 C ATOM 2871 CE1 HIS C 139 18.833 10.728 -5.375 1.00 46.94 C ANISOU 2871 CE1 HIS C 139 7068 5794 4973 -640 713 581 C ATOM 2872 NE2 HIS C 139 19.068 9.840 -6.324 1.00 55.03 N ANISOU 2872 NE2 HIS C 139 8072 6891 5948 -638 758 568 N ATOM 2873 N ARG C 140 16.658 12.102 -8.480 1.00 51.31 N ANISOU 2873 N ARG C 140 7865 6326 5305 -582 656 727 N ATOM 2874 CA ARG C 140 17.166 13.419 -8.844 1.00 59.64 C ANISOU 2874 CA ARG C 140 8992 7321 6347 -639 677 808 C ATOM 2875 C ARG C 140 16.376 13.976 -10.022 1.00 65.23 C ANISOU 2875 C ARG C 140 9797 8024 6964 -613 646 880 C ATOM 2876 O ARG C 140 16.046 15.161 -10.062 1.00 58.22 O ANISOU 2876 O ARG C 140 8983 7054 6083 -613 616 949 O ATOM 2877 CB ARG C 140 18.646 13.334 -9.194 1.00 59.26 C ANISOU 2877 CB ARG C 140 8911 7311 6292 -727 768 816 C ATOM 2878 CG ARG C 140 19.517 12.916 -8.036 1.00 63.66 C ANISOU 2878 CG ARG C 140 9373 7873 6943 -756 791 756 C ATOM 2879 CD ARG C 140 20.965 12.890 -8.454 1.00 70.23 C ANISOU 2879 CD ARG C 140 10168 8744 7774 -842 881 767 C ATOM 2880 NE ARG C 140 21.412 14.202 -8.910 1.00 76.82 N ANISOU 2880 NE ARG C 140 11076 9519 8593 -910 910 845 N ATOM 2881 CZ ARG C 140 22.684 14.519 -9.118 1.00 83.11 C ANISOU 2881 CZ ARG C 140 11846 10325 9406 -999 986 864 C ATOM 2882 NH1 ARG C 140 23.633 13.617 -8.903 1.00 80.39 N ANISOU 2882 NH1 ARG C 140 11399 10051 9095 -1023 1038 808 N ATOM 2883 NH2 ARG C 140 23.008 15.736 -9.534 1.00 87.17 N ANISOU 2883 NH2 ARG C 140 12435 10777 9910 -1062 1013 939 N ATOM 2884 N LYS C 141 16.067 13.101 -10.973 1.00 71.50 N ANISOU 2884 N LYS C 141 10589 8906 7673 -589 651 863 N ATOM 2885 CA LYS C 141 15.298 13.472 -12.152 1.00 77.53 C ANISOU 2885 CA LYS C 141 11438 9686 8332 -562 615 927 C ATOM 2886 C LYS C 141 13.906 13.999 -11.787 1.00 67.36 C ANISOU 2886 C LYS C 141 10185 8336 7072 -480 514 945 C ATOM 2887 O LYS C 141 13.370 14.883 -12.460 1.00 63.13 O ANISOU 2887 O LYS C 141 9735 7766 6486 -462 475 1029 O ATOM 2888 CB LYS C 141 15.190 12.271 -13.095 1.00 85.87 C ANISOU 2888 CB LYS C 141 12472 10857 9297 -550 635 880 C ATOM 2889 CG LYS C 141 14.557 12.571 -14.439 1.00 95.81 C ANISOU 2889 CG LYS C 141 13819 12156 10427 -534 603 944 C ATOM 2890 CD LYS C 141 14.748 11.400 -15.394 1.00102.91 C ANISOU 2890 CD LYS C 141 14697 13174 11231 -546 646 887 C ATOM 2891 CE LYS C 141 13.921 11.565 -16.659 1.00107.94 C ANISOU 2891 CE LYS C 141 15415 13865 11731 -519 595 937 C ATOM 2892 NZ LYS C 141 12.462 11.484 -16.372 1.00107.86 N ANISOU 2892 NZ LYS C 141 15400 13840 11742 -430 481 918 N ATOM 2893 N LYS C 142 13.326 13.462 -10.719 1.00 61.13 N ANISOU 2893 N LYS C 142 9330 7533 6365 -431 476 870 N ATOM 2894 CA LYS C 142 11.969 13.837 -10.321 1.00 58.53 C ANISOU 2894 CA LYS C 142 9016 7151 6070 -350 387 872 C ATOM 2895 C LYS C 142 11.918 14.530 -8.956 1.00 60.18 C ANISOU 2895 C LYS C 142 9211 7261 6395 -344 372 858 C ATOM 2896 O LYS C 142 10.845 14.688 -8.363 1.00 55.55 O ANISOU 2896 O LYS C 142 8617 6633 5858 -276 310 837 O ATOM 2897 CB LYS C 142 11.052 12.614 -10.346 1.00 56.46 C ANISOU 2897 CB LYS C 142 8696 6962 5795 -289 347 794 C ATOM 2898 CG LYS C 142 11.163 11.815 -11.639 1.00 60.62 C ANISOU 2898 CG LYS C 142 9231 7594 6208 -302 368 787 C ATOM 2899 CD LYS C 142 9.829 11.207 -12.026 1.00 70.16 C ANISOU 2899 CD LYS C 142 10425 8850 7382 -230 293 751 C ATOM 2900 CE LYS C 142 8.843 12.267 -12.495 1.00 79.03 C ANISOU 2900 CE LYS C 142 11622 9931 8476 -180 210 832 C ATOM 2901 NZ LYS C 142 9.130 12.733 -13.880 1.00 81.29 N ANISOU 2901 NZ LYS C 142 11993 10259 8636 -209 215 917 N ATOM 2902 N ASN C 143 13.084 14.948 -8.473 1.00 62.53 N ANISOU 2902 N ASN C 143 9502 7524 6734 -416 431 866 N ATOM 2903 CA ASN C 143 13.178 15.701 -7.229 1.00 71.41 C ANISOU 2903 CA ASN C 143 10620 8556 7958 -425 423 852 C ATOM 2904 C ASN C 143 12.608 14.951 -6.011 1.00 66.37 C ANISOU 2904 C ASN C 143 9906 7925 7387 -376 394 761 C ATOM 2905 O ASN C 143 11.859 15.525 -5.222 1.00 61.71 O ANISOU 2905 O ASN C 143 9326 7262 6857 -335 351 749 O ATOM 2906 CB ASN C 143 12.488 17.058 -7.399 1.00 80.72 C ANISOU 2906 CB ASN C 143 11886 9631 9152 -396 378 926 C ATOM 2907 CG ASN C 143 13.015 18.106 -6.441 1.00 88.92 C ANISOU 2907 CG ASN C 143 12943 10565 10278 -441 397 931 C ATOM 2908 OD1 ASN C 143 14.107 17.967 -5.884 1.00 90.46 O ANISOU 2908 OD1 ASN C 143 13096 10771 10505 -512 448 898 O ATOM 2909 ND2 ASN C 143 12.242 19.171 -6.250 1.00 89.67 N ANISOU 2909 ND2 ASN C 143 13097 10558 10416 -400 353 969 N ATOM 2910 N LEU C 144 12.973 13.673 -5.879 1.00 59.86 N ANISOU 2910 N LEU C 144 9006 7185 6553 -382 422 699 N ATOM 2911 CA LEU C 144 12.551 12.814 -4.768 1.00 50.69 C ANISOU 2911 CA LEU C 144 7770 6040 5448 -343 405 618 C ATOM 2912 C LEU C 144 13.720 12.563 -3.830 1.00 46.13 C ANISOU 2912 C LEU C 144 7137 5470 4921 -400 450 584 C ATOM 2913 O LEU C 144 14.874 12.771 -4.202 1.00 51.91 O ANISOU 2913 O LEU C 144 7869 6216 5638 -468 500 611 O ATOM 2914 CB LEU C 144 12.106 11.451 -5.296 1.00 48.85 C ANISOU 2914 CB LEU C 144 7491 5896 5175 -306 403 574 C ATOM 2915 CG LEU C 144 10.689 11.210 -5.813 1.00 56.26 C ANISOU 2915 CG LEU C 144 8444 6847 6083 -232 343 566 C ATOM 2916 CD1 LEU C 144 10.145 12.420 -6.543 1.00 57.26 C ANISOU 2916 CD1 LEU C 144 8656 6924 6177 -214 301 644 C ATOM 2917 CD2 LEU C 144 10.679 9.980 -6.708 1.00 47.16 C ANISOU 2917 CD2 LEU C 144 7259 5791 4870 -227 362 532 C ATOM 2918 N GLN C 145 13.433 12.065 -2.630 1.00 44.88 N ANISOU 2918 N GLN C 145 6925 5309 4819 -374 434 524 N ATOM 2919 CA GLN C 145 14.499 11.689 -1.707 1.00 39.17 C ANISOU 2919 CA GLN C 145 6141 4605 4137 -420 467 491 C ATOM 2920 C GLN C 145 14.820 10.209 -1.902 1.00 37.36 C ANISOU 2920 C GLN C 145 5839 4462 3894 -409 496 452 C ATOM 2921 O GLN C 145 13.925 9.412 -2.176 1.00 36.44 O ANISOU 2921 O GLN C 145 5710 4375 3761 -353 478 426 O ATOM 2922 CB GLN C 145 14.093 11.994 -0.252 1.00 37.04 C ANISOU 2922 CB GLN C 145 5859 4287 3928 -403 435 451 C ATOM 2923 CG GLN C 145 15.102 11.560 0.793 1.00 39.70 C ANISOU 2923 CG GLN C 145 6130 4652 4300 -444 456 416 C ATOM 2924 CD GLN C 145 16.417 12.325 0.704 1.00 50.01 C ANISOU 2924 CD GLN C 145 7441 5945 5615 -529 487 445 C ATOM 2925 OE1 GLN C 145 16.434 13.532 0.490 1.00 55.06 O ANISOU 2925 OE1 GLN C 145 8144 6518 6260 -560 483 479 O ATOM 2926 NE2 GLN C 145 17.525 11.615 0.878 1.00 52.35 N ANISOU 2926 NE2 GLN C 145 7667 6303 5921 -567 519 432 N ATOM 2927 N TYR C 146 16.098 9.847 -1.800 1.00 36.75 N ANISOU 2927 N TYR C 146 5712 4423 3829 -462 542 448 N ATOM 2928 CA TYR C 146 16.514 8.451 -1.968 1.00 35.41 C ANISOU 2928 CA TYR C 146 5469 4326 3658 -451 577 412 C ATOM 2929 C TYR C 146 17.246 7.932 -0.723 1.00 37.82 C ANISOU 2929 C TYR C 146 5700 4647 4023 -463 583 381 C ATOM 2930 O TYR C 146 17.986 8.685 -0.101 1.00 35.89 O ANISOU 2930 O TYR C 146 5453 4379 3807 -512 581 394 O ATOM 2931 CB TYR C 146 17.414 8.243 -3.216 1.00 32.44 C ANISOU 2931 CB TYR C 146 5090 3999 3236 -494 637 435 C ATOM 2932 CG TYR C 146 17.973 6.824 -3.220 1.00 32.57 C ANISOU 2932 CG TYR C 146 5023 4082 3271 -483 678 391 C ATOM 2933 CD1 TYR C 146 17.190 5.749 -3.647 1.00 29.48 C ANISOU 2933 CD1 TYR C 146 4618 3723 2860 -429 677 353 C ATOM 2934 CD2 TYR C 146 19.247 6.552 -2.731 1.00 30.32 C ANISOU 2934 CD2 TYR C 146 4668 3821 3032 -524 716 385 C ATOM 2935 CE1 TYR C 146 17.658 4.450 -3.594 1.00 29.31 C ANISOU 2935 CE1 TYR C 146 4521 3747 2866 -416 717 311 C ATOM 2936 CE2 TYR C 146 19.731 5.247 -2.682 1.00 36.90 C ANISOU 2936 CE2 TYR C 146 5422 4706 3894 -505 752 347 C ATOM 2937 CZ TYR C 146 18.932 4.202 -3.117 1.00 33.35 C ANISOU 2937 CZ TYR C 146 4967 4279 3427 -450 755 311 C ATOM 2938 OH TYR C 146 19.395 2.906 -3.076 1.00 33.77 O ANISOU 2938 OH TYR C 146 4945 4371 3517 -429 795 272 O ATOM 2939 N TYR C 147 17.020 6.664 -0.358 1.00 31.62 N ANISOU 2939 N TYR C 147 4856 3899 3258 -420 586 341 N ATOM 2940 CA TYR C 147 17.818 5.991 0.690 1.00 31.18 C ANISOU 2940 CA TYR C 147 4724 3869 3253 -427 595 321 C ATOM 2941 C TYR C 147 18.184 4.555 0.300 1.00 33.86 C ANISOU 2941 C TYR C 147 4997 4265 3605 -403 637 296 C ATOM 2942 O TYR C 147 17.369 3.848 -0.266 1.00 30.07 O ANISOU 2942 O TYR C 147 4525 3793 3106 -360 641 274 O ATOM 2943 CB TYR C 147 17.101 5.977 2.073 1.00 32.29 C ANISOU 2943 CB TYR C 147 4862 3981 3425 -393 547 298 C ATOM 2944 CG TYR C 147 16.874 7.353 2.671 1.00 30.94 C ANISOU 2944 CG TYR C 147 4748 3754 3255 -419 511 310 C ATOM 2945 CD1 TYR C 147 17.933 8.106 3.165 1.00 35.77 C ANISOU 2945 CD1 TYR C 147 5349 4359 3885 -482 512 323 C ATOM 2946 CD2 TYR C 147 15.596 7.906 2.716 1.00 30.65 C ANISOU 2946 CD2 TYR C 147 4771 3667 3207 -381 478 305 C ATOM 2947 CE1 TYR C 147 17.723 9.389 3.685 1.00 34.22 C ANISOU 2947 CE1 TYR C 147 5208 4101 3693 -510 484 326 C ATOM 2948 CE2 TYR C 147 15.379 9.172 3.235 1.00 32.36 C ANISOU 2948 CE2 TYR C 147 5040 3823 3433 -402 451 311 C ATOM 2949 CZ TYR C 147 16.439 9.909 3.716 1.00 34.19 C ANISOU 2949 CZ TYR C 147 5267 4043 3681 -467 455 320 C ATOM 2950 OH TYR C 147 16.201 11.174 4.228 1.00 38.50 O ANISOU 2950 OH TYR C 147 5868 4520 4240 -490 432 319 O ATOM 2951 N ASP C 148 19.417 4.142 0.596 1.00 34.92 N ANISOU 2951 N ASP C 148 5060 4432 3775 -431 667 298 N ATOM 2952 CA ASP C 148 19.777 2.730 0.632 1.00 33.40 C ANISOU 2952 CA ASP C 148 4793 4279 3617 -398 699 273 C ATOM 2953 C ASP C 148 19.088 2.160 1.884 1.00 34.96 C ANISOU 2953 C ASP C 148 4973 4460 3848 -349 658 257 C ATOM 2954 O ASP C 148 19.040 2.820 2.924 1.00 30.57 O ANISOU 2954 O ASP C 148 4430 3884 3301 -361 615 268 O ATOM 2955 CB ASP C 148 21.295 2.560 0.829 1.00 34.85 C ANISOU 2955 CB ASP C 148 4899 4499 3842 -437 732 284 C ATOM 2956 CG ASP C 148 22.103 2.557 -0.482 1.00 43.01 C ANISOU 2956 CG ASP C 148 5921 5565 4856 -475 800 288 C ATOM 2957 OD1 ASP C 148 21.533 2.574 -1.595 1.00 37.90 O ANISOU 2957 OD1 ASP C 148 5327 4919 4156 -470 823 281 O ATOM 2958 OD2 ASP C 148 23.351 2.535 -0.375 1.00 40.67 O ANISOU 2958 OD2 ASP C 148 5557 5298 4597 -511 830 296 O ATOM 2959 N ILE C 149 18.563 0.947 1.801 1.00 32.13 N ANISOU 2959 N ILE C 149 4590 4111 3509 -299 674 230 N ATOM 2960 CA ILE C 149 18.045 0.291 2.997 1.00 33.02 C ANISOU 2960 CA ILE C 149 4680 4210 3657 -256 646 222 C ATOM 2961 C ILE C 149 18.353 -1.199 2.990 1.00 32.91 C ANISOU 2961 C ILE C 149 4598 4215 3691 -219 685 207 C ATOM 2962 O ILE C 149 18.584 -1.803 1.932 1.00 30.09 O ANISOU 2962 O ILE C 149 4224 3875 3336 -215 733 186 O ATOM 2963 CB ILE C 149 16.498 0.462 3.154 1.00 41.95 C ANISOU 2963 CB ILE C 149 5869 5305 4765 -222 614 203 C ATOM 2964 CG1 ILE C 149 15.768 -0.068 1.929 1.00 40.52 C ANISOU 2964 CG1 ILE C 149 5705 5128 4562 -200 639 174 C ATOM 2965 CG2 ILE C 149 16.114 1.924 3.428 1.00 47.11 C ANISOU 2965 CG2 ILE C 149 6587 5928 5386 -248 572 218 C ATOM 2966 CD1 ILE C 149 14.269 -0.135 2.113 1.00 44.67 C ANISOU 2966 CD1 ILE C 149 6267 5626 5081 -161 609 150 C ATOM 2967 N SER C 150 18.353 -1.796 4.172 1.00 30.28 N ANISOU 2967 N SER C 150 4231 3878 3397 -190 666 216 N ATOM 2968 CA SER C 150 18.357 -3.246 4.265 1.00 33.74 C ANISOU 2968 CA SER C 150 4616 4316 3887 -145 699 205 C ATOM 2969 C SER C 150 17.289 -3.645 5.271 1.00 33.60 C ANISOU 2969 C SER C 150 4619 4270 3878 -107 671 203 C ATOM 2970 O SER C 150 17.486 -3.489 6.477 1.00 34.21 O ANISOU 2970 O SER C 150 4687 4350 3961 -106 637 232 O ATOM 2971 CB SER C 150 19.715 -3.757 4.712 1.00 33.43 C ANISOU 2971 CB SER C 150 4498 4305 3899 -145 712 232 C ATOM 2972 OG SER C 150 19.626 -5.126 5.067 1.00 34.68 O ANISOU 2972 OG SER C 150 4612 4451 4115 -93 736 231 O ATOM 2973 N ALA C 151 16.157 -4.125 4.762 1.00 32.50 N ANISOU 2973 N ALA C 151 4506 4107 3736 -82 687 168 N ATOM 2974 CA ALA C 151 15.033 -4.517 5.594 1.00 36.46 C ANISOU 2974 CA ALA C 151 5026 4579 4248 -50 671 161 C ATOM 2975 C ALA C 151 15.476 -5.552 6.618 1.00 41.76 C ANISOU 2975 C ALA C 151 5648 5247 4973 -21 682 189 C ATOM 2976 O ALA C 151 15.122 -5.458 7.789 1.00 33.73 O ANISOU 2976 O ALA C 151 4642 4222 3950 -12 654 212 O ATOM 2977 CB ALA C 151 13.898 -5.065 4.734 1.00 32.17 C ANISOU 2977 CB ALA C 151 4500 4015 3706 -30 694 112 C ATOM 2978 N LYS C 152 16.286 -6.513 6.183 1.00 36.18 N ANISOU 2978 N LYS C 152 4886 4547 4315 -6 723 191 N ATOM 2979 CA LYS C 152 16.663 -7.637 7.043 1.00 44.67 C ANISOU 2979 CA LYS C 152 5912 5610 5451 31 737 223 C ATOM 2980 C LYS C 152 17.619 -7.273 8.186 1.00 39.99 C ANISOU 2980 C LYS C 152 5292 5046 4854 24 695 281 C ATOM 2981 O LYS C 152 17.744 -8.016 9.160 1.00 43.22 O ANISOU 2981 O LYS C 152 5676 5448 5296 56 688 320 O ATOM 2982 CB LYS C 152 17.238 -8.780 6.203 1.00 46.85 C ANISOU 2982 CB LYS C 152 6135 5876 5791 54 797 204 C ATOM 2983 CG LYS C 152 16.204 -9.527 5.385 1.00 48.46 C ANISOU 2983 CG LYS C 152 6357 6045 6012 69 839 145 C ATOM 2984 CD LYS C 152 15.449 -10.540 6.233 1.00 56.13 C ANISOU 2984 CD LYS C 152 7325 6970 7032 106 851 156 C ATOM 2985 CE LYS C 152 14.970 -11.725 5.398 1.00 62.93 C ANISOU 2985 CE LYS C 152 8170 7792 7950 125 913 100 C ATOM 2986 NZ LYS C 152 16.115 -12.462 4.780 1.00 68.31 N ANISOU 2986 NZ LYS C 152 8793 8472 8687 140 962 94 N ATOM 2987 N SER C 153 18.286 -6.132 8.075 1.00 34.18 N ANISOU 2987 N SER C 153 4563 4345 4079 -19 664 288 N ATOM 2988 CA SER C 153 19.188 -5.685 9.135 1.00 39.14 C ANISOU 2988 CA SER C 153 5165 5008 4698 -34 617 333 C ATOM 2989 C SER C 153 18.717 -4.385 9.794 1.00 36.40 C ANISOU 2989 C SER C 153 4879 4667 4283 -72 565 331 C ATOM 2990 O SER C 153 19.421 -3.816 10.620 1.00 37.49 O ANISOU 2990 O SER C 153 5005 4838 4403 -97 521 357 O ATOM 2991 CB SER C 153 20.603 -5.500 8.590 1.00 35.84 C ANISOU 2991 CB SER C 153 4686 4627 4305 -58 626 344 C ATOM 2992 OG SER C 153 20.638 -4.454 7.622 1.00 39.34 O ANISOU 2992 OG SER C 153 5163 5076 4709 -106 634 314 O ATOM 2993 N ASN C 154 17.529 -3.918 9.428 1.00 29.63 N ANISOU 2993 N ASN C 154 4085 3778 3393 -76 569 295 N ATOM 2994 CA ASN C 154 17.012 -2.648 9.947 1.00 29.22 C ANISOU 2994 CA ASN C 154 4094 3721 3286 -107 528 285 C ATOM 2995 C ASN C 154 17.800 -1.406 9.522 1.00 34.36 C ANISOU 2995 C ASN C 154 4754 4389 3912 -162 508 283 C ATOM 2996 O ASN C 154 17.552 -0.318 10.031 1.00 30.13 O ANISOU 2996 O ASN C 154 4264 3846 3338 -193 474 276 O ATOM 2997 CB ASN C 154 16.899 -2.677 11.487 1.00 30.30 C ANISOU 2997 CB ASN C 154 4238 3871 3405 -101 492 309 C ATOM 2998 CG ASN C 154 15.931 -3.722 11.979 1.00 37.79 C ANISOU 2998 CG ASN C 154 5193 4795 4371 -54 515 313 C ATOM 2999 OD1 ASN C 154 14.972 -4.092 11.281 1.00 34.48 O ANISOU 2999 OD1 ASN C 154 4791 4341 3967 -33 548 281 O ATOM 3000 ND2 ASN C 154 16.166 -4.206 13.198 1.00 37.85 N ANISOU 3000 ND2 ASN C 154 5186 4822 4374 -39 496 351 N ATOM 3001 N TYR C 155 18.716 -1.562 8.570 1.00 35.48 N ANISOU 3001 N TYR C 155 4855 4550 4077 -177 536 287 N ATOM 3002 CA TYR C 155 19.577 -0.468 8.138 1.00 31.85 C ANISOU 3002 CA TYR C 155 4397 4106 3600 -235 527 290 C ATOM 3003 C TYR C 155 18.774 0.633 7.469 1.00 32.56 C ANISOU 3003 C TYR C 155 4564 4160 3648 -259 524 269 C ATOM 3004 O TYR C 155 18.060 0.386 6.504 1.00 30.77 O ANISOU 3004 O TYR C 155 4363 3915 3413 -238 552 251 O ATOM 3005 CB TYR C 155 20.679 -0.978 7.198 1.00 31.58 C ANISOU 3005 CB TYR C 155 4297 4098 3602 -243 571 297 C ATOM 3006 CG TYR C 155 21.554 0.121 6.624 1.00 34.30 C ANISOU 3006 CG TYR C 155 4643 4459 3932 -308 574 300 C ATOM 3007 CD1 TYR C 155 22.462 0.817 7.426 1.00 39.59 C ANISOU 3007 CD1 TYR C 155 5284 5153 4605 -353 535 317 C ATOM 3008 CD2 TYR C 155 21.466 0.465 5.277 1.00 34.31 C ANISOU 3008 CD2 TYR C 155 4674 4450 3913 -328 616 287 C ATOM 3009 CE1 TYR C 155 23.268 1.834 6.891 1.00 40.05 C ANISOU 3009 CE1 TYR C 155 5341 5220 4657 -420 544 319 C ATOM 3010 CE2 TYR C 155 22.265 1.466 4.729 1.00 33.91 C ANISOU 3010 CE2 TYR C 155 4628 4409 3850 -391 626 296 C ATOM 3011 CZ TYR C 155 23.162 2.144 5.535 1.00 37.04 C ANISOU 3011 CZ TYR C 155 4993 4823 4259 -438 593 311 C ATOM 3012 OH TYR C 155 23.934 3.133 4.972 1.00 43.66 O ANISOU 3012 OH TYR C 155 5834 5666 5090 -507 610 319 O ATOM 3013 N ASN C 156 18.897 1.842 8.017 1.00 29.92 N ANISOU 3013 N ASN C 156 4265 3817 3287 -302 487 270 N ATOM 3014 CA ASN C 156 18.184 3.037 7.574 1.00 31.16 C ANISOU 3014 CA ASN C 156 4498 3931 3411 -324 477 257 C ATOM 3015 C ASN C 156 16.664 2.902 7.643 1.00 30.14 C ANISOU 3015 C ASN C 156 4419 3766 3268 -276 471 234 C ATOM 3016 O ASN C 156 15.945 3.586 6.909 1.00 32.29 O ANISOU 3016 O ASN C 156 4744 4003 3520 -276 471 226 O ATOM 3017 CB ASN C 156 18.606 3.463 6.156 1.00 29.89 C ANISOU 3017 CB ASN C 156 4348 3768 3242 -354 510 264 C ATOM 3018 CG ASN C 156 19.915 4.236 6.129 1.00 35.19 C ANISOU 3018 CG ASN C 156 4995 4456 3919 -421 511 282 C ATOM 3019 OD1 ASN C 156 20.408 4.712 7.158 1.00 36.28 O ANISOU 3019 OD1 ASN C 156 5120 4602 4063 -451 476 282 O ATOM 3020 ND2 ASN C 156 20.478 4.383 4.925 1.00 31.02 N ANISOU 3020 ND2 ASN C 156 4462 3938 3387 -449 552 293 N ATOM 3021 N PHE C 157 16.173 2.044 8.529 1.00 31.11 N ANISOU 3021 N PHE C 157 4522 3895 3403 -237 466 229 N ATOM 3022 CA PHE C 157 14.737 1.794 8.596 1.00 30.27 C ANISOU 3022 CA PHE C 157 4451 3758 3293 -193 468 205 C ATOM 3023 C PHE C 157 13.912 3.061 8.811 1.00 28.02 C ANISOU 3023 C PHE C 157 4232 3431 2983 -203 442 186 C ATOM 3024 O PHE C 157 12.860 3.244 8.189 1.00 30.51 O ANISOU 3024 O PHE C 157 4581 3717 3295 -176 445 169 O ATOM 3025 CB PHE C 157 14.380 0.803 9.705 1.00 28.71 C ANISOU 3025 CB PHE C 157 4229 3572 3110 -158 470 206 C ATOM 3026 CG PHE C 157 12.894 0.571 9.818 1.00 31.02 C ANISOU 3026 CG PHE C 157 4551 3832 3404 -119 478 178 C ATOM 3027 CD1 PHE C 157 12.268 -0.377 9.022 1.00 26.74 C ANISOU 3027 CD1 PHE C 157 3991 3283 2887 -85 508 163 C ATOM 3028 CD2 PHE C 157 12.119 1.344 10.675 1.00 26.97 C ANISOU 3028 CD2 PHE C 157 4081 3296 2870 -119 457 159 C ATOM 3029 CE1 PHE C 157 10.891 -0.566 9.087 1.00 25.25 C ANISOU 3029 CE1 PHE C 157 3820 3067 2704 -53 514 133 C ATOM 3030 CE2 PHE C 157 10.746 1.149 10.752 1.00 28.87 C ANISOU 3030 CE2 PHE C 157 4340 3509 3119 -84 468 130 C ATOM 3031 CZ PHE C 157 10.136 0.182 9.954 1.00 25.45 C ANISOU 3031 CZ PHE C 157 3883 3073 2714 -51 495 119 C ATOM 3032 N GLU C 158 14.365 3.914 9.725 1.00 27.59 N ANISOU 3032 N GLU C 158 4195 3374 2915 -238 415 187 N ATOM 3033 CA GLU C 158 13.594 5.095 10.091 1.00 29.69 C ANISOU 3033 CA GLU C 158 4522 3593 3165 -245 395 163 C ATOM 3034 C GLU C 158 13.644 6.196 9.034 1.00 29.79 C ANISOU 3034 C GLU C 158 4577 3567 3173 -270 392 170 C ATOM 3035 O GLU C 158 12.779 7.075 9.022 1.00 30.09 O ANISOU 3035 O GLU C 158 4668 3555 3210 -259 380 154 O ATOM 3036 CB GLU C 158 14.080 5.671 11.427 1.00 30.82 C ANISOU 3036 CB GLU C 158 4673 3745 3292 -281 369 152 C ATOM 3037 CG GLU C 158 15.307 6.597 11.334 1.00 35.09 C ANISOU 3037 CG GLU C 158 5214 4290 3830 -348 353 163 C ATOM 3038 CD GLU C 158 16.624 5.849 11.139 1.00 40.93 C ANISOU 3038 CD GLU C 158 5884 5088 4581 -369 358 194 C ATOM 3039 OE1 GLU C 158 16.606 4.612 10.947 1.00 41.54 O ANISOU 3039 OE1 GLU C 158 5916 5196 4672 -329 377 210 O ATOM 3040 OE2 GLU C 158 17.690 6.508 11.181 1.00 44.55 O ANISOU 3040 OE2 GLU C 158 6327 5558 5040 -427 345 201 O ATOM 3041 N LYS C 159 14.668 6.169 8.181 1.00 28.75 N ANISOU 3041 N LYS C 159 4424 3458 3043 -303 406 197 N ATOM 3042 CA LYS C 159 14.950 7.305 7.274 1.00 31.43 C ANISOU 3042 CA LYS C 159 4806 3762 3373 -341 406 214 C ATOM 3043 C LYS C 159 13.795 7.773 6.369 1.00 27.19 C ANISOU 3043 C LYS C 159 4325 3180 2827 -305 403 216 C ATOM 3044 O LYS C 159 13.492 8.970 6.297 1.00 28.95 O ANISOU 3044 O LYS C 159 4603 3347 3048 -319 387 219 O ATOM 3045 CB LYS C 159 16.204 7.034 6.437 1.00 34.54 C ANISOU 3045 CB LYS C 159 5161 4195 3768 -380 433 243 C ATOM 3046 CG LYS C 159 17.491 6.897 7.259 1.00 39.52 C ANISOU 3046 CG LYS C 159 5736 4867 4415 -425 428 247 C ATOM 3047 CD LYS C 159 17.957 8.224 7.796 1.00 47.96 C ANISOU 3047 CD LYS C 159 6837 5903 5482 -486 406 242 C ATOM 3048 CE LYS C 159 19.445 8.177 8.119 1.00 58.65 C ANISOU 3048 CE LYS C 159 8127 7304 6852 -544 406 252 C ATOM 3049 NZ LYS C 159 19.791 7.032 9.012 1.00 62.83 N ANISOU 3049 NZ LYS C 159 8588 7894 7391 -516 392 248 N ATOM 3050 N PRO C 160 13.191 6.850 5.620 1.00 31.82 N ANISOU 3050 N PRO C 160 4893 3788 3408 -261 416 213 N ATOM 3051 CA PRO C 160 12.066 7.267 4.771 1.00 28.86 C ANISOU 3051 CA PRO C 160 4565 3380 3022 -225 403 215 C ATOM 3052 C PRO C 160 10.953 7.930 5.592 1.00 29.22 C ANISOU 3052 C PRO C 160 4645 3374 3085 -193 376 189 C ATOM 3053 O PRO C 160 10.423 8.971 5.218 1.00 30.47 O ANISOU 3053 O PRO C 160 4855 3480 3242 -186 356 200 O ATOM 3054 CB PRO C 160 11.558 5.946 4.180 1.00 32.95 C ANISOU 3054 CB PRO C 160 5044 3939 3537 -183 419 199 C ATOM 3055 CG PRO C 160 12.681 4.977 4.337 1.00 38.90 C ANISOU 3055 CG PRO C 160 5739 4742 4299 -206 450 202 C ATOM 3056 CD PRO C 160 13.494 5.412 5.512 1.00 27.92 C ANISOU 3056 CD PRO C 160 4337 3348 2922 -242 442 208 C ATOM 3057 N PHE C 161 10.622 7.324 6.726 1.00 31.34 N ANISOU 3057 N PHE C 161 4884 3655 3370 -174 378 158 N ATOM 3058 CA PHE C 161 9.564 7.840 7.602 1.00 30.00 C ANISOU 3058 CA PHE C 161 4739 3443 3216 -145 363 125 C ATOM 3059 C PHE C 161 9.869 9.213 8.183 1.00 28.48 C ANISOU 3059 C PHE C 161 4595 3199 3027 -180 348 121 C ATOM 3060 O PHE C 161 8.997 10.068 8.245 1.00 28.69 O ANISOU 3060 O PHE C 161 4661 3168 3070 -155 335 107 O ATOM 3061 CB PHE C 161 9.281 6.834 8.717 1.00 28.43 C ANISOU 3061 CB PHE C 161 4500 3276 3026 -125 377 97 C ATOM 3062 CG PHE C 161 8.908 5.473 8.207 1.00 22.24 C ANISOU 3062 CG PHE C 161 3670 2531 2250 -91 395 95 C ATOM 3063 CD1 PHE C 161 7.619 5.222 7.731 1.00 22.66 C ANISOU 3063 CD1 PHE C 161 3722 2569 2318 -43 392 73 C ATOM 3064 CD2 PHE C 161 9.838 4.454 8.187 1.00 24.54 C ANISOU 3064 CD2 PHE C 161 3916 2869 2539 -107 415 112 C ATOM 3065 CE1 PHE C 161 7.265 3.963 7.262 1.00 30.34 C ANISOU 3065 CE1 PHE C 161 4653 3575 3302 -19 411 63 C ATOM 3066 CE2 PHE C 161 9.495 3.184 7.718 1.00 26.25 C ANISOU 3066 CE2 PHE C 161 4093 3112 2771 -78 438 104 C ATOM 3067 CZ PHE C 161 8.201 2.940 7.258 1.00 27.28 C ANISOU 3067 CZ PHE C 161 4226 3227 2914 -37 436 77 C ATOM 3068 N LEU C 162 11.110 9.453 8.576 1.00 26.51 N ANISOU 3068 N LEU C 162 4338 2966 2768 -239 351 132 N ATOM 3069 CA LEU C 162 11.467 10.780 9.064 1.00 25.72 C ANISOU 3069 CA LEU C 162 4283 2813 2674 -282 339 124 C ATOM 3070 C LEU C 162 11.364 11.876 7.977 1.00 27.47 C ANISOU 3070 C LEU C 162 4560 2973 2905 -290 334 155 C ATOM 3071 O LEU C 162 10.871 12.989 8.241 1.00 29.74 O ANISOU 3071 O LEU C 162 4899 3188 3214 -288 323 141 O ATOM 3072 CB LEU C 162 12.872 10.759 9.664 1.00 28.36 C ANISOU 3072 CB LEU C 162 4589 3187 2998 -349 340 127 C ATOM 3073 CG LEU C 162 13.382 12.056 10.299 1.00 33.25 C ANISOU 3073 CG LEU C 162 5248 3759 3625 -408 328 107 C ATOM 3074 CD1 LEU C 162 12.501 12.491 11.475 1.00 32.62 C ANISOU 3074 CD1 LEU C 162 5200 3645 3549 -387 319 52 C ATOM 3075 CD2 LEU C 162 14.837 11.893 10.741 1.00 33.89 C ANISOU 3075 CD2 LEU C 162 5286 3894 3696 -475 323 112 C ATOM 3076 N TRP C 163 11.841 11.573 6.768 1.00 26.64 N ANISOU 3076 N TRP C 163 4446 2894 2783 -300 344 199 N ATOM 3077 CA TRP C 163 11.804 12.542 5.660 1.00 25.71 C ANISOU 3077 CA TRP C 163 4383 2724 2663 -309 340 242 C ATOM 3078 C TRP C 163 10.352 12.879 5.321 1.00 29.06 C ANISOU 3078 C TRP C 163 4842 3100 3099 -239 318 239 C ATOM 3079 O TRP C 163 9.978 14.052 5.176 1.00 32.58 O ANISOU 3079 O TRP C 163 5346 3469 3566 -235 304 253 O ATOM 3080 CB TRP C 163 12.508 11.995 4.414 1.00 30.98 C ANISOU 3080 CB TRP C 163 5031 3441 3297 -329 361 286 C ATOM 3081 CG TRP C 163 12.676 13.020 3.331 1.00 38.04 C ANISOU 3081 CG TRP C 163 5987 4287 4179 -352 362 339 C ATOM 3082 CD1 TRP C 163 13.697 13.922 3.206 1.00 43.80 C ANISOU 3082 CD1 TRP C 163 6743 4985 4915 -423 379 367 C ATOM 3083 CD2 TRP C 163 11.789 13.265 2.232 1.00 34.52 C ANISOU 3083 CD2 TRP C 163 5584 3820 3712 -306 346 374 C ATOM 3084 NE1 TRP C 163 13.505 14.706 2.091 1.00 40.33 N ANISOU 3084 NE1 TRP C 163 6365 4501 4458 -424 380 424 N ATOM 3085 CE2 TRP C 163 12.342 14.324 1.475 1.00 38.61 C ANISOU 3085 CE2 TRP C 163 6160 4292 4220 -351 355 431 C ATOM 3086 CE3 TRP C 163 10.588 12.683 1.806 1.00 32.58 C ANISOU 3086 CE3 TRP C 163 5332 3593 3455 -233 322 365 C ATOM 3087 CZ2 TRP C 163 11.735 14.816 0.316 1.00 45.57 C ANISOU 3087 CZ2 TRP C 163 7097 5145 5072 -320 339 485 C ATOM 3088 CZ3 TRP C 163 9.982 13.177 0.653 1.00 45.98 C ANISOU 3088 CZ3 TRP C 163 7077 5268 5125 -204 300 412 C ATOM 3089 CH2 TRP C 163 10.559 14.235 -0.078 1.00 49.51 C ANISOU 3089 CH2 TRP C 163 7587 5670 5555 -245 307 475 C ATOM 3090 N LEU C 164 9.539 11.844 5.188 1.00 28.58 N ANISOU 3090 N LEU C 164 4744 3083 3032 -184 314 221 N ATOM 3091 CA LEU C 164 8.109 12.023 4.940 1.00 32.82 C ANISOU 3091 CA LEU C 164 5298 3587 3587 -114 289 211 C ATOM 3092 C LEU C 164 7.442 12.812 6.070 1.00 32.99 C ANISOU 3092 C LEU C 164 5341 3544 3650 -95 282 169 C ATOM 3093 O LEU C 164 6.657 13.718 5.814 1.00 37.09 O ANISOU 3093 O LEU C 164 5900 3997 4195 -59 262 177 O ATOM 3094 CB LEU C 164 7.418 10.664 4.751 1.00 23.96 C ANISOU 3094 CB LEU C 164 4120 2528 2457 -69 291 186 C ATOM 3095 CG LEU C 164 7.798 9.891 3.486 1.00 27.59 C ANISOU 3095 CG LEU C 164 4561 3045 2875 -75 297 216 C ATOM 3096 CD1 LEU C 164 7.283 8.454 3.515 1.00 32.54 C ANISOU 3096 CD1 LEU C 164 5128 3731 3504 -43 308 180 C ATOM 3097 CD2 LEU C 164 7.323 10.625 2.222 1.00 29.70 C ANISOU 3097 CD2 LEU C 164 4878 3287 3120 -53 268 260 C ATOM 3098 N ALA C 165 7.748 12.484 7.326 1.00 31.26 N ANISOU 3098 N ALA C 165 5097 3344 3436 -118 299 126 N ATOM 3099 CA ALA C 165 7.134 13.216 8.448 1.00 29.17 C ANISOU 3099 CA ALA C 165 4855 3024 3204 -104 300 77 C ATOM 3100 C ALA C 165 7.433 14.716 8.390 1.00 31.78 C ANISOU 3100 C ALA C 165 5250 3268 3558 -133 293 88 C ATOM 3101 O ALA C 165 6.552 15.568 8.614 1.00 30.37 O ANISOU 3101 O ALA C 165 5105 3015 3420 -95 286 67 O ATOM 3102 CB ALA C 165 7.573 12.631 9.793 1.00 30.34 C ANISOU 3102 CB ALA C 165 4973 3218 3338 -134 319 33 C ATOM 3103 N ARG C 166 8.686 15.046 8.101 1.00 34.97 N ANISOU 3103 N ARG C 166 5668 3675 3943 -202 298 120 N ATOM 3104 CA ARG C 166 9.079 16.443 8.028 1.00 39.61 C ANISOU 3104 CA ARG C 166 6317 4176 4558 -241 297 133 C ATOM 3105 C ARG C 166 8.330 17.135 6.897 1.00 38.92 C ANISOU 3105 C ARG C 166 6275 4023 4491 -193 280 183 C ATOM 3106 O ARG C 166 7.911 18.274 7.053 1.00 33.84 O ANISOU 3106 O ARG C 166 5682 3283 3891 -181 276 178 O ATOM 3107 CB ARG C 166 10.595 16.583 7.855 1.00 36.78 C ANISOU 3107 CB ARG C 166 5956 3841 4179 -330 310 160 C ATOM 3108 CG ARG C 166 11.359 16.145 9.094 1.00 32.58 C ANISOU 3108 CG ARG C 166 5384 3364 3633 -379 316 110 C ATOM 3109 CD ARG C 166 12.850 16.096 8.838 1.00 37.29 C ANISOU 3109 CD ARG C 166 5957 4000 4212 -460 325 138 C ATOM 3110 NE ARG C 166 13.596 16.178 10.087 1.00 40.72 N ANISOU 3110 NE ARG C 166 6370 4460 4643 -517 321 89 N ATOM 3111 CZ ARG C 166 14.871 15.829 10.218 1.00 51.37 C ANISOU 3111 CZ ARG C 166 7673 5870 5976 -581 323 98 C ATOM 3112 NH1 ARG C 166 15.539 15.352 9.178 1.00 54.18 N ANISOU 3112 NH1 ARG C 166 7999 6266 6323 -595 337 151 N ATOM 3113 NH2 ARG C 166 15.474 15.945 11.391 1.00 52.81 N ANISOU 3113 NH2 ARG C 166 7836 6079 6151 -630 309 50 N ATOM 3114 N LYS C 167 8.143 16.426 5.787 1.00 35.07 N ANISOU 3114 N LYS C 167 5768 3586 3971 -163 270 230 N ATOM 3115 CA LYS C 167 7.443 16.956 4.616 1.00 35.52 C ANISOU 3115 CA LYS C 167 5864 3599 4032 -115 245 286 C ATOM 3116 C LYS C 167 5.955 17.138 4.871 1.00 36.30 C ANISOU 3116 C LYS C 167 5961 3658 4174 -29 220 257 C ATOM 3117 O LYS C 167 5.375 18.143 4.475 1.00 35.18 O ANISOU 3117 O LYS C 167 5866 3433 4067 8 200 286 O ATOM 3118 CB LYS C 167 7.610 16.023 3.407 1.00 38.72 C ANISOU 3118 CB LYS C 167 6246 4087 4381 -108 239 332 C ATOM 3119 CG LYS C 167 9.006 15.991 2.800 1.00 42.35 C ANISOU 3119 CG LYS C 167 6713 4578 4799 -186 265 376 C ATOM 3120 CD LYS C 167 9.411 17.368 2.261 1.00 59.37 C ANISOU 3120 CD LYS C 167 8945 6647 6968 -221 267 435 C ATOM 3121 CE LYS C 167 8.487 17.831 1.145 1.00 61.62 C ANISOU 3121 CE LYS C 167 9276 6896 7241 -159 233 496 C ATOM 3122 NZ LYS C 167 8.991 19.077 0.494 1.00 66.98 N ANISOU 3122 NZ LYS C 167 10033 7493 7925 -197 240 569 N ATOM 3123 N LEU C 168 5.337 16.157 5.518 1.00 30.02 N ANISOU 3123 N LEU C 168 5108 2920 3380 5 224 201 N ATOM 3124 CA LEU C 168 3.896 16.202 5.774 1.00 30.22 C ANISOU 3124 CA LEU C 168 5115 2918 3449 86 207 167 C ATOM 3125 C LEU C 168 3.552 17.243 6.833 1.00 37.80 C ANISOU 3125 C LEU C 168 6106 3788 4467 94 221 119 C ATOM 3126 O LEU C 168 2.645 18.072 6.654 1.00 40.14 O ANISOU 3126 O LEU C 168 6427 4008 4817 152 203 123 O ATOM 3127 CB LEU C 168 3.387 14.822 6.193 1.00 28.47 C ANISOU 3127 CB LEU C 168 4822 2782 3215 110 217 120 C ATOM 3128 CG LEU C 168 3.399 13.800 5.060 1.00 32.37 C ANISOU 3128 CG LEU C 168 5283 3353 3663 120 201 155 C ATOM 3129 CD1 LEU C 168 3.435 12.388 5.619 1.00 29.00 C ANISOU 3129 CD1 LEU C 168 4792 3007 3220 112 227 111 C ATOM 3130 CD2 LEU C 168 2.189 14.015 4.162 1.00 34.85 C ANISOU 3130 CD2 LEU C 168 5595 3651 3996 194 157 175 C ATOM 3131 N ILE C 169 4.293 17.216 7.932 1.00 37.82 N ANISOU 3131 N ILE C 169 6108 3800 4461 35 252 73 N ATOM 3132 CA ILE C 169 4.022 18.143 9.019 1.00 33.31 C ANISOU 3132 CA ILE C 169 5568 3152 3938 33 271 14 C ATOM 3133 C ILE C 169 4.467 19.558 8.647 1.00 36.14 C ANISOU 3133 C ILE C 169 5997 3404 4330 6 267 47 C ATOM 3134 O ILE C 169 3.939 20.546 9.164 1.00 37.14 O ANISOU 3134 O ILE C 169 6159 3437 4516 30 275 11 O ATOM 3135 CB ILE C 169 4.671 17.671 10.333 1.00 32.17 C ANISOU 3135 CB ILE C 169 5402 3058 3762 -25 301 -49 C ATOM 3136 CG1 ILE C 169 4.099 16.304 10.712 1.00 36.29 C ANISOU 3136 CG1 ILE C 169 5858 3670 4259 9 311 -75 C ATOM 3137 CG2 ILE C 169 4.433 18.694 11.441 1.00 35.75 C ANISOU 3137 CG2 ILE C 169 5894 3433 4256 -34 323 -118 C ATOM 3138 CD1 ILE C 169 2.600 16.274 10.611 1.00 43.27 C ANISOU 3138 CD1 ILE C 169 6721 4529 5190 95 307 -98 C ATOM 3139 N GLY C 170 5.423 19.662 7.726 1.00 36.51 N ANISOU 3139 N GLY C 170 6066 3460 4344 -42 258 117 N ATOM 3140 CA GLY C 170 5.919 20.974 7.344 1.00 39.53 C ANISOU 3140 CA GLY C 170 6519 3740 4760 -77 259 156 C ATOM 3141 C GLY C 170 6.860 21.540 8.393 1.00 46.22 C ANISOU 3141 C GLY C 170 7388 4557 5618 -161 288 102 C ATOM 3142 O GLY C 170 6.862 22.737 8.663 1.00 45.87 O ANISOU 3142 O GLY C 170 7399 4403 5628 -176 298 87 O ATOM 3143 N ASP C 171 7.678 20.670 8.974 1.00 43.61 N ANISOU 3143 N ASP C 171 7012 4322 5236 -217 299 72 N ATOM 3144 CA ASP C 171 8.626 21.076 10.011 1.00 38.97 C ANISOU 3144 CA ASP C 171 6433 3727 4646 -302 318 17 C ATOM 3145 C ASP C 171 9.962 20.374 9.790 1.00 39.48 C ANISOU 3145 C ASP C 171 6460 3883 4657 -377 319 47 C ATOM 3146 O ASP C 171 10.117 19.178 10.108 1.00 31.91 O ANISOU 3146 O ASP C 171 5441 3029 3653 -372 317 34 O ATOM 3147 CB ASP C 171 8.073 20.720 11.387 1.00 40.72 C ANISOU 3147 CB ASP C 171 6630 3978 4864 -283 329 -75 C ATOM 3148 CG ASP C 171 9.003 21.125 12.522 1.00 48.22 C ANISOU 3148 CG ASP C 171 7590 4930 5801 -371 341 -139 C ATOM 3149 OD1 ASP C 171 10.085 21.709 12.260 1.00 42.02 O ANISOU 3149 OD1 ASP C 171 6825 4120 5019 -448 341 -117 O ATOM 3150 OD2 ASP C 171 8.637 20.846 13.685 1.00 47.04 O ANISOU 3150 OD2 ASP C 171 7426 4813 5635 -364 351 -213 O ATOM 3151 N PRO C 172 10.932 21.113 9.241 1.00 37.53 N ANISOU 3151 N PRO C 172 6245 3593 4420 -446 327 88 N ATOM 3152 CA PRO C 172 12.247 20.554 8.902 1.00 43.07 C ANISOU 3152 CA PRO C 172 6907 4375 5081 -519 333 120 C ATOM 3153 C PRO C 172 13.042 20.129 10.141 1.00 42.59 C ANISOU 3153 C PRO C 172 6800 4384 4998 -579 332 55 C ATOM 3154 O PRO C 172 14.037 19.428 10.001 1.00 49.17 O ANISOU 3154 O PRO C 172 7582 5302 5800 -624 333 75 O ATOM 3155 CB PRO C 172 12.967 21.725 8.206 1.00 47.41 C ANISOU 3155 CB PRO C 172 7513 4839 5664 -584 348 167 C ATOM 3156 CG PRO C 172 11.948 22.806 8.034 1.00 47.70 C ANISOU 3156 CG PRO C 172 7621 4748 5756 -532 346 173 C ATOM 3157 CD PRO C 172 10.880 22.574 9.045 1.00 42.92 C ANISOU 3157 CD PRO C 172 7002 4143 5163 -466 336 97 C ATOM 3158 N ASN C 173 12.614 20.556 11.326 1.00 35.65 N ANISOU 3158 N ASN C 173 5939 3472 4135 -578 330 -23 N ATOM 3159 CA ASN C 173 13.377 20.310 12.550 1.00 43.49 C ANISOU 3159 CA ASN C 173 6898 4528 5099 -640 324 -86 C ATOM 3160 C ASN C 173 12.780 19.194 13.392 1.00 43.04 C ANISOU 3160 C ASN C 173 6797 4557 4999 -588 316 -123 C ATOM 3161 O ASN C 173 13.204 18.941 14.521 1.00 43.07 O ANISOU 3161 O ASN C 173 6778 4617 4969 -625 306 -176 O ATOM 3162 CB ASN C 173 13.484 21.593 13.370 1.00 47.27 C ANISOU 3162 CB ASN C 173 7430 4917 5614 -694 330 -156 C ATOM 3163 CG ASN C 173 14.140 22.708 12.596 1.00 47.65 C ANISOU 3163 CG ASN C 173 7523 4873 5711 -756 343 -119 C ATOM 3164 OD1 ASN C 173 15.282 22.577 12.145 1.00 47.26 O ANISOU 3164 OD1 ASN C 173 7443 4864 5650 -824 343 -81 O ATOM 3165 ND2 ASN C 173 13.417 23.809 12.418 1.00 46.84 N ANISOU 3165 ND2 ASN C 173 7490 4641 5667 -731 357 -128 N ATOM 3166 N LEU C 174 11.780 18.539 12.823 1.00 37.28 N ANISOU 3166 N LEU C 174 6057 3838 4269 -502 319 -92 N ATOM 3167 CA LEU C 174 11.106 17.440 13.475 1.00 35.64 C ANISOU 3167 CA LEU C 174 5809 3703 4028 -448 318 -117 C ATOM 3168 C LEU C 174 12.101 16.307 13.642 1.00 31.80 C ANISOU 3168 C LEU C 174 5258 3328 3495 -482 308 -94 C ATOM 3169 O LEU C 174 12.885 16.036 12.746 1.00 30.07 O ANISOU 3169 O LEU C 174 5015 3136 3275 -506 306 -39 O ATOM 3170 CB LEU C 174 9.935 16.985 12.622 1.00 37.73 C ANISOU 3170 CB LEU C 174 6069 3955 4311 -359 322 -83 C ATOM 3171 CG LEU C 174 9.155 15.819 13.226 1.00 46.67 C ANISOU 3171 CG LEU C 174 7159 5156 5419 -304 329 -108 C ATOM 3172 CD1 LEU C 174 7.978 16.346 14.011 1.00 54.05 C ANISOU 3172 CD1 LEU C 174 8122 6036 6380 -261 344 -172 C ATOM 3173 CD2 LEU C 174 8.679 14.881 12.149 1.00 45.12 C ANISOU 3173 CD2 LEU C 174 6927 4995 5221 -248 326 -56 C ATOM 3174 N GLU C 175 12.078 15.654 14.798 1.00 32.54 N ANISOU 3174 N GLU C 175 5325 3487 3551 -482 305 -134 N ATOM 3175 CA GLU C 175 12.984 14.545 15.053 1.00 34.77 C ANISOU 3175 CA GLU C 175 5544 3873 3793 -505 292 -108 C ATOM 3176 C GLU C 175 12.179 13.403 15.651 1.00 36.10 C ANISOU 3176 C GLU C 175 5686 4097 3934 -444 300 -117 C ATOM 3177 O GLU C 175 11.091 13.631 16.195 1.00 30.55 O ANISOU 3177 O GLU C 175 5013 3360 3235 -405 315 -160 O ATOM 3178 CB GLU C 175 14.070 14.966 16.051 1.00 44.79 C ANISOU 3178 CB GLU C 175 6808 5175 5036 -586 270 -145 C ATOM 3179 CG GLU C 175 14.937 16.149 15.604 1.00 46.28 C ANISOU 3179 CG GLU C 175 7021 5306 5257 -661 265 -146 C ATOM 3180 CD GLU C 175 15.959 15.754 14.551 1.00 55.40 C ANISOU 3180 CD GLU C 175 8129 6496 6423 -689 264 -79 C ATOM 3181 OE1 GLU C 175 16.061 14.544 14.246 1.00 53.97 O ANISOU 3181 OE1 GLU C 175 7894 6387 6225 -651 265 -39 O ATOM 3182 OE2 GLU C 175 16.657 16.650 14.021 1.00 58.93 O ANISOU 3182 OE2 GLU C 175 8594 6896 6900 -750 269 -69 O ATOM 3183 N PHE C 176 12.705 12.183 15.544 1.00 30.12 N ANISOU 3183 N PHE C 176 4869 3419 3155 -436 295 -76 N ATOM 3184 CA PHE C 176 12.159 11.033 16.261 1.00 32.13 C ANISOU 3184 CA PHE C 176 5095 3731 3381 -391 304 -79 C ATOM 3185 C PHE C 176 12.886 10.976 17.597 1.00 38.49 C ANISOU 3185 C PHE C 176 5893 4596 4137 -439 282 -103 C ATOM 3186 O PHE C 176 14.121 10.994 17.624 1.00 40.69 O ANISOU 3186 O PHE C 176 6141 4915 4406 -491 255 -84 O ATOM 3187 CB PHE C 176 12.401 9.731 15.491 1.00 36.21 C ANISOU 3187 CB PHE C 176 5555 4298 3906 -359 311 -21 C ATOM 3188 CG PHE C 176 11.547 9.575 14.254 1.00 36.78 C ANISOU 3188 CG PHE C 176 5632 4328 4013 -307 330 -2 C ATOM 3189 CD1 PHE C 176 10.435 10.382 14.048 1.00 40.58 C ANISOU 3189 CD1 PHE C 176 6160 4740 4518 -276 338 -32 C ATOM 3190 CD2 PHE C 176 11.851 8.611 13.303 1.00 37.32 C ANISOU 3190 CD2 PHE C 176 5656 4430 4092 -287 339 42 C ATOM 3191 CE1 PHE C 176 9.651 10.240 12.896 1.00 36.20 C ANISOU 3191 CE1 PHE C 176 5607 4156 3993 -228 346 -12 C ATOM 3192 CE2 PHE C 176 11.062 8.451 12.168 1.00 32.68 C ANISOU 3192 CE2 PHE C 176 5074 3814 3529 -243 351 55 C ATOM 3193 CZ PHE C 176 9.959 9.263 11.967 1.00 33.06 C ANISOU 3193 CZ PHE C 176 5167 3799 3595 -214 351 30 C ATOM 3194 N VAL C 177 12.141 10.926 18.700 1.00 41.15 N ANISOU 3194 N VAL C 177 6254 4941 4440 -422 293 -147 N ATOM 3195 CA VAL C 177 12.766 10.936 20.022 1.00 41.70 C ANISOU 3195 CA VAL C 177 6325 5072 4449 -469 268 -174 C ATOM 3196 C VAL C 177 13.402 9.585 20.328 1.00 35.20 C ANISOU 3196 C VAL C 177 5442 4339 3592 -458 251 -118 C ATOM 3197 O VAL C 177 14.367 9.501 21.081 1.00 36.87 O ANISOU 3197 O VAL C 177 5634 4616 3760 -503 214 -114 O ATOM 3198 CB VAL C 177 11.787 11.356 21.170 1.00 45.57 C ANISOU 3198 CB VAL C 177 6866 5545 4901 -460 291 -244 C ATOM 3199 CG1 VAL C 177 11.161 12.707 20.880 1.00 52.60 C ANISOU 3199 CG1 VAL C 177 7813 6337 5836 -465 309 -301 C ATOM 3200 CG2 VAL C 177 10.717 10.316 21.390 1.00 45.15 C ANISOU 3200 CG2 VAL C 177 6803 5512 4841 -393 327 -229 C ATOM 3201 N ALA C 178 12.876 8.533 19.716 1.00 28.33 N ANISOU 3201 N ALA C 178 4542 3473 2748 -398 277 -73 N ATOM 3202 CA ALA C 178 13.386 7.186 19.959 1.00 29.18 C ANISOU 3202 CA ALA C 178 4596 3654 2839 -378 269 -16 C ATOM 3203 C ALA C 178 12.986 6.290 18.806 1.00 32.74 C ANISOU 3203 C ALA C 178 5013 4084 3343 -324 298 26 C ATOM 3204 O ALA C 178 11.925 6.488 18.205 1.00 36.64 O ANISOU 3204 O ALA C 178 5531 4522 3869 -289 329 5 O ATOM 3205 CB ALA C 178 12.827 6.642 21.280 1.00 29.32 C ANISOU 3205 CB ALA C 178 4630 3712 2796 -362 278 -26 C ATOM 3206 N MET C 179 13.828 5.312 18.484 1.00 36.05 N ANISOU 3206 N MET C 179 5373 4548 3774 -317 289 81 N ATOM 3207 CA MET C 179 13.489 4.337 17.434 1.00 33.92 C ANISOU 3207 CA MET C 179 5071 4265 3554 -268 321 114 C ATOM 3208 C MET C 179 12.345 3.439 17.898 1.00 35.84 C ANISOU 3208 C MET C 179 5321 4504 3795 -217 355 114 C ATOM 3209 O MET C 179 12.261 3.095 19.071 1.00 39.53 O ANISOU 3209 O MET C 179 5796 5005 4219 -217 352 119 O ATOM 3210 CB MET C 179 14.699 3.466 17.094 1.00 39.20 C ANISOU 3210 CB MET C 179 5672 4982 4241 -271 308 168 C ATOM 3211 CG MET C 179 15.851 4.212 16.421 1.00 47.76 C ANISOU 3211 CG MET C 179 6736 6070 5340 -321 285 172 C ATOM 3212 SD MET C 179 15.587 4.535 14.652 1.00 48.37 S ANISOU 3212 SD MET C 179 6820 6092 5466 -312 318 169 S ATOM 3213 CE MET C 179 15.055 2.938 14.027 1.00 39.06 C ANISOU 3213 CE MET C 179 5602 4919 4321 -244 358 197 C ATOM 3214 N PRO C 180 11.457 3.051 16.973 1.00 40.64 N ANISOU 3214 N PRO C 180 5924 5071 4446 -177 389 109 N ATOM 3215 CA PRO C 180 10.403 2.106 17.344 1.00 39.68 C ANISOU 3215 CA PRO C 180 5799 4944 4332 -133 427 109 C ATOM 3216 C PRO C 180 11.027 0.754 17.638 1.00 31.05 C ANISOU 3216 C PRO C 180 4660 3893 3245 -117 433 164 C ATOM 3217 O PRO C 180 12.154 0.494 17.207 1.00 33.20 O ANISOU 3217 O PRO C 180 4895 4191 3530 -129 412 198 O ATOM 3218 CB PRO C 180 9.553 2.002 16.070 1.00 40.13 C ANISOU 3218 CB PRO C 180 5850 4956 4441 -101 451 91 C ATOM 3219 CG PRO C 180 10.007 3.097 15.187 1.00 47.77 C ANISOU 3219 CG PRO C 180 6835 5901 5415 -126 425 81 C ATOM 3220 CD PRO C 180 11.432 3.361 15.538 1.00 46.55 C ANISOU 3220 CD PRO C 180 6667 5784 5235 -171 394 107 C ATOM 3221 N ALA C 181 10.308 -0.088 18.359 1.00 32.57 N ANISOU 3221 N ALA C 181 4854 4090 3431 -90 464 174 N ATOM 3222 CA ALA C 181 10.767 -1.450 18.621 1.00 34.56 C ANISOU 3222 CA ALA C 181 5065 4367 3698 -68 476 232 C ATOM 3223 C ALA C 181 10.724 -2.257 17.327 1.00 34.90 C ANISOU 3223 C ALA C 181 5067 4382 3812 -39 502 240 C ATOM 3224 O ALA C 181 9.648 -2.453 16.746 1.00 26.58 O ANISOU 3224 O ALA C 181 4018 3289 2792 -18 536 208 O ATOM 3225 CB ALA C 181 9.900 -2.109 19.696 1.00 27.93 C ANISOU 3225 CB ALA C 181 4247 3531 2836 -49 511 242 C ATOM 3226 N LEU C 182 11.893 -2.708 16.871 1.00 31.23 N ANISOU 3226 N LEU C 182 4558 3938 3369 -41 486 279 N ATOM 3227 CA LEU C 182 12.005 -3.448 15.614 1.00 34.09 C ANISOU 3227 CA LEU C 182 4881 4277 3794 -19 513 280 C ATOM 3228 C LEU C 182 12.422 -4.887 15.883 1.00 32.51 C ANISOU 3228 C LEU C 182 4637 4082 3632 13 536 331 C ATOM 3229 O LEU C 182 13.159 -5.149 16.822 1.00 34.25 O ANISOU 3229 O LEU C 182 4845 4338 3830 13 512 380 O ATOM 3230 CB LEU C 182 13.055 -2.790 14.685 1.00 26.10 C ANISOU 3230 CB LEU C 182 3850 3280 2788 -46 488 277 C ATOM 3231 CG LEU C 182 12.820 -1.321 14.328 1.00 35.26 C ANISOU 3231 CG LEU C 182 5054 4427 3917 -79 465 236 C ATOM 3232 CD1 LEU C 182 13.926 -0.788 13.434 1.00 36.80 C ANISOU 3232 CD1 LEU C 182 5228 4636 4119 -110 448 242 C ATOM 3233 CD2 LEU C 182 11.452 -1.145 13.684 1.00 27.76 C ANISOU 3233 CD2 LEU C 182 4134 3433 2980 -59 489 192 C ATOM 3234 N ALA C 183 11.962 -5.816 15.055 1.00 29.21 N ANISOU 3234 N ALA C 183 4195 3629 3273 41 581 321 N ATOM 3235 CA ALA C 183 12.528 -7.166 15.063 1.00 32.66 C ANISOU 3235 CA ALA C 183 4585 4059 3764 72 606 367 C ATOM 3236 C ALA C 183 14.059 -7.103 14.946 1.00 36.68 C ANISOU 3236 C ALA C 183 5051 4607 4279 65 574 404 C ATOM 3237 O ALA C 183 14.597 -6.306 14.175 1.00 40.07 O ANISOU 3237 O ALA C 183 5473 5051 4699 39 555 379 O ATOM 3238 CB ALA C 183 11.944 -7.999 13.918 1.00 30.23 C ANISOU 3238 CB ALA C 183 4257 3706 3522 93 658 331 C ATOM 3239 N PRO C 184 14.762 -7.954 15.702 1.00 34.83 N ANISOU 3239 N PRO C 184 4784 4388 4063 90 567 468 N ATOM 3240 CA PRO C 184 16.231 -7.999 15.679 1.00 38.49 C ANISOU 3240 CA PRO C 184 5192 4892 4542 90 534 508 C ATOM 3241 C PRO C 184 16.741 -8.338 14.275 1.00 38.99 C ANISOU 3241 C PRO C 184 5209 4936 4671 97 568 481 C ATOM 3242 O PRO C 184 16.109 -9.141 13.580 1.00 36.32 O ANISOU 3242 O PRO C 184 4868 4551 4383 121 622 456 O ATOM 3243 CB PRO C 184 16.571 -9.158 16.625 1.00 41.38 C ANISOU 3243 CB PRO C 184 5531 5259 4933 132 534 584 C ATOM 3244 CG PRO C 184 15.307 -9.460 17.376 1.00 39.60 C ANISOU 3244 CG PRO C 184 5361 5004 4680 140 560 587 C ATOM 3245 CD PRO C 184 14.175 -9.045 16.501 1.00 36.44 C ANISOU 3245 CD PRO C 184 4994 4565 4286 123 598 509 C ATOM 3246 N PRO C 185 17.867 -7.738 13.860 1.00 41.82 N ANISOU 3246 N PRO C 185 5531 5333 5027 73 542 481 N ATOM 3247 CA PRO C 185 18.367 -7.994 12.503 1.00 46.44 C ANISOU 3247 CA PRO C 185 6075 5906 5665 75 581 451 C ATOM 3248 C PRO C 185 18.563 -9.479 12.247 1.00 43.98 C ANISOU 3248 C PRO C 185 5714 5560 5437 128 630 472 C ATOM 3249 O PRO C 185 19.079 -10.186 13.108 1.00 44.13 O ANISOU 3249 O PRO C 185 5698 5585 5483 161 615 533 O ATOM 3250 CB PRO C 185 19.721 -7.279 12.489 1.00 49.34 C ANISOU 3250 CB PRO C 185 6397 6327 6023 43 543 468 C ATOM 3251 CG PRO C 185 19.568 -6.179 13.478 1.00 47.82 C ANISOU 3251 CG PRO C 185 6250 6166 5754 5 483 473 C ATOM 3252 CD PRO C 185 18.686 -6.741 14.571 1.00 41.72 C ANISOU 3252 CD PRO C 185 5514 5377 4961 35 478 500 C ATOM 3253 N GLU C 186 18.159 -9.946 11.072 1.00 37.84 N ANISOU 3253 N GLU C 186 4934 4744 4699 136 687 421 N ATOM 3254 CA GLU C 186 18.362 -11.345 10.709 1.00 47.18 C ANISOU 3254 CA GLU C 186 6070 5886 5969 183 742 428 C ATOM 3255 C GLU C 186 19.692 -11.565 9.986 1.00 51.73 C ANISOU 3255 C GLU C 186 6575 6484 6598 190 761 429 C ATOM 3256 O GLU C 186 20.228 -12.678 9.969 1.00 52.72 O ANISOU 3256 O GLU C 186 6644 6582 6804 235 795 452 O ATOM 3257 CB GLU C 186 17.182 -11.864 9.892 1.00 58.13 C ANISOU 3257 CB GLU C 186 7490 7220 7377 187 797 365 C ATOM 3258 CG GLU C 186 15.935 -12.059 10.743 1.00 69.38 C ANISOU 3258 CG GLU C 186 8964 8614 8782 194 793 374 C ATOM 3259 CD GLU C 186 14.669 -12.169 9.923 1.00 79.69 C ANISOU 3259 CD GLU C 186 10306 9884 10089 183 829 302 C ATOM 3260 OE1 GLU C 186 14.717 -12.754 8.819 1.00 82.21 O ANISOU 3260 OE1 GLU C 186 10603 10181 10453 188 875 253 O ATOM 3261 OE2 GLU C 186 13.623 -11.671 10.394 1.00 81.71 O ANISOU 3261 OE2 GLU C 186 10608 10136 10299 168 811 290 O ATOM 3262 N VAL C 187 20.219 -10.492 9.402 1.00 41.06 N ANISOU 3262 N VAL C 187 5222 5177 5203 144 743 404 N ATOM 3263 CA VAL C 187 21.563 -10.483 8.842 1.00 48.25 C ANISOU 3263 CA VAL C 187 6061 6120 6153 140 757 407 C ATOM 3264 C VAL C 187 22.322 -9.274 9.382 1.00 50.88 C ANISOU 3264 C VAL C 187 6386 6514 6433 96 693 435 C ATOM 3265 O VAL C 187 21.718 -8.310 9.865 1.00 50.71 O ANISOU 3265 O VAL C 187 6427 6504 6338 60 648 431 O ATOM 3266 CB VAL C 187 21.531 -10.403 7.301 1.00 49.86 C ANISOU 3266 CB VAL C 187 6269 6317 6360 119 818 338 C ATOM 3267 CG1 VAL C 187 20.727 -11.557 6.728 1.00 49.59 C ANISOU 3267 CG1 VAL C 187 6245 6224 6372 155 879 297 C ATOM 3268 CG2 VAL C 187 20.938 -9.074 6.852 1.00 49.68 C ANISOU 3268 CG2 VAL C 187 6316 6314 6246 61 793 305 C ATOM 3269 N VAL C 188 23.646 -9.322 9.300 1.00 50.29 N ANISOU 3269 N VAL C 188 6231 6477 6401 96 690 457 N ATOM 3270 CA VAL C 188 24.463 -8.198 9.733 1.00 54.15 C ANISOU 3270 CA VAL C 188 6701 7024 6849 46 632 475 C ATOM 3271 C VAL C 188 24.725 -7.243 8.568 1.00 52.87 C ANISOU 3271 C VAL C 188 6552 6878 6659 -13 662 426 C ATOM 3272 O VAL C 188 25.078 -7.669 7.469 1.00 58.44 O ANISOU 3272 O VAL C 188 7224 7575 7404 -7 727 395 O ATOM 3273 CB VAL C 188 25.797 -8.667 10.335 1.00 56.53 C ANISOU 3273 CB VAL C 188 6900 7366 7213 73 604 528 C ATOM 3274 CG1 VAL C 188 26.735 -7.487 10.535 1.00 57.58 C ANISOU 3274 CG1 VAL C 188 7002 7563 7314 10 555 531 C ATOM 3275 CG2 VAL C 188 25.550 -9.382 11.650 1.00 59.69 C ANISOU 3275 CG2 VAL C 188 7300 7760 7620 123 558 591 C ATOM 3276 N MET C 189 24.513 -5.954 8.807 1.00 50.13 N ANISOU 3276 N MET C 189 6258 6548 6239 -71 618 419 N ATOM 3277 CA MET C 189 24.897 -4.930 7.848 1.00 45.02 C ANISOU 3277 CA MET C 189 5624 5918 5565 -133 639 387 C ATOM 3278 C MET C 189 26.334 -4.562 8.163 1.00 48.72 C ANISOU 3278 C MET C 189 6008 6441 6065 -164 614 412 C ATOM 3279 O MET C 189 26.607 -3.891 9.158 1.00 47.90 O ANISOU 3279 O MET C 189 5903 6365 5933 -193 547 434 O ATOM 3280 CB MET C 189 23.997 -3.694 7.977 1.00 44.48 C ANISOU 3280 CB MET C 189 5652 5834 5416 -179 604 370 C ATOM 3281 CG MET C 189 24.289 -2.594 6.957 1.00 41.43 C ANISOU 3281 CG MET C 189 5293 5453 4997 -242 627 346 C ATOM 3282 SD MET C 189 24.109 -3.170 5.259 1.00 49.77 S ANISOU 3282 SD MET C 189 6353 6493 6064 -230 716 308 S ATOM 3283 CE MET C 189 24.912 -1.867 4.324 1.00 53.18 C ANISOU 3283 CE MET C 189 6794 6948 6463 -313 739 303 C ATOM 3284 N ASP C 190 27.259 -5.029 7.334 1.00 58.03 N ANISOU 3284 N ASP C 190 7110 7636 7303 -159 670 403 N ATOM 3285 CA ASP C 190 28.670 -4.708 7.525 1.00 55.69 C ANISOU 3285 CA ASP C 190 6719 7394 7047 -190 653 422 C ATOM 3286 C ASP C 190 28.885 -3.201 7.611 1.00 46.39 C ANISOU 3286 C ASP C 190 5576 6238 5812 -277 617 413 C ATOM 3287 O ASP C 190 28.649 -2.483 6.643 1.00 46.69 O ANISOU 3287 O ASP C 190 5667 6260 5813 -324 659 384 O ATOM 3288 CB ASP C 190 29.514 -5.293 6.392 1.00 62.08 C ANISOU 3288 CB ASP C 190 7451 8213 7923 -181 737 400 C ATOM 3289 CG ASP C 190 30.996 -4.995 6.555 1.00 66.66 C ANISOU 3289 CG ASP C 190 7918 8851 8556 -213 726 417 C ATOM 3290 OD1 ASP C 190 31.394 -4.472 7.617 1.00 67.90 O ANISOU 3290 OD1 ASP C 190 8051 9044 8704 -235 645 447 O ATOM 3291 OD2 ASP C 190 31.764 -5.282 5.616 1.00 69.44 O ANISOU 3291 OD2 ASP C 190 8205 9219 8961 -217 799 395 O ATOM 3292 N PRO C 191 29.342 -2.719 8.778 1.00 52.10 N ANISOU 3292 N PRO C 191 6273 6998 6526 -300 538 439 N ATOM 3293 CA PRO C 191 29.619 -1.295 9.017 1.00 51.08 C ANISOU 3293 CA PRO C 191 6171 6886 6350 -386 499 427 C ATOM 3294 C PRO C 191 30.509 -0.670 7.937 1.00 58.15 C ANISOU 3294 C PRO C 191 7027 7797 7270 -450 555 407 C ATOM 3295 O PRO C 191 30.291 0.483 7.556 1.00 59.11 O ANISOU 3295 O PRO C 191 7215 7899 7346 -518 561 388 O ATOM 3296 CB PRO C 191 30.355 -1.307 10.358 1.00 54.36 C ANISOU 3296 CB PRO C 191 6518 7356 6779 -388 414 458 C ATOM 3297 CG PRO C 191 29.830 -2.522 11.055 1.00 55.86 C ANISOU 3297 CG PRO C 191 6705 7537 6980 -300 394 491 C ATOM 3298 CD PRO C 191 29.610 -3.545 9.971 1.00 55.93 C ANISOU 3298 CD PRO C 191 6701 7508 7041 -244 480 483 C ATOM 3299 N ALA C 192 31.501 -1.419 7.463 1.00 61.66 N ANISOU 3299 N ALA C 192 7365 8274 7790 -428 600 413 N ATOM 3300 CA ALA C 192 32.408 -0.938 6.422 1.00 62.79 C ANISOU 3300 CA ALA C 192 7461 8437 7961 -488 666 394 C ATOM 3301 C ALA C 192 31.678 -0.788 5.088 1.00 56.91 C ANISOU 3301 C ALA C 192 6803 7648 7173 -498 747 366 C ATOM 3302 O ALA C 192 31.812 0.222 4.397 1.00 54.85 O ANISOU 3302 O ALA C 192 6582 7382 6878 -571 778 354 O ATOM 3303 CB ALA C 192 33.602 -1.883 6.277 1.00 63.01 C ANISOU 3303 CB ALA C 192 7345 8509 8086 -452 698 403 C ATOM 3304 N LEU C 193 30.912 -1.813 4.735 1.00 58.91 N ANISOU 3304 N LEU C 193 7085 7872 7428 -425 780 358 N ATOM 3305 CA LEU C 193 30.040 -1.770 3.567 1.00 55.82 C ANISOU 3305 CA LEU C 193 6783 7442 6984 -426 843 330 C ATOM 3306 C LEU C 193 29.121 -0.553 3.631 1.00 51.38 C ANISOU 3306 C LEU C 193 6339 6847 6337 -474 804 330 C ATOM 3307 O LEU C 193 28.984 0.191 2.663 1.00 49.69 O ANISOU 3307 O LEU C 193 6181 6620 6077 -522 845 320 O ATOM 3308 CB LEU C 193 29.207 -3.050 3.505 1.00 55.35 C ANISOU 3308 CB LEU C 193 6739 7352 6940 -341 861 318 C ATOM 3309 CG LEU C 193 28.490 -3.364 2.196 1.00 57.00 C ANISOU 3309 CG LEU C 193 7011 7536 7112 -331 934 279 C ATOM 3310 CD1 LEU C 193 29.476 -3.395 1.033 1.00 58.85 C ANISOU 3310 CD1 LEU C 193 7190 7801 7368 -365 1022 257 C ATOM 3311 CD2 LEU C 193 27.754 -4.688 2.320 1.00 58.90 C ANISOU 3311 CD2 LEU C 193 7252 7743 7383 -250 946 265 C ATOM 3312 N ALA C 194 28.497 -0.348 4.787 1.00 54.37 N ANISOU 3312 N ALA C 194 6755 7210 6695 -457 725 344 N ATOM 3313 CA ALA C 194 27.576 0.767 4.970 1.00 49.73 C ANISOU 3313 CA ALA C 194 6275 6584 6037 -493 687 341 C ATOM 3314 C ALA C 194 28.278 2.101 4.729 1.00 50.68 C ANISOU 3314 C ALA C 194 6403 6711 6143 -583 688 344 C ATOM 3315 O ALA C 194 27.771 2.968 4.008 1.00 48.14 O ANISOU 3315 O ALA C 194 6165 6353 5772 -621 708 340 O ATOM 3316 CB ALA C 194 26.963 0.724 6.365 1.00 48.79 C ANISOU 3316 CB ALA C 194 6179 6455 5903 -463 608 351 C ATOM 3317 N ALA C 195 29.444 2.258 5.345 1.00 49.46 N ANISOU 3317 N ALA C 195 6158 6599 6034 -619 664 353 N ATOM 3318 CA ALA C 195 30.264 3.446 5.147 1.00 47.74 C ANISOU 3318 CA ALA C 195 5931 6391 5819 -712 670 353 C ATOM 3319 C ALA C 195 30.648 3.634 3.673 1.00 41.47 C ANISOU 3319 C ALA C 195 5139 5594 5022 -749 762 350 C ATOM 3320 O ALA C 195 30.610 4.744 3.155 1.00 41.51 O ANISOU 3320 O ALA C 195 5208 5572 4994 -817 781 354 O ATOM 3321 CB ALA C 195 31.514 3.380 6.026 1.00 50.90 C ANISOU 3321 CB ALA C 195 6212 6849 6278 -738 628 359 C ATOM 3322 N GLN C 196 31.012 2.547 3.002 1.00 48.60 N ANISOU 3322 N GLN C 196 5980 6526 5961 -704 823 343 N ATOM 3323 CA GLN C 196 31.376 2.616 1.586 1.00 51.34 C ANISOU 3323 CA GLN C 196 6330 6879 6298 -736 919 336 C ATOM 3324 C GLN C 196 30.200 3.104 0.723 1.00 49.06 C ANISOU 3324 C GLN C 196 6176 6542 5924 -739 939 336 C ATOM 3325 O GLN C 196 30.357 4.006 -0.101 1.00 46.43 O ANISOU 3325 O GLN C 196 5891 6197 5552 -804 981 346 O ATOM 3326 CB GLN C 196 31.884 1.256 1.097 1.00 51.84 C ANISOU 3326 CB GLN C 196 6303 6978 6416 -678 981 319 C ATOM 3327 CG GLN C 196 32.302 1.226 -0.370 1.00 53.65 C ANISOU 3327 CG GLN C 196 6531 7223 6632 -710 1089 303 C ATOM 3328 CD GLN C 196 33.529 2.074 -0.651 1.00 64.21 C ANISOU 3328 CD GLN C 196 7809 8592 7997 -801 1129 312 C ATOM 3329 OE1 GLN C 196 34.534 1.995 0.061 1.00 64.84 O ANISOU 3329 OE1 GLN C 196 7777 8709 8152 -814 1105 315 O ATOM 3330 NE2 GLN C 196 33.458 2.884 -1.703 1.00 67.78 N ANISOU 3330 NE2 GLN C 196 8333 9031 8388 -865 1189 317 N ATOM 3331 N TYR C 197 29.022 2.515 0.929 1.00 43.66 N ANISOU 3331 N TYR C 197 5549 5830 5211 -668 908 327 N ATOM 3332 CA TYR C 197 27.829 2.882 0.150 1.00 43.13 C ANISOU 3332 CA TYR C 197 5600 5722 5065 -660 916 326 C ATOM 3333 C TYR C 197 27.380 4.334 0.393 1.00 40.46 C ANISOU 3333 C TYR C 197 5351 5338 4683 -713 871 348 C ATOM 3334 O TYR C 197 26.924 5.024 -0.526 1.00 43.91 O ANISOU 3334 O TYR C 197 5872 5750 5063 -740 897 361 O ATOM 3335 CB TYR C 197 26.672 1.922 0.446 1.00 37.40 C ANISOU 3335 CB TYR C 197 4903 4977 4330 -575 888 308 C ATOM 3336 CG TYR C 197 26.865 0.509 -0.063 1.00 39.29 C ANISOU 3336 CG TYR C 197 5080 5242 4605 -521 944 280 C ATOM 3337 CD1 TYR C 197 27.721 0.245 -1.119 1.00 38.73 C ANISOU 3337 CD1 TYR C 197 4966 5207 4545 -546 1028 267 C ATOM 3338 CD2 TYR C 197 26.156 -0.552 0.487 1.00 46.46 C ANISOU 3338 CD2 TYR C 197 5979 6136 5538 -446 919 265 C ATOM 3339 CE1 TYR C 197 27.891 -1.039 -1.602 1.00 50.73 C ANISOU 3339 CE1 TYR C 197 6430 6743 6101 -496 1085 234 C ATOM 3340 CE2 TYR C 197 26.312 -1.846 0.008 1.00 52.27 C ANISOU 3340 CE2 TYR C 197 6661 6885 6314 -397 975 237 C ATOM 3341 CZ TYR C 197 27.185 -2.080 -1.041 1.00 55.79 C ANISOU 3341 CZ TYR C 197 7062 7363 6772 -421 1057 218 C ATOM 3342 OH TYR C 197 27.361 -3.353 -1.530 1.00 54.36 O ANISOU 3342 OH TYR C 197 6829 7190 6636 -373 1119 182 O ATOM 3343 N GLU C 198 27.504 4.782 1.637 1.00 43.86 N ANISOU 3343 N GLU C 198 5766 5760 5140 -726 804 352 N ATOM 3344 CA GLU C 198 27.143 6.143 2.017 1.00 36.75 C ANISOU 3344 CA GLU C 198 4943 4810 4211 -777 762 364 C ATOM 3345 C GLU C 198 28.078 7.110 1.313 1.00 47.93 C ANISOU 3345 C GLU C 198 6356 6226 5630 -867 810 382 C ATOM 3346 O GLU C 198 27.652 8.125 0.758 1.00 46.17 O ANISOU 3346 O GLU C 198 6223 5953 5365 -905 819 402 O ATOM 3347 CB GLU C 198 27.241 6.309 3.537 1.00 45.68 C ANISOU 3347 CB GLU C 198 6043 5942 5370 -777 686 354 C ATOM 3348 CG GLU C 198 26.109 5.589 4.283 1.00 51.00 C ANISOU 3348 CG GLU C 198 6746 6603 6029 -695 638 342 C ATOM 3349 CD GLU C 198 26.386 5.364 5.770 1.00 59.89 C ANISOU 3349 CD GLU C 198 7820 7754 7180 -685 573 335 C ATOM 3350 OE1 GLU C 198 27.456 5.789 6.258 1.00 55.87 O ANISOU 3350 OE1 GLU C 198 7251 7276 6702 -742 555 336 O ATOM 3351 OE2 GLU C 198 25.525 4.751 6.447 1.00 58.35 O ANISOU 3351 OE2 GLU C 198 7646 7551 6973 -623 540 329 O ATOM 3352 N HIS C 199 29.361 6.768 1.327 1.00 53.52 N ANISOU 3352 N HIS C 199 6957 6987 6391 -900 843 378 N ATOM 3353 CA HIS C 199 30.355 7.521 0.588 1.00 51.86 C ANISOU 3353 CA HIS C 199 6727 6785 6192 -988 904 393 C ATOM 3354 C HIS C 199 29.984 7.591 -0.889 1.00 51.18 C ANISOU 3354 C HIS C 199 6713 6687 6047 -992 979 410 C ATOM 3355 O HIS C 199 29.931 8.673 -1.468 1.00 48.85 O ANISOU 3355 O HIS C 199 6493 6353 5717 -1054 1002 438 O ATOM 3356 CB HIS C 199 31.732 6.884 0.750 1.00 57.45 C ANISOU 3356 CB HIS C 199 7293 7563 6974 -1007 934 380 C ATOM 3357 CG HIS C 199 32.852 7.756 0.281 1.00 70.99 C ANISOU 3357 CG HIS C 199 8970 9288 8716 -1109 988 391 C ATOM 3358 ND1 HIS C 199 33.476 7.581 -0.936 1.00 74.36 N ANISOU 3358 ND1 HIS C 199 9370 9743 9140 -1139 1088 397 N ATOM 3359 CD2 HIS C 199 33.451 8.823 0.861 1.00 74.93 C ANISOU 3359 CD2 HIS C 199 9455 9772 9244 -1194 959 393 C ATOM 3360 CE1 HIS C 199 34.416 8.495 -1.080 1.00 76.46 C ANISOU 3360 CE1 HIS C 199 9605 10010 9436 -1238 1121 407 C ATOM 3361 NE2 HIS C 199 34.422 9.263 -0.004 1.00 77.69 N ANISOU 3361 NE2 HIS C 199 9767 10139 9615 -1274 1043 404 N ATOM 3362 N ASP C 200 29.728 6.434 -1.496 1.00 50.41 N ANISOU 3362 N ASP C 200 6595 6622 5936 -928 1016 394 N ATOM 3363 CA ASP C 200 29.391 6.381 -2.917 1.00 48.55 C ANISOU 3363 CA ASP C 200 6423 6389 5634 -930 1087 403 C ATOM 3364 C ASP C 200 28.198 7.273 -3.251 1.00 51.92 C ANISOU 3364 C ASP C 200 6987 6755 5985 -928 1052 432 C ATOM 3365 O ASP C 200 28.158 7.885 -4.320 1.00 46.95 O ANISOU 3365 O ASP C 200 6426 6115 5298 -969 1100 462 O ATOM 3366 CB ASP C 200 29.102 4.948 -3.370 1.00 49.11 C ANISOU 3366 CB ASP C 200 6459 6498 5702 -853 1119 369 C ATOM 3367 CG ASP C 200 30.314 4.044 -3.271 1.00 57.57 C ANISOU 3367 CG ASP C 200 7397 7627 6852 -849 1170 344 C ATOM 3368 OD1 ASP C 200 31.448 4.537 -3.450 1.00 61.99 O ANISOU 3368 OD1 ASP C 200 7898 8210 7445 -919 1215 354 O ATOM 3369 OD2 ASP C 200 30.129 2.835 -3.012 1.00 62.24 O ANISOU 3369 OD2 ASP C 200 7936 8234 7477 -776 1166 314 O ATOM 3370 N LEU C 201 27.230 7.341 -2.337 1.00 49.65 N ANISOU 3370 N LEU C 201 6739 6428 5698 -880 969 425 N ATOM 3371 CA LEU C 201 26.018 8.132 -2.559 1.00 50.97 C ANISOU 3371 CA LEU C 201 7026 6534 5806 -865 929 448 C ATOM 3372 C LEU C 201 26.308 9.622 -2.572 1.00 53.83 C ANISOU 3372 C LEU C 201 7446 6843 6164 -944 927 487 C ATOM 3373 O LEU C 201 25.767 10.361 -3.390 1.00 56.12 O ANISOU 3373 O LEU C 201 7831 7094 6397 -958 938 525 O ATOM 3374 CB LEU C 201 24.938 7.815 -1.507 1.00 45.90 C ANISOU 3374 CB LEU C 201 6401 5864 5175 -795 849 425 C ATOM 3375 CG LEU C 201 24.041 6.614 -1.825 1.00 45.90 C ANISOU 3375 CG LEU C 201 6402 5886 5150 -712 847 398 C ATOM 3376 CD1 LEU C 201 22.998 6.399 -0.731 1.00 45.10 C ANISOU 3376 CD1 LEU C 201 6317 5754 5064 -651 774 379 C ATOM 3377 CD2 LEU C 201 23.360 6.792 -3.197 1.00 40.71 C ANISOU 3377 CD2 LEU C 201 5827 5225 4415 -705 876 416 C ATOM 3378 N GLU C 202 27.164 10.062 -1.659 1.00 59.77 N ANISOU 3378 N GLU C 202 8139 7592 6978 -996 910 479 N ATOM 3379 CA GLU C 202 27.488 11.478 -1.565 1.00 58.79 C ANISOU 3379 CA GLU C 202 8065 7410 6864 -1078 909 507 C ATOM 3380 C GLU C 202 28.296 11.923 -2.782 1.00 54.38 C ANISOU 3380 C GLU C 202 7515 6861 6284 -1151 996 545 C ATOM 3381 O GLU C 202 28.033 12.976 -3.361 1.00 54.21 O ANISOU 3381 O GLU C 202 7588 6781 6229 -1193 1011 589 O ATOM 3382 CB GLU C 202 28.232 11.785 -0.262 1.00 65.84 C ANISOU 3382 CB GLU C 202 8885 8304 7826 -1121 866 478 C ATOM 3383 CG GLU C 202 27.997 13.198 0.270 1.00 77.57 C ANISOU 3383 CG GLU C 202 10445 9706 9323 -1176 829 488 C ATOM 3384 CD GLU C 202 26.554 13.444 0.715 1.00 89.66 C ANISOU 3384 CD GLU C 202 12068 11175 10823 -1107 766 483 C ATOM 3385 OE1 GLU C 202 25.636 12.721 0.262 1.00 87.78 O ANISOU 3385 OE1 GLU C 202 11860 10950 10542 -1027 761 487 O ATOM 3386 OE2 GLU C 202 26.337 14.374 1.522 1.00 96.83 O ANISOU 3386 OE2 GLU C 202 13015 12022 11754 -1136 723 470 O ATOM 3387 N VAL C 203 29.269 11.109 -3.173 1.00 54.52 N ANISOU 3387 N VAL C 203 7437 6953 6323 -1165 1058 528 N ATOM 3388 CA VAL C 203 30.021 11.359 -4.399 1.00 55.42 C ANISOU 3388 CA VAL C 203 7554 7091 6411 -1230 1154 559 C ATOM 3389 C VAL C 203 29.079 11.600 -5.575 1.00 59.41 C ANISOU 3389 C VAL C 203 8183 7572 6819 -1206 1176 600 C ATOM 3390 O VAL C 203 29.112 12.656 -6.209 1.00 58.65 O ANISOU 3390 O VAL C 203 8167 7430 6687 -1266 1206 653 O ATOM 3391 CB VAL C 203 30.945 10.183 -4.750 1.00 54.82 C ANISOU 3391 CB VAL C 203 7361 7103 6365 -1220 1220 525 C ATOM 3392 CG1 VAL C 203 31.587 10.406 -6.126 1.00 49.59 C ANISOU 3392 CG1 VAL C 203 6714 6468 5659 -1282 1331 553 C ATOM 3393 CG2 VAL C 203 32.002 10.000 -3.674 1.00 56.03 C ANISOU 3393 CG2 VAL C 203 7384 7287 6616 -1248 1199 493 C ATOM 3394 N ALA C 204 28.232 10.616 -5.859 1.00 58.91 N ANISOU 3394 N ALA C 204 8133 7538 6712 -1119 1159 577 N ATOM 3395 CA ALA C 204 27.308 10.710 -6.984 1.00 63.56 C ANISOU 3395 CA ALA C 204 8829 8119 7203 -1091 1170 610 C ATOM 3396 C ALA C 204 26.417 11.944 -6.881 1.00 67.92 C ANISOU 3396 C ALA C 204 9497 8583 7726 -1094 1112 661 C ATOM 3397 O ALA C 204 26.069 12.556 -7.892 1.00 65.14 O ANISOU 3397 O ALA C 204 9239 8210 7299 -1112 1136 716 O ATOM 3398 CB ALA C 204 26.461 9.442 -7.087 1.00 57.56 C ANISOU 3398 CB ALA C 204 8056 7399 6415 -996 1145 564 C ATOM 3399 N GLN C 205 26.066 12.306 -5.651 1.00 68.87 N ANISOU 3399 N GLN C 205 9610 8652 7905 -1077 1038 643 N ATOM 3400 CA GLN C 205 25.128 13.391 -5.397 1.00 82.36 C ANISOU 3400 CA GLN C 205 11420 10270 9602 -1066 978 679 C ATOM 3401 C GLN C 205 25.681 14.738 -5.855 1.00 95.03 C ANISOU 3401 C GLN C 205 13087 11814 11205 -1156 1018 740 C ATOM 3402 O GLN C 205 24.964 15.739 -5.877 1.00 95.77 O ANISOU 3402 O GLN C 205 13276 11824 11287 -1153 982 783 O ATOM 3403 CB GLN C 205 24.765 13.438 -3.908 1.00 89.14 C ANISOU 3403 CB GLN C 205 12248 11093 10527 -1035 901 634 C ATOM 3404 CG GLN C 205 23.557 14.312 -3.578 1.00 93.79 C ANISOU 3404 CG GLN C 205 12934 11594 11108 -998 836 654 C ATOM 3405 CD GLN C 205 22.272 13.819 -4.228 1.00 95.73 C ANISOU 3405 CD GLN C 205 13236 11848 11288 -910 807 663 C ATOM 3406 OE1 GLN C 205 21.950 12.629 -4.182 1.00 95.43 O ANISOU 3406 OE1 GLN C 205 13148 11873 11240 -852 798 622 O ATOM 3407 NE2 GLN C 205 21.526 14.739 -4.831 1.00 94.88 N ANISOU 3407 NE2 GLN C 205 13231 11677 11143 -901 789 719 N ATOM 3408 N THR C 206 26.957 14.756 -6.228 1.00105.58 N ANISOU 3408 N THR C 206 14366 13190 12561 -1237 1096 746 N ATOM 3409 CA THR C 206 27.596 15.973 -6.718 1.00111.24 C ANISOU 3409 CA THR C 206 15134 13852 13280 -1334 1149 806 C ATOM 3410 C THR C 206 28.041 15.837 -8.175 1.00114.03 C ANISOU 3410 C THR C 206 15515 14255 13556 -1371 1242 852 C ATOM 3411 O THR C 206 29.156 16.216 -8.526 1.00116.12 O ANISOU 3411 O THR C 206 15747 14531 13843 -1463 1321 871 O ATOM 3412 CB THR C 206 28.817 16.351 -5.857 1.00113.13 C ANISOU 3412 CB THR C 206 15282 14086 13615 -1421 1167 775 C ATOM 3413 OG1 THR C 206 29.830 15.347 -5.993 1.00114.24 O ANISOU 3413 OG1 THR C 206 15302 14326 13777 -1437 1223 735 O ATOM 3414 CG2 THR C 206 28.420 16.470 -4.392 1.00112.00 C ANISOU 3414 CG2 THR C 206 15114 13905 13537 -1389 1075 724 C ATOM 3415 N THR C 207 27.165 15.302 -9.021 1.00115.22 N ANISOU 3415 N THR C 207 15725 14438 13616 -1302 1234 868 N ATOM 3416 CA THR C 207 27.482 15.086 -10.432 1.00116.68 C ANISOU 3416 CA THR C 207 15944 14680 13709 -1331 1320 906 C ATOM 3417 C THR C 207 26.199 14.981 -11.258 1.00117.36 C ANISOU 3417 C THR C 207 16136 14768 13687 -1257 1278 942 C ATOM 3418 O THR C 207 25.134 14.706 -10.713 1.00120.16 O ANISOU 3418 O THR C 207 16504 15102 14048 -1174 1190 917 O ATOM 3419 CB THR C 207 28.302 13.794 -10.624 1.00116.94 C ANISOU 3419 CB THR C 207 15860 14821 13753 -1329 1385 840 C ATOM 3420 OG1 THR C 207 29.320 13.711 -9.618 1.00113.93 O ANISOU 3420 OG1 THR C 207 15362 14444 13484 -1371 1394 794 O ATOM 3421 CG2 THR C 207 28.945 13.762 -12.004 1.00120.60 C ANISOU 3421 CG2 THR C 207 16348 15340 14134 -1387 1496 875 C ATOM 3422 N ALA C 208 26.292 15.192 -12.568 1.00113.38 N ANISOU 3422 N ALA C 208 15704 14293 13081 -1289 1341 1002 N ATOM 3423 CA ALA C 208 25.112 15.091 -13.430 1.00110.67 C ANISOU 3423 CA ALA C 208 15461 13965 12626 -1222 1297 1038 C ATOM 3424 C ALA C 208 25.191 13.913 -14.396 1.00108.60 C ANISOU 3424 C ALA C 208 15174 13817 12274 -1202 1350 996 C ATOM 3425 O ALA C 208 24.202 13.564 -15.040 1.00106.61 O ANISOU 3425 O ALA C 208 14982 13596 11929 -1141 1307 1002 O ATOM 3426 CB ALA C 208 24.887 16.387 -14.192 1.00111.69 C ANISOU 3426 CB ALA C 208 15720 14027 12691 -1262 1305 1152 C TER 3427 ALA C 208 ATOM 3428 N GLY D 723 -18.973 15.558 11.223 1.00116.71 N ANISOU 3428 N GLY D 723 10712 12961 20671 -605 3610 -3137 N ATOM 3429 CA GLY D 723 -17.543 15.472 10.991 1.00112.67 C ANISOU 3429 CA GLY D 723 10680 12668 19462 -576 3396 -2836 C ATOM 3430 C GLY D 723 -17.164 14.165 10.325 1.00111.04 C ANISOU 3430 C GLY D 723 10679 12686 18825 -512 2944 -2592 C ATOM 3431 O GLY D 723 -17.980 13.248 10.232 1.00114.15 O ANISOU 3431 O GLY D 723 10899 13100 19373 -560 2857 -2673 O ATOM 3432 N THR D 724 -15.922 14.078 9.859 1.00102.79 N ANISOU 3432 N THR D 724 10003 11804 17247 -414 2677 -2306 N ATOM 3433 CA THR D 724 -15.444 12.884 9.169 1.00 95.03 C ANISOU 3433 CA THR D 724 9236 11013 15860 -348 2269 -2064 C ATOM 3434 C THR D 724 -15.438 11.659 10.078 1.00 84.96 C ANISOU 3434 C THR D 724 8124 9897 14258 -696 2448 -2157 C ATOM 3435 O THR D 724 -15.709 11.756 11.276 1.00 86.27 O ANISOU 3435 O THR D 724 8289 10035 14454 -1027 2886 -2404 O ATOM 3436 CB THR D 724 -14.024 13.086 8.622 1.00 95.78 C ANISOU 3436 CB THR D 724 9698 11229 15465 -219 2029 -1785 C ATOM 3437 OG1 THR D 724 -13.087 13.050 9.706 1.00 98.08 O ANISOU 3437 OG1 THR D 724 10293 11657 15315 -509 2329 -1807 O ATOM 3438 CG2 THR D 724 -13.916 14.422 7.902 1.00 96.57 C ANISOU 3438 CG2 THR D 724 9715 11165 15812 61 1915 -1726 C ATOM 3439 N TRP D 725 -15.127 10.505 9.496 1.00 72.31 N ANISOU 3439 N TRP D 725 6687 8447 12339 -645 2113 -1961 N ATOM 3440 CA TRP D 725 -15.043 9.259 10.249 1.00 64.38 C ANISOU 3440 CA TRP D 725 5882 7594 10984 -952 2214 -2009 C ATOM 3441 C TRP D 725 -13.975 8.339 9.662 1.00 59.53 C ANISOU 3441 C TRP D 725 5596 7153 9871 -871 1868 -1705 C ATOM 3442 O TRP D 725 -13.715 8.369 8.460 1.00 55.56 O ANISOU 3442 O TRP D 725 5089 6641 9379 -577 1517 -1495 O ATOM 3443 CB TRP D 725 -16.400 8.553 10.286 1.00 61.88 C ANISOU 3443 CB TRP D 725 5289 7233 10991 -1029 2257 -2212 C ATOM 3444 CG TRP D 725 -16.960 8.212 8.935 1.00 65.74 C ANISOU 3444 CG TRP D 725 5578 7698 11702 -714 1837 -2055 C ATOM 3445 CD1 TRP D 725 -17.668 9.036 8.111 1.00 67.86 C ANISOU 3445 CD1 TRP D 725 5506 7792 12487 -439 1674 -2051 C ATOM 3446 CD2 TRP D 725 -16.873 6.948 8.257 1.00 62.55 C ANISOU 3446 CD2 TRP D 725 5322 7433 11012 -676 1522 -1869 C ATOM 3447 NE1 TRP D 725 -18.022 8.370 6.961 1.00 61.84 N ANISOU 3447 NE1 TRP D 725 4684 7055 11756 -257 1259 -1862 N ATOM 3448 CE2 TRP D 725 -17.549 7.087 7.027 1.00 60.84 C ANISOU 3448 CE2 TRP D 725 4857 7124 11135 -402 1185 -1756 C ATOM 3449 CE3 TRP D 725 -16.284 5.721 8.567 1.00 59.77 C ANISOU 3449 CE3 TRP D 725 5297 7258 10156 -858 1489 -1778 C ATOM 3450 CZ2 TRP D 725 -17.651 6.044 6.106 1.00 60.62 C ANISOU 3450 CZ2 TRP D 725 4917 7186 10930 -333 851 -1561 C ATOM 3451 CZ3 TRP D 725 -16.391 4.683 7.652 1.00 62.73 C ANISOU 3451 CZ3 TRP D 725 5738 7715 10381 -756 1172 -1596 C ATOM 3452 CH2 TRP D 725 -17.068 4.853 6.435 1.00 59.61 C ANISOU 3452 CH2 TRP D 725 5109 7236 10304 -510 873 -1492 C ATOM 3453 N ASP D 726 -13.353 7.527 10.511 1.00 56.50 N ANISOU 3453 N ASP D 726 5504 6901 9065 -1154 1971 -1686 N ATOM 3454 CA ASP D 726 -12.295 6.625 10.063 1.00 56.83 C ANISOU 3454 CA ASP D 726 5839 7081 8674 -1092 1678 -1412 C ATOM 3455 C ASP D 726 -12.824 5.205 9.848 1.00 51.07 C ANISOU 3455 C ASP D 726 5134 6424 7846 -1153 1533 -1396 C ATOM 3456 O ASP D 726 -13.550 4.673 10.686 1.00 46.96 O ANISOU 3456 O ASP D 726 4591 5912 7339 -1428 1743 -1602 O ATOM 3457 CB ASP D 726 -11.127 6.622 11.059 1.00 63.00 C ANISOU 3457 CB ASP D 726 6938 7949 9049 -1341 1814 -1344 C ATOM 3458 CG ASP D 726 -10.327 7.929 11.041 1.00 78.15 C ANISOU 3458 CG ASP D 726 8897 9837 10960 -1240 1889 -1285 C ATOM 3459 OD1 ASP D 726 -10.620 8.814 10.207 1.00 79.50 O ANISOU 3459 OD1 ASP D 726 8875 9912 11419 -961 1815 -1288 O ATOM 3460 OD2 ASP D 726 -9.397 8.071 11.865 1.00 81.33 O ANISOU 3460 OD2 ASP D 726 9540 10307 11055 -1457 2007 -1227 O ATOM 3461 N CYS D 727 -12.467 4.597 8.719 1.00 46.14 N ANISOU 3461 N CYS D 727 4577 5841 7112 -925 1196 -1166 N ATOM 3462 CA CYS D 727 -12.855 3.218 8.448 1.00 40.91 C ANISOU 3462 CA CYS D 727 3980 5254 6308 -982 1061 -1121 C ATOM 3463 C CYS D 727 -12.165 2.282 9.434 1.00 43.68 C ANISOU 3463 C CYS D 727 4637 5707 6252 -1258 1144 -1092 C ATOM 3464 O CYS D 727 -10.942 2.333 9.601 1.00 45.72 O ANISOU 3464 O CYS D 727 5114 6001 6256 -1256 1080 -924 O ATOM 3465 CB CYS D 727 -12.491 2.813 7.013 1.00 32.42 C ANISOU 3465 CB CYS D 727 2960 4181 5178 -716 715 -868 C ATOM 3466 SG CYS D 727 -12.906 1.113 6.648 1.00 41.16 S ANISOU 3466 SG CYS D 727 4182 5380 6077 -801 581 -794 S ATOM 3467 N ASP D 728 -12.955 1.424 10.068 1.00 45.38 N ANISOU 3467 N ASP D 728 4870 5959 6415 -1503 1267 -1257 N ATOM 3468 CA ASP D 728 -12.464 0.479 11.059 1.00 54.38 C ANISOU 3468 CA ASP D 728 6317 7168 7175 -1811 1325 -1249 C ATOM 3469 C ASP D 728 -11.754 -0.702 10.403 1.00 57.91 C ANISOU 3469 C ASP D 728 6976 7686 7342 -1695 1044 -985 C ATOM 3470 O ASP D 728 -11.105 -1.492 11.083 1.00 58.29 O ANISOU 3470 O ASP D 728 7297 7774 7077 -1893 1014 -906 O ATOM 3471 CB ASP D 728 -13.630 -0.024 11.922 1.00 63.48 C ANISOU 3471 CB ASP D 728 7438 8319 8362 -2139 1566 -1552 C ATOM 3472 CG ASP D 728 -13.208 -1.095 12.912 1.00 72.66 C ANISOU 3472 CG ASP D 728 8965 9536 9106 -2493 1588 -1545 C ATOM 3473 OD1 ASP D 728 -12.380 -0.799 13.797 1.00 75.53 O ANISOU 3473 OD1 ASP D 728 9544 9883 9272 -2707 1657 -1500 O ATOM 3474 OD2 ASP D 728 -13.710 -2.235 12.807 1.00 78.62 O ANISOU 3474 OD2 ASP D 728 9807 10345 9719 -2573 1523 -1576 O ATOM 3475 N THR D 729 -11.885 -0.822 9.083 1.00 48.33 N ANISOU 3475 N THR D 729 5646 6465 6253 -1398 838 -848 N ATOM 3476 CA THR D 729 -11.262 -1.921 8.345 1.00 45.70 C ANISOU 3476 CA THR D 729 5501 6170 5692 -1294 614 -614 C ATOM 3477 C THR D 729 -9.881 -1.541 7.801 1.00 41.97 C ANISOU 3477 C THR D 729 5135 5665 5148 -1098 464 -380 C ATOM 3478 O THR D 729 -8.918 -2.282 7.989 1.00 46.04 O ANISOU 3478 O THR D 729 5866 6196 5431 -1138 380 -225 O ATOM 3479 CB THR D 729 -12.164 -2.430 7.187 1.00 52.56 C ANISOU 3479 CB THR D 729 6243 7043 6686 -1153 488 -588 C ATOM 3480 OG1 THR D 729 -13.402 -2.915 7.717 1.00 46.58 O ANISOU 3480 OG1 THR D 729 5395 6330 5973 -1350 630 -813 O ATOM 3481 CG2 THR D 729 -11.487 -3.566 6.418 1.00 53.35 C ANISOU 3481 CG2 THR D 729 6563 7161 6545 -1079 309 -352 C ATOM 3482 N CYS D 730 -9.785 -0.381 7.156 1.00 37.12 N ANISOU 3482 N CYS D 730 4367 4990 4748 -897 432 -369 N ATOM 3483 CA CYS D 730 -8.551 0.013 6.453 1.00 37.93 C ANISOU 3483 CA CYS D 730 4566 5051 4793 -708 293 -179 C ATOM 3484 C CYS D 730 -7.949 1.331 6.964 1.00 36.29 C ANISOU 3484 C CYS D 730 4326 4827 4636 -691 396 -223 C ATOM 3485 O CYS D 730 -6.876 1.750 6.525 1.00 36.18 O ANISOU 3485 O CYS D 730 4399 4790 4557 -562 311 -97 O ATOM 3486 CB CYS D 730 -8.805 0.095 4.942 1.00 32.81 C ANISOU 3486 CB CYS D 730 3854 4330 4280 -492 111 -87 C ATOM 3487 SG CYS D 730 -9.615 1.613 4.387 1.00 34.89 S ANISOU 3487 SG CYS D 730 3859 4501 4897 -339 93 -196 S ATOM 3488 N LEU D 731 -8.651 1.969 7.899 1.00 37.61 N ANISOU 3488 N LEU D 731 4375 4999 4915 -844 607 -418 N ATOM 3489 CA LEU D 731 -8.191 3.187 8.575 1.00 34.70 C ANISOU 3489 CA LEU D 731 3995 4618 4572 -895 770 -483 C ATOM 3490 C LEU D 731 -8.245 4.482 7.752 1.00 41.32 C ANISOU 3490 C LEU D 731 4683 5375 5641 -651 740 -497 C ATOM 3491 O LEU D 731 -7.841 5.543 8.235 1.00 43.68 O ANISOU 3491 O LEU D 731 4985 5663 5949 -679 886 -547 O ATOM 3492 CB LEU D 731 -6.799 2.993 9.189 1.00 35.12 C ANISOU 3492 CB LEU D 731 4286 4728 4329 -1002 744 -332 C ATOM 3493 CG LEU D 731 -6.629 1.785 10.116 1.00 44.51 C ANISOU 3493 CG LEU D 731 5660 5970 5281 -1271 739 -294 C ATOM 3494 CD1 LEU D 731 -5.252 1.791 10.763 1.00 44.40 C ANISOU 3494 CD1 LEU D 731 5847 5990 5035 -1381 685 -130 C ATOM 3495 CD2 LEU D 731 -7.725 1.769 11.182 1.00 48.95 C ANISOU 3495 CD2 LEU D 731 6186 6531 5880 -1578 980 -531 C ATOM 3496 N VAL D 732 -8.747 4.402 6.524 1.00 39.87 N ANISOU 3496 N VAL D 732 4395 5127 5627 -441 546 -448 N ATOM 3497 CA VAL D 732 -8.886 5.589 5.674 1.00 42.57 C ANISOU 3497 CA VAL D 732 4618 5363 6194 -226 464 -452 C ATOM 3498 C VAL D 732 -9.913 6.576 6.270 1.00 48.20 C ANISOU 3498 C VAL D 732 5075 6004 7233 -263 674 -666 C ATOM 3499 O VAL D 732 -10.953 6.164 6.786 1.00 48.78 O ANISOU 3499 O VAL D 732 4988 6078 7468 -391 797 -816 O ATOM 3500 CB VAL D 732 -9.228 5.184 4.195 1.00 41.56 C ANISOU 3500 CB VAL D 732 4476 5159 6157 -53 169 -329 C ATOM 3501 CG1 VAL D 732 -10.016 6.256 3.493 1.00 51.55 C ANISOU 3501 CG1 VAL D 732 5541 6285 7762 104 69 -380 C ATOM 3502 CG2 VAL D 732 -7.948 4.876 3.416 1.00 36.84 C ANISOU 3502 CG2 VAL D 732 4133 4561 5303 23 12 -146 C ATOM 3503 N GLN D 733 -9.597 7.870 6.239 1.00 47.42 N ANISOU 3503 N GLN D 733 4947 5838 7232 -166 742 -698 N ATOM 3504 CA GLN D 733 -10.526 8.912 6.681 1.00 54.82 C ANISOU 3504 CA GLN D 733 5628 6666 8534 -169 950 -897 C ATOM 3505 C GLN D 733 -11.611 9.116 5.632 1.00 49.77 C ANISOU 3505 C GLN D 733 4734 5884 8291 34 726 -902 C ATOM 3506 O GLN D 733 -11.312 9.290 4.454 1.00 52.44 O ANISOU 3506 O GLN D 733 5147 6161 8616 224 425 -742 O ATOM 3507 CB GLN D 733 -9.782 10.233 6.915 1.00 69.36 C ANISOU 3507 CB GLN D 733 7548 8474 10330 -125 1088 -910 C ATOM 3508 CG GLN D 733 -9.190 10.852 5.643 1.00 85.05 C ANISOU 3508 CG GLN D 733 9633 10392 12288 136 803 -759 C ATOM 3509 CD GLN D 733 -8.239 12.014 5.913 1.00 98.15 C ANISOU 3509 CD GLN D 733 11445 12060 13787 153 945 -763 C ATOM 3510 OE1 GLN D 733 -7.659 12.126 6.995 1.00101.62 O ANISOU 3510 OE1 GLN D 733 11994 12604 14011 -45 1209 -806 O ATOM 3511 NE2 GLN D 733 -8.069 12.879 4.917 1.00102.36 N ANISOU 3511 NE2 GLN D 733 12012 12481 14401 363 756 -711 N ATOM 3512 N ASN D 734 -12.873 9.077 6.048 1.00 43.35 N ANISOU 3512 N ASN D 734 3628 5005 7838 -32 864 -1088 N ATOM 3513 CA ASN D 734 -13.971 9.261 5.099 1.00 51.48 C ANISOU 3513 CA ASN D 734 4375 5889 9295 150 625 -1084 C ATOM 3514 C ASN D 734 -14.833 10.494 5.367 1.00 62.90 C ANISOU 3514 C ASN D 734 5484 7147 11268 228 786 -1271 C ATOM 3515 O ASN D 734 -14.876 11.008 6.486 1.00 68.68 O ANISOU 3515 O ASN D 734 6156 7866 12071 75 1177 -1473 O ATOM 3516 CB ASN D 734 -14.864 8.022 5.041 1.00 46.87 C ANISOU 3516 CB ASN D 734 3678 5367 8762 49 559 -1118 C ATOM 3517 CG ASN D 734 -14.235 6.883 4.264 1.00 49.12 C ANISOU 3517 CG ASN D 734 4244 5767 8651 56 289 -884 C ATOM 3518 OD1 ASN D 734 -14.452 6.745 3.058 1.00 49.07 O ANISOU 3518 OD1 ASN D 734 4233 5694 8717 192 -42 -721 O ATOM 3519 ND2 ASN D 734 -13.446 6.064 4.949 1.00 49.75 N ANISOU 3519 ND2 ASN D 734 4581 6000 8321 -113 427 -863 N ATOM 3520 N LYS D 735 -15.516 10.953 4.322 1.00 70.02 N ANISOU 3520 N LYS D 735 6175 7881 12548 447 476 -1195 N ATOM 3521 CA LYS D 735 -16.514 12.016 4.427 1.00 80.29 C ANISOU 3521 CA LYS D 735 7086 8959 14461 556 563 -1358 C ATOM 3522 C LYS D 735 -17.667 11.602 5.335 1.00 81.53 C ANISOU 3522 C LYS D 735 6909 9100 14968 387 873 -1635 C ATOM 3523 O LYS D 735 -18.034 10.427 5.377 1.00 81.64 O ANISOU 3523 O LYS D 735 6933 9240 14847 260 829 -1642 O ATOM 3524 CB LYS D 735 -17.081 12.325 3.042 1.00 89.64 C ANISOU 3524 CB LYS D 735 8121 9965 15972 795 74 -1178 C ATOM 3525 CG LYS D 735 -16.063 12.788 2.015 1.00 94.22 C ANISOU 3525 CG LYS D 735 9042 10514 16244 933 -256 -931 C ATOM 3526 CD LYS D 735 -15.990 14.304 1.965 1.00106.24 C ANISOU 3526 CD LYS D 735 10483 11834 18049 1094 -227 -975 C ATOM 3527 CE LYS D 735 -15.489 14.788 0.612 1.00109.92 C ANISOU 3527 CE LYS D 735 11194 12178 18393 1245 -694 -734 C ATOM 3528 NZ LYS D 735 -15.772 16.236 0.401 1.00111.33 N ANISOU 3528 NZ LYS D 735 11225 12101 18975 1426 -759 -769 N ATOM 3529 N PRO D 736 -18.256 12.571 6.055 1.00 84.83 N ANISOU 3529 N PRO D 736 7036 9349 15845 369 1208 -1881 N ATOM 3530 CA PRO D 736 -19.435 12.320 6.894 1.00 84.56 C ANISOU 3530 CA PRO D 736 6645 9246 16236 194 1543 -2198 C ATOM 3531 C PRO D 736 -20.628 11.923 6.033 1.00 83.89 C ANISOU 3531 C PRO D 736 6193 9062 16621 346 1203 -2167 C ATOM 3532 O PRO D 736 -21.533 11.224 6.491 1.00 85.57 O ANISOU 3532 O PRO D 736 6183 9298 17033 185 1368 -2375 O ATOM 3533 CB PRO D 736 -19.702 13.680 7.549 1.00 93.42 C ANISOU 3533 CB PRO D 736 7535 10147 17813 205 1920 -2423 C ATOM 3534 CG PRO D 736 -18.430 14.455 7.391 1.00 94.57 C ANISOU 3534 CG PRO D 736 8035 10333 17565 294 1880 -2238 C ATOM 3535 CD PRO D 736 -17.816 13.974 6.119 1.00 90.81 C ANISOU 3535 CD PRO D 736 7802 9958 16743 495 1322 -1892 C ATOM 3536 N GLU D 737 -20.609 12.372 4.783 1.00 83.76 N ANISOU 3536 N GLU D 737 6138 8928 16757 627 720 -1905 N ATOM 3537 CA GLU D 737 -21.675 12.093 3.828 1.00 90.89 C ANISOU 3537 CA GLU D 737 6718 9716 18099 770 311 -1810 C ATOM 3538 C GLU D 737 -21.551 10.695 3.207 1.00 84.84 C ANISOU 3538 C GLU D 737 6194 9167 16875 680 19 -1611 C ATOM 3539 O GLU D 737 -22.483 10.207 2.566 1.00 86.84 O ANISOU 3539 O GLU D 737 6206 9377 17410 716 -265 -1552 O ATOM 3540 CB GLU D 737 -21.672 13.164 2.734 1.00 95.98 C ANISOU 3540 CB GLU D 737 7281 10122 19063 1059 -121 -1589 C ATOM 3541 CG GLU D 737 -20.297 13.384 2.118 1.00 99.43 C ANISOU 3541 CG GLU D 737 8232 10643 18902 1119 -338 -1323 C ATOM 3542 CD GLU D 737 -20.061 14.816 1.665 1.00105.97 C ANISOU 3542 CD GLU D 737 9039 11230 19995 1336 -488 -1249 C ATOM 3543 OE1 GLU D 737 -21.014 15.624 1.697 1.00111.83 O ANISOU 3543 OE1 GLU D 737 9347 11714 21431 1471 -494 -1362 O ATOM 3544 OE2 GLU D 737 -18.916 15.132 1.276 1.00102.91 O ANISOU 3544 OE2 GLU D 737 9069 10901 19132 1367 -595 -1088 O ATOM 3545 N ALA D 738 -20.401 10.055 3.403 1.00 75.14 N ANISOU 3545 N ALA D 738 5433 8160 14956 556 94 -1506 N ATOM 3546 CA ALA D 738 -20.152 8.723 2.850 1.00 70.85 C ANISOU 3546 CA ALA D 738 5160 7812 13949 463 -134 -1318 C ATOM 3547 C ALA D 738 -20.794 7.631 3.706 1.00 69.13 C ANISOU 3547 C ALA D 738 4854 7744 13666 224 153 -1540 C ATOM 3548 O ALA D 738 -20.678 7.643 4.929 1.00 69.83 O ANISOU 3548 O ALA D 738 4963 7888 13681 39 591 -1791 O ATOM 3549 CB ALA D 738 -18.645 8.476 2.705 1.00 59.42 C ANISOU 3549 CB ALA D 738 4221 6509 11848 436 -167 -1124 C ATOM 3550 N VAL D 739 -21.472 6.689 3.062 1.00 67.54 N ANISOU 3550 N VAL D 739 4588 7605 13469 193 -93 -1449 N ATOM 3551 CA VAL D 739 -22.139 5.611 3.784 1.00 66.48 C ANISOU 3551 CA VAL D 739 4389 7616 13252 -40 154 -1664 C ATOM 3552 C VAL D 739 -21.255 4.360 3.868 1.00 64.96 C ANISOU 3552 C VAL D 739 4674 7663 12347 -202 167 -1531 C ATOM 3553 O VAL D 739 -21.514 3.447 4.655 1.00 63.17 O ANISOU 3553 O VAL D 739 4517 7574 11909 -433 419 -1712 O ATOM 3554 CB VAL D 739 -23.507 5.274 3.156 1.00 68.84 C ANISOU 3554 CB VAL D 739 4308 7856 13995 -7 -74 -1683 C ATOM 3555 CG1 VAL D 739 -23.329 4.530 1.841 1.00 59.76 C ANISOU 3555 CG1 VAL D 739 3385 6779 12542 42 -542 -1321 C ATOM 3556 CG2 VAL D 739 -24.343 4.466 4.124 1.00 77.62 C ANISOU 3556 CG2 VAL D 739 5269 9074 15148 -258 285 -2018 C ATOM 3557 N LYS D 740 -20.210 4.324 3.051 1.00 58.35 N ANISOU 3557 N LYS D 740 4167 6852 11151 -92 -99 -1225 N ATOM 3558 CA LYS D 740 -19.225 3.259 3.140 1.00 61.64 C ANISOU 3558 CA LYS D 740 5020 7454 10946 -217 -72 -1094 C ATOM 3559 C LYS D 740 -17.852 3.784 2.748 1.00 52.92 C ANISOU 3559 C LYS D 740 4217 6323 9565 -96 -181 -886 C ATOM 3560 O LYS D 740 -17.742 4.843 2.134 1.00 54.21 O ANISOU 3560 O LYS D 740 4292 6334 9970 84 -357 -800 O ATOM 3561 CB LYS D 740 -19.628 2.048 2.289 1.00 67.24 C ANISOU 3561 CB LYS D 740 5829 8257 11461 -275 -310 -929 C ATOM 3562 CG LYS D 740 -19.803 2.326 0.808 1.00 69.11 C ANISOU 3562 CG LYS D 740 6041 8375 11843 -125 -745 -657 C ATOM 3563 CD LYS D 740 -20.682 1.265 0.176 1.00 74.77 C ANISOU 3563 CD LYS D 740 6720 9166 12522 -234 -917 -576 C ATOM 3564 CE LYS D 740 -20.952 1.550 -1.295 1.00 81.60 C ANISOU 3564 CE LYS D 740 7572 9891 13540 -148 -1373 -293 C ATOM 3565 NZ LYS D 740 -19.819 1.140 -2.168 1.00 81.03 N ANISOU 3565 NZ LYS D 740 7960 9828 12998 -177 -1535 -18 N ATOM 3566 N CYS D 741 -16.812 3.044 3.119 1.00 50.89 N ANISOU 3566 N CYS D 741 4314 6205 8817 -203 -79 -814 N ATOM 3567 CA CYS D 741 -15.434 3.484 2.905 1.00 49.61 C ANISOU 3567 CA CYS D 741 4431 6032 8388 -116 -130 -655 C ATOM 3568 C CYS D 741 -15.091 3.606 1.420 1.00 51.25 C ANISOU 3568 C CYS D 741 4767 6147 8559 30 -493 -399 C ATOM 3569 O CYS D 741 -15.262 2.661 0.655 1.00 56.85 O ANISOU 3569 O CYS D 741 5593 6889 9118 -21 -668 -257 O ATOM 3570 CB CYS D 741 -14.449 2.530 3.580 1.00 37.04 C ANISOU 3570 CB CYS D 741 3157 4591 6325 -268 20 -619 C ATOM 3571 SG CYS D 741 -12.709 3.042 3.386 1.00 40.96 S ANISOU 3571 SG CYS D 741 3959 5078 6527 -170 -25 -444 S ATOM 3572 N VAL D 742 -14.589 4.774 1.033 1.00 54.25 N ANISOU 3572 N VAL D 742 5160 6403 9051 177 -587 -349 N ATOM 3573 CA VAL D 742 -14.217 5.054 -0.352 1.00 52.02 C ANISOU 3573 CA VAL D 742 5043 5997 8726 273 -925 -132 C ATOM 3574 C VAL D 742 -13.127 4.114 -0.885 1.00 54.81 C ANISOU 3574 C VAL D 742 5778 6420 8626 196 -976 36 C ATOM 3575 O VAL D 742 -12.966 3.966 -2.100 1.00 53.51 O ANISOU 3575 O VAL D 742 5790 6159 8384 188 -1235 209 O ATOM 3576 CB VAL D 742 -13.769 6.535 -0.524 1.00 59.60 C ANISOU 3576 CB VAL D 742 5991 6814 9842 425 -976 -144 C ATOM 3577 CG1 VAL D 742 -12.443 6.793 0.188 1.00 50.05 C ANISOU 3577 CG1 VAL D 742 5004 5697 8314 413 -735 -184 C ATOM 3578 CG2 VAL D 742 -13.665 6.897 -1.997 1.00 64.48 C ANISOU 3578 CG2 VAL D 742 6764 7261 10476 484 -1364 54 C ATOM 3579 N ALA D 743 -12.388 3.472 0.018 1.00 45.08 N ANISOU 3579 N ALA D 743 4680 5334 7114 114 -730 -15 N ATOM 3580 CA ALA D 743 -11.298 2.592 -0.387 1.00 43.92 C ANISOU 3580 CA ALA D 743 4856 5231 6599 56 -748 128 C ATOM 3581 C ALA D 743 -11.696 1.120 -0.408 1.00 52.27 C ANISOU 3581 C ALA D 743 5982 6385 7495 -80 -727 176 C ATOM 3582 O ALA D 743 -11.569 0.453 -1.438 1.00 57.42 O ANISOU 3582 O ALA D 743 6814 6988 8016 -129 -875 330 O ATOM 3583 CB ALA D 743 -10.072 2.800 0.507 1.00 39.84 C ANISOU 3583 CB ALA D 743 4469 4789 5881 57 -545 85 C ATOM 3584 N CYS D 744 -12.169 0.612 0.728 1.00 44.16 N ANISOU 3584 N CYS D 744 4841 5483 6456 -172 -527 37 N ATOM 3585 CA CYS D 744 -12.421 -0.819 0.863 1.00 42.63 C ANISOU 3585 CA CYS D 744 4755 5393 6048 -314 -477 67 C ATOM 3586 C CYS D 744 -13.897 -1.223 0.798 1.00 42.78 C ANISOU 3586 C CYS D 744 4566 5450 6237 -390 -506 -18 C ATOM 3587 O CYS D 744 -14.209 -2.413 0.800 1.00 49.46 O ANISOU 3587 O CYS D 744 5515 6385 6891 -516 -472 6 O ATOM 3588 CB CYS D 744 -11.808 -1.340 2.161 1.00 46.49 C ANISOU 3588 CB CYS D 744 5349 5993 6322 -419 -254 -15 C ATOM 3589 SG CYS D 744 -12.652 -0.762 3.657 1.00 41.91 S ANISOU 3589 SG CYS D 744 4526 5472 5926 -530 -11 -300 S ATOM 3590 N GLU D 745 -14.794 -0.241 0.772 1.00 43.21 N ANISOU 3590 N GLU D 745 4321 5432 6664 -315 -558 -124 N ATOM 3591 CA GLU D 745 -16.234 -0.501 0.665 1.00 50.36 C ANISOU 3591 CA GLU D 745 4968 6354 7813 -373 -605 -215 C ATOM 3592 C GLU D 745 -16.920 -0.850 1.990 1.00 51.46 C ANISOU 3592 C GLU D 745 4952 6603 7998 -515 -315 -486 C ATOM 3593 O GLU D 745 -18.137 -1.026 2.037 1.00 58.27 O ANISOU 3593 O GLU D 745 5567 7480 9093 -575 -307 -615 O ATOM 3594 CB GLU D 745 -16.520 -1.581 -0.393 1.00 56.76 C ANISOU 3594 CB GLU D 745 5939 7193 8433 -458 -792 -24 C ATOM 3595 CG GLU D 745 -15.853 -1.326 -1.728 1.00 61.76 C ANISOU 3595 CG GLU D 745 6784 7694 8988 -397 -1051 227 C ATOM 3596 CD GLU D 745 -16.177 0.049 -2.272 1.00 69.28 C ANISOU 3596 CD GLU D 745 7535 8475 10314 -255 -1270 247 C ATOM 3597 OE1 GLU D 745 -17.311 0.519 -2.043 1.00 71.85 O ANISOU 3597 OE1 GLU D 745 7514 8772 11016 -218 -1314 131 O ATOM 3598 OE2 GLU D 745 -15.300 0.661 -2.921 1.00 74.16 O ANISOU 3598 OE2 GLU D 745 8340 8974 10863 -186 -1395 368 O ATOM 3599 N THR D 746 -16.149 -0.947 3.065 1.00 48.81 N ANISOU 3599 N THR D 746 4770 6331 7443 -598 -84 -579 N ATOM 3600 CA THR D 746 -16.735 -1.276 4.358 1.00 51.17 C ANISOU 3600 CA THR D 746 4991 6710 7740 -801 201 -848 C ATOM 3601 C THR D 746 -17.804 -0.268 4.762 1.00 55.22 C ANISOU 3601 C THR D 746 5109 7133 8739 -787 325 -1097 C ATOM 3602 O THR D 746 -17.570 0.941 4.750 1.00 53.39 O ANISOU 3602 O THR D 746 4739 6784 8761 -649 329 -1109 O ATOM 3603 CB THR D 746 -15.676 -1.375 5.463 1.00 58.57 C ANISOU 3603 CB THR D 746 6177 7697 8380 -926 395 -885 C ATOM 3604 OG1 THR D 746 -14.727 -2.392 5.118 1.00 66.35 O ANISOU 3604 OG1 THR D 746 7492 8745 8974 -934 282 -664 O ATOM 3605 CG2 THR D 746 -16.328 -1.731 6.797 1.00 57.77 C ANISOU 3605 CG2 THR D 746 6049 7653 8248 -1208 687 -1176 C ATOM 3606 N PRO D 747 -18.998 -0.767 5.102 1.00 63.95 N ANISOU 3606 N PRO D 747 6024 8280 9993 -931 439 -1307 N ATOM 3607 CA PRO D 747 -20.078 0.140 5.493 1.00 69.59 C ANISOU 3607 CA PRO D 747 6319 8882 11241 -926 587 -1574 C ATOM 3608 C PRO D 747 -19.715 0.882 6.770 1.00 68.77 C ANISOU 3608 C PRO D 747 6219 8727 11183 -1055 934 -1803 C ATOM 3609 O PRO D 747 -19.099 0.295 7.667 1.00 62.16 O ANISOU 3609 O PRO D 747 5685 7983 9948 -1278 1119 -1857 O ATOM 3610 CB PRO D 747 -21.257 -0.805 5.750 1.00 76.89 C ANISOU 3610 CB PRO D 747 7120 9894 12202 -1120 691 -1779 C ATOM 3611 CG PRO D 747 -20.919 -2.063 5.012 1.00 76.90 C ANISOU 3611 CG PRO D 747 7432 10035 11752 -1141 477 -1528 C ATOM 3612 CD PRO D 747 -19.430 -2.175 5.077 1.00 67.28 C ANISOU 3612 CD PRO D 747 6598 8843 10123 -1103 442 -1315 C ATOM 3613 N LYS D 748 -20.074 2.161 6.839 1.00 74.32 N ANISOU 3613 N LYS D 748 6608 9269 12363 -935 1012 -1920 N ATOM 3614 CA LYS D 748 -19.918 2.931 8.064 1.00 80.84 C ANISOU 3614 CA LYS D 748 7405 10022 13289 -1100 1397 -2174 C ATOM 3615 C LYS D 748 -20.580 2.189 9.223 1.00 91.83 C ANISOU 3615 C LYS D 748 8827 11472 14594 -1473 1749 -2508 C ATOM 3616 O LYS D 748 -21.753 1.813 9.141 1.00 86.31 O ANISOU 3616 O LYS D 748 7864 10760 14168 -1533 1793 -2700 O ATOM 3617 CB LYS D 748 -20.534 4.325 7.912 1.00 82.16 C ANISOU 3617 CB LYS D 748 7156 9979 14082 -924 1459 -2297 C ATOM 3618 CG LYS D 748 -20.305 5.228 9.121 1.00 82.00 C ANISOU 3618 CG LYS D 748 7127 9864 14165 -1104 1891 -2545 C ATOM 3619 CD LYS D 748 -21.134 6.504 9.060 1.00 82.73 C ANISOU 3619 CD LYS D 748 6757 9722 14955 -958 2016 -2728 C ATOM 3620 CE LYS D 748 -20.780 7.348 7.851 1.00 84.42 C ANISOU 3620 CE LYS D 748 6882 9838 15355 -568 1624 -2431 C ATOM 3621 NZ LYS D 748 -21.464 8.675 7.870 1.00 88.12 N ANISOU 3621 NZ LYS D 748 6929 10051 16500 -420 1749 -2594 N ATOM 3622 N PRO D 749 -19.821 1.961 10.305 1.00104.17 N ANISOU 3622 N PRO D 749 10729 13092 15760 -1753 1986 -2577 N ATOM 3623 CA PRO D 749 -20.336 1.272 11.494 1.00113.81 C ANISOU 3623 CA PRO D 749 12071 14347 16826 -2179 2325 -2901 C ATOM 3624 C PRO D 749 -21.469 2.044 12.174 1.00122.48 C ANISOU 3624 C PRO D 749 12797 15277 18463 -2345 2718 -3324 C ATOM 3625 O PRO D 749 -22.028 2.971 11.585 1.00125.41 O ANISOU 3625 O PRO D 749 12754 15511 19383 -2080 2673 -3348 O ATOM 3626 CB PRO D 749 -19.113 1.207 12.417 1.00113.04 C ANISOU 3626 CB PRO D 749 12410 14293 16246 -2416 2437 -2821 C ATOM 3627 CG PRO D 749 -17.935 1.327 11.503 1.00108.15 C ANISOU 3627 CG PRO D 749 11941 13734 15418 -2083 2074 -2404 C ATOM 3628 CD PRO D 749 -18.380 2.249 10.412 1.00105.11 C ANISOU 3628 CD PRO D 749 11175 13248 15512 -1704 1905 -2328 C TER 3629 PRO D 749 HETATM 3630 MG MG A 301 2.571 10.070 40.793 1.00 44.00 MG ANISOU 3630 MG MG A 301 7652 4749 4315 -464 800 -91 MG HETATM 3631 PB GDP A 302 5.497 9.537 42.439 1.00 39.06 P ANISOU 3631 PB GDP A 302 7137 4341 3362 -314 606 -15 P HETATM 3632 O1B GDP A 302 4.587 9.353 41.262 1.00 36.16 O ANISOU 3632 O1B GDP A 302 6697 3905 3137 -356 673 -16 O HETATM 3633 O2B GDP A 302 4.857 10.444 43.478 1.00 35.56 O ANISOU 3633 O2B GDP A 302 6763 3838 2909 -376 645 -70 O HETATM 3634 O3B GDP A 302 5.828 8.211 43.050 1.00 36.04 O ANISOU 3634 O3B GDP A 302 6886 3954 2853 -199 636 30 O HETATM 3635 O3A GDP A 302 6.922 10.138 42.035 1.00 33.86 O ANISOU 3635 O3A GDP A 302 6354 3837 2675 -313 458 -13 O HETATM 3636 PA GDP A 302 7.250 11.037 40.762 1.00 39.08 P ANISOU 3636 PA GDP A 302 6849 4550 3450 -394 398 -23 P HETATM 3637 O1A GDP A 302 7.309 10.203 39.515 1.00 41.21 O ANISOU 3637 O1A GDP A 302 7052 4829 3778 -356 407 23 O HETATM 3638 O2A GDP A 302 6.287 12.188 40.586 1.00 36.55 O ANISOU 3638 O2A GDP A 302 6510 4142 3236 -496 441 -66 O HETATM 3639 O5' GDP A 302 8.720 11.494 41.212 1.00 39.86 O ANISOU 3639 O5' GDP A 302 6892 4800 3452 -384 274 -44 O HETATM 3640 C5' GDP A 302 8.920 12.340 42.354 1.00 37.52 C ANISOU 3640 C5' GDP A 302 6640 4525 3089 -422 241 -98 C HETATM 3641 C4' GDP A 302 10.250 13.053 42.121 1.00 45.92 C ANISOU 3641 C4' GDP A 302 7577 5738 4132 -464 128 -136 C HETATM 3642 O4' GDP A 302 11.312 12.091 42.023 1.00 44.50 O ANISOU 3642 O4' GDP A 302 7357 5684 3868 -356 56 -112 O HETATM 3643 C3' GDP A 302 10.221 13.800 40.798 1.00 46.37 C ANISOU 3643 C3' GDP A 302 7518 5783 4320 -563 133 -136 C HETATM 3644 O3' GDP A 302 10.845 15.069 41.005 1.00 51.53 O ANISOU 3644 O3' GDP A 302 8112 6492 4975 -668 83 -203 O HETATM 3645 C2' GDP A 302 11.075 12.960 39.872 1.00 41.30 C ANISOU 3645 C2' GDP A 302 6781 5238 3673 -501 89 -97 C HETATM 3646 O2' GDP A 302 11.772 13.724 38.882 1.00 42.88 O ANISOU 3646 O2' GDP A 302 6852 5503 3938 -590 52 -117 O HETATM 3647 C1' GDP A 302 12.050 12.284 40.817 1.00 43.36 C ANISOU 3647 C1' GDP A 302 7061 5623 3792 -397 13 -110 C HETATM 3648 N9 GDP A 302 12.467 10.980 40.246 1.00 44.02 N ANISOU 3648 N9 GDP A 302 7125 5754 3845 -278 1 -54 N HETATM 3649 C8 GDP A 302 11.640 10.004 39.822 1.00 43.32 C ANISOU 3649 C8 GDP A 302 7110 5560 3789 -218 82 9 C HETATM 3650 N7 GDP A 302 12.340 8.931 39.358 1.00 40.51 N ANISOU 3650 N7 GDP A 302 6724 5279 3390 -110 50 48 N HETATM 3651 C5 GDP A 302 13.649 9.227 39.487 1.00 41.04 C ANISOU 3651 C5 GDP A 302 6684 5512 3397 -94 -58 5 C HETATM 3652 C6 GDP A 302 14.924 8.542 39.189 1.00 46.25 C ANISOU 3652 C6 GDP A 302 7251 6330 3992 9 -145 4 C HETATM 3653 O6 GDP A 302 14.941 7.394 38.687 1.00 55.25 O ANISOU 3653 O6 GDP A 302 8419 7455 5118 115 -122 61 O HETATM 3654 N1 GDP A 302 16.058 9.188 39.462 1.00 47.91 N ANISOU 3654 N1 GDP A 302 7341 6702 4159 -17 -245 -70 N HETATM 3655 C2 GDP A 302 16.076 10.424 39.993 1.00 48.38 C ANISOU 3655 C2 GDP A 302 7374 6777 4233 -139 -265 -140 C HETATM 3656 N2 GDP A 302 17.279 10.991 40.229 1.00 51.79 N ANISOU 3656 N2 GDP A 302 7672 7383 4622 -168 -363 -228 N HETATM 3657 N3 GDP A 302 14.950 11.119 40.296 1.00 47.17 N ANISOU 3657 N3 GDP A 302 7315 6473 4134 -234 -189 -135 N HETATM 3658 C4 GDP A 302 13.728 10.578 40.068 1.00 45.83 C ANISOU 3658 C4 GDP A 302 7261 6140 4014 -212 -88 -65 C HETATM 3659 MG MG A 304 4.607 9.644 24.475 1.00 48.31 MG ANISOU 3659 MG MG A 304 7247 5679 5428 -355 370 149 MG HETATM 3660 MG MG A 306 7.135 0.300 22.003 1.00 43.69 MG ANISOU 3660 MG MG A 306 6663 5252 4683 7 571 263 MG HETATM 3661 ZN ZN B 300 -13.711 0.628 34.353 1.00 67.86 ZN ANISOU 3661 ZN ZN B 300 6786 8536 10460 -1886 2992 -3964 ZN HETATM 3662 MG MG C 301 4.996 -8.773 -0.265 1.00 34.23 MG ANISOU 3662 MG MG C 301 4767 4230 4007 39 710 -335 MG HETATM 3663 PB GDP C 302 7.978 -8.328 -1.588 1.00 33.15 P ANISOU 3663 PB GDP C 302 4660 4152 3784 3 760 -279 P HETATM 3664 O1B GDP C 302 6.992 -8.128 -0.488 1.00 27.59 O ANISOU 3664 O1B GDP C 302 3953 3415 3116 23 728 -264 O HETATM 3665 O2B GDP C 302 7.380 -9.252 -2.629 1.00 33.80 O ANISOU 3665 O2B GDP C 302 4727 4247 3867 -4 781 -363 O HETATM 3666 O3B GDP C 302 8.341 -7.026 -2.226 1.00 31.81 O ANISOU 3666 O3B GDP C 302 4537 4021 3527 -14 720 -242 O HETATM 3667 O3A GDP C 302 9.330 -8.957 -1.004 1.00 33.97 O ANISOU 3667 O3A GDP C 302 4730 4237 3942 6 816 -246 O HETATM 3668 PA GDP C 302 9.422 -9.878 0.297 1.00 34.80 P ANISOU 3668 PA GDP C 302 4794 4290 4139 30 847 -224 P HETATM 3669 O1A GDP C 302 9.312 -9.075 1.584 1.00 33.35 O ANISOU 3669 O1A GDP C 302 4626 4093 3951 39 806 -160 O HETATM 3670 O2A GDP C 302 8.428 -10.992 0.222 1.00 35.10 O ANISOU 3670 O2A GDP C 302 4810 4295 4233 40 873 -286 O HETATM 3671 O5' GDP C 302 10.932 -10.384 0.100 1.00 33.54 O ANISOU 3671 O5' GDP C 302 4603 4135 4006 29 899 -206 O HETATM 3672 C5' GDP C 302 11.212 -11.262 -1.001 1.00 35.02 C ANISOU 3672 C5' GDP C 302 4771 4329 4207 22 953 -270 C HETATM 3673 C4' GDP C 302 12.516 -11.987 -0.735 1.00 35.99 C ANISOU 3673 C4' GDP C 302 4845 4435 4393 36 1009 -247 C HETATM 3674 O4' GDP C 302 13.549 -11.025 -0.502 1.00 38.26 O ANISOU 3674 O4' GDP C 302 5136 4756 4644 25 988 -184 O HETATM 3675 C3' GDP C 302 12.372 -12.800 0.537 1.00 47.11 C ANISOU 3675 C3' GDP C 302 6223 5786 5890 69 1020 -213 C HETATM 3676 O3' GDP C 302 13.004 -14.071 0.324 1.00 49.57 O ANISOU 3676 O3' GDP C 302 6488 6063 6285 89 1090 -239 O HETATM 3677 C2' GDP C 302 13.099 -11.975 1.585 1.00 40.70 C ANISOU 3677 C2' GDP C 302 5412 4989 5064 74 981 -126 C HETATM 3678 O2' GDP C 302 13.663 -12.794 2.611 1.00 39.79 O ANISOU 3678 O2' GDP C 302 5255 4836 5028 106 1003 -79 O HETATM 3679 C1' GDP C 302 14.159 -11.246 0.771 1.00 39.58 C ANISOU 3679 C1' GDP C 302 5270 4898 4872 49 984 -120 C HETATM 3680 N9 GDP C 302 14.542 -9.944 1.372 1.00 38.04 N ANISOU 3680 N9 GDP C 302 5098 4732 4623 31 928 -57 N HETATM 3681 C8 GDP C 302 13.728 -8.903 1.649 1.00 32.08 C ANISOU 3681 C8 GDP C 302 4394 3985 3810 17 871 -44 C HETATM 3682 N7 GDP C 302 14.424 -7.875 2.187 1.00 33.71 N ANISOU 3682 N7 GDP C 302 4610 4213 3986 -1 836 11 N HETATM 3683 C5 GDP C 302 15.713 -8.265 2.248 1.00 32.93 C ANISOU 3683 C5 GDP C 302 4460 4126 3925 0 868 34 C HETATM 3684 C6 GDP C 302 16.984 -7.671 2.700 1.00 34.39 C ANISOU 3684 C6 GDP C 302 4618 4339 4111 -17 854 85 C HETATM 3685 O6 GDP C 302 17.009 -6.521 3.179 1.00 35.06 O ANISOU 3685 O6 GDP C 302 4734 4437 4149 -43 805 117 O HETATM 3686 N1 GDP C 302 18.095 -8.409 2.592 1.00 40.37 N ANISOU 3686 N1 GDP C 302 5311 5104 4925 -5 897 92 N HETATM 3687 C2 GDP C 302 18.093 -9.665 2.095 1.00 37.93 C ANISOU 3687 C2 GDP C 302 4966 4771 4673 25 955 54 C HETATM 3688 N2 GDP C 302 19.258 -10.347 2.022 1.00 37.26 N ANISOU 3688 N2 GDP C 302 4812 4691 4653 42 999 63 N HETATM 3689 N3 GDP C 302 16.975 -10.271 1.650 1.00 33.68 N ANISOU 3689 N3 GDP C 302 4457 4204 4137 38 973 2 N HETATM 3690 C4 GDP C 302 15.781 -9.623 1.704 1.00 35.93 C ANISOU 3690 C4 GDP C 302 4801 4485 4365 25 929 -10 C HETATM 3691 MG MG C 303 5.021 10.403 21.527 1.00 57.98 MG ANISOU 3691 MG MG C 303 8480 6962 6588 -176 514 -370 MG HETATM 3692 MG MG C 305 7.329 0.853 19.013 1.00 40.50 MG ANISOU 3692 MG MG C 305 5935 5022 4434 -61 532 63 MG HETATM 3693 ZN ZN D 300 -11.870 1.269 4.457 1.00 40.61 ZN ANISOU 3693 ZN ZN D 300 4249 5226 5955 -429 141 -410 ZN HETATM 3694 O HOH A 217 3.556 5.170 29.768 1.00 30.49 O ANISOU 3694 O HOH A 217 5284 3271 3032 -271 671 92 O HETATM 3695 O HOH A 218 1.980 0.246 24.561 1.00 41.95 O ANISOU 3695 O HOH A 218 6592 4678 4670 -175 850 -9 O HETATM 3696 O HOH A 219 5.165 13.034 43.952 1.00 38.16 O ANISOU 3696 O HOH A 219 7002 4217 3281 -525 542 -163 O HETATM 3697 O HOH A 220 13.845 -0.788 20.885 1.00 39.75 O ANISOU 3697 O HOH A 220 5922 5274 3906 268 371 432 O HETATM 3698 O HOH A 221 6.819 2.777 23.587 1.00 37.15 O ANISOU 3698 O HOH A 221 5832 4416 3868 -99 505 249 O HETATM 3699 O HOH A 222 0.463 -13.176 23.202 1.00 57.92 O ANISOU 3699 O HOH A 222 9568 5862 6577 -147 2025 -251 O HETATM 3700 O HOH A 223 13.841 -18.710 25.328 1.00 67.53 O ANISOU 3700 O HOH A 223 11731 7430 6496 1842 1438 742 O HETATM 3701 O HOH A 224 14.261 -11.043 27.080 1.00 50.99 O ANISOU 3701 O HOH A 224 8657 6082 4634 1343 798 647 O HETATM 3702 O HOH A 225 0.679 8.817 35.096 1.00 42.39 O ANISOU 3702 O HOH A 225 7038 4527 4541 -468 825 -108 O HETATM 3703 O HOH A 226 9.425 9.811 32.878 1.00 37.65 O ANISOU 3703 O HOH A 226 6084 4614 3609 -394 267 142 O HETATM 3704 O HOH A 227 15.806 -12.343 37.656 1.00 63.87 O ANISOU 3704 O HOH A 227 11704 7469 5095 2335 687 889 O HETATM 3705 O HOH A 228 -0.558 -16.002 42.068 1.00 72.68 O ANISOU 3705 O HOH A 228 14774 6017 6825 247 3582 363 O HETATM 3706 O HOH A 229 -4.188 -14.646 44.010 1.00 93.19 O ANISOU 3706 O HOH A 229 17371 8384 9651 -343 4104 38 O HETATM 3707 O HOH A 230 13.908 12.067 28.060 1.00 53.76 O ANISOU 3707 O HOH A 230 7668 7030 5728 -649 141 143 O HETATM 3708 O HOH A 231 1.134 1.894 18.707 1.00 42.08 O ANISOU 3708 O HOH A 231 6258 4899 4830 -116 567 -99 O HETATM 3709 O HOH A 232 12.355 -15.775 40.150 1.00 83.64 O ANISOU 3709 O HOH A 232 15511 8973 7295 2349 1483 1050 O HETATM 3710 O HOH A 233 7.209 2.723 49.254 1.00 45.42 O ANISOU 3710 O HOH A 233 9318 4930 3009 540 842 252 O HETATM 3711 O HOH A 234 15.424 -20.468 28.978 1.00 70.43 O ANISOU 3711 O HOH A 234 12824 7609 6328 2482 1447 943 O HETATM 3712 O HOH A 235 14.618 1.180 24.771 1.00 42.57 O ANISOU 3712 O HOH A 235 6310 5717 4147 228 248 397 O HETATM 3713 O HOH A 236 0.326 6.710 19.938 1.00 39.62 O ANISOU 3713 O HOH A 236 5967 4543 4545 -150 400 -83 O HETATM 3714 O HOH A 237 14.080 3.217 23.269 1.00 36.01 O ANISOU 3714 O HOH A 237 5376 4864 3441 12 250 376 O HETATM 3715 O HOH A 238 7.271 -2.838 22.822 1.00 44.69 O ANISOU 3715 O HOH A 238 6987 5270 4724 144 735 278 O HETATM 3716 O HOH A 239 3.654 12.127 40.467 1.00 38.55 O ANISOU 3716 O HOH A 239 6835 4167 3646 -540 635 -109 O HETATM 3717 O HOH A 240 0.527 10.798 40.360 1.00 35.19 O ANISOU 3717 O HOH A 240 6484 3505 3383 -550 917 -186 O HETATM 3718 O HOH A 241 2.335 10.394 43.052 1.00 35.52 O ANISOU 3718 O HOH A 241 6778 3617 3099 -467 863 -129 O HETATM 3719 O HOH A 242 1.821 7.890 41.073 1.00 40.66 O ANISOU 3719 O HOH A 242 7380 4220 3849 -392 972 -66 O HETATM 3720 O HOH A 243 13.926 2.235 34.587 1.00 41.35 O ANISOU 3720 O HOH A 243 6770 5448 3491 432 138 324 O HETATM 3721 O HOH A 244 4.749 -9.181 19.226 1.00 54.46 O ANISOU 3721 O HOH A 244 8443 6162 6088 162 1193 48 O HETATM 3722 O HOH A 245 8.893 -4.934 23.586 1.00 39.13 O ANISOU 3722 O HOH A 245 6444 4569 3856 343 781 364 O HETATM 3723 O HOH A 246 19.074 -1.494 31.851 1.00 57.73 O ANISOU 3723 O HOH A 246 8497 8079 5361 1023 -109 362 O HETATM 3724 O HOH A 247 17.324 -2.346 30.189 1.00 49.50 O ANISOU 3724 O HOH A 247 7563 6766 4477 914 90 439 O HETATM 3725 O HOH A 248 9.311 9.963 30.062 1.00 54.90 O ANISOU 3725 O HOH A 248 8141 6793 5925 -431 273 181 O HETATM 3726 O HOH A 249 -12.781 9.248 33.535 1.00 65.21 O ANISOU 3726 O HOH A 249 9159 7173 8445 -650 1492 -1334 O HETATM 3727 O HOH A 250 -4.070 1.140 49.897 1.00 64.71 O ANISOU 3727 O HOH A 250 12207 6138 6241 -471 2541 -197 O HETATM 3728 O HOH A 251 16.401 0.289 29.540 1.00 52.52 O ANISOU 3728 O HOH A 251 7763 7135 5058 550 93 377 O HETATM 3729 O HOH A 252 17.696 3.589 27.532 1.00 51.31 O ANISOU 3729 O HOH A 252 7194 7210 5091 177 13 271 O HETATM 3730 O HOH A 253 13.288 -9.972 34.974 1.00 55.02 O ANISOU 3730 O HOH A 253 9994 6324 4586 1570 826 737 O HETATM 3731 O HOH A 254 16.664 1.284 26.965 1.00 60.51 O ANISOU 3731 O HOH A 254 8535 8212 6243 360 109 360 O HETATM 3732 O HOH A 256 10.060 12.333 29.013 1.00 65.18 O ANISOU 3732 O HOH A 256 9370 8117 7277 -599 234 159 O HETATM 3733 O HOH A 257 6.880 12.623 35.768 1.00 58.72 O ANISOU 3733 O HOH A 257 8966 7026 6321 -565 360 10 O HETATM 3734 O HOH A 260 -1.863 -16.231 35.004 1.00 60.05 O ANISOU 3734 O HOH A 260 11882 4832 6101 -220 3356 -53 O HETATM 3735 O HOH A 261 18.346 -12.666 27.953 1.00 77.75 O ANISOU 3735 O HOH A 261 12072 9825 7646 2013 522 726 O HETATM 3736 O HOH A 262 16.013 -14.549 35.773 1.00 69.48 O ANISOU 3736 O HOH A 262 12523 8025 5851 2469 843 942 O HETATM 3737 O HOH A 263 4.016 -19.254 37.114 1.00 55.51 O ANISOU 3737 O HOH A 263 12382 4131 4576 948 3053 631 O HETATM 3738 O HOH A 264 20.182 3.142 28.317 1.00 55.03 O ANISOU 3738 O HOH A 264 7481 8007 5422 335 -133 187 O HETATM 3739 O HOH A 265 2.806 -11.953 48.433 1.00 73.45 O ANISOU 3739 O HOH A 265 15315 6562 6033 976 2832 721 O HETATM 3740 O HOH A 266 -6.898 -9.344 42.182 1.00 62.67 O ANISOU 3740 O HOH A 266 12049 5195 6569 -843 3631 -429 O HETATM 3741 O HOH A 267 2.126 -20.947 28.761 1.00 54.47 O ANISOU 3741 O HOH A 267 11134 4214 5347 310 3113 120 O HETATM 3742 O HOH A 268 -12.595 1.841 49.248 1.00 63.41 O ANISOU 3742 O HOH A 268 11425 5635 7033 -1342 3598 -1097 O HETATM 3743 O HOH A 269 -14.169 -0.093 50.832 1.00 91.42 O ANISOU 3743 O HOH A 269 15376 8856 10504 -1569 4215 -1240 O HETATM 3744 O HOH A 270 -6.601 -2.227 50.539 1.00 67.28 O ANISOU 3744 O HOH A 270 13044 5959 6559 -686 3319 -311 O HETATM 3745 O HOH A 271 21.104 10.828 48.887 1.00 73.56 O ANISOU 3745 O HOH A 271 10693 10928 6327 510 -1066 -689 O HETATM 3746 O HOH A 272 21.151 -3.658 40.326 1.00 60.33 O ANISOU 3746 O HOH A 272 9692 8592 4639 2078 -514 356 O HETATM 3747 O HOH A 273 16.522 -1.602 21.349 1.00 60.04 O ANISOU 3747 O HOH A 273 8380 8091 6343 442 288 442 O HETATM 3748 O HOH A 274 16.015 -4.159 21.913 1.00 42.85 O ANISOU 3748 O HOH A 274 6422 5773 4087 664 374 483 O HETATM 3749 O HOH A 275 16.319 -6.713 20.102 1.00 61.03 O ANISOU 3749 O HOH A 275 8795 8024 6371 841 477 508 O HETATM 3750 O HOH A 276 6.911 -10.735 19.251 1.00 57.98 O ANISOU 3750 O HOH A 276 9033 6625 6371 375 1201 188 O HETATM 3751 O HOH A 277 33.507 1.372 40.298 1.00 69.85 O ANISOU 3751 O HOH A 277 8265 12535 5739 2277 -1918 -1046 O HETATM 3752 O HOH A 278 21.003 4.297 31.086 1.00 62.93 O ANISOU 3752 O HOH A 278 8466 9169 6274 351 -289 67 O HETATM 3753 O HOH A 279 6.253 10.956 26.053 1.00 48.44 O ANISOU 3753 O HOH A 279 7295 5751 5360 -449 335 179 O HETATM 3754 O HOH A 280 18.642 -14.224 56.196 1.00114.56 O ANISOU 3754 O HOH A 280 21714 13551 8263 4922 171 1306 O HETATM 3755 O HOH A 281 15.411 -11.236 20.346 1.00 50.14 O ANISOU 3755 O HOH A 281 7909 6276 4866 1163 745 555 O HETATM 3756 O HOH A 282 1.143 -16.074 38.456 1.00 64.51 O ANISOU 3756 O HOH A 282 13100 5375 6036 384 3125 379 O HETATM 3757 O HOH A 283 -2.872 -15.214 41.287 1.00 78.58 O ANISOU 3757 O HOH A 283 15145 6762 7950 -203 3783 82 O HETATM 3758 O HOH A 284 20.898 -0.214 31.136 1.00 48.39 O ANISOU 3758 O HOH A 284 6954 7209 4221 937 -250 249 O HETATM 3759 O HOH A 285 -15.466 9.208 42.750 1.00 61.17 O ANISOU 3759 O HOH A 285 9331 6151 7761 -1126 2519 -1621 O HETATM 3760 O HOH A 286 -5.601 -11.498 28.792 1.00 62.94 O ANISOU 3760 O HOH A 286 10384 6065 7466 -791 2719 -735 O HETATM 3761 O HOH A 287 -13.469 2.272 45.157 1.00 70.64 O ANISOU 3761 O HOH A 287 11556 6850 8434 -1361 3281 -1295 O HETATM 3762 O HOH A 288 0.951 -15.697 24.566 1.00 67.45 O ANISOU 3762 O HOH A 288 11281 6747 7600 -56 2344 -170 O HETATM 3763 O HOH A 289 2.597 -16.272 19.219 1.00 72.48 O ANISOU 3763 O HOH A 289 11430 7755 8354 73 1998 -212 O HETATM 3764 O HOH A 290 15.267 5.758 23.979 1.00 42.89 O ANISOU 3764 O HOH A 290 6131 5857 4307 -173 176 318 O HETATM 3765 O HOH A 292 6.403 -19.707 37.628 1.00 72.06 O ANISOU 3765 O HOH A 292 14651 6366 6363 1436 2773 835 O HETATM 3766 O HOH A 293 6.930 9.949 28.332 1.00 43.41 O ANISOU 3766 O HOH A 293 6704 5160 4629 -427 353 172 O HETATM 3767 O HOH A 294 1.031 4.860 41.226 1.00 43.04 O ANISOU 3767 O HOH A 294 7911 4357 4084 -309 1225 -28 O HETATM 3768 O HOH A 295 7.716 -18.719 35.276 1.00 57.19 O ANISOU 3768 O HOH A 295 12114 4915 4700 1465 2378 801 O HETATM 3769 O HOH A 296 -5.431 -13.697 33.214 1.00 74.57 O ANISOU 3769 O HOH A 296 12826 6958 8550 -784 3329 -555 O HETATM 3770 O HOH A 297 -10.076 -4.952 44.789 1.00 97.83 O ANISOU 3770 O HOH A 297 16089 9792 11291 -1191 3708 -793 O HETATM 3771 O HOH A 298 8.955 -22.902 27.654 1.00 68.86 O ANISOU 3771 O HOH A 298 13173 6404 6585 1496 2480 652 O HETATM 3772 O HOH A 299 11.241 17.401 40.015 1.00 81.67 O ANISOU 3772 O HOH A 299 11817 10292 8921 -904 79 -276 O HETATM 3773 O HOH A 300 -1.666 10.146 37.021 1.00 51.43 O ANISOU 3773 O HOH A 300 8266 5510 5763 -560 982 -269 O HETATM 3774 O HOH A 303 15.164 -7.297 24.289 1.00 59.07 O ANISOU 3774 O HOH A 303 8949 7542 5952 972 526 547 O HETATM 3775 O HOH A 305 3.020 8.427 50.412 1.00 49.99 O ANISOU 3775 O HOH A 305 9593 5301 4101 -178 1071 -96 O HETATM 3776 O HOH A 307 -6.794 13.192 39.422 1.00 53.62 O ANISOU 3776 O HOH A 307 8517 5532 6324 -690 1278 -686 O HETATM 3777 O HOH A 310 10.170 13.394 36.566 1.00 56.72 O ANISOU 3777 O HOH A 310 8586 7071 5893 -609 173 -27 O HETATM 3778 O HOH A 311 1.280 -17.938 22.947 1.00 68.79 O ANISOU 3778 O HOH A 311 11584 6793 7761 -19 2493 -215 O HETATM 3779 O HOH A 312 9.671 10.282 51.390 1.00 63.41 O ANISOU 3779 O HOH A 312 10928 7837 5328 119 194 -167 O HETATM 3780 O HOH A 313 17.281 9.780 54.126 1.00 61.37 O ANISOU 3780 O HOH A 313 10336 8756 4223 832 -807 -477 O HETATM 3781 O HOH A 314 9.375 12.319 33.758 1.00 56.52 O ANISOU 3781 O HOH A 314 8480 6975 6021 -561 236 66 O HETATM 3782 O HOH A 315 18.579 11.044 50.805 1.00 71.92 O ANISOU 3782 O HOH A 315 10999 10309 6018 485 -862 -571 O HETATM 3783 O HOH A 317 18.406 2.664 56.090 1.00 76.82 O ANISOU 3783 O HOH A 317 13385 10575 5230 2190 -857 -30 O HETATM 3784 O HOH A 318 10.121 -2.471 55.232 1.00 70.30 O ANISOU 3784 O HOH A 318 14091 7910 4711 1762 813 578 O HETATM 3785 O HOH A 319 8.491 -10.851 16.895 1.00 54.79 O ANISOU 3785 O HOH A 319 8455 6414 5949 471 1071 230 O HETATM 3786 O HOH A 320 7.980 15.101 37.696 1.00 59.71 O ANISOU 3786 O HOH A 320 9123 7211 6353 -717 277 -91 O HETATM 3787 O HOH A 321 7.541 14.342 46.179 1.00 60.81 O ANISOU 3787 O HOH A 321 9907 7321 5876 -525 322 -250 O HETATM 3788 O HOH A 323 13.456 11.415 52.712 1.00 76.69 O ANISOU 3788 O HOH A 323 12355 10096 6687 276 -308 -367 O HETATM 3789 O HOH A 324 2.659 5.572 53.232 1.00 68.37 O ANISOU 3789 O HOH A 324 12643 7374 5959 76 1368 13 O HETATM 3790 O HOH A 325 16.961 0.070 23.769 1.00 59.93 O ANISOU 3790 O HOH A 325 8349 8154 6268 380 187 401 O HETATM 3791 O HOH A 326 -4.245 8.866 56.328 1.00 62.44 O ANISOU 3791 O HOH A 326 12059 6046 5618 -591 2234 -452 O HETATM 3792 O HOH A 327 -5.189 -12.152 51.200 1.00 84.35 O ANISOU 3792 O HOH A 327 17225 6970 7855 -288 4446 146 O HETATM 3793 O HOH A 328 -7.749 -13.079 35.534 1.00 65.51 O ANISOU 3793 O HOH A 328 11809 5614 7469 -1080 3715 -765 O HETATM 3794 O HOH A 329 4.894 13.560 26.753 1.00 57.11 O ANISOU 3794 O HOH A 329 8485 6699 6517 -528 335 116 O HETATM 3795 O HOH A 336 18.065 -10.940 19.585 1.00 66.95 O ANISOU 3795 O HOH A 336 9777 8738 6923 1333 578 563 O HETATM 3796 O HOH A 338 -7.986 -14.885 18.503 1.00 70.94 O ANISOU 3796 O HOH A 338 10375 7544 9037 -1041 2504 -1559 O HETATM 3797 O HOH A 339 18.339 1.937 22.464 1.00 63.75 O ANISOU 3797 O HOH A 339 8589 8822 6812 193 143 346 O HETATM 3798 O HOH A 344 10.177 16.278 43.627 1.00 70.54 O ANISOU 3798 O HOH A 344 10712 8827 7263 -721 98 -308 O HETATM 3799 O HOH A 345 19.359 -13.799 20.832 1.00 65.44 O ANISOU 3799 O HOH A 345 9909 8469 6487 1807 622 629 O HETATM 3800 O HOH A 346 1.334 -8.787 54.048 1.00 75.25 O ANISOU 3800 O HOH A 346 16065 6702 5823 864 2967 646 O HETATM 3801 O HOH B 1 -6.999 -2.212 33.559 1.00 48.98 O ANISOU 3801 O HOH B 1 6001 5265 7344 -1893 2891 -2293 O HETATM 3802 O HOH B 2 -7.043 -4.454 32.119 1.00 51.62 O ANISOU 3802 O HOH B 2 6457 5665 7490 -2012 2849 -2299 O HETATM 3803 O HOH B 162 -11.409 3.400 23.421 1.00 77.05 O ANISOU 3803 O HOH B 162 8058 9567 11649 314 1043 -2848 O HETATM 3804 O HOH B 270 -17.375 0.904 29.038 1.00 80.54 O ANISOU 3804 O HOH B 270 7406 10699 12497 -1064 2200 -4680 O HETATM 3805 O HOH C 217 -11.733 -3.712 -6.447 1.00 66.86 O ANISOU 3805 O HOH C 217 8514 8779 8112 310 -234 -774 O HETATM 3806 O HOH C 218 26.627 -10.278 1.209 1.00 63.50 O ANISOU 3806 O HOH C 218 7732 8190 8204 12 1150 148 O HETATM 3807 O HOH C 219 10.860 -8.713 8.424 1.00 35.64 O ANISOU 3807 O HOH C 219 4900 4331 4312 89 753 123 O HETATM 3808 O HOH C 220 0.992 9.512 -14.040 1.00 52.24 O ANISOU 3808 O HOH C 220 8013 6805 5030 207 -290 589 O HETATM 3809 O HOH C 221 23.479 -5.053 -2.527 1.00 55.32 O ANISOU 3809 O HOH C 221 7144 7224 6652 -254 1101 81 O HETATM 3810 O HOH C 222 3.400 -3.545 -0.723 1.00 32.96 O ANISOU 3810 O HOH C 222 4759 4118 3647 71 472 -213 O HETATM 3811 O HOH C 223 15.559 -1.192 7.031 1.00 31.91 O ANISOU 3811 O HOH C 223 4537 4013 3575 -136 561 210 O HETATM 3812 O HOH C 224 17.443 0.858 12.432 1.00 36.03 O ANISOU 3812 O HOH C 224 5058 4609 4022 -229 394 277 O HETATM 3813 O HOH C 225 6.662 -11.208 10.781 1.00 63.60 O ANISOU 3813 O HOH C 225 8450 7739 7977 131 863 85 O HETATM 3814 O HOH C 226 19.790 4.827 13.825 1.00 65.86 O ANISOU 3814 O HOH C 226 8875 8420 7729 -442 274 235 O HETATM 3815 O HOH C 227 2.182 -7.612 5.511 1.00 40.37 O ANISOU 3815 O HOH C 227 5538 4880 4920 103 693 -225 O HETATM 3816 O HOH C 228 4.596 -3.726 10.825 1.00 32.06 O ANISOU 3816 O HOH C 228 4639 3834 3709 84 631 -10 O HETATM 3817 O HOH C 229 10.701 -1.971 -8.191 1.00 34.28 O ANISOU 3817 O HOH C 229 5139 4567 3319 -167 656 -81 O HETATM 3818 O HOH C 231 6.593 6.633 -17.369 1.00 59.03 O ANISOU 3818 O HOH C 231 8988 7973 5467 -152 133 497 O HETATM 3819 O HOH C 232 13.834 1.779 20.832 1.00 38.67 O ANISOU 3819 O HOH C 232 5635 5021 4037 -231 300 205 O HETATM 3820 O HOH C 233 -1.328 3.615 -14.903 1.00 73.66 O ANISOU 3820 O HOH C 233 10402 9855 7732 172 -308 81 O HETATM 3821 O HOH C 234 4.864 -8.276 16.122 1.00 34.95 O ANISOU 3821 O HOH C 234 4973 4179 4128 102 816 174 O HETATM 3822 O HOH C 235 5.793 -10.824 0.258 1.00 31.23 O ANISOU 3822 O HOH C 235 4330 3795 3742 42 815 -357 O HETATM 3823 O HOH C 236 4.209 -6.691 -0.735 1.00 28.84 O ANISOU 3823 O HOH C 236 4146 3588 3225 46 606 -301 O HETATM 3824 O HOH C 237 2.798 -9.505 0.132 1.00 34.14 O ANISOU 3824 O HOH C 237 4713 4189 4070 52 698 -413 O HETATM 3825 O HOH C 238 4.748 -9.136 -2.471 1.00 28.96 O ANISOU 3825 O HOH C 238 4108 3626 3269 14 702 -427 O HETATM 3826 O HOH C 239 25.163 3.452 -2.169 1.00 35.55 O ANISOU 3826 O HOH C 239 4891 4696 3919 -628 945 324 O HETATM 3827 O HOH C 240 -0.172 0.011 -9.920 1.00 44.37 O ANISOU 3827 O HOH C 240 6424 5925 4510 113 25 -192 O HETATM 3828 O HOH C 241 6.346 -7.260 -9.902 1.00 37.61 O ANISOU 3828 O HOH C 241 5408 5062 3819 -112 642 -514 O HETATM 3829 O HOH C 242 20.640 2.350 10.413 1.00 42.43 O ANISOU 3829 O HOH C 242 5778 5468 4873 -361 404 297 O HETATM 3830 O HOH C 243 -9.008 -0.315 -10.480 1.00 55.13 O ANISOU 3830 O HOH C 243 7389 7442 6114 354 -461 -458 O HETATM 3831 O HOH C 244 7.077 -1.402 17.352 1.00 37.27 O ANISOU 3831 O HOH C 244 5438 4590 4132 -5 578 112 O HETATM 3832 O HOH C 245 3.900 -1.015 -12.485 1.00 64.87 O ANISOU 3832 O HOH C 245 9148 8652 6849 -54 242 -185 O HETATM 3833 O HOH C 246 9.420 6.153 17.772 1.00 49.13 O ANISOU 3833 O HOH C 246 7140 6030 5497 -198 394 -34 O HETATM 3834 O HOH C 247 15.485 11.942 14.485 1.00 34.79 O ANISOU 3834 O HOH C 247 5377 4089 3754 -542 269 4 O HETATM 3835 O HOH C 248 13.456 -9.008 -9.833 1.00 46.85 O ANISOU 3835 O HOH C 248 6467 6204 5131 -185 1068 -469 O HETATM 3836 O HOH C 249 9.832 -7.636 -14.520 1.00 51.69 O ANISOU 3836 O HOH C 249 7316 7082 5244 -260 861 -601 O HETATM 3837 O HOH C 252 36.298 4.678 -1.452 1.00 58.46 O ANISOU 3837 O HOH C 252 6973 7916 7324 -1072 1237 337 O HETATM 3838 O HOH C 253 35.137 5.234 -3.800 1.00 68.02 O ANISOU 3838 O HOH C 253 8395 9079 8369 -1104 1368 354 O HETATM 3839 O HOH C 254 -0.618 -12.919 -4.881 1.00 34.40 O ANISOU 3839 O HOH C 254 4625 4341 4103 -46 676 -863 O HETATM 3840 O HOH C 255 2.565 1.073 16.127 1.00 37.78 O ANISOU 3840 O HOH C 255 5543 4523 4290 62 616 -89 O HETATM 3841 O HOH C 256 14.435 -2.110 18.285 1.00 43.00 O ANISOU 3841 O HOH C 256 6015 5537 4787 -96 386 347 O HETATM 3842 O HOH C 257 -4.691 -4.193 -6.455 1.00 41.17 O ANISOU 3842 O HOH C 257 5628 5427 4588 159 80 -560 O HETATM 3843 O HOH C 258 15.484 -4.826 17.852 1.00 40.92 O ANISOU 3843 O HOH C 258 5638 5278 4631 -16 423 457 O HETATM 3844 O HOH C 259 -4.371 12.672 11.047 1.00 47.08 O ANISOU 3844 O HOH C 259 6874 5153 5861 429 351 -284 O HETATM 3845 O HOH C 260 14.138 -10.978 13.569 1.00 55.05 O ANISOU 3845 O HOH C 260 7267 6820 6832 172 718 436 O HETATM 3846 O HOH C 261 15.375 10.883 6.782 1.00 37.78 O ANISOU 3846 O HOH C 261 5753 4423 4179 -450 384 238 O HETATM 3847 O HOH C 262 -11.052 -7.781 5.687 1.00 45.26 O ANISOU 3847 O HOH C 262 5687 5505 6003 177 634 -740 O HETATM 3848 O HOH C 263 -0.338 9.952 15.920 1.00 54.82 O ANISOU 3848 O HOH C 263 7919 6351 6560 144 523 -330 O HETATM 3849 O HOH C 264 21.849 -3.247 11.320 1.00 58.24 O ANISOU 3849 O HOH C 264 7527 7552 7048 -148 463 406 O HETATM 3850 O HOH C 265 9.821 20.224 6.047 1.00 46.67 O ANISOU 3850 O HOH C 265 7409 4792 5532 -316 297 271 O HETATM 3851 O HOH C 266 -0.681 0.729 20.265 1.00 46.06 O ANISOU 3851 O HOH C 266 6620 5578 5303 73 807 -196 O HETATM 3852 O HOH C 267 24.057 3.735 2.116 1.00 39.32 O ANISOU 3852 O HOH C 267 5349 5106 4486 -558 723 324 O HETATM 3853 O HOH C 268 7.589 4.012 17.946 1.00 42.16 O ANISOU 3853 O HOH C 268 6213 5161 4647 -107 467 -21 O HETATM 3854 O HOH C 269 -1.995 0.923 -11.303 1.00 52.07 O ANISOU 3854 O HOH C 269 7411 6977 5394 172 -148 -171 O HETATM 3855 O HOH C 270 34.606 1.273 4.006 1.00 61.45 O ANISOU 3855 O HOH C 270 7220 8313 7817 -712 827 353 O HETATM 3856 O HOH C 271 1.660 -11.087 13.711 1.00 61.66 O ANISOU 3856 O HOH C 271 8239 7432 7756 113 960 14 O HETATM 3857 O HOH C 272 18.559 3.287 11.964 1.00 46.26 O ANISOU 3857 O HOH C 272 6391 5896 5291 -342 358 255 O HETATM 3858 O HOH C 273 20.404 9.364 0.474 1.00 53.68 O ANISOU 3858 O HOH C 273 7633 6652 6112 -639 627 411 O HETATM 3859 O HOH C 274 17.636 -7.595 -13.540 1.00 55.57 O ANISOU 3859 O HOH C 274 7639 7521 5955 -346 1325 -445 O HETATM 3860 O HOH C 275 11.604 -11.987 4.645 1.00 51.48 O ANISOU 3860 O HOH C 275 6798 6288 6472 111 918 -27 O HETATM 3861 O HOH C 277 -3.940 10.900 -2.672 1.00 56.06 O ANISOU 3861 O HOH C 277 8058 6680 6564 515 -195 215 O HETATM 3862 O HOH C 278 -2.630 3.531 -11.298 1.00 53.05 O ANISOU 3862 O HOH C 278 7620 7037 5501 259 -272 6 O HETATM 3863 O HOH C 279 4.612 -12.715 1.809 1.00 57.11 O ANISOU 3863 O HOH C 279 7548 6973 7179 59 886 -383 O HETATM 3864 O HOH C 280 15.365 16.827 1.276 1.00 65.37 O ANISOU 3864 O HOH C 280 9621 7573 7642 -576 430 513 O HETATM 3865 O HOH C 281 23.344 -10.836 3.457 1.00 52.57 O ANISOU 3865 O HOH C 281 6515 6694 6765 81 1009 196 O HETATM 3866 O HOH C 282 6.234 20.614 3.688 1.00 47.19 O ANISOU 3866 O HOH C 282 7528 4769 5633 -48 203 388 O HETATM 3867 O HOH C 283 21.458 10.521 -1.578 1.00 54.16 O ANISOU 3867 O HOH C 283 7756 6706 6117 -738 711 487 O HETATM 3868 O HOH C 284 -0.837 -9.643 13.777 1.00 62.57 O ANISOU 3868 O HOH C 284 8348 7559 7869 107 953 -98 O HETATM 3869 O HOH C 285 16.154 5.007 20.116 1.00 46.21 O ANISOU 3869 O HOH C 285 6595 5974 4987 -390 200 124 O HETATM 3870 O HOH C 286 28.614 4.356 -7.237 1.00 51.70 O ANISOU 3870 O HOH C 286 6923 6892 5830 -869 1323 356 O HETATM 3871 O HOH C 287 18.293 -2.842 14.801 1.00 40.92 O ANISOU 3871 O HOH C 287 5541 5310 4697 -111 388 400 O HETATM 3872 O HOH C 288 1.352 -10.359 17.001 1.00 75.95 O ANISOU 3872 O HOH C 288 10130 9275 9452 102 994 111 O HETATM 3873 O HOH C 289 -7.661 -7.806 10.371 1.00 47.36 O ANISOU 3873 O HOH C 289 6183 5658 6154 148 859 -484 O HETATM 3874 O HOH C 290 14.795 3.586 -13.883 1.00 52.58 O ANISOU 3874 O HOH C 290 7846 7060 5074 -440 790 293 O HETATM 3875 O HOH C 291 10.955 23.967 13.255 1.00 58.69 O ANISOU 3875 O HOH C 291 9031 6065 7205 -572 365 -207 O HETATM 3876 O HOH C 292 3.824 17.326 2.082 1.00 43.32 O ANISOU 3876 O HOH C 292 6877 4540 5044 129 121 378 O HETATM 3877 O HOH C 293 -5.252 -1.859 14.729 1.00 61.62 O ANISOU 3877 O HOH C 293 8288 7463 7661 202 804 -330 O HETATM 3878 O HOH C 294 -0.011 14.432 1.665 1.00 36.62 O ANISOU 3878 O HOH C 294 5818 3875 4222 340 34 255 O HETATM 3879 O HOH C 295 4.355 24.399 8.074 1.00 50.54 O ANISOU 3879 O HOH C 295 8056 4780 6367 9 272 109 O HETATM 3880 O HOH C 297 20.083 -7.571 -12.596 1.00 49.49 O ANISOU 3880 O HOH C 297 6750 6721 5332 -355 1439 -382 O HETATM 3881 O HOH C 298 27.129 -11.120 -2.561 1.00 57.32 O ANISOU 3881 O HOH C 298 6950 7436 7394 -32 1402 -41 O HETATM 3882 O HOH C 299 4.227 -12.284 9.985 1.00 63.29 O ANISOU 3882 O HOH C 299 8382 7639 8027 123 927 -33 O HETATM 3883 O HOH C 300 8.477 -13.836 0.153 1.00 70.13 O ANISOU 3883 O HOH C 300 9168 8643 8834 58 999 -370 O HETATM 3884 O HOH C 304 9.944 -9.945 10.756 1.00 53.44 O ANISOU 3884 O HOH C 304 7156 6539 6610 123 782 184 O HETATM 3885 O HOH C 306 25.034 0.036 -11.030 1.00 45.53 O ANISOU 3885 O HOH C 306 6295 6224 4782 -649 1419 132 O HETATM 3886 O HOH C 307 14.124 13.877 23.277 1.00 54.45 O ANISOU 3886 O HOH C 307 8052 6707 5928 -681 200 -389 O HETATM 3887 O HOH C 308 10.123 16.073 22.824 1.00 60.57 O ANISOU 3887 O HOH C 308 8989 7181 6844 -543 351 -545 O HETATM 3888 O HOH C 309 10.119 20.995 15.744 1.00 50.31 O ANISOU 3888 O HOH C 309 7834 5297 5984 -503 354 -327 O HETATM 3889 O HOH C 310 20.257 12.849 0.054 1.00 59.66 O ANISOU 3889 O HOH C 310 8575 7233 6860 -747 609 494 O HETATM 3890 O HOH C 311 3.426 10.137 -14.654 1.00 53.44 O ANISOU 3890 O HOH C 311 8286 6942 5076 83 -147 690 O HETATM 3891 O HOH C 312 -1.211 -13.923 -1.203 1.00 42.73 O ANISOU 3891 O HOH C 312 5615 5213 5407 -13 792 -766 O HETATM 3892 O HOH C 313 6.679 13.020 -7.724 1.00 43.40 O ANISOU 3892 O HOH C 313 6958 5152 4380 -26 111 686 O HETATM 3893 O HOH C 315 10.877 -7.749 -11.457 1.00 43.00 O ANISOU 3893 O HOH C 315 6108 5809 4422 -203 904 -495 O HETATM 3894 O HOH C 316 8.480 13.713 -3.172 1.00 43.61 O ANISOU 3894 O HOH C 316 6895 4998 4679 -120 227 561 O HETATM 3895 O HOH C 317 -1.127 -9.795 17.355 1.00 53.96 O ANISOU 3895 O HOH C 317 7328 6474 6700 90 1052 8 O HETATM 3896 O HOH C 318 -6.466 9.686 -3.825 1.00 48.22 O ANISOU 3896 O HOH C 318 6915 5812 5594 612 -318 135 O HETATM 3897 O HOH C 319 -9.934 13.328 2.031 1.00 61.39 O ANISOU 3897 O HOH C 319 8457 7063 7803 856 -185 -31 O HETATM 3898 O HOH C 320 21.134 6.057 1.982 1.00 42.22 O ANISOU 3898 O HOH C 320 5968 5332 4741 -547 635 336 O HETATM 3899 O HOH C 321 29.584 6.895 -6.662 1.00 53.18 O ANISOU 3899 O HOH C 321 7151 7017 6040 -1018 1301 448 O HETATM 3900 O HOH C 322 15.151 -0.152 16.816 1.00 47.35 O ANISOU 3900 O HOH C 322 6577 6068 5347 -163 357 285 O HETATM 3901 O HOH C 323 -0.101 -5.147 20.064 1.00 41.16 O ANISOU 3901 O HOH C 323 5879 4978 4783 72 930 2 O HETATM 3902 O HOH C 324 15.669 13.381 19.110 1.00 53.94 O ANISOU 3902 O HOH C 324 7874 6573 6050 -660 200 -191 O HETATM 3903 O HOH C 325 -4.829 -12.264 0.501 1.00 55.92 O ANISOU 3903 O HOH C 325 7208 6894 7146 24 685 -771 O HETATM 3904 O HOH C 326 21.258 -2.943 14.238 1.00 54.54 O ANISOU 3904 O HOH C 326 7113 7120 6490 -145 354 450 O HETATM 3905 O HOH C 327 21.998 -10.472 -8.503 1.00 54.96 O ANISOU 3905 O HOH C 327 7116 7213 6554 -186 1489 -359 O HETATM 3906 O HOH C 328 23.720 -5.466 11.244 1.00 49.99 O ANISOU 3906 O HOH C 328 6305 6546 6143 -68 498 473 O HETATM 3907 O HOH C 329 8.146 12.107 24.243 1.00 52.25 O ANISOU 3907 O HOH C 329 7848 6343 5662 -390 425 -456 O HETATM 3908 O HOH C 330 12.515 22.460 16.571 1.00 72.39 O ANISOU 3908 O HOH C 330 10663 8065 8778 -713 339 -391 O HETATM 3909 O HOH C 331 20.331 0.661 -14.641 1.00 62.27 O ANISOU 3909 O HOH C 331 8809 8425 6425 -603 1255 119 O HETATM 3910 O HOH C 333 -6.466 14.044 -4.425 1.00 71.35 O ANISOU 3910 O HOH C 333 10048 8497 8564 741 -432 389 O HETATM 3911 O HOH C 334 20.722 -0.004 13.389 1.00 61.83 O ANISOU 3911 O HOH C 334 8152 8006 7336 -264 340 358 O HETATM 3912 O HOH C 335 16.642 -13.088 14.337 1.00 61.55 O ANISOU 3912 O HOH C 335 7962 7640 7784 259 721 588 O HETATM 3913 O HOH C 336 10.269 3.597 -18.323 1.00 64.21 O ANISOU 3913 O HOH C 336 9555 8785 6056 -346 502 279 O HETATM 3914 O HOH C 337 20.247 -9.672 15.638 1.00 55.06 O ANISOU 3914 O HOH C 337 7064 7069 6787 157 486 655 O HETATM 3915 O HOH C 338 15.700 8.692 17.514 1.00 50.85 O ANISOU 3915 O HOH C 338 7295 6350 5676 -478 232 18 O HETATM 3916 O HOH C 339 1.276 14.150 17.265 1.00 53.87 O ANISOU 3916 O HOH C 339 7989 6049 6429 47 501 -418 O HETATM 3917 O HOH C 340 27.115 -2.754 -11.426 1.00 67.63 O ANISOU 3917 O HOH C 340 8855 9090 7750 -609 1630 -22 O HETATM 3918 O HOH C 341 29.679 -2.749 -3.932 1.00 71.47 O ANISOU 3918 O HOH C 341 8916 9449 8789 -494 1316 153 O HETATM 3919 O HOH C 342 19.068 -11.185 -4.055 1.00 67.54 O ANISOU 3919 O HOH C 342 8713 8614 8336 -48 1235 -232 O HETATM 3920 O HOH C 343 16.561 -11.904 -2.087 1.00 59.34 O ANISOU 3920 O HOH C 343 7713 7472 7363 13 1131 -214 O HETATM 3921 O HOH C 344 23.625 -10.186 -6.072 1.00 59.91 O ANISOU 3921 O HOH C 344 7605 7796 7360 -143 1437 -217 O HETATM 3922 O HOH C 345 26.735 -7.303 5.035 1.00 61.21 O ANISOU 3922 O HOH C 345 7491 7970 7795 -68 851 328 O HETATM 3923 O HOH C 346 17.551 -0.505 15.021 1.00 46.35 O ANISOU 3923 O HOH C 346 6332 5978 5302 -187 351 329 O HETATM 3924 O HOH C 347 6.574 -9.678 14.769 1.00 42.62 O ANISOU 3924 O HOH C 347 5884 5136 5173 121 817 217 O HETATM 3925 O HOH C 348 21.957 -11.285 12.493 1.00 66.31 O ANISOU 3925 O HOH C 348 8322 8435 8438 213 625 595 O HETATM 3926 O HOH C 349 26.200 2.077 -4.221 1.00 48.81 O ANISOU 3926 O HOH C 349 6504 6458 5584 -633 1103 281 O HETATM 3927 O HOH C 350 12.247 -9.276 -7.619 1.00 57.79 O ANISOU 3927 O HOH C 350 7810 7486 6663 -124 989 -427 O HETATM 3928 O HOH C 351 12.276 -16.162 1.813 1.00 57.32 O ANISOU 3928 O HOH C 351 7424 6915 7438 143 1147 -225 O HETATM 3929 O HOH C 352 20.697 4.487 -14.390 1.00 55.07 O ANISOU 3929 O HOH C 352 8064 7415 5444 -701 1177 383 O HETATM 3930 O HOH C 353 1.178 -0.384 21.448 1.00 47.71 O ANISOU 3930 O HOH C 353 6861 5860 5408 27 794 -91 O HETATM 3931 O HOH C 354 8.715 -8.825 -10.161 1.00 53.87 O ANISOU 3931 O HOH C 354 7422 7108 5938 -148 828 -566 O HETATM 3932 O HOH C 355 11.734 16.120 4.478 1.00 46.47 O ANISOU 3932 O HOH C 355 7193 5129 5333 -360 326 328 O HETATM 3933 O HOH C 356 7.456 7.784 -14.478 1.00 56.94 O ANISOU 3933 O HOH C 356 8666 7479 5491 -143 192 545 O HETATM 3934 O HOH C 357 15.868 12.134 21.393 1.00 56.26 O ANISOU 3934 O HOH C 357 8138 7022 6218 -661 159 -213 O HETATM 3935 O HOH C 358 7.302 11.982 21.583 1.00 48.75 O ANISOU 3935 O HOH C 358 7358 5785 5381 -295 434 -378 O HETATM 3936 O HOH C 359 6.632 24.038 11.117 1.00 56.52 O ANISOU 3936 O HOH C 359 8788 5636 7051 -216 346 -94 O HETATM 3937 O HOH C 360 12.157 -11.602 7.482 1.00 55.31 O ANISOU 3937 O HOH C 360 7287 6770 6958 136 865 118 O HETATM 3938 O HOH C 361 19.661 13.700 13.815 1.00 79.41 O ANISOU 3938 O HOH C 361 10945 9775 9451 -796 237 31 O HETATM 3939 O HOH C 362 7.682 -11.846 -2.881 1.00 49.02 O ANISOU 3939 O HOH C 362 6580 6123 5924 -2 901 -466 O HETATM 3940 O HOH C 363 17.955 -4.103 17.487 1.00 48.26 O ANISOU 3940 O HOH C 363 6481 6285 5572 -61 346 484 O HETATM 3941 O HOH C 364 7.505 4.275 -17.222 1.00 75.19 O ANISOU 3941 O HOH C 364 10920 10096 7554 -209 270 301 O HETATM 3942 O HOH C 365 7.442 -8.731 12.592 1.00 45.56 O ANISOU 3942 O HOH C 365 6237 5531 5542 109 765 159 O HETATM 3943 O HOH C 366 -4.969 15.007 12.843 1.00 76.17 O ANISOU 3943 O HOH C 366 10630 8679 9633 460 412 -384 O HETATM 3944 O HOH C 367 -2.453 -6.734 -9.737 1.00 41.69 O ANISOU 3944 O HOH C 367 5757 5644 4440 19 182 -710 O HETATM 3945 O HOH C 368 30.987 -0.153 -9.846 1.00 85.35 O ANISOU 3945 O HOH C 368 10893 11351 10184 -788 1684 139 O HETATM 3946 O HOH C 369 9.979 -10.907 7.447 1.00 55.81 O ANISOU 3946 O HOH C 369 7409 6821 6976 117 843 55 O HETATM 3947 O HOH C 370 16.241 6.124 -13.820 1.00 57.19 O ANISOU 3947 O HOH C 370 8524 7564 5641 -531 826 478 O HETATM 3948 O HOH C 371 -4.625 2.032 -10.019 1.00 52.72 O ANISOU 3948 O HOH C 371 7396 6988 5648 300 -288 -163 O HETATM 3949 O HOH C 372 8.818 21.116 2.906 1.00 57.41 O ANISOU 3949 O HOH C 372 8873 6072 6870 -223 256 471 O HETATM 3950 O HOH C 373 10.272 25.965 11.035 1.00 58.30 O ANISOU 3950 O HOH C 373 9104 5761 7287 -516 377 -68 O HETATM 3951 O HOH C 374 8.587 -12.027 -7.749 1.00 56.44 O ANISOU 3951 O HOH C 374 7586 7250 6610 -94 956 -663 O HETATM 3952 O HOH C 375 -3.647 13.229 7.993 1.00 49.38 O ANISOU 3952 O HOH C 375 7210 5439 6112 448 217 -132 O HETATM 3953 O HOH C 377 5.850 9.579 -13.672 1.00 58.36 O ANISOU 3953 O HOH C 377 8886 7529 5761 -41 49 646 O HETATM 3954 O HOH C 378 28.961 1.095 -4.648 1.00 59.83 O ANISOU 3954 O HOH C 378 7685 7944 7102 -680 1250 253 O HETATM 3955 O HOH C 379 22.279 0.645 11.141 1.00 53.14 O ANISOU 3955 O HOH C 379 6987 6910 6292 -327 395 348 O HETATM 3956 O HOH C 380 22.474 4.539 9.564 1.00 60.07 O ANISOU 3956 O HOH C 380 8004 7708 7112 -506 401 294 O HETATM 3957 O HOH C 381 3.786 -0.204 21.048 1.00 54.09 O ANISOU 3957 O HOH C 381 7682 6714 6157 -9 688 -8 O HETATM 3958 O HOH C 382 -3.580 13.555 -3.604 1.00 53.27 O ANISOU 3958 O HOH C 382 7855 6195 6188 560 -266 387 O HETATM 3959 O HOH C 383 10.444 11.718 25.430 1.00 51.17 O ANISOU 3959 O HOH C 383 7691 6356 5395 -500 333 -423 O HETATM 3960 O HOH C 384 18.577 16.749 10.984 1.00 72.58 O ANISOU 3960 O HOH C 384 10277 8623 8677 -827 316 82 O HETATM 3961 O HOH C 385 16.161 7.569 22.046 1.00 53.97 O ANISOU 3961 O HOH C 385 7689 6956 5861 -510 147 -13 O HETATM 3962 O HOH C 386 18.249 13.910 11.513 1.00 59.62 O ANISOU 3962 O HOH C 386 8516 7159 6977 -712 300 97 O HETATM 3963 O HOH C 387 -4.370 2.070 14.599 1.00 51.37 O ANISOU 3963 O HOH C 387 7117 6120 6283 237 680 -333 O HETATM 3964 O HOH C 388 -0.084 -8.652 2.775 1.00 51.89 O ANISOU 3964 O HOH C 388 6928 6376 6414 94 661 -401 O HETATM 3965 O HOH C 389 15.447 8.344 -14.909 1.00 58.24 O ANISOU 3965 O HOH C 389 8838 7653 5637 -542 744 650 O HETATM 3966 O HOH C 390 11.524 -12.188 -7.969 1.00 58.44 O ANISOU 3966 O HOH C 390 7811 7509 6883 -103 1089 -610 O HETATM 3967 O HOH C 391 -2.059 -8.057 19.125 1.00 64.36 O ANISOU 3967 O HOH C 391 8703 7834 7917 81 1066 -19 O HETATM 3968 O HOH C 392 19.758 -13.050 1.269 1.00 58.49 O ANISOU 3968 O HOH C 392 7405 7311 7509 116 1135 -8 O HETATM 3969 O HOH C 393 -4.130 17.445 13.687 1.00 59.15 O ANISOU 3969 O HOH C 393 8604 6358 7511 428 431 -419 O HETATM 3970 O HOH C 394 13.733 -15.189 4.272 1.00 74.01 O ANISOU 3970 O HOH C 394 9522 9053 9545 180 1071 -25 O HETATM 3971 O HOH C 395 15.896 -14.558 2.505 1.00 68.71 O ANISOU 3971 O HOH C 395 8804 8464 8839 157 1105 -57 O HETATM 3972 O HOH C 396 25.210 -9.828 5.355 1.00 65.25 O ANISOU 3972 O HOH C 396 8022 8377 8392 66 898 317 O HETATM 3973 O HOH C 397 16.315 7.756 15.246 1.00 63.93 O ANISOU 3973 O HOH C 397 8883 8004 7404 -446 265 97 O HETATM 3974 O HOH D 3 -5.096 3.775 5.840 1.00 34.27 O ANISOU 3974 O HOH D 3 4226 4488 4309 -308 273 -7 O HETATM 3975 O HOH D 4 -5.163 6.198 7.258 1.00 34.59 O ANISOU 3975 O HOH D 4 4154 4549 4440 -423 641 -228 O HETATM 3976 O HOH D 75 -9.445 -4.710 8.724 1.00 48.25 O ANISOU 3976 O HOH D 75 6450 6554 5329 -1465 365 -229 O HETATM 3977 O HOH D 95 -11.484 3.506 -4.473 1.00 53.14 O ANISOU 3977 O HOH D 95 6403 5909 7878 59 -1595 547 O HETATM 3978 O HOH D 187 -7.109 8.691 4.666 1.00 60.93 O ANISOU 3978 O HOH D 187 7093 7544 8514 120 413 -388 O HETATM 3979 O HOH D 195 -15.139 9.245 1.988 1.00 61.30 O ANISOU 3979 O HOH D 195 5428 6862 11004 552 -316 -717 O HETATM 3980 O HOH D 209 -23.616 2.426 6.961 1.00 72.20 O ANISOU 3980 O HOH D 209 5266 8793 13374 -1018 1232 -2552 O HETATM 3981 O HOH D 219 -6.323 10.383 9.057 1.00 69.62 O ANISOU 3981 O HOH D 219 8295 8853 9304 -590 1437 -711 O HETATM 3982 O HOH D 224 -10.753 11.322 9.674 1.00 94.31 O ANISOU 3982 O HOH D 224 10511 11574 13747 -655 1971 -1383 O HETATM 3983 O HOH D 252 -20.847 6.725 -0.057 1.00 85.64 O ANISOU 3983 O HOH D 252 7247 9756 15535 478 -1181 -698 O HETATM 3984 O HOH D 272 -15.852 1.113 8.256 1.00 62.71 O ANISOU 3984 O HOH D 272 6402 8077 9350 -1208 1089 -1459 O HETATM 3985 O HOH D 275 -12.641 -0.239 -3.993 1.00 72.09 O ANISOU 3985 O HOH D 275 8845 8653 9892 -287 -1341 630 O HETATM 3986 O HOH D 287 -15.150 -2.286 9.743 1.00 61.89 O ANISOU 3986 O HOH D 287 7093 8249 8173 -1823 1145 -1417 O HETATM 3987 O HOH D 314 -5.161 9.151 6.740 1.00 51.05 O ANISOU 3987 O HOH D 314 7210 5885 6300 466 211 -184 O CONECT 128 3630 CONECT 1649 3661 CONECT 1670 3661 CONECT 1754 3661 CONECT 1772 3661 CONECT 1940 3662 CONECT 3466 3693 CONECT 3487 3693 CONECT 3571 3693 CONECT 3589 3693 CONECT 3630 128 3632 3716 3717 CONECT 3630 3718 3719 CONECT 3631 3632 3633 3634 3635 CONECT 3632 3630 3631 CONECT 3633 3631 CONECT 3634 3631 CONECT 3635 3631 3636 CONECT 3636 3635 3637 3638 3639 CONECT 3637 3636 CONECT 3638 3636 CONECT 3639 3636 3640 CONECT 3640 3639 3641 CONECT 3641 3640 3642 3643 CONECT 3642 3641 3647 CONECT 3643 3641 3644 3645 CONECT 3644 3643 CONECT 3645 3643 3646 3647 CONECT 3646 3645 CONECT 3647 3642 3645 3648 CONECT 3648 3647 3649 3658 CONECT 3649 3648 3650 CONECT 3650 3649 3651 CONECT 3651 3650 3652 3658 CONECT 3652 3651 3653 3654 CONECT 3653 3652 CONECT 3654 3652 3655 CONECT 3655 3654 3656 3657 CONECT 3656 3655 CONECT 3657 3655 3658 CONECT 3658 3648 3651 3657 CONECT 3661 1649 1670 1754 1772 CONECT 3662 1940 3664 3822 3823 CONECT 3662 3824 3825 CONECT 3663 3664 3665 3666 3667 CONECT 3664 3662 3663 CONECT 3665 3663 CONECT 3666 3663 CONECT 3667 3663 3668 CONECT 3668 3667 3669 3670 3671 CONECT 3669 3668 CONECT 3670 3668 CONECT 3671 3668 3672 CONECT 3672 3671 3673 CONECT 3673 3672 3674 3675 CONECT 3674 3673 3679 CONECT 3675 3673 3676 3677 CONECT 3676 3675 CONECT 3677 3675 3678 3679 CONECT 3678 3677 CONECT 3679 3674 3677 3680 CONECT 3680 3679 3681 3690 CONECT 3681 3680 3682 CONECT 3682 3681 3683 CONECT 3683 3682 3684 3690 CONECT 3684 3683 3685 3686 CONECT 3685 3684 CONECT 3686 3684 3687 CONECT 3687 3686 3688 3689 CONECT 3688 3687 CONECT 3689 3687 3690 CONECT 3690 3680 3683 3689 CONECT 3693 3466 3487 3571 3589 CONECT 3716 3630 CONECT 3717 3630 CONECT 3718 3630 CONECT 3719 3630 CONECT 3822 3662 CONECT 3823 3662 CONECT 3824 3662 CONECT 3825 3662 MASTER 528 0 10 22 21 0 21 6 3983 4 80 50 END
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Related entries of code: 3gj7
Entries with 90% protein sequence similarity cutoff in PDBbind
PDB Code
Check Database
Protein Sequence Similarity
3ch5
RCSB PDB
PDBbind
52aa, >3CH5_2|Chain... at 92%
3gj6
RCSB PDB
PDBbind
34aa, >3GJ6_2|Chain... at 100%
Complexes with the same small molecule ligand
PDB Code
Check Database
Ligand Name
No complexes with the same small molecule ligand are found!
Entry Information
PDB ID
3gj7
Complex Type
Protein-Protein
PDBbind Subset
general set
Protein Name
GTP-binding nuclear protein Ran
Ligand Name
98-mer
EC.Number
E.C.-.-.-.-
Resolution
1.93(Å)
Affinity (Kd/Ki/IC50)
Kd=4uM
Release Year
2009
Protein/NA Sequence
Check fasta file
Primary Reference
(2009) J.Mol.Biol. Vol. 391: pp. 375-389
Links to External Databases
RCSB PDB
The mother database
PDBsum
Enhanced annotations on PDB entries
Pubchem
Comprehensive collection of chemical and biological data
UniProtKB AC
UniProt accession number (AC):
P49791
P62826
Entrez Gene ID
NCBI Entrez Gene ID:
5901
ASD
Information of known allosteric effects of PDB entries
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娌叕缃戝畨澶囷細姝ｅ湪鐢宠涓