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*** SIGNALING PROTEIN 01-APR-11 3AXC ***elNémo ID: 240110220248539074Job options:ID = 240110220248539074 JOBID = SIGNALING PROTEIN 01-APR-11 3AXC USERID = unknown PRIVAT = 0 NMODES = 25 DQMIN = -100 DQMAX = 100 DQSTEP = 20 DOGRAPHS = on DOPROJMODS = 0 DORMSD = 0 NRBL = 0 CUTOFF = 0 CAONLY = 0 Input data for this run:HEADER SIGNALING PROTEIN 01-APR-11 3AXC TITLE CRYSTAL STRUCTURE OF LINEAR DIUBIQUITIN COMPND MOL_ID: 1; COMPND 2 MOLECULE: UBIQUITIN; COMPND 3 CHAIN: A; COMPND 4 ENGINEERED: YES; COMPND 5 OTHER_DETAILS: LINEAR DIUBIQUITIN SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606; SOURCE 5 GENE: RPS27A, UBA80, UBCEP1; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PGEX-4T-1 KEYWDS NF KAPPA B SIGNALING, SIGNALING PROTEIN EXPDTA X-RAY DIFFRACTION AUTHOR A.ROHAIM,M.KAWASAKI,R.KATO,I.DIKIC,S.WAKATSUKI REVDAT 4 01-NOV-23 3AXC 1 REMARK SEQADV REVDAT 3 09-AUG-17 3AXC 1 SOURCE REMARK REVDAT 2 25-APR-12 3AXC 1 JRNL REVDAT 1 25-JAN-12 3AXC 0 JRNL AUTH A.ROHAIM,M.KAWASAKI,R.KATO,I.DIKIC,S.WAKATSUKI JRNL TITL STRUCTURE OF A COMPACT CONFORMATION OF LINEAR DIUBIQUITIN JRNL REF ACTA CRYSTALLOGR.,SECT.D V. 68 102 2012 JRNL REFN ISSN 0907-4449 JRNL PMID 22281738 JRNL DOI 10.1107/S0907444911051195 REMARK 2 REMARK 2 RESOLUTION. 2.19 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC 5.5.0109 REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER, REMARK 3 : NICHOLLS,WINN,LONG,VAGIN REMARK 3 REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.19 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 32.26 REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL REMARK 3 COMPLETENESS FOR RANGE (%) : 97.4 REMARK 3 NUMBER OF REFLECTIONS : 6485 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM REMARK 3 R VALUE (WORKING + TEST SET) : 0.209 REMARK 3 R VALUE (WORKING SET) : 0.206 REMARK 3 FREE R VALUE : 0.278 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.800 REMARK 3 FREE R VALUE TEST SET COUNT : 325 REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : 20 REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.19 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.24 REMARK 3 REFLECTION IN BIN (WORKING SET) : 450 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 90.23 REMARK 3 BIN R VALUE (WORKING SET) : 0.2410 REMARK 3 BIN FREE R VALUE SET COUNT : 21 REMARK 3 BIN FREE R VALUE : 0.4430 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 1183 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 6 REMARK 3 SOLVENT ATOMS : 35 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 36.48 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 2.08000 REMARK 3 B22 (A**2) : -3.05000 REMARK 3 B33 (A**2) : 0.80000 REMARK 3 B12 (A**2) : -2.65000 REMARK 3 B13 (A**2) : 2.66000 REMARK 3 B23 (A**2) : -2.78000 REMARK 3 REMARK 3 ESTIMATED OVERALL COORDINATE ERROR. REMARK 3 ESU BASED ON R VALUE (A): NULL REMARK 3 ESU BASED ON FREE R VALUE (A): 0.271 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.211 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 18.216 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.950 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.915 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1201 ; 0.013 ; 0.022 REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 1616 ; 1.509 ; 2.000 REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 148 ; 6.760 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 53 ;34.683 ;25.849 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 245 ;18.624 ;15.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 7 ;16.890 ;15.000 REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 193 ; 0.110 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 859 ; 0.006 ; 0.021 REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL REMARK 3 REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 740 ; 0.675 ; 1.500 REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1209 ; 1.262 ; 2.000 REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 461 ; 1.997 ; 3.000 REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 407 ; 3.458 ; 4.500 REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 REMARK 3 NCS RESTRAINTS STATISTICS REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 1 REMARK 3 REMARK 3 TLS GROUP : 1 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : A 1 A 149 REMARK 3 ORIGIN FOR THE GROUP (A): -3.4089 9.4905 -9.3952 REMARK 3 T TENSOR REMARK 3 T11: 0.1371 T22: 0.1114 REMARK 3 T33: 0.1511 T12: -0.0176 REMARK 3 T13: 0.0384 T23: -0.0637 REMARK 3 L TENSOR REMARK 3 L11: 0.5482 L22: 1.2710 REMARK 3 L33: 1.9345 L12: -0.3073 REMARK 3 L13: 0.4975 L23: -1.5080 REMARK 3 S TENSOR REMARK 3 S11: 0.0134 S12: 0.0153 S13: -0.0974 REMARK 3 S21: -0.0662 S22: 0.0461 S23: -0.0009 REMARK 3 S31: 0.0236 S32: 0.0519 S33: -0.0595 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : MASK REMARK 3 PARAMETERS FOR MASK CALCULATION REMARK 3 VDW PROBE RADIUS : 1.40 REMARK 3 ION PROBE RADIUS : 0.80 REMARK 3 SHRINKAGE RADIUS : 0.80 REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING REMARK 3 POSITIONS REMARK 4 REMARK 4 3AXC COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 13-APR-11. REMARK 100 THE DEPOSITION ID IS D_1000029812. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 05-JUN-09 REMARK 200 TEMPERATURE (KELVIN) : 95 REMARK 200 PH : 7.5 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : PHOTON FACTORY REMARK 200 BEAMLINE : BL-5A REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.0000 REMARK 200 MONOCHROMATOR : SILICON 111 REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000 REMARK 200 DATA SCALING SOFTWARE : HKL-2000 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 6959 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.190 REMARK 200 RESOLUTION RANGE LOW (A) : 32.260 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 97.4 REMARK 200 DATA REDUNDANCY : NULL REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : NULL REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.19 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.24 REMARK 200 COMPLETENESS FOR SHELL (%) : NULL REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : NULL REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: MOLREP REMARK 200 STARTING MODEL: PDB ENTRY 1UBQ REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 39.12 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.02 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 30% PEG 4000, 0.1M TRIS-HCL, 0.1M REMARK 280 MGCL2, 30% DIOXANE, 30% ISOPROPANOL , PH 7.5, VAPOR DIFFUSION, REMARK 280 TEMPERATURE 289K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,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 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 APPLY THE FOLLOWING TO CHAINS: A REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 GLY A -1 REMARK 465 SER A 0 REMARK 465 ARG A 150 REMARK 465 GLY A 151 REMARK 465 GLY A 152 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS REMARK 500 REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15 REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375 REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS. REMARK 500 REMARK 500 DISTANCE CUTOFF: REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE REMARK 500 O HOH A 154 O HOH A 181 1556 1.22 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 GLU A 64 18.41 51.28 REMARK 500 ARG A 74 145.69 91.08 REMARK 500 MET A 77 105.44 -163.02 REMARK 500 REMARK 500 REMARK: NULL REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 153 DBREF 3AXC A 1 76 UNP P62979 RS27A_HUMAN 1 76 DBREF 3AXC A 77 152 UNP P62979 RS27A_HUMAN 1 76 SEQADV 3AXC GLY A -1 UNP P62979 EXPRESSION TAG SEQADV 3AXC SER A 0 UNP P62979 EXPRESSION TAG SEQRES 1 A 154 GLY SER MET GLN ILE PHE VAL LYS THR LEU THR GLY LYS SEQRES 2 A 154 THR ILE THR LEU GLU VAL GLU PRO SER ASP THR ILE GLU SEQRES 3 A 154 ASN VAL LYS ALA LYS ILE GLN ASP LYS GLU GLY ILE PRO SEQRES 4 A 154 PRO ASP GLN GLN ARG LEU ILE PHE ALA GLY LYS GLN LEU SEQRES 5 A 154 GLU ASP GLY ARG THR LEU SER ASP TYR ASN ILE GLN LYS SEQRES 6 A 154 GLU SER THR LEU HIS LEU VAL LEU ARG LEU ARG GLY GLY SEQRES 7 A 154 MET GLN ILE PHE VAL LYS THR LEU THR GLY LYS THR ILE SEQRES 8 A 154 THR LEU GLU VAL GLU PRO SER ASP THR ILE GLU ASN VAL SEQRES 9 A 154 LYS ALA LYS ILE GLN ASP LYS GLU GLY ILE PRO PRO ASP SEQRES 10 A 154 GLN GLN ARG LEU ILE PHE ALA GLY LYS GLN LEU GLU ASP SEQRES 11 A 154 GLY ARG THR LEU SER ASP TYR ASN ILE GLN LYS GLU SER SEQRES 12 A 154 THR LEU HIS LEU VAL LEU ARG LEU ARG GLY GLY HET GOL A 153 6 HETNAM GOL GLYCEROL HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL FORMUL 2 GOL C3 H8 O3 FORMUL 3 HOH *35(H2 O) HELIX 1 1 THR A 22 GLY A 35 1 14 HELIX 2 2 PRO A 37 ASP A 39 5 3 HELIX 3 3 THR A 98 GLY A 111 1 14 HELIX 4 4 PRO A 113 ASP A 115 5 3 HELIX 5 5 LEU A 132 ASN A 136 5 5 SHEET 1 A 5 THR A 12 GLU A 16 0 SHEET 2 A 5 GLN A 2 LYS A 6 -1 N VAL A 5 O ILE A 13 SHEET 3 A 5 THR A 66 LEU A 71 1 O LEU A 67 N PHE A 4 SHEET 4 A 5 GLN A 41 PHE A 45 -1 N ILE A 44 O HIS A 68 SHEET 5 A 5 LYS A 48 GLN A 49 -1 O LYS A 48 N PHE A 45 SHEET 1 B 5 THR A 88 GLU A 92 0 SHEET 2 B 5 GLN A 78 THR A 83 -1 N VAL A 81 O ILE A 89 SHEET 3 B 5 THR A 142 LEU A 147 1 O LEU A 143 N LYS A 82 SHEET 4 B 5 GLN A 117 PHE A 121 -1 N ILE A 120 O HIS A 144 SHEET 5 B 5 LYS A 124 GLN A 125 -1 O LYS A 124 N PHE A 121 SITE 1 AC1 9 GLU A 16 VAL A 17 ASP A 21 ASN A 25 SITE 2 AC1 9 LYS A 29 GLU A 94 ASP A 97 LYS A 105 SITE 3 AC1 9 HOH A 171 CRYST1 33.261 35.314 35.841 91.79 112.85 112.88 P 1 1 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 0.030065 0.012686 0.015754 0.00000 SCALE2 0.000000 0.030735 0.006751 0.00000 SCALE3 0.000000 0.000000 0.030998 0.00000 ATOM 1 N MET A 1 9.166 -10.955 2.551 1.00 41.47 N ANISOU 1 N MET A 1 4932 4889 5936 718 462 -116 N ATOM 2 CA MET A 1 9.020 -9.474 2.672 1.00 40.69 C ANISOU 2 CA MET A 1 4742 4887 5830 605 456 -117 C ATOM 3 C MET A 1 7.568 -9.057 2.946 1.00 39.07 C ANISOU 3 C MET A 1 4582 4630 5634 481 377 -179 C ATOM 4 O MET A 1 6.749 -8.916 2.034 1.00 39.32 O ANISOU 4 O MET A 1 4709 4593 5637 470 358 -246 O ATOM 5 CB MET A 1 9.586 -8.757 1.442 1.00 41.54 C ANISOU 5 CB MET A 1 4856 5041 5887 665 525 -126 C ATOM 6 CG MET A 1 9.504 -7.211 1.501 1.00 42.02 C ANISOU 6 CG MET A 1 4836 5191 5938 551 513 -123 C ATOM 7 SD MET A 1 10.422 -6.388 0.184 1.00 46.30 S ANISOU 7 SD MET A 1 5348 5816 6429 620 596 -96 S ATOM 8 CE MET A 1 9.732 -4.730 0.311 1.00 43.63 C ANISOU 8 CE MET A 1 4979 5516 6082 457 541 -131 C ATOM 9 N GLN A 2 7.277 -8.882 4.228 1.00 37.67 N ANISOU 9 N GLN A 2 4330 4491 5491 395 333 -143 N ATOM 10 CA GLN A 2 5.989 -8.429 4.733 1.00 35.92 C ANISOU 10 CA GLN A 2 4121 4250 5276 291 272 -169 C ATOM 11 C GLN A 2 5.989 -6.912 4.911 1.00 34.93 C ANISOU 11 C GLN A 2 3943 4208 5120 220 281 -173 C ATOM 12 O GLN A 2 6.979 -6.342 5.393 1.00 34.52 O ANISOU 12 O GLN A 2 3814 4240 5062 208 300 -126 O ATOM 13 CB GLN A 2 5.804 -9.038 6.110 1.00 36.65 C ANISOU 13 CB GLN A 2 4164 4351 5410 258 232 -115 C ATOM 14 CG GLN A 2 4.461 -9.594 6.387 1.00 36.10 C ANISOU 14 CG GLN A 2 4141 4211 5363 211 169 -121 C ATOM 15 CD GLN A 2 4.492 -10.615 7.491 1.00 36.83 C ANISOU 15 CD GLN A 2 4200 4293 5503 211 135 -61 C ATOM 16 OE1 GLN A 2 3.845 -11.646 7.385 1.00 39.68 O ANISOU 16 OE1 GLN A 2 4620 4565 5892 212 84 -54 O ATOM 17 NE2 GLN A 2 5.232 -10.338 8.564 1.00 36.79 N ANISOU 17 NE2 GLN A 2 4103 4373 5503 201 152 -11 N ATOM 18 N ILE A 3 4.891 -6.265 4.515 1.00 33.61 N ANISOU 18 N ILE A 3 3823 4015 4931 170 260 -219 N ATOM 19 CA ILE A 3 4.590 -4.880 4.936 1.00 32.45 C ANISOU 19 CA ILE A 3 3650 3927 4752 100 255 -223 C ATOM 20 C ILE A 3 3.210 -4.812 5.609 1.00 31.82 C ANISOU 20 C ILE A 3 3588 3827 4674 54 217 -219 C ATOM 21 O ILE A 3 2.355 -5.675 5.368 1.00 31.71 O ANISOU 21 O ILE A 3 3608 3753 4689 58 188 -218 O ATOM 22 CB ILE A 3 4.650 -3.862 3.764 1.00 32.36 C ANISOU 22 CB ILE A 3 3669 3925 4700 96 283 -268 C ATOM 23 CG1 ILE A 3 3.667 -4.250 2.643 1.00 30.90 C ANISOU 23 CG1 ILE A 3 3565 3662 4512 113 275 -320 C ATOM 24 CG2 ILE A 3 6.071 -3.755 3.229 1.00 32.72 C ANISOU 24 CG2 ILE A 3 3673 4021 4740 141 327 -243 C ATOM 25 CD1 ILE A 3 3.484 -3.181 1.593 1.00 30.41 C ANISOU 25 CD1 ILE A 3 3534 3611 4411 99 296 -364 C ATOM 26 N PHE A 4 3.011 -3.789 6.444 1.00 30.82 N ANISOU 26 N PHE A 4 3446 3752 4512 12 214 -205 N ATOM 27 CA PHE A 4 1.758 -3.570 7.178 1.00 30.34 C ANISOU 27 CA PHE A 4 3395 3694 4437 -8 197 -184 C ATOM 28 C PHE A 4 1.072 -2.296 6.719 1.00 29.89 C ANISOU 28 C PHE A 4 3380 3647 4329 -24 214 -215 C ATOM 29 O PHE A 4 1.643 -1.208 6.797 1.00 30.59 O ANISOU 29 O PHE A 4 3488 3764 4370 -40 224 -235 O ATOM 30 CB PHE A 4 2.006 -3.518 8.698 1.00 29.93 C ANISOU 30 CB PHE A 4 3313 3689 4370 -18 186 -135 C ATOM 31 CG PHE A 4 2.830 -4.686 9.215 1.00 30.92 C ANISOU 31 CG PHE A 4 3389 3814 4546 -3 172 -97 C ATOM 32 CD1 PHE A 4 4.125 -4.492 9.671 1.00 32.87 C ANISOU 32 CD1 PHE A 4 3603 4102 4785 -12 171 -77 C ATOM 33 CD2 PHE A 4 2.319 -5.975 9.201 1.00 28.78 C ANISOU 33 CD2 PHE A 4 3106 3498 4331 14 152 -71 C ATOM 34 CE1 PHE A 4 4.898 -5.574 10.119 1.00 34.54 C ANISOU 34 CE1 PHE A 4 3762 4318 5044 10 164 -32 C ATOM 35 CE2 PHE A 4 3.087 -7.072 9.655 1.00 32.79 C ANISOU 35 CE2 PHE A 4 3577 3997 4884 37 140 -35 C ATOM 36 CZ PHE A 4 4.376 -6.867 10.106 1.00 32.41 C ANISOU 36 CZ PHE A 4 3489 3998 4828 41 153 -17 C ATOM 37 N VAL A 5 -0.140 -2.450 6.211 1.00 29.30 N ANISOU 37 N VAL A 5 3322 3547 4266 -24 208 -210 N ATOM 38 CA VAL A 5 -0.977 -1.336 5.820 1.00 28.70 C ANISOU 38 CA VAL A 5 3278 3482 4145 -29 226 -224 C ATOM 39 C VAL A 5 -2.078 -1.142 6.865 1.00 29.76 C ANISOU 39 C VAL A 5 3398 3651 4256 -12 233 -158 C ATOM 40 O VAL A 5 -2.916 -2.034 7.082 1.00 29.65 O ANISOU 40 O VAL A 5 3345 3636 4286 -13 212 -95 O ATOM 41 CB VAL A 5 -1.620 -1.593 4.457 1.00 28.88 C ANISOU 41 CB VAL A 5 3321 3459 4191 -39 214 -246 C ATOM 42 CG1 VAL A 5 -2.417 -0.344 4.016 1.00 26.32 C ANISOU 42 CG1 VAL A 5 3026 3155 3822 -41 238 -256 C ATOM 43 CG2 VAL A 5 -0.554 -1.967 3.423 1.00 26.26 C ANISOU 43 CG2 VAL A 5 3013 3092 3874 -31 216 -303 C ATOM 44 N LYS A 6 -2.065 0.001 7.533 1.00 29.91 N ANISOU 44 N LYS A 6 3458 3704 4203 8 261 -163 N ATOM 45 CA LYS A 6 -2.988 0.225 8.633 1.00 31.13 C ANISOU 45 CA LYS A 6 3614 3899 4316 52 283 -96 C ATOM 46 C LYS A 6 -4.069 1.260 8.287 1.00 31.70 C ANISOU 46 C LYS A 6 3722 3987 4335 90 323 -82 C ATOM 47 O LYS A 6 -3.778 2.284 7.700 1.00 31.75 O ANISOU 47 O LYS A 6 3792 3975 4299 86 334 -143 O ATOM 48 CB LYS A 6 -2.216 0.623 9.901 1.00 31.64 C ANISOU 48 CB LYS A 6 3720 3982 4319 65 282 -100 C ATOM 49 CG LYS A 6 -1.194 -0.452 10.361 1.00 32.41 C ANISOU 49 CG LYS A 6 3765 4077 4472 32 246 -92 C ATOM 50 CD LYS A 6 -0.642 -0.159 11.729 1.00 33.83 C ANISOU 50 CD LYS A 6 3983 4281 4592 41 236 -74 C ATOM 51 CE LYS A 6 -1.667 -0.442 12.836 1.00 34.86 C ANISOU 51 CE LYS A 6 4103 4450 4691 100 261 2 C ATOM 52 NZ LYS A 6 -1.048 -0.197 14.176 1.00 38.21 N ANISOU 52 NZ LYS A 6 4581 4892 5045 109 245 14 N ATOM 53 N THR A 7 -5.307 0.966 8.654 1.00 32.74 N ANISOU 53 N THR A 7 3808 4160 4474 130 343 12 N ATOM 54 CA THR A 7 -6.453 1.848 8.434 1.00 34.57 C ANISOU 54 CA THR A 7 4055 4424 4657 186 391 58 C ATOM 55 C THR A 7 -6.609 2.818 9.605 1.00 35.75 C ANISOU 55 C THR A 7 4285 4605 4694 279 448 75 C ATOM 56 O THR A 7 -5.961 2.636 10.646 1.00 37.14 O ANISOU 56 O THR A 7 4492 4782 4837 290 439 66 O ATOM 57 CB THR A 7 -7.747 1.023 8.334 1.00 35.04 C ANISOU 57 CB THR A 7 4009 4528 4777 188 384 187 C ATOM 58 OG1 THR A 7 -8.147 0.620 9.647 1.00 36.46 O ANISOU 58 OG1 THR A 7 4149 4767 4937 244 409 284 O ATOM 59 CG2 THR A 7 -7.523 -0.212 7.493 1.00 35.15 C ANISOU 59 CG2 THR A 7 3970 4492 4893 94 307 177 C ATOM 60 N LEU A 8 -7.482 3.814 9.446 1.00 36.47 N ANISOU 60 N LEU A 8 4419 4717 4719 353 504 105 N ATOM 61 CA LEU A 8 -7.801 4.805 10.497 1.00 37.43 C ANISOU 61 CA LEU A 8 4649 4861 4713 471 568 127 C ATOM 62 C LEU A 8 -8.105 4.229 11.888 1.00 38.02 C ANISOU 62 C LEU A 8 4698 4992 4754 542 596 217 C ATOM 63 O LEU A 8 -7.670 4.794 12.885 1.00 38.75 O ANISOU 63 O LEU A 8 4912 5068 4741 600 612 185 O ATOM 64 CB LEU A 8 -8.951 5.742 10.057 1.00 37.98 C ANISOU 64 CB LEU A 8 4741 4960 4728 563 638 181 C ATOM 65 CG LEU A 8 -10.436 5.399 10.247 1.00 38.95 C ANISOU 65 CG LEU A 8 4751 5181 4867 648 700 349 C ATOM 66 CD1 LEU A 8 -11.323 6.612 9.942 1.00 39.21 C ANISOU 66 CD1 LEU A 8 4845 5236 4817 762 780 388 C ATOM 67 CD2 LEU A 8 -10.847 4.196 9.384 1.00 39.48 C ANISOU 67 CD2 LEU A 8 4651 5271 5077 538 638 416 C ATOM 68 N THR A 9 -8.842 3.115 11.933 1.00 37.98 N ANISOU 68 N THR A 9 4546 5050 4837 529 592 332 N ATOM 69 CA THR A 9 -9.236 2.445 13.178 1.00 38.88 C ANISOU 69 CA THR A 9 4606 5232 4934 591 618 442 C ATOM 70 C THR A 9 -8.130 1.545 13.763 1.00 38.54 C ANISOU 70 C THR A 9 4552 5156 4934 513 552 391 C ATOM 71 O THR A 9 -8.352 0.840 14.759 1.00 38.02 O ANISOU 71 O THR A 9 4432 5143 4871 546 561 479 O ATOM 72 CB THR A 9 -10.477 1.546 12.959 1.00 39.31 C ANISOU 72 CB THR A 9 4490 5370 5078 588 622 611 C ATOM 73 OG1 THR A 9 -10.179 0.578 11.943 1.00 40.39 O ANISOU 73 OG1 THR A 9 4546 5456 5346 445 529 582 O ATOM 74 CG2 THR A 9 -11.661 2.364 12.529 1.00 39.11 C ANISOU 74 CG2 THR A 9 4449 5401 5011 677 694 701 C ATOM 75 N GLY A 10 -6.960 1.548 13.123 1.00 37.93 N ANISOU 75 N GLY A 10 4516 5001 4895 415 490 264 N ATOM 76 CA GLY A 10 -5.845 0.694 13.549 1.00 38.27 C ANISOU 76 CA GLY A 10 4538 5016 4987 342 430 224 C ATOM 77 C GLY A 10 -5.920 -0.736 13.045 1.00 38.37 C ANISOU 77 C GLY A 10 4421 5024 5132 265 378 267 C ATOM 78 O GLY A 10 -5.109 -1.576 13.441 1.00 39.29 O ANISOU 78 O GLY A 10 4511 5124 5295 220 335 253 O ATOM 79 N LYS A 11 -6.890 -1.029 12.184 1.00 38.02 N ANISOU 79 N LYS A 11 4307 4991 5147 249 374 326 N ATOM 80 CA LYS A 11 -6.900 -2.298 11.443 1.00 37.93 C ANISOU 80 CA LYS A 11 4216 4943 5253 161 302 347 C ATOM 81 C LYS A 11 -5.638 -2.448 10.605 1.00 36.28 C ANISOU 81 C LYS A 11 4056 4653 5077 98 261 216 C ATOM 82 O LYS A 11 -5.265 -1.537 9.869 1.00 35.62 O ANISOU 82 O LYS A 11 4035 4543 4957 95 278 130 O ATOM 83 CB LYS A 11 -8.129 -2.400 10.526 1.00 38.55 C ANISOU 83 CB LYS A 11 4237 5036 5376 140 289 428 C ATOM 84 CG LYS A 11 -9.206 -3.332 11.049 1.00 42.36 C ANISOU 84 CG LYS A 11 4605 5577 5911 133 264 599 C ATOM 85 CD LYS A 11 -10.486 -3.272 10.200 1.00 48.38 C ANISOU 85 CD LYS A 11 5304 6369 6709 108 246 707 C ATOM 86 CE LYS A 11 -10.393 -4.131 8.952 1.00 49.19 C ANISOU 86 CE LYS A 11 5412 6379 6900 -12 139 673 C ATOM 87 NZ LYS A 11 -11.773 -4.552 8.569 1.00 51.76 N ANISOU 87 NZ LYS A 11 5640 6748 7280 -63 85 846 N ATOM 88 N THR A 12 -4.973 -3.589 10.753 1.00 35.59 N ANISOU 88 N THR A 12 3937 4531 5053 56 212 211 N ATOM 89 CA THR A 12 -3.801 -3.932 9.961 1.00 34.11 C ANISOU 89 CA THR A 12 3783 4276 4901 15 181 113 C ATOM 90 C THR A 12 -4.193 -4.852 8.811 1.00 33.98 C ANISOU 90 C THR A 12 3758 4196 4958 -32 126 118 C ATOM 91 O THR A 12 -4.946 -5.834 8.997 1.00 34.16 O ANISOU 91 O THR A 12 3735 4211 5035 -58 78 207 O ATOM 92 CB THR A 12 -2.746 -4.617 10.830 1.00 34.41 C ANISOU 92 CB THR A 12 3805 4313 4957 14 166 109 C ATOM 93 OG1 THR A 12 -2.363 -3.725 11.883 1.00 34.64 O ANISOU 93 OG1 THR A 12 3863 4391 4907 46 200 103 O ATOM 94 CG2 THR A 12 -1.508 -5.009 10.026 1.00 33.70 C ANISOU 94 CG2 THR A 12 3736 4166 4900 -7 147 30 C ATOM 95 N ILE A 13 -3.722 -4.513 7.615 1.00 32.52 N ANISOU 95 N ILE A 13 3625 3962 4767 -45 126 30 N ATOM 96 CA ILE A 13 -3.698 -5.478 6.548 1.00 32.20 C ANISOU 96 CA ILE A 13 3615 3840 4780 -79 70 9 C ATOM 97 C ILE A 13 -2.239 -5.854 6.207 1.00 32.66 C ANISOU 97 C ILE A 13 3712 3855 4842 -56 79 -73 C ATOM 98 O ILE A 13 -1.425 -5.019 5.764 1.00 32.27 O ANISOU 98 O ILE A 13 3687 3822 4755 -37 123 -141 O ATOM 99 CB ILE A 13 -4.597 -5.102 5.329 1.00 32.23 C ANISOU 99 CB ILE A 13 3650 3816 4779 -109 49 4 C ATOM 100 CG1 ILE A 13 -3.843 -5.171 4.018 1.00 31.30 C ANISOU 100 CG1 ILE A 13 3612 3627 4654 -109 42 -96 C ATOM 101 CG2 ILE A 13 -5.388 -3.785 5.525 1.00 31.10 C ANISOU 101 CG2 ILE A 13 3482 3749 4586 -90 102 34 C ATOM 102 CD1 ILE A 13 -4.712 -5.606 2.904 1.00 34.46 C ANISOU 102 CD1 ILE A 13 4059 3961 5073 -157 -25 -82 C ATOM 103 N THR A 14 -1.881 -7.105 6.459 1.00 33.56 N ANISOU 103 N THR A 14 3825 3922 5002 -54 40 -51 N ATOM 104 CA THR A 14 -0.516 -7.530 6.140 1.00 34.20 C ANISOU 104 CA THR A 14 3937 3972 5087 -12 59 -108 C ATOM 105 C THR A 14 -0.345 -8.194 4.779 1.00 35.54 C ANISOU 105 C THR A 14 4198 4044 5262 6 34 -161 C ATOM 106 O THR A 14 -1.084 -9.117 4.389 1.00 36.34 O ANISOU 106 O THR A 14 4353 4063 5391 -22 -38 -138 O ATOM 107 CB THR A 14 0.204 -8.275 7.272 1.00 34.04 C ANISOU 107 CB THR A 14 3869 3970 5095 8 58 -67 C ATOM 108 OG1 THR A 14 0.833 -9.453 6.744 1.00 36.87 O ANISOU 108 OG1 THR A 14 4278 4247 5484 45 36 -84 O ATOM 109 CG2 THR A 14 -0.725 -8.626 8.361 1.00 31.70 C ANISOU 109 CG2 THR A 14 3519 3702 4823 -24 24 19 C ATOM 110 N LEU A 15 0.657 -7.690 4.066 1.00 36.03 N ANISOU 110 N LEU A 15 4284 4116 5289 53 88 -224 N ATOM 111 CA LEU A 15 0.877 -8.017 2.667 1.00 37.16 C ANISOU 111 CA LEU A 15 4527 4183 5411 90 87 -283 C ATOM 112 C LEU A 15 2.268 -8.590 2.450 1.00 37.78 C ANISOU 112 C LEU A 15 4623 4249 5481 181 134 -301 C ATOM 113 O LEU A 15 3.249 -8.034 2.953 1.00 37.58 O ANISOU 113 O LEU A 15 4517 4310 5450 205 191 -285 O ATOM 114 CB LEU A 15 0.747 -6.735 1.851 1.00 36.75 C ANISOU 114 CB LEU A 15 4479 4170 5314 77 124 -328 C ATOM 115 CG LEU A 15 -0.545 -6.349 1.128 1.00 38.33 C ANISOU 115 CG LEU A 15 4722 4339 5504 19 81 -334 C ATOM 116 CD1 LEU A 15 -1.778 -7.208 1.444 1.00 39.72 C ANISOU 116 CD1 LEU A 15 4910 4461 5721 -41 -8 -271 C ATOM 117 CD2 LEU A 15 -0.809 -4.888 1.374 1.00 38.14 C ANISOU 117 CD2 LEU A 15 4636 4403 5453 -8 124 -333 C ATOM 118 N GLU A 16 2.344 -9.695 1.702 1.00 38.24 N ANISOU 118 N GLU A 16 4796 4199 5534 235 106 -325 N ATOM 119 CA GLU A 16 3.621 -10.225 1.217 1.00 39.10 C ANISOU 119 CA GLU A 16 4946 4291 5618 354 167 -342 C ATOM 120 C GLU A 16 3.948 -9.567 -0.112 1.00 38.43 C ANISOU 120 C GLU A 16 4919 4211 5472 405 220 -398 C ATOM 121 O GLU A 16 3.168 -9.670 -1.077 1.00 37.73 O ANISOU 121 O GLU A 16 4947 4037 5352 387 175 -445 O ATOM 122 CB GLU A 16 3.567 -11.752 1.017 1.00 40.42 C ANISOU 122 CB GLU A 16 5244 4324 5791 410 115 -345 C ATOM 123 CG GLU A 16 3.764 -12.541 2.286 1.00 43.89 C ANISOU 123 CG GLU A 16 5619 4771 6288 404 92 -281 C ATOM 124 CD GLU A 16 5.233 -12.778 2.626 1.00 46.99 C ANISOU 124 CD GLU A 16 5950 5224 6679 516 180 -250 C ATOM 125 OE1 GLU A 16 5.495 -13.377 3.708 1.00 48.87 O ANISOU 125 OE1 GLU A 16 6124 5480 6965 513 165 -193 O ATOM 126 OE2 GLU A 16 6.109 -12.377 1.816 1.00 45.83 O ANISOU 126 OE2 GLU A 16 5813 5116 6486 608 262 -270 O ATOM 127 N VAL A 17 5.107 -8.913 -0.165 1.00 37.42 N ANISOU 127 N VAL A 17 4707 4183 5325 463 308 -380 N ATOM 128 CA VAL A 17 5.447 -8.070 -1.297 1.00 36.82 C ANISOU 128 CA VAL A 17 4650 4143 5195 499 364 -415 C ATOM 129 C VAL A 17 6.878 -8.296 -1.778 1.00 37.88 C ANISOU 129 C VAL A 17 4769 4326 5298 638 460 -383 C ATOM 130 O VAL A 17 7.639 -9.038 -1.168 1.00 38.79 O ANISOU 130 O VAL A 17 4847 4456 5436 705 485 -330 O ATOM 131 CB VAL A 17 5.227 -6.559 -0.959 1.00 35.95 C ANISOU 131 CB VAL A 17 4431 4136 5092 397 369 -405 C ATOM 132 CG1 VAL A 17 3.745 -6.250 -0.770 1.00 33.15 C ANISOU 132 CG1 VAL A 17 4105 3739 4752 289 295 -431 C ATOM 133 CG2 VAL A 17 6.060 -6.135 0.280 1.00 34.44 C ANISOU 133 CG2 VAL A 17 4100 4052 4935 369 390 -334 C ATOM 134 N GLU A 18 7.214 -7.663 -2.898 1.00 37.82 N ANISOU 134 N GLU A 18 4786 4349 5235 688 516 -404 N ATOM 135 CA GLU A 18 8.557 -7.671 -3.456 1.00 38.86 C ANISOU 135 CA GLU A 18 4881 4556 5330 825 620 -352 C ATOM 136 C GLU A 18 8.919 -6.229 -3.809 1.00 38.38 C ANISOU 136 C GLU A 18 4710 4615 5256 771 657 -325 C ATOM 137 O GLU A 18 8.034 -5.429 -4.090 1.00 36.37 O ANISOU 137 O GLU A 18 4480 4343 4996 670 612 -379 O ATOM 138 CB GLU A 18 8.610 -8.552 -4.703 1.00 39.86 C ANISOU 138 CB GLU A 18 5190 4577 5378 975 656 -403 C ATOM 139 CG GLU A 18 8.298 -10.021 -4.423 1.00 42.69 C ANISOU 139 CG GLU A 18 5686 4794 5739 1032 608 -429 C ATOM 140 CD GLU A 18 8.448 -10.911 -5.641 1.00 45.50 C ANISOU 140 CD GLU A 18 6260 5030 5999 1197 641 -481 C ATOM 141 OE1 GLU A 18 8.784 -12.099 -5.469 1.00 48.69 O ANISOU 141 OE1 GLU A 18 6763 5348 6388 1309 646 -472 O ATOM 142 OE2 GLU A 18 8.228 -10.433 -6.770 1.00 46.48 O ANISOU 142 OE2 GLU A 18 6469 5137 6054 1220 659 -531 O ATOM 143 N PRO A 19 10.223 -5.888 -3.788 1.00 39.30 N ANISOU 143 N PRO A 19 4703 4858 5372 834 734 -226 N ATOM 144 CA PRO A 19 10.692 -4.544 -4.132 1.00 38.82 C ANISOU 144 CA PRO A 19 4534 4914 5301 779 760 -178 C ATOM 145 C PRO A 19 10.116 -3.980 -5.430 1.00 38.40 C ANISOU 145 C PRO A 19 4575 4825 5189 785 773 -252 C ATOM 146 O PRO A 19 9.789 -2.797 -5.470 1.00 37.41 O ANISOU 146 O PRO A 19 4402 4741 5070 671 740 -260 O ATOM 147 CB PRO A 19 12.200 -4.742 -4.275 1.00 40.12 C ANISOU 147 CB PRO A 19 4588 5199 5458 903 855 -46 C ATOM 148 CG PRO A 19 12.504 -5.722 -3.234 1.00 41.24 C ANISOU 148 CG PRO A 19 4701 5325 5645 932 843 -5 C ATOM 149 CD PRO A 19 11.338 -6.719 -3.304 1.00 40.76 C ANISOU 149 CD PRO A 19 4821 5092 5572 947 792 -131 C ATOM 150 N SER A 20 10.008 -4.809 -6.472 1.00 39.08 N ANISOU 150 N SER A 20 4807 4829 5212 921 815 -304 N ATOM 151 CA SER A 20 9.538 -4.349 -7.785 1.00 38.86 C ANISOU 151 CA SER A 20 4881 4768 5118 941 830 -369 C ATOM 152 C SER A 20 8.020 -4.372 -7.985 1.00 37.52 C ANISOU 152 C SER A 20 4842 4467 4945 837 732 -483 C ATOM 153 O SER A 20 7.542 -4.171 -9.104 1.00 37.43 O ANISOU 153 O SER A 20 4940 4408 4875 856 732 -543 O ATOM 154 CB SER A 20 10.216 -5.142 -8.903 1.00 40.58 C ANISOU 154 CB SER A 20 5208 4964 5248 1149 927 -362 C ATOM 155 OG SER A 20 9.738 -6.478 -8.922 1.00 41.62 O ANISOU 155 OG SER A 20 5518 4942 5353 1223 894 -431 O ATOM 156 N ASP A 21 7.266 -4.656 -6.920 1.00 36.77 N ANISOU 156 N ASP A 21 4737 4321 4913 731 648 -501 N ATOM 157 CA ASP A 21 5.809 -4.511 -6.960 1.00 35.27 C ANISOU 157 CA ASP A 21 4625 4041 4735 614 553 -572 C ATOM 158 C ASP A 21 5.446 -3.051 -6.932 1.00 34.03 C ANISOU 158 C ASP A 21 4378 3961 4592 501 543 -569 C ATOM 159 O ASP A 21 6.010 -2.269 -6.154 1.00 34.03 O ANISOU 159 O ASP A 21 4244 4061 4626 452 559 -512 O ATOM 160 CB ASP A 21 5.147 -5.205 -5.787 1.00 35.25 C ANISOU 160 CB ASP A 21 4617 3981 4794 544 476 -567 C ATOM 161 CG ASP A 21 5.229 -6.700 -5.882 1.00 36.96 C ANISOU 161 CG ASP A 21 4960 4087 4996 636 458 -582 C ATOM 162 OD1 ASP A 21 5.217 -7.246 -7.021 1.00 39.65 O ANISOU 162 OD1 ASP A 21 5459 4341 5266 726 467 -630 O ATOM 163 OD2 ASP A 21 5.309 -7.327 -4.807 1.00 36.28 O ANISOU 163 OD2 ASP A 21 4828 3994 4962 621 432 -546 O ATOM 164 N THR A 22 4.493 -2.687 -7.777 1.00 33.03 N ANISOU 164 N THR A 22 4336 3781 4435 457 506 -626 N ATOM 165 CA THR A 22 4.051 -1.326 -7.893 1.00 31.90 C ANISOU 165 CA THR A 22 4130 3694 4296 363 498 -628 C ATOM 166 C THR A 22 3.039 -1.028 -6.805 1.00 31.60 C ANISOU 166 C THR A 22 4048 3645 4312 249 429 -622 C ATOM 167 O THR A 22 2.526 -1.938 -6.146 1.00 31.01 O ANISOU 167 O THR A 22 4000 3511 4269 235 380 -619 O ATOM 168 CB THR A 22 3.349 -1.102 -9.220 1.00 32.09 C ANISOU 168 CB THR A 22 4262 3664 4267 362 483 -684 C ATOM 169 OG1 THR A 22 2.244 -2.001 -9.312 1.00 31.64 O ANISOU 169 OG1 THR A 22 4319 3489 4212 331 400 -721 O ATOM 170 CG2 THR A 22 4.298 -1.336 -10.409 1.00 33.94 C ANISOU 170 CG2 THR A 22 4556 3912 4428 493 561 -690 C ATOM 171 N ILE A 23 2.710 0.256 -6.660 1.00 31.33 N ANISOU 171 N ILE A 23 3957 3666 4282 173 426 -615 N ATOM 172 CA ILE A 23 1.642 0.679 -5.765 1.00 30.40 C ANISOU 172 CA ILE A 23 3814 3542 4196 87 375 -606 C ATOM 173 C ILE A 23 0.302 0.173 -6.279 1.00 30.38 C ANISOU 173 C ILE A 23 3890 3459 4194 57 318 -629 C ATOM 174 O ILE A 23 -0.531 -0.260 -5.489 1.00 30.42 O ANISOU 174 O ILE A 23 3884 3439 4235 17 270 -601 O ATOM 175 CB ILE A 23 1.649 2.213 -5.559 1.00 29.59 C ANISOU 175 CB ILE A 23 3657 3504 4081 32 389 -594 C ATOM 176 CG1 ILE A 23 2.968 2.636 -4.919 1.00 30.66 C ANISOU 176 CG1 ILE A 23 3717 3712 4220 37 418 -552 C ATOM 177 CG2 ILE A 23 0.454 2.686 -4.692 1.00 29.42 C ANISOU 177 CG2 ILE A 23 3628 3474 4075 -28 352 -581 C ATOM 178 CD1 ILE A 23 3.416 1.767 -3.732 1.00 32.06 C ANISOU 178 CD1 ILE A 23 3854 3894 4433 51 407 -516 C ATOM 179 N GLU A 24 0.106 0.187 -7.591 1.00 30.81 N ANISOU 179 N GLU A 24 4022 3475 4208 74 316 -667 N ATOM 180 CA GLU A 24 -1.122 -0.359 -8.173 1.00 31.56 C ANISOU 180 CA GLU A 24 4205 3488 4301 33 242 -677 C ATOM 181 C GLU A 24 -1.299 -1.809 -7.738 1.00 31.80 C ANISOU 181 C GLU A 24 4290 3437 4355 43 184 -666 C ATOM 182 O GLU A 24 -2.400 -2.220 -7.305 1.00 32.39 O ANISOU 182 O GLU A 24 4366 3475 4467 -27 108 -626 O ATOM 183 CB GLU A 24 -1.108 -0.267 -9.702 1.00 32.51 C ANISOU 183 CB GLU A 24 4425 3568 4358 60 245 -725 C ATOM 184 CG GLU A 24 -2.215 -1.112 -10.369 1.00 36.67 C ANISOU 184 CG GLU A 24 5074 3986 4873 16 146 -733 C ATOM 185 CD GLU A 24 -2.218 -1.043 -11.911 1.00 42.56 C ANISOU 185 CD GLU A 24 5945 4684 5544 44 140 -784 C ATOM 186 OE1 GLU A 24 -1.209 -1.430 -12.560 1.00 40.31 O ANISOU 186 OE1 GLU A 24 5737 4381 5199 149 195 -826 O ATOM 187 OE2 GLU A 24 -3.266 -0.626 -12.463 1.00 44.95 O ANISOU 187 OE2 GLU A 24 6268 4969 5842 -35 82 -772 O ATOM 188 N ASN A 25 -0.225 -2.582 -7.839 1.00 30.89 N ANISOU 188 N ASN A 25 4217 3299 4220 133 221 -686 N ATOM 189 CA ASN A 25 -0.243 -3.959 -7.357 1.00 30.79 C ANISOU 189 CA ASN A 25 4263 3205 4229 154 171 -675 C ATOM 190 C ASN A 25 -0.670 -4.062 -5.885 1.00 30.22 C ANISOU 190 C ASN A 25 4084 3170 4229 92 142 -615 C ATOM 191 O ASN A 25 -1.541 -4.864 -5.552 1.00 30.81 O ANISOU 191 O ASN A 25 4193 3178 4335 39 57 -584 O ATOM 192 CB ASN A 25 1.130 -4.633 -7.546 1.00 31.22 C ANISOU 192 CB ASN A 25 4359 3254 4251 284 241 -694 C ATOM 193 CG ASN A 25 1.086 -6.124 -7.254 1.00 30.31 C ANISOU 193 CG ASN A 25 4344 3028 4144 319 184 -692 C ATOM 194 OD1 ASN A 25 0.464 -6.882 -7.988 1.00 31.50 O ANISOU 194 OD1 ASN A 25 4652 3055 4259 312 106 -722 O ATOM 195 ND2 ASN A 25 1.707 -6.537 -6.173 1.00 27.70 N ANISOU 195 ND2 ASN A 25 3932 2735 3858 348 211 -653 N ATOM 196 N VAL A 26 -0.056 -3.258 -5.010 1.00 29.58 N ANISOU 196 N VAL A 26 3880 3192 4168 96 205 -592 N ATOM 197 CA VAL A 26 -0.393 -3.274 -3.573 1.00 28.67 C ANISOU 197 CA VAL A 26 3673 3117 4104 51 187 -537 C ATOM 198 C VAL A 26 -1.888 -2.976 -3.376 1.00 27.81 C ANISOU 198 C VAL A 26 3548 3002 4015 -33 128 -497 C ATOM 199 O VAL A 26 -2.573 -3.678 -2.638 1.00 28.07 O ANISOU 199 O VAL A 26 3562 3014 4089 -68 74 -443 O ATOM 200 CB VAL A 26 0.431 -2.271 -2.763 1.00 28.74 C ANISOU 200 CB VAL A 26 3579 3227 4112 56 250 -521 C ATOM 201 CG1 VAL A 26 -0.072 -2.217 -1.315 1.00 27.64 C ANISOU 201 CG1 VAL A 26 3371 3123 4007 14 228 -468 C ATOM 202 CG2 VAL A 26 1.927 -2.615 -2.816 1.00 28.04 C ANISOU 202 CG2 VAL A 26 3475 3166 4015 132 304 -523 C ATOM 203 N LYS A 27 -2.394 -1.966 -4.072 1.00 26.64 N ANISOU 203 N LYS A 27 3403 2879 3840 -60 140 -512 N ATOM 204 CA LYS A 27 -3.825 -1.651 -4.044 1.00 26.52 C ANISOU 204 CA LYS A 27 3368 2867 3840 -127 92 -459 C ATOM 205 C LYS A 27 -4.713 -2.819 -4.528 1.00 27.89 C ANISOU 205 C LYS A 27 3612 2951 4036 -176 -11 -425 C ATOM 206 O LYS A 27 -5.833 -2.999 -4.029 1.00 28.20 O ANISOU 206 O LYS A 27 3603 3001 4113 -235 -66 -337 O ATOM 207 CB LYS A 27 -4.132 -0.405 -4.857 1.00 25.80 C ANISOU 207 CB LYS A 27 3279 2811 3713 -139 123 -482 C ATOM 208 CG LYS A 27 -3.544 0.882 -4.313 1.00 25.49 C ANISOU 208 CG LYS A 27 3182 2852 3652 -115 198 -496 C ATOM 209 CD LYS A 27 -4.040 2.054 -5.138 1.00 27.06 C ANISOU 209 CD LYS A 27 3391 3072 3818 -133 216 -509 C ATOM 210 CE LYS A 27 -3.467 3.340 -4.607 1.00 30.37 C ANISOU 210 CE LYS A 27 3778 3552 4209 -117 274 -521 C ATOM 211 NZ LYS A 27 -3.691 4.467 -5.567 1.00 31.26 N ANISOU 211 NZ LYS A 27 3914 3678 4288 -129 294 -544 N ATOM 212 N ALA A 28 -4.215 -3.600 -5.484 1.00 28.39 N ANISOU 212 N ALA A 28 3793 2923 4070 -149 -41 -483 N ATOM 213 CA ALA A 28 -4.952 -4.752 -5.977 1.00 29.77 C ANISOU 213 CA ALA A 28 4072 2987 4253 -202 -158 -458 C ATOM 214 C ALA A 28 -5.012 -5.836 -4.914 1.00 29.98 C ANISOU 214 C ALA A 28 4076 2983 4331 -215 -207 -402 C ATOM 215 O ALA A 28 -6.040 -6.481 -4.774 1.00 30.14 O ANISOU 215 O ALA A 28 4107 2958 4388 -299 -314 -322 O ATOM 216 CB ALA A 28 -4.330 -5.299 -7.262 1.00 30.44 C ANISOU 216 CB ALA A 28 4325 2969 4272 -148 -172 -544 C ATOM 217 N LYS A 29 -3.913 -6.035 -4.177 1.00 30.29 N ANISOU 217 N LYS A 29 4080 3052 4377 -139 -135 -430 N ATOM 218 CA LYS A 29 -3.863 -7.055 -3.130 1.00 30.95 C ANISOU 218 CA LYS A 29 4138 3111 4508 -144 -174 -378 C ATOM 219 C LYS A 29 -4.784 -6.661 -1.985 1.00 30.72 C ANISOU 219 C LYS A 29 3970 3170 4531 -207 -184 -277 C ATOM 220 O LYS A 29 -5.383 -7.516 -1.345 1.00 31.19 O ANISOU 220 O LYS A 29 4011 3203 4638 -256 -259 -197 O ATOM 221 CB LYS A 29 -2.456 -7.234 -2.581 1.00 31.66 C ANISOU 221 CB LYS A 29 4206 3231 4594 -47 -88 -419 C ATOM 222 CG LYS A 29 -1.621 -8.256 -3.324 1.00 32.95 C ANISOU 222 CG LYS A 29 4512 3288 4720 35 -95 -478 C ATOM 223 CD LYS A 29 -0.141 -7.926 -3.173 1.00 33.61 C ANISOU 223 CD LYS A 29 4548 3441 4781 145 24 -513 C ATOM 224 CE LYS A 29 0.722 -8.993 -3.859 1.00 36.27 C ANISOU 224 CE LYS A 29 5026 3681 5074 259 36 -556 C ATOM 225 NZ LYS A 29 2.073 -9.022 -3.300 1.00 37.62 N ANISOU 225 NZ LYS A 29 5117 3926 5249 357 134 -542 N ATOM 226 N ILE A 30 -4.889 -5.360 -1.747 1.00 30.17 N ANISOU 226 N ILE A 30 3813 3205 4447 -199 -108 -276 N ATOM 227 CA ILE A 30 -5.801 -4.821 -0.739 1.00 30.36 C ANISOU 227 CA ILE A 30 3720 3318 4497 -231 -99 -180 C ATOM 228 C ILE A 30 -7.238 -5.077 -1.173 1.00 30.90 C ANISOU 228 C ILE A 30 3784 3366 4591 -315 -191 -84 C ATOM 229 O ILE A 30 -8.015 -5.622 -0.392 1.00 31.73 O ANISOU 229 O ILE A 30 3821 3492 4741 -357 -241 30 O ATOM 230 CB ILE A 30 -5.542 -3.326 -0.451 1.00 29.20 C ANISOU 230 CB ILE A 30 3516 3267 4311 -190 2 -208 C ATOM 231 CG1 ILE A 30 -4.140 -3.141 0.123 1.00 28.39 C ANISOU 231 CG1 ILE A 30 3406 3190 4190 -130 69 -272 C ATOM 232 CG2 ILE A 30 -6.623 -2.762 0.497 1.00 29.83 C ANISOU 232 CG2 ILE A 30 3502 3432 4400 -200 18 -103 C ATOM 233 CD1 ILE A 30 -3.741 -1.706 0.373 1.00 27.76 C ANISOU 233 CD1 ILE A 30 3299 3184 4066 -104 144 -303 C ATOM 234 N GLN A 31 -7.582 -4.725 -2.410 1.00 31.15 N ANISOU 234 N GLN A 31 3880 3359 4595 -345 -219 -116 N ATOM 235 CA GLN A 31 -8.901 -5.083 -2.957 1.00 32.63 C ANISOU 235 CA GLN A 31 4075 3516 4808 -442 -331 -16 C ATOM 236 C GLN A 31 -9.169 -6.560 -2.769 1.00 34.14 C ANISOU 236 C GLN A 31 4317 3614 5042 -506 -456 45 C ATOM 237 O GLN A 31 -10.178 -6.935 -2.200 1.00 35.20 O ANISOU 237 O GLN A 31 4367 3780 5226 -576 -525 188 O ATOM 238 CB GLN A 31 -9.018 -4.735 -4.437 1.00 32.53 C ANISOU 238 CB GLN A 31 4163 3446 4751 -468 -362 -78 C ATOM 239 CG GLN A 31 -10.359 -5.175 -5.063 1.00 35.97 C ANISOU 239 CG GLN A 31 4615 3839 5212 -588 -502 36 C ATOM 240 CD GLN A 31 -10.524 -4.713 -6.512 1.00 38.76 C ANISOU 240 CD GLN A 31 5068 4146 5515 -616 -532 -21 C ATOM 241 OE1 GLN A 31 -9.602 -4.819 -7.313 1.00 39.09 O ANISOU 241 OE1 GLN A 31 5239 4111 5500 -564 -510 -153 O ATOM 242 NE2 GLN A 31 -11.709 -4.197 -6.849 1.00 41.35 N ANISOU 242 NE2 GLN A 31 5327 4524 5859 -691 -578 89 N ATOM 243 N ASP A 32 -8.260 -7.406 -3.246 1.00 35.06 N ANISOU 243 N ASP A 32 4571 3615 5134 -476 -484 -54 N ATOM 244 CA ASP A 32 -8.408 -8.858 -3.074 1.00 36.59 C ANISOU 244 CA ASP A 32 4845 3696 5360 -528 -609 -9 C ATOM 245 C ASP A 32 -8.707 -9.249 -1.630 1.00 36.38 C ANISOU 245 C ASP A 32 4684 3740 5400 -544 -610 104 C ATOM 246 O ASP A 32 -9.611 -10.043 -1.369 1.00 36.70 O ANISOU 246 O ASP A 32 4708 3748 5490 -641 -733 230 O ATOM 247 CB ASP A 32 -7.138 -9.602 -3.531 1.00 36.92 C ANISOU 247 CB ASP A 32 5048 3623 5357 -442 -593 -140 C ATOM 248 CG ASP A 32 -7.291 -11.115 -3.462 1.00 39.67 C ANISOU 248 CG ASP A 32 5518 3828 5726 -489 -731 -103 C ATOM 249 OD1 ASP A 32 -8.124 -11.679 -4.229 1.00 40.99 O ANISOU 249 OD1 ASP A 32 5801 3886 5886 -591 -882 -60 O ATOM 250 OD2 ASP A 32 -6.569 -11.738 -2.642 1.00 41.02 O ANISOU 250 OD2 ASP A 32 5676 3992 5920 -430 -698 -114 O ATOM 251 N LYS A 33 -7.924 -8.702 -0.704 1.00 35.54 N ANISOU 251 N LYS A 33 4486 3727 5289 -453 -480 64 N ATOM 252 CA LYS A 33 -7.971 -9.131 0.688 1.00 36.08 C ANISOU 252 CA LYS A 33 4448 3854 5406 -447 -469 150 C ATOM 253 C LYS A 33 -9.104 -8.498 1.513 1.00 35.83 C ANISOU 253 C LYS A 33 4256 3955 5403 -479 -449 295 C ATOM 254 O LYS A 33 -9.651 -9.136 2.399 1.00 35.69 O ANISOU 254 O LYS A 33 4160 3966 5433 -515 -496 420 O ATOM 255 CB LYS A 33 -6.633 -8.834 1.351 1.00 35.80 C ANISOU 255 CB LYS A 33 4394 3861 5348 -341 -350 55 C ATOM 256 CG LYS A 33 -6.380 -9.642 2.596 1.00 38.13 C ANISOU 256 CG LYS A 33 4631 4170 5686 -331 -359 114 C ATOM 257 CD LYS A 33 -5.023 -9.289 3.193 1.00 39.14 C ANISOU 257 CD LYS A 33 4739 4343 5789 -236 -249 28 C ATOM 258 CE LYS A 33 -4.975 -9.673 4.653 1.00 38.56 C ANISOU 258 CE LYS A 33 4570 4332 5751 -228 -237 106 C ATOM 259 NZ LYS A 33 -5.872 -8.821 5.474 1.00 35.10 N ANISOU 259 NZ LYS A 33 4015 4012 5307 -239 -198 197 N ATOM 260 N GLU A 34 -9.431 -7.240 1.230 1.00 35.21 N ANISOU 260 N GLU A 34 4131 3958 5288 -452 -373 286 N ATOM 261 CA GLU A 34 -10.377 -6.499 2.054 1.00 35.46 C ANISOU 261 CA GLU A 34 4021 4124 5327 -439 -321 416 C ATOM 262 C GLU A 34 -11.670 -6.124 1.355 1.00 35.91 C ANISOU 262 C GLU A 34 4036 4214 5395 -506 -373 529 C ATOM 263 O GLU A 34 -12.640 -5.779 2.026 1.00 37.13 O ANISOU 263 O GLU A 34 4064 4480 5565 -499 -348 681 O ATOM 264 CB GLU A 34 -9.725 -5.245 2.636 1.00 34.80 C ANISOU 264 CB GLU A 34 3910 4127 5186 -332 -175 336 C ATOM 265 CG GLU A 34 -8.504 -5.510 3.526 1.00 34.53 C ANISOU 265 CG GLU A 34 3890 4087 5141 -273 -124 257 C ATOM 266 CD GLU A 34 -8.844 -6.264 4.810 1.00 34.62 C ANISOU 266 CD GLU A 34 3819 4143 5192 -275 -143 374 C ATOM 267 OE1 GLU A 34 -9.967 -6.166 5.299 1.00 34.68 O ANISOU 267 OE1 GLU A 34 3734 4229 5216 -286 -148 519 O ATOM 268 OE2 GLU A 34 -7.969 -6.941 5.351 1.00 38.42 O ANISOU 268 OE2 GLU A 34 4320 4589 5687 -258 -146 330 O ATOM 269 N GLY A 35 -11.694 -6.218 0.026 1.00 35.68 N ANISOU 269 N GLY A 35 4111 4093 5354 -564 -444 467 N ATOM 270 CA GLY A 35 -12.857 -5.824 -0.785 1.00 35.82 C ANISOU 270 CA GLY A 35 4098 4135 5379 -636 -503 568 C ATOM 271 C GLY A 35 -12.979 -4.332 -1.088 1.00 34.36 C ANISOU 271 C GLY A 35 3875 4036 5144 -567 -386 531 C ATOM 272 O GLY A 35 -14.031 -3.875 -1.527 1.00 34.90 O ANISOU 272 O GLY A 35 3882 4158 5220 -608 -411 644 O ATOM 273 N ILE A 36 -11.909 -3.579 -0.849 1.00 33.28 N ANISOU 273 N ILE A 36 3775 3913 4956 -466 -265 385 N ATOM 274 CA ILE A 36 -11.867 -2.122 -1.073 1.00 32.32 C ANISOU 274 CA ILE A 36 3640 3858 4780 -395 -155 334 C ATOM 275 C ILE A 36 -11.390 -1.807 -2.490 1.00 32.35 C ANISOU 275 C ILE A 36 3755 3785 4751 -419 -174 208 C ATOM 276 O ILE A 36 -10.276 -2.182 -2.867 1.00 31.69 O ANISOU 276 O ILE A 36 3768 3623 4649 -403 -175 77 O ATOM 277 CB ILE A 36 -10.935 -1.390 -0.064 1.00 31.62 C ANISOU 277 CB ILE A 36 3547 3820 4649 -287 -31 251 C ATOM 278 CG1 ILE A 36 -11.261 -1.766 1.382 1.00 31.13 C ANISOU 278 CG1 ILE A 36 3395 3827 4606 -252 -8 360 C ATOM 279 CG2 ILE A 36 -11.015 0.156 -0.249 1.00 30.84 C ANISOU 279 CG2 ILE A 36 3450 3779 4489 -220 67 215 C ATOM 280 CD1 ILE A 36 -10.102 -1.461 2.338 1.00 28.53 C ANISOU 280 CD1 ILE A 36 3095 3507 4238 -174 71 262 C ATOM 281 N PRO A 37 -12.222 -1.110 -3.285 1.00 32.80 N ANISOU 281 N PRO A 37 3795 3871 4798 -448 -184 258 N ATOM 282 CA PRO A 37 -11.816 -0.861 -4.667 1.00 32.92 C ANISOU 282 CA PRO A 37 3918 3813 4778 -473 -208 146 C ATOM 283 C PRO A 37 -10.584 0.034 -4.717 1.00 32.58 C ANISOU 283 C PRO A 37 3922 3777 4682 -385 -96 -6 C ATOM 284 O PRO A 37 -10.509 0.983 -3.936 1.00 32.67 O ANISOU 284 O PRO A 37 3876 3866 4673 -317 -1 1 O ATOM 285 CB PRO A 37 -13.031 -0.144 -5.266 1.00 33.50 C ANISOU 285 CB PRO A 37 3933 3942 4853 -513 -226 254 C ATOM 286 CG PRO A 37 -14.210 -0.656 -4.452 1.00 34.16 C ANISOU 286 CG PRO A 37 3892 4093 4993 -554 -276 455 C ATOM 287 CD PRO A 37 -13.623 -0.720 -3.042 1.00 33.38 C ANISOU 287 CD PRO A 37 3749 4040 4894 -466 -190 438 C ATOM 288 N PRO A 38 -9.611 -0.271 -5.608 1.00 32.43 N ANISOU 288 N PRO A 38 4013 3675 4635 -383 -109 -132 N ATOM 289 CA PRO A 38 -8.391 0.520 -5.715 1.00 32.09 C ANISOU 289 CA PRO A 38 4001 3646 4546 -311 -14 -253 C ATOM 290 C PRO A 38 -8.627 2.028 -5.868 1.00 32.35 C ANISOU 290 C PRO A 38 3997 3749 4546 -283 61 -256 C ATOM 291 O PRO A 38 -7.859 2.819 -5.302 1.00 31.64 O ANISOU 291 O PRO A 38 3894 3698 4429 -228 139 -305 O ATOM 292 CB PRO A 38 -7.702 -0.071 -6.948 1.00 31.92 C ANISOU 292 CB PRO A 38 4100 3533 4495 -317 -52 -346 C ATOM 293 CG PRO A 38 -8.080 -1.516 -6.879 1.00 32.24 C ANISOU 293 CG PRO A 38 4189 3492 4568 -366 -159 -302 C ATOM 294 CD PRO A 38 -9.534 -1.473 -6.457 1.00 33.47 C ANISOU 294 CD PRO A 38 4254 3693 4769 -439 -218 -159 C ATOM 295 N ASP A 39 -9.681 2.428 -6.589 1.00 33.43 N ANISOU 295 N ASP A 39 4121 3898 4682 -325 29 -195 N ATOM 296 CA ASP A 39 -9.948 3.864 -6.793 1.00 34.14 C ANISOU 296 CA ASP A 39 4186 4047 4738 -292 99 -195 C ATOM 297 C ASP A 39 -10.396 4.622 -5.526 1.00 33.13 C ANISOU 297 C ASP A 39 3984 4000 4605 -229 171 -123 C ATOM 298 O ASP A 39 -10.394 5.850 -5.492 1.00 33.09 O ANISOU 298 O ASP A 39 3985 4029 4559 -181 238 -140 O ATOM 299 CB ASP A 39 -10.884 4.117 -7.999 1.00 35.63 C ANISOU 299 CB ASP A 39 4384 4228 4924 -348 48 -150 C ATOM 300 CG ASP A 39 -12.239 3.436 -7.859 1.00 39.67 C ANISOU 300 CG ASP A 39 4832 4757 5484 -413 -35 3 C ATOM 301 OD1 ASP A 39 -12.335 2.184 -7.968 1.00 45.31 O ANISOU 301 OD1 ASP A 39 5578 5409 6229 -478 -134 26 O ATOM 302 OD2 ASP A 39 -13.231 4.163 -7.672 1.00 44.49 O ANISOU 302 OD2 ASP A 39 5361 5444 6100 -400 -7 113 O ATOM 303 N GLN A 40 -10.773 3.897 -4.482 1.00 32.74 N ANISOU 303 N GLN A 40 3878 3973 4588 -223 156 -41 N ATOM 304 CA GLN A 40 -11.072 4.544 -3.205 1.00 32.42 C ANISOU 304 CA GLN A 40 3789 4005 4525 -143 233 19 C ATOM 305 C GLN A 40 -9.854 4.594 -2.281 1.00 30.67 C ANISOU 305 C GLN A 40 3606 3769 4277 -98 275 -71 C ATOM 306 O GLN A 40 -9.904 5.238 -1.242 1.00 31.22 O ANISOU 306 O GLN A 40 3672 3882 4308 -28 337 -47 O ATOM 307 CB GLN A 40 -12.190 3.800 -2.497 1.00 32.94 C ANISOU 307 CB GLN A 40 3759 4122 4634 -152 202 179 C ATOM 308 CG GLN A 40 -13.481 3.830 -3.251 1.00 37.01 C ANISOU 308 CG GLN A 40 4214 4670 5176 -200 156 306 C ATOM 309 CD GLN A 40 -14.568 3.098 -2.539 1.00 40.96 C ANISOU 309 CD GLN A 40 4602 5236 5726 -216 120 493 C ATOM 310 OE1 GLN A 40 -15.504 2.602 -3.164 1.00 46.32 O ANISOU 310 OE1 GLN A 40 5227 5924 6450 -301 33 614 O ATOM 311 NE2 GLN A 40 -14.456 3.010 -1.226 1.00 40.71 N ANISOU 311 NE2 GLN A 40 4533 5252 5682 -141 179 530 N ATOM 312 N GLN A 41 -8.784 3.897 -2.649 1.00 29.03 N ANISOU 312 N GLN A 41 3441 3502 4086 -134 240 -163 N ATOM 313 CA GLN A 41 -7.597 3.765 -1.796 1.00 27.98 C ANISOU 313 CA GLN A 41 3328 3362 3940 -105 266 -227 C ATOM 314 C GLN A 41 -6.537 4.845 -1.997 1.00 27.80 C ANISOU 314 C GLN A 41 3360 3336 3868 -85 310 -320 C ATOM 315 O GLN A 41 -6.158 5.146 -3.127 1.00 27.30 O ANISOU 315 O GLN A 41 3329 3247 3795 -108 305 -377 O ATOM 316 CB GLN A 41 -6.927 2.422 -2.025 1.00 27.80 C ANISOU 316 CB GLN A 41 3318 3286 3961 -140 211 -260 C ATOM 317 CG GLN A 41 -7.851 1.254 -1.983 1.00 26.64 C ANISOU 317 CG GLN A 41 3137 3119 3865 -183 140 -172 C ATOM 318 CD GLN A 41 -7.102 -0.025 -2.100 1.00 26.72 C ANISOU 318 CD GLN A 41 3185 3061 3905 -202 90 -213 C ATOM 319 OE1 GLN A 41 -5.929 -0.089 -1.750 1.00 27.59 O ANISOU 319 OE1 GLN A 41 3313 3166 4004 -166 125 -280 O ATOM 320 NE2 GLN A 41 -7.760 -1.059 -2.599 1.00 27.67 N ANISOU 320 NE2 GLN A 41 3326 3126 4063 -260 1 -166 N ATOM 321 N ARG A 42 -6.056 5.416 -0.896 1.00 27.09 N ANISOU 321 N ARG A 42 3285 3268 3741 -47 345 -327 N ATOM 322 CA ARG A 42 -4.875 6.277 -0.941 1.00 27.73 C ANISOU 322 CA ARG A 42 3417 3338 3781 -50 361 -401 C ATOM 323 C ARG A 42 -3.842 5.667 -0.014 1.00 27.09 C ANISOU 323 C ARG A 42 3325 3258 3711 -53 348 -413 C ATOM 324 O ARG A 42 -4.138 5.339 1.135 1.00 27.36 O ANISOU 324 O ARG A 42 3344 3309 3741 -26 352 -368 O ATOM 325 CB ARG A 42 -5.176 7.720 -0.481 1.00 27.68 C ANISOU 325 CB ARG A 42 3471 3343 3704 -12 396 -397 C ATOM 326 CG ARG A 42 -6.426 8.437 -1.143 1.00 30.51 C ANISOU 326 CG ARG A 42 3835 3714 4045 14 423 -359 C ATOM 327 CD ARG A 42 -6.251 8.789 -2.640 1.00 34.01 C ANISOU 327 CD ARG A 42 4286 4138 4499 -31 410 -406 C ATOM 328 NE ARG A 42 -7.483 9.355 -3.229 1.00 38.88 N ANISOU 328 NE ARG A 42 4895 4771 5106 -10 430 -355 N ATOM 329 CZ ARG A 42 -8.446 8.656 -3.843 1.00 39.48 C ANISOU 329 CZ ARG A 42 4912 4861 5227 -32 407 -295 C ATOM 330 NH1 ARG A 42 -8.346 7.330 -3.986 1.00 37.91 N ANISOU 330 NH1 ARG A 42 4675 4647 5083 -76 357 -287 N ATOM 331 NH2 ARG A 42 -9.514 9.289 -4.327 1.00 39.33 N ANISOU 331 NH2 ARG A 42 4879 4866 5196 -13 425 -235 N ATOM 332 N LEU A 43 -2.625 5.530 -0.492 1.00 26.28 N ANISOU 332 N LEU A 43 3222 3145 3618 -79 338 -460 N ATOM 333 CA LEU A 43 -1.596 4.939 0.335 1.00 26.91 C ANISOU 333 CA LEU A 43 3279 3233 3712 -83 325 -457 C ATOM 334 C LEU A 43 -0.555 5.968 0.708 1.00 27.52 C ANISOU 334 C LEU A 43 3388 3322 3745 -106 320 -473 C ATOM 335 O LEU A 43 -0.120 6.746 -0.148 1.00 28.52 O ANISOU 335 O LEU A 43 3534 3450 3854 -130 322 -498 O ATOM 336 CB LEU A 43 -0.962 3.746 -0.373 1.00 26.24 C ANISOU 336 CB LEU A 43 3161 3132 3677 -83 315 -472 C ATOM 337 CG LEU A 43 -1.841 2.499 -0.405 1.00 27.32 C ANISOU 337 CG LEU A 43 3282 3239 3858 -75 292 -445 C ATOM 338 CD1 LEU A 43 -1.242 1.433 -1.366 1.00 25.22 C ANISOU 338 CD1 LEU A 43 3030 2933 3620 -63 280 -475 C ATOM 339 CD2 LEU A 43 -2.038 1.949 1.033 1.00 24.57 C ANISOU 339 CD2 LEU A 43 2901 2908 3526 -65 282 -394 C ATOM 340 N ILE A 44 -0.189 5.989 1.989 1.00 27.71 N ANISOU 340 N ILE A 44 3423 3356 3749 -107 303 -449 N ATOM 341 CA ILE A 44 0.740 6.980 2.538 1.00 28.59 C ANISOU 341 CA ILE A 44 3584 3469 3810 -146 273 -450 C ATOM 342 C ILE A 44 1.968 6.271 3.138 1.00 28.72 C ANISOU 342 C ILE A 44 3544 3511 3857 -175 244 -421 C ATOM 343 O ILE A 44 1.823 5.282 3.863 1.00 28.66 O ANISOU 343 O ILE A 44 3501 3512 3879 -150 247 -399 O ATOM 344 CB ILE A 44 0.076 7.854 3.679 1.00 29.48 C ANISOU 344 CB ILE A 44 3798 3560 3843 -120 267 -443 C ATOM 345 CG1 ILE A 44 -1.346 8.384 3.327 1.00 29.84 C ANISOU 345 CG1 ILE A 44 3886 3594 3858 -62 312 -447 C ATOM 346 CG2 ILE A 44 1.032 8.946 4.173 1.00 29.65 C ANISOU 346 CG2 ILE A 44 3906 3560 3801 -177 211 -447 C ATOM 347 CD1 ILE A 44 -1.516 8.961 1.946 1.00 31.99 C ANISOU 347 CD1 ILE A 44 4157 3857 4141 -80 324 -476 C ATOM 348 N PHE A 45 3.169 6.751 2.825 1.00 28.45 N ANISOU 348 N PHE A 45 3493 3496 3819 -228 215 -406 N ATOM 349 CA PHE A 45 4.375 6.309 3.535 1.00 28.84 C ANISOU 349 CA PHE A 45 3489 3579 3889 -264 179 -354 C ATOM 350 C PHE A 45 5.366 7.467 3.571 1.00 29.38 C ANISOU 350 C PHE A 45 3586 3658 3919 -348 117 -320 C ATOM 351 O PHE A 45 5.529 8.178 2.581 1.00 28.61 O ANISOU 351 O PHE A 45 3492 3563 3814 -371 120 -326 O ATOM 352 CB PHE A 45 4.995 5.071 2.869 1.00 28.99 C ANISOU 352 CB PHE A 45 3402 3634 3979 -227 216 -333 C ATOM 353 CG PHE A 45 6.234 4.542 3.575 1.00 30.02 C ANISOU 353 CG PHE A 45 3460 3811 4136 -251 188 -263 C ATOM 354 CD1 PHE A 45 6.168 4.073 4.882 1.00 30.27 C ANISOU 354 CD1 PHE A 45 3498 3838 4166 -255 160 -241 C ATOM 355 CD2 PHE A 45 7.463 4.522 2.927 1.00 31.85 C ANISOU 355 CD2 PHE A 45 3609 4101 4392 -264 194 -203 C ATOM 356 CE1 PHE A 45 7.298 3.602 5.529 1.00 31.44 C ANISOU 356 CE1 PHE A 45 3574 4032 4339 -281 131 -168 C ATOM 357 CE2 PHE A 45 8.611 4.042 3.572 1.00 32.25 C ANISOU 357 CE2 PHE A 45 3577 4206 4470 -283 170 -116 C ATOM 358 CZ PHE A 45 8.523 3.579 4.874 1.00 32.30 C ANISOU 358 CZ PHE A 45 3594 4202 4478 -296 135 -102 C ATOM 359 N ALA A 46 5.995 7.658 4.727 1.00 30.28 N ANISOU 359 N ALA A 46 3726 3773 4005 -401 51 -276 N ATOM 360 CA ALA A 46 6.874 8.784 4.973 1.00 31.68 C ANISOU 360 CA ALA A 46 3955 3945 4136 -503 -38 -231 C ATOM 361 C ALA A 46 6.175 10.095 4.589 1.00 32.28 C ANISOU 361 C ALA A 46 4163 3958 4144 -516 -54 -283 C ATOM 362 O ALA A 46 6.748 10.968 3.937 1.00 32.36 O ANISOU 362 O ALA A 46 4182 3970 4144 -586 -97 -257 O ATOM 363 CB ALA A 46 8.217 8.609 4.222 1.00 32.28 C ANISOU 363 CB ALA A 46 3896 4098 4270 -554 -51 -145 C ATOM 364 N GLY A 47 4.912 10.197 4.970 1.00 32.65 N ANISOU 364 N GLY A 47 4304 3954 4145 -441 -13 -346 N ATOM 365 CA GLY A 47 4.134 11.400 4.748 1.00 34.40 C ANISOU 365 CA GLY A 47 4664 4112 4293 -428 -17 -392 C ATOM 366 C GLY A 47 3.991 11.781 3.297 1.00 34.57 C ANISOU 366 C GLY A 47 4640 4147 4348 -430 20 -411 C ATOM 367 O GLY A 47 3.741 12.944 3.005 1.00 35.06 O ANISOU 367 O GLY A 47 4808 4159 4353 -451 -6 -431 O ATOM 368 N LYS A 48 4.169 10.805 2.406 1.00 34.28 N ANISOU 368 N LYS A 48 4461 4169 4394 -405 77 -403 N ATOM 369 CA LYS A 48 4.008 10.993 0.957 1.00 34.98 C ANISOU 369 CA LYS A 48 4503 4276 4513 -394 121 -422 C ATOM 370 C LYS A 48 2.855 10.105 0.458 1.00 34.11 C ANISOU 370 C LYS A 48 4357 4166 4437 -306 200 -465 C ATOM 371 O LYS A 48 2.835 8.915 0.738 1.00 33.55 O ANISOU 371 O LYS A 48 4221 4116 4410 -269 224 -457 O ATOM 372 CB LYS A 48 5.313 10.643 0.206 1.00 34.79 C ANISOU 372 CB LYS A 48 4357 4320 4541 -437 115 -364 C ATOM 373 CG LYS A 48 6.368 11.779 0.118 1.00 38.13 C ANISOU 373 CG LYS A 48 4795 4754 4938 -544 33 -300 C ATOM 374 CD LYS A 48 7.839 11.297 -0.084 1.00 40.17 C ANISOU 374 CD LYS A 48 4912 5102 5248 -587 16 -195 C ATOM 375 CE LYS A 48 8.456 10.507 1.135 1.00 41.36 C ANISOU 375 CE LYS A 48 5021 5276 5417 -601 -18 -144 C ATOM 376 NZ LYS A 48 9.477 11.183 2.139 1.00 38.70 N ANISOU 376 NZ LYS A 48 4708 4943 5053 -730 -146 -50 N ATOM 377 N GLN A 49 1.898 10.692 -0.259 1.00 34.33 N ANISOU 377 N GLN A 49 4431 4168 4444 -278 230 -501 N ATOM 378 CA GLN A 49 0.900 9.921 -1.002 1.00 34.93 C ANISOU 378 CA GLN A 49 4464 4249 4557 -220 286 -524 C ATOM 379 C GLN A 49 1.582 9.139 -2.107 1.00 34.14 C ANISOU 379 C GLN A 49 4280 4182 4509 -222 305 -524 C ATOM 380 O GLN A 49 2.342 9.707 -2.893 1.00 33.85 O ANISOU 380 O GLN A 49 4228 4168 4468 -255 300 -515 O ATOM 381 CB GLN A 49 -0.194 10.831 -1.589 1.00 35.82 C ANISOU 381 CB GLN A 49 4640 4335 4636 -198 307 -547 C ATOM 382 CG GLN A 49 -1.317 10.048 -2.291 1.00 38.47 C ANISOU 382 CG GLN A 49 4933 4676 5009 -154 347 -552 C ATOM 383 CD GLN A 49 -2.525 10.908 -2.646 1.00 43.40 C ANISOU 383 CD GLN A 49 5607 5284 5599 -124 370 -551 C ATOM 384 OE1 GLN A 49 -3.213 10.651 -3.639 1.00 47.38 O ANISOU 384 OE1 GLN A 49 6080 5793 6129 -118 386 -551 O ATOM 385 NE2 GLN A 49 -2.793 11.921 -1.838 1.00 44.65 N ANISOU 385 NE2 GLN A 49 5851 5419 5693 -101 370 -544 N ATOM 386 N LEU A 50 1.315 7.836 -2.162 1.00 33.52 N ANISOU 386 N LEU A 50 4156 4106 4474 -180 327 -527 N ATOM 387 CA LEU A 50 2.066 6.933 -3.043 1.00 33.37 C ANISOU 387 CA LEU A 50 4081 4108 4491 -158 349 -526 C ATOM 388 C LEU A 50 1.390 6.759 -4.393 1.00 33.76 C ANISOU 388 C LEU A 50 4150 4136 4540 -133 373 -561 C ATOM 389 O LEU A 50 0.191 6.497 -4.455 1.00 33.56 O ANISOU 389 O LEU A 50 4154 4077 4520 -124 368 -576 O ATOM 390 CB LEU A 50 2.290 5.568 -2.376 1.00 32.74 C ANISOU 390 CB LEU A 50 3963 4026 4450 -125 349 -509 C ATOM 391 CG LEU A 50 2.978 5.578 -1.004 1.00 31.92 C ANISOU 391 CG LEU A 50 3835 3945 4347 -149 322 -468 C ATOM 392 CD1 LEU A 50 3.185 4.145 -0.521 1.00 29.48 C ANISOU 392 CD1 LEU A 50 3485 3634 4083 -109 327 -451 C ATOM 393 CD2 LEU A 50 4.300 6.336 -1.032 1.00 28.37 C ANISOU 393 CD2 LEU A 50 3353 3542 3884 -195 303 -425 C ATOM 394 N GLU A 51 2.174 6.886 -5.463 1.00 34.17 N ANISOU 394 N GLU A 51 4185 4215 4584 -123 396 -562 N ATOM 395 CA GLU A 51 1.641 6.891 -6.830 1.00 35.38 C ANISOU 395 CA GLU A 51 4372 4348 4721 -103 415 -597 C ATOM 396 C GLU A 51 1.640 5.512 -7.443 1.00 35.14 C ANISOU 396 C GLU A 51 4362 4288 4702 -43 429 -617 C ATOM 397 O GLU A 51 2.597 4.762 -7.288 1.00 34.76 O ANISOU 397 O GLU A 51 4285 4259 4664 2 450 -597 O ATOM 398 CB GLU A 51 2.450 7.843 -7.725 1.00 36.22 C ANISOU 398 CB GLU A 51 4461 4502 4801 -117 435 -582 C ATOM 399 CG GLU A 51 2.144 9.311 -7.457 1.00 38.82 C ANISOU 399 CG GLU A 51 4811 4831 5108 -181 409 -576 C ATOM 400 CD GLU A 51 0.790 9.728 -8.017 1.00 43.15 C ANISOU 400 CD GLU A 51 5415 5339 5641 -183 408 -614 C ATOM 401 OE1 GLU A 51 0.282 9.039 -8.937 1.00 45.85 O ANISOU 401 OE1 GLU A 51 5773 5663 5986 -152 422 -640 O ATOM 402 OE2 GLU A 51 0.240 10.748 -7.544 1.00 45.78 O ANISOU 402 OE2 GLU A 51 5785 5657 5955 -213 390 -612 O ATOM 403 N ASP A 52 0.561 5.216 -8.159 1.00 35.84 N ANISOU 403 N ASP A 52 4509 4326 4784 -43 411 -650 N ATOM 404 CA ASP A 52 0.301 3.888 -8.724 1.00 36.84 C ANISOU 404 CA ASP A 52 4695 4393 4910 0 397 -673 C ATOM 405 C ASP A 52 1.468 3.323 -9.522 1.00 37.06 C ANISOU 405 C ASP A 52 4743 4432 4908 81 444 -683 C ATOM 406 O ASP A 52 1.804 2.142 -9.405 1.00 37.07 O ANISOU 406 O ASP A 52 4778 4396 4913 138 445 -686 O ATOM 407 CB ASP A 52 -0.978 3.914 -9.586 1.00 37.53 C ANISOU 407 CB ASP A 52 4848 4429 4984 -33 357 -695 C ATOM 408 CG ASP A 52 -2.252 3.950 -8.748 1.00 39.35 C ANISOU 408 CG ASP A 52 5057 4644 5250 -88 310 -660 C ATOM 409 OD1 ASP A 52 -3.355 4.022 -9.324 1.00 41.33 O ANISOU 409 OD1 ASP A 52 5338 4866 5498 -125 271 -651 O ATOM 410 OD2 ASP A 52 -2.159 3.921 -7.503 1.00 42.11 O ANISOU 410 OD2 ASP A 52 5355 5016 5627 -92 313 -631 O ATOM 411 N GLY A 53 2.087 4.186 -10.322 1.00 37.24 N ANISOU 411 N GLY A 53 4745 4507 4897 93 487 -677 N ATOM 412 CA GLY A 53 3.124 3.757 -11.259 1.00 37.91 C ANISOU 412 CA GLY A 53 4848 4618 4939 188 546 -672 C ATOM 413 C GLY A 53 4.496 3.507 -10.657 1.00 37.83 C ANISOU 413 C GLY A 53 4750 4679 4944 241 594 -608 C ATOM 414 O GLY A 53 5.411 3.126 -11.377 1.00 38.44 O ANISOU 414 O GLY A 53 4829 4793 4984 341 658 -583 O ATOM 415 N ARG A 54 4.642 3.734 -9.351 1.00 36.94 N ANISOU 415 N ARG A 54 4563 4593 4881 181 565 -572 N ATOM 416 CA ARG A 54 5.940 3.590 -8.677 1.00 37.28 C ANISOU 416 CA ARG A 54 4508 4712 4945 208 595 -494 C ATOM 417 C ARG A 54 6.031 2.276 -7.893 1.00 37.07 C ANISOU 417 C ARG A 54 4494 4645 4946 259 590 -494 C ATOM 418 O ARG A 54 5.008 1.716 -7.496 1.00 36.95 O ANISOU 418 O ARG A 54 4542 4548 4947 233 543 -545 O ATOM 419 CB ARG A 54 6.229 4.787 -7.760 1.00 37.07 C ANISOU 419 CB ARG A 54 4399 4741 4943 101 556 -443 C ATOM 420 CG ARG A 54 6.291 6.194 -8.428 1.00 39.89 C ANISOU 420 CG ARG A 54 4741 5139 5276 41 551 -428 C ATOM 421 CD ARG A 54 7.498 6.412 -9.359 1.00 45.76 C ANISOU 421 CD ARG A 54 5415 5975 5997 93 609 -350 C ATOM 422 NE ARG A 54 7.099 6.445 -10.775 1.00 50.44 N ANISOU 422 NE ARG A 54 6070 6551 6543 150 652 -397 N ATOM 423 CZ ARG A 54 7.541 5.622 -11.735 1.00 53.54 C ANISOU 423 CZ ARG A 54 6489 6958 6895 277 724 -393 C ATOM 424 NH1 ARG A 54 8.440 4.665 -11.477 1.00 54.46 N ANISOU 424 NH1 ARG A 54 6566 7110 7015 374 773 -339 N ATOM 425 NH2 ARG A 54 7.086 5.767 -12.978 1.00 53.77 N ANISOU 425 NH2 ARG A 54 6594 6964 6873 316 750 -442 N ATOM 426 N THR A 55 7.253 1.777 -7.693 1.00 37.26 N ANISOU 426 N THR A 55 4451 4732 4976 332 638 -423 N ATOM 427 CA THR A 55 7.457 0.515 -6.976 1.00 37.00 C ANISOU 427 CA THR A 55 4426 4663 4968 390 639 -414 C ATOM 428 C THR A 55 7.743 0.776 -5.502 1.00 36.73 C ANISOU 428 C THR A 55 4297 4671 4987 307 596 -360 C ATOM 429 O THR A 55 7.878 1.916 -5.069 1.00 36.17 O ANISOU 429 O THR A 55 4166 4652 4924 211 565 -327 O ATOM 430 CB THR A 55 8.617 -0.332 -7.550 1.00 37.95 C ANISOU 430 CB THR A 55 4536 4824 5060 543 725 -359 C ATOM 431 OG1 THR A 55 9.873 0.338 -7.339 1.00 37.75 O ANISOU 431 OG1 THR A 55 4361 4933 5047 540 764 -239 O ATOM 432 CG2 THR A 55 8.413 -0.631 -9.051 1.00 38.58 C ANISOU 432 CG2 THR A 55 4737 4856 5065 648 774 -413 C ATOM 433 N LEU A 56 7.857 -0.301 -4.740 1.00 36.74 N ANISOU 433 N LEU A 56 4298 4643 5017 346 590 -349 N ATOM 434 CA LEU A 56 8.105 -0.198 -3.324 1.00 36.11 C ANISOU 434 CA LEU A 56 4142 4597 4981 275 547 -299 C ATOM 435 C LEU A 56 9.531 0.227 -3.090 1.00 36.37 C ANISOU 435 C LEU A 56 4050 4746 5023 277 574 -184 C ATOM 436 O LEU A 56 9.813 0.911 -2.111 1.00 36.51 O ANISOU 436 O LEU A 56 4004 4808 5060 179 522 -134 O ATOM 437 CB LEU A 56 7.808 -1.519 -2.617 1.00 35.90 C ANISOU 437 CB LEU A 56 4150 4507 4985 317 532 -314 C ATOM 438 CG LEU A 56 6.343 -1.996 -2.642 1.00 35.60 C ANISOU 438 CG LEU A 56 4218 4359 4951 289 482 -398 C ATOM 439 CD1 LEU A 56 6.222 -3.313 -1.952 1.00 34.15 C ANISOU 439 CD1 LEU A 56 4058 4119 4800 327 461 -391 C ATOM 440 CD2 LEU A 56 5.384 -1.011 -2.007 1.00 33.22 C ANISOU 440 CD2 LEU A 56 3909 4057 4655 177 429 -418 C ATOM 441 N SER A 57 10.427 -0.186 -3.980 1.00 37.03 N ANISOU 441 N SER A 57 4103 4880 5085 392 652 -132 N ATOM 442 CA SER A 57 11.838 0.194 -3.884 1.00 38.03 C ANISOU 442 CA SER A 57 4088 5138 5222 403 684 11 C ATOM 443 C SER A 57 12.028 1.672 -4.225 1.00 37.38 C ANISOU 443 C SER A 57 3955 5120 5127 296 653 50 C ATOM 444 O SER A 57 12.880 2.324 -3.652 1.00 38.02 O ANISOU 444 O SER A 57 3926 5290 5230 215 615 164 O ATOM 445 CB SER A 57 12.703 -0.661 -4.809 1.00 39.55 C ANISOU 445 CB SER A 57 4264 5377 5387 582 793 70 C ATOM 446 OG SER A 57 12.158 -0.677 -6.123 1.00 39.76 O ANISOU 446 OG SER A 57 4403 5349 5355 657 838 -14 O ATOM 447 N ASP A 58 11.233 2.176 -5.163 1.00 36.78 N ANISOU 447 N ASP A 58 3965 4994 5015 291 659 -38 N ATOM 448 CA ASP A 58 11.192 3.597 -5.487 1.00 36.79 C ANISOU 448 CA ASP A 58 3946 5031 5003 184 620 -21 C ATOM 449 C ASP A 58 10.982 4.456 -4.238 1.00 36.21 C ANISOU 449 C ASP A 58 3863 4943 4951 30 517 -13 C ATOM 450 O ASP A 58 11.608 5.496 -4.071 1.00 36.29 O ANISOU 450 O ASP A 58 3812 5014 4962 -67 468 72 O ATOM 451 CB ASP A 58 10.059 3.869 -6.473 1.00 36.18 C ANISOU 451 CB ASP A 58 3985 4873 4887 196 631 -141 C ATOM 452 CG ASP A 58 10.435 3.575 -7.903 1.00 38.37 C ANISOU 452 CG ASP A 58 4275 5183 5120 320 720 -131 C ATOM 453 OD1 ASP A 58 9.513 3.547 -8.760 1.00 40.79 O ANISOU 453 OD1 ASP A 58 4692 5416 5391 344 729 -231 O ATOM 454 OD2 ASP A 58 11.639 3.376 -8.183 1.00 41.53 O ANISOU 454 OD2 ASP A 58 4577 5687 5516 397 782 -14 O ATOM 455 N TYR A 59 10.091 4.001 -3.361 1.00 35.26 N ANISOU 455 N TYR A 59 3815 4738 4843 10 480 -94 N ATOM 456 CA TYR A 59 9.751 4.731 -2.153 1.00 34.80 C ANISOU 456 CA TYR A 59 3782 4652 4787 -109 391 -100 C ATOM 457 C TYR A 59 10.538 4.333 -0.913 1.00 35.22 C ANISOU 457 C TYR A 59 3767 4746 4870 -142 351 -17 C ATOM 458 O TYR A 59 10.258 4.829 0.168 1.00 35.44 O ANISOU 458 O TYR A 59 3836 4743 4889 -230 277 -25 O ATOM 459 CB TYR A 59 8.265 4.577 -1.869 1.00 33.98 C ANISOU 459 CB TYR A 59 3790 4447 4673 -109 377 -219 C ATOM 460 CG TYR A 59 7.397 5.353 -2.804 1.00 34.45 C ANISOU 460 CG TYR A 59 3921 4469 4702 -121 384 -288 C ATOM 461 CD1 TYR A 59 6.521 4.698 -3.681 1.00 32.97 C ANISOU 461 CD1 TYR A 59 3790 4228 4509 -50 427 -362 C ATOM 462 CD2 TYR A 59 7.432 6.758 -2.811 1.00 34.47 C ANISOU 462 CD2 TYR A 59 3944 4480 4675 -209 339 -274 C ATOM 463 CE1 TYR A 59 5.700 5.415 -4.526 1.00 33.43 C ANISOU 463 CE1 TYR A 59 3907 4255 4540 -67 429 -416 C ATOM 464 CE2 TYR A 59 6.614 7.490 -3.671 1.00 35.01 C ANISOU 464 CE2 TYR A 59 4075 4513 4715 -216 348 -333 C ATOM 465 CZ TYR A 59 5.752 6.813 -4.527 1.00 34.94 C ANISOU 465 CZ TYR A 59 4105 4463 4706 -144 396 -402 C ATOM 466 OH TYR A 59 4.935 7.533 -5.374 1.00 36.71 O ANISOU 466 OH TYR A 59 4386 4658 4904 -156 402 -451 O ATOM 467 N ASN A 60 11.512 3.439 -1.068 1.00 35.94 N ANISOU 467 N ASN A 60 3762 4904 4988 -62 403 67 N ATOM 468 CA ASN A 60 12.302 2.927 0.047 1.00 36.71 C ANISOU 468 CA ASN A 60 3782 5048 5119 -82 373 159 C ATOM 469 C ASN A 60 11.462 2.222 1.114 1.00 36.22 C ANISOU 469 C ASN A 60 3789 4905 5068 -82 345 81 C ATOM 470 O ASN A 60 11.668 2.395 2.319 1.00 37.00 O ANISOU 470 O ASN A 60 3875 5010 5173 -161 275 121 O ATOM 471 CB ASN A 60 13.199 4.016 0.635 1.00 37.51 C ANISOU 471 CB ASN A 60 3814 5218 5219 -219 283 278 C ATOM 472 CG ASN A 60 14.219 4.529 -0.373 1.00 39.54 C ANISOU 472 CG ASN A 60 3964 5582 5477 -214 314 399 C ATOM 473 OD1 ASN A 60 15.237 3.877 -0.641 1.00 42.82 O ANISOU 473 OD1 ASN A 60 4255 6096 5920 -134 374 521 O ATOM 474 ND2 ASN A 60 13.950 5.696 -0.942 1.00 40.71 N ANISOU 474 ND2 ASN A 60 4156 5716 5595 -290 278 377 N ATOM 475 N ILE A 61 10.515 1.421 0.646 1.00 35.15 N ANISOU 475 N ILE A 61 3729 4693 4933 3 393 -20 N ATOM 476 CA ILE A 61 9.755 0.530 1.501 1.00 34.72 C ANISOU 476 CA ILE A 61 3723 4573 4898 21 377 -72 C ATOM 477 C ILE A 61 10.510 -0.791 1.641 1.00 35.68 C ANISOU 477 C ILE A 61 3784 4718 5055 117 421 -15 C ATOM 478 O ILE A 61 10.796 -1.452 0.655 1.00 36.95 O ANISOU 478 O ILE A 61 3950 4877 5212 227 490 -16 O ATOM 479 CB ILE A 61 8.337 0.311 0.942 1.00 33.89 C ANISOU 479 CB ILE A 61 3725 4374 4778 48 388 -187 C ATOM 480 CG1 ILE A 61 7.519 1.591 1.111 1.00 31.85 C ANISOU 480 CG1 ILE A 61 3523 4093 4485 -41 343 -232 C ATOM 481 CG2 ILE A 61 7.641 -0.831 1.659 1.00 33.98 C ANISOU 481 CG2 ILE A 61 3769 4324 4818 79 375 -216 C ATOM 482 CD1 ILE A 61 6.529 1.851 0.050 1.00 30.17 C ANISOU 482 CD1 ILE A 61 3382 3830 4252 -22 365 -309 C ATOM 483 N GLN A 62 10.853 -1.149 2.874 1.00 35.91 N ANISOU 483 N GLN A 62 3766 4767 5110 83 382 39 N ATOM 484 CA GLN A 62 11.586 -2.372 3.159 1.00 36.50 C ANISOU 484 CA GLN A 62 3780 4867 5222 170 419 104 C ATOM 485 C GLN A 62 10.736 -3.296 4.022 1.00 35.92 C ANISOU 485 C GLN A 62 3762 4715 5171 177 391 50 C ATOM 486 O GLN A 62 9.568 -3.020 4.257 1.00 35.25 O ANISOU 486 O GLN A 62 3756 4566 5073 127 355 -31 O ATOM 487 CB GLN A 62 12.910 -2.056 3.850 1.00 37.53 C ANISOU 487 CB GLN A 62 3781 5107 5371 121 393 247 C ATOM 488 CG GLN A 62 13.883 -1.246 3.023 1.00 38.71 C ANISOU 488 CG GLN A 62 3847 5353 5507 113 417 341 C ATOM 489 CD GLN A 62 15.139 -0.876 3.810 1.00 44.26 C ANISOU 489 CD GLN A 62 4415 6169 6234 33 365 506 C ATOM 490 OE1 GLN A 62 16.039 -1.705 4.021 1.00 46.17 O ANISOU 490 OE1 GLN A 62 4555 6479 6510 107 405 617 O ATOM 491 NE2 GLN A 62 15.213 0.376 4.236 1.00 43.07 N ANISOU 491 NE2 GLN A 62 4270 6034 6062 -119 268 533 N ATOM 492 N LYS A 63 11.324 -4.403 4.465 1.00 36.57 N ANISOU 492 N LYS A 63 3798 4808 5288 246 413 107 N ATOM 493 CA LYS A 63 10.662 -5.383 5.318 1.00 36.52 C ANISOU 493 CA LYS A 63 3829 4735 5310 254 384 78 C ATOM 494 C LYS A 63 10.016 -4.734 6.545 1.00 35.24 C ANISOU 494 C LYS A 63 3676 4573 5140 136 310 65 C ATOM 495 O LYS A 63 10.590 -3.822 7.141 1.00 35.20 O ANISOU 495 O LYS A 63 3623 4633 5118 54 271 119 O ATOM 496 CB LYS A 63 11.659 -6.482 5.745 1.00 37.61 C ANISOU 496 CB LYS A 63 3895 4909 5487 336 415 169 C ATOM 497 CG LYS A 63 13.155 -6.272 5.305 1.00 41.39 C ANISOU 497 CG LYS A 63 4259 5501 5966 390 470 289 C ATOM 498 CD LYS A 63 13.828 -5.091 6.035 1.00 45.30 C ANISOU 498 CD LYS A 63 4654 6098 6459 256 408 379 C ATOM 499 CE LYS A 63 15.290 -4.915 5.674 1.00 47.25 C ANISOU 499 CE LYS A 63 4764 6472 6717 294 450 533 C ATOM 500 NZ LYS A 63 16.189 -5.654 6.627 1.00 49.59 N ANISOU 500 NZ LYS A 63 4951 6833 7056 313 442 660 N ATOM 501 N GLU A 64 8.832 -5.219 6.919 1.00 34.36 N ANISOU 501 N GLU A 64 3632 4387 5036 130 286 5 N ATOM 502 CA GLU A 64 8.034 -4.668 8.041 1.00 33.57 C ANISOU 502 CA GLU A 64 3556 4284 4915 48 232 -8 C ATOM 503 C GLU A 64 7.776 -3.155 8.041 1.00 31.32 C ANISOU 503 C GLU A 64 3308 4019 4573 -28 208 -35 C ATOM 504 O GLU A 64 7.464 -2.585 9.079 1.00 31.10 O ANISOU 504 O GLU A 64 3305 4000 4511 -84 166 -27 O ATOM 505 CB GLU A 64 8.636 -5.059 9.394 1.00 34.36 C ANISOU 505 CB GLU A 64 3596 4427 5033 22 199 67 C ATOM 506 CG GLU A 64 8.096 -6.360 9.949 1.00 38.85 C ANISOU 506 CG GLU A 64 4167 4950 5644 63 195 73 C ATOM 507 CD GLU A 64 8.982 -7.519 9.627 1.00 44.63 C ANISOU 507 CD GLU A 64 4854 5680 6425 145 228 118 C ATOM 508 OE1 GLU A 64 10.206 -7.384 9.873 1.00 48.01 O ANISOU 508 OE1 GLU A 64 5200 6182 6859 146 236 195 O ATOM 509 OE2 GLU A 64 8.464 -8.554 9.134 1.00 48.10 O ANISOU 509 OE2 GLU A 64 5342 6042 6891 209 241 86 O ATOM 510 N SER A 65 7.937 -2.494 6.902 1.00 30.08 N ANISOU 510 N SER A 65 3166 3866 4398 -23 234 -63 N ATOM 511 CA SER A 65 7.547 -1.079 6.811 1.00 28.16 C ANISOU 511 CA SER A 65 2976 3625 4099 -90 209 -96 C ATOM 512 C SER A 65 6.061 -0.965 7.098 1.00 27.14 C ANISOU 512 C SER A 65 2923 3441 3948 -89 204 -155 C ATOM 513 O SER A 65 5.327 -1.902 6.804 1.00 25.57 O ANISOU 513 O SER A 65 2732 3201 3784 -42 223 -178 O ATOM 514 CB SER A 65 7.838 -0.520 5.433 1.00 27.89 C ANISOU 514 CB SER A 65 2943 3600 4055 -76 243 -117 C ATOM 515 OG SER A 65 9.161 -0.039 5.376 1.00 28.39 O ANISOU 515 OG SER A 65 2934 3734 4117 -110 231 -37 O ATOM 516 N THR A 66 5.630 0.167 7.677 1.00 27.00 N ANISOU 516 N THR A 66 2967 3422 3870 -138 174 -169 N ATOM 517 CA THR A 66 4.199 0.440 7.929 1.00 27.10 C ANISOU 517 CA THR A 66 3047 3399 3850 -120 183 -207 C ATOM 518 C THR A 66 3.655 1.514 6.992 1.00 27.24 C ANISOU 518 C THR A 66 3123 3398 3830 -128 198 -256 C ATOM 519 O THR A 66 4.230 2.613 6.921 1.00 27.19 O ANISOU 519 O THR A 66 3153 3400 3778 -173 174 -260 O ATOM 520 CB THR A 66 3.938 0.902 9.379 1.00 27.72 C ANISOU 520 CB THR A 66 3176 3486 3870 -137 152 -184 C ATOM 521 OG1 THR A 66 4.214 -0.167 10.279 1.00 28.17 O ANISOU 521 OG1 THR A 66 3178 3561 3964 -126 140 -137 O ATOM 522 CG2 THR A 66 2.431 1.370 9.586 1.00 27.76 C ANISOU 522 CG2 THR A 66 3251 3470 3827 -96 178 -205 C ATOM 523 N LEU A 67 2.577 1.202 6.262 1.00 26.81 N ANISOU 523 N LEU A 67 3078 3314 3794 -92 228 -285 N ATOM 524 CA LEU A 67 1.947 2.192 5.400 1.00 27.18 C ANISOU 524 CA LEU A 67 3177 3345 3806 -96 244 -325 C ATOM 525 C LEU A 67 0.561 2.524 5.927 1.00 27.70 C ANISOU 525 C LEU A 67 3286 3402 3837 -68 257 -317 C ATOM 526 O LEU A 67 -0.050 1.731 6.652 1.00 27.82 O ANISOU 526 O LEU A 67 3273 3423 3872 -42 258 -277 O ATOM 527 CB LEU A 67 1.874 1.777 3.912 1.00 27.05 C ANISOU 527 CB LEU A 67 3142 3307 3827 -81 266 -357 C ATOM 528 CG LEU A 67 2.813 0.839 3.145 1.00 28.61 C ANISOU 528 CG LEU A 67 3295 3504 4071 -59 277 -357 C ATOM 529 CD1 LEU A 67 2.600 0.896 1.574 1.00 25.54 C ANISOU 529 CD1 LEU A 67 2933 3088 3681 -39 301 -401 C ATOM 530 CD2 LEU A 67 4.268 1.002 3.539 1.00 25.01 C ANISOU 530 CD2 LEU A 67 2791 3095 3614 -76 271 -319 C ATOM 531 N HIS A 68 0.083 3.713 5.591 1.00 27.61 N ANISOU 531 N HIS A 68 3339 3382 3770 -66 269 -341 N ATOM 532 CA HIS A 68 -1.221 4.127 6.051 1.00 28.10 C ANISOU 532 CA HIS A 68 3441 3446 3789 -19 296 -318 C ATOM 533 C HIS A 68 -2.147 4.199 4.846 1.00 27.61 C ANISOU 533 C HIS A 68 3363 3374 3752 -9 318 -326 C ATOM 534 O HIS A 68 -1.777 4.730 3.787 1.00 27.27 O ANISOU 534 O HIS A 68 3336 3315 3708 -36 317 -371 O ATOM 535 CB HIS A 68 -1.136 5.423 6.849 1.00 28.66 C ANISOU 535 CB HIS A 68 3621 3507 3760 -5 292 -328 C ATOM 536 CG HIS A 68 -0.372 5.275 8.131 1.00 31.19 C ANISOU 536 CG HIS A 68 3968 3833 4049 -19 258 -310 C ATOM 537 ND1 HIS A 68 -0.974 4.927 9.324 1.00 34.07 N ANISOU 537 ND1 HIS A 68 4348 4217 4381 37 274 -265 N ATOM 538 CD2 HIS A 68 0.952 5.365 8.391 1.00 31.74 C ANISOU 538 CD2 HIS A 68 4041 3900 4117 -85 204 -316 C ATOM 539 CE1 HIS A 68 -0.053 4.824 10.264 1.00 34.31 C ANISOU 539 CE1 HIS A 68 4403 4248 4387 4 230 -258 C ATOM 540 NE2 HIS A 68 1.123 5.090 9.723 1.00 34.84 N ANISOU 540 NE2 HIS A 68 4460 4301 4475 -74 183 -284 N ATOM 541 N LEU A 69 -3.301 3.571 4.996 1.00 27.08 N ANISOU 541 N LEU A 69 3254 3322 3711 22 331 -270 N ATOM 542 CA LEU A 69 -4.346 3.546 3.968 1.00 27.83 C ANISOU 542 CA LEU A 69 3328 3414 3832 22 339 -252 C ATOM 543 C LEU A 69 -5.442 4.538 4.335 1.00 28.70 C ANISOU 543 C LEU A 69 3471 3554 3881 81 384 -205 C ATOM 544 O LEU A 69 -5.983 4.486 5.440 1.00 28.87 O ANISOU 544 O LEU A 69 3487 3610 3872 136 408 -141 O ATOM 545 CB LEU A 69 -4.940 2.139 3.849 1.00 26.79 C ANISOU 545 CB LEU A 69 3123 3278 3776 3 307 -194 C ATOM 546 CG LEU A 69 -6.205 1.935 2.998 1.00 27.56 C ANISOU 546 CG LEU A 69 3190 3377 3904 -12 292 -138 C ATOM 547 CD1 LEU A 69 -5.958 2.221 1.511 1.00 23.54 C ANISOU 547 CD1 LEU A 69 2718 2827 3401 -49 277 -208 C ATOM 548 CD2 LEU A 69 -6.714 0.511 3.191 1.00 25.02 C ANISOU 548 CD2 LEU A 69 2809 3047 3652 -43 238 -63 C ATOM 549 N VAL A 70 -5.765 5.430 3.403 1.00 30.29 N ANISOU 549 N VAL A 70 3706 3744 4058 81 400 -232 N ATOM 550 CA VAL A 70 -6.803 6.457 3.602 1.00 31.48 C ANISOU 550 CA VAL A 70 3895 3920 4146 152 451 -186 C ATOM 551 C VAL A 70 -7.872 6.276 2.521 1.00 32.39 C ANISOU 551 C VAL A 70 3948 4052 4307 137 450 -134 C ATOM 552 O VAL A 70 -7.540 6.073 1.382 1.00 31.56 O ANISOU 552 O VAL A 70 3834 3915 4242 74 415 -184 O ATOM 553 CB VAL A 70 -6.178 7.878 3.583 1.00 31.62 C ANISOU 553 CB VAL A 70 4032 3902 4080 166 464 -259 C ATOM 554 CG1 VAL A 70 -7.261 8.995 3.613 1.00 30.99 C ANISOU 554 CG1 VAL A 70 4011 3836 3927 254 522 -217 C ATOM 555 CG2 VAL A 70 -5.228 8.034 4.770 1.00 31.65 C ANISOU 555 CG2 VAL A 70 4106 3889 4032 170 446 -289 C ATOM 556 N LEU A 71 -9.151 6.328 2.882 1.00 34.64 N ANISOU 556 N LEU A 71 4187 4392 4583 198 486 -21 N ATOM 557 CA LEU A 71 -10.214 5.966 1.935 1.00 36.39 C ANISOU 557 CA LEU A 71 4328 4638 4860 165 466 60 C ATOM 558 C LEU A 71 -11.047 7.148 1.506 1.00 38.14 C ANISOU 558 C LEU A 71 4571 4887 5032 226 520 99 C ATOM 559 O LEU A 71 -11.292 8.047 2.289 1.00 37.81 O ANISOU 559 O LEU A 71 4587 4870 4911 330 590 120 O ATOM 560 CB LEU A 71 -11.156 4.922 2.535 1.00 36.69 C ANISOU 560 CB LEU A 71 4259 4734 4950 168 449 203 C ATOM 561 CG LEU A 71 -10.781 3.444 2.587 1.00 37.27 C ANISOU 561 CG LEU A 71 4282 4776 5101 84 370 207 C ATOM 562 CD1 LEU A 71 -9.623 3.136 1.646 1.00 33.86 C ANISOU 562 CD1 LEU A 71 3912 4260 4695 9 318 67 C ATOM 563 CD2 LEU A 71 -10.476 3.027 4.021 1.00 37.26 C ANISOU 563 CD2 LEU A 71 4269 4805 5085 133 393 236 C ATOM 564 N ARG A 72 -11.505 7.120 0.262 1.00 40.68 N ANISOU 564 N ARG A 72 4858 5202 5395 166 486 112 N ATOM 565 CA ARG A 72 -12.324 8.207 -0.273 1.00 43.99 C ANISOU 565 CA ARG A 72 5287 5650 5776 217 534 157 C ATOM 566 C ARG A 72 -13.629 7.709 -0.843 1.00 46.03 C ANISOU 566 C ARG A 72 5431 5966 6093 186 506 307 C ATOM 567 O ARG A 72 -13.671 6.686 -1.533 1.00 46.52 O ANISOU 567 O ARG A 72 5445 6004 6227 77 417 318 O ATOM 568 CB ARG A 72 -11.572 8.977 -1.367 1.00 43.42 C ANISOU 568 CB ARG A 72 5296 5515 5685 171 520 29 C ATOM 569 CG ARG A 72 -10.514 9.967 -0.870 1.00 45.71 C ANISOU 569 CG ARG A 72 5708 5760 5900 211 553 -83 C ATOM 570 CD ARG A 72 -11.063 10.980 0.145 1.00 49.78 C ANISOU 570 CD ARG A 72 6291 6300 6324 343 631 -33 C ATOM 571 NE ARG A 72 -10.882 10.515 1.522 1.00 51.84 N ANISOU 571 NE ARG A 72 6562 6577 6559 395 648 -8 N ATOM 572 CZ ARG A 72 -10.179 11.147 2.459 1.00 51.71 C ANISOU 572 CZ ARG A 72 6668 6520 6458 445 665 -70 C ATOM 573 NH1 ARG A 72 -9.593 12.312 2.210 1.00 52.85 N ANISOU 573 NH1 ARG A 72 6943 6602 6536 447 662 -156 N ATOM 574 NH2 ARG A 72 -10.086 10.619 3.661 1.00 49.84 N ANISOU 574 NH2 ARG A 72 6432 6305 6201 488 676 -39 N ATOM 575 N LEU A 73 -14.696 8.438 -0.547 1.00 48.70 N ANISOU 575 N LEU A 73 5732 6379 6393 285 578 431 N ATOM 576 CA LEU A 73 -15.980 8.186 -1.177 1.00 51.76 C ANISOU 576 CA LEU A 73 6000 6835 6832 256 553 596 C ATOM 577 C LEU A 73 -15.893 8.633 -2.646 1.00 52.54 C ANISOU 577 C LEU A 73 6133 6885 6945 177 509 526 C ATOM 578 O LEU A 73 -16.219 7.859 -3.540 1.00 53.07 O ANISOU 578 O LEU A 73 6147 6939 7078 58 414 566 O ATOM 579 CB LEU A 73 -17.122 8.931 -0.456 1.00 52.58 C ANISOU 579 CB LEU A 73 6049 7046 6884 409 661 765 C ATOM 580 CG LEU A 73 -17.371 8.840 1.055 1.00 54.11 C ANISOU 580 CG LEU A 73 6226 7306 7029 541 742 853 C ATOM 581 CD1 LEU A 73 -18.112 10.090 1.528 1.00 54.34 C ANISOU 581 CD1 LEU A 73 6289 7400 6958 732 876 940 C ATOM 582 CD2 LEU A 73 -18.147 7.582 1.463 1.00 55.16 C ANISOU 582 CD2 LEU A 73 6194 7522 7242 491 692 1039 C ATOM 583 N ARG A 74 -15.427 9.872 -2.871 1.00 53.82 N ANISOU 583 N ARG A 74 6398 7014 7038 239 571 422 N ATOM 584 CA ARG A 74 -15.399 10.527 -4.201 1.00 54.68 C ANISOU 584 CA ARG A 74 6541 7088 7145 188 549 366 C ATOM 585 C ARG A 74 -16.683 11.357 -4.510 1.00 55.74 C ANISOU 585 C ARG A 74 6617 7300 7263 260 605 513 C ATOM 586 O ARG A 74 -17.781 10.997 -4.072 1.00 57.09 O ANISOU 586 O ARG A 74 6672 7561 7458 299 621 697 O ATOM 587 CB ARG A 74 -15.036 9.512 -5.311 1.00 54.55 C ANISOU 587 CB ARG A 74 6510 7019 7198 35 434 312 C ATOM 588 CG ARG A 74 -15.716 9.693 -6.674 1.00 55.73 C ANISOU 588 CG ARG A 74 6631 7173 7372 -37 384 359 C ATOM 589 CD ARG A 74 -17.039 8.926 -6.792 1.00 58.83 C ANISOU 589 CD ARG A 74 6895 7632 7825 -90 322 558 C ATOM 590 NE ARG A 74 -17.666 9.189 -8.089 1.00 61.44 N ANISOU 590 NE ARG A 74 7207 7966 8172 -163 268 605 N ATOM 591 CZ ARG A 74 -18.913 8.855 -8.421 1.00 63.83 C ANISOU 591 CZ ARG A 74 7397 8334 8520 -217 210 798 C ATOM 592 NH1 ARG A 74 -19.704 8.232 -7.550 1.00 64.89 N ANISOU 592 NH1 ARG A 74 7415 8546 8693 -204 201 974 N ATOM 593 NH2 ARG A 74 -19.376 9.151 -9.634 1.00 63.60 N ANISOU 593 NH2 ARG A 74 7365 8301 8499 -289 155 828 N ATOM 594 N GLY A 75 -16.527 12.473 -5.236 1.00 55.74 N ANISOU 594 N GLY A 75 6690 7269 7220 283 636 445 N ATOM 595 CA GLY A 75 -17.663 13.304 -5.686 1.00 55.98 C ANISOU 595 CA GLY A 75 6671 7365 7234 349 686 576 C ATOM 596 C GLY A 75 -18.031 13.142 -7.166 1.00 55.63 C ANISOU 596 C GLY A 75 6575 7317 7245 225 605 598 C ATOM 597 O GLY A 75 -17.664 12.143 -7.806 1.00 55.51 O ANISOU 597 O GLY A 75 6544 7260 7286 86 500 550 O ATOM 598 N GLY A 76 -18.748 14.132 -7.712 1.00 55.24 N ANISOU 598 N GLY A 76 6513 7306 7171 281 653 671 N ATOM 599 CA GLY A 76 -19.308 14.056 -9.068 1.00 53.59 C ANISOU 599 CA GLY A 76 6243 7110 7008 173 579 727 C ATOM 600 C GLY A 76 -18.801 15.013 -10.147 1.00 51.86 C ANISOU 600 C GLY A 76 6116 6830 6757 148 580 604 C ATOM 601 O GLY A 76 -19.580 15.801 -10.707 1.00 52.52 O ANISOU 601 O GLY A 76 6165 6958 6830 186 612 696 O ATOM 602 N MET A 77 -17.500 14.953 -10.437 1.00 49.17 N ANISOU 602 N MET A 77 5884 6398 6402 89 548 411 N ATOM 603 CA MET A 77 -16.967 15.429 -11.723 1.00 46.36 C ANISOU 603 CA MET A 77 5589 5989 6036 15 510 305 C ATOM 604 C MET A 77 -15.570 14.931 -12.055 1.00 44.21 C ANISOU 604 C MET A 77 5399 5636 5763 -65 461 129 C ATOM 605 O MET A 77 -14.562 15.409 -11.515 1.00 43.96 O ANISOU 605 O MET A 77 5449 5561 5692 -22 501 19 O ATOM 606 CB MET A 77 -17.065 16.931 -11.931 1.00 46.11 C ANISOU 606 CB MET A 77 5617 5955 5949 103 588 293 C ATOM 607 CG MET A 77 -16.502 17.319 -13.290 1.00 44.33 C ANISOU 607 CG MET A 77 5441 5683 5720 15 542 194 C ATOM 608 SD MET A 77 -17.200 18.825 -13.943 1.00 43.16 S ANISOU 608 SD MET A 77 5307 5558 5535 82 600 256 S ATOM 609 CE MET A 77 -16.308 19.007 -15.475 1.00 39.93 C ANISOU 609 CE MET A 77 4954 5093 5124 -40 534 124 C ATOM 610 N GLN A 78 -15.539 13.988 -12.984 1.00 42.04 N ANISOU 610 N GLN A 78 5108 5340 5526 -178 368 117 N ATOM 611 CA GLN A 78 -14.311 13.430 -13.492 1.00 40.14 C ANISOU 611 CA GLN A 78 4941 5031 5279 -241 325 -29 C ATOM 612 C GLN A 78 -14.135 13.835 -14.960 1.00 38.13 C ANISOU 612 C GLN A 78 4729 4754 5006 -299 293 -80 C ATOM 613 O GLN A 78 -15.114 13.981 -15.713 1.00 37.52 O ANISOU 613 O GLN A 78 4612 4705 4940 -337 258 11 O ATOM 614 CB GLN A 78 -14.315 11.905 -13.321 1.00 40.64 C ANISOU 614 CB GLN A 78 4986 5072 5384 -307 245 -14 C ATOM 615 CG GLN A 78 -15.410 11.204 -14.115 1.00 45.36 C ANISOU 615 CG GLN A 78 5539 5680 6017 -398 146 99 C ATOM 616 CD GLN A 78 -16.074 10.059 -13.375 1.00 50.44 C ANISOU 616 CD GLN A 78 6116 6340 6711 -434 85 213 C ATOM 617 OE1 GLN A 78 -15.528 9.528 -12.398 1.00 53.32 O ANISOU 617 OE1 GLN A 78 6484 6691 7084 -400 106 176 O ATOM 618 NE2 GLN A 78 -17.263 9.670 -13.836 1.00 51.11 N ANISOU 618 NE2 GLN A 78 6132 6455 6830 -511 1 365 N ATOM 619 N ILE A 79 -12.885 14.067 -15.336 1.00 35.63 N ANISOU 619 N ILE A 79 4485 4396 4658 -302 309 -212 N ATOM 620 CA ILE A 79 -12.510 14.170 -16.741 1.00 34.53 C ANISOU 620 CA ILE A 79 4393 4233 4495 -356 275 -271 C ATOM 621 C ILE A 79 -11.378 13.195 -17.026 1.00 33.66 C ANISOU 621 C ILE A 79 4341 4075 4374 -380 246 -373 C ATOM 622 O ILE A 79 -10.745 12.666 -16.090 1.00 33.47 O ANISOU 622 O ILE A 79 4316 4039 4361 -352 262 -406 O ATOM 623 CB ILE A 79 -12.101 15.617 -17.175 1.00 34.16 C ANISOU 623 CB ILE A 79 4374 4195 4411 -324 333 -310 C ATOM 624 CG1 ILE A 79 -10.896 16.104 -16.372 1.00 33.38 C ANISOU 624 CG1 ILE A 79 4310 4079 4292 -279 385 -389 C ATOM 625 CG2 ILE A 79 -13.314 16.585 -17.113 1.00 33.87 C ANISOU 625 CG2 ILE A 79 4293 4199 4376 -289 363 -203 C ATOM 626 CD1 ILE A 79 -10.273 17.415 -16.895 1.00 33.44 C ANISOU 626 CD1 ILE A 79 4359 4084 4263 -272 418 -432 C ATOM 627 N PHE A 80 -11.146 12.959 -18.314 1.00 33.11 N ANISOU 627 N PHE A 80 4326 3980 4275 -421 207 -415 N ATOM 628 CA PHE A 80 -10.112 12.050 -18.799 1.00 33.25 C ANISOU 628 CA PHE A 80 4416 3953 4263 -423 188 -505 C ATOM 629 C PHE A 80 -9.076 12.889 -19.486 1.00 33.08 C ANISOU 629 C PHE A 80 4421 3949 4199 -394 245 -573 C ATOM 630 O PHE A 80 -9.409 13.792 -20.254 1.00 33.10 O ANISOU 630 O PHE A 80 4421 3973 4183 -409 253 -556 O ATOM 631 CB PHE A 80 -10.680 11.009 -19.789 1.00 33.79 C ANISOU 631 CB PHE A 80 4554 3969 4314 -484 90 -494 C ATOM 632 CG PHE A 80 -11.760 10.134 -19.205 1.00 34.92 C ANISOU 632 CG PHE A 80 4667 4096 4504 -536 10 -402 C ATOM 633 CD1 PHE A 80 -13.059 10.190 -19.691 1.00 35.36 C ANISOU 633 CD1 PHE A 80 4695 4163 4577 -609 -65 -296 C ATOM 634 CD2 PHE A 80 -11.480 9.258 -18.159 1.00 36.71 C ANISOU 634 CD2 PHE A 80 4882 4303 4762 -518 5 -405 C ATOM 635 CE1 PHE A 80 -14.069 9.410 -19.142 1.00 37.37 C ANISOU 635 CE1 PHE A 80 4901 4416 4881 -667 -146 -182 C ATOM 636 CE2 PHE A 80 -12.492 8.460 -17.595 1.00 37.05 C ANISOU 636 CE2 PHE A 80 4886 4338 4854 -572 -74 -302 C ATOM 637 CZ PHE A 80 -13.785 8.540 -18.086 1.00 38.36 C ANISOU 637 CZ PHE A 80 5014 4521 5038 -649 -150 -185 C ATOM 638 N VAL A 81 -7.817 12.610 -19.193 1.00 33.13 N ANISOU 638 N VAL A 81 4443 3953 4192 -352 284 -635 N ATOM 639 CA VAL A 81 -6.718 13.254 -19.886 1.00 33.68 C ANISOU 639 CA VAL A 81 4526 4050 4221 -326 334 -679 C ATOM 640 C VAL A 81 -5.951 12.106 -20.533 1.00 34.51 C ANISOU 640 C VAL A 81 4699 4126 4285 -293 327 -731 C ATOM 641 O VAL A 81 -5.515 11.187 -19.849 1.00 34.95 O ANISOU 641 O VAL A 81 4763 4161 4356 -264 326 -747 O ATOM 642 CB VAL A 81 -5.847 14.084 -18.921 1.00 33.52 C ANISOU 642 CB VAL A 81 4454 4064 4218 -304 386 -680 C ATOM 643 CG1 VAL A 81 -4.613 14.623 -19.610 1.00 33.66 C ANISOU 643 CG1 VAL A 81 4469 4119 4201 -288 427 -701 C ATOM 644 CG2 VAL A 81 -6.673 15.241 -18.314 1.00 34.62 C ANISOU 644 CG2 VAL A 81 4564 4213 4379 -319 392 -634 C ATOM 645 N LYS A 82 -5.813 12.176 -21.854 1.00 34.64 N ANISOU 645 N LYS A 82 4776 4142 4244 -286 326 -753 N ATOM 646 CA LYS A 82 -5.375 11.071 -22.689 1.00 35.44 C ANISOU 646 CA LYS A 82 4983 4200 4282 -242 312 -799 C ATOM 647 C LYS A 82 -4.102 11.441 -23.454 1.00 35.70 C ANISOU 647 C LYS A 82 5022 4286 4257 -170 391 -821 C ATOM 648 O LYS A 82 -4.079 12.439 -24.171 1.00 34.96 O ANISOU 648 O LYS A 82 4904 4237 4142 -185 414 -805 O ATOM 649 CB LYS A 82 -6.512 10.735 -23.663 1.00 35.78 C ANISOU 649 CB LYS A 82 5116 4188 4292 -298 227 -792 C ATOM 650 CG LYS A 82 -6.241 9.636 -24.673 1.00 37.76 C ANISOU 650 CG LYS A 82 5524 4368 4454 -257 192 -845 C ATOM 651 CD LYS A 82 -7.281 9.718 -25.795 1.00 38.80 C ANISOU 651 CD LYS A 82 5739 4460 4542 -328 106 -829 C ATOM 652 CE LYS A 82 -6.862 8.903 -27.013 1.00 40.59 C ANISOU 652 CE LYS A 82 6152 4620 4650 -271 84 -891 C ATOM 653 NZ LYS A 82 -5.870 9.648 -27.839 1.00 37.96 N ANISOU 653 NZ LYS A 82 5812 4360 4253 -185 189 -915 N ATOM 654 N THR A 83 -3.054 10.636 -23.284 1.00 35.99 N ANISOU 654 N THR A 83 5082 4324 4267 -87 435 -844 N ATOM 655 CA THR A 83 -1.826 10.777 -24.051 1.00 37.01 C ANISOU 655 CA THR A 83 5216 4513 4332 2 517 -844 C ATOM 656 C THR A 83 -2.002 10.049 -25.394 1.00 38.38 C ANISOU 656 C THR A 83 5547 4633 4402 58 501 -887 C ATOM 657 O THR A 83 -2.896 9.212 -25.550 1.00 37.68 O ANISOU 657 O THR A 83 5574 4447 4296 26 417 -921 O ATOM 658 CB THR A 83 -0.611 10.172 -23.303 1.00 37.64 C ANISOU 658 CB THR A 83 5252 4626 4424 84 577 -832 C ATOM 659 OG1 THR A 83 -0.751 8.753 -23.273 1.00 38.49 O ANISOU 659 OG1 THR A 83 5478 4648 4499 139 549 -877 O ATOM 660 CG2 THR A 83 -0.534 10.673 -21.855 1.00 35.58 C ANISOU 660 CG2 THR A 83 4868 4394 4257 22 569 -797 C ATOM 661 N LEU A 84 -1.142 10.354 -26.357 1.00 39.46 N ANISOU 661 N LEU A 84 5697 4830 4464 141 576 -878 N ATOM 662 CA LEU A 84 -1.262 9.750 -27.686 1.00 41.44 C ANISOU 662 CA LEU A 84 6119 5031 4597 209 569 -920 C ATOM 663 C LEU A 84 -0.576 8.385 -27.751 1.00 43.19 C ANISOU 663 C LEU A 84 6469 5197 4743 344 600 -957 C ATOM 664 O LEU A 84 -0.580 7.725 -28.793 1.00 44.81 O ANISOU 664 O LEU A 84 6854 5342 4830 427 596 -1000 O ATOM 665 CB LEU A 84 -0.755 10.710 -28.763 1.00 41.87 C ANISOU 665 CB LEU A 84 6139 5176 4593 246 637 -887 C ATOM 666 CG LEU A 84 -1.629 11.936 -29.082 1.00 39.92 C ANISOU 666 CG LEU A 84 5827 4952 4387 122 590 -864 C ATOM 667 CD1 LEU A 84 -1.780 12.890 -27.910 1.00 40.95 C ANISOU 667 CD1 LEU A 84 5792 5126 4640 26 582 -819 C ATOM 668 CD2 LEU A 84 -1.058 12.668 -30.271 1.00 39.82 C ANISOU 668 CD2 LEU A 84 5809 5022 4301 175 657 -833 C ATOM 669 N THR A 85 0.009 7.974 -26.626 1.00 43.95 N ANISOU 669 N THR A 85 6485 5312 4904 372 631 -940 N ATOM 670 CA THR A 85 0.435 6.579 -26.392 1.00 46.02 C ANISOU 670 CA THR A 85 6868 5500 5119 481 639 -975 C ATOM 671 C THR A 85 -0.769 5.784 -25.865 1.00 46.48 C ANISOU 671 C THR A 85 7022 5423 5217 378 505 -1020 C ATOM 672 O THR A 85 -0.731 4.558 -25.764 1.00 47.50 O ANISOU 672 O THR A 85 7293 5453 5304 439 473 -1059 O ATOM 673 CB THR A 85 1.610 6.473 -25.351 1.00 45.60 C ANISOU 673 CB THR A 85 6671 5531 5124 549 727 -921 C ATOM 674 OG1 THR A 85 1.134 6.801 -24.046 1.00 44.48 O ANISOU 674 OG1 THR A 85 6402 5391 5108 422 671 -904 O ATOM 675 CG2 THR A 85 2.752 7.425 -25.686 1.00 46.46 C ANISOU 675 CG2 THR A 85 6636 5793 5223 611 841 -840 C ATOM 676 N GLY A 86 -1.833 6.496 -25.500 1.00 46.42 N ANISOU 676 N GLY A 86 6931 5416 5292 226 428 -1000 N ATOM 677 CA GLY A 86 -3.082 5.855 -25.100 1.00 46.85 C ANISOU 677 CA GLY A 86 7052 5363 5386 117 296 -1012 C ATOM 678 C GLY A 86 -3.254 5.627 -23.614 1.00 46.57 C ANISOU 678 C GLY A 86 6901 5332 5461 65 276 -982 C ATOM 679 O GLY A 86 -4.173 4.904 -23.207 1.00 46.89 O ANISOU 679 O GLY A 86 6996 5288 5534 -11 171 -978 O ATOM 680 N LYS A 87 -2.376 6.222 -22.799 1.00 46.14 N ANISOU 680 N LYS A 87 6692 5376 5462 99 368 -953 N ATOM 681 CA LYS A 87 -2.580 6.243 -21.349 1.00 45.33 C ANISOU 681 CA LYS A 87 6471 5290 5462 43 353 -921 C ATOM 682 C LYS A 87 -3.654 7.250 -20.986 1.00 44.62 C ANISOU 682 C LYS A 87 6287 5229 5438 -74 309 -880 C ATOM 683 O LYS A 87 -3.473 8.454 -21.175 1.00 44.05 O ANISOU 683 O LYS A 87 6132 5230 5373 -90 356 -860 O ATOM 684 CB LYS A 87 -1.303 6.596 -20.598 1.00 45.37 C ANISOU 684 CB LYS A 87 6355 5387 5498 106 450 -895 C ATOM 685 CG LYS A 87 -1.477 6.563 -19.079 1.00 44.77 C ANISOU 685 CG LYS A 87 6177 5320 5514 53 429 -866 C ATOM 686 CD LYS A 87 -0.129 6.528 -18.367 1.00 47.61 C ANISOU 686 CD LYS A 87 6451 5749 5891 121 506 -840 C ATOM 687 CE LYS A 87 -0.263 6.066 -16.897 1.00 47.77 C ANISOU 687 CE LYS A 87 6413 5752 5984 89 477 -823 C ATOM 688 NZ LYS A 87 -0.891 7.052 -15.980 1.00 46.65 N ANISOU 688 NZ LYS A 87 6180 5641 5904 -4 451 -793 N ATOM 689 N THR A 88 -4.776 6.753 -20.476 1.00 44.66 N ANISOU 689 N THR A 88 6306 5176 5488 -151 220 -858 N ATOM 690 CA THR A 88 -5.834 7.621 -19.995 1.00 44.20 C ANISOU 690 CA THR A 88 6150 5152 5491 -239 190 -801 C ATOM 691 C THR A 88 -5.665 7.851 -18.490 1.00 43.86 C ANISOU 691 C THR A 88 5991 5151 5521 -238 224 -770 C ATOM 692 O THR A 88 -5.637 6.911 -17.694 1.00 43.95 O ANISOU 692 O THR A 88 6009 5129 5561 -231 199 -765 O ATOM 693 CB THR A 88 -7.246 7.097 -20.368 1.00 44.84 C ANISOU 693 CB THR A 88 6290 5168 5580 -328 72 -761 C ATOM 694 OG1 THR A 88 -7.389 7.104 -21.796 1.00 44.97 O ANISOU 694 OG1 THR A 88 6418 5149 5520 -335 39 -789 O ATOM 695 CG2 THR A 88 -8.341 7.987 -19.752 1.00 43.69 C ANISOU 695 CG2 THR A 88 6023 5076 5501 -396 60 -677 C ATOM 696 N ILE A 89 -5.524 9.119 -18.120 1.00 43.04 N ANISOU 696 N ILE A 89 5798 5117 5439 -244 278 -748 N ATOM 697 CA ILE A 89 -5.423 9.511 -16.725 1.00 42.54 C ANISOU 697 CA ILE A 89 5649 5088 5427 -244 305 -719 C ATOM 698 C ILE A 89 -6.715 10.245 -16.330 1.00 41.61 C ANISOU 698 C ILE A 89 5485 4985 5341 -290 283 -658 C ATOM 699 O ILE A 89 -7.074 11.248 -16.947 1.00 41.79 O ANISOU 699 O ILE A 89 5501 5031 5348 -306 295 -645 O ATOM 700 CB ILE A 89 -4.081 10.318 -16.438 1.00 42.54 C ANISOU 700 CB ILE A 89 5602 5143 5417 -207 377 -736 C ATOM 701 CG1 ILE A 89 -4.121 11.079 -15.120 1.00 42.40 C ANISOU 701 CG1 ILE A 89 5523 5151 5435 -221 391 -705 C ATOM 702 CG2 ILE A 89 -3.679 11.218 -17.589 1.00 43.40 C ANISOU 702 CG2 ILE A 89 5721 5286 5484 -206 406 -746 C ATOM 703 CD1 ILE A 89 -3.481 10.289 -14.009 1.00 44.58 C ANISOU 703 CD1 ILE A 89 5776 5425 5738 -197 396 -706 C ATOM 704 N THR A 90 -7.423 9.726 -15.325 1.00 40.06 N ANISOU 704 N THR A 90 5254 4779 5187 -301 255 -611 N ATOM 705 CA THR A 90 -8.684 10.331 -14.923 1.00 38.68 C ANISOU 705 CA THR A 90 5028 4631 5038 -323 245 -530 C ATOM 706 C THR A 90 -8.498 11.300 -13.749 1.00 37.81 C ANISOU 706 C THR A 90 4874 4559 4933 -280 308 -515 C ATOM 707 O THR A 90 -7.647 11.102 -12.885 1.00 37.98 O ANISOU 707 O THR A 90 4892 4580 4958 -253 332 -546 O ATOM 708 CB THR A 90 -9.850 9.292 -14.726 1.00 39.22 C ANISOU 708 CB THR A 90 5080 4678 5143 -368 168 -451 C ATOM 709 OG1 THR A 90 -10.165 9.142 -13.342 1.00 38.30 O ANISOU 709 OG1 THR A 90 4900 4588 5063 -343 187 -395 O ATOM 710 CG2 THR A 90 -9.542 7.947 -15.373 1.00 37.87 C ANISOU 710 CG2 THR A 90 4991 4437 4961 -398 97 -492 C ATOM 711 N LEU A 91 -9.257 12.383 -13.764 1.00 36.99 N ANISOU 711 N LEU A 91 4751 4483 4821 -270 332 -467 N ATOM 712 CA LEU A 91 -9.051 13.471 -12.820 1.00 35.91 C ANISOU 712 CA LEU A 91 4615 4363 4666 -221 387 -464 C ATOM 713 C LEU A 91 -10.371 13.943 -12.296 1.00 35.30 C ANISOU 713 C LEU A 91 4505 4314 4593 -183 407 -368 C ATOM 714 O LEU A 91 -11.341 13.992 -13.044 1.00 35.13 O ANISOU 714 O LEU A 91 4454 4311 4582 -205 387 -306 O ATOM 715 CB LEU A 91 -8.387 14.660 -13.514 1.00 36.06 C ANISOU 715 CB LEU A 91 4673 4380 4648 -226 411 -510 C ATOM 716 CG LEU A 91 -6.904 14.977 -13.409 1.00 36.69 C ANISOU 716 CG LEU A 91 4779 4452 4708 -233 423 -575 C ATOM 717 CD1 LEU A 91 -5.977 13.765 -13.174 1.00 37.00 C ANISOU 717 CD1 LEU A 91 4804 4487 4767 -238 410 -611 C ATOM 718 CD2 LEU A 91 -6.525 15.722 -14.677 1.00 35.73 C ANISOU 718 CD2 LEU A 91 4674 4338 4562 -260 426 -598 C ATOM 719 N GLU A 92 -10.373 14.296 -11.011 1.00 34.75 N ANISOU 719 N GLU A 92 4443 4252 4508 -121 447 -349 N ATOM 720 CA GLU A 92 -11.510 14.855 -10.303 1.00 34.75 C ANISOU 720 CA GLU A 92 4423 4285 4494 -47 491 -252 C ATOM 721 C GLU A 92 -11.324 16.358 -10.271 1.00 34.14 C ANISOU 721 C GLU A 92 4424 4188 4358 4 537 -279 C ATOM 722 O GLU A 92 -10.312 16.854 -9.761 1.00 34.07 O ANISOU 722 O GLU A 92 4490 4141 4315 11 542 -352 O ATOM 723 CB GLU A 92 -11.534 14.340 -8.875 1.00 35.54 C ANISOU 723 CB GLU A 92 4513 4397 4595 5 511 -222 C ATOM 724 CG GLU A 92 -12.016 12.909 -8.747 1.00 38.98 C ANISOU 724 CG GLU A 92 4865 4855 5090 -36 465 -161 C ATOM 725 CD GLU A 92 -13.541 12.793 -8.690 1.00 42.30 C ANISOU 725 CD GLU A 92 5199 5338 5533 -10 472 -6 C ATOM 726 OE1 GLU A 92 -14.249 13.834 -8.577 1.00 42.41 O ANISOU 726 OE1 GLU A 92 5215 5386 5511 69 533 59 O ATOM 727 OE2 GLU A 92 -14.023 11.641 -8.750 1.00 44.99 O ANISOU 727 OE2 GLU A 92 5472 5696 5928 -67 412 62 O ATOM 728 N VAL A 93 -12.309 17.071 -10.807 1.00 33.12 N ANISOU 728 N VAL A 93 4281 4084 4218 36 562 -209 N ATOM 729 CA VAL A 93 -12.194 18.491 -11.088 1.00 32.41 C ANISOU 729 CA VAL A 93 4272 3966 4076 74 594 -234 C ATOM 730 C VAL A 93 -13.555 19.161 -10.870 1.00 32.49 C ANISOU 730 C VAL A 93 4267 4016 4063 176 654 -115 C ATOM 731 O VAL A 93 -14.557 18.458 -10.712 1.00 33.23 O ANISOU 731 O VAL A 93 4262 4172 4193 195 661 -5 O ATOM 732 CB VAL A 93 -11.781 18.725 -12.570 1.00 31.67 C ANISOU 732 CB VAL A 93 4174 3862 3996 -14 556 -283 C ATOM 733 CG1 VAL A 93 -10.343 18.234 -12.848 1.00 31.31 C ANISOU 733 CG1 VAL A 93 4148 3787 3961 -91 514 -388 C ATOM 734 CG2 VAL A 93 -12.790 18.072 -13.513 1.00 30.94 C ANISOU 734 CG2 VAL A 93 3991 3816 3950 -57 527 -206 C ATOM 735 N GLU A 94 -13.585 20.499 -10.891 1.00 31.76 N ANISOU 735 N GLU A 94 4269 3888 3909 241 694 -126 N ATOM 736 CA GLU A 94 -14.820 21.294 -10.789 1.00 33.07 C ANISOU 736 CA GLU A 94 4434 4088 4041 360 764 -12 C ATOM 737 C GLU A 94 -14.914 22.223 -12.009 1.00 32.76 C ANISOU 737 C GLU A 94 4417 4034 3997 327 755 -22 C ATOM 738 O GLU A 94 -13.889 22.538 -12.596 1.00 32.98 O ANISOU 738 O GLU A 94 4501 4008 4022 242 709 -128 O ATOM 739 CB GLU A 94 -14.831 22.110 -9.474 1.00 34.03 C ANISOU 739 CB GLU A 94 4691 4166 4072 506 831 -12 C ATOM 740 CG GLU A 94 -14.887 21.263 -8.175 1.00 35.56 C ANISOU 740 CG GLU A 94 4865 4386 4260 561 852 16 C ATOM 741 CD GLU A 94 -14.209 21.937 -6.966 1.00 40.38 C ANISOU 741 CD GLU A 94 5657 4913 4774 645 873 -57 C ATOM 742 OE1 GLU A 94 -13.746 21.215 -6.047 1.00 41.90 O ANISOU 742 OE1 GLU A 94 5851 5102 4965 637 859 -84 O ATOM 743 OE2 GLU A 94 -14.126 23.183 -6.927 1.00 42.62 O ANISOU 743 OE2 GLU A 94 6091 5125 4976 713 895 -87 O ATOM 744 N PRO A 95 -16.128 22.675 -12.393 1.00 33.61 N ANISOU 744 N PRO A 95 4471 4195 4105 397 802 101 N ATOM 745 CA PRO A 95 -16.226 23.602 -13.546 1.00 33.67 C ANISOU 745 CA PRO A 95 4501 4188 4105 368 794 95 C ATOM 746 C PRO A 95 -15.353 24.878 -13.447 1.00 34.19 C ANISOU 746 C PRO A 95 4737 4153 4101 394 799 -9 C ATOM 747 O PRO A 95 -14.776 25.315 -14.449 1.00 34.25 O ANISOU 747 O PRO A 95 4764 4132 4118 304 754 -70 O ATOM 748 CB PRO A 95 -17.716 23.964 -13.587 1.00 34.64 C ANISOU 748 CB PRO A 95 4549 4387 4225 479 862 266 C ATOM 749 CG PRO A 95 -18.396 22.783 -12.927 1.00 34.79 C ANISOU 749 CG PRO A 95 4443 4487 4288 493 867 373 C ATOM 750 CD PRO A 95 -17.460 22.344 -11.838 1.00 33.70 C ANISOU 750 CD PRO A 95 4383 4295 4125 500 861 268 C ATOM 751 N SER A 96 -15.238 25.442 -12.248 1.00 35.03 N ANISOU 751 N SER A 96 4973 4205 4133 510 844 -24 N ATOM 752 CA SER A 96 -14.486 26.679 -12.021 1.00 35.02 C ANISOU 752 CA SER A 96 5161 4092 4053 534 832 -108 C ATOM 753 C SER A 96 -12.964 26.496 -11.854 1.00 34.14 C ANISOU 753 C SER A 96 5113 3913 3944 408 747 -236 C ATOM 754 O SER A 96 -12.246 27.465 -11.605 1.00 34.61 O ANISOU 754 O SER A 96 5332 3875 3942 403 713 -298 O ATOM 755 CB SER A 96 -15.050 27.400 -10.801 1.00 35.53 C ANISOU 755 CB SER A 96 5371 4111 4017 723 909 -65 C ATOM 756 OG SER A 96 -14.869 26.606 -9.635 1.00 36.35 O ANISOU 756 OG SER A 96 5476 4225 4108 757 920 -74 O ATOM 757 N ASP A 97 -12.476 25.263 -11.971 1.00 33.95 N ANISOU 757 N ASP A 97 4971 3940 3990 309 708 -265 N ATOM 758 CA ASP A 97 -11.031 24.988 -11.968 1.00 32.91 C ANISOU 758 CA ASP A 97 4864 3770 3873 189 634 -363 C ATOM 759 C ASP A 97 -10.387 25.539 -13.243 1.00 32.59 C ANISOU 759 C ASP A 97 4814 3717 3851 85 586 -399 C ATOM 760 O ASP A 97 -10.946 25.428 -14.346 1.00 31.69 O ANISOU 760 O ASP A 97 4610 3655 3775 60 597 -364 O ATOM 761 CB ASP A 97 -10.753 23.480 -11.876 1.00 32.80 C ANISOU 761 CB ASP A 97 4721 3817 3926 128 615 -373 C ATOM 762 CG ASP A 97 -10.867 22.940 -10.461 1.00 31.63 C ANISOU 762 CG ASP A 97 4598 3665 3756 199 638 -362 C ATOM 763 OD1 ASP A 97 -10.927 23.748 -9.542 1.00 33.35 O ANISOU 763 OD1 ASP A 97 4951 3824 3897 286 661 -363 O ATOM 764 OD2 ASP A 97 -10.873 21.702 -10.263 1.00 29.79 O ANISOU 764 OD2 ASP A 97 4262 3481 3575 170 631 -352 O ATOM 765 N THR A 98 -9.217 26.148 -13.091 1.00 32.51 N ANISOU 765 N THR A 98 4899 3642 3813 19 528 -457 N ATOM 766 CA THR A 98 -8.487 26.660 -14.265 1.00 32.55 C ANISOU 766 CA THR A 98 4885 3647 3837 -85 481 -478 C ATOM 767 C THR A 98 -7.627 25.542 -14.846 1.00 31.85 C ANISOU 767 C THR A 98 4668 3625 3810 -181 454 -505 C ATOM 768 O THR A 98 -7.434 24.513 -14.212 1.00 31.30 O ANISOU 768 O THR A 98 4550 3579 3762 -177 458 -519 O ATOM 769 CB THR A 98 -7.566 27.831 -13.900 1.00 32.41 C ANISOU 769 CB THR A 98 5017 3533 3763 -128 415 -504 C ATOM 770 OG1 THR A 98 -6.593 27.374 -12.953 1.00 31.35 O ANISOU 770 OG1 THR A 98 4911 3378 3624 -172 368 -535 O ATOM 771 CG2 THR A 98 -8.372 28.984 -13.315 1.00 33.83 C ANISOU 771 CG2 THR A 98 5366 3625 3864 -16 440 -484 C ATOM 772 N ILE A 99 -7.096 25.769 -16.044 1.00 32.78 N ANISOU 772 N ILE A 99 4737 3770 3947 -258 430 -509 N ATOM 773 CA ILE A 99 -6.205 24.818 -16.707 1.00 31.92 C ANISOU 773 CA ILE A 99 4524 3724 3880 -329 414 -530 C ATOM 774 C ILE A 99 -4.890 24.716 -15.922 1.00 33.07 C ANISOU 774 C ILE A 99 4691 3853 4022 -380 370 -547 C ATOM 775 O ILE A 99 -4.303 23.635 -15.802 1.00 33.18 O ANISOU 775 O ILE A 99 4631 3911 4066 -395 372 -561 O ATOM 776 CB ILE A 99 -5.990 25.225 -18.190 1.00 32.12 C ANISOU 776 CB ILE A 99 4505 3787 3912 -382 409 -518 C ATOM 777 CG1 ILE A 99 -7.309 25.135 -18.990 1.00 29.94 C ANISOU 777 CG1 ILE A 99 4196 3537 3644 -342 444 -493 C ATOM 778 CG2 ILE A 99 -4.900 24.406 -18.837 1.00 30.74 C ANISOU 778 CG2 ILE A 99 4246 3674 3760 -435 400 -532 C ATOM 779 CD1 ILE A 99 -7.972 23.764 -18.986 1.00 29.41 C ANISOU 779 CD1 ILE A 99 4058 3510 3607 -317 464 -493 C ATOM 780 N GLU A 100 -4.448 25.839 -15.364 1.00 34.41 N ANISOU 780 N GLU A 100 4969 3953 4152 -405 321 -539 N ATOM 781 CA GLU A 100 -3.298 25.872 -14.436 1.00 35.59 C ANISOU 781 CA GLU A 100 5159 4072 4291 -462 259 -540 C ATOM 782 C GLU A 100 -3.465 24.781 -13.380 1.00 34.73 C ANISOU 782 C GLU A 100 5029 3973 4193 -411 284 -563 C ATOM 783 O GLU A 100 -2.557 23.973 -13.146 1.00 34.46 O ANISOU 783 O GLU A 100 4924 3981 4189 -452 267 -562 O ATOM 784 CB GLU A 100 -3.175 27.270 -13.783 1.00 36.84 C ANISOU 784 CB GLU A 100 5490 4121 4386 -481 192 -531 C ATOM 785 CG GLU A 100 -1.957 27.500 -12.870 1.00 41.08 C ANISOU 785 CG GLU A 100 6092 4612 4904 -567 97 -516 C ATOM 786 CD GLU A 100 -1.852 28.956 -12.370 1.00 44.92 C ANISOU 786 CD GLU A 100 6782 4969 5316 -600 9 -506 C ATOM 787 OE1 GLU A 100 -2.612 29.356 -11.460 1.00 46.10 O ANISOU 787 OE1 GLU A 100 7092 5027 5399 -508 20 -537 O ATOM 788 OE2 GLU A 100 -0.996 29.706 -12.887 1.00 48.96 O ANISOU 788 OE2 GLU A 100 7303 5468 5832 -713 -75 -460 O ATOM 789 N ASN A 101 -4.644 24.746 -12.767 1.00 34.22 N ANISOU 789 N ASN A 101 5020 3878 4105 -314 330 -570 N ATOM 790 CA ASN A 101 -4.926 23.785 -11.701 1.00 34.19 C ANISOU 790 CA ASN A 101 5001 3883 4106 -258 356 -581 C ATOM 791 C ASN A 101 -4.867 22.308 -12.164 1.00 34.09 C ANISOU 791 C ASN A 101 4839 3954 4161 -269 385 -586 C ATOM 792 O ASN A 101 -4.167 21.452 -11.565 1.00 34.24 O ANISOU 792 O ASN A 101 4818 3991 4201 -289 371 -597 O ATOM 793 CB ASN A 101 -6.281 24.120 -11.086 1.00 34.11 C ANISOU 793 CB ASN A 101 5065 3840 4054 -140 410 -563 C ATOM 794 CG ASN A 101 -6.462 23.512 -9.728 1.00 35.41 C ANISOU 794 CG ASN A 101 5261 3994 4199 -77 426 -564 C ATOM 795 OD1 ASN A 101 -5.911 24.014 -8.729 1.00 35.90 O ANISOU 795 OD1 ASN A 101 5448 3987 4204 -77 384 -582 O ATOM 796 ND2 ASN A 101 -7.244 22.433 -9.660 1.00 31.09 N ANISOU 796 ND2 ASN A 101 4607 3511 3695 -28 478 -539 N ATOM 797 N VAL A 102 -5.600 22.014 -13.236 1.00 33.54 N ANISOU 797 N VAL A 102 4700 3926 4118 -256 419 -576 N ATOM 798 CA VAL A 102 -5.576 20.698 -13.862 1.00 32.55 C ANISOU 798 CA VAL A 102 4469 3860 4041 -270 433 -584 C ATOM 799 C VAL A 102 -4.123 20.303 -14.140 1.00 32.85 C ANISOU 799 C VAL A 102 4464 3924 4093 -331 407 -602 C ATOM 800 O VAL A 102 -3.706 19.180 -13.829 1.00 31.97 O ANISOU 800 O VAL A 102 4303 3837 4008 -326 411 -614 O ATOM 801 CB VAL A 102 -6.391 20.718 -15.189 1.00 32.74 C ANISOU 801 CB VAL A 102 4452 3912 4075 -272 450 -568 C ATOM 802 CG1 VAL A 102 -6.374 19.363 -15.892 1.00 30.98 C ANISOU 802 CG1 VAL A 102 4158 3729 3886 -288 449 -581 C ATOM 803 CG2 VAL A 102 -7.826 21.226 -14.959 1.00 32.59 C ANISOU 803 CG2 VAL A 102 4459 3880 4043 -210 479 -522 C ATOM 804 N LYS A 103 -3.351 21.238 -14.711 1.00 33.66 N ANISOU 804 N LYS A 103 4582 4027 4179 -383 382 -591 N ATOM 805 CA LYS A 103 -1.933 20.992 -15.012 1.00 35.01 C ANISOU 805 CA LYS A 103 4696 4243 4363 -436 362 -578 C ATOM 806 C LYS A 103 -1.117 20.611 -13.775 1.00 35.97 C ANISOU 806 C LYS A 103 4820 4356 4492 -452 333 -571 C ATOM 807 O LYS A 103 -0.226 19.760 -13.869 1.00 36.46 O ANISOU 807 O LYS A 103 4805 4470 4578 -460 340 -558 O ATOM 808 CB LYS A 103 -1.291 22.170 -15.769 1.00 35.00 C ANISOU 808 CB LYS A 103 4704 4250 4345 -499 332 -542 C ATOM 809 CG LYS A 103 -1.702 22.233 -17.254 1.00 35.34 C ANISOU 809 CG LYS A 103 4709 4333 4387 -490 367 -542 C ATOM 810 CD LYS A 103 -0.951 23.301 -18.053 1.00 34.40 C ANISOU 810 CD LYS A 103 4580 4237 4254 -554 339 -494 C ATOM 811 CE LYS A 103 -1.478 23.354 -19.480 1.00 34.29 C ANISOU 811 CE LYS A 103 4537 4259 4231 -536 376 -498 C ATOM 812 NZ LYS A 103 -0.726 24.284 -20.375 1.00 33.59 N ANISOU 812 NZ LYS A 103 4422 4209 4131 -593 357 -442 N ATOM 813 N ALA A 104 -1.448 21.210 -12.628 1.00 37.51 N ANISOU 813 N ALA A 104 5110 4485 4659 -446 303 -575 N ATOM 814 CA ALA A 104 -0.828 20.842 -11.353 1.00 39.31 C ANISOU 814 CA ALA A 104 5355 4695 4884 -459 269 -571 C ATOM 815 C ALA A 104 -1.220 19.454 -10.906 1.00 39.89 C ANISOU 815 C ALA A 104 5371 4796 4990 -400 313 -593 C ATOM 816 O ALA A 104 -0.389 18.743 -10.362 1.00 40.81 O ANISOU 816 O ALA A 104 5443 4938 5127 -417 298 -582 O ATOM 817 CB ALA A 104 -1.142 21.853 -10.274 1.00 40.05 C ANISOU 817 CB ALA A 104 5595 4699 4921 -455 225 -575 C ATOM 818 N LYS A 105 -2.470 19.053 -11.152 1.00 40.50 N ANISOU 818 N LYS A 105 5444 4870 5074 -337 359 -611 N ATOM 819 CA LYS A 105 -2.893 17.665 -10.900 1.00 40.49 C ANISOU 819 CA LYS A 105 5382 4893 5108 -294 388 -621 C ATOM 820 C LYS A 105 -2.157 16.664 -11.778 1.00 40.68 C ANISOU 820 C LYS A 105 5325 4967 5166 -309 398 -629 C ATOM 821 O LYS A 105 -1.757 15.582 -11.311 1.00 40.95 O ANISOU 821 O LYS A 105 5319 5015 5224 -294 402 -634 O ATOM 822 CB LYS A 105 -4.404 17.497 -11.070 1.00 40.70 C ANISOU 822 CB LYS A 105 5413 4914 5138 -241 420 -612 C ATOM 823 CG LYS A 105 -5.227 17.921 -9.841 1.00 40.90 C ANISOU 823 CG LYS A 105 5503 4907 5132 -181 433 -591 C ATOM 824 CD LYS A 105 -6.707 17.900 -10.148 1.00 41.42 C ANISOU 824 CD LYS A 105 5550 4986 5203 -127 470 -550 C ATOM 825 CE LYS A 105 -7.504 18.716 -9.139 1.00 43.57 C ANISOU 825 CE LYS A 105 5902 5230 5422 -44 500 -516 C ATOM 826 NZ LYS A 105 -8.123 17.789 -8.182 1.00 43.36 N ANISOU 826 NZ LYS A 105 5835 5230 5412 10 523 -476 N ATOM 827 N ILE A 106 -1.982 17.013 -13.050 1.00 40.23 N ANISOU 827 N ILE A 106 5250 4933 5102 -328 408 -629 N ATOM 828 CA ILE A 106 -1.192 16.180 -13.950 1.00 40.27 C ANISOU 828 CA ILE A 106 5197 4985 5118 -321 427 -632 C ATOM 829 C ILE A 106 0.261 16.055 -13.469 1.00 40.68 C ANISOU 829 C ILE A 106 5203 5074 5178 -342 418 -599 C ATOM 830 O ILE A 106 0.806 14.965 -13.432 1.00 39.95 O ANISOU 830 O ILE A 106 5069 5009 5102 -307 438 -599 O ATOM 831 CB ILE A 106 -1.251 16.660 -15.417 1.00 40.19 C ANISOU 831 CB ILE A 106 5185 4999 5088 -329 443 -631 C ATOM 832 CG1 ILE A 106 -2.683 16.520 -15.965 1.00 39.92 C ANISOU 832 CG1 ILE A 106 5182 4935 5049 -312 446 -652 C ATOM 833 CG2 ILE A 106 -0.273 15.848 -16.267 1.00 40.34 C ANISOU 833 CG2 ILE A 106 5157 5070 5099 -300 474 -626 C ATOM 834 CD1 ILE A 106 -2.924 17.217 -17.320 1.00 37.12 C ANISOU 834 CD1 ILE A 106 4837 4597 4671 -328 454 -647 C ATOM 835 N GLN A 107 0.874 17.164 -13.079 1.00 42.20 N ANISOU 835 N GLN A 107 5410 5267 5359 -400 379 -562 N ATOM 836 CA GLN A 107 2.209 17.106 -12.461 1.00 44.52 C ANISOU 836 CA GLN A 107 5654 5597 5664 -439 350 -507 C ATOM 837 C GLN A 107 2.312 16.026 -11.359 1.00 45.40 C ANISOU 837 C GLN A 107 5750 5701 5798 -407 353 -519 C ATOM 838 O GLN A 107 3.205 15.168 -11.416 1.00 46.68 O ANISOU 838 O GLN A 107 5838 5917 5980 -385 374 -489 O ATOM 839 CB GLN A 107 2.643 18.481 -11.953 1.00 45.02 C ANISOU 839 CB GLN A 107 5768 5632 5707 -525 278 -464 C ATOM 840 CG GLN A 107 4.079 18.540 -11.436 1.00 47.80 C ANISOU 840 CG GLN A 107 6059 6030 6072 -592 227 -380 C ATOM 841 CD GLN A 107 4.526 19.957 -11.152 1.00 49.92 C ANISOU 841 CD GLN A 107 6390 6261 6316 -698 133 -326 C ATOM 842 OE1 GLN A 107 3.753 20.776 -10.647 1.00 50.97 O ANISOU 842 OE1 GLN A 107 6653 6302 6411 -711 94 -370 O ATOM 843 NE2 GLN A 107 5.779 20.261 -11.485 1.00 50.54 N ANISOU 843 NE2 GLN A 107 6381 6411 6410 -773 93 -220 N ATOM 844 N ASP A 108 1.382 16.020 -10.405 1.00 45.68 N ANISOU 844 N ASP A 108 5853 5675 5827 -392 339 -557 N ATOM 845 CA ASP A 108 1.406 15.032 -9.316 1.00 46.61 C ANISOU 845 CA ASP A 108 5959 5787 5966 -364 339 -564 C ATOM 846 C ASP A 108 1.425 13.589 -9.786 1.00 47.24 C ANISOU 846 C ASP A 108 5978 5894 6076 -306 384 -580 C ATOM 847 O ASP A 108 2.201 12.770 -9.270 1.00 47.53 O ANISOU 847 O ASP A 108 5968 5958 6135 -293 387 -558 O ATOM 848 CB ASP A 108 0.224 15.213 -8.372 1.00 46.10 C ANISOU 848 CB ASP A 108 5971 5663 5882 -337 334 -592 C ATOM 849 CG ASP A 108 0.206 16.566 -7.728 1.00 47.62 C ANISOU 849 CG ASP A 108 6260 5806 6026 -374 288 -583 C ATOM 850 OD1 ASP A 108 1.291 17.182 -7.603 1.00 49.18 O ANISOU 850 OD1 ASP A 108 6464 6010 6213 -444 235 -547 O ATOM 851 OD2 ASP A 108 -0.898 17.019 -7.352 1.00 50.22 O ANISOU 851 OD2 ASP A 108 6667 6091 6324 -330 301 -601 O ATOM 852 N LYS A 109 0.566 13.280 -10.752 1.00 47.47 N ANISOU 852 N LYS A 109 6022 5912 6103 -272 413 -614 N ATOM 853 CA LYS A 109 0.330 11.906 -11.126 1.00 48.18 C ANISOU 853 CA LYS A 109 6099 5998 6211 -219 437 -638 C ATOM 854 C LYS A 109 1.284 11.399 -12.199 1.00 49.21 C ANISOU 854 C LYS A 109 6196 6170 6329 -183 472 -630 C ATOM 855 O LYS A 109 1.344 10.193 -12.456 1.00 49.72 O ANISOU 855 O LYS A 109 6269 6223 6397 -128 491 -649 O ATOM 856 CB LYS A 109 -1.127 11.719 -11.548 1.00 48.04 C ANISOU 856 CB LYS A 109 6123 5938 6192 -209 432 -665 C ATOM 857 CG LYS A 109 -2.118 12.357 -10.578 1.00 48.87 C ANISOU 857 CG LYS A 109 6254 6018 6298 -222 415 -653 C ATOM 858 CD LYS A 109 -3.557 12.137 -10.987 1.00 48.36 C ANISOU 858 CD LYS A 109 6205 5930 6238 -212 410 -648 C ATOM 859 CE LYS A 109 -4.097 10.859 -10.387 1.00 49.25 C ANISOU 859 CE LYS A 109 6302 6026 6384 -196 394 -635 C ATOM 860 NZ LYS A 109 -5.575 10.898 -10.323 1.00 49.58 N ANISOU 860 NZ LYS A 109 6342 6061 6437 -195 381 -592 N ATOM 861 N GLU A 110 2.027 12.303 -12.827 1.00 49.92 N ANISOU 861 N GLU A 110 6259 6309 6401 -207 482 -596 N ATOM 862 CA GLU A 110 2.885 11.912 -13.941 1.00 51.46 C ANISOU 862 CA GLU A 110 6420 6558 6573 -154 530 -574 C ATOM 863 C GLU A 110 4.317 12.425 -13.852 1.00 52.14 C ANISOU 863 C GLU A 110 6420 6729 6664 -173 540 -485 C ATOM 864 O GLU A 110 5.210 11.858 -14.470 1.00 53.32 O ANISOU 864 O GLU A 110 6520 6940 6798 -104 593 -443 O ATOM 865 CB GLU A 110 2.256 12.304 -15.285 1.00 51.73 C ANISOU 865 CB GLU A 110 6500 6584 6572 -145 546 -604 C ATOM 866 CG GLU A 110 0.945 11.575 -15.615 1.00 52.64 C ANISOU 866 CG GLU A 110 6695 6625 6680 -125 531 -670 C ATOM 867 CD GLU A 110 1.094 10.060 -15.767 1.00 55.57 C ANISOU 867 CD GLU A 110 7104 6969 7042 -50 546 -697 C ATOM 868 OE1 GLU A 110 2.220 9.574 -16.035 1.00 57.25 O ANISOU 868 OE1 GLU A 110 7291 7227 7235 18 594 -671 O ATOM 869 OE2 GLU A 110 0.068 9.349 -15.629 1.00 56.73 O ANISOU 869 OE2 GLU A 110 7310 7047 7198 -56 509 -734 O ATOM 870 N GLY A 111 4.530 13.490 -13.084 1.00 52.02 N ANISOU 870 N GLY A 111 6389 6715 6662 -263 484 -446 N ATOM 871 CA GLY A 111 5.852 14.091 -12.945 1.00 52.20 C ANISOU 871 CA GLY A 111 6326 6814 6692 -313 465 -339 C ATOM 872 C GLY A 111 6.235 14.894 -14.174 1.00 52.37 C ANISOU 872 C GLY A 111 6313 6893 6690 -326 484 -289 C ATOM 873 O GLY A 111 7.370 14.787 -14.674 1.00 53.04 O ANISOU 873 O GLY A 111 6301 7077 6773 -301 518 -191 O ATOM 874 N ILE A 112 5.277 15.684 -14.668 1.00 51.11 N ANISOU 874 N ILE A 112 6227 6681 6512 -357 467 -345 N ATOM 875 CA ILE A 112 5.493 16.522 -15.841 1.00 50.55 C ANISOU 875 CA ILE A 112 6133 6655 6417 -375 479 -304 C ATOM 876 C ILE A 112 5.277 17.983 -15.454 1.00 49.58 C ANISOU 876 C ILE A 112 6054 6488 6295 -488 397 -284 C ATOM 877 O ILE A 112 4.167 18.369 -15.091 1.00 49.16 O ANISOU 877 O ILE A 112 6098 6348 6234 -502 371 -359 O ATOM 878 CB ILE A 112 4.566 16.135 -17.060 1.00 50.45 C ANISOU 878 CB ILE A 112 6176 6621 6370 -301 536 -382 C ATOM 879 CG1 ILE A 112 4.450 14.618 -17.239 1.00 50.62 C ANISOU 879 CG1 ILE A 112 6217 6635 6381 -192 593 -432 C ATOM 880 CG2 ILE A 112 5.083 16.755 -18.350 1.00 51.04 C ANISOU 880 CG2 ILE A 112 6208 6771 6415 -296 568 -322 C ATOM 881 CD1 ILE A 112 3.333 14.171 -18.201 1.00 50.05 C ANISOU 881 CD1 ILE A 112 6235 6509 6274 -144 613 -517 C ATOM 882 N PRO A 113 6.342 18.798 -15.524 1.00 49.52 N ANISOU 882 N PRO A 113 5982 6541 6294 -567 353 -171 N ATOM 883 CA PRO A 113 6.224 20.226 -15.283 1.00 49.11 C ANISOU 883 CA PRO A 113 5990 6436 6233 -679 262 -144 C ATOM 884 C PRO A 113 5.130 20.839 -16.151 1.00 47.97 C ANISOU 884 C PRO A 113 5922 6242 6063 -662 283 -215 C ATOM 885 O PRO A 113 5.055 20.527 -17.333 1.00 47.95 O ANISOU 885 O PRO A 113 5875 6295 6048 -602 352 -219 O ATOM 886 CB PRO A 113 7.588 20.768 -15.716 1.00 50.29 C ANISOU 886 CB PRO A 113 6025 6689 6396 -751 229 11 C ATOM 887 CG PRO A 113 8.517 19.624 -15.578 1.00 51.22 C ANISOU 887 CG PRO A 113 6023 6904 6534 -687 285 75 C ATOM 888 CD PRO A 113 7.717 18.408 -15.888 1.00 50.59 C ANISOU 888 CD PRO A 113 5979 6801 6441 -549 385 -45 C ATOM 889 N PRO A 114 4.273 21.692 -15.556 1.00 47.25 N ANISOU 889 N PRO A 114 5951 6045 5956 -703 226 -268 N ATOM 890 CA PRO A 114 3.195 22.412 -16.249 1.00 46.07 C ANISOU 890 CA PRO A 114 5877 5845 5783 -690 239 -321 C ATOM 891 C PRO A 114 3.601 23.131 -17.551 1.00 46.04 C ANISOU 891 C PRO A 114 5820 5900 5771 -724 244 -258 C ATOM 892 O PRO A 114 2.826 23.128 -18.521 1.00 45.35 O ANISOU 892 O PRO A 114 5744 5816 5669 -676 295 -302 O ATOM 893 CB PRO A 114 2.737 23.427 -15.203 1.00 46.08 C ANISOU 893 CB PRO A 114 6013 5734 5761 -742 159 -340 C ATOM 894 CG PRO A 114 2.980 22.746 -13.893 1.00 46.52 C ANISOU 894 CG PRO A 114 6083 5767 5824 -734 139 -354 C ATOM 895 CD PRO A 114 4.136 21.790 -14.088 1.00 46.77 C ANISOU 895 CD PRO A 114 5974 5904 5891 -734 164 -291 C ATOM 896 N ASP A 115 4.784 23.750 -17.571 1.00 46.49 N ANISOU 896 N ASP A 115 5819 6007 5838 -813 185 -146 N ATOM 897 CA ASP A 115 5.236 24.522 -18.748 1.00 46.33 C ANISOU 897 CA ASP A 115 5740 6050 5811 -855 182 -64 C ATOM 898 C ASP A 115 5.545 23.631 -19.944 1.00 45.19 C ANISOU 898 C ASP A 115 5485 6025 5662 -762 290 -46 C ATOM 899 O ASP A 115 5.730 24.122 -21.053 1.00 46.28 O ANISOU 899 O ASP A 115 5578 6221 5785 -767 311 6 O ATOM 900 CB ASP A 115 6.444 25.440 -18.420 1.00 47.81 C ANISOU 900 CB ASP A 115 5887 6265 6013 -991 74 78 C ATOM 901 CG ASP A 115 7.721 24.663 -18.035 1.00 49.48 C ANISOU 901 CG ASP A 115 5963 6584 6254 -999 77 185 C ATOM 902 OD1 ASP A 115 7.690 23.417 -17.956 1.00 49.85 O ANISOU 902 OD1 ASP A 115 5961 6673 6307 -892 166 138 O ATOM 903 OD2 ASP A 115 8.771 25.313 -17.792 1.00 52.23 O ANISOU 903 OD2 ASP A 115 6253 6972 6621 -1118 -17 329 O ATOM 904 N GLN A 116 5.608 22.328 -19.694 1.00 43.65 N ANISOU 904 N GLN A 116 5257 5857 5471 -671 355 -87 N ATOM 905 CA GLN A 116 5.867 21.319 -20.714 1.00 42.94 C ANISOU 905 CA GLN A 116 5100 5856 5358 -557 459 -85 C ATOM 906 C GLN A 116 4.613 20.584 -21.171 1.00 40.95 C ANISOU 906 C GLN A 116 4937 5543 5081 -469 512 -218 C ATOM 907 O GLN A 116 4.669 19.823 -22.133 1.00 40.85 O ANISOU 907 O GLN A 116 4911 5579 5032 -376 587 -232 O ATOM 908 CB GLN A 116 6.868 20.286 -20.198 1.00 43.31 C ANISOU 908 CB GLN A 116 5062 5974 5421 -504 495 -29 C ATOM 909 CG GLN A 116 8.258 20.821 -19.992 1.00 45.97 C ANISOU 909 CG GLN A 116 5275 6410 5782 -579 454 140 C ATOM 910 CD GLN A 116 9.200 19.765 -19.469 1.00 49.75 C ANISOU 910 CD GLN A 116 5660 6964 6277 -516 496 205 C ATOM 911 OE1 GLN A 116 10.347 20.061 -19.118 1.00 54.01 O ANISOU 911 OE1 GLN A 116 6086 7591 6845 -580 456 359 O ATOM 912 NE2 GLN A 116 8.727 18.515 -19.413 1.00 50.10 N ANISOU 912 NE2 GLN A 116 5752 6977 6305 -395 569 100 N ATOM 913 N GLN A 117 3.498 20.786 -20.473 1.00 38.80 N ANISOU 913 N GLN A 117 4759 5164 4820 -496 471 -305 N ATOM 914 CA GLN A 117 2.229 20.170 -20.862 1.00 37.37 C ANISOU 914 CA GLN A 117 4650 4926 4622 -435 502 -405 C ATOM 915 C GLN A 117 1.452 21.009 -21.852 1.00 36.56 C ANISOU 915 C GLN A 117 4586 4808 4496 -455 499 -418 C ATOM 916 O GLN A 117 1.294 22.206 -21.653 1.00 36.64 O ANISOU 916 O GLN A 117 4619 4788 4515 -525 451 -392 O ATOM 917 CB GLN A 117 1.335 19.966 -19.656 1.00 36.29 C ANISOU 917 CB GLN A 117 4579 4701 4510 -443 468 -467 C ATOM 918 CG GLN A 117 1.912 19.163 -18.531 1.00 36.99 C ANISOU 918 CG GLN A 117 4641 4789 4622 -430 463 -463 C ATOM 919 CD GLN A 117 0.970 19.131 -17.354 1.00 37.43 C ANISOU 919 CD GLN A 117 4765 4762 4695 -436 430 -514 C ATOM 920 OE1 GLN A 117 -0.258 19.204 -17.521 1.00 37.34 O ANISOU 920 OE1 GLN A 117 4808 4703 4677 -418 435 -560 O ATOM 921 NE2 GLN A 117 1.530 19.042 -16.150 1.00 37.79 N ANISOU 921 NE2 GLN A 117 4805 4795 4758 -461 398 -495 N ATOM 922 N ARG A 118 0.946 20.375 -22.906 1.00 36.23 N ANISOU 922 N ARG A 118 4567 4779 4422 -395 543 -458 N ATOM 923 CA ARG A 118 0.007 21.017 -23.835 1.00 35.55 C ANISOU 923 CA ARG A 118 4523 4672 4313 -411 537 -477 C ATOM 924 C ARG A 118 -1.308 20.268 -23.711 1.00 33.94 C ANISOU 924 C ARG A 118 4385 4400 4110 -384 528 -550 C ATOM 925 O ARG A 118 -1.352 19.069 -23.949 1.00 34.57 O ANISOU 925 O ARG A 118 4487 4477 4171 -329 549 -587 O ATOM 926 CB ARG A 118 0.483 20.929 -25.298 1.00 36.41 C ANISOU 926 CB ARG A 118 4610 4855 4370 -371 584 -450 C ATOM 927 CG ARG A 118 1.765 21.700 -25.661 1.00 41.37 C ANISOU 927 CG ARG A 118 5150 5575 4994 -397 597 -347 C ATOM 928 CD ARG A 118 2.156 21.582 -27.166 1.00 46.01 C ANISOU 928 CD ARG A 118 5718 6246 5518 -336 658 -314 C ATOM 929 NE ARG A 118 1.654 22.692 -27.983 1.00 50.39 N ANISOU 929 NE ARG A 118 6284 6800 6061 -391 636 -294 N ATOM 930 CZ ARG A 118 0.466 22.704 -28.594 1.00 52.72 C ANISOU 930 CZ ARG A 118 6657 7042 6334 -389 626 -360 C ATOM 931 NH1 ARG A 118 -0.353 21.665 -28.497 1.00 53.21 N ANISOU 931 NH1 ARG A 118 6792 7043 6382 -345 625 -443 N ATOM 932 NH2 ARG A 118 0.080 23.756 -29.300 1.00 53.19 N ANISOU 932 NH2 ARG A 118 6717 7106 6386 -438 607 -331 N ATOM 933 N LEU A 119 -2.371 20.966 -23.325 1.00 32.07 N ANISOU 933 N LEU A 119 4184 4108 3894 -420 496 -559 N ATOM 934 CA LEU A 119 -3.702 20.386 -23.277 1.00 30.08 C ANISOU 934 CA LEU A 119 3973 3808 3648 -404 482 -594 C ATOM 935 C LEU A 119 -4.548 20.883 -24.446 1.00 29.49 C ANISOU 935 C LEU A 119 3919 3736 3549 -420 475 -585 C ATOM 936 O LEU A 119 -4.608 22.096 -24.709 1.00 28.45 O ANISOU 936 O LEU A 119 3783 3610 3416 -451 471 -553 O ATOM 937 CB LEU A 119 -4.395 20.709 -21.942 1.00 29.63 C ANISOU 937 CB LEU A 119 3932 3699 3628 -411 461 -591 C ATOM 938 CG LEU A 119 -3.841 19.996 -20.703 1.00 30.27 C ANISOU 938 CG LEU A 119 4001 3768 3732 -394 460 -605 C ATOM 939 CD1 LEU A 119 -4.339 20.640 -19.446 1.00 30.01 C ANISOU 939 CD1 LEU A 119 3998 3689 3716 -395 445 -594 C ATOM 940 CD2 LEU A 119 -4.181 18.523 -20.697 1.00 30.40 C ANISOU 940 CD2 LEU A 119 4021 3776 3755 -360 462 -636 C ATOM 941 N ILE A 120 -5.198 19.932 -25.127 1.00 28.41 N ANISOU 941 N ILE A 120 3816 3588 3391 -404 464 -609 N ATOM 942 CA ILE A 120 -5.999 20.185 -26.316 1.00 27.35 C ANISOU 942 CA ILE A 120 3709 3457 3227 -424 446 -598 C ATOM 943 C ILE A 120 -7.426 19.695 -26.095 1.00 27.40 C ANISOU 943 C ILE A 120 3733 3421 3255 -444 400 -586 C ATOM 944 O ILE A 120 -7.647 18.557 -25.637 1.00 26.13 O ANISOU 944 O ILE A 120 3593 3230 3104 -434 376 -605 O ATOM 945 CB ILE A 120 -5.471 19.412 -27.581 1.00 28.67 C ANISOU 945 CB ILE A 120 3921 3646 3324 -394 458 -627 C ATOM 946 CG1 ILE A 120 -3.929 19.256 -27.628 1.00 29.29 C ANISOU 946 CG1 ILE A 120 3973 3778 3378 -343 514 -629 C ATOM 947 CG2 ILE A 120 -6.152 19.887 -28.903 1.00 28.41 C ANISOU 947 CG2 ILE A 120 3921 3624 3251 -422 438 -610 C ATOM 948 CD1 ILE A 120 -3.119 20.495 -27.794 1.00 32.85 C ANISOU 948 CD1 ILE A 120 4358 4288 3834 -364 542 -577 C ATOM 949 N PHE A 121 -8.378 20.556 -26.460 1.00 26.29 N ANISOU 949 N PHE A 121 3582 3283 3124 -473 386 -540 N ATOM 950 CA PHE A 121 -9.809 20.265 -26.443 1.00 26.23 C ANISOU 950 CA PHE A 121 3570 3257 3138 -498 340 -492 C ATOM 951 C PHE A 121 -10.469 21.126 -27.506 1.00 26.71 C ANISOU 951 C PHE A 121 3628 3339 3181 -529 328 -447 C ATOM 952 O PHE A 121 -10.020 22.270 -27.747 1.00 25.68 O ANISOU 952 O PHE A 121 3486 3229 3043 -523 364 -442 O ATOM 953 CB PHE A 121 -10.417 20.610 -25.079 1.00 26.31 C ANISOU 953 CB PHE A 121 3539 3257 3200 -475 355 -449 C ATOM 954 CG PHE A 121 -11.839 20.114 -24.891 1.00 25.75 C ANISOU 954 CG PHE A 121 3440 3184 3159 -492 313 -373 C ATOM 955 CD1 PHE A 121 -12.095 18.766 -24.653 1.00 23.86 C ANISOU 955 CD1 PHE A 121 3209 2924 2932 -513 263 -375 C ATOM 956 CD2 PHE A 121 -12.917 21.014 -24.927 1.00 24.57 C ANISOU 956 CD2 PHE A 121 3251 3057 3027 -486 321 -285 C ATOM 957 CE1 PHE A 121 -13.388 18.304 -24.453 1.00 25.58 C ANISOU 957 CE1 PHE A 121 3388 3149 3184 -544 212 -280 C ATOM 958 CE2 PHE A 121 -14.231 20.562 -24.736 1.00 23.55 C ANISOU 958 CE2 PHE A 121 3073 2945 2930 -502 283 -184 C ATOM 959 CZ PHE A 121 -14.465 19.209 -24.488 1.00 25.05 C ANISOU 959 CZ PHE A 121 3261 3119 3137 -538 224 -176 C ATOM 960 N ALA A 122 -11.503 20.563 -28.139 1.00 27.22 N ANISOU 960 N ALA A 122 3706 3398 3240 -571 267 -407 N ATOM 961 CA ALA A 122 -12.162 21.122 -29.326 1.00 29.29 C ANISOU 961 CA ALA A 122 3973 3679 3476 -612 238 -362 C ATOM 962 C ALA A 122 -11.177 21.688 -30.330 1.00 30.69 C ANISOU 962 C ALA A 122 4182 3880 3598 -603 272 -409 C ATOM 963 O ALA A 122 -11.439 22.730 -30.935 1.00 31.70 O ANISOU 963 O ALA A 122 4289 4034 3722 -618 283 -370 O ATOM 964 CB ALA A 122 -13.240 22.152 -28.956 1.00 29.12 C ANISOU 964 CB ALA A 122 3883 3680 3500 -610 251 -266 C ATOM 965 N GLY A 123 -10.035 21.015 -30.482 1.00 31.49 N ANISOU 965 N GLY A 123 4329 3978 3660 -572 293 -482 N ATOM 966 CA GLY A 123 -9.028 21.387 -31.477 1.00 33.47 C ANISOU 966 CA GLY A 123 4603 4266 3850 -551 332 -511 C ATOM 967 C GLY A 123 -8.182 22.603 -31.109 1.00 34.31 C ANISOU 967 C GLY A 123 4646 4409 3980 -536 391 -495 C ATOM 968 O GLY A 123 -7.432 23.114 -31.939 1.00 35.64 O ANISOU 968 O GLY A 123 4811 4622 4108 -528 421 -490 O ATOM 969 N LYS A 124 -8.277 23.045 -29.861 1.00 33.76 N ANISOU 969 N LYS A 124 4536 4321 3972 -533 402 -480 N ATOM 970 CA LYS A 124 -7.602 24.242 -29.406 1.00 33.94 C ANISOU 970 CA LYS A 124 4525 4355 4016 -535 432 -459 C ATOM 971 C LYS A 124 -6.615 23.899 -28.301 1.00 33.15 C ANISOU 971 C LYS A 124 4410 4247 3937 -512 451 -485 C ATOM 972 O LYS A 124 -6.905 23.077 -27.438 1.00 31.87 O ANISOU 972 O LYS A 124 4256 4055 3798 -493 443 -509 O ATOM 973 CB LYS A 124 -8.646 25.207 -28.843 1.00 34.51 C ANISOU 973 CB LYS A 124 4590 4395 4127 -543 422 -413 C ATOM 974 CG LYS A 124 -9.614 25.761 -29.878 1.00 36.71 C ANISOU 974 CG LYS A 124 4867 4688 4393 -567 405 -366 C ATOM 975 CD LYS A 124 -10.987 26.030 -29.241 1.00 40.94 C ANISOU 975 CD LYS A 124 5390 5198 4966 -551 396 -309 C ATOM 976 CE LYS A 124 -10.890 26.982 -28.054 1.00 43.94 C ANISOU 976 CE LYS A 124 5785 5541 5371 -511 426 -296 C ATOM 977 NZ LYS A 124 -12.164 27.095 -27.283 1.00 44.78 N ANISOU 977 NZ LYS A 124 5879 5630 5504 -462 436 -235 N ATOM 978 N GLN A 125 -5.458 24.547 -28.337 1.00 33.88 N ANISOU 978 N GLN A 125 4477 4372 4023 -522 470 -469 N ATOM 979 CA GLN A 125 -4.503 24.592 -27.214 1.00 34.21 C ANISOU 979 CA GLN A 125 4499 4407 4091 -522 473 -468 C ATOM 980 C GLN A 125 -5.105 25.409 -26.081 1.00 33.67 C ANISOU 980 C GLN A 125 4462 4274 4058 -535 449 -458 C ATOM 981 O GLN A 125 -5.364 26.606 -26.237 1.00 33.36 O ANISOU 981 O GLN A 125 4444 4213 4018 -561 434 -424 O ATOM 982 CB GLN A 125 -3.185 25.239 -27.665 1.00 35.27 C ANISOU 982 CB GLN A 125 4589 4601 4212 -548 483 -420 C ATOM 983 CG GLN A 125 -2.045 25.107 -26.645 1.00 38.50 C ANISOU 983 CG GLN A 125 4965 5019 4644 -557 477 -401 C ATOM 984 CD GLN A 125 -1.125 26.339 -26.526 1.00 44.18 C ANISOU 984 CD GLN A 125 5656 5757 5376 -627 442 -324 C ATOM 985 OE1 GLN A 125 -0.164 26.312 -25.753 1.00 47.01 O ANISOU 985 OE1 GLN A 125 5983 6127 5753 -653 422 -290 O ATOM 986 NE2 GLN A 125 -1.418 27.416 -27.274 1.00 46.08 N ANISOU 986 NE2 GLN A 125 5908 5995 5605 -665 425 -289 N ATOM 987 N LEU A 126 -5.323 24.763 -24.935 1.00 33.76 N ANISOU 987 N LEU A 126 4485 4249 4092 -509 446 -484 N ATOM 988 CA LEU A 126 -6.039 25.376 -23.808 1.00 33.28 C ANISOU 988 CA LEU A 126 4470 4125 4049 -493 435 -476 C ATOM 989 C LEU A 126 -5.183 26.336 -23.000 1.00 33.48 C ANISOU 989 C LEU A 126 4535 4114 4073 -522 408 -461 C ATOM 990 O LEU A 126 -4.009 26.046 -22.751 1.00 33.72 O ANISOU 990 O LEU A 126 4537 4169 4108 -551 396 -460 O ATOM 991 CB LEU A 126 -6.619 24.276 -22.901 1.00 33.28 C ANISOU 991 CB LEU A 126 4467 4108 4069 -452 443 -500 C ATOM 992 CG LEU A 126 -7.544 23.269 -23.608 1.00 33.49 C ANISOU 992 CG LEU A 126 4469 4156 4099 -441 444 -501 C ATOM 993 CD1 LEU A 126 -8.123 22.285 -22.602 1.00 32.71 C ANISOU 993 CD1 LEU A 126 4364 4038 4026 -410 441 -506 C ATOM 994 CD2 LEU A 126 -8.679 23.979 -24.398 1.00 34.70 C ANISOU 994 CD2 LEU A 126 4624 4313 4246 -447 440 -455 C ATOM 995 N GLU A 127 -5.770 27.461 -22.574 1.00 33.18 N ANISOU 995 N GLU A 127 4570 4013 4024 -513 394 -442 N ATOM 996 CA GLU A 127 -5.009 28.512 -21.882 1.00 33.32 C ANISOU 996 CA GLU A 127 4662 3972 4026 -553 346 -425 C ATOM 997 C GLU A 127 -5.074 28.340 -20.382 1.00 33.79 C ANISOU 997 C GLU A 127 4792 3968 4078 -516 335 -449 C ATOM 998 O GLU A 127 -6.134 28.012 -19.839 1.00 32.74 O ANISOU 998 O GLU A 127 4682 3816 3943 -439 373 -461 O ATOM 999 CB GLU A 127 -5.489 29.924 -22.242 1.00 33.42 C ANISOU 999 CB GLU A 127 4752 3930 4015 -559 327 -394 C ATOM 1000 CG GLU A 127 -5.353 30.307 -23.698 1.00 31.73 C ANISOU 1000 CG GLU A 127 4478 3773 3803 -603 329 -362 C ATOM 1001 CD GLU A 127 -3.923 30.692 -24.133 1.00 31.14 C ANISOU 1001 CD GLU A 127 4366 3735 3731 -695 282 -322 C ATOM 1002 OE1 GLU A 127 -3.693 30.798 -25.359 1.00 30.25 O ANISOU 1002 OE1 GLU A 127 4186 3691 3618 -723 295 -291 O ATOM 1003 OE2 GLU A 127 -3.036 30.893 -23.278 1.00 26.81 O ANISOU 1003 OE2 GLU A 127 3851 3153 3184 -741 230 -309 O ATOM 1004 N ASP A 128 -3.941 28.604 -19.728 1.00 34.53 N ANISOU 1004 N ASP A 128 4917 4036 4166 -575 279 -441 N ATOM 1005 CA ASP A 128 -3.736 28.288 -18.319 1.00 36.25 C ANISOU 1005 CA ASP A 128 5195 4204 4374 -555 259 -464 C ATOM 1006 C ASP A 128 -4.696 28.990 -17.356 1.00 36.92 C ANISOU 1006 C ASP A 128 5425 4189 4413 -478 263 -477 C ATOM 1007 O ASP A 128 -5.016 28.445 -16.286 1.00 36.66 O ANISOU 1007 O ASP A 128 5426 4134 4370 -418 283 -500 O ATOM 1008 CB ASP A 128 -2.283 28.555 -17.897 1.00 36.83 C ANISOU 1008 CB ASP A 128 5276 4270 4448 -653 180 -433 C ATOM 1009 CG ASP A 128 -1.304 27.553 -18.496 1.00 38.78 C ANISOU 1009 CG ASP A 128 5371 4629 4736 -691 199 -412 C ATOM 1010 OD1 ASP A 128 -0.083 27.789 -18.410 1.00 42.54 O ANISOU 1010 OD1 ASP A 128 5815 5129 5220 -774 140 -356 O ATOM 1011 OD2 ASP A 128 -1.743 26.536 -19.071 1.00 38.60 O ANISOU 1011 OD2 ASP A 128 5265 4669 4732 -634 268 -440 O ATOM 1012 N GLY A 129 -5.155 30.175 -17.751 1.00 37.68 N ANISOU 1012 N GLY A 129 5609 4229 4478 -469 251 -457 N ATOM 1013 CA GLY A 129 -5.958 31.031 -16.882 1.00 39.24 C ANISOU 1013 CA GLY A 129 5975 4320 4613 -380 256 -462 C ATOM 1014 C GLY A 129 -7.450 30.930 -17.112 1.00 39.35 C ANISOU 1014 C GLY A 129 5967 4358 4625 -259 347 -446 C ATOM 1015 O GLY A 129 -8.221 31.489 -16.339 1.00 40.40 O ANISOU 1015 O GLY A 129 6226 4421 4702 -151 376 -438 O ATOM 1016 N ARG A 130 -7.849 30.247 -18.184 1.00 38.44 N ANISOU 1016 N ARG A 130 5701 4343 4563 -273 388 -430 N ATOM 1017 CA ARG A 130 -9.257 30.005 -18.488 1.00 38.17 C ANISOU 1017 CA ARG A 130 5614 4351 4538 -180 461 -392 C ATOM 1018 C ARG A 130 -9.742 28.744 -17.736 1.00 37.47 C ANISOU 1018 C ARG A 130 5456 4309 4473 -126 501 -392 C ATOM 1019 O ARG A 130 -8.930 27.942 -17.247 1.00 36.97 O ANISOU 1019 O ARG A 130 5364 4257 4428 -171 476 -432 O ATOM 1020 CB ARG A 130 -9.506 29.891 -20.009 1.00 38.18 C ANISOU 1020 CB ARG A 130 5502 4426 4576 -233 468 -367 C ATOM 1021 CG ARG A 130 -8.958 31.051 -20.902 1.00 39.41 C ANISOU 1021 CG ARG A 130 5702 4554 4718 -300 426 -358 C ATOM 1022 CD ARG A 130 -9.753 31.180 -22.204 1.00 42.74 C ANISOU 1022 CD ARG A 130 6047 5036 5159 -302 453 -316 C ATOM 1023 NE ARG A 130 -9.159 31.997 -23.293 1.00 44.06 N ANISOU 1023 NE ARG A 130 6212 5206 5322 -381 416 -304 N ATOM 1024 CZ ARG A 130 -8.025 32.690 -23.219 1.00 44.11 C ANISOU 1024 CZ ARG A 130 6277 5168 5314 -453 357 -314 C ATOM 1025 NH1 ARG A 130 -7.327 32.686 -22.099 1.00 46.92 N ANISOU 1025 NH1 ARG A 130 6707 5465 5654 -463 321 -341 N ATOM 1026 NH2 ARG A 130 -7.588 33.405 -24.255 1.00 42.42 N ANISOU 1026 NH2 ARG A 130 6047 4970 5101 -523 327 -285 N ATOM 1027 N THR A 131 -11.060 28.585 -17.629 1.00 36.78 N ANISOU 1027 N THR A 131 5335 4252 4386 -31 562 -334 N ATOM 1028 CA THR A 131 -11.637 27.522 -16.793 1.00 36.58 C ANISOU 1028 CA THR A 131 5253 4268 4380 28 598 -311 C ATOM 1029 C THR A 131 -12.215 26.359 -17.592 1.00 35.32 C ANISOU 1029 C THR A 131 4939 4200 4283 -15 599 -275 C ATOM 1030 O THR A 131 -12.321 26.411 -18.809 1.00 35.55 O ANISOU 1030 O THR A 131 4913 4261 4333 -75 581 -264 O ATOM 1031 CB THR A 131 -12.759 28.053 -15.895 1.00 36.67 C ANISOU 1031 CB THR A 131 5331 4258 4343 181 666 -242 C ATOM 1032 OG1 THR A 131 -13.863 28.455 -16.707 1.00 37.32 O ANISOU 1032 OG1 THR A 131 5357 4386 4436 224 705 -156 O ATOM 1033 CG2 THR A 131 -12.272 29.227 -15.071 1.00 38.78 C ANISOU 1033 CG2 THR A 131 5794 4412 4528 236 657 -282 C ATOM 1034 N LEU A 132 -12.634 25.319 -16.893 1.00 34.80 N ANISOU 1034 N LEU A 132 4814 4169 4241 15 614 -249 N ATOM 1035 CA LEU A 132 -13.247 24.200 -17.572 1.00 33.51 C ANISOU 1035 CA LEU A 132 4526 4076 4131 -33 597 -205 C ATOM 1036 C LEU A 132 -14.563 24.659 -18.233 1.00 33.79 C ANISOU 1036 C LEU A 132 4509 4156 4173 4 622 -94 C ATOM 1037 O LEU A 132 -14.783 24.420 -19.431 1.00 33.28 O ANISOU 1037 O LEU A 132 4385 4125 4134 -72 585 -78 O ATOM 1038 CB LEU A 132 -13.395 23.008 -16.611 1.00 33.39 C ANISOU 1038 CB LEU A 132 4463 4082 4141 -15 597 -191 C ATOM 1039 CG LEU A 132 -12.055 22.427 -16.079 1.00 32.23 C ANISOU 1039 CG LEU A 132 4351 3900 3995 -63 567 -293 C ATOM 1040 CD1 LEU A 132 -12.317 21.293 -15.146 1.00 31.69 C ANISOU 1040 CD1 LEU A 132 4235 3854 3953 -40 569 -268 C ATOM 1041 CD2 LEU A 132 -11.109 21.937 -17.161 1.00 31.82 C ANISOU 1041 CD2 LEU A 132 4275 3853 3963 -165 519 -361 C ATOM 1042 N SER A 133 -15.398 25.365 -17.472 1.00 34.22 N ANISOU 1042 N SER A 133 4594 4210 4196 128 686 -16 N ATOM 1043 CA SER A 133 -16.653 25.934 -18.009 1.00 35.35 C ANISOU 1043 CA SER A 133 4685 4403 4342 185 723 110 C ATOM 1044 C SER A 133 -16.426 26.833 -19.215 1.00 34.19 C ANISOU 1044 C SER A 133 4569 4236 4186 133 702 83 C ATOM 1045 O SER A 133 -17.183 26.759 -20.183 1.00 33.92 O ANISOU 1045 O SER A 133 4449 4259 4182 95 686 163 O ATOM 1046 CB SER A 133 -17.440 26.686 -16.933 1.00 36.12 C ANISOU 1046 CB SER A 133 4837 4497 4388 360 814 196 C ATOM 1047 OG SER A 133 -16.578 27.540 -16.187 1.00 39.97 O ANISOU 1047 OG SER A 133 5495 4883 4807 415 829 96 O ATOM 1048 N ASP A 134 -15.386 27.668 -19.154 1.00 33.79 N ANISOU 1048 N ASP A 134 4639 4106 4095 121 691 -18 N ATOM 1049 CA ASP A 134 -15.039 28.563 -20.266 1.00 33.63 C ANISOU 1049 CA ASP A 134 4651 4063 4065 64 666 -43 C ATOM 1050 C ASP A 134 -14.926 27.761 -21.569 1.00 32.92 C ANISOU 1050 C ASP A 134 4456 4032 4020 -61 611 -52 C ATOM 1051 O ASP A 134 -15.399 28.194 -22.625 1.00 33.63 O ANISOU 1051 O ASP A 134 4513 4150 4116 -89 603 -6 O ATOM 1052 CB ASP A 134 -13.696 29.277 -20.012 1.00 34.45 C ANISOU 1052 CB ASP A 134 4880 4078 4130 27 634 -149 C ATOM 1053 CG ASP A 134 -13.769 30.390 -18.960 1.00 35.78 C ANISOU 1053 CG ASP A 134 5207 4157 4232 141 668 -147 C ATOM 1054 OD1 ASP A 134 -12.697 30.746 -18.430 1.00 37.07 O ANISOU 1054 OD1 ASP A 134 5479 4244 4364 105 626 -223 O ATOM 1055 OD2 ASP A 134 -14.863 30.909 -18.652 1.00 39.14 O ANISOU 1055 OD2 ASP A 134 5657 4585 4628 268 732 -63 O ATOM 1056 N TYR A 135 -14.296 26.591 -21.482 1.00 31.32 N ANISOU 1056 N TYR A 135 4216 3841 3841 -129 574 -112 N ATOM 1057 CA TYR A 135 -14.081 25.744 -22.638 1.00 30.71 C ANISOU 1057 CA TYR A 135 4077 3803 3788 -232 520 -135 C ATOM 1058 C TYR A 135 -15.184 24.698 -22.804 1.00 31.24 C ANISOU 1058 C TYR A 135 4054 3924 3891 -250 495 -49 C ATOM 1059 O TYR A 135 -15.135 23.895 -23.713 1.00 31.35 O ANISOU 1059 O TYR A 135 4040 3957 3916 -333 439 -63 O ATOM 1060 CB TYR A 135 -12.732 25.037 -22.528 1.00 29.84 C ANISOU 1060 CB TYR A 135 3990 3672 3676 -286 493 -241 C ATOM 1061 CG TYR A 135 -11.516 25.900 -22.748 1.00 27.67 C ANISOU 1061 CG TYR A 135 3777 3364 3374 -313 490 -306 C ATOM 1062 CD1 TYR A 135 -10.582 26.080 -21.724 1.00 26.73 C ANISOU 1062 CD1 TYR A 135 3712 3201 3243 -299 493 -355 C ATOM 1063 CD2 TYR A 135 -11.290 26.518 -23.963 1.00 26.04 C ANISOU 1063 CD2 TYR A 135 3569 3172 3153 -360 477 -305 C ATOM 1064 CE1 TYR A 135 -9.437 26.846 -21.911 1.00 25.67 C ANISOU 1064 CE1 TYR A 135 3624 3040 3088 -342 472 -392 C ATOM 1065 CE2 TYR A 135 -10.137 27.299 -24.174 1.00 28.23 C ANISOU 1065 CE2 TYR A 135 3889 3428 3410 -394 466 -344 C ATOM 1066 CZ TYR A 135 -9.217 27.444 -23.142 1.00 26.46 C ANISOU 1066 CZ TYR A 135 3712 3162 3180 -390 460 -381 C ATOM 1067 OH TYR A 135 -8.088 28.204 -23.330 1.00 27.95 O ANISOU 1067 OH TYR A 135 3933 3334 3353 -441 433 -395 O ATOM 1068 N ASN A 136 -16.156 24.704 -21.895 1.00 32.16 N ANISOU 1068 N ASN A 136 4135 4064 4021 -169 533 47 N ATOM 1069 CA ASN A 136 -17.291 23.803 -21.942 1.00 32.94 C ANISOU 1069 CA ASN A 136 4133 4223 4159 -188 504 165 C ATOM 1070 C ASN A 136 -16.804 22.359 -21.851 1.00 32.40 C ANISOU 1070 C ASN A 136 4053 4145 4114 -267 440 107 C ATOM 1071 O ASN A 136 -17.286 21.456 -22.542 1.00 32.83 O ANISOU 1071 O ASN A 136 4062 4221 4191 -353 365 152 O ATOM 1072 CB ASN A 136 -18.163 24.077 -23.189 1.00 34.38 C ANISOU 1072 CB ASN A 136 4258 4451 4353 -241 468 259 C ATOM 1073 CG ASN A 136 -19.575 23.525 -23.056 1.00 37.11 C ANISOU 1073 CG ASN A 136 4488 4872 4740 -241 446 436 C ATOM 1074 OD1 ASN A 136 -20.234 23.227 -24.060 1.00 38.36 O ANISOU 1074 OD1 ASN A 136 4591 5067 4917 -329 376 516 O ATOM 1075 ND2 ASN A 136 -20.049 23.386 -21.808 1.00 39.43 N ANISOU 1075 ND2 ASN A 136 4744 5193 5046 -145 502 512 N ATOM 1076 N ILE A 137 -15.814 22.163 -20.986 1.00 31.07 N ANISOU 1076 N ILE A 137 3939 3934 3933 -239 463 8 N ATOM 1077 CA ILE A 137 -15.327 20.858 -20.682 1.00 29.65 C ANISOU 1077 CA ILE A 137 3753 3740 3772 -287 419 -43 C ATOM 1078 C ILE A 137 -16.298 20.310 -19.642 1.00 30.44 C ANISOU 1078 C ILE A 137 3784 3876 3904 -240 430 69 C ATOM 1079 O ILE A 137 -16.540 20.943 -18.610 1.00 30.42 O ANISOU 1079 O ILE A 137 3787 3882 3888 -137 502 106 O ATOM 1080 CB ILE A 137 -13.879 20.909 -20.162 1.00 28.81 C ANISOU 1080 CB ILE A 137 3718 3585 3643 -275 440 -174 C ATOM 1081 CG1 ILE A 137 -12.929 21.193 -21.321 1.00 28.20 C ANISOU 1081 CG1 ILE A 137 3684 3491 3539 -333 420 -259 C ATOM 1082 CG2 ILE A 137 -13.488 19.590 -19.514 1.00 27.90 C ANISOU 1082 CG2 ILE A 137 3593 3458 3550 -294 411 -209 C ATOM 1083 CD1 ILE A 137 -11.651 21.829 -20.902 1.00 26.58 C ANISOU 1083 CD1 ILE A 137 3535 3255 3310 -315 450 -342 C ATOM 1084 N GLN A 138 -16.844 19.131 -19.908 1.00 30.11 N ANISOU 1084 N GLN A 138 3686 3854 3898 -314 355 128 N ATOM 1085 CA GLN A 138 -17.859 18.592 -19.035 1.00 31.17 C ANISOU 1085 CA GLN A 138 3733 4039 4070 -284 356 266 C ATOM 1086 C GLN A 138 -17.514 17.244 -18.420 1.00 30.74 C ANISOU 1086 C GLN A 138 3675 3962 4042 -326 305 236 C ATOM 1087 O GLN A 138 -16.408 16.740 -18.597 1.00 28.51 O ANISOU 1087 O GLN A 138 3467 3621 3745 -364 280 98 O ATOM 1088 CB GLN A 138 -19.167 18.542 -19.794 1.00 32.57 C ANISOU 1088 CB GLN A 138 3820 4278 4276 -336 303 429 C ATOM 1089 CG GLN A 138 -19.751 19.924 -19.917 1.00 36.49 C ANISOU 1089 CG GLN A 138 4295 4817 4753 -246 385 504 C ATOM 1090 CD GLN A 138 -20.726 20.055 -21.036 1.00 43.20 C ANISOU 1090 CD GLN A 138 5076 5715 5622 -317 326 629 C ATOM 1091 OE1 GLN A 138 -21.132 21.166 -21.375 1.00 45.79 O ANISOU 1091 OE1 GLN A 138 5393 6072 5933 -257 383 681 O ATOM 1092 NE2 GLN A 138 -21.121 18.929 -21.630 1.00 45.48 N ANISOU 1092 NE2 GLN A 138 5328 6009 5943 -449 203 684 N ATOM 1093 N LYS A 139 -18.458 16.686 -17.654 1.00 31.83 N ANISOU 1093 N LYS A 139 3722 4153 4218 -309 296 378 N ATOM 1094 CA LYS A 139 -18.326 15.321 -17.147 1.00 31.81 C ANISOU 1094 CA LYS A 139 3706 4132 4250 -365 230 379 C ATOM 1095 C LYS A 139 -17.919 14.369 -18.275 1.00 31.15 C ANISOU 1095 C LYS A 139 3686 3983 4165 -497 111 304 C ATOM 1096 O LYS A 139 -18.626 14.259 -19.297 1.00 31.09 O ANISOU 1096 O LYS A 139 3663 3985 4165 -583 30 379 O ATOM 1097 CB LYS A 139 -19.637 14.834 -16.523 1.00 33.16 C ANISOU 1097 CB LYS A 139 3746 4383 4468 -362 208 589 C ATOM 1098 CG LYS A 139 -19.466 13.566 -15.677 1.00 35.97 C ANISOU 1098 CG LYS A 139 4086 4724 4858 -394 160 597 C ATOM 1099 CD LYS A 139 -18.390 13.784 -14.578 1.00 38.36 C ANISOU 1099 CD LYS A 139 4454 4993 5130 -292 254 460 C ATOM 1100 CE LYS A 139 -18.575 12.856 -13.379 1.00 38.29 C ANISOU 1100 CE LYS A 139 4388 5006 5153 -274 248 529 C ATOM 1101 NZ LYS A 139 -19.779 13.255 -12.592 1.00 41.88 N ANISOU 1101 NZ LYS A 139 4723 5569 5620 -182 314 729 N ATOM 1102 N GLU A 140 -16.772 13.721 -18.071 1.00 29.76 N ANISOU 1102 N GLU A 140 3592 3741 3974 -503 103 160 N ATOM 1103 CA GLU A 140 -16.273 12.603 -18.881 1.00 30.59 C ANISOU 1103 CA GLU A 140 3783 3772 4068 -596 1 82 C ATOM 1104 C GLU A 140 -15.788 13.006 -20.269 1.00 30.43 C ANISOU 1104 C GLU A 140 3849 3716 3996 -630 -17 -8 C ATOM 1105 O GLU A 140 -15.627 12.172 -21.163 1.00 31.37 O ANISOU 1105 O GLU A 140 4054 3775 4089 -703 -109 -50 O ATOM 1106 CB GLU A 140 -17.234 11.390 -18.865 1.00 31.04 C ANISOU 1106 CB GLU A 140 3805 3821 4167 -694 -125 208 C ATOM 1107 CG GLU A 140 -17.214 10.705 -17.491 1.00 32.97 C ANISOU 1107 CG GLU A 140 3997 4078 4452 -658 -108 245 C ATOM 1108 CD GLU A 140 -17.965 9.382 -17.387 1.00 36.77 C ANISOU 1108 CD GLU A 140 4455 4539 4977 -763 -243 360 C ATOM 1109 OE1 GLU A 140 -18.694 8.988 -18.330 1.00 37.60 O ANISOU 1109 OE1 GLU A 140 4577 4624 5086 -876 -366 441 O ATOM 1110 OE2 GLU A 140 -17.815 8.732 -16.325 1.00 37.63 O ANISOU 1110 OE2 GLU A 140 4533 4649 5116 -738 -234 376 O ATOM 1111 N SER A 141 -15.518 14.300 -20.398 1.00 29.70 N ANISOU 1111 N SER A 141 3746 3657 3883 -568 73 -39 N ATOM 1112 CA SER A 141 -14.859 14.871 -21.532 1.00 29.26 C ANISOU 1112 CA SER A 141 3759 3580 3776 -578 84 -130 C ATOM 1113 C SER A 141 -13.430 14.387 -21.498 1.00 29.20 C ANISOU 1113 C SER A 141 3834 3525 3738 -551 107 -273 C ATOM 1114 O SER A 141 -12.898 14.041 -20.417 1.00 28.98 O ANISOU 1114 O SER A 141 3793 3491 3729 -507 143 -303 O ATOM 1115 CB SER A 141 -14.908 16.399 -21.456 1.00 28.99 C ANISOU 1115 CB SER A 141 3691 3591 3734 -514 175 -115 C ATOM 1116 OG SER A 141 -16.204 16.901 -21.805 1.00 30.23 O ANISOU 1116 OG SER A 141 3779 3797 3911 -533 156 21 O ATOM 1117 N THR A 142 -12.822 14.319 -22.678 1.00 28.61 N ANISOU 1117 N THR A 142 3839 3422 3610 -573 88 -348 N ATOM 1118 CA THR A 142 -11.439 13.901 -22.811 1.00 29.17 C ANISOU 1118 CA THR A 142 3979 3461 3641 -533 121 -465 C ATOM 1119 C THR A 142 -10.599 15.064 -23.329 1.00 28.53 C ANISOU 1119 C THR A 142 3899 3414 3526 -496 196 -514 C ATOM 1120 O THR A 142 -10.946 15.691 -24.336 1.00 29.05 O ANISOU 1120 O THR A 142 3977 3495 3566 -522 185 -496 O ATOM 1121 CB THR A 142 -11.282 12.640 -23.726 1.00 29.84 C ANISOU 1121 CB THR A 142 4181 3480 3677 -567 40 -510 C ATOM 1122 OG1 THR A 142 -11.908 11.509 -23.097 1.00 31.90 O ANISOU 1122 OG1 THR A 142 4448 3699 3974 -608 -39 -465 O ATOM 1123 CG2 THR A 142 -9.807 12.307 -23.973 1.00 30.19 C ANISOU 1123 CG2 THR A 142 4295 3507 3669 -497 96 -617 C ATOM 1124 N LEU A 143 -9.519 15.364 -22.611 1.00 28.00 N ANISOU 1124 N LEU A 143 3814 3361 3464 -443 263 -562 N ATOM 1125 CA LEU A 143 -8.495 16.280 -23.099 1.00 28.19 C ANISOU 1125 CA LEU A 143 3840 3414 3455 -419 320 -601 C ATOM 1126 C LEU A 143 -7.298 15.497 -23.608 1.00 28.30 C ANISOU 1126 C LEU A 143 3904 3423 3425 -384 336 -666 C ATOM 1127 O LEU A 143 -6.879 14.486 -23.009 1.00 28.25 O ANISOU 1127 O LEU A 143 3914 3391 3426 -358 332 -693 O ATOM 1128 CB LEU A 143 -8.041 17.263 -22.006 1.00 27.79 C ANISOU 1128 CB LEU A 143 3742 3384 3434 -393 371 -592 C ATOM 1129 CG LEU A 143 -9.043 17.844 -21.021 1.00 29.08 C ANISOU 1129 CG LEU A 143 3870 3545 3633 -385 375 -533 C ATOM 1130 CD1 LEU A 143 -8.329 18.880 -20.124 1.00 30.61 C ANISOU 1130 CD1 LEU A 143 4064 3739 3827 -358 417 -544 C ATOM 1131 CD2 LEU A 143 -10.175 18.483 -21.730 1.00 29.81 C ANISOU 1131 CD2 LEU A 143 3951 3651 3724 -406 360 -473 C ATOM 1132 N HIS A 144 -6.733 15.967 -24.708 1.00 27.80 N ANISOU 1132 N HIS A 144 3865 3387 3311 -374 361 -683 N ATOM 1133 CA HIS A 144 -5.521 15.380 -25.208 1.00 27.93 C ANISOU 1133 CA HIS A 144 3918 3417 3276 -315 399 -725 C ATOM 1134 C HIS A 144 -4.367 16.018 -24.457 1.00 28.18 C ANISOU 1134 C HIS A 144 3874 3500 3334 -291 459 -713 C ATOM 1135 O HIS A 144 -4.362 17.250 -24.248 1.00 27.32 O ANISOU 1135 O HIS A 144 3713 3419 3250 -325 470 -679 O ATOM 1136 CB HIS A 144 -5.377 15.677 -26.704 1.00 28.67 C ANISOU 1136 CB HIS A 144 4063 3532 3298 -305 409 -732 C ATOM 1137 CG HIS A 144 -6.327 14.916 -27.570 1.00 28.38 C ANISOU 1137 CG HIS A 144 4130 3437 3216 -331 337 -748 C ATOM 1138 ND1 HIS A 144 -6.402 13.541 -27.561 1.00 29.03 N ANISOU 1138 ND1 HIS A 144 4311 3451 3267 -310 293 -785 N ATOM 1139 CD2 HIS A 144 -7.221 15.337 -28.500 1.00 29.10 C ANISOU 1139 CD2 HIS A 144 4252 3521 3282 -385 291 -725 C ATOM 1140 CE1 HIS A 144 -7.306 13.143 -28.439 1.00 31.04 C ANISOU 1140 CE1 HIS A 144 4663 3653 3478 -357 211 -784 C ATOM 1141 NE2 HIS A 144 -7.807 14.212 -29.035 1.00 32.13 N ANISOU 1141 NE2 HIS A 144 4756 3833 3620 -403 210 -746 N ATOM 1142 N LEU A 145 -3.396 15.197 -24.061 1.00 28.64 N ANISOU 1142 N LEU A 145 3932 3566 3385 -236 488 -731 N ATOM 1143 CA LEU A 145 -2.158 15.700 -23.439 1.00 29.86 C ANISOU 1143 CA LEU A 145 4009 3778 3560 -220 535 -701 C ATOM 1144 C LEU A 145 -0.945 15.317 -24.260 1.00 31.66 C ANISOU 1144 C LEU A 145 4236 4064 3731 -144 594 -691 C ATOM 1145 O LEU A 145 -0.720 14.133 -24.576 1.00 31.53 O ANISOU 1145 O LEU A 145 4284 4024 3670 -71 611 -724 O ATOM 1146 CB LEU A 145 -1.962 15.230 -21.990 1.00 29.44 C ANISOU 1146 CB LEU A 145 3923 3704 3559 -220 526 -702 C ATOM 1147 CG LEU A 145 -0.596 15.519 -21.302 1.00 28.88 C ANISOU 1147 CG LEU A 145 3777 3691 3507 -209 559 -662 C ATOM 1148 CD1 LEU A 145 -0.300 16.990 -21.093 1.00 25.15 C ANISOU 1148 CD1 LEU A 145 3255 3248 3052 -273 548 -613 C ATOM 1149 CD2 LEU A 145 -0.452 14.785 -19.974 1.00 26.86 C ANISOU 1149 CD2 LEU A 145 3506 3408 3292 -201 546 -670 C ATOM 1150 N VAL A 146 -0.160 16.346 -24.567 1.00 32.96 N ANISOU 1150 N VAL A 146 4330 4302 3892 -158 626 -634 N ATOM 1151 CA VAL A 146 0.971 16.265 -25.468 1.00 35.18 C ANISOU 1151 CA VAL A 146 4585 4665 4117 -86 692 -592 C ATOM 1152 C VAL A 146 2.137 17.091 -24.907 1.00 36.22 C ANISOU 1152 C VAL A 146 4594 4879 4287 -117 709 -500 C ATOM 1153 O VAL A 146 1.919 18.051 -24.177 1.00 35.95 O ANISOU 1153 O VAL A 146 4525 4828 4307 -210 660 -479 O ATOM 1154 CB VAL A 146 0.496 16.742 -26.877 1.00 35.51 C ANISOU 1154 CB VAL A 146 4677 4718 4099 -85 697 -598 C ATOM 1155 CG1 VAL A 146 1.263 17.919 -27.371 1.00 34.43 C ANISOU 1155 CG1 VAL A 146 4450 4673 3959 -109 726 -515 C ATOM 1156 CG2 VAL A 146 0.494 15.599 -27.851 1.00 35.85 C ANISOU 1156 CG2 VAL A 146 4830 4740 4050 18 728 -645 C ATOM 1157 N LEU A 147 3.366 16.728 -25.242 1.00 38.70 N ANISOU 1157 N LEU A 147 4851 5283 4570 -39 775 -435 N ATOM 1158 CA LEU A 147 4.532 17.439 -24.706 1.00 40.69 C ANISOU 1158 CA LEU A 147 4974 5624 4863 -81 778 -320 C ATOM 1159 C LEU A 147 4.959 18.662 -25.524 1.00 42.11 C ANISOU 1159 C LEU A 147 5086 5882 5031 -130 781 -230 C ATOM 1160 O LEU A 147 4.721 18.734 -26.728 1.00 42.06 O ANISOU 1160 O LEU A 147 5117 5899 4966 -82 819 -240 O ATOM 1161 CB LEU A 147 5.723 16.482 -24.516 1.00 41.58 C ANISOU 1161 CB LEU A 147 5025 5812 4960 24 847 -258 C ATOM 1162 CG LEU A 147 6.684 16.779 -23.339 1.00 42.71 C ANISOU 1162 CG LEU A 147 5049 6007 5171 -39 817 -160 C ATOM 1163 CD1 LEU A 147 5.960 16.651 -21.984 1.00 40.51 C ANISOU 1163 CD1 LEU A 147 4820 5620 4951 -116 740 -239 C ATOM 1164 CD2 LEU A 147 7.941 15.906 -23.347 1.00 40.30 C ANISOU 1164 CD2 LEU A 147 4660 5804 4846 78 899 -66 C ATOM 1165 N ARG A 148 5.552 19.631 -24.824 1.00 43.88 N ANISOU 1165 N ARG A 148 5223 6138 5311 -234 727 -140 N ATOM 1166 CA ARG A 148 6.314 20.749 -25.386 1.00 46.71 C ANISOU 1166 CA ARG A 148 5488 6589 5672 -294 718 -12 C ATOM 1167 C ARG A 148 7.378 20.218 -26.344 1.00 48.63 C ANISOU 1167 C ARG A 148 5646 6971 5860 -174 820 89 C ATOM 1168 O ARG A 148 8.065 19.239 -26.012 1.00 49.65 O ANISOU 1168 O ARG A 148 5737 7147 5982 -82 875 118 O ATOM 1169 CB ARG A 148 7.046 21.449 -24.224 1.00 47.47 C ANISOU 1169 CB ARG A 148 5510 6694 5834 -413 634 83 C ATOM 1170 CG ARG A 148 7.705 22.799 -24.521 1.00 51.47 C ANISOU 1170 CG ARG A 148 5936 7261 6358 -527 576 222 C ATOM 1171 CD ARG A 148 6.881 23.978 -23.987 1.00 54.52 C ANISOU 1171 CD ARG A 148 6419 7524 6773 -658 466 170 C ATOM 1172 NE ARG A 148 5.815 24.393 -24.907 1.00 57.79 N ANISOU 1172 NE ARG A 148 6913 7891 7155 -639 485 88 N ATOM 1173 CZ ARG A 148 4.565 23.932 -24.880 1.00 58.39 C ANISOU 1173 CZ ARG A 148 7095 7873 7215 -588 505 -53 C ATOM 1174 NH1 ARG A 148 4.194 23.033 -23.977 1.00 58.89 N ANISOU 1174 NH1 ARG A 148 7203 7878 7293 -548 510 -134 N ATOM 1175 NH2 ARG A 148 3.671 24.376 -25.753 1.00 59.29 N ANISOU 1175 NH2 ARG A 148 7266 7958 7303 -583 514 -101 N ATOM 1176 N LEU A 149 7.527 20.853 -27.513 1.00 50.10 N ANISOU 1176 N LEU A 149 5802 7228 6005 -164 851 151 N ATOM 1177 CA LEU A 149 8.637 20.550 -28.439 1.00 51.89 C ANISOU 1177 CA LEU A 149 5931 7611 6175 -46 955 282 C ATOM 1178 C LEU A 149 9.761 21.581 -28.282 1.00 52.91 C ANISOU 1178 C LEU A 149 5889 7862 6354 -147 917 484 C ATOM 1179 O LEU A 149 9.505 22.789 -28.226 1.00 52.42 O ANISOU 1179 O LEU A 149 5818 7768 6333 -293 824 513 O ATOM 1180 CB LEU A 149 8.164 20.522 -29.903 1.00 52.76 C ANISOU 1180 CB LEU A 149 6114 7737 6194 43 1021 239 C ATOM 1181 CG LEU A 149 7.678 19.240 -30.600 1.00 53.11 C ANISOU 1181 CG LEU A 149 6302 7736 6140 211 1103 118 C ATOM 1182 CD1 LEU A 149 7.046 19.575 -31.961 1.00 54.25 C ANISOU 1182 CD1 LEU A 149 6532 7876 6205 241 1125 76 C ATOM 1183 CD2 LEU A 149 8.800 18.218 -30.775 1.00 55.57 C ANISOU 1183 CD2 LEU A 149 6568 8153 6393 389 1220 200 C TER 1184 LEU A 149 HETATM 1185 C1 GOL A 153 -9.913 20.562 -6.818 1.00 37.98 C HETATM 1186 O1 GOL A 153 -10.560 20.495 -8.080 1.00 36.62 O HETATM 1187 C2 GOL A 153 -10.346 21.818 -6.088 1.00 35.77 C HETATM 1188 O2 GOL A 153 -10.893 22.770 -6.999 1.00 37.42 O HETATM 1189 C3 GOL A 153 -9.086 22.402 -5.469 1.00 35.06 C HETATM 1190 O3 GOL A 153 -9.363 22.813 -4.156 1.00 32.92 O HETATM 1191 O HOH A 154 -9.671 6.861 5.959 1.00 5.89 O HETATM 1192 O HOH A 155 -14.523 11.774 -23.570 1.00 16.13 O HETATM 1193 O HOH A 156 -7.725 13.859 -9.256 1.00 20.99 O HETATM 1194 O HOH A 157 -17.149 24.996 -9.721 1.00 18.28 O HETATM 1195 O HOH A 158 -12.271 30.939 -24.109 1.00 23.59 O HETATM 1196 O HOH A 159 -2.160 6.303 -3.276 1.00 14.31 O HETATM 1197 O HOH A 160 -6.060 -6.387 11.864 1.00 6.44 O HETATM 1198 O HOH A 161 0.892 12.437 -25.826 1.00 15.28 O HETATM 1199 O HOH A 162 -13.853 -4.601 -4.266 1.00 27.86 O HETATM 1200 O HOH A 163 1.280 -2.521 -11.661 1.00 21.53 O HETATM 1201 O HOH A 164 -2.239 23.956 -22.796 1.00 17.75 O HETATM 1202 O HOH A 165 -3.935 31.877 -19.683 1.00 22.58 O HETATM 1203 O HOH A 166 -1.464 28.012 -23.347 1.00 33.73 O HETATM 1204 O HOH A 167 -7.789 -6.599 -6.890 1.00 19.63 O HETATM 1205 O HOH A 168 -3.693 -4.758 14.397 1.00 30.62 O HETATM 1206 O HOH A 169 2.034 26.651 -17.922 1.00 31.63 O HETATM 1207 O HOH A 170 -15.079 2.800 -6.167 1.00 27.75 O HETATM 1208 O HOH A 171 -12.502 18.345 -7.172 1.00 38.95 O HETATM 1209 O HOH A 172 12.552 -2.814 -7.997 1.00 19.33 O HETATM 1210 O HOH A 173 13.417 1.620 -7.591 1.00 16.92 O HETATM 1211 O HOH A 174 -4.642 11.989 -26.802 1.00 12.20 O HETATM 1212 O HOH A 175 -8.400 15.756 -33.444 1.00 18.89 O HETATM 1213 O HOH A 176 -9.554 14.165 -31.312 1.00 15.75 O HETATM 1214 O HOH A 177 -9.192 8.051 -25.061 1.00 25.86 O HETATM 1215 O HOH A 178 -21.134 18.238 -17.015 1.00 20.57 O HETATM 1216 O HOH A 179 -12.349 7.002 -21.569 1.00 21.59 O HETATM 1217 O HOH A 180 -11.871 8.906 -23.270 1.00 14.14 O HETATM 1218 O HOH A 181 3.295 13.202 -26.147 1.00 14.63 O HETATM 1219 O HOH A 182 -14.882 14.491 -24.889 1.00 2.91 O HETATM 1220 O HOH A 183 -16.402 16.267 -25.214 1.00 7.46 O HETATM 1221 O HOH A 184 -14.410 11.261 0.731 1.00 13.01 O HETATM 1222 O HOH A 185 1.460 19.915 -9.064 1.00 25.66 O HETATM 1223 O HOH A 186 -7.700 34.358 -19.204 1.00 56.01 O HETATM 1224 O HOH A 187 -2.185 -8.501 11.073 1.00 25.85 O HETATM 1225 O HOH A 188 11.778 0.177 -9.249 1.00 28.38 O CONECT 1185 1186 1187 CONECT 1186 1185 CONECT 1187 1185 1188 1189 CONECT 1188 1187 CONECT 1189 1187 1190 CONECT 1190 1189 MASTER 299 0 1 5 10 0 3 6 1224 1 6 12 END If you find results from this site helpful for your research, please cite one of our papers:
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