HEADER IMMUNE SYSTEM 13-JUN-18 6GRZ TITLE CRYSTAL STRUCTURE OF THE LIGHT CHAIN DIMER MH6 COMPND MOL_ID: 1; COMPND 2 MOLECULE: MH6; COMPND 3 CHAIN: A, B; COMPND 4 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_TAXID: 9606; SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3); SOURCE 5 EXPRESSION_SYSTEM_TAXID: 469008; SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PASK-IBA33PLUS KEYWDS LIGHT CHAIN DIMER, LIGHT CHAIN AMYLOIDOSIS, IMMUNOGLOBULIN FOLD, KEYWDS 2 PROTEIN AGGREGATION, IMMUNE SYSTEM EXPDTA X-RAY DIFFRACTION AUTHOR M.MARITAN,S.RICAGNO,A.AMBROSETTI,L.OBERTI REVDAT 1 12-JUN-19 6GRZ 0 JRNL AUTH M.MARITAN,A.AMBROSETTI,L.OBERTI,R.RUSSO,P.SORMANNI,M.ROMEO, JRNL AUTH 2 L.DIOMEDE,P.ROGNONI,F.LAVATELLI,M.BOLOGNESI,S.RICAGNO, JRNL AUTH 3 A.BARBIROLI,G.MERLINI JRNL TITL MODULATING THE TOXIC BEHAVIOUR OF A AMYLOIDOGENIC LIGHT JRNL TITL 2 CHAIN DIMER THROUGH POINT MUTATIONS JRNL REF TO BE PUBLISHED JRNL REFN REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH L.OBERTI,P.ROGNONI,A.BARBIROLI,F.LAVATELLI,R.RUSSO, REMARK 1 AUTH 2 M.MARITAN,G.PALLADINI,M.BOLOGNESI,G.MERLINI,S.RICAGNO REMARK 1 TITL CONCURRENT STRUCTURAL AND BIOPHYSICAL TRAITS LINK WITH REMARK 1 TITL 2 IMMUNOGLOBULIN LIGHT CHAINS AMYLOID PROPENSITY. REMARK 1 REF SCI REP V. 7 16809 2017 REMARK 1 REFN ESSN 2045-2322 REMARK 1 PMID 29196671 REMARK 1 DOI 10.1038/S41598-017-16953-7 REMARK 2 REMARK 2 RESOLUTION. 2.10 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : BUSTER 2.10.3 REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER, REMARK 3 : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN, REMARK 3 : WOMACK,MATTHEWS,TEN EYCK,TRONRUD REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 38.46 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000 REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8 REMARK 3 NUMBER OF REFLECTIONS : 27332 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) : 0.208 REMARK 3 R VALUE (WORKING SET) : 0.206 REMARK 3 FREE R VALUE : 0.238 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.430 REMARK 3 FREE R VALUE TEST SET COUNT : 1483 REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : 14 REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10 REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 2.18 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.02 REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 2822 REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2327 REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2654 REMARK 3 BIN R VALUE (WORKING SET) : 0.2315 REMARK 3 BIN FREE R VALUE : 0.2526 REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.95 REMARK 3 BIN FREE R VALUE TEST SET COUNT : 168 REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 3179 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 30 REMARK 3 SOLVENT ATOMS : 126 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 57.30 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 68.54 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : -16.31430 REMARK 3 B22 (A**2) : 11.76850 REMARK 3 B33 (A**2) : 4.54580 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : -0.11930 REMARK 3 B23 (A**2) : 0.00000 REMARK 3 REMARK 3 ESTIMATED COORDINATE ERROR. REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.320 REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : 0.208 REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.172 REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.213 REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : 0.175 REMARK 3 REMARK 3 REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797 REMARK 3 CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.944 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.938 REMARK 3 REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15 REMARK 3 TERM COUNT WEIGHT FUNCTION. REMARK 3 BOND LENGTHS : 3328 ; 2.000 ; HARMONIC REMARK 3 BOND ANGLES : 4559 ; 2.000 ; HARMONIC REMARK 3 TORSION ANGLES : 1087 ; 2.000 ; SINUSOIDAL REMARK 3 TRIGONAL CARBON PLANES : 70 ; 2.000 ; HARMONIC REMARK 3 GENERAL PLANES : 475 ; 5.000 ; HARMONIC REMARK 3 ISOTROPIC THERMAL FACTORS : 3328 ; 20.000 ; HARMONIC REMARK 3 BAD NON-BONDED CONTACTS : NULL ; NULL ; NULL REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL REMARK 3 CHIRAL IMPROPER TORSION : 444 ; 5.000 ; SEMIHARMONIC REMARK 3 SUM OF OCCUPANCIES : NULL ; NULL ; NULL REMARK 3 UTILITY DISTANCES : NULL ; NULL ; NULL REMARK 3 UTILITY ANGLES : NULL ; NULL ; NULL REMARK 3 UTILITY TORSION : NULL ; NULL ; NULL REMARK 3 IDEAL-DIST CONTACT TERM : 3631 ; 4.000 ; SEMIHARMONIC REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. REMARK 3 BOND LENGTHS (A) : 0.010 REMARK 3 BOND ANGLES (DEGREES) : 1.19 REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.01 REMARK 3 OTHER TORSION ANGLES (DEGREES) : 17.68 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 2 REMARK 3 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: { A|* } REMARK 3 ORIGIN FOR THE GROUP (A): -19.5045 18.6147 -4.8887 REMARK 3 T TENSOR REMARK 3 T11: -0.2614 T22: -0.3871 REMARK 3 T33: -0.2238 T12: 0.0604 REMARK 3 T13: -0.0274 T23: -0.0164 REMARK 3 L TENSOR REMARK 3 L11: 0.7604 L22: 0.8351 REMARK 3 L33: 1.1706 L12: 0.5316 REMARK 3 L13: -0.1098 L23: -0.2237 REMARK 3 S TENSOR REMARK 3 S11: 0.0924 S12: -0.1507 S13: -0.0286 REMARK 3 S21: 0.0371 S22: -0.0643 S23: 0.2844 REMARK 3 S31: -0.0265 S32: -0.2119 S33: -0.0281 REMARK 3 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: { B|* } REMARK 3 ORIGIN FOR THE GROUP (A): -19.2388 3.1754 -4.5254 REMARK 3 T TENSOR REMARK 3 T11: -0.2882 T22: -0.4404 REMARK 3 T33: -0.3931 T12: 0.0335 REMARK 3 T13: -0.0513 T23: 0.0839 REMARK 3 L TENSOR REMARK 3 L11: 1.9184 L22: 1.1614 REMARK 3 L33: 5.5288 L12: 0.0795 REMARK 3 L13: -2.2851 L23: 0.8857 REMARK 3 S TENSOR REMARK 3 S11: -0.0594 S12: -0.0773 S13: 0.0081 REMARK 3 S21: -0.0860 S22: 0.0503 S23: -0.0037 REMARK 3 S31: 0.4187 S32: -0.1577 S33: 0.0092 REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 6GRZ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 13-JUN-18. REMARK 100 THE DEPOSITION ID IS D_1200010461. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 16-APR-18 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 8.5 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : ESRF REMARK 200 BEAMLINE : ID29 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.07227 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M-F REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : AIMLESS REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 27333 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100 REMARK 200 RESOLUTION RANGE LOW (A) : 38.460 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9 REMARK 200 DATA REDUNDANCY : 3.400 REMARK 200 R MERGE (I) : 0.04000 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 13.0000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.16 REMARK 200 COMPLETENESS FOR SHELL (%) : 99.0 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 : 0.800 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: PHASER REMARK 200 STARTING MODEL: 5MUD REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 49.00 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.44 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.02M SODIUM POTASSIUM PHOSPHATE, 0.1M REMARK 280 BIS-TRIS PROPANE PH 8.5, 20% W/V PEG 3350, VAPOR DIFFUSION, REMARK 280 SITTING DROP, TEMPERATURE 293.15K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 1 2 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,Y,-Z REMARK 290 3555 X+1/2,Y+1/2,Z+1/2 REMARK 290 4555 -X+1/2,Y+1/2,-Z+1/2 REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 28.48655 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 36.28900 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 40.84146 REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 28.48655 REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 36.28900 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 40.84146 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: DIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 4150 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 19950 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -25.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 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 SER A 216 REMARK 465 GLN B 1 REMARK 465 SER B 216 REMARK 470 REMARK 470 MISSING ATOM REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 470 I=INSERTION CODE): REMARK 470 M RES CSSEQI ATOMS REMARK 470 LYS A 31 CE NZ REMARK 470 GLU B 214 CG CD OE1 OE2 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 ASN A 28 -95.92 -104.26 REMARK 500 ASN A 28 -95.92 -104.37 REMARK 500 ASN A 52 -50.69 74.95 REMARK 500 ASN A 174 -2.82 77.49 REMARK 500 ASN B 28 -91.78 -111.61 REMARK 500 ASN B 52 -54.00 70.01 REMARK 500 GLU B 84 105.71 -56.84 REMARK 500 ASP B 155 -114.45 64.61 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 301 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 302 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 303 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 301 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 302 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 5MUD RELATED DB: PDB REMARK 900 THIS STRUCTURE IS THE WILD TYPE OF THE MUTANT DEPOSITED IN THE REMARK 900 CURRENT DEPOSITION DBREF 6GRZ A 1 216 PDB 6GRZ 6GRZ 1 216 DBREF 6GRZ B 1 216 PDB 6GRZ 6GRZ 1 216 SEQRES 1 A 216 GLN SER VAL LEU THR GLN PRO PRO SER VAL SER ALA ALA SEQRES 2 A 216 PRO GLY GLN LYS VAL THR ILE SER CYS SER GLY ASN ASN SEQRES 3 A 216 SER ASN ILE GLY LYS ASN TYR VAL SER TRP TYR GLN GLN SEQRES 4 A 216 LEU PRO GLY ARG THR PRO LYS LEU ILE MET TYR GLU ASN SEQRES 5 A 216 ASN LYS ARG SER SER GLY ILE PRO ASP ARG PHE SER GLY SEQRES 6 A 216 SER LYS SER GLY ASN SER ALA THR LEU THR ILE THR GLY SEQRES 7 A 216 LEU GLN THR GLY ASP GLU ALA ASP TYR TYR CYS GLY VAL SEQRES 8 A 216 TRP ASP SER SER LEU SER GLY GLY VAL PHE GLY GLY GLY SEQRES 9 A 216 THR LYS VAL THR VAL LEU GLY GLN PRO LYS ALA ALA PRO SEQRES 10 A 216 SER VAL THR LEU PHE PRO PRO SER SER GLU GLU LEU GLN SEQRES 11 A 216 ALA ASN LYS ALA THR LEU VAL CYS LEU ILE SER ASP PHE SEQRES 12 A 216 TYR PRO GLY ALA VAL THR VAL ALA TRP LYS ALA ASP SER SEQRES 13 A 216 SER PRO VAL LYS ALA GLY VAL GLU THR THR THR PRO SER SEQRES 14 A 216 LYS GLN SER ASN ASN LYS TYR ALA ALA SER SER TYR LEU SEQRES 15 A 216 SER LEU THR PRO GLU GLN TRP LYS SER HIS ARG SER TYR SEQRES 16 A 216 SER CYS GLN VAL THR HIS GLU GLY SER THR VAL GLU LYS SEQRES 17 A 216 THR VAL ALA PRO THR GLU CYS SER SEQRES 1 B 216 GLN SER VAL LEU THR GLN PRO PRO SER VAL SER ALA ALA SEQRES 2 B 216 PRO GLY GLN LYS VAL THR ILE SER CYS SER GLY ASN ASN SEQRES 3 B 216 SER ASN ILE GLY LYS ASN TYR VAL SER TRP TYR GLN GLN SEQRES 4 B 216 LEU PRO GLY ARG THR PRO LYS LEU ILE MET TYR GLU ASN SEQRES 5 B 216 ASN LYS ARG SER SER GLY ILE PRO ASP ARG PHE SER GLY SEQRES 6 B 216 SER LYS SER GLY ASN SER ALA THR LEU THR ILE THR GLY SEQRES 7 B 216 LEU GLN THR GLY ASP GLU ALA ASP TYR TYR CYS GLY VAL SEQRES 8 B 216 TRP ASP SER SER LEU SER GLY GLY VAL PHE GLY GLY GLY SEQRES 9 B 216 THR LYS VAL THR VAL LEU GLY GLN PRO LYS ALA ALA PRO SEQRES 10 B 216 SER VAL THR LEU PHE PRO PRO SER SER GLU GLU LEU GLN SEQRES 11 B 216 ALA ASN LYS ALA THR LEU VAL CYS LEU ILE SER ASP PHE SEQRES 12 B 216 TYR PRO GLY ALA VAL THR VAL ALA TRP LYS ALA ASP SER SEQRES 13 B 216 SER PRO VAL LYS ALA GLY VAL GLU THR THR THR PRO SER SEQRES 14 B 216 LYS GLN SER ASN ASN LYS TYR ALA ALA SER SER TYR LEU SEQRES 15 B 216 SER LEU THR PRO GLU GLN TRP LYS SER HIS ARG SER TYR SEQRES 16 B 216 SER CYS GLN VAL THR HIS GLU GLY SER THR VAL GLU LYS SEQRES 17 B 216 THR VAL ALA PRO THR GLU CYS SER HET GOL A 301 14 HET GOL A 302 14 HET GOL A 303 14 HET GOL B 301 14 HET GOL B 302 14 HETNAM GOL GLYCEROL HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL FORMUL 3 GOL 5(C3 H8 O3) FORMUL 8 HOH *126(H2 O) HELIX 1 AA1 GLN A 80 GLU A 84 5 5 HELIX 2 AA2 SER A 125 ALA A 131 1 7 HELIX 3 AA3 THR A 185 HIS A 192 1 8 HELIX 4 AA4 GLN B 80 GLU B 84 5 5 HELIX 5 AA5 SER B 125 ALA B 131 1 7 HELIX 6 AA6 THR B 185 HIS B 192 1 8 SHEET 1 AA1 6 SER A 9 ALA A 12 0 SHEET 2 AA1 6 THR A 105 VAL A 109 1 O LYS A 106 N VAL A 10 SHEET 3 AA1 6 ALA A 85 ASP A 93 -1 N TYR A 87 O THR A 105 SHEET 4 AA1 6 VAL A 34 GLN A 39 -1 N SER A 35 O GLY A 90 SHEET 5 AA1 6 LYS A 46 TYR A 50 -1 O LYS A 46 N GLN A 38 SHEET 6 AA1 6 LYS A 54 ARG A 55 -1 O LYS A 54 N TYR A 50 SHEET 1 AA2 4 SER A 9 ALA A 12 0 SHEET 2 AA2 4 THR A 105 VAL A 109 1 O LYS A 106 N VAL A 10 SHEET 3 AA2 4 ALA A 85 ASP A 93 -1 N TYR A 87 O THR A 105 SHEET 4 AA2 4 GLY A 98 PHE A 101 -1 O VAL A 100 N VAL A 91 SHEET 1 AA3 3 VAL A 18 SER A 23 0 SHEET 2 AA3 3 SER A 71 ILE A 76 -1 O LEU A 74 N ILE A 20 SHEET 3 AA3 3 PHE A 63 SER A 68 -1 N SER A 64 O THR A 75 SHEET 1 AA4 4 SER A 118 PHE A 122 0 SHEET 2 AA4 4 ALA A 134 PHE A 143 -1 O VAL A 137 N PHE A 122 SHEET 3 AA4 4 TYR A 176 LEU A 184 -1 O SER A 180 N CYS A 138 SHEET 4 AA4 4 VAL A 163 THR A 165 -1 N GLU A 164 O TYR A 181 SHEET 1 AA5 4 SER A 118 PHE A 122 0 SHEET 2 AA5 4 ALA A 134 PHE A 143 -1 O VAL A 137 N PHE A 122 SHEET 3 AA5 4 TYR A 176 LEU A 184 -1 O SER A 180 N CYS A 138 SHEET 4 AA5 4 SER A 169 LYS A 170 -1 N SER A 169 O ALA A 177 SHEET 1 AA6 4 SER A 157 PRO A 158 0 SHEET 2 AA6 4 THR A 149 ALA A 154 -1 N ALA A 154 O SER A 157 SHEET 3 AA6 4 TYR A 195 HIS A 201 -1 O THR A 200 N THR A 149 SHEET 4 AA6 4 SER A 204 VAL A 210 -1 O SER A 204 N HIS A 201 SHEET 1 AA7 6 SER B 9 ALA B 12 0 SHEET 2 AA7 6 THR B 105 VAL B 109 1 O THR B 108 N VAL B 10 SHEET 3 AA7 6 ALA B 85 ASP B 93 -1 N ALA B 85 O VAL B 107 SHEET 4 AA7 6 SER B 35 GLN B 39 -1 N TYR B 37 O TYR B 88 SHEET 5 AA7 6 LYS B 46 TYR B 50 -1 O ILE B 48 N TRP B 36 SHEET 6 AA7 6 LYS B 54 ARG B 55 -1 O LYS B 54 N TYR B 50 SHEET 1 AA8 4 SER B 9 ALA B 12 0 SHEET 2 AA8 4 THR B 105 VAL B 109 1 O THR B 108 N VAL B 10 SHEET 3 AA8 4 ALA B 85 ASP B 93 -1 N ALA B 85 O VAL B 107 SHEET 4 AA8 4 GLY B 98 PHE B 101 -1 O GLY B 98 N ASP B 93 SHEET 1 AA9 3 VAL B 18 SER B 23 0 SHEET 2 AA9 3 SER B 71 ILE B 76 -1 O LEU B 74 N ILE B 20 SHEET 3 AA9 3 PHE B 63 SER B 68 -1 N SER B 68 O SER B 71 SHEET 1 AB1 4 SER B 118 PHE B 122 0 SHEET 2 AB1 4 ALA B 134 PHE B 143 -1 O LEU B 139 N THR B 120 SHEET 3 AB1 4 TYR B 176 LEU B 184 -1 O SER B 180 N CYS B 138 SHEET 4 AB1 4 VAL B 163 THR B 165 -1 N GLU B 164 O TYR B 181 SHEET 1 AB2 4 SER B 118 PHE B 122 0 SHEET 2 AB2 4 ALA B 134 PHE B 143 -1 O LEU B 139 N THR B 120 SHEET 3 AB2 4 TYR B 176 LEU B 184 -1 O SER B 180 N CYS B 138 SHEET 4 AB2 4 SER B 169 LYS B 170 -1 N SER B 169 O ALA B 177 SHEET 1 AB3 4 SER B 157 PRO B 158 0 SHEET 2 AB3 4 THR B 149 ALA B 154 -1 N ALA B 154 O SER B 157 SHEET 3 AB3 4 TYR B 195 HIS B 201 -1 O GLN B 198 N ALA B 151 SHEET 4 AB3 4 SER B 204 VAL B 210 -1 O VAL B 206 N VAL B 199 SSBOND 1 CYS A 138 CYS A 197 1555 1555 2.10 SSBOND 2 CYS A 215 CYS B 215 1555 1555 2.04 SSBOND 3 CYS B 138 CYS B 197 1555 1555 2.11 CISPEP 1 TYR A 144 PRO A 145 0 -0.48 CISPEP 2 TYR B 144 PRO B 145 0 -3.02 SITE 1 AC1 6 GLN A 38 ILE A 59 ARG A 62 PHE A 63 SITE 2 AC1 6 GLY A 82 ASP A 83 SITE 1 AC2 1 ASN A 173 SITE 1 AC3 6 PRO A 14 GLN A 112 LEU A 129 HOH A 402 SITE 2 AC3 6 HOH A 408 HOH A 412 SITE 1 AC4 2 SER B 196 THR B 209 SITE 1 AC5 6 SER A 118 THR A 120 SER A 141 GLU B 128 SITE 2 AC5 6 LYS B 133 THR B 135 CRYST1 79.887 72.578 84.836 90.00 105.67 90.00 I 1 2 1 8 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 0.012518 0.000000 0.003511 0.00000 SCALE2 0.000000 0.013778 0.000000 0.00000 SCALE3 0.000000 0.000000 0.012242 0.00000 ATOM 1 N GLN A 1 -34.949 13.167 2.548 1.00103.71 N ANISOU 1 N GLN A 1 12110 13053 14241 -28 260 -39 N ATOM 2 CA GLN A 1 -35.206 14.469 1.935 1.00103.75 C ANISOU 2 CA GLN A 1 12063 13052 14305 111 268 -82 C ATOM 3 C GLN A 1 -34.272 15.557 2.513 1.00106.98 C ANISOU 3 C GLN A 1 12569 13416 14662 188 339 -131 C ATOM 4 O GLN A 1 -34.085 15.612 3.732 1.00107.37 O ANISOU 4 O GLN A 1 12647 13498 14650 141 437 -147 O ATOM 5 CB GLN A 1 -36.677 14.856 2.130 1.00106.55 C ANISOU 5 CB GLN A 1 12239 13511 14736 133 332 -93 C ATOM 6 CG GLN A 1 -37.265 15.634 0.964 1.00120.48 C ANISOU 6 CG GLN A 1 13914 15270 16591 248 272 -99 C ATOM 7 CD GLN A 1 -38.670 16.095 1.254 1.00141.00 C ANISOU 7 CD GLN A 1 16328 17976 19271 284 346 -109 C ATOM 8 OE1 GLN A 1 -39.574 15.297 1.530 1.00137.36 O ANISOU 8 OE1 GLN A 1 15759 17603 18829 190 357 -79 O ATOM 9 NE2 GLN A 1 -38.888 17.397 1.179 1.00134.56 N ANISOU 9 NE2 GLN A 1 15468 17153 18507 422 398 -149 N ATOM 10 N SER A 2 -33.684 16.408 1.634 1.00101.50 N ANISOU 10 N SER A 2 11929 12649 13987 296 288 -153 N ATOM 11 CA SER A 2 -32.750 17.487 2.013 1.00 99.88 C ANISOU 11 CA SER A 2 11824 12391 13733 369 342 -199 C ATOM 12 C SER A 2 -32.934 18.807 1.242 1.00101.06 C ANISOU 12 C SER A 2 11948 12504 13944 509 335 -236 C ATOM 13 O SER A 2 -32.810 18.849 0.007 1.00100.76 O ANISOU 13 O SER A 2 11919 12419 13946 556 230 -216 O ATOM 14 CB SER A 2 -31.300 17.017 1.891 1.00101.91 C ANISOU 14 CB SER A 2 12235 12572 13912 330 280 -179 C ATOM 15 OG SER A 2 -30.368 18.091 1.923 1.00106.38 O ANISOU 15 OG SER A 2 12896 13083 14441 404 303 -218 O ATOM 16 N VAL A 3 -33.153 19.889 2.001 1.00 94.75 N ANISOU 16 N VAL A 3 11134 11721 13147 572 449 -289 N ATOM 17 CA VAL A 3 -33.302 21.261 1.505 1.00 93.22 C ANISOU 17 CA VAL A 3 10929 11483 13007 709 467 -329 C ATOM 18 C VAL A 3 -31.992 22.071 1.751 1.00 89.60 C ANISOU 18 C VAL A 3 10629 10944 12471 739 490 -367 C ATOM 19 O VAL A 3 -31.867 23.191 1.233 1.00 89.91 O ANISOU 19 O VAL A 3 10695 10925 12543 846 489 -396 O ATOM 20 CB VAL A 3 -34.561 21.938 2.139 1.00 99.37 C ANISOU 20 CB VAL A 3 11571 12330 13854 767 587 -366 C ATOM 21 CG1 VAL A 3 -34.284 22.428 3.560 1.00 99.42 C ANISOU 21 CG1 VAL A 3 11634 12353 13789 742 734 -425 C ATOM 22 CG2 VAL A 3 -35.108 23.067 1.261 1.00 99.90 C ANISOU 22 CG2 VAL A 3 11574 12361 14020 915 569 -379 C ATOM 23 N LEU A 4 -31.025 21.499 2.537 1.00 78.43 N ANISOU 23 N LEU A 4 9319 9527 10953 641 508 -362 N ATOM 24 CA LEU A 4 -29.766 22.168 2.899 1.00 74.33 C ANISOU 24 CA LEU A 4 8944 8948 10349 647 531 -393 C ATOM 25 C LEU A 4 -28.747 22.254 1.745 1.00 72.87 C ANISOU 25 C LEU A 4 8851 8681 10154 683 415 -371 C ATOM 26 O LEU A 4 -28.222 21.242 1.283 1.00 70.91 O ANISOU 26 O LEU A 4 8634 8423 9887 625 325 -323 O ATOM 27 CB LEU A 4 -29.106 21.574 4.159 1.00 73.18 C ANISOU 27 CB LEU A 4 8870 8839 10097 529 586 -388 C ATOM 28 CG LEU A 4 -29.898 21.440 5.471 1.00 76.93 C ANISOU 28 CG LEU A 4 9282 9399 10548 467 711 -411 C ATOM 29 CD1 LEU A 4 -28.956 21.196 6.609 1.00 75.57 C ANISOU 29 CD1 LEU A 4 9218 9243 10254 366 755 -410 C ATOM 30 CD2 LEU A 4 -30.744 22.670 5.788 1.00 79.23 C ANISOU 30 CD2 LEU A 4 9514 9702 10890 559 826 -482 C ATOM 31 N THR A 5 -28.476 23.497 1.308 1.00 67.27 N ANISOU 31 N THR A 5 8189 7911 9460 778 424 -409 N ATOM 32 CA THR A 5 -27.579 23.844 0.210 1.00 64.86 C ANISOU 32 CA THR A 5 7969 7529 9146 823 328 -397 C ATOM 33 C THR A 5 -26.328 24.566 0.710 1.00 63.71 C ANISOU 33 C THR A 5 7961 7338 8908 812 364 -430 C ATOM 34 O THR A 5 -26.411 25.541 1.452 1.00 62.43 O ANISOU 34 O THR A 5 7826 7167 8727 840 462 -483 O ATOM 35 CB THR A 5 -28.347 24.631 -0.868 1.00 71.56 C ANISOU 35 CB THR A 5 8753 8344 10091 937 288 -401 C ATOM 36 OG1 THR A 5 -29.490 23.862 -1.240 1.00 77.39 O ANISOU 36 OG1 THR A 5 9358 9140 10906 928 251 -365 O ATOM 37 CG2 THR A 5 -27.500 24.932 -2.108 1.00 62.90 C ANISOU 37 CG2 THR A 5 7741 7173 8986 975 182 -383 C ATOM 38 N GLN A 6 -25.177 24.072 0.250 1.00 57.94 N ANISOU 38 N GLN A 6 7315 6576 8123 770 284 -398 N ATOM 39 CA GLN A 6 -23.836 24.544 0.547 1.00 56.75 C ANISOU 39 CA GLN A 6 7290 6390 7880 744 290 -412 C ATOM 40 C GLN A 6 -23.097 24.711 -0.776 1.00 59.94 C ANISOU 40 C GLN A 6 7749 6731 8292 786 187 -393 C ATOM 41 O GLN A 6 -23.329 23.914 -1.699 1.00 58.91 O ANISOU 41 O GLN A 6 7577 6599 8209 789 102 -354 O ATOM 42 CB GLN A 6 -23.074 23.429 1.315 1.00 57.31 C ANISOU 42 CB GLN A 6 7396 6504 7875 633 283 -373 C ATOM 43 CG GLN A 6 -23.528 23.186 2.743 1.00 59.09 C ANISOU 43 CG GLN A 6 7593 6796 8061 563 381 -385 C ATOM 44 CD GLN A 6 -22.629 22.185 3.417 1.00 62.38 C ANISOU 44 CD GLN A 6 8058 7245 8398 459 359 -336 C ATOM 45 OE1 GLN A 6 -23.090 21.224 3.985 1.00 62.74 O ANISOU 45 OE1 GLN A 6 8054 7341 8443 394 372 -304 O ATOM 46 NE2 GLN A 6 -21.321 22.354 3.343 1.00 53.59 N ANISOU 46 NE2 GLN A 6 7039 6104 7217 440 321 -323 N ATOM 47 N PRO A 7 -22.097 25.613 -0.856 1.00 57.60 N ANISOU 47 N PRO A 7 7558 6389 7940 800 191 -416 N ATOM 48 CA PRO A 7 -21.284 25.670 -2.082 1.00 56.50 C ANISOU 48 CA PRO A 7 7475 6197 7795 825 95 -395 C ATOM 49 C PRO A 7 -20.455 24.392 -2.226 1.00 61.75 C ANISOU 49 C PRO A 7 8158 6884 8422 753 32 -346 C ATOM 50 O PRO A 7 -19.950 23.887 -1.229 1.00 62.02 O ANISOU 50 O PRO A 7 8213 6956 8397 682 68 -334 O ATOM 51 CB PRO A 7 -20.397 26.899 -1.869 1.00 57.79 C ANISOU 51 CB PRO A 7 7745 6318 7895 837 131 -432 C ATOM 52 CG PRO A 7 -20.334 27.090 -0.387 1.00 62.59 C ANISOU 52 CG PRO A 7 8374 6966 8442 780 233 -462 C ATOM 53 CD PRO A 7 -21.653 26.613 0.144 1.00 58.88 C ANISOU 53 CD PRO A 7 7795 6544 8034 786 284 -465 C ATOM 54 N PRO A 8 -20.303 23.815 -3.436 1.00 57.66 N ANISOU 54 N PRO A 8 7634 6340 7935 769 -60 -316 N ATOM 55 CA PRO A 8 -19.503 22.590 -3.558 1.00 56.22 C ANISOU 55 CA PRO A 8 7471 6166 7722 709 -110 -274 C ATOM 56 C PRO A 8 -18.039 22.794 -3.178 1.00 57.49 C ANISOU 56 C PRO A 8 7722 6323 7797 674 -104 -269 C ATOM 57 O PRO A 8 -17.386 21.881 -2.679 1.00 56.42 O ANISOU 57 O PRO A 8 7598 6212 7625 616 -111 -234 O ATOM 58 CB PRO A 8 -19.624 22.250 -5.053 1.00 58.02 C ANISOU 58 CB PRO A 8 7691 6357 7996 744 -201 -260 C ATOM 59 CG PRO A 8 -20.838 22.975 -5.521 1.00 61.83 C ANISOU 59 CG PRO A 8 8112 6832 8547 808 -201 -279 C ATOM 60 CD PRO A 8 -20.838 24.235 -4.745 1.00 58.29 C ANISOU 60 CD PRO A 8 7691 6380 8078 840 -122 -318 C ATOM 61 N SER A 9 -17.536 24.007 -3.390 1.00 54.31 N ANISOU 61 N SER A 9 7382 5890 7362 707 -90 -301 N ATOM 62 CA SER A 9 -16.140 24.330 -3.211 1.00 52.38 C ANISOU 62 CA SER A 9 7222 5644 7038 674 -93 -297 C ATOM 63 C SER A 9 -15.883 25.714 -2.711 1.00 54.71 C ANISOU 63 C SER A 9 7578 5924 7284 680 -35 -340 C ATOM 64 O SER A 9 -16.473 26.685 -3.202 1.00 56.28 O ANISOU 64 O SER A 9 7783 6080 7519 742 -26 -374 O ATOM 65 CB SER A 9 -15.426 24.180 -4.560 1.00 55.67 C ANISOU 65 CB SER A 9 7671 6022 7459 699 -172 -282 C ATOM 66 OG SER A 9 -14.037 24.466 -4.479 1.00 63.51 O ANISOU 66 OG SER A 9 8734 7018 8377 667 -178 -274 O ATOM 67 N VAL A 10 -14.905 25.819 -1.805 1.00 49.16 N ANISOU 67 N VAL A 10 6928 5254 6496 614 -4 -335 N ATOM 68 CA VAL A 10 -14.345 27.087 -1.319 1.00 48.23 C ANISOU 68 CA VAL A 10 6892 5124 6309 596 45 -374 C ATOM 69 C VAL A 10 -12.845 26.906 -1.259 1.00 48.69 C ANISOU 69 C VAL A 10 7005 5208 6286 536 10 -341 C ATOM 70 O VAL A 10 -12.365 25.785 -1.093 1.00 46.56 O ANISOU 70 O VAL A 10 6703 4978 6008 499 -23 -291 O ATOM 71 CB VAL A 10 -14.901 27.683 0.009 1.00 53.60 C ANISOU 71 CB VAL A 10 7582 5827 6958 566 144 -415 C ATOM 72 CG1 VAL A 10 -16.381 28.051 -0.106 1.00 55.12 C ANISOU 72 CG1 VAL A 10 7716 5992 7237 640 187 -452 C ATOM 73 CG2 VAL A 10 -14.636 26.774 1.206 1.00 53.52 C ANISOU 73 CG2 VAL A 10 7550 5891 6893 477 169 -382 C ATOM 74 N SER A 11 -12.102 28.003 -1.376 1.00 47.38 N ANISOU 74 N SER A 11 6921 5020 6064 524 20 -367 N ATOM 75 CA SER A 11 -10.656 27.951 -1.326 1.00 48.29 C ANISOU 75 CA SER A 11 7082 5167 6099 463 -11 -337 C ATOM 76 C SER A 11 -10.058 29.292 -1.057 1.00 56.60 C ANISOU 76 C SER A 11 8228 6203 7076 428 23 -375 C ATOM 77 O SER A 11 -10.687 30.340 -1.287 1.00 57.60 O ANISOU 77 O SER A 11 8395 6268 7224 473 57 -427 O ATOM 78 CB SER A 11 -10.091 27.387 -2.636 1.00 50.73 C ANISOU 78 CB SER A 11 7376 5458 6441 500 -91 -303 C ATOM 79 OG SER A 11 -10.489 28.177 -3.742 1.00 55.37 O ANISOU 79 OG SER A 11 7991 5980 7068 564 -111 -335 O ATOM 80 N ALA A 12 -8.808 29.266 -0.607 1.00 52.05 N ANISOU 80 N ALA A 12 7686 5678 6411 349 11 -347 N ATOM 81 CA ALA A 12 -8.042 30.482 -0.394 1.00 51.89 C ANISOU 81 CA ALA A 12 7761 5649 6306 296 34 -378 C ATOM 82 C ALA A 12 -6.583 30.086 -0.257 1.00 53.53 C ANISOU 82 C ALA A 12 7973 5928 6439 219 -9 -323 C ATOM 83 O ALA A 12 -6.252 28.908 -0.088 1.00 51.90 O ANISOU 83 O ALA A 12 7699 5776 6245 208 -44 -264 O ATOM 84 CB ALA A 12 -8.523 31.217 0.866 1.00 53.57 C ANISOU 84 CB ALA A 12 8022 5864 6467 247 121 -427 C ATOM 85 N ALA A 13 -5.723 31.073 -0.291 1.00 50.21 N ANISOU 85 N ALA A 13 7631 5506 5941 166 -6 -340 N ATOM 86 CA ALA A 13 -4.304 30.878 -0.141 1.00 50.50 C ANISOU 86 CA ALA A 13 7672 5617 5900 87 -45 -290 C ATOM 87 C ALA A 13 -4.031 30.658 1.364 1.00 54.86 C ANISOU 87 C ALA A 13 8224 6249 6373 -13 -13 -269 C ATOM 88 O ALA A 13 -4.872 31.028 2.198 1.00 54.47 O ANISOU 88 O ALA A 13 8203 6182 6312 -28 51 -314 O ATOM 89 CB ALA A 13 -3.573 32.101 -0.666 1.00 51.20 C ANISOU 89 CB ALA A 13 7850 5677 5929 53 -48 -319 C ATOM 90 N PRO A 14 -2.922 29.978 1.743 1.00 50.84 N ANISOU 90 N PRO A 14 7675 5830 5813 -77 -56 -198 N ATOM 91 CA PRO A 14 -2.658 29.763 3.181 1.00 49.43 C ANISOU 91 CA PRO A 14 7496 5733 5551 -180 -34 -169 C ATOM 92 C PRO A 14 -2.607 31.095 3.951 1.00 52.65 C ANISOU 92 C PRO A 14 8013 6136 5857 -272 25 -232 C ATOM 93 O PRO A 14 -2.129 32.077 3.415 1.00 52.46 O ANISOU 93 O PRO A 14 8057 6077 5798 -286 25 -266 O ATOM 94 CB PRO A 14 -1.293 29.060 3.186 1.00 50.76 C ANISOU 94 CB PRO A 14 7610 5992 5684 -227 -102 -79 C ATOM 95 CG PRO A 14 -1.105 28.539 1.811 1.00 55.31 C ANISOU 95 CG PRO A 14 8136 6530 6350 -127 -149 -60 C ATOM 96 CD PRO A 14 -1.831 29.435 0.896 1.00 51.46 C ANISOU 96 CD PRO A 14 7705 5943 5903 -62 -123 -139 C ATOM 97 N GLY A 15 -3.146 31.136 5.162 1.00 49.10 N ANISOU 97 N GLY A 15 7585 5712 5358 -332 81 -252 N ATOM 98 CA GLY A 15 -3.165 32.353 5.970 1.00 48.77 C ANISOU 98 CA GLY A 15 7655 5661 5216 -423 149 -320 C ATOM 99 C GLY A 15 -4.419 33.194 5.807 1.00 52.60 C ANISOU 99 C GLY A 15 8197 6036 5753 -351 230 -418 C ATOM 100 O GLY A 15 -4.687 34.082 6.626 1.00 53.75 O ANISOU 100 O GLY A 15 8432 6164 5827 -415 306 -483 O ATOM 101 N GLN A 16 -5.195 32.913 4.763 1.00 48.90 N ANISOU 101 N GLN A 16 7676 5496 5409 -219 215 -427 N ATOM 102 CA GLN A 16 -6.433 33.602 4.409 1.00 50.08 C ANISOU 102 CA GLN A 16 7854 5541 5633 -125 277 -505 C ATOM 103 C GLN A 16 -7.653 32.959 5.072 1.00 58.43 C ANISOU 103 C GLN A 16 8849 6606 6745 -88 330 -518 C ATOM 104 O GLN A 16 -7.498 32.085 5.922 1.00 58.37 O ANISOU 104 O GLN A 16 8795 6683 6699 -153 325 -472 O ATOM 105 CB GLN A 16 -6.605 33.687 2.876 1.00 50.18 C ANISOU 105 CB GLN A 16 7843 5478 5745 -9 223 -501 C ATOM 106 CG GLN A 16 -5.442 34.368 2.139 1.00 61.03 C ANISOU 106 CG GLN A 16 9282 6842 7066 -46 175 -490 C ATOM 107 CD GLN A 16 -5.527 35.869 2.239 1.00 79.48 C ANISOU 107 CD GLN A 16 11745 9101 9355 -70 233 -565 C ATOM 108 OE1 GLN A 16 -5.055 36.490 3.206 1.00 62.56 O ANISOU 108 OE1 GLN A 16 9681 6983 7104 -180 278 -593 O ATOM 109 NE2 GLN A 16 -6.166 36.476 1.249 1.00 85.01 N ANISOU 109 NE2 GLN A 16 12469 9698 10133 31 234 -599 N ATOM 110 N LYS A 17 -8.869 33.433 4.722 1.00 57.48 N ANISOU 110 N LYS A 17 8728 6402 6712 11 383 -579 N ATOM 111 CA LYS A 17 -10.084 32.932 5.347 1.00 57.59 C ANISOU 111 CA LYS A 17 8678 6425 6778 44 443 -598 C ATOM 112 C LYS A 17 -11.119 32.433 4.350 1.00 59.57 C ANISOU 112 C LYS A 17 8837 6628 7170 177 416 -590 C ATOM 113 O LYS A 17 -11.261 32.968 3.251 1.00 59.65 O ANISOU 113 O LYS A 17 8860 6562 7241 260 386 -604 O ATOM 114 CB LYS A 17 -10.692 33.958 6.343 1.00 60.76 C ANISOU 114 CB LYS A 17 9160 6795 7130 12 563 -687 C ATOM 115 CG LYS A 17 -11.788 34.878 5.817 1.00 73.16 C ANISOU 115 CG LYS A 17 10749 8256 8792 129 624 -761 C ATOM 116 CD LYS A 17 -12.701 35.356 6.942 1.00 84.30 C ANISOU 116 CD LYS A 17 12187 9658 10184 114 754 -837 C ATOM 117 CE LYS A 17 -13.671 36.410 6.465 1.00 97.15 C ANISOU 117 CE LYS A 17 13843 11171 11900 233 820 -911 C ATOM 118 NZ LYS A 17 -14.604 36.850 7.538 1.00107.27 N ANISOU 118 NZ LYS A 17 15143 12442 13171 228 957 -991 N ATOM 119 N VAL A 18 -11.815 31.368 4.741 1.00 53.29 N ANISOU 119 N VAL A 18 7949 5880 6418 185 421 -560 N ATOM 120 CA VAL A 18 -12.909 30.815 3.962 1.00 51.84 C ANISOU 120 CA VAL A 18 7672 5664 6362 293 401 -552 C ATOM 121 C VAL A 18 -14.162 30.859 4.841 1.00 56.21 C ANISOU 121 C VAL A 18 8188 6227 6943 304 498 -598 C ATOM 122 O VAL A 18 -14.075 30.860 6.072 1.00 54.78 O ANISOU 122 O VAL A 18 8036 6099 6680 215 564 -614 O ATOM 123 CB VAL A 18 -12.650 29.389 3.373 1.00 55.80 C ANISOU 123 CB VAL A 18 8087 6206 6909 302 307 -470 C ATOM 124 CG1 VAL A 18 -11.595 29.402 2.266 1.00 55.09 C ANISOU 124 CG1 VAL A 18 8023 6095 6815 318 219 -435 C ATOM 125 CG2 VAL A 18 -12.323 28.367 4.458 1.00 55.30 C ANISOU 125 CG2 VAL A 18 7993 6232 6787 208 310 -419 C ATOM 126 N THR A 19 -15.321 30.899 4.204 1.00 55.57 N ANISOU 126 N THR A 19 8040 6100 6974 410 508 -618 N ATOM 127 CA THR A 19 -16.619 30.882 4.871 1.00 56.69 C ANISOU 127 CA THR A 19 8123 6253 7163 437 598 -658 C ATOM 128 C THR A 19 -17.432 29.873 4.090 1.00 58.97 C ANISOU 128 C THR A 19 8291 6552 7562 505 538 -611 C ATOM 129 O THR A 19 -17.437 29.908 2.862 1.00 59.30 O ANISOU 129 O THR A 19 8314 6546 7671 579 462 -591 O ATOM 130 CB THR A 19 -17.285 32.278 4.899 1.00 64.45 C ANISOU 130 CB THR A 19 9154 7157 8175 508 688 -742 C ATOM 131 OG1 THR A 19 -17.468 32.720 3.563 1.00 68.55 O ANISOU 131 OG1 THR A 19 9664 7600 8782 615 626 -735 O ATOM 132 CG2 THR A 19 -16.481 33.314 5.674 1.00 61.56 C ANISOU 132 CG2 THR A 19 8924 6773 7694 431 752 -795 C ATOM 133 N ILE A 20 -18.087 28.967 4.798 1.00 54.38 N ANISOU 133 N ILE A 20 7633 6036 6992 468 569 -593 N ATOM 134 CA ILE A 20 -18.903 27.899 4.233 1.00 52.99 C ANISOU 134 CA ILE A 20 7343 5881 6911 508 518 -548 C ATOM 135 C ILE A 20 -20.273 28.163 4.752 1.00 58.17 C ANISOU 135 C ILE A 20 7931 6549 7623 547 614 -594 C ATOM 136 O ILE A 20 -20.539 27.970 5.944 1.00 57.39 O ANISOU 136 O ILE A 20 7826 6508 7472 476 696 -611 O ATOM 137 CB ILE A 20 -18.412 26.475 4.652 1.00 54.58 C ANISOU 137 CB ILE A 20 7515 6151 7072 418 468 -475 C ATOM 138 CG1 ILE A 20 -16.957 26.233 4.222 1.00 53.08 C ANISOU 138 CG1 ILE A 20 7391 5954 6824 382 382 -428 C ATOM 139 CG2 ILE A 20 -19.363 25.389 4.106 1.00 54.64 C ANISOU 139 CG2 ILE A 20 7411 6173 7176 452 424 -436 C ATOM 140 CD1 ILE A 20 -16.254 25.399 5.072 1.00 56.39 C ANISOU 140 CD1 ILE A 20 7823 6437 7168 283 370 -377 C ATOM 141 N SER A 21 -21.138 28.580 3.846 1.00 56.15 N ANISOU 141 N SER A 21 7617 6244 7472 656 602 -611 N ATOM 142 CA SER A 21 -22.523 28.893 4.128 1.00 58.51 C ANISOU 142 CA SER A 21 7830 6551 7849 718 686 -651 C ATOM 143 C SER A 21 -23.388 27.687 3.880 1.00 62.57 C ANISOU 143 C SER A 21 8216 7121 8435 715 645 -601 C ATOM 144 O SER A 21 -23.121 26.879 2.981 1.00 62.25 O ANISOU 144 O SER A 21 8150 7078 8423 715 535 -543 O ATOM 145 CB SER A 21 -22.989 30.030 3.222 1.00 64.41 C ANISOU 145 CB SER A 21 8579 7214 8679 844 685 -685 C ATOM 146 OG SER A 21 -22.975 29.596 1.868 1.00 74.06 O ANISOU 146 OG SER A 21 9760 8412 9968 895 562 -631 O ATOM 147 N CYS A 22 -24.452 27.582 4.649 1.00 59.73 N ANISOU 147 N CYS A 22 7777 6813 8105 712 737 -627 N ATOM 148 CA CYS A 22 -25.433 26.536 4.452 1.00 60.26 C ANISOU 148 CA CYS A 22 7714 6936 8245 708 709 -585 C ATOM 149 C CYS A 22 -26.790 27.153 4.620 1.00 65.36 C ANISOU 149 C CYS A 22 8262 7594 8978 788 800 -631 C ATOM 150 O CYS A 22 -27.108 27.659 5.685 1.00 66.58 O ANISOU 150 O CYS A 22 8426 7773 9099 771 925 -687 O ATOM 151 CB CYS A 22 -25.231 25.349 5.387 1.00 60.82 C ANISOU 151 CB CYS A 22 7776 7085 8246 581 719 -547 C ATOM 152 SG CYS A 22 -26.390 23.997 5.076 1.00 65.60 S ANISOU 152 SG CYS A 22 8232 7754 8937 562 675 -490 S ATOM 153 N SER A 23 -27.577 27.140 3.573 1.00 62.95 N ANISOU 153 N SER A 23 7863 7272 8784 877 740 -608 N ATOM 154 CA SER A 23 -28.899 27.726 3.637 1.00 64.24 C ANISOU 154 CA SER A 23 7914 7449 9044 967 818 -642 C ATOM 155 C SER A 23 -29.968 26.651 3.750 1.00 66.16 C ANISOU 155 C SER A 23 8010 7783 9344 930 813 -603 C ATOM 156 O SER A 23 -29.956 25.661 3.013 1.00 62.30 O ANISOU 156 O SER A 23 7482 7313 8877 895 701 -540 O ATOM 157 CB SER A 23 -29.148 28.630 2.437 1.00 69.34 C ANISOU 157 CB SER A 23 8548 8017 9781 1100 762 -641 C ATOM 158 OG SER A 23 -30.189 29.539 2.757 1.00 84.48 O ANISOU 158 OG SER A 23 10394 9929 11777 1197 869 -690 O ATOM 159 N GLY A 24 -30.859 26.859 4.708 1.00 65.51 N ANISOU 159 N GLY A 24 7855 7758 9280 931 941 -645 N ATOM 160 CA GLY A 24 -31.988 25.987 4.989 1.00 66.74 C ANISOU 160 CA GLY A 24 7861 8009 9486 894 965 -619 C ATOM 161 C GLY A 24 -33.304 26.728 5.046 1.00 73.98 C ANISOU 161 C GLY A 24 8647 8950 10513 1002 1057 -657 C ATOM 162 O GLY A 24 -33.548 27.667 4.279 1.00 75.80 O ANISOU 162 O GLY A 24 8861 9115 10823 1130 1038 -669 O ATOM 163 N ASN A 25 -34.162 26.298 5.956 1.00 70.51 N ANISOU 163 N ASN A 25 8108 8604 10077 951 1157 -671 N ATOM 164 CA ASN A 25 -35.464 26.884 6.164 1.00 71.39 C ANISOU 164 CA ASN A 25 8077 8757 10291 1044 1262 -707 C ATOM 165 C ASN A 25 -35.722 27.066 7.652 1.00 76.38 C ANISOU 165 C ASN A 25 8716 9445 10858 987 1438 -776 C ATOM 166 O ASN A 25 -34.815 26.830 8.449 1.00 73.53 O ANISOU 166 O ASN A 25 8485 9082 10369 878 1466 -793 O ATOM 167 CB ASN A 25 -36.555 26.089 5.426 1.00 71.77 C ANISOU 167 CB ASN A 25 7945 8881 10444 1053 1184 -639 C ATOM 168 CG ASN A 25 -36.808 24.688 5.915 1.00 95.70 C ANISOU 168 CG ASN A 25 10922 12013 13429 904 1168 -595 C ATOM 169 OD1 ASN A 25 -36.972 24.429 7.111 1.00 86.38 O ANISOU 169 OD1 ASN A 25 9739 10897 12184 820 1284 -627 O ATOM 170 ND2 ASN A 25 -36.973 23.770 4.981 1.00 90.89 N ANISOU 170 ND2 ASN A 25 10256 11421 12856 869 1029 -520 N ATOM 171 N ASN A 26 -36.933 27.533 8.018 1.00 77.03 N ANISOU 171 N ASN A 26 8663 9579 11028 1061 1558 -816 N ATOM 172 CA ASN A 26 -37.354 27.796 9.403 1.00 78.48 C ANISOU 172 CA ASN A 26 8836 9821 11161 1019 1745 -892 C ATOM 173 C ASN A 26 -37.463 26.548 10.273 1.00 80.71 C ANISOU 173 C ASN A 26 9091 10217 11356 847 1767 -862 C ATOM 174 O ASN A 26 -37.108 26.614 11.450 1.00 81.42 O ANISOU 174 O ASN A 26 9268 10333 11335 757 1880 -914 O ATOM 175 CB ASN A 26 -38.661 28.609 9.454 1.00 83.81 C ANISOU 175 CB ASN A 26 9357 10519 11967 1159 1867 -939 C ATOM 176 CG ASN A 26 -39.695 28.191 8.435 0.50112.03 C ANISOU 176 CG ASN A 26 12737 14145 15685 1231 1773 -866 C ATOM 177 OD1 ASN A 26 -39.542 28.413 7.225 0.50106.65 O ANISOU 177 OD1 ASN A 26 12051 13396 15073 1317 1639 -817 O ATOM 178 ND2 ASN A 26 -40.762 27.556 8.899 0.50106.23 N ANISOU 178 ND2 ASN A 26 11838 13536 14988 1185 1837 -853 N ATOM 179 N ASER A 27 -37.949 25.432 9.699 0.50 75.94 N ANISOU 179 N ASER A 27 8374 9681 10800 797 1659 -779 N ATOM 180 N BSER A 27 -37.953 25.427 9.708 0.50 75.69 N ANISOU 180 N BSER A 27 8342 9649 10767 796 1660 -779 N ATOM 181 CA ASER A 27 -38.132 24.148 10.382 0.50 75.44 C ANISOU 181 CA ASER A 27 8276 9721 10667 633 1662 -736 C ATOM 182 CA BSER A 27 -38.131 24.167 10.435 0.50 75.09 C ANISOU 182 CA BSER A 27 8234 9678 10620 631 1669 -739 C ATOM 183 C ASER A 27 -36.810 23.490 10.794 0.50 75.81 C ANISOU 183 C ASER A 27 8496 9738 10569 497 1599 -707 C ATOM 184 C BSER A 27 -36.806 23.481 10.801 0.50 75.61 C ANISOU 184 C BSER A 27 8472 9713 10544 496 1599 -707 C ATOM 185 O ASER A 27 -36.771 22.769 11.794 0.50 74.58 O ANISOU 185 O ASER A 27 8359 9655 10322 359 1653 -698 O ATOM 186 O BSER A 27 -36.757 22.747 11.791 0.50 74.34 O ANISOU 186 O BSER A 27 8331 9625 10290 357 1650 -697 O ATOM 187 CB ASER A 27 -38.957 23.190 9.522 0.50 79.14 C ANISOU 187 CB ASER A 27 8590 10251 11230 619 1551 -654 C ATOM 188 CB BSER A 27 -39.070 23.217 9.688 0.50 78.51 C ANISOU 188 CB BSER A 27 8499 10184 11148 615 1576 -662 C ATOM 189 OG ASER A 27 -40.348 23.450 9.631 0.50 87.82 O ANISOU 189 OG ASER A 27 9499 11435 12434 683 1644 -673 O ATOM 190 OG BSER A 27 -38.553 22.761 8.450 0.50 81.39 O ANISOU 190 OG BSER A 27 8898 10487 11542 628 1394 -593 O ATOM 191 N ASN A 28 -35.732 23.749 10.031 1.00 70.66 N ANISOU 191 N ASN A 28 7967 8982 9898 536 1485 -689 N ATOM 192 CA ASN A 28 -34.414 23.184 10.301 1.00 68.02 C ANISOU 192 CA ASN A 28 7790 8616 9440 426 1415 -656 C ATOM 193 C ASN A 28 -33.465 24.231 10.928 1.00 70.81 C ANISOU 193 C ASN A 28 8299 8907 9700 438 1490 -725 C ATOM 194 O ASN A 28 -33.538 24.407 12.145 1.00 69.75 O ANISOU 194 O ASN A 28 8197 8822 9483 366 1619 -774 O ATOM 195 CB ASN A 28 -33.819 22.437 9.096 1.00 63.15 C ANISOU 195 CB ASN A 28 7198 7947 8851 426 1232 -575 C ATOM 196 CG ASN A 28 -33.908 23.112 7.756 1.00 71.12 C ANISOU 196 CG ASN A 28 8179 8880 9964 568 1148 -574 C ATOM 197 OD1 ASN A 28 -33.383 24.193 7.539 1.00 63.91 O ANISOU 197 OD1 ASN A 28 7346 7889 9047 655 1165 -619 O ATOM 198 ND2 ASN A 28 -34.435 22.407 6.786 1.00 61.57 N ANISOU 198 ND2 ASN A 28 6873 7686 8834 579 1041 -514 N ATOM 199 N ILE A 29 -32.606 24.922 10.127 1.00 68.14 N ANISOU 199 N ILE A 29 8056 8464 9369 519 1413 -731 N ATOM 200 CA ILE A 29 -31.607 25.916 10.579 1.00 68.00 C ANISOU 200 CA ILE A 29 8196 8379 9263 524 1463 -791 C ATOM 201 C ILE A 29 -32.238 27.051 11.405 1.00 75.03 C ANISOU 201 C ILE A 29 9081 9272 10157 577 1643 -893 C ATOM 202 O ILE A 29 -31.663 27.464 12.418 1.00 75.95 O ANISOU 202 O ILE A 29 9311 9389 10156 504 1734 -946 O ATOM 203 CB ILE A 29 -30.733 26.445 9.391 1.00 69.76 C ANISOU 203 CB ILE A 29 8500 8492 9513 610 1342 -773 C ATOM 204 CG1 ILE A 29 -29.893 25.291 8.780 1.00 67.97 C ANISOU 204 CG1 ILE A 29 8309 8264 9254 536 1184 -682 C ATOM 205 CG2 ILE A 29 -29.816 27.602 9.826 1.00 70.62 C ANISOU 205 CG2 ILE A 29 8763 8530 9539 621 1403 -841 C ATOM 206 CD1 ILE A 29 -29.088 25.623 7.570 1.00 70.64 C ANISOU 206 CD1 ILE A 29 8711 8510 9618 607 1061 -657 C ATOM 207 N GLY A 30 -33.422 27.497 11.000 1.00 72.98 N ANISOU 207 N GLY A 30 8685 9017 10026 698 1694 -918 N ATOM 208 CA GLY A 30 -34.148 28.558 11.685 1.00 74.89 C ANISOU 208 CA GLY A 30 8903 9256 10296 771 1870 -1016 C ATOM 209 C GLY A 30 -34.505 28.316 13.145 1.00 80.46 C ANISOU 209 C GLY A 30 9605 10055 10909 657 2025 -1066 C ATOM 210 O GLY A 30 -34.444 29.259 13.946 1.00 80.96 O ANISOU 210 O GLY A 30 9748 10093 10922 668 2169 -1159 O ATOM 211 N LYS A 31 -34.889 27.064 13.520 1.00 76.40 N ANISOU 211 N LYS A 31 9008 9651 10370 540 2003 -1006 N ATOM 212 CA LYS A 31 -35.300 26.806 14.910 1.00 77.12 C ANISOU 212 CA LYS A 31 9090 9841 10371 424 2153 -1050 C ATOM 213 C LYS A 31 -34.438 25.770 15.685 1.00 79.07 C ANISOU 213 C LYS A 31 9437 10144 10463 230 2105 -995 C ATOM 214 O LYS A 31 -34.582 25.664 16.903 1.00 77.97 O ANISOU 214 O LYS A 31 9324 10078 10222 120 2227 -1033 O ATOM 215 CB LYS A 31 -36.808 26.437 14.994 1.00 80.49 C ANISOU 215 CB LYS A 31 9312 10368 10903 454 2231 -1049 C ATOM 216 CG LYS A 31 -37.225 25.106 14.387 1.00 76.88 C ANISOU 216 CG LYS A 31 8735 9979 10498 398 2100 -942 C ATOM 217 CD LYS A 31 -38.672 24.781 14.689 1.00 85.82 C ANISOU 217 CD LYS A 31 9674 11225 11709 401 2197 -948 C ATOM 218 N ASN A 32 -33.527 25.057 15.011 1.00 75.51 N ANISOU 218 N ASN A 32 9044 9655 9990 191 1933 -907 N ATOM 219 CA ASN A 32 -32.743 24.011 15.675 1.00 74.81 C ANISOU 219 CA ASN A 32 9037 9616 9771 21 1877 -842 C ATOM 220 C ASN A 32 -31.226 24.269 15.720 1.00 76.17 C ANISOU 220 C ASN A 32 9386 9720 9836 -22 1803 -829 C ATOM 221 O ASN A 32 -30.719 25.132 15.003 1.00 74.65 O ANISOU 221 O ASN A 32 9251 9434 9680 82 1763 -857 O ATOM 222 CB ASN A 32 -33.065 22.637 15.040 1.00 74.23 C ANISOU 222 CB ASN A 32 8866 9582 9757 -21 1748 -736 C ATOM 223 CG ASN A 32 -34.499 22.216 15.282 1.00 83.40 C ANISOU 223 CG ASN A 32 9859 10839 10990 -30 1829 -740 C ATOM 224 OD1 ASN A 32 -34.927 22.047 16.420 1.00 77.83 O ANISOU 224 OD1 ASN A 32 9140 10220 10212 -128 1952 -768 O ATOM 225 ND2 ASN A 32 -35.292 22.104 14.228 1.00 72.09 N ANISOU 225 ND2 ASN A 32 8293 9399 9698 70 1768 -715 N ATOM 226 N TYR A 33 -30.521 23.507 16.590 1.00 71.73 N ANISOU 226 N TYR A 33 8905 9210 9139 -180 1784 -781 N ATOM 227 CA TYR A 33 -29.075 23.572 16.777 1.00 70.47 C ANISOU 227 CA TYR A 33 8900 9011 8865 -246 1710 -753 C ATOM 228 C TYR A 33 -28.307 22.977 15.589 1.00 68.99 C ANISOU 228 C TYR A 33 8722 8758 8732 -203 1527 -665 C ATOM 229 O TYR A 33 -28.537 21.829 15.175 1.00 66.97 O ANISOU 229 O TYR A 33 8396 8526 8523 -231 1437 -583 O ATOM 230 CB TYR A 33 -28.645 22.923 18.106 1.00 73.65 C ANISOU 230 CB TYR A 33 9372 9499 9112 -429 1745 -720 C ATOM 231 CG TYR A 33 -28.958 23.738 19.347 1.00 79.60 C ANISOU 231 CG TYR A 33 10177 10301 9766 -490 1924 -819 C ATOM 232 CD1 TYR A 33 -28.586 25.079 19.440 1.00 82.05 C ANISOU 232 CD1 TYR A 33 10581 10548 10047 -431 1999 -916 C ATOM 233 CD2 TYR A 33 -29.540 23.145 20.465 1.00 82.61 C ANISOU 233 CD2 TYR A 33 10529 10789 10069 -621 2015 -814 C ATOM 234 CE1 TYR A 33 -28.833 25.821 20.594 1.00 84.81 C ANISOU 234 CE1 TYR A 33 10992 10936 10297 -495 2168 -1014 C ATOM 235 CE2 TYR A 33 -29.789 23.878 21.629 1.00 85.45 C ANISOU 235 CE2 TYR A 33 10945 11195 10325 -687 2185 -909 C ATOM 236 CZ TYR A 33 -29.441 25.219 21.685 1.00 94.74 C ANISOU 236 CZ TYR A 33 12215 12304 11478 -621 2263 -1012 C ATOM 237 OH TYR A 33 -29.695 25.950 22.822 1.00100.73 O ANISOU 237 OH TYR A 33 13039 13103 12133 -689 2438 -1115 O ATOM 238 N VAL A 34 -27.374 23.775 15.068 1.00 62.79 N ANISOU 238 N VAL A 34 8032 7891 7934 -142 1479 -687 N ATOM 239 CA VAL A 34 -26.545 23.448 13.905 1.00 59.95 C ANISOU 239 CA VAL A 34 7697 7462 7621 -90 1321 -621 C ATOM 240 C VAL A 34 -25.207 22.872 14.307 1.00 59.65 C ANISOU 240 C VAL A 34 7765 7434 7466 -200 1239 -553 C ATOM 241 O VAL A 34 -24.479 23.455 15.121 1.00 58.83 O ANISOU 241 O VAL A 34 7766 7342 7245 -269 1288 -583 O ATOM 242 CB VAL A 34 -26.409 24.675 12.952 1.00 62.23 C ANISOU 242 CB VAL A 34 8012 7654 7980 53 1313 -682 C ATOM 243 CG1 VAL A 34 -25.408 24.422 11.827 1.00 60.05 C ANISOU 243 CG1 VAL A 34 7779 7310 7727 93 1159 -620 C ATOM 244 CG2 VAL A 34 -27.764 25.078 12.386 1.00 62.52 C ANISOU 244 CG2 VAL A 34 7922 7680 8153 176 1367 -725 C ATOM 245 N SER A 35 -24.876 21.737 13.703 1.00 53.92 N ANISOU 245 N SER A 35 7010 6703 6776 -216 1113 -458 N ATOM 246 CA SER A 35 -23.583 21.086 13.900 1.00 53.04 C ANISOU 246 CA SER A 35 6982 6592 6579 -299 1017 -378 C ATOM 247 C SER A 35 -22.825 21.095 12.578 1.00 54.68 C ANISOU 247 C SER A 35 7208 6717 6852 -207 892 -347 C ATOM 248 O SER A 35 -23.448 21.162 11.519 1.00 54.56 O ANISOU 248 O SER A 35 7123 6656 6952 -103 861 -362 O ATOM 249 CB SER A 35 -23.761 19.651 14.388 1.00 56.03 C ANISOU 249 CB SER A 35 7322 7030 6937 -403 978 -288 C ATOM 250 OG SER A 35 -24.021 19.614 15.778 1.00 68.03 O ANISOU 250 OG SER A 35 8863 8633 8351 -523 1078 -300 O ATOM 251 N TRP A 36 -21.495 21.011 12.642 1.00 49.98 N ANISOU 251 N TRP A 36 6702 6108 6182 -249 822 -302 N ATOM 252 CA TRP A 36 -20.615 20.938 11.472 1.00 49.01 C ANISOU 252 CA TRP A 36 6602 5915 6104 -177 706 -266 C ATOM 253 C TRP A 36 -19.709 19.745 11.624 1.00 53.17 C ANISOU 253 C TRP A 36 7151 6459 6591 -250 611 -161 C ATOM 254 O TRP A 36 -19.213 19.467 12.724 1.00 54.29 O ANISOU 254 O TRP A 36 7338 6660 6629 -359 628 -123 O ATOM 255 CB TRP A 36 -19.785 22.223 11.296 1.00 47.79 C ANISOU 255 CB TRP A 36 6536 5720 5903 -141 718 -322 C ATOM 256 CG TRP A 36 -20.604 23.404 10.869 1.00 48.78 C ANISOU 256 CG TRP A 36 6643 5800 6089 -42 794 -419 C ATOM 257 CD1 TRP A 36 -21.203 24.326 11.676 1.00 52.80 C ANISOU 257 CD1 TRP A 36 7171 6328 6562 -52 922 -502 C ATOM 258 CD2 TRP A 36 -20.943 23.764 9.521 1.00 47.97 C ANISOU 258 CD2 TRP A 36 6501 5625 6101 86 746 -438 C ATOM 259 NE1 TRP A 36 -21.863 25.266 10.912 1.00 52.48 N ANISOU 259 NE1 TRP A 36 7104 6223 6612 70 956 -570 N ATOM 260 CE2 TRP A 36 -21.736 24.930 9.585 1.00 53.34 C ANISOU 260 CE2 TRP A 36 7174 6279 6813 154 845 -528 C ATOM 261 CE3 TRP A 36 -20.601 23.246 8.258 1.00 48.37 C ANISOU 261 CE3 TRP A 36 6528 5627 6224 148 629 -389 C ATOM 262 CZ2 TRP A 36 -22.225 25.569 8.434 1.00 52.78 C ANISOU 262 CZ2 TRP A 36 7067 6138 6848 283 823 -560 C ATOM 263 CZ3 TRP A 36 -21.096 23.874 7.121 1.00 49.68 C ANISOU 263 CZ3 TRP A 36 6663 5729 6486 266 609 -426 C ATOM 264 CH2 TRP A 36 -21.882 25.030 7.216 1.00 51.04 C ANISOU 264 CH2 TRP A 36 6825 5879 6690 332 701 -505 C ATOM 265 N TYR A 37 -19.499 19.028 10.526 1.00 47.45 N ANISOU 265 N TYR A 37 6395 5682 5950 -190 510 -113 N ATOM 266 CA TYR A 37 -18.675 17.831 10.542 1.00 46.60 C ANISOU 266 CA TYR A 37 6303 5575 5826 -239 419 -12 C ATOM 267 C TYR A 37 -17.548 17.982 9.547 1.00 49.78 C ANISOU 267 C TYR A 37 6747 5920 6249 -173 332 6 C ATOM 268 O TYR A 37 -17.738 18.579 8.502 1.00 48.59 O ANISOU 268 O TYR A 37 6584 5714 6164 -78 318 -44 O ATOM 269 CB TYR A 37 -19.530 16.589 10.217 1.00 47.28 C ANISOU 269 CB TYR A 37 6316 5654 5994 -243 386 35 C ATOM 270 CG TYR A 37 -20.718 16.429 11.133 1.00 50.17 C ANISOU 270 CG TYR A 37 6632 6085 6347 -310 476 15 C ATOM 271 CD1 TYR A 37 -21.873 17.183 10.948 1.00 51.53 C ANISOU 271 CD1 TYR A 37 6743 6264 6571 -256 555 -68 C ATOM 272 CD2 TYR A 37 -20.690 15.527 12.191 1.00 52.82 C ANISOU 272 CD2 TYR A 37 6976 6476 6618 -426 484 84 C ATOM 273 CE1 TYR A 37 -22.939 17.099 11.834 1.00 51.83 C ANISOU 273 CE1 TYR A 37 6730 6371 6593 -318 649 -90 C ATOM 274 CE2 TYR A 37 -21.783 15.380 13.040 1.00 55.03 C ANISOU 274 CE2 TYR A 37 7209 6821 6879 -495 571 66 C ATOM 275 CZ TYR A 37 -22.898 16.187 12.872 1.00 61.12 C ANISOU 275 CZ TYR A 37 7918 7605 7699 -441 658 -25 C ATOM 276 OH TYR A 37 -23.979 16.084 13.726 1.00 63.99 O ANISOU 276 OH TYR A 37 8227 8041 8044 -507 756 -49 O ATOM 277 N GLN A 38 -16.378 17.437 9.877 1.00 47.80 N ANISOU 277 N GLN A 38 6539 5682 5941 -223 272 83 N ATOM 278 CA GLN A 38 -15.216 17.454 9.003 1.00 47.46 C ANISOU 278 CA GLN A 38 6527 5593 5912 -168 190 110 C ATOM 279 C GLN A 38 -14.991 16.016 8.545 1.00 51.89 C ANISOU 279 C GLN A 38 7059 6121 6534 -160 109 196 C ATOM 280 O GLN A 38 -15.042 15.104 9.349 1.00 49.26 O ANISOU 280 O GLN A 38 6720 5822 6175 -234 103 264 O ATOM 281 CB GLN A 38 -13.977 17.982 9.739 1.00 49.47 C ANISOU 281 CB GLN A 38 6848 5893 6055 -230 185 134 C ATOM 282 CG GLN A 38 -12.731 18.047 8.855 1.00 52.77 C ANISOU 282 CG GLN A 38 7289 6274 6485 -177 105 164 C ATOM 283 CD GLN A 38 -11.479 18.317 9.649 1.00 67.10 C ANISOU 283 CD GLN A 38 9154 8148 8192 -253 87 211 C ATOM 284 OE1 GLN A 38 -11.047 17.518 10.492 1.00 57.18 O ANISOU 284 OE1 GLN A 38 7896 6941 6888 -329 60 297 O ATOM 285 NE2 GLN A 38 -10.855 19.443 9.366 1.00 58.20 N ANISOU 285 NE2 GLN A 38 8073 7018 7024 -238 95 161 N ATOM 286 N GLN A 39 -14.749 15.827 7.257 1.00 51.17 N ANISOU 286 N GLN A 39 6960 5962 6522 -72 50 191 N ATOM 287 CA GLN A 39 -14.503 14.519 6.691 1.00 52.23 C ANISOU 287 CA GLN A 39 7077 6049 6718 -55 -22 260 C ATOM 288 C GLN A 39 -13.134 14.598 6.001 1.00 61.08 C ANISOU 288 C GLN A 39 8232 7139 7836 -5 -83 285 C ATOM 289 O GLN A 39 -12.966 15.226 4.943 1.00 58.18 O ANISOU 289 O GLN A 39 7872 6730 7502 70 -98 233 O ATOM 290 CB GLN A 39 -15.655 14.127 5.741 1.00 52.76 C ANISOU 290 CB GLN A 39 7096 6065 6885 -3 -28 223 C ATOM 291 CG GLN A 39 -15.845 12.628 5.528 1.00 74.58 C ANISOU 291 CG GLN A 39 9843 8790 9705 -22 -77 291 C ATOM 292 CD GLN A 39 -17.163 12.272 4.854 1.00 91.35 C ANISOU 292 CD GLN A 39 11916 10884 11910 -3 -74 255 C ATOM 293 OE1 GLN A 39 -17.744 13.035 4.056 1.00 83.25 O ANISOU 293 OE1 GLN A 39 10865 9844 10924 57 -63 185 O ATOM 294 NE2 GLN A 39 -17.648 11.074 5.141 1.00 91.98 N ANISOU 294 NE2 GLN A 39 11979 10953 12016 -58 -88 308 N ATOM 295 N LEU A 40 -12.138 14.008 6.655 1.00 64.33 N ANISOU 295 N LEU A 40 8663 7579 8202 -51 -117 370 N ATOM 296 CA LEU A 40 -10.775 13.985 6.141 1.00 66.17 C ANISOU 296 CA LEU A 40 8916 7795 8430 -11 -173 407 C ATOM 297 C LEU A 40 -10.631 12.865 5.140 1.00 73.85 C ANISOU 297 C LEU A 40 9874 8690 9497 54 -228 441 C ATOM 298 O LEU A 40 -11.440 11.927 5.194 1.00 72.63 O ANISOU 298 O LEU A 40 9700 8504 9391 38 -231 463 O ATOM 299 CB LEU A 40 -9.753 13.897 7.282 1.00 66.95 C ANISOU 299 CB LEU A 40 9034 7966 8440 -86 -188 487 C ATOM 300 CG LEU A 40 -9.468 15.233 7.946 1.00 71.48 C ANISOU 300 CG LEU A 40 9640 8608 8911 -138 -143 441 C ATOM 301 CD1 LEU A 40 -8.816 15.051 9.289 1.00 71.90 C ANISOU 301 CD1 LEU A 40 9710 8744 8866 -241 -151 520 C ATOM 302 CD2 LEU A 40 -8.650 16.126 7.049 1.00 74.86 C ANISOU 302 CD2 LEU A 40 10089 9018 9338 -78 -161 397 C ATOM 303 N PRO A 41 -9.692 12.981 4.154 0.90 74.73 N ANISOU 303 N PRO A 41 9996 8764 9635 124 -267 437 N ATOM 304 CA PRO A 41 -9.587 11.939 3.122 0.90 76.02 C ANISOU 304 CA PRO A 41 10152 8844 9887 188 -309 456 C ATOM 305 C PRO A 41 -9.384 10.540 3.694 1.00 81.95 C ANISOU 305 C PRO A 41 10897 9575 10664 160 -339 553 C ATOM 306 O PRO A 41 -8.431 10.297 4.450 1.00 82.53 O ANISOU 306 O PRO A 41 10972 9689 10696 132 -360 633 O ATOM 307 CB PRO A 41 -8.421 12.414 2.246 0.90 77.67 C ANISOU 307 CB PRO A 41 10375 9041 10096 252 -335 442 C ATOM 308 CG PRO A 41 -8.332 13.884 2.488 1.00 81.40 C ANISOU 308 CG PRO A 41 10862 9571 10495 232 -302 384 C ATOM 309 CD PRO A 41 -8.697 14.053 3.925 1.00 76.91 C ANISOU 309 CD PRO A 41 10293 9072 9859 143 -269 411 C ATOM 310 N GLY A 42 -10.357 9.677 3.399 1.00 78.09 N ANISOU 310 N GLY A 42 10403 9030 10240 158 -340 549 N ATOM 311 CA GLY A 42 -10.402 8.290 3.852 1.00 78.29 C ANISOU 311 CA GLY A 42 10430 9016 10299 128 -365 634 C ATOM 312 C GLY A 42 -10.641 8.090 5.334 1.00 82.32 C ANISOU 312 C GLY A 42 10936 9595 10747 32 -349 700 C ATOM 313 O GLY A 42 -10.513 6.962 5.820 1.00 83.98 O ANISOU 313 O GLY A 42 11154 9777 10977 3 -376 788 O ATOM 314 N ARG A 43 -11.019 9.164 6.063 1.00 77.19 N ANISOU 314 N ARG A 43 10278 9030 10020 -21 -303 659 N ATOM 315 CA ARG A 43 -11.299 9.094 7.507 1.00 76.43 C ANISOU 315 CA ARG A 43 10183 9010 9848 -125 -278 710 C ATOM 316 C ARG A 43 -12.788 9.216 7.832 1.00 78.20 C ANISOU 316 C ARG A 43 10386 9253 10072 -178 -222 656 C ATOM 317 O ARG A 43 -13.558 9.758 7.028 1.00 78.18 O ANISOU 317 O ARG A 43 10365 9228 10111 -132 -196 567 O ATOM 318 CB ARG A 43 -10.469 10.133 8.289 1.00 74.28 C ANISOU 318 CB ARG A 43 9924 8827 9473 -164 -264 714 C ATOM 319 CG ARG A 43 -8.977 9.945 8.069 1.00 84.21 C ANISOU 319 CG ARG A 43 11188 10080 10727 -122 -323 782 C ATOM 320 CD ARG A 43 -8.110 10.480 9.188 1.00 99.49 C ANISOU 320 CD ARG A 43 13135 12114 12553 -196 -328 836 C ATOM 321 NE ARG A 43 -6.754 9.935 9.088 1.00110.16 N ANISOU 321 NE ARG A 43 14476 13462 13918 -161 -394 932 N ATOM 322 CZ ARG A 43 -5.781 10.454 8.341 1.00122.56 C ANISOU 322 CZ ARG A 43 16039 15031 15498 -95 -416 914 C ATOM 323 NH1 ARG A 43 -5.992 11.562 7.636 1.00104.52 N ANISOU 323 NH1 ARG A 43 13765 12743 13205 -62 -380 805 N ATOM 324 NH2 ARG A 43 -4.589 9.872 8.297 1.00108.97 N ANISOU 324 NH2 ARG A 43 14297 13311 13797 -62 -472 1007 N ATOM 325 N THR A 44 -13.190 8.711 9.016 1.00 72.80 N ANISOU 325 N THR A 44 9703 8617 9340 -276 -204 715 N ATOM 326 CA THR A 44 -14.565 8.794 9.517 1.00 71.43 C ANISOU 326 CA THR A 44 9505 8481 9156 -341 -142 673 C ATOM 327 C THR A 44 -14.921 10.269 9.888 1.00 70.17 C ANISOU 327 C THR A 44 9337 8395 8930 -352 -68 580 C ATOM 328 O THR A 44 -14.057 10.955 10.443 1.00 67.74 O ANISOU 328 O THR A 44 9059 8137 8543 -373 -64 590 O ATOM 329 CB THR A 44 -14.821 7.756 10.642 1.00 79.83 C ANISOU 329 CB THR A 44 10576 9571 10184 -447 -145 769 C ATOM 330 OG1 THR A 44 -16.222 7.678 10.914 1.00 82.61 O ANISOU 330 OG1 THR A 44 10895 9949 10545 -502 -88 726 O ATOM 331 CG2 THR A 44 -14.068 8.052 11.921 1.00 78.14 C ANISOU 331 CG2 THR A 44 10390 9442 9857 -527 -140 830 C ATOM 332 N PRO A 45 -16.142 10.786 9.546 1.00 64.24 N ANISOU 332 N PRO A 45 8547 7647 8214 -334 -12 492 N ATOM 333 CA PRO A 45 -16.455 12.187 9.860 1.00 62.87 C ANISOU 333 CA PRO A 45 8371 7529 7989 -332 63 403 C ATOM 334 C PRO A 45 -16.491 12.497 11.346 1.00 65.94 C ANISOU 334 C PRO A 45 8781 8008 8266 -441 124 418 C ATOM 335 O PRO A 45 -17.019 11.722 12.151 1.00 67.63 O ANISOU 335 O PRO A 45 8983 8256 8458 -527 141 468 O ATOM 336 CB PRO A 45 -17.802 12.434 9.175 1.00 64.59 C ANISOU 336 CB PRO A 45 8531 7726 8283 -287 102 325 C ATOM 337 CG PRO A 45 -18.369 11.127 8.946 1.00 69.50 C ANISOU 337 CG PRO A 45 9124 8314 8967 -312 65 378 C ATOM 338 CD PRO A 45 -17.255 10.143 8.819 1.00 65.33 C ANISOU 338 CD PRO A 45 8641 7737 8444 -313 -16 470 C ATOM 339 N LYS A 46 -15.879 13.613 11.712 1.00 59.56 N ANISOU 339 N LYS A 46 8010 7238 7381 -447 155 378 N ATOM 340 CA LYS A 46 -15.844 14.014 13.105 1.00 59.77 C ANISOU 340 CA LYS A 46 8069 7353 7289 -557 216 382 C ATOM 341 C LYS A 46 -16.564 15.332 13.335 1.00 61.59 C ANISOU 341 C LYS A 46 8300 7613 7488 -549 320 266 C ATOM 342 O LYS A 46 -16.528 16.237 12.495 1.00 59.45 O ANISOU 342 O LYS A 46 8031 7299 7259 -459 329 191 O ATOM 343 CB LYS A 46 -14.410 14.014 13.694 1.00 62.30 C ANISOU 343 CB LYS A 46 8445 7709 7516 -610 163 458 C ATOM 344 CG LYS A 46 -13.416 14.973 13.040 1.00 69.51 C ANISOU 344 CG LYS A 46 9390 8601 8420 -543 137 420 C ATOM 345 CD LYS A 46 -12.077 15.024 13.775 0.50 72.80 C ANISOU 345 CD LYS A 46 9852 9075 8733 -615 91 496 C ATOM 346 CE LYS A 46 -12.007 16.127 14.803 0.50 74.80 C ANISOU 346 CE LYS A 46 10157 9405 8858 -707 163 443 C ATOM 347 NZ LYS A 46 -10.601 16.451 15.156 0.50 75.11 N ANISOU 347 NZ LYS A 46 10239 9491 8808 -755 109 498 N ATOM 348 N LEU A 47 -17.257 15.404 14.469 1.00 59.32 N ANISOU 348 N LEU A 47 8011 7396 7131 -644 403 251 N ATOM 349 CA LEU A 47 -17.961 16.593 14.909 1.00 59.86 C ANISOU 349 CA LEU A 47 8086 7498 7161 -650 518 142 C ATOM 350 C LEU A 47 -16.906 17.634 15.270 1.00 62.13 C ANISOU 350 C LEU A 47 8454 7804 7349 -673 527 114 C ATOM 351 O LEU A 47 -15.929 17.317 15.959 1.00 61.57 O ANISOU 351 O LEU A 47 8432 7777 7187 -759 481 190 O ATOM 352 CB LEU A 47 -18.875 16.279 16.124 1.00 60.70 C ANISOU 352 CB LEU A 47 8175 7683 7204 -762 606 142 C ATOM 353 CG LEU A 47 -19.787 17.411 16.584 1.00 65.09 C ANISOU 353 CG LEU A 47 8725 8273 7734 -762 743 23 C ATOM 354 CD1 LEU A 47 -20.749 17.824 15.491 1.00 64.40 C ANISOU 354 CD1 LEU A 47 8562 8128 7779 -631 768 -53 C ATOM 355 CD2 LEU A 47 -20.554 17.023 17.844 1.00 67.68 C ANISOU 355 CD2 LEU A 47 9041 8688 7985 -887 830 30 C ATOM 356 N ILE A 48 -17.062 18.854 14.727 1.00 56.92 N ANISOU 356 N ILE A 48 7808 7105 6712 -594 575 13 N ATOM 357 CA ILE A 48 -16.123 19.940 14.987 1.00 55.16 C ANISOU 357 CA ILE A 48 7668 6891 6398 -616 588 -25 C ATOM 358 C ILE A 48 -16.810 21.163 15.590 1.00 57.23 C ANISOU 358 C ILE A 48 7965 7170 6610 -633 721 -141 C ATOM 359 O ILE A 48 -16.143 22.000 16.183 1.00 57.00 O ANISOU 359 O ILE A 48 8019 7166 6475 -694 753 -174 O ATOM 360 CB ILE A 48 -15.285 20.293 13.724 1.00 56.74 C ANISOU 360 CB ILE A 48 7880 7018 6660 -512 505 -25 C ATOM 361 CG1 ILE A 48 -16.139 21.029 12.644 1.00 54.88 C ANISOU 361 CG1 ILE A 48 7609 6708 6535 -382 541 -117 C ATOM 362 CG2 ILE A 48 -14.555 19.045 13.167 1.00 56.66 C ANISOU 362 CG2 ILE A 48 7840 6991 6698 -496 384 88 C ATOM 363 CD1 ILE A 48 -15.379 21.915 11.765 1.00 55.21 C ANISOU 363 CD1 ILE A 48 7695 6693 6590 -310 504 -151 C ATOM 364 N MET A 49 -18.135 21.274 15.416 1.00 52.36 N ANISOU 364 N MET A 49 7283 6539 6071 -577 798 -204 N ATOM 365 CA MET A 49 -18.925 22.422 15.860 1.00 51.38 C ANISOU 365 CA MET A 49 7178 6417 5927 -565 934 -321 C ATOM 366 C MET A 49 -20.331 21.933 16.132 1.00 56.44 C ANISOU 366 C MET A 49 7727 7090 6626 -562 1008 -340 C ATOM 367 O MET A 49 -20.864 21.144 15.365 1.00 54.25 O ANISOU 367 O MET A 49 7365 6790 6459 -501 951 -299 O ATOM 368 CB MET A 49 -18.945 23.501 14.765 1.00 52.78 C ANISOU 368 CB MET A 49 7364 6505 6185 -430 935 -397 C ATOM 369 CG MET A 49 -19.400 24.892 15.223 1.00 56.00 C ANISOU 369 CG MET A 49 7824 6896 6558 -415 1068 -518 C ATOM 370 SD MET A 49 -18.163 25.812 16.174 1.00 59.25 S ANISOU 370 SD MET A 49 8387 7333 6793 -535 1099 -547 S ATOM 371 CE MET A 49 -16.907 26.087 14.987 1.00 53.72 C ANISOU 371 CE MET A 49 7726 6563 6120 -469 969 -508 C ATOM 372 N TYR A 50 -20.913 22.363 17.247 1.00 56.16 N ANISOU 372 N TYR A 50 7711 7113 6513 -638 1135 -401 N ATOM 373 CA TYR A 50 -22.263 21.981 17.627 1.00 57.22 C ANISOU 373 CA TYR A 50 7756 7292 6693 -645 1224 -426 C ATOM 374 C TYR A 50 -22.919 23.164 18.303 1.00 64.05 C ANISOU 374 C TYR A 50 8647 8170 7518 -643 1385 -549 C ATOM 375 O TYR A 50 -22.225 24.117 18.677 1.00 64.34 O ANISOU 375 O TYR A 50 8790 8191 7466 -670 1424 -603 O ATOM 376 CB TYR A 50 -22.241 20.745 18.552 1.00 58.44 C ANISOU 376 CB TYR A 50 7901 7532 6771 -788 1202 -333 C ATOM 377 CG TYR A 50 -21.560 20.980 19.885 1.00 60.48 C ANISOU 377 CG TYR A 50 8263 7861 6856 -938 1249 -330 C ATOM 378 CD1 TYR A 50 -20.178 20.871 20.013 1.00 62.05 C ANISOU 378 CD1 TYR A 50 8546 8061 6969 -997 1151 -260 C ATOM 379 CD2 TYR A 50 -22.302 21.270 21.028 1.00 61.99 C ANISOU 379 CD2 TYR A 50 8465 8126 6965 -1029 1391 -391 C ATOM 380 CE1 TYR A 50 -19.547 21.087 21.235 1.00 63.92 C ANISOU 380 CE1 TYR A 50 8877 8371 7040 -1145 1185 -250 C ATOM 381 CE2 TYR A 50 -21.683 21.464 22.261 1.00 63.14 C ANISOU 381 CE2 TYR A 50 8710 8341 6938 -1181 1431 -387 C ATOM 382 CZ TYR A 50 -20.304 21.381 22.357 1.00 70.06 C ANISOU 382 CZ TYR A 50 9672 9218 7729 -1241 1324 -315 C ATOM 383 OH TYR A 50 -19.690 21.555 23.571 1.00 72.37 O ANISOU 383 OH TYR A 50 10062 9588 7848 -1400 1354 -302 O ATOM 384 N GLU A 51 -24.251 23.097 18.478 1.00 61.80 N ANISOU 384 N GLU A 51 8268 7916 7298 -615 1484 -595 N ATOM 385 CA GLU A 51 -25.042 24.145 19.122 1.00 62.81 C ANISOU 385 CA GLU A 51 8403 8057 7405 -600 1655 -716 C ATOM 386 C GLU A 51 -24.763 25.515 18.477 1.00 65.61 C ANISOU 386 C GLU A 51 8816 8314 7800 -480 1679 -803 C ATOM 387 O GLU A 51 -24.631 26.536 19.165 1.00 63.75 O ANISOU 387 O GLU A 51 8670 8070 7481 -509 1790 -894 O ATOM 388 CB GLU A 51 -24.849 24.137 20.660 1.00 64.76 C ANISOU 388 CB GLU A 51 8731 8393 7480 -771 1751 -734 C ATOM 389 CG GLU A 51 -25.544 22.973 21.346 1.00 71.17 C ANISOU 389 CG GLU A 51 9469 9303 8271 -875 1771 -673 C ATOM 390 CD GLU A 51 -25.397 22.918 22.859 1.00 83.65 C ANISOU 390 CD GLU A 51 11128 10979 9676 -1052 1865 -685 C ATOM 391 OE1 GLU A 51 -25.341 23.992 23.498 1.00 87.57 O ANISOU 391 OE1 GLU A 51 11707 11476 10091 -1076 1987 -789 O ATOM 392 OE2 GLU A 51 -25.358 21.797 23.410 1.00 71.57 O ANISOU 392 OE2 GLU A 51 9583 9522 8089 -1172 1819 -591 O ATOM 393 N ASN A 52 -24.656 25.501 17.124 1.00 62.76 N ANISOU 393 N ASN A 52 8409 7875 7563 -351 1571 -772 N ATOM 394 CA ASN A 52 -24.385 26.651 16.240 1.00 63.12 C ANISOU 394 CA ASN A 52 8497 7817 7669 -224 1561 -831 C ATOM 395 C ASN A 52 -22.940 27.140 16.248 1.00 65.65 C ANISOU 395 C ASN A 52 8957 8101 7888 -274 1498 -821 C ATOM 396 O ASN A 52 -22.399 27.337 15.175 1.00 64.44 O ANISOU 396 O ASN A 52 8814 7876 7795 -191 1398 -796 O ATOM 397 CB ASN A 52 -25.330 27.859 16.496 1.00 65.85 C ANISOU 397 CB ASN A 52 8835 8130 8055 -142 1722 -955 C ATOM 398 CG ASN A 52 -26.797 27.547 16.599 1.00 80.84 C ANISOU 398 CG ASN A 52 10591 10076 10051 -93 1808 -978 C ATOM 399 OD1 ASN A 52 -27.504 28.102 17.438 1.00 80.99 O ANISOU 399 OD1 ASN A 52 10607 10124 10044 -105 1965 -1064 O ATOM 400 ND2 ASN A 52 -27.298 26.679 15.744 1.00 65.68 N ANISOU 400 ND2 ASN A 52 8549 8165 8244 -37 1714 -906 N ATOM 401 N ASN A 53 -22.337 27.392 17.435 1.00 62.39 N ANISOU 401 N ASN A 53 8650 7737 7318 -410 1559 -844 N ATOM 402 CA ASN A 53 -20.999 27.982 17.530 1.00 60.94 C ANISOU 402 CA ASN A 53 8599 7527 7029 -468 1510 -843 C ATOM 403 C ASN A 53 -20.047 27.408 18.609 1.00 62.95 C ANISOU 403 C ASN A 53 8929 7872 7118 -649 1477 -779 C ATOM 404 O ASN A 53 -19.049 28.068 18.945 1.00 62.32 O ANISOU 404 O ASN A 53 8965 7785 6928 -719 1469 -796 O ATOM 405 CB ASN A 53 -21.152 29.484 17.745 1.00 62.60 C ANISOU 405 CB ASN A 53 8899 7672 7214 -429 1634 -970 C ATOM 406 CG ASN A 53 -21.851 29.886 19.029 1.00 85.79 C ANISOU 406 CG ASN A 53 11868 10660 10068 -507 1806 -1059 C ATOM 407 OD1 ASN A 53 -22.300 29.055 19.831 1.00 84.27 O ANISOU 407 OD1 ASN A 53 11627 10562 9831 -598 1841 -1028 O ATOM 408 ND2 ASN A 53 -21.933 31.183 19.265 1.00 79.31 N ANISOU 408 ND2 ASN A 53 11138 9775 9220 -478 1920 -1174 N ATOM 409 N LYS A 54 -20.333 26.213 19.135 1.00 57.87 N ANISOU 409 N LYS A 54 8221 7311 6455 -728 1454 -702 N ATOM 410 CA LYS A 54 -19.469 25.586 20.139 1.00 58.31 C ANISOU 410 CA LYS A 54 8339 7455 6360 -897 1412 -625 C ATOM 411 C LYS A 54 -18.514 24.609 19.471 1.00 62.82 C ANISOU 411 C LYS A 54 8885 8022 6961 -893 1239 -495 C ATOM 412 O LYS A 54 -18.940 23.643 18.835 1.00 61.01 O ANISOU 412 O LYS A 54 8558 7782 6840 -831 1172 -430 O ATOM 413 CB LYS A 54 -20.266 24.883 21.268 1.00 61.26 C ANISOU 413 CB LYS A 54 8678 7926 6674 -1008 1494 -613 C ATOM 414 CG LYS A 54 -21.059 25.810 22.169 1.00 60.65 C ANISOU 414 CG LYS A 54 8641 7870 6532 -1046 1678 -741 C ATOM 415 CD LYS A 54 -21.774 25.020 23.249 1.00 70.72 C ANISOU 415 CD LYS A 54 9879 9250 7741 -1166 1750 -719 C ATOM 416 CE LYS A 54 -22.530 25.890 24.230 1.00 80.64 C ANISOU 416 CE LYS A 54 11181 10538 8922 -1215 1944 -849 C ATOM 417 NZ LYS A 54 -23.849 26.337 23.702 1.00 88.35 N ANISOU 417 NZ LYS A 54 12056 11468 10046 -1066 2053 -940 N ATOM 418 N ARG A 55 -17.219 24.871 19.628 1.00 62.00 N ANISOU 418 N ARG A 55 8869 7928 6759 -960 1170 -458 N ATOM 419 CA ARG A 55 -16.137 24.066 19.080 1.00 61.84 C ANISOU 419 CA ARG A 55 8834 7908 6753 -961 1013 -337 C ATOM 420 C ARG A 55 -15.996 22.766 19.846 1.00 69.44 C ANISOU 420 C ARG A 55 9768 8955 7661 -1072 961 -222 C ATOM 421 O ARG A 55 -16.113 22.760 21.077 1.00 70.42 O ANISOU 421 O ARG A 55 9937 9159 7661 -1207 1028 -226 O ATOM 422 CB ARG A 55 -14.808 24.846 19.149 1.00 59.51 C ANISOU 422 CB ARG A 55 8641 7612 6358 -1012 969 -338 C ATOM 423 CG ARG A 55 -14.664 25.930 18.084 1.00 62.53 C ANISOU 423 CG ARG A 55 9050 7897 6813 -890 973 -417 C ATOM 424 CD ARG A 55 -13.442 26.802 18.303 1.00 72.65 C ANISOU 424 CD ARG A 55 10441 9185 7978 -964 949 -429 C ATOM 425 NE ARG A 55 -13.679 27.822 19.330 1.00 82.17 N ANISOU 425 NE ARG A 55 11747 10410 9063 -1057 1078 -531 N ATOM 426 CZ ARG A 55 -14.182 29.032 19.097 1.00 97.33 C ANISOU 426 CZ ARG A 55 13720 12252 11008 -992 1179 -656 C ATOM 427 NH1 ARG A 55 -14.377 29.878 20.097 1.00 95.86 N ANISOU 427 NH1 ARG A 55 13632 12083 10707 -1085 1303 -749 N ATOM 428 NH2 ARG A 55 -14.501 29.402 17.862 1.00 78.33 N ANISOU 428 NH2 ARG A 55 11273 9747 8742 -833 1159 -687 N ATOM 429 N SER A 56 -15.714 21.662 19.130 1.00 66.58 N ANISOU 429 N SER A 56 9338 8573 7387 -1021 841 -117 N ATOM 430 CA SER A 56 -15.446 20.401 19.812 1.00 67.63 C ANISOU 430 CA SER A 56 9452 8773 7472 -1122 777 7 C ATOM 431 C SER A 56 -13.977 20.464 20.324 1.00 73.15 C ANISOU 431 C SER A 56 10224 9523 8048 -1220 696 83 C ATOM 432 O SER A 56 -13.193 21.291 19.829 1.00 70.37 O ANISOU 432 O SER A 56 9915 9138 7685 -1181 670 50 O ATOM 433 CB SER A 56 -15.671 19.212 18.881 1.00 70.28 C ANISOU 433 CB SER A 56 9699 9060 7947 -1033 684 87 C ATOM 434 OG SER A 56 -17.047 19.101 18.556 1.00 77.15 O ANISOU 434 OG SER A 56 10498 9903 8914 -969 755 26 O ATOM 435 N SER A 57 -13.622 19.639 21.345 1.00 71.78 N ANISOU 435 N SER A 57 10064 9433 7776 -1354 659 186 N ATOM 436 CA SER A 57 -12.271 19.624 21.913 1.00 71.72 C ANISOU 436 CA SER A 57 10114 9488 7649 -1456 577 273 C ATOM 437 C SER A 57 -11.193 19.402 20.856 1.00 71.32 C ANISOU 437 C SER A 57 10035 9386 7678 -1359 452 340 C ATOM 438 O SER A 57 -11.372 18.592 19.942 1.00 70.31 O ANISOU 438 O SER A 57 9836 9194 7685 -1249 392 384 O ATOM 439 CB SER A 57 -12.155 18.589 23.027 1.00 77.26 C ANISOU 439 CB SER A 57 10818 10278 8258 -1596 541 393 C ATOM 440 OG SER A 57 -12.504 19.189 24.263 1.00 92.67 O ANISOU 440 OG SER A 57 12840 12309 10059 -1739 647 333 O ATOM 441 N GLY A 58 -10.107 20.152 20.980 1.00 66.93 N ANISOU 441 N GLY A 58 9537 8859 7033 -1405 419 341 N ATOM 442 CA GLY A 58 -8.981 20.079 20.058 1.00 66.29 C ANISOU 442 CA GLY A 58 9433 8745 7009 -1327 309 399 C ATOM 443 C GLY A 58 -9.112 20.937 18.813 1.00 69.51 C ANISOU 443 C GLY A 58 9838 9059 7515 -1189 332 295 C ATOM 444 O GLY A 58 -8.103 21.185 18.147 1.00 71.09 O ANISOU 444 O GLY A 58 10039 9243 7731 -1147 260 322 O ATOM 445 N ILE A 59 -10.348 21.407 18.491 1.00 62.98 N ANISOU 445 N ILE A 59 9004 8172 6755 -1119 432 181 N ATOM 446 CA ILE A 59 -10.628 22.261 17.327 1.00 61.37 C ANISOU 446 CA ILE A 59 8798 7874 6647 -986 460 81 C ATOM 447 C ILE A 59 -10.115 23.681 17.591 1.00 63.69 C ANISOU 447 C ILE A 59 9187 8174 6840 -1037 512 -4 C ATOM 448 O ILE A 59 -10.572 24.296 18.549 1.00 63.39 O ANISOU 448 O ILE A 59 9210 8172 6705 -1127 610 -72 O ATOM 449 CB ILE A 59 -12.130 22.183 16.907 1.00 63.54 C ANISOU 449 CB ILE A 59 9019 8090 7034 -893 539 6 C ATOM 450 CG1 ILE A 59 -12.489 20.782 16.393 1.00 63.47 C ANISOU 450 CG1 ILE A 59 8919 8060 7136 -835 469 93 C ATOM 451 CG2 ILE A 59 -12.563 23.275 15.943 1.00 63.05 C ANISOU 451 CG2 ILE A 59 8966 7939 7048 -775 588 -108 C ATOM 452 CD1 ILE A 59 -11.565 20.191 15.311 1.00 69.03 C ANISOU 452 CD1 ILE A 59 9589 8719 7920 -753 346 171 C ATOM 453 N PRO A 60 -9.146 24.199 16.783 1.00 59.36 N ANISOU 453 N PRO A 60 8658 7592 6305 -990 448 -1 N ATOM 454 CA PRO A 60 -8.612 25.553 17.046 1.00 59.37 C ANISOU 454 CA PRO A 60 8759 7596 6203 -1051 494 -79 C ATOM 455 C PRO A 60 -9.653 26.676 16.951 1.00 62.72 C ANISOU 455 C PRO A 60 9233 7949 6649 -1001 622 -225 C ATOM 456 O PRO A 60 -10.654 26.534 16.229 1.00 60.41 O ANISOU 456 O PRO A 60 8882 7586 6486 -877 653 -266 O ATOM 457 CB PRO A 60 -7.505 25.714 15.998 1.00 60.05 C ANISOU 457 CB PRO A 60 8835 7653 6330 -989 396 -39 C ATOM 458 CG PRO A 60 -7.814 24.729 14.929 1.00 62.87 C ANISOU 458 CG PRO A 60 9093 7954 6841 -854 334 11 C ATOM 459 CD PRO A 60 -8.465 23.571 15.630 1.00 59.48 C ANISOU 459 CD PRO A 60 8609 7568 6422 -889 337 73 C ATOM 460 N ASP A 61 -9.385 27.805 17.658 1.00 59.30 N ANISOU 460 N ASP A 61 8910 7532 6091 -1099 694 -302 N ATOM 461 CA ASP A 61 -10.249 28.986 17.730 1.00 60.43 C ANISOU 461 CA ASP A 61 9119 7604 6236 -1066 826 -444 C ATOM 462 C ASP A 61 -10.451 29.665 16.371 1.00 61.82 C ANISOU 462 C ASP A 61 9287 7664 6539 -909 819 -502 C ATOM 463 O ASP A 61 -11.391 30.448 16.220 1.00 61.36 O ANISOU 463 O ASP A 61 9253 7532 6531 -837 921 -608 O ATOM 464 CB ASP A 61 -9.781 29.995 18.821 1.00 64.67 C ANISOU 464 CB ASP A 61 9791 8183 6598 -1221 898 -508 C ATOM 465 CG ASP A 61 -8.328 30.483 18.764 1.00 85.76 C ANISOU 465 CG ASP A 61 12531 10886 9169 -1309 817 -469 C ATOM 466 OD1 ASP A 61 -7.665 30.290 17.709 1.00 88.08 O ANISOU 466 OD1 ASP A 61 12777 11149 9540 -1227 715 -412 O ATOM 467 OD2 ASP A 61 -7.856 31.069 19.771 1.00 94.18 O ANISOU 467 OD2 ASP A 61 13699 12009 10076 -1464 857 -497 O ATOM 468 N ARG A 62 -9.610 29.303 15.374 1.00 57.31 N ANISOU 468 N ARG A 62 8674 7077 6024 -852 700 -428 N ATOM 469 CA ARG A 62 -9.668 29.749 13.974 1.00 56.36 C ANISOU 469 CA ARG A 62 8536 6857 6023 -709 668 -458 C ATOM 470 C ARG A 62 -10.979 29.310 13.325 1.00 57.76 C ANISOU 470 C ARG A 62 8623 6973 6349 -571 697 -482 C ATOM 471 O ARG A 62 -11.381 29.895 12.321 1.00 57.16 O ANISOU 471 O ARG A 62 8544 6808 6368 -454 703 -532 O ATOM 472 CB ARG A 62 -8.545 29.095 13.143 1.00 57.35 C ANISOU 472 CB ARG A 62 8613 7000 6177 -686 533 -355 C ATOM 473 CG ARG A 62 -7.128 29.459 13.525 1.00 62.71 C ANISOU 473 CG ARG A 62 9355 7743 6729 -806 480 -313 C ATOM 474 CD ARG A 62 -6.185 28.986 12.442 1.00 55.23 C ANISOU 474 CD ARG A 62 8352 6792 5842 -745 364 -234 C ATOM 475 NE ARG A 62 -5.959 27.540 12.458 1.00 58.59 N ANISOU 475 NE ARG A 62 8678 7273 6312 -733 285 -120 N ATOM 476 CZ ARG A 62 -6.379 26.690 11.523 1.00 63.84 C ANISOU 476 CZ ARG A 62 9256 7889 7110 -612 242 -88 C ATOM 477 NH1 ARG A 62 -7.096 27.124 10.491 1.00 47.59 N ANISOU 477 NH1 ARG A 62 7193 5736 5153 -493 268 -158 N ATOM 478 NH2 ARG A 62 -6.082 25.405 11.609 1.00 51.75 N ANISOU 478 NH2 ARG A 62 7649 6402 5610 -612 173 15 N ATOM 479 N PHE A 63 -11.597 28.230 13.853 1.00 53.16 N ANISOU 479 N PHE A 63 7966 6445 5787 -591 702 -434 N ATOM 480 CA PHE A 63 -12.851 27.674 13.348 1.00 51.86 C ANISOU 480 CA PHE A 63 7707 6243 5756 -482 725 -446 C ATOM 481 C PHE A 63 -13.980 28.278 14.141 1.00 58.09 C ANISOU 481 C PHE A 63 8516 7029 6527 -495 864 -541 C ATOM 482 O PHE A 63 -13.958 28.240 15.367 1.00 58.89 O ANISOU 482 O PHE A 63 8659 7201 6517 -616 923 -548 O ATOM 483 CB PHE A 63 -12.867 26.130 13.467 1.00 52.72 C ANISOU 483 CB PHE A 63 7726 6409 5895 -504 651 -338 C ATOM 484 CG PHE A 63 -12.010 25.375 12.473 1.00 53.02 C ANISOU 484 CG PHE A 63 7721 6431 5992 -452 522 -248 C ATOM 485 CD1 PHE A 63 -10.621 25.329 12.615 1.00 54.64 C ANISOU 485 CD1 PHE A 63 7966 6679 6116 -522 448 -184 C ATOM 486 CD2 PHE A 63 -12.589 24.680 11.414 1.00 52.02 C ANISOU 486 CD2 PHE A 63 7511 6253 6002 -339 476 -227 C ATOM 487 CE1 PHE A 63 -9.828 24.633 11.696 1.00 53.75 C ANISOU 487 CE1 PHE A 63 7809 6551 6062 -468 340 -106 C ATOM 488 CE2 PHE A 63 -11.790 23.982 10.494 1.00 54.34 C ANISOU 488 CE2 PHE A 63 7772 6527 6346 -293 367 -153 C ATOM 489 CZ PHE A 63 -10.415 23.955 10.647 1.00 51.97 C ANISOU 489 CZ PHE A 63 7510 6267 5970 -353 303 -94 C ATOM 490 N SER A 64 -14.940 28.902 13.457 1.00 56.61 N ANISOU 490 N SER A 64 8304 6761 6446 -371 920 -618 N ATOM 491 CA SER A 64 -16.065 29.507 14.155 1.00 57.48 C ANISOU 491 CA SER A 64 8422 6862 6555 -365 1062 -713 C ATOM 492 C SER A 64 -17.384 29.305 13.400 1.00 61.86 C ANISOU 492 C SER A 64 8867 7371 7267 -225 1086 -736 C ATOM 493 O SER A 64 -17.428 29.325 12.174 1.00 60.12 O ANISOU 493 O SER A 64 8605 7086 7153 -112 1015 -719 O ATOM 494 CB SER A 64 -15.797 30.968 14.529 1.00 60.64 C ANISOU 494 CB SER A 64 8949 7213 6877 -391 1151 -814 C ATOM 495 OG SER A 64 -15.815 31.877 13.446 1.00 66.10 O ANISOU 495 OG SER A 64 9664 7798 7653 -269 1139 -859 O ATOM 496 N GLY A 65 -18.423 28.996 14.166 1.00 60.33 N ANISOU 496 N GLY A 65 8620 7224 7080 -247 1180 -763 N ATOM 497 CA GLY A 65 -19.756 28.755 13.646 1.00 60.09 C ANISOU 497 CA GLY A 65 8473 7172 7188 -134 1214 -782 C ATOM 498 C GLY A 65 -20.669 29.910 13.973 1.00 66.17 C ANISOU 498 C GLY A 65 9261 7898 7982 -75 1360 -898 C ATOM 499 O GLY A 65 -20.493 30.578 14.995 1.00 65.72 O ANISOU 499 O GLY A 65 9298 7858 7816 -158 1462 -964 O ATOM 500 N SER A 66 -21.608 30.191 13.073 1.00 64.14 N ANISOU 500 N SER A 66 8921 7580 7868 71 1369 -924 N ATOM 501 CA SER A 66 -22.621 31.227 13.257 1.00 65.44 C ANISOU 501 CA SER A 66 9078 7696 8089 157 1506 -1027 C ATOM 502 C SER A 66 -23.868 30.864 12.482 1.00 70.45 C ANISOU 502 C SER A 66 9559 8324 8884 284 1498 -1012 C ATOM 503 O SER A 66 -23.848 29.973 11.631 1.00 68.71 O ANISOU 503 O SER A 66 9260 8115 8731 313 1376 -929 O ATOM 504 CB SER A 66 -22.103 32.627 12.920 1.00 69.34 C ANISOU 504 CB SER A 66 9693 8085 8569 211 1534 -1097 C ATOM 505 OG SER A 66 -21.781 32.802 11.551 1.00 81.03 O ANISOU 505 OG SER A 66 11162 9489 10138 315 1418 -1057 O ATOM 506 N LYS A 67 -24.969 31.496 12.848 1.00 70.69 N ANISOU 506 N LYS A 67 9546 8343 8971 351 1633 -1091 N ATOM 507 CA LYS A 67 -26.285 31.272 12.282 1.00 71.73 C ANISOU 507 CA LYS A 67 9521 8481 9252 469 1649 -1086 C ATOM 508 C LYS A 67 -27.032 32.619 12.252 1.00 77.02 C ANISOU 508 C LYS A 67 10198 9070 9996 596 1775 -1186 C ATOM 509 O LYS A 67 -26.997 33.376 13.230 1.00 76.31 O ANISOU 509 O LYS A 67 10197 8968 9827 555 1911 -1274 O ATOM 510 CB LYS A 67 -27.019 30.236 13.154 1.00 75.12 C ANISOU 510 CB LYS A 67 9853 9029 9661 381 1704 -1065 C ATOM 511 CG LYS A 67 -28.230 29.605 12.509 1.00 86.55 C ANISOU 511 CG LYS A 67 11124 10511 11252 465 1679 -1026 C ATOM 512 CD LYS A 67 -28.811 28.516 13.387 0.50 93.94 C ANISOU 512 CD LYS A 67 11977 11565 12150 356 1723 -997 C ATOM 513 CE LYS A 67 -29.651 29.013 14.539 0.50 99.31 C ANISOU 513 CE LYS A 67 12637 12294 12802 336 1911 -1086 C ATOM 514 NZ LYS A 67 -30.368 27.896 15.199 0.50104.14 N ANISOU 514 NZ LYS A 67 13145 13024 13400 240 1943 -1047 N ATOM 515 N SER A 68 -27.653 32.925 11.102 1.00 74.86 N ANISOU 515 N SER A 68 9839 8736 9870 747 1724 -1169 N ATOM 516 CA SER A 68 -28.429 34.147 10.856 1.00 76.26 C ANISOU 516 CA SER A 68 10002 8825 10147 895 1822 -1244 C ATOM 517 C SER A 68 -29.659 33.743 10.051 1.00 80.56 C ANISOU 517 C SER A 68 10358 9395 10855 1016 1786 -1199 C ATOM 518 O SER A 68 -29.533 33.289 8.910 1.00 80.90 O ANISOU 518 O SER A 68 10350 9424 10963 1059 1638 -1120 O ATOM 519 CB SER A 68 -27.590 35.180 10.101 1.00 79.60 C ANISOU 519 CB SER A 68 10556 9121 10567 956 1766 -1259 C ATOM 520 OG SER A 68 -28.372 36.268 9.633 1.00 91.19 O ANISOU 520 OG SER A 68 11998 10493 12156 1118 1831 -1309 O ATOM 521 N GLY A 69 -30.823 33.844 10.678 1.00 76.68 N ANISOU 521 N GLY A 69 9762 8952 10421 1056 1920 -1248 N ATOM 522 CA GLY A 69 -32.081 33.448 10.069 1.00 76.37 C ANISOU 522 CA GLY A 69 9527 8957 10533 1158 1901 -1207 C ATOM 523 C GLY A 69 -32.135 31.953 9.823 1.00 78.18 C ANISOU 523 C GLY A 69 9659 9291 10754 1064 1784 -1112 C ATOM 524 O GLY A 69 -32.039 31.151 10.760 1.00 77.68 O ANISOU 524 O GLY A 69 9596 9319 10598 930 1825 -1107 O ATOM 525 N ASN A 70 -32.244 31.582 8.542 1.00 72.33 N ANISOU 525 N ASN A 70 8846 8531 10105 1130 1634 -1033 N ATOM 526 CA ASN A 70 -32.347 30.208 8.070 1.00 69.96 C ANISOU 526 CA ASN A 70 8455 8309 9818 1060 1509 -941 C ATOM 527 C ASN A 70 -31.061 29.708 7.432 1.00 72.00 C ANISOU 527 C ASN A 70 8824 8530 10004 993 1358 -880 C ATOM 528 O ASN A 70 -31.074 28.651 6.804 1.00 71.21 O ANISOU 528 O ASN A 70 8661 8468 9926 955 1239 -803 O ATOM 529 CB ASN A 70 -33.509 30.076 7.089 1.00 68.53 C ANISOU 529 CB ASN A 70 8099 8146 9793 1174 1455 -896 C ATOM 530 CG ASN A 70 -34.850 30.396 7.686 1.00 84.62 C ANISOU 530 CG ASN A 70 9996 10242 11913 1237 1598 -942 C ATOM 531 OD1 ASN A 70 -35.163 30.018 8.812 1.00 80.51 O ANISOU 531 OD1 ASN A 70 9453 9803 11335 1149 1711 -977 O ATOM 532 ND2 ASN A 70 -35.658 31.129 6.950 1.00 76.99 N ANISOU 532 ND2 ASN A 70 8933 9237 11084 1392 1598 -943 N ATOM 533 N SER A 71 -29.947 30.428 7.626 1.00 67.08 N ANISOU 533 N SER A 71 8364 7834 9291 972 1365 -916 N ATOM 534 CA SER A 71 -28.648 30.031 7.090 1.00 64.70 C ANISOU 534 CA SER A 71 8169 7500 8915 909 1234 -864 C ATOM 535 C SER A 71 -27.592 29.995 8.191 1.00 67.17 C ANISOU 535 C SER A 71 8618 7832 9074 778 1283 -890 C ATOM 536 O SER A 71 -27.637 30.810 9.114 1.00 69.39 O ANISOU 536 O SER A 71 8961 8101 9302 766 1413 -968 O ATOM 537 CB SER A 71 -28.222 30.924 5.927 1.00 67.35 C ANISOU 537 CB SER A 71 8563 7726 9301 1017 1157 -862 C ATOM 538 OG SER A 71 -28.435 32.295 6.225 1.00 81.56 O ANISOU 538 OG SER A 71 10421 9452 11116 1098 1267 -942 O ATOM 539 N ALA A 72 -26.686 29.004 8.118 1.00 59.14 N ANISOU 539 N ALA A 72 7640 6847 7984 676 1180 -822 N ATOM 540 CA ALA A 72 -25.590 28.800 9.066 1.00 56.81 C ANISOU 540 CA ALA A 72 7461 6581 7541 543 1195 -821 C ATOM 541 C ALA A 72 -24.254 28.904 8.327 1.00 57.16 C ANISOU 541 C ALA A 72 7609 6568 7541 534 1078 -784 C ATOM 542 O ALA A 72 -24.213 28.687 7.128 1.00 55.57 O ANISOU 542 O ALA A 72 7372 6327 7416 603 971 -740 O ATOM 543 CB ALA A 72 -25.720 27.431 9.727 1.00 56.81 C ANISOU 543 CB ALA A 72 7406 6682 7499 427 1180 -763 C ATOM 544 N THR A 73 -23.174 29.279 9.014 1.00 52.97 N ANISOU 544 N THR A 73 7205 6034 6885 447 1099 -802 N ATOM 545 CA THR A 73 -21.871 29.402 8.363 1.00 51.99 C ANISOU 545 CA THR A 73 7173 5866 6715 431 994 -767 C ATOM 546 C THR A 73 -20.763 28.891 9.244 1.00 56.37 C ANISOU 546 C THR A 73 7805 6481 7133 289 977 -732 C ATOM 547 O THR A 73 -20.767 29.126 10.450 1.00 58.33 O ANISOU 547 O THR A 73 8099 6773 7291 204 1074 -772 O ATOM 548 CB THR A 73 -21.505 30.869 7.939 1.00 59.76 C ANISOU 548 CB THR A 73 8256 6753 7698 501 1021 -830 C ATOM 549 OG1 THR A 73 -21.344 31.660 9.103 1.00 71.32 O ANISOU 549 OG1 THR A 73 9813 8220 9066 437 1142 -904 O ATOM 550 CG2 THR A 73 -22.506 31.510 6.995 1.00 54.06 C ANISOU 550 CG2 THR A 73 7468 5959 7113 652 1028 -857 C ATOM 551 N LEU A 74 -19.781 28.265 8.623 1.00 51.47 N ANISOU 551 N LEU A 74 7202 5858 6495 265 856 -660 N ATOM 552 CA LEU A 74 -18.564 27.837 9.277 1.00 51.12 C ANISOU 552 CA LEU A 74 7229 5864 6330 145 818 -614 C ATOM 553 C LEU A 74 -17.487 28.692 8.642 1.00 54.86 C ANISOU 553 C LEU A 74 7797 6278 6771 164 768 -625 C ATOM 554 O LEU A 74 -17.342 28.700 7.421 1.00 54.17 O ANISOU 554 O LEU A 74 7689 6136 6757 247 688 -603 O ATOM 555 CB LEU A 74 -18.273 26.338 9.038 1.00 49.97 C ANISOU 555 CB LEU A 74 7019 5766 6203 107 717 -514 C ATOM 556 CG LEU A 74 -16.971 25.774 9.681 1.00 52.28 C ANISOU 556 CG LEU A 74 7371 6113 6381 -10 664 -448 C ATOM 557 CD1 LEU A 74 -17.100 25.671 11.200 1.00 52.76 C ANISOU 557 CD1 LEU A 74 7458 6252 6336 -131 749 -456 C ATOM 558 CD2 LEU A 74 -16.632 24.414 9.101 1.00 48.90 C ANISOU 558 CD2 LEU A 74 6883 5697 5998 -8 553 -352 C ATOM 559 N THR A 75 -16.775 29.443 9.462 1.00 51.95 N ANISOU 559 N THR A 75 7533 5919 6285 82 820 -662 N ATOM 560 CA THR A 75 -15.697 30.321 9.018 1.00 51.47 C ANISOU 560 CA THR A 75 7573 5810 6173 76 783 -675 C ATOM 561 C THR A 75 -14.376 29.748 9.505 1.00 54.04 C ANISOU 561 C THR A 75 7939 6206 6386 -45 716 -606 C ATOM 562 O THR A 75 -14.296 29.270 10.641 1.00 51.43 O ANISOU 562 O THR A 75 7614 5954 5974 -150 750 -587 O ATOM 563 CB THR A 75 -15.929 31.762 9.546 1.00 62.28 C ANISOU 563 CB THR A 75 9040 7126 7496 75 898 -779 C ATOM 564 OG1 THR A 75 -17.261 32.155 9.226 1.00 61.33 O ANISOU 564 OG1 THR A 75 8861 6953 7489 192 967 -834 O ATOM 565 CG2 THR A 75 -14.918 32.782 8.981 1.00 58.40 C ANISOU 565 CG2 THR A 75 8658 6571 6962 76 863 -799 C ATOM 566 N ILE A 76 -13.335 29.794 8.629 1.00 52.13 N ANISOU 566 N ILE A 76 7723 5941 6143 -31 620 -564 N ATOM 567 CA ILE A 76 -11.989 29.306 8.961 1.00 50.59 C ANISOU 567 CA ILE A 76 7557 5813 5852 -132 549 -492 C ATOM 568 C ILE A 76 -11.017 30.402 8.563 1.00 53.59 C ANISOU 568 C ILE A 76 8033 6154 6174 -149 532 -520 C ATOM 569 O ILE A 76 -10.942 30.742 7.396 1.00 53.39 O ANISOU 569 O ILE A 76 8006 6061 6218 -60 488 -527 O ATOM 570 CB ILE A 76 -11.622 27.930 8.286 1.00 51.25 C ANISOU 570 CB ILE A 76 7551 5923 5998 -103 439 -392 C ATOM 571 CG1 ILE A 76 -12.786 26.894 8.369 1.00 50.72 C ANISOU 571 CG1 ILE A 76 7386 5868 6017 -64 451 -371 C ATOM 572 CG2 ILE A 76 -10.297 27.383 8.873 1.00 49.58 C ANISOU 572 CG2 ILE A 76 7360 5793 5687 -212 378 -311 C ATOM 573 CD1 ILE A 76 -12.695 25.500 7.360 1.00 49.52 C ANISOU 573 CD1 ILE A 76 7144 5709 5963 -3 343 -285 C ATOM 574 N THR A 77 -10.284 30.948 9.529 1.00 51.94 N ANISOU 574 N THR A 77 7910 5990 5833 -270 565 -535 N ATOM 575 CA THR A 77 -9.252 31.975 9.328 1.00 51.65 C ANISOU 575 CA THR A 77 7975 5932 5720 -317 550 -558 C ATOM 576 C THR A 77 -7.877 31.289 9.464 1.00 54.98 C ANISOU 576 C THR A 77 8381 6443 6067 -408 453 -461 C ATOM 577 O THR A 77 -7.823 30.139 9.909 1.00 54.87 O ANISOU 577 O THR A 77 8294 6500 6053 -438 417 -387 O ATOM 578 CB THR A 77 -9.413 33.130 10.340 1.00 60.70 C ANISOU 578 CB THR A 77 9237 7064 6764 -400 660 -649 C ATOM 579 OG1 THR A 77 -9.174 32.646 11.656 1.00 59.95 O ANISOU 579 OG1 THR A 77 9150 7070 6560 -532 684 -622 O ATOM 580 CG2 THR A 77 -10.773 33.813 10.256 1.00 59.39 C ANISOU 580 CG2 THR A 77 9081 6808 6678 -301 764 -745 C ATOM 581 N GLY A 78 -6.806 31.955 9.027 1.00 49.87 N ANISOU 581 N GLY A 78 7794 5788 5366 -443 411 -456 N ATOM 582 CA GLY A 78 -5.455 31.405 9.082 1.00 49.82 C ANISOU 582 CA GLY A 78 7765 5869 5295 -521 320 -364 C ATOM 583 C GLY A 78 -5.407 30.032 8.429 1.00 54.95 C ANISOU 583 C GLY A 78 8295 6540 6043 -443 239 -276 C ATOM 584 O GLY A 78 -4.852 29.092 8.999 1.00 55.32 O ANISOU 584 O GLY A 78 8291 6672 6054 -503 191 -191 O ATOM 585 N LEU A 79 -6.064 29.894 7.252 1.00 50.54 N ANISOU 585 N LEU A 79 7694 5900 5610 -309 225 -296 N ATOM 586 CA LEU A 79 -6.208 28.620 6.542 1.00 48.65 C ANISOU 586 CA LEU A 79 7351 5661 5472 -228 159 -229 C ATOM 587 C LEU A 79 -4.875 27.908 6.345 1.00 50.47 C ANISOU 587 C LEU A 79 7543 5958 5675 -264 72 -135 C ATOM 588 O LEU A 79 -3.888 28.523 5.947 1.00 51.54 O ANISOU 588 O LEU A 79 7717 6103 5763 -292 42 -132 O ATOM 589 CB LEU A 79 -6.939 28.862 5.215 1.00 48.81 C ANISOU 589 CB LEU A 79 7355 5584 5608 -97 154 -274 C ATOM 590 CG LEU A 79 -7.537 27.669 4.496 1.00 53.56 C ANISOU 590 CG LEU A 79 7861 6165 6325 -7 111 -234 C ATOM 591 CD1 LEU A 79 -8.807 27.115 5.218 1.00 53.23 C ANISOU 591 CD1 LEU A 79 7773 6129 6322 0 164 -246 C ATOM 592 CD2 LEU A 79 -7.811 28.010 3.053 1.00 56.38 C ANISOU 592 CD2 LEU A 79 8215 6440 6767 98 82 -264 C ATOM 593 N GLN A 80 -4.819 26.653 6.743 1.00 46.87 N ANISOU 593 N GLN A 80 7014 5552 5241 -273 36 -57 N ATOM 594 CA GLN A 80 -3.621 25.827 6.626 1.00 47.37 C ANISOU 594 CA GLN A 80 7027 5678 5293 -293 -45 41 C ATOM 595 C GLN A 80 -3.944 24.476 5.988 1.00 53.57 C ANISOU 595 C GLN A 80 7727 6436 6194 -202 -89 95 C ATOM 596 O GLN A 80 -5.098 24.056 5.991 1.00 52.15 O ANISOU 596 O GLN A 80 7523 6214 6079 -157 -59 69 O ATOM 597 CB GLN A 80 -2.879 25.651 7.954 1.00 48.69 C ANISOU 597 CB GLN A 80 7202 5951 5346 -424 -56 105 C ATOM 598 CG GLN A 80 -3.711 25.878 9.179 1.00 51.19 C ANISOU 598 CG GLN A 80 7560 6290 5600 -500 15 69 C ATOM 599 CD GLN A 80 -2.861 26.172 10.379 1.00 54.32 C ANISOU 599 CD GLN A 80 7997 6788 5853 -649 9 109 C ATOM 600 OE1 GLN A 80 -2.212 25.307 10.930 1.00 53.54 O ANISOU 600 OE1 GLN A 80 7850 6767 5725 -700 -48 210 O ATOM 601 NE2 GLN A 80 -2.903 27.380 10.848 1.00 56.24 N ANISOU 601 NE2 GLN A 80 8333 7030 6004 -723 70 31 N ATOM 602 N THR A 81 -2.919 23.816 5.436 1.00 52.94 N ANISOU 602 N THR A 81 7600 6378 6137 -178 -157 166 N ATOM 603 CA THR A 81 -3.018 22.549 4.701 1.00 53.34 C ANISOU 603 CA THR A 81 7579 6394 6295 -90 -202 216 C ATOM 604 C THR A 81 -3.934 21.497 5.399 1.00 56.13 C ANISOU 604 C THR A 81 7895 6746 6688 -94 -190 250 C ATOM 605 O THR A 81 -4.831 20.956 4.750 1.00 55.19 O ANISOU 605 O THR A 81 7750 6559 6662 -18 -186 227 O ATOM 606 CB THR A 81 -1.624 22.003 4.367 1.00 63.45 C ANISOU 606 CB THR A 81 8816 7720 7573 -85 -266 299 C ATOM 607 OG1 THR A 81 -0.849 21.842 5.554 1.00 78.23 O ANISOU 607 OG1 THR A 81 10678 9689 9357 -185 -286 375 O ATOM 608 CG2 THR A 81 -0.897 22.873 3.430 1.00 53.10 C ANISOU 608 CG2 THR A 81 7531 6398 6246 -65 -276 261 C ATOM 609 N GLY A 82 -3.765 21.327 6.702 1.00 51.78 N ANISOU 609 N GLY A 82 7349 6268 6058 -190 -183 299 N ATOM 610 CA GLY A 82 -4.547 20.411 7.531 1.00 51.06 C ANISOU 610 CA GLY A 82 7230 6188 5981 -218 -170 338 C ATOM 611 C GLY A 82 -6.034 20.693 7.655 1.00 52.43 C ANISOU 611 C GLY A 82 7418 6317 6185 -203 -100 257 C ATOM 612 O GLY A 82 -6.737 19.908 8.289 1.00 52.07 O ANISOU 612 O GLY A 82 7347 6282 6154 -228 -86 287 O ATOM 613 N ASP A 83 -6.531 21.833 7.107 1.00 46.56 N ANISOU 613 N ASP A 83 6716 5527 5448 -166 -53 156 N ATOM 614 CA ASP A 83 -7.957 22.187 7.139 1.00 45.56 C ANISOU 614 CA ASP A 83 6593 5357 5361 -137 16 77 C ATOM 615 C ASP A 83 -8.652 21.618 5.899 1.00 48.18 C ANISOU 615 C ASP A 83 6876 5612 5820 -26 -10 63 C ATOM 616 O ASP A 83 -9.876 21.659 5.815 1.00 45.59 O ANISOU 616 O ASP A 83 6528 5251 5544 8 33 15 O ATOM 617 CB ASP A 83 -8.153 23.716 7.148 1.00 47.78 C ANISOU 617 CB ASP A 83 6943 5619 5593 -144 79 -19 C ATOM 618 CG ASP A 83 -7.504 24.507 8.268 1.00 49.82 C ANISOU 618 CG ASP A 83 7269 5943 5718 -260 113 -27 C ATOM 619 OD1 ASP A 83 -7.198 23.915 9.316 1.00 49.64 O ANISOU 619 OD1 ASP A 83 7238 5993 5629 -350 106 35 O ATOM 620 OD2 ASP A 83 -7.299 25.716 8.085 1.00 47.04 O ANISOU 620 OD2 ASP A 83 6983 5566 5324 -265 144 -93 O ATOM 621 N GLU A 84 -7.860 21.158 4.906 1.00 47.01 N ANISOU 621 N GLU A 84 6709 5437 5715 29 -77 101 N ATOM 622 CA GLU A 84 -8.331 20.559 3.650 1.00 47.41 C ANISOU 622 CA GLU A 84 6722 5416 5875 124 -111 92 C ATOM 623 C GLU A 84 -9.102 19.306 3.963 1.00 50.42 C ANISOU 623 C GLU A 84 7054 5792 6313 122 -116 134 C ATOM 624 O GLU A 84 -8.573 18.372 4.570 1.00 51.17 O ANISOU 624 O GLU A 84 7130 5920 6391 81 -145 213 O ATOM 625 CB GLU A 84 -7.175 20.256 2.718 1.00 48.93 C ANISOU 625 CB GLU A 84 6912 5595 6087 165 -173 128 C ATOM 626 CG GLU A 84 -6.760 21.490 1.968 1.00 60.20 C ANISOU 626 CG GLU A 84 8385 7001 7489 191 -168 69 C ATOM 627 CD GLU A 84 -5.634 21.315 0.974 1.00 76.91 C ANISOU 627 CD GLU A 84 10497 9107 9618 229 -220 95 C ATOM 628 OE1 GLU A 84 -4.590 20.739 1.360 1.00 76.75 O ANISOU 628 OE1 GLU A 84 10456 9136 9570 199 -251 166 O ATOM 629 OE2 GLU A 84 -5.751 21.860 -0.149 1.00 50.76 O ANISOU 629 OE2 GLU A 84 7205 5743 6337 285 -227 44 O ATOM 630 N ALA A 85 -10.403 19.352 3.661 1.00 44.72 N ANISOU 630 N ALA A 85 6310 5032 5651 158 -85 82 N ATOM 631 CA ALA A 85 -11.364 18.319 3.997 1.00 42.46 C ANISOU 631 CA ALA A 85 5977 4743 5414 144 -78 108 C ATOM 632 C ALA A 85 -12.680 18.701 3.378 1.00 46.25 C ANISOU 632 C ALA A 85 6430 5183 5961 198 -48 39 C ATOM 633 O ALA A 85 -12.801 19.786 2.810 1.00 45.46 O ANISOU 633 O ALA A 85 6352 5058 5864 243 -32 -24 O ATOM 634 CB ALA A 85 -11.536 18.285 5.517 1.00 42.31 C ANISOU 634 CB ALA A 85 5963 4794 5318 49 -31 133 C ATOM 635 N ASP A 86 -13.680 17.827 3.524 1.00 45.16 N ANISOU 635 N ASP A 86 6243 5040 5876 188 -42 55 N ATOM 636 CA ASP A 86 -15.066 18.115 3.149 1.00 47.01 C ANISOU 636 CA ASP A 86 6434 5256 6172 225 -10 -2 C ATOM 637 C ASP A 86 -15.775 18.444 4.469 1.00 51.04 C ANISOU 637 C ASP A 86 6931 5827 6636 161 72 -19 C ATOM 638 O ASP A 86 -15.603 17.742 5.467 1.00 51.46 O ANISOU 638 O ASP A 86 6983 5924 6643 84 82 33 O ATOM 639 CB ASP A 86 -15.754 16.890 2.510 1.00 49.29 C ANISOU 639 CB ASP A 86 6673 5511 6545 240 -53 28 C ATOM 640 CG ASP A 86 -15.165 16.478 1.180 1.00 62.36 C ANISOU 640 CG ASP A 86 8343 7103 8247 299 -126 38 C ATOM 641 OD1 ASP A 86 -14.961 17.360 0.324 1.00 60.06 O ANISOU 641 OD1 ASP A 86 8073 6785 7964 356 -137 -7 O ATOM 642 OD2 ASP A 86 -14.920 15.266 0.990 1.00 73.97 O ANISOU 642 OD2 ASP A 86 9809 8549 9746 285 -168 91 O ATOM 643 N TYR A 87 -16.566 19.484 4.466 1.00 45.69 N ANISOU 643 N TYR A 87 6243 5148 5969 194 132 -91 N ATOM 644 CA TYR A 87 -17.295 19.888 5.641 1.00 45.97 C ANISOU 644 CA TYR A 87 6267 5237 5964 143 223 -122 C ATOM 645 C TYR A 87 -18.728 19.863 5.317 1.00 51.09 C ANISOU 645 C TYR A 87 6838 5878 6695 185 255 -158 C ATOM 646 O TYR A 87 -19.087 20.272 4.223 1.00 51.06 O ANISOU 646 O TYR A 87 6813 5826 6761 269 227 -189 O ATOM 647 CB TYR A 87 -16.912 21.328 6.048 1.00 45.88 C ANISOU 647 CB TYR A 87 6319 5228 5884 145 283 -185 C ATOM 648 CG TYR A 87 -15.476 21.436 6.491 1.00 45.79 C ANISOU 648 CG TYR A 87 6382 5239 5777 86 255 -149 C ATOM 649 CD1 TYR A 87 -14.445 21.548 5.563 1.00 45.92 C ANISOU 649 CD1 TYR A 87 6431 5217 5799 127 182 -130 C ATOM 650 CD2 TYR A 87 -15.136 21.339 7.832 1.00 46.19 C ANISOU 650 CD2 TYR A 87 6463 5357 5729 -18 296 -126 C ATOM 651 CE1 TYR A 87 -13.113 21.583 5.966 1.00 45.54 C ANISOU 651 CE1 TYR A 87 6436 5200 5668 71 152 -88 C ATOM 652 CE2 TYR A 87 -13.817 21.441 8.250 1.00 46.81 C ANISOU 652 CE2 TYR A 87 6602 5466 5719 -78 263 -85 C ATOM 653 CZ TYR A 87 -12.807 21.562 7.315 1.00 51.93 C ANISOU 653 CZ TYR A 87 7272 6078 6380 -31 190 -65 C ATOM 654 OH TYR A 87 -11.509 21.610 7.751 1.00 50.49 O ANISOU 654 OH TYR A 87 7136 5937 6113 -94 156 -18 O ATOM 655 N TYR A 88 -19.568 19.413 6.257 1.00 47.41 N ANISOU 655 N TYR A 88 6327 5466 6221 125 313 -152 N ATOM 656 CA TYR A 88 -20.996 19.456 6.013 1.00 47.84 C ANISOU 656 CA TYR A 88 6294 5527 6355 164 352 -187 C ATOM 657 C TYR A 88 -21.747 19.835 7.291 1.00 54.58 C ANISOU 657 C TYR A 88 7125 6446 7165 110 467 -224 C ATOM 658 O TYR A 88 -21.296 19.595 8.417 1.00 52.61 O ANISOU 658 O TYR A 88 6918 6246 6826 16 502 -201 O ATOM 659 CB TYR A 88 -21.542 18.184 5.314 1.00 48.02 C ANISOU 659 CB TYR A 88 6252 5537 6455 162 282 -136 C ATOM 660 CG TYR A 88 -21.373 16.937 6.138 1.00 49.16 C ANISOU 660 CG TYR A 88 6398 5719 6560 61 272 -66 C ATOM 661 CD1 TYR A 88 -22.332 16.563 7.079 1.00 50.78 C ANISOU 661 CD1 TYR A 88 6550 5988 6757 -8 340 -63 C ATOM 662 CD2 TYR A 88 -20.254 16.121 5.979 1.00 49.55 C ANISOU 662 CD2 TYR A 88 6502 5740 6585 34 196 0 C ATOM 663 CE1 TYR A 88 -22.165 15.426 7.865 1.00 49.34 C ANISOU 663 CE1 TYR A 88 6378 5838 6533 -108 328 7 C ATOM 664 CE2 TYR A 88 -20.071 14.986 6.767 1.00 50.54 C ANISOU 664 CE2 TYR A 88 6635 5893 6676 -55 184 72 C ATOM 665 CZ TYR A 88 -21.026 14.650 7.714 1.00 57.10 C ANISOU 665 CZ TYR A 88 7420 6784 7490 -130 248 77 C ATOM 666 OH TYR A 88 -20.853 13.541 8.493 1.00 55.00 O ANISOU 666 OH TYR A 88 7167 6542 7188 -223 233 154 O ATOM 667 N CYS A 89 -22.865 20.491 7.073 1.00 54.15 N ANISOU 667 N CYS A 89 7007 6393 7176 173 525 -282 N ATOM 668 CA CYS A 89 -23.765 21.026 8.066 1.00 57.03 C ANISOU 668 CA CYS A 89 7335 6811 7523 151 647 -336 C ATOM 669 C CYS A 89 -24.800 19.965 8.381 1.00 56.35 C ANISOU 669 C CYS A 89 7151 6782 7476 98 661 -301 C ATOM 670 O CYS A 89 -25.213 19.238 7.495 1.00 53.52 O ANISOU 670 O CYS A 89 6732 6405 7196 125 586 -264 O ATOM 671 CB CYS A 89 -24.406 22.295 7.515 1.00 59.52 C ANISOU 671 CB CYS A 89 7623 7086 7904 265 696 -412 C ATOM 672 SG CYS A 89 -25.565 23.091 8.642 1.00 67.08 S ANISOU 672 SG CYS A 89 8532 8099 8856 263 863 -492 S ATOM 673 N GLY A 90 -25.188 19.873 9.642 1.00 52.66 N ANISOU 673 N GLY A 90 6677 6386 6947 14 756 -313 N ATOM 674 CA GLY A 90 -26.178 18.909 10.105 1.00 52.91 C ANISOU 674 CA GLY A 90 6620 6483 7000 -54 783 -281 C ATOM 675 C GLY A 90 -27.109 19.589 11.081 1.00 58.54 C ANISOU 675 C GLY A 90 7288 7260 7694 -71 928 -349 C ATOM 676 O GLY A 90 -26.657 20.333 11.960 1.00 57.44 O ANISOU 676 O GLY A 90 7224 7135 7464 -103 1008 -394 O ATOM 677 N VAL A 91 -28.424 19.385 10.904 1.00 56.52 N ANISOU 677 N VAL A 91 6908 7044 7523 -46 967 -362 N ATOM 678 CA VAL A 91 -29.434 20.046 11.740 1.00 57.25 C ANISOU 678 CA VAL A 91 6938 7200 7614 -45 1115 -432 C ATOM 679 C VAL A 91 -30.724 19.217 11.839 1.00 59.88 C ANISOU 679 C VAL A 91 7134 7608 8010 -84 1140 -406 C ATOM 680 O VAL A 91 -31.067 18.448 10.923 1.00 57.81 O ANISOU 680 O VAL A 91 6805 7332 7827 -68 1042 -353 O ATOM 681 CB VAL A 91 -29.687 21.514 11.262 1.00 61.44 C ANISOU 681 CB VAL A 91 7462 7678 8204 95 1172 -518 C ATOM 682 CG1 VAL A 91 -30.389 21.547 9.919 1.00 61.33 C ANISOU 682 CG1 VAL A 91 7345 7627 8329 211 1098 -506 C ATOM 683 CG2 VAL A 91 -30.444 22.352 12.299 1.00 62.78 C ANISOU 683 CG2 VAL A 91 7604 7899 8351 96 1344 -604 C ATOM 684 N TRP A 92 -31.436 19.396 12.952 1.00 56.65 N ANISOU 684 N TRP A 92 6683 7280 7560 -142 1276 -448 N ATOM 685 CA TRP A 92 -32.714 18.745 13.152 1.00 57.90 C ANISOU 685 CA TRP A 92 6704 7523 7773 -183 1321 -433 C ATOM 686 C TRP A 92 -33.784 19.502 12.365 1.00 64.65 C ANISOU 686 C TRP A 92 7428 8374 8762 -43 1354 -482 C ATOM 687 O TRP A 92 -33.777 20.733 12.332 1.00 62.77 O ANISOU 687 O TRP A 92 7208 8099 8544 60 1424 -557 O ATOM 688 CB TRP A 92 -33.087 18.689 14.647 1.00 57.15 C ANISOU 688 CB TRP A 92 6611 7524 7581 -299 1464 -461 C ATOM 689 CG TRP A 92 -34.233 17.762 14.903 1.00 58.51 C ANISOU 689 CG TRP A 92 6653 7788 7789 -375 1492 -425 C ATOM 690 CD1 TRP A 92 -35.555 18.097 15.004 1.00 62.67 C ANISOU 690 CD1 TRP A 92 7034 8386 8392 -334 1597 -473 C ATOM 691 CD2 TRP A 92 -34.179 16.334 14.919 1.00 57.98 C ANISOU 691 CD2 TRP A 92 6583 7745 7701 -495 1402 -328 C ATOM 692 NE1 TRP A 92 -36.321 16.966 15.140 1.00 62.56 N ANISOU 692 NE1 TRP A 92 6926 8449 8395 -435 1580 -413 N ATOM 693 CE2 TRP A 92 -35.503 15.864 15.077 1.00 63.03 C ANISOU 693 CE2 TRP A 92 7076 8476 8396 -536 1459 -324 C ATOM 694 CE3 TRP A 92 -33.135 15.398 14.809 1.00 58.59 C ANISOU 694 CE3 TRP A 92 6766 7773 7721 -571 1278 -243 C ATOM 695 CZ2 TRP A 92 -35.804 14.504 15.197 1.00 62.28 C ANISOU 695 CZ2 TRP A 92 6952 8424 8290 -663 1401 -239 C ATOM 696 CZ3 TRP A 92 -33.436 14.046 14.908 1.00 60.30 C ANISOU 696 CZ3 TRP A 92 6954 8022 7934 -685 1221 -159 C ATOM 697 CH2 TRP A 92 -34.760 13.612 15.087 1.00 62.07 C ANISOU 697 CH2 TRP A 92 7043 8335 8206 -734 1281 -158 C ATOM 698 N ASP A 93 -34.688 18.760 11.715 1.00 64.74 N ANISOU 698 N ASP A 93 7311 8422 8866 -43 1298 -437 N ATOM 699 CA ASP A 93 -35.803 19.354 10.981 1.00 65.67 C ANISOU 699 CA ASP A 93 7283 8553 9115 80 1320 -468 C ATOM 700 C ASP A 93 -37.065 18.942 11.703 1.00 70.88 C ANISOU 700 C ASP A 93 7802 9332 9795 15 1424 -473 C ATOM 701 O ASP A 93 -37.435 17.768 11.686 1.00 70.86 O ANISOU 701 O ASP A 93 7749 9383 9793 -91 1370 -407 O ATOM 702 CB ASP A 93 -35.808 18.926 9.509 1.00 67.05 C ANISOU 702 CB ASP A 93 7420 8674 9381 138 1161 -411 C ATOM 703 CG ASP A 93 -36.724 19.776 8.651 1.00 72.77 C ANISOU 703 CG ASP A 93 8019 9394 10236 285 1167 -441 C ATOM 704 OD1 ASP A 93 -37.956 19.729 8.868 1.00 75.37 O ANISOU 704 OD1 ASP A 93 8194 9811 10630 289 1237 -449 O ATOM 705 OD2 ASP A 93 -36.216 20.455 7.745 1.00 74.37 O ANISOU 705 OD2 ASP A 93 8272 9509 10475 391 1097 -450 O ATOM 706 N SER A 94 -37.680 19.910 12.399 1.00 70.57 N ANISOU 706 N SER A 94 7712 9336 9767 69 1581 -554 N ATOM 707 CA SER A 94 -38.856 19.750 13.260 1.00 72.35 C ANISOU 707 CA SER A 94 7805 9681 10002 16 1718 -579 C ATOM 708 C SER A 94 -40.136 19.330 12.539 1.00 77.57 C ANISOU 708 C SER A 94 8268 10411 10793 50 1684 -542 C ATOM 709 O SER A 94 -40.968 18.643 13.146 1.00 78.42 O ANISOU 709 O SER A 94 8274 10628 10893 -51 1745 -523 O ATOM 710 CB SER A 94 -39.083 21.007 14.083 1.00 76.96 C ANISOU 710 CB SER A 94 8398 10273 10568 86 1897 -685 C ATOM 711 OG SER A 94 -37.999 21.157 14.985 1.00 84.47 O ANISOU 711 OG SER A 94 9527 11195 11373 0 1937 -711 O ATOM 712 N SER A 95 -40.279 19.700 11.259 1.00 74.47 N ANISOU 712 N SER A 95 7821 9960 10514 180 1583 -525 N ATOM 713 CA SER A 95 -41.430 19.308 10.441 1.00 75.72 C ANISOU 713 CA SER A 95 7793 10181 10795 211 1527 -481 C ATOM 714 C SER A 95 -41.263 17.874 9.906 1.00 78.29 C ANISOU 714 C SER A 95 8131 10515 11101 83 1377 -387 C ATOM 715 O SER A 95 -42.252 17.164 9.715 1.00 78.60 O ANISOU 715 O SER A 95 8027 10643 11194 26 1358 -344 O ATOM 716 CB SER A 95 -41.635 20.290 9.287 1.00 80.66 C ANISOU 716 CB SER A 95 8364 10741 11542 393 1472 -494 C ATOM 717 OG SER A 95 -40.563 20.275 8.357 1.00 90.77 O ANISOU 717 OG SER A 95 9779 11905 12804 424 1326 -464 O ATOM 718 N LEU A 96 -40.002 17.469 9.659 1.00 72.78 N ANISOU 718 N LEU A 96 7605 9722 10326 41 1273 -357 N ATOM 719 CA LEU A 96 -39.613 16.168 9.138 1.00 70.76 C ANISOU 719 CA LEU A 96 7398 9442 10045 -68 1132 -275 C ATOM 720 C LEU A 96 -39.396 15.123 10.254 1.00 71.12 C ANISOU 720 C LEU A 96 7503 9537 9981 -244 1171 -241 C ATOM 721 O LEU A 96 -39.525 13.920 9.994 1.00 69.83 O ANISOU 721 O LEU A 96 7331 9387 9815 -351 1084 -172 O ATOM 722 CB LEU A 96 -38.345 16.358 8.295 1.00 69.74 C ANISOU 722 CB LEU A 96 7421 9183 9896 -7 1013 -264 C ATOM 723 CG LEU A 96 -37.801 15.138 7.545 1.00 75.23 C ANISOU 723 CG LEU A 96 8181 9825 10576 -87 859 -188 C ATOM 724 CD1 LEU A 96 -38.484 14.959 6.195 1.00 75.98 C ANISOU 724 CD1 LEU A 96 8174 9915 10778 -32 749 -159 C ATOM 725 CD2 LEU A 96 -36.275 15.216 7.402 1.00 76.21 C ANISOU 725 CD2 LEU A 96 8491 9840 10626 -75 796 -184 C ATOM 726 N SER A 97 -39.100 15.580 11.496 1.00 66.06 N ANISOU 726 N SER A 97 6925 8924 9251 -277 1301 -289 N ATOM 727 CA SER A 97 -38.819 14.731 12.667 1.00 65.36 C ANISOU 727 CA SER A 97 6907 8884 9045 -443 1347 -258 C ATOM 728 C SER A 97 -37.599 13.804 12.413 1.00 66.42 C ANISOU 728 C SER A 97 7196 8929 9111 -518 1212 -186 C ATOM 729 O SER A 97 -37.570 12.630 12.788 1.00 65.79 O ANISOU 729 O SER A 97 7142 8873 8982 -656 1175 -118 O ATOM 730 CB SER A 97 -40.064 13.981 13.144 1.00 70.47 C ANISOU 730 CB SER A 97 7410 9655 9710 -551 1407 -233 C ATOM 731 OG SER A 97 -40.959 14.850 13.817 1.00 76.74 O ANISOU 731 OG SER A 97 8091 10539 10529 -504 1571 -307 O ATOM 732 N GLY A 98 -36.579 14.405 11.819 1.00 61.73 N ANISOU 732 N GLY A 98 6707 8232 8514 -421 1148 -203 N ATOM 733 CA GLY A 98 -35.318 13.768 11.489 1.00 59.73 C ANISOU 733 CA GLY A 98 6599 7888 8209 -455 1027 -146 C ATOM 734 C GLY A 98 -34.269 14.797 11.142 1.00 62.48 C ANISOU 734 C GLY A 98 7051 8149 8541 -343 1008 -189 C ATOM 735 O GLY A 98 -34.584 15.968 10.912 1.00 62.70 O ANISOU 735 O GLY A 98 7036 8172 8615 -227 1068 -259 O ATOM 736 N GLY A 99 -33.020 14.356 11.109 1.00 57.77 N ANISOU 736 N GLY A 99 6589 7482 7878 -379 925 -145 N ATOM 737 CA GLY A 99 -31.888 15.186 10.734 1.00 55.60 C ANISOU 737 CA GLY A 99 6422 7124 7580 -290 890 -173 C ATOM 738 C GLY A 99 -31.774 15.382 9.238 1.00 58.20 C ANISOU 738 C GLY A 99 6735 7375 8003 -177 782 -171 C ATOM 739 O GLY A 99 -32.034 14.467 8.449 1.00 57.37 O ANISOU 739 O GLY A 99 6594 7251 7952 -198 687 -120 O ATOM 740 N VAL A 100 -31.387 16.595 8.850 1.00 56.64 N ANISOU 740 N VAL A 100 6571 7131 7821 -63 798 -229 N ATOM 741 CA VAL A 100 -31.081 17.001 7.482 1.00 55.64 C ANISOU 741 CA VAL A 100 6453 6923 7764 49 701 -234 C ATOM 742 C VAL A 100 -29.613 17.448 7.447 1.00 57.93 C ANISOU 742 C VAL A 100 6888 7140 7982 71 666 -239 C ATOM 743 O VAL A 100 -29.078 17.932 8.446 1.00 56.23 O ANISOU 743 O VAL A 100 6743 6941 7681 36 742 -265 O ATOM 744 CB VAL A 100 -32.051 18.035 6.849 1.00 60.50 C ANISOU 744 CB VAL A 100 6964 7545 8480 173 736 -287 C ATOM 745 CG1 VAL A 100 -33.421 17.412 6.586 1.00 61.33 C ANISOU 745 CG1 VAL A 100 6915 7721 8668 150 733 -263 C ATOM 746 CG2 VAL A 100 -32.181 19.288 7.702 1.00 60.60 C ANISOU 746 CG2 VAL A 100 6984 7575 8465 223 873 -365 C ATOM 747 N PHE A 101 -28.957 17.234 6.312 1.00 54.45 N ANISOU 747 N PHE A 101 6492 6624 7572 118 551 -211 N ATOM 748 CA PHE A 101 -27.549 17.539 6.153 1.00 52.54 C ANISOU 748 CA PHE A 101 6376 6317 7270 135 505 -207 C ATOM 749 C PHE A 101 -27.308 18.348 4.888 1.00 59.65 C ANISOU 749 C PHE A 101 7289 7147 8227 253 445 -234 C ATOM 750 O PHE A 101 -28.053 18.214 3.917 1.00 61.16 O ANISOU 750 O PHE A 101 7404 7329 8504 302 393 -228 O ATOM 751 CB PHE A 101 -26.737 16.209 6.155 1.00 51.93 C ANISOU 751 CB PHE A 101 6359 6218 7152 50 421 -129 C ATOM 752 CG PHE A 101 -26.929 15.388 7.419 1.00 52.90 C ANISOU 752 CG PHE A 101 6478 6407 7213 -73 473 -91 C ATOM 753 CD1 PHE A 101 -26.126 15.597 8.536 1.00 56.00 C ANISOU 753 CD1 PHE A 101 6952 6824 7502 -133 522 -87 C ATOM 754 CD2 PHE A 101 -27.957 14.453 7.515 1.00 54.96 C ANISOU 754 CD2 PHE A 101 6655 6712 7515 -136 475 -60 C ATOM 755 CE1 PHE A 101 -26.343 14.878 9.721 1.00 57.23 C ANISOU 755 CE1 PHE A 101 7106 7046 7595 -253 571 -49 C ATOM 756 CE2 PHE A 101 -28.168 13.731 8.693 1.00 57.19 C ANISOU 756 CE2 PHE A 101 6936 7057 7736 -256 525 -23 C ATOM 757 CZ PHE A 101 -27.350 13.933 9.781 1.00 55.92 C ANISOU 757 CZ PHE A 101 6858 6917 7470 -312 571 -15 C ATOM 758 N GLY A 102 -26.290 19.200 4.920 1.00 55.66 N ANISOU 758 N GLY A 102 6880 6598 7669 290 451 -262 N ATOM 759 CA GLY A 102 -25.831 19.929 3.746 1.00 54.99 C ANISOU 759 CA GLY A 102 6832 6441 7620 388 387 -280 C ATOM 760 C GLY A 102 -25.133 18.940 2.814 1.00 57.45 C ANISOU 760 C GLY A 102 7179 6708 7941 370 267 -223 C ATOM 761 O GLY A 102 -24.728 17.858 3.252 1.00 55.54 O ANISOU 761 O GLY A 102 6960 6480 7661 287 243 -174 O ATOM 762 N GLY A 103 -25.038 19.278 1.528 1.00 54.02 N ANISOU 762 N GLY A 103 6749 6218 7558 448 194 -230 N ATOM 763 CA GLY A 103 -24.429 18.419 0.510 1.00 52.25 C ANISOU 763 CA GLY A 103 6560 5947 7346 440 87 -188 C ATOM 764 C GLY A 103 -22.919 18.373 0.576 1.00 55.13 C ANISOU 764 C GLY A 103 7035 6273 7637 424 59 -172 C ATOM 765 O GLY A 103 -22.298 17.547 -0.103 1.00 55.39 O ANISOU 765 O GLY A 103 7103 6269 7673 410 -17 -136 O ATOM 766 N GLY A 104 -22.322 19.224 1.424 1.00 50.35 N ANISOU 766 N GLY A 104 6483 5681 6965 419 124 -198 N ATOM 767 CA GLY A 104 -20.875 19.213 1.638 1.00 49.74 C ANISOU 767 CA GLY A 104 6502 5585 6812 393 102 -178 C ATOM 768 C GLY A 104 -20.095 20.205 0.806 1.00 53.92 C ANISOU 768 C GLY A 104 7094 6063 7331 460 71 -207 C ATOM 769 O GLY A 104 -20.489 20.557 -0.324 1.00 52.16 O ANISOU 769 O GLY A 104 6851 5801 7168 529 28 -225 O ATOM 770 N THR A 105 -18.969 20.654 1.372 1.00 50.36 N ANISOU 770 N THR A 105 6721 5616 6799 432 89 -208 N ATOM 771 CA THR A 105 -18.074 21.630 0.750 1.00 49.91 C ANISOU 771 CA THR A 105 6734 5517 6713 477 67 -233 C ATOM 772 C THR A 105 -16.641 21.143 0.926 1.00 52.51 C ANISOU 772 C THR A 105 7123 5852 6975 428 28 -188 C ATOM 773 O THR A 105 -16.216 20.924 2.054 1.00 50.28 O ANISOU 773 O THR A 105 6861 5617 6628 358 63 -165 O ATOM 774 CB THR A 105 -18.205 23.024 1.433 1.00 52.28 C ANISOU 774 CB THR A 105 7070 5822 6972 488 151 -293 C ATOM 775 OG1 THR A 105 -19.543 23.512 1.365 1.00 54.60 O ANISOU 775 OG1 THR A 105 7299 6112 7333 541 198 -333 O ATOM 776 CG2 THR A 105 -17.234 24.093 0.849 1.00 46.38 C ANISOU 776 CG2 THR A 105 6406 5028 6186 522 131 -318 C ATOM 777 N LYS A 106 -15.878 21.103 -0.168 1.00 50.19 N ANISOU 777 N LYS A 106 6861 5516 6692 466 -39 -177 N ATOM 778 CA LYS A 106 -14.460 20.778 -0.145 1.00 49.35 C ANISOU 778 CA LYS A 106 6805 5414 6530 436 -76 -137 C ATOM 779 C LYS A 106 -13.737 22.103 0.069 1.00 53.61 C ANISOU 779 C LYS A 106 7411 5957 7001 434 -46 -173 C ATOM 780 O LYS A 106 -14.048 23.119 -0.573 1.00 52.49 O ANISOU 780 O LYS A 106 7289 5777 6878 487 -38 -222 O ATOM 781 CB LYS A 106 -14.014 20.175 -1.482 1.00 50.27 C ANISOU 781 CB LYS A 106 6925 5484 6691 479 -151 -118 C ATOM 782 CG LYS A 106 -12.526 19.847 -1.521 1.00 53.08 C ANISOU 782 CG LYS A 106 7322 5847 6998 459 -184 -77 C ATOM 783 CD LYS A 106 -12.069 19.336 -2.883 1.00 61.20 C ANISOU 783 CD LYS A 106 8359 6827 8067 505 -246 -70 C ATOM 784 CE LYS A 106 -10.645 18.842 -2.811 1.00 65.62 C ANISOU 784 CE LYS A 106 8942 7401 8589 488 -271 -22 C ATOM 785 NZ LYS A 106 -10.555 17.541 -2.093 1.00 70.36 N ANISOU 785 NZ LYS A 106 9514 8017 9204 452 -277 40 N ATOM 786 N VAL A 107 -12.777 22.092 0.986 1.00 50.49 N ANISOU 786 N VAL A 107 7052 5607 6526 367 -32 -144 N ATOM 787 CA VAL A 107 -11.982 23.260 1.289 1.00 48.44 C ANISOU 787 CA VAL A 107 6861 5358 6188 344 -7 -172 C ATOM 788 C VAL A 107 -10.629 22.930 0.723 1.00 50.87 C ANISOU 788 C VAL A 107 7190 5667 6469 339 -69 -128 C ATOM 789 O VAL A 107 -10.041 21.922 1.108 1.00 46.95 O ANISOU 789 O VAL A 107 6672 5206 5961 303 -98 -65 O ATOM 790 CB VAL A 107 -11.893 23.546 2.818 1.00 51.48 C ANISOU 790 CB VAL A 107 7269 5803 6487 257 58 -173 C ATOM 791 CG1 VAL A 107 -10.773 24.537 3.127 1.00 51.02 C ANISOU 791 CG1 VAL A 107 7288 5763 6333 211 67 -187 C ATOM 792 CG2 VAL A 107 -13.215 24.036 3.371 1.00 51.18 C ANISOU 792 CG2 VAL A 107 7213 5763 6472 266 137 -230 C ATOM 793 N THR A 108 -10.103 23.834 -0.129 1.00 50.05 N ANISOU 793 N THR A 108 7133 5530 6353 372 -87 -159 N ATOM 794 CA THR A 108 -8.782 23.716 -0.732 1.00 48.21 C ANISOU 794 CA THR A 108 6921 5304 6091 369 -137 -127 C ATOM 795 C THR A 108 -7.880 24.865 -0.289 1.00 50.58 C ANISOU 795 C THR A 108 7289 5631 6297 316 -115 -144 C ATOM 796 O THR A 108 -8.267 26.019 -0.357 1.00 47.85 O ANISOU 796 O THR A 108 6991 5253 5935 326 -79 -202 O ATOM 797 CB THR A 108 -8.898 23.573 -2.271 1.00 52.51 C ANISOU 797 CB THR A 108 7460 5789 6703 445 -185 -141 C ATOM 798 OG1 THR A 108 -9.715 22.430 -2.577 1.00 48.65 O ANISOU 798 OG1 THR A 108 6913 5280 6293 476 -206 -122 O ATOM 799 CG2 THR A 108 -7.530 23.441 -2.955 1.00 45.99 C ANISOU 799 CG2 THR A 108 6653 4973 5849 443 -229 -112 C ATOM 800 N VAL A 109 -6.655 24.541 0.144 1.00 48.78 N ANISOU 800 N VAL A 109 7064 5462 6009 259 -139 -91 N ATOM 801 CA VAL A 109 -5.643 25.532 0.506 1.00 47.92 C ANISOU 801 CA VAL A 109 7014 5390 5804 195 -129 -98 C ATOM 802 C VAL A 109 -4.842 25.693 -0.769 1.00 48.98 C ANISOU 802 C VAL A 109 7157 5499 5953 236 -176 -95 C ATOM 803 O VAL A 109 -4.167 24.758 -1.179 1.00 46.21 O ANISOU 803 O VAL A 109 6761 5168 5627 253 -219 -42 O ATOM 804 CB VAL A 109 -4.820 25.029 1.710 1.00 53.21 C ANISOU 804 CB VAL A 109 7668 6148 6401 106 -135 -33 C ATOM 805 CG1 VAL A 109 -3.635 25.938 1.998 1.00 53.20 C ANISOU 805 CG1 VAL A 109 7720 6196 6298 30 -138 -29 C ATOM 806 CG2 VAL A 109 -5.721 24.883 2.928 1.00 53.94 C ANISOU 806 CG2 VAL A 109 7756 6262 6475 61 -84 -41 C ATOM 807 N LEU A 110 -5.001 26.853 -1.464 1.00 46.58 N ANISOU 807 N LEU A 110 6913 5143 5641 259 -164 -154 N ATOM 808 CA LEU A 110 -4.401 27.077 -2.771 1.00 46.13 C ANISOU 808 CA LEU A 110 6871 5057 5598 298 -204 -158 C ATOM 809 C LEU A 110 -2.880 27.064 -2.762 1.00 51.17 C ANISOU 809 C LEU A 110 7512 5761 6170 243 -231 -114 C ATOM 810 O LEU A 110 -2.252 27.971 -2.213 1.00 52.61 O ANISOU 810 O LEU A 110 7745 5977 6267 170 -213 -122 O ATOM 811 CB LEU A 110 -4.943 28.361 -3.433 1.00 45.28 C ANISOU 811 CB LEU A 110 6833 4878 5492 328 -187 -223 C ATOM 812 CG LEU A 110 -6.460 28.445 -3.553 1.00 47.74 C ANISOU 812 CG LEU A 110 7131 5127 5880 394 -163 -263 C ATOM 813 CD1 LEU A 110 -6.890 29.874 -3.914 1.00 48.20 C ANISOU 813 CD1 LEU A 110 7266 5119 5929 415 -138 -321 C ATOM 814 CD2 LEU A 110 -6.999 27.388 -4.519 1.00 42.93 C ANISOU 814 CD2 LEU A 110 6459 4493 5361 464 -208 -244 C ATOM 815 N GLY A 111 -2.329 26.027 -3.384 1.00 46.61 N ANISOU 815 N GLY A 111 6877 5199 5634 278 -270 -69 N ATOM 816 CA GLY A 111 -0.890 25.790 -3.483 1.00 45.86 C ANISOU 816 CA GLY A 111 6758 5170 5496 244 -298 -18 C ATOM 817 C GLY A 111 -0.352 25.981 -4.882 1.00 49.07 C ANISOU 817 C GLY A 111 7177 5551 5918 284 -321 -34 C ATOM 818 O GLY A 111 0.845 25.854 -5.120 1.00 48.87 O ANISOU 818 O GLY A 111 7129 5580 5861 262 -338 2 O ATOM 819 N GLN A 112 -1.233 26.320 -5.807 1.00 45.92 N ANISOU 819 N GLN A 112 6811 5072 5563 340 -320 -87 N ATOM 820 CA GLN A 112 -0.872 26.501 -7.202 1.00 46.47 C ANISOU 820 CA GLN A 112 6901 5112 5646 375 -343 -106 C ATOM 821 C GLN A 112 -1.963 27.332 -7.888 1.00 50.80 C ANISOU 821 C GLN A 112 7507 5578 6217 412 -340 -164 C ATOM 822 O GLN A 112 -3.049 27.493 -7.309 1.00 51.31 O ANISOU 822 O GLN A 112 7576 5610 6310 426 -320 -185 O ATOM 823 CB GLN A 112 -0.737 25.107 -7.889 1.00 46.13 C ANISOU 823 CB GLN A 112 6793 5062 5672 435 -365 -78 C ATOM 824 CG GLN A 112 -2.026 24.365 -8.095 1.00 45.84 C ANISOU 824 CG GLN A 112 6736 4963 5717 492 -370 -95 C ATOM 825 CD GLN A 112 -1.796 22.916 -8.460 1.00 56.29 C ANISOU 825 CD GLN A 112 8004 6284 7102 535 -385 -62 C ATOM 826 OE1 GLN A 112 -1.624 22.051 -7.598 1.00 53.99 O ANISOU 826 OE1 GLN A 112 7664 6022 6828 528 -382 -15 O ATOM 827 NE2 GLN A 112 -1.755 22.631 -9.736 1.00 47.17 N ANISOU 827 NE2 GLN A 112 6859 5089 5975 576 -401 -86 N ATOM 828 N PRO A 113 -1.740 27.825 -9.121 1.00 46.95 N ANISOU 828 N PRO A 113 7059 5057 5724 430 -360 -187 N ATOM 829 CA PRO A 113 -2.813 28.575 -9.797 1.00 46.56 C ANISOU 829 CA PRO A 113 7060 4928 5703 470 -367 -231 C ATOM 830 C PRO A 113 -4.047 27.715 -10.030 1.00 48.69 C ANISOU 830 C PRO A 113 7282 5156 6061 535 -379 -236 C ATOM 831 O PRO A 113 -3.964 26.506 -10.211 1.00 48.73 O ANISOU 831 O PRO A 113 7231 5176 6106 557 -393 -214 O ATOM 832 CB PRO A 113 -2.175 28.959 -11.153 1.00 48.03 C ANISOU 832 CB PRO A 113 7287 5101 5863 470 -394 -239 C ATOM 833 CG PRO A 113 -0.708 28.941 -10.910 1.00 51.63 C ANISOU 833 CG PRO A 113 7734 5633 6252 410 -386 -211 C ATOM 834 CD PRO A 113 -0.520 27.774 -9.964 1.00 47.89 C ANISOU 834 CD PRO A 113 7179 5211 5806 413 -377 -172 C ATOM 835 N LYS A 114 -5.199 28.344 -9.977 1.00 46.25 N ANISOU 835 N LYS A 114 6996 4795 5784 565 -373 -266 N ATOM 836 CA LYS A 114 -6.483 27.715 -10.285 1.00 45.75 C ANISOU 836 CA LYS A 114 6888 4693 5803 622 -388 -272 C ATOM 837 C LYS A 114 -6.508 27.437 -11.797 1.00 50.54 C ANISOU 837 C LYS A 114 7503 5267 6432 654 -438 -276 C ATOM 838 O LYS A 114 -5.888 28.163 -12.562 1.00 50.69 O ANISOU 838 O LYS A 114 7579 5276 6406 641 -453 -284 O ATOM 839 CB LYS A 114 -7.641 28.647 -9.902 1.00 47.10 C ANISOU 839 CB LYS A 114 7078 4818 6000 649 -366 -302 C ATOM 840 CG LYS A 114 -7.893 28.725 -8.412 1.00 44.77 C ANISOU 840 CG LYS A 114 6766 4552 5692 621 -311 -306 C ATOM 841 CD LYS A 114 -9.195 29.473 -8.202 1.00 46.53 C ANISOU 841 CD LYS A 114 6993 4724 5961 666 -285 -338 C ATOM 842 CE LYS A 114 -9.443 29.786 -6.758 1.00 49.38 C ANISOU 842 CE LYS A 114 7355 5108 6298 634 -217 -355 C ATOM 843 NZ LYS A 114 -10.856 30.189 -6.525 1.00 49.93 N ANISOU 843 NZ LYS A 114 7400 5137 6434 691 -185 -384 N ATOM 844 N ALA A 115 -7.120 26.344 -12.211 1.00 47.98 N ANISOU 844 N ALA A 115 7129 4933 6168 685 -461 -269 N ATOM 845 CA ALA A 115 -7.189 25.978 -13.627 1.00 48.74 C ANISOU 845 CA ALA A 115 7237 5001 6280 706 -506 -276 C ATOM 846 C ALA A 115 -8.562 25.461 -13.910 1.00 51.55 C ANISOU 846 C ALA A 115 7553 5326 6709 742 -533 -281 C ATOM 847 O ALA A 115 -9.062 24.618 -13.181 1.00 50.62 O ANISOU 847 O ALA A 115 7380 5221 6633 745 -518 -269 O ATOM 848 CB ALA A 115 -6.167 24.896 -13.962 1.00 49.38 C ANISOU 848 CB ALA A 115 7300 5111 6349 692 -507 -262 C ATOM 849 N ALA A 116 -9.158 25.957 -14.980 1.00 48.80 N ANISOU 849 N ALA A 116 7232 4939 6371 763 -575 -292 N ATOM 850 CA ALA A 116 -10.478 25.576 -15.456 1.00 48.75 C ANISOU 850 CA ALA A 116 7187 4908 6429 793 -613 -293 C ATOM 851 C ALA A 116 -10.364 24.224 -16.099 1.00 51.57 C ANISOU 851 C ALA A 116 7523 5268 6802 780 -637 -291 C ATOM 852 O ALA A 116 -9.390 23.955 -16.826 1.00 52.18 O ANISOU 852 O ALA A 116 7640 5349 6838 761 -643 -297 O ATOM 853 CB ALA A 116 -10.988 26.610 -16.480 1.00 49.76 C ANISOU 853 CB ALA A 116 7358 4998 6552 815 -660 -297 C ATOM 854 N PRO A 117 -11.329 23.324 -15.866 1.00 49.31 N ANISOU 854 N PRO A 117 7179 4981 6577 786 -647 -284 N ATOM 855 CA PRO A 117 -11.226 22.014 -16.499 1.00 49.88 C ANISOU 855 CA PRO A 117 7244 5045 6663 769 -667 -286 C ATOM 856 C PRO A 117 -11.318 22.032 -18.006 1.00 53.99 C ANISOU 856 C PRO A 117 7808 5542 7164 761 -721 -302 C ATOM 857 O PRO A 117 -12.000 22.856 -18.586 1.00 53.36 O ANISOU 857 O PRO A 117 7740 5450 7085 773 -761 -301 O ATOM 858 CB PRO A 117 -12.377 21.213 -15.890 1.00 51.55 C ANISOU 858 CB PRO A 117 7387 5259 6940 769 -669 -275 C ATOM 859 CG PRO A 117 -13.315 22.187 -15.374 1.00 55.38 C ANISOU 859 CG PRO A 117 7841 5751 7451 794 -666 -271 C ATOM 860 CD PRO A 117 -12.534 23.420 -15.021 1.00 51.47 C ANISOU 860 CD PRO A 117 7391 5259 6905 805 -635 -277 C ATOM 861 N SER A 118 -10.655 21.057 -18.618 1.00 50.84 N ANISOU 861 N SER A 118 7433 5134 6749 740 -719 -314 N ATOM 862 CA SER A 118 -10.738 20.786 -20.035 1.00 49.90 C ANISOU 862 CA SER A 118 7359 4994 6608 720 -763 -335 C ATOM 863 C SER A 118 -11.821 19.686 -20.065 1.00 50.47 C ANISOU 863 C SER A 118 7389 5051 6737 705 -789 -333 C ATOM 864 O SER A 118 -11.696 18.700 -19.351 1.00 48.32 O ANISOU 864 O SER A 118 7087 4775 6497 703 -756 -328 O ATOM 865 CB SER A 118 -9.389 20.288 -20.557 1.00 51.08 C ANISOU 865 CB SER A 118 7554 5142 6710 706 -731 -355 C ATOM 866 OG SER A 118 -9.593 19.327 -21.573 1.00 67.93 O ANISOU 866 OG SER A 118 9717 7250 8846 681 -754 -379 O ATOM 867 N VAL A 119 -12.941 19.931 -20.780 1.00 47.67 N ANISOU 867 N VAL A 119 7026 4690 6396 695 -851 -331 N ATOM 868 CA VAL A 119 -14.079 19.008 -20.873 1.00 46.99 C ANISOU 868 CA VAL A 119 6897 4598 6359 670 -885 -327 C ATOM 869 C VAL A 119 -14.150 18.408 -22.271 1.00 54.35 C ANISOU 869 C VAL A 119 7883 5509 7259 623 -933 -351 C ATOM 870 O VAL A 119 -14.282 19.137 -23.251 1.00 54.18 O ANISOU 870 O VAL A 119 7898 5490 7198 613 -982 -353 O ATOM 871 CB VAL A 119 -15.410 19.696 -20.457 1.00 48.99 C ANISOU 871 CB VAL A 119 7079 4873 6662 691 -918 -299 C ATOM 872 CG1 VAL A 119 -16.561 18.694 -20.434 1.00 49.09 C ANISOU 872 CG1 VAL A 119 7035 4890 6727 657 -949 -291 C ATOM 873 CG2 VAL A 119 -15.283 20.414 -19.109 1.00 47.02 C ANISOU 873 CG2 VAL A 119 6790 4641 6433 734 -862 -284 C ATOM 874 N THR A 120 -14.043 17.074 -22.369 1.00 52.85 N ANISOU 874 N THR A 120 7706 5294 7081 591 -916 -371 N ATOM 875 CA THR A 120 -14.107 16.342 -23.638 1.00 52.10 C ANISOU 875 CA THR A 120 7671 5172 6952 536 -951 -403 C ATOM 876 C THR A 120 -15.198 15.290 -23.486 1.00 55.38 C ANISOU 876 C THR A 120 8048 5576 7417 494 -977 -398 C ATOM 877 O THR A 120 -15.091 14.362 -22.672 1.00 51.95 O ANISOU 877 O THR A 120 7593 5121 7023 495 -934 -396 O ATOM 878 CB THR A 120 -12.736 15.725 -23.972 1.00 60.37 C ANISOU 878 CB THR A 120 8787 6189 7962 537 -892 -440 C ATOM 879 OG1 THR A 120 -11.687 16.623 -23.600 1.00 58.13 O ANISOU 879 OG1 THR A 120 8510 5927 7650 581 -851 -432 O ATOM 880 CG2 THR A 120 -12.620 15.290 -25.426 1.00 56.34 C ANISOU 880 CG2 THR A 120 8358 5654 7395 483 -918 -483 C ATOM 881 N LEU A 121 -16.264 15.478 -24.240 1.00 54.27 N ANISOU 881 N LEU A 121 7895 5453 7273 454 -1053 -390 N ATOM 882 CA LEU A 121 -17.446 14.638 -24.245 1.00 54.96 C ANISOU 882 CA LEU A 121 7940 5542 7399 400 -1094 -381 C ATOM 883 C LEU A 121 -17.438 13.619 -25.415 1.00 57.14 C ANISOU 883 C LEU A 121 8297 5783 7632 320 -1122 -422 C ATOM 884 O LEU A 121 -17.482 13.992 -26.590 1.00 55.98 O ANISOU 884 O LEU A 121 8201 5642 7426 284 -1173 -436 O ATOM 885 CB LEU A 121 -18.691 15.542 -24.250 1.00 56.40 C ANISOU 885 CB LEU A 121 8041 5777 7610 408 -1163 -337 C ATOM 886 CG LEU A 121 -20.047 14.894 -24.033 1.00 64.16 C ANISOU 886 CG LEU A 121 8948 6784 8644 361 -1206 -314 C ATOM 887 CD1 LEU A 121 -20.085 14.143 -22.742 1.00 65.57 C ANISOU 887 CD1 LEU A 121 9080 6955 8879 370 -1142 -309 C ATOM 888 CD2 LEU A 121 -21.156 15.934 -24.052 1.00 65.68 C ANISOU 888 CD2 LEU A 121 9052 7033 8870 387 -1268 -268 C ATOM 889 N PHE A 122 -17.373 12.315 -25.056 1.00 51.30 N ANISOU 889 N PHE A 122 7574 4999 6919 288 -1084 -442 N ATOM 890 CA PHE A 122 -17.348 11.206 -25.990 1.00 49.88 C ANISOU 890 CA PHE A 122 7478 4770 6705 211 -1093 -489 C ATOM 891 C PHE A 122 -18.713 10.519 -26.132 1.00 57.47 C ANISOU 891 C PHE A 122 8404 5742 7691 127 -1156 -476 C ATOM 892 O PHE A 122 -19.250 9.987 -25.137 1.00 59.17 O ANISOU 892 O PHE A 122 8555 5957 7968 126 -1140 -449 O ATOM 893 CB PHE A 122 -16.298 10.161 -25.575 1.00 49.34 C ANISOU 893 CB PHE A 122 7466 4632 6651 232 -1005 -522 C ATOM 894 CG PHE A 122 -14.896 10.678 -25.411 1.00 49.06 C ANISOU 894 CG PHE A 122 7457 4589 6594 308 -939 -533 C ATOM 895 CD1 PHE A 122 -14.563 11.514 -24.349 1.00 51.70 C ANISOU 895 CD1 PHE A 122 7723 4963 6957 382 -912 -491 C ATOM 896 CD2 PHE A 122 -13.884 10.259 -26.258 1.00 50.80 C ANISOU 896 CD2 PHE A 122 7771 4765 6767 303 -896 -587 C ATOM 897 CE1 PHE A 122 -13.241 11.936 -24.161 1.00 52.16 C ANISOU 897 CE1 PHE A 122 7804 5021 6995 442 -852 -499 C ATOM 898 CE2 PHE A 122 -12.570 10.685 -26.071 1.00 52.65 C ANISOU 898 CE2 PHE A 122 8019 5000 6984 371 -832 -594 C ATOM 899 CZ PHE A 122 -12.259 11.543 -25.044 1.00 49.55 C ANISOU 899 CZ PHE A 122 7556 4654 6618 437 -816 -547 C ATOM 900 N PRO A 123 -19.207 10.403 -27.393 1.00 53.13 N ANISOU 900 N PRO A 123 7905 5198 7085 45 -1225 -497 N ATOM 901 CA PRO A 123 -20.448 9.638 -27.636 1.00 53.49 C ANISOU 901 CA PRO A 123 7927 5254 7143 -53 -1288 -488 C ATOM 902 C PRO A 123 -20.201 8.118 -27.485 1.00 57.55 C ANISOU 902 C PRO A 123 8512 5687 7669 -106 -1236 -532 C ATOM 903 O PRO A 123 -19.036 7.712 -27.382 1.00 56.44 O ANISOU 903 O PRO A 123 8443 5480 7520 -62 -1155 -570 O ATOM 904 CB PRO A 123 -20.794 10.004 -29.108 1.00 54.25 C ANISOU 904 CB PRO A 123 8077 5378 7158 -127 -1373 -502 C ATOM 905 CG PRO A 123 -19.485 10.178 -29.747 1.00 57.51 C ANISOU 905 CG PRO A 123 8597 5749 7508 -98 -1320 -554 C ATOM 906 CD PRO A 123 -18.626 10.882 -28.670 1.00 52.93 C ANISOU 906 CD PRO A 123 7968 5170 6973 25 -1247 -532 C ATOM 907 N PRO A 124 -21.238 7.243 -27.536 1.00 57.35 N ANISOU 907 N PRO A 124 8473 5659 7659 -203 -1279 -527 N ATOM 908 CA PRO A 124 -20.978 5.784 -27.494 1.00 57.75 C ANISOU 908 CA PRO A 124 8610 5616 7716 -260 -1229 -572 C ATOM 909 C PRO A 124 -20.224 5.335 -28.750 1.00 63.02 C ANISOU 909 C PRO A 124 9422 6218 8304 -305 -1211 -648 C ATOM 910 O PRO A 124 -20.537 5.789 -29.847 1.00 63.56 O ANISOU 910 O PRO A 124 9521 6326 8303 -365 -1277 -662 O ATOM 911 CB PRO A 124 -22.392 5.179 -27.461 1.00 59.75 C ANISOU 911 CB PRO A 124 8814 5901 7989 -371 -1298 -546 C ATOM 912 CG PRO A 124 -23.288 6.292 -27.028 1.00 63.83 C ANISOU 912 CG PRO A 124 9186 6528 8539 -337 -1359 -477 C ATOM 913 CD PRO A 124 -22.681 7.494 -27.690 1.00 59.53 C ANISOU 913 CD PRO A 124 8658 6014 7947 -271 -1375 -481 C ATOM 914 N SER A 125 -19.198 4.506 -28.585 1.00 60.97 N ANISOU 914 N SER A 125 9249 5863 8054 -272 -1119 -695 N ATOM 915 CA SER A 125 -18.383 4.021 -29.705 1.00 62.31 C ANISOU 915 CA SER A 125 9558 5962 8155 -303 -1080 -775 C ATOM 916 C SER A 125 -19.170 3.066 -30.599 1.00 67.46 C ANISOU 916 C SER A 125 10295 6576 8759 -449 -1126 -820 C ATOM 917 O SER A 125 -20.213 2.546 -30.185 1.00 68.13 O ANISOU 917 O SER A 125 10336 6672 8879 -521 -1172 -788 O ATOM 918 CB SER A 125 -17.107 3.351 -29.195 1.00 67.03 C ANISOU 918 CB SER A 125 10211 6465 8791 -218 -965 -807 C ATOM 919 OG SER A 125 -17.352 2.074 -28.625 1.00 75.60 O ANISOU 919 OG SER A 125 11326 7466 9931 -251 -932 -811 O ATOM 920 N SER A 126 -18.694 2.870 -31.835 1.00 64.86 N ANISOU 920 N SER A 126 10088 6210 8344 -503 -1114 -893 N ATOM 921 CA SER A 126 -19.349 2.003 -32.804 1.00 66.46 C ANISOU 921 CA SER A 126 10393 6376 8484 -653 -1154 -946 C ATOM 922 C SER A 126 -19.376 0.570 -32.315 1.00 68.46 C ANISOU 922 C SER A 126 10709 6514 8788 -687 -1094 -977 C ATOM 923 O SER A 126 -20.433 -0.045 -32.346 1.00 68.74 O ANISOU 923 O SER A 126 10744 6550 8824 -802 -1153 -967 O ATOM 924 CB SER A 126 -18.687 2.093 -34.174 1.00 71.77 C ANISOU 924 CB SER A 126 11193 7027 9049 -696 -1135 -1025 C ATOM 925 OG SER A 126 -19.468 1.349 -35.100 1.00 83.73 O ANISOU 925 OG SER A 126 12799 8521 10492 -858 -1190 -1071 O ATOM 926 N GLU A 127 -18.232 0.084 -31.795 1.00 64.44 N ANISOU 926 N GLU A 127 10244 5912 8329 -583 -982 -1005 N ATOM 927 CA GLU A 127 -18.040 -1.251 -31.236 1.00 65.95 C ANISOU 927 CA GLU A 127 10499 5976 8581 -586 -911 -1028 C ATOM 928 C GLU A 127 -19.061 -1.467 -30.119 1.00 67.12 C ANISOU 928 C GLU A 127 10542 6158 8803 -611 -961 -948 C ATOM 929 O GLU A 127 -19.676 -2.529 -30.044 1.00 68.08 O ANISOU 929 O GLU A 127 10717 6213 8939 -708 -969 -961 O ATOM 930 CB GLU A 127 -16.600 -1.422 -30.654 1.00 67.72 C ANISOU 930 CB GLU A 127 10740 6126 8864 -435 -792 -1039 C ATOM 931 CG GLU A 127 -15.442 -1.079 -31.589 1.00 80.29 C ANISOU 931 CG GLU A 127 12411 7702 10395 -384 -728 -1110 C ATOM 932 CD GLU A 127 -14.097 -1.643 -31.172 0.10 97.02 C ANISOU 932 CD GLU A 127 14569 9721 12572 -261 -604 -1136 C ATOM 933 OE1 GLU A 127 -13.581 -1.236 -30.106 0.10 87.85 O ANISOU 933 OE1 GLU A 127 13307 8589 11482 -144 -578 -1069 O ATOM 934 OE2 GLU A 127 -13.548 -2.479 -31.925 0.10 89.54 O ANISOU 934 OE2 GLU A 127 13753 8668 11598 -281 -530 -1223 O ATOM 935 N GLU A 128 -19.218 -0.458 -29.246 1.00 59.68 N ANISOU 935 N GLU A 128 9453 5317 7905 -528 -990 -868 N ATOM 936 CA GLU A 128 -20.160 -0.506 -28.133 1.00 58.08 C ANISOU 936 CA GLU A 128 9135 5162 7769 -543 -1031 -790 C ATOM 937 C GLU A 128 -21.626 -0.662 -28.608 1.00 60.07 C ANISOU 937 C GLU A 128 9362 5475 7988 -695 -1134 -777 C ATOM 938 O GLU A 128 -22.352 -1.523 -28.097 1.00 57.57 O ANISOU 938 O GLU A 128 9040 5128 7708 -771 -1145 -758 O ATOM 939 CB GLU A 128 -19.997 0.722 -27.250 1.00 57.78 C ANISOU 939 CB GLU A 128 8958 5225 7772 -426 -1036 -720 C ATOM 940 CG GLU A 128 -20.703 0.539 -25.934 1.00 67.00 C ANISOU 940 CG GLU A 128 10019 6422 9016 -423 -1044 -648 C ATOM 941 CD GLU A 128 -20.487 1.580 -24.859 1.00 72.46 C ANISOU 941 CD GLU A 128 10584 7194 9752 -308 -1030 -583 C ATOM 942 OE1 GLU A 128 -20.232 2.773 -25.160 1.00 68.27 O ANISOU 942 OE1 GLU A 128 10009 6736 9193 -249 -1050 -577 O ATOM 943 OE2 GLU A 128 -20.682 1.189 -23.691 1.00 54.24 O ANISOU 943 OE2 GLU A 128 8223 4879 7507 -292 -1004 -536 O ATOM 944 N LEU A 129 -22.047 0.184 -29.569 1.00 56.75 N ANISOU 944 N LEU A 129 8924 5142 7497 -740 -1211 -782 N ATOM 945 CA LEU A 129 -23.403 0.157 -30.134 1.00 57.89 C ANISOU 945 CA LEU A 129 9033 5359 7601 -882 -1321 -763 C ATOM 946 C LEU A 129 -23.690 -1.151 -30.869 1.00 59.38 C ANISOU 946 C LEU A 129 9363 5457 7742 -1032 -1323 -830 C ATOM 947 O LEU A 129 -24.830 -1.608 -30.856 1.00 59.73 O ANISOU 947 O LEU A 129 9374 5535 7785 -1156 -1392 -805 O ATOM 948 CB LEU A 129 -23.645 1.348 -31.063 1.00 58.32 C ANISOU 948 CB LEU A 129 9049 5520 7589 -890 -1402 -751 C ATOM 949 CG LEU A 129 -23.588 2.734 -30.423 1.00 63.98 C ANISOU 949 CG LEU A 129 9625 6334 8349 -760 -1417 -681 C ATOM 950 CD1 LEU A 129 -23.245 3.775 -31.469 1.00 64.53 C ANISOU 950 CD1 LEU A 129 9719 6455 8342 -742 -1459 -692 C ATOM 951 CD2 LEU A 129 -24.894 3.070 -29.655 1.00 65.43 C ANISOU 951 CD2 LEU A 129 9647 6618 8594 -781 -1487 -597 C ATOM 952 N GLN A 130 -22.649 -1.765 -31.469 1.00 54.14 N ANISOU 952 N GLN A 130 8854 4676 7041 -1020 -1242 -915 N ATOM 953 CA GLN A 130 -22.723 -3.063 -32.168 1.00 54.52 C ANISOU 953 CA GLN A 130 9063 4609 7043 -1149 -1220 -994 C ATOM 954 C GLN A 130 -23.042 -4.201 -31.184 1.00 56.43 C ANISOU 954 C GLN A 130 9313 4764 7364 -1177 -1183 -975 C ATOM 955 O GLN A 130 -23.595 -5.228 -31.579 1.00 53.80 O ANISOU 955 O GLN A 130 9077 4364 7002 -1318 -1198 -1014 O ATOM 956 CB GLN A 130 -21.403 -3.374 -32.885 1.00 55.85 C ANISOU 956 CB GLN A 130 9383 4667 7170 -1096 -1119 -1089 C ATOM 957 CG GLN A 130 -21.245 -2.631 -34.222 1.00 60.55 C ANISOU 957 CG GLN A 130 10029 5325 7653 -1140 -1160 -1134 C ATOM 958 CD GLN A 130 -19.979 -3.033 -34.934 1.00 69.87 C ANISOU 958 CD GLN A 130 11362 6396 8791 -1098 -1050 -1235 C ATOM 959 OE1 GLN A 130 -18.892 -3.043 -34.350 1.00 71.68 O ANISOU 959 OE1 GLN A 130 11588 6567 9082 -953 -950 -1240 O ATOM 960 NE2 GLN A 130 -20.087 -3.381 -36.209 1.00 62.01 N ANISOU 960 NE2 GLN A 130 10501 5375 7685 -1227 -1064 -1316 N ATOM 961 N ALA A 131 -22.693 -3.987 -29.915 1.00 54.43 N ANISOU 961 N ALA A 131 8962 4514 7204 -1048 -1137 -913 N ATOM 962 CA ALA A 131 -22.912 -4.879 -28.774 1.00 55.72 C ANISOU 962 CA ALA A 131 9110 4609 7451 -1049 -1100 -874 C ATOM 963 C ALA A 131 -24.198 -4.478 -28.008 1.00 60.67 C ANISOU 963 C ALA A 131 9576 5364 8113 -1101 -1184 -784 C ATOM 964 O ALA A 131 -24.448 -4.995 -26.919 1.00 62.14 O ANISOU 964 O ALA A 131 9718 5525 8369 -1095 -1160 -735 O ATOM 965 CB ALA A 131 -21.698 -4.836 -27.847 1.00 54.82 C ANISOU 965 CB ALA A 131 8984 4433 7411 -877 -1000 -856 C ATOM 966 N ASN A 132 -25.042 -3.612 -28.616 1.00 57.04 N ANISOU 966 N ASN A 132 9031 5038 7603 -1161 -1282 -762 N ATOM 967 CA ASN A 132 -26.291 -3.081 -28.041 1.00 57.59 C ANISOU 967 CA ASN A 132 8932 5245 7704 -1202 -1365 -679 C ATOM 968 C ASN A 132 -26.083 -2.446 -26.615 1.00 61.68 C ANISOU 968 C ASN A 132 9312 5813 8311 -1060 -1321 -606 C ATOM 969 O ASN A 132 -26.894 -2.623 -25.693 1.00 62.80 O ANISOU 969 O ASN A 132 9353 6003 8505 -1092 -1337 -546 O ATOM 970 CB ASN A 132 -27.409 -4.117 -28.072 1.00 60.91 C ANISOU 970 CB ASN A 132 9372 5655 8117 -1379 -1414 -673 C ATOM 971 CG ASN A 132 -28.795 -3.580 -27.836 1.00 81.74 C ANISOU 971 CG ASN A 132 11840 8448 10767 -1450 -1513 -598 C ATOM 972 OD1 ASN A 132 -29.513 -4.073 -26.958 1.00 78.98 O ANISOU 972 OD1 ASN A 132 11422 8117 10469 -1503 -1516 -551 O ATOM 973 ND2 ASN A 132 -29.210 -2.585 -28.619 1.00 66.74 N ANISOU 973 ND2 ASN A 132 9871 6664 8822 -1457 -1596 -583 N ATOM 974 N LYS A 133 -24.977 -1.698 -26.467 1.00 56.09 N ANISOU 974 N LYS A 133 8604 5096 7613 -910 -1265 -613 N ATOM 975 CA LYS A 133 -24.608 -0.972 -25.248 1.00 54.70 C ANISOU 975 CA LYS A 133 8314 4966 7503 -772 -1222 -554 C ATOM 976 C LYS A 133 -24.275 0.453 -25.636 1.00 58.67 C ANISOU 976 C LYS A 133 8755 5556 7980 -678 -1245 -546 C ATOM 977 O LYS A 133 -23.953 0.714 -26.791 1.00 57.22 O ANISOU 977 O LYS A 133 8646 5366 7730 -697 -1269 -594 O ATOM 978 CB LYS A 133 -23.422 -1.622 -24.512 1.00 56.26 C ANISOU 978 CB LYS A 133 8587 5046 7745 -681 -1118 -566 C ATOM 979 CG LYS A 133 -23.782 -2.865 -23.709 1.00 65.01 C ANISOU 979 CG LYS A 133 9724 6076 8900 -749 -1091 -545 C ATOM 980 CD LYS A 133 -22.668 -3.280 -22.765 1.00 73.57 C ANISOU 980 CD LYS A 133 10842 7071 10040 -638 -999 -529 C ATOM 981 CE LYS A 133 -22.765 -4.768 -22.440 1.00 94.71 C ANISOU 981 CE LYS A 133 13617 9620 12748 -714 -966 -534 C ATOM 982 NZ LYS A 133 -21.825 -5.192 -21.358 1.00 94.25 N ANISOU 982 NZ LYS A 133 13573 9485 12754 -610 -888 -496 N ATOM 983 N ALA A 134 -24.391 1.391 -24.683 1.00 56.85 N ANISOU 983 N ALA A 134 8393 5410 7798 -584 -1239 -486 N ATOM 984 CA ALA A 134 -24.132 2.791 -24.945 1.00 56.56 C ANISOU 984 CA ALA A 134 8294 5452 7742 -493 -1260 -472 C ATOM 985 C ALA A 134 -23.637 3.481 -23.653 1.00 61.75 C ANISOU 985 C ALA A 134 8866 6139 8459 -365 -1200 -428 C ATOM 986 O ALA A 134 -24.258 3.379 -22.592 1.00 60.49 O ANISOU 986 O ALA A 134 8614 6017 8352 -367 -1191 -380 O ATOM 987 CB ALA A 134 -25.392 3.465 -25.487 1.00 57.93 C ANISOU 987 CB ALA A 134 8372 5738 7899 -558 -1364 -439 C ATOM 988 N THR A 135 -22.460 4.095 -23.740 1.00 57.83 N ANISOU 988 N THR A 135 8409 5621 7945 -262 -1153 -448 N ATOM 989 CA THR A 135 -21.847 4.804 -22.631 1.00 55.90 C ANISOU 989 CA THR A 135 8099 5401 7739 -147 -1097 -412 C ATOM 990 C THR A 135 -21.351 6.143 -23.130 1.00 58.75 C ANISOU 990 C THR A 135 8446 5812 8065 -70 -1111 -417 C ATOM 991 O THR A 135 -20.623 6.210 -24.122 1.00 57.91 O ANISOU 991 O THR A 135 8430 5670 7905 -67 -1109 -463 O ATOM 992 CB THR A 135 -20.760 3.959 -21.935 1.00 54.79 C ANISOU 992 CB THR A 135 8025 5168 7625 -101 -1011 -421 C ATOM 993 OG1 THR A 135 -21.326 2.699 -21.618 1.00 55.90 O ANISOU 993 OG1 THR A 135 8191 5255 7794 -186 -1009 -416 O ATOM 994 CG2 THR A 135 -20.261 4.594 -20.647 1.00 47.46 C ANISOU 994 CG2 THR A 135 7022 4277 6735 -2 -960 -375 C ATOM 995 N LEU A 136 -21.792 7.203 -22.464 1.00 56.12 N ANISOU 995 N LEU A 136 8003 5561 7760 -15 -1123 -371 N ATOM 996 CA LEU A 136 -21.335 8.556 -22.731 1.00 56.81 C ANISOU 996 CA LEU A 136 8072 5692 7822 65 -1130 -367 C ATOM 997 C LEU A 136 -20.271 8.833 -21.689 1.00 58.88 C ANISOU 997 C LEU A 136 8331 5936 8105 157 -1048 -358 C ATOM 998 O LEU A 136 -20.458 8.504 -20.515 1.00 56.62 O ANISOU 998 O LEU A 136 7991 5656 7865 168 -1010 -327 O ATOM 999 CB LEU A 136 -22.470 9.573 -22.603 1.00 57.49 C ANISOU 999 CB LEU A 136 8042 5871 7932 74 -1189 -323 C ATOM 1000 CG LEU A 136 -23.589 9.519 -23.649 1.00 64.46 C ANISOU 1000 CG LEU A 136 8905 6793 8795 -12 -1286 -317 C ATOM 1001 CD1 LEU A 136 -24.609 10.565 -23.352 1.00 64.42 C ANISOU 1001 CD1 LEU A 136 8770 6878 8830 23 -1331 -265 C ATOM 1002 CD2 LEU A 136 -23.082 9.820 -25.036 1.00 69.12 C ANISOU 1002 CD2 LEU A 136 9589 7363 9310 -32 -1328 -352 C ATOM 1003 N VAL A 137 -19.123 9.344 -22.123 1.00 55.63 N ANISOU 1003 N VAL A 137 7981 5503 7652 213 -1020 -384 N ATOM 1004 CA VAL A 137 -18.033 9.666 -21.190 1.00 53.73 C ANISOU 1004 CA VAL A 137 7736 5255 7424 296 -948 -372 C ATOM 1005 C VAL A 137 -17.676 11.123 -21.308 1.00 52.85 C ANISOU 1005 C VAL A 137 7604 5193 7285 359 -955 -364 C ATOM 1006 O VAL A 137 -17.426 11.628 -22.395 1.00 49.86 O ANISOU 1006 O VAL A 137 7274 4815 6856 354 -987 -389 O ATOM 1007 CB VAL A 137 -16.799 8.730 -21.321 1.00 57.73 C ANISOU 1007 CB VAL A 137 8333 5681 7919 309 -888 -404 C ATOM 1008 CG1 VAL A 137 -15.562 9.321 -20.629 1.00 56.79 C ANISOU 1008 CG1 VAL A 137 8208 5573 7797 395 -827 -390 C ATOM 1009 CG2 VAL A 137 -17.124 7.374 -20.732 1.00 58.69 C ANISOU 1009 CG2 VAL A 137 8463 5751 8087 265 -867 -393 C ATOM 1010 N CYS A 138 -17.685 11.788 -20.173 1.00 52.27 N ANISOU 1010 N CYS A 138 7461 5159 7240 411 -924 -330 N ATOM 1011 CA CYS A 138 -17.349 13.178 -20.004 1.00 51.53 C ANISOU 1011 CA CYS A 138 7345 5105 7127 472 -919 -319 C ATOM 1012 C CYS A 138 -16.022 13.171 -19.276 1.00 53.75 C ANISOU 1012 C CYS A 138 7655 5371 7398 520 -848 -319 C ATOM 1013 O CYS A 138 -15.979 12.941 -18.072 1.00 55.04 O ANISOU 1013 O CYS A 138 7775 5544 7593 534 -807 -292 O ATOM 1014 CB CYS A 138 -18.437 13.870 -19.186 1.00 53.57 C ANISOU 1014 CB CYS A 138 7505 5420 7430 489 -931 -284 C ATOM 1015 SG CYS A 138 -18.414 15.680 -19.259 0.90 58.14 S ANISOU 1015 SG CYS A 138 8061 6039 7991 556 -943 -273 S ATOM 1016 N LEU A 139 -14.924 13.361 -20.016 1.00 49.36 N ANISOU 1016 N LEU A 139 7169 4792 6794 538 -834 -347 N ATOM 1017 CA LEU A 139 -13.593 13.456 -19.436 1.00 48.14 C ANISOU 1017 CA LEU A 139 7034 4633 6625 583 -773 -343 C ATOM 1018 C LEU A 139 -13.359 14.889 -18.948 1.00 51.84 C ANISOU 1018 C LEU A 139 7473 5150 7072 625 -765 -326 C ATOM 1019 O LEU A 139 -13.593 15.838 -19.691 1.00 51.52 O ANISOU 1019 O LEU A 139 7448 5126 7002 628 -802 -335 O ATOM 1020 CB LEU A 139 -12.521 13.016 -20.451 1.00 48.37 C ANISOU 1020 CB LEU A 139 7144 4622 6613 582 -754 -382 C ATOM 1021 CG LEU A 139 -11.056 13.171 -19.973 1.00 53.83 C ANISOU 1021 CG LEU A 139 7848 5318 7288 631 -693 -376 C ATOM 1022 CD1 LEU A 139 -10.676 12.113 -18.856 1.00 53.46 C ANISOU 1022 CD1 LEU A 139 7774 5247 7291 647 -647 -345 C ATOM 1023 CD2 LEU A 139 -10.092 13.117 -21.151 1.00 57.38 C ANISOU 1023 CD2 LEU A 139 8369 5746 7688 632 -678 -419 C ATOM 1024 N ILE A 140 -12.911 15.048 -17.693 1.00 47.08 N ANISOU 1024 N ILE A 140 6835 4570 6483 652 -718 -298 N ATOM 1025 CA ILE A 140 -12.674 16.346 -17.066 1.00 46.65 C ANISOU 1025 CA ILE A 140 6760 4557 6407 684 -702 -284 C ATOM 1026 C ILE A 140 -11.211 16.371 -16.602 1.00 50.59 C ANISOU 1026 C ILE A 140 7283 5064 6874 704 -652 -277 C ATOM 1027 O ILE A 140 -10.821 15.603 -15.723 1.00 49.18 O ANISOU 1027 O ILE A 140 7083 4885 6718 705 -618 -252 O ATOM 1028 CB ILE A 140 -13.749 16.625 -15.952 1.00 49.27 C ANISOU 1028 CB ILE A 140 7019 4921 6781 685 -695 -259 C ATOM 1029 CG1 ILE A 140 -15.171 16.342 -16.496 1.00 50.78 C ANISOU 1029 CG1 ILE A 140 7176 5108 7011 659 -747 -262 C ATOM 1030 CG2 ILE A 140 -13.680 18.059 -15.433 1.00 49.14 C ANISOU 1030 CG2 ILE A 140 6992 4938 6743 716 -678 -254 C ATOM 1031 CD1 ILE A 140 -16.132 15.809 -15.510 1.00 59.70 C ANISOU 1031 CD1 ILE A 140 8236 6256 8191 640 -733 -238 C ATOM 1032 N SER A 141 -10.381 17.230 -17.206 1.00 47.86 N ANISOU 1032 N SER A 141 6980 4729 6477 717 -651 -292 N ATOM 1033 CA SER A 141 -8.980 17.181 -16.836 1.00 46.87 C ANISOU 1033 CA SER A 141 6868 4620 6323 731 -607 -283 C ATOM 1034 C SER A 141 -8.372 18.537 -16.662 1.00 51.61 C ANISOU 1034 C SER A 141 7482 5257 6871 739 -596 -281 C ATOM 1035 O SER A 141 -8.993 19.550 -16.989 1.00 53.58 O ANISOU 1035 O SER A 141 7744 5509 7106 739 -624 -291 O ATOM 1036 CB SER A 141 -8.200 16.313 -17.830 1.00 48.17 C ANISOU 1036 CB SER A 141 7076 4751 6477 732 -598 -307 C ATOM 1037 OG SER A 141 -7.955 16.991 -19.052 1.00 54.91 O ANISOU 1037 OG SER A 141 7981 5603 7280 723 -619 -341 O ATOM 1038 N ASP A 142 -7.176 18.577 -16.066 1.00 50.22 N ANISOU 1038 N ASP A 142 7302 5111 6669 744 -558 -262 N ATOM 1039 CA ASP A 142 -6.400 19.822 -15.845 1.00 50.20 C ANISOU 1039 CA ASP A 142 7317 5148 6607 739 -544 -258 C ATOM 1040 C ASP A 142 -7.103 20.877 -14.988 1.00 49.11 C ANISOU 1040 C ASP A 142 7168 5026 6465 734 -544 -251 C ATOM 1041 O ASP A 142 -7.028 22.069 -15.268 1.00 47.23 O ANISOU 1041 O ASP A 142 6965 4792 6187 730 -551 -263 O ATOM 1042 CB ASP A 142 -5.931 20.437 -17.188 1.00 52.35 C ANISOU 1042 CB ASP A 142 7648 5412 6831 733 -561 -289 C ATOM 1043 CG ASP A 142 -5.167 19.454 -18.047 1.00 64.82 C ANISOU 1043 CG ASP A 142 9243 6977 8408 737 -548 -306 C ATOM 1044 OD1 ASP A 142 -4.462 18.597 -17.480 1.00 68.03 O ANISOU 1044 OD1 ASP A 142 9618 7394 8837 751 -514 -285 O ATOM 1045 OD2 ASP A 142 -5.316 19.507 -19.281 1.00 71.93 O ANISOU 1045 OD2 ASP A 142 10190 7853 9287 727 -571 -338 O ATOM 1046 N PHE A 143 -7.789 20.448 -13.963 1.00 46.86 N ANISOU 1046 N PHE A 143 6837 4747 6220 734 -531 -231 N ATOM 1047 CA PHE A 143 -8.438 21.415 -13.093 1.00 46.80 C ANISOU 1047 CA PHE A 143 6818 4756 6209 730 -518 -230 C ATOM 1048 C PHE A 143 -7.834 21.451 -11.704 1.00 50.41 C ANISOU 1048 C PHE A 143 7253 5257 6642 708 -477 -202 C ATOM 1049 O PHE A 143 -7.295 20.472 -11.211 1.00 51.16 O ANISOU 1049 O PHE A 143 7321 5368 6747 700 -465 -172 O ATOM 1050 CB PHE A 143 -9.971 21.249 -13.038 1.00 48.35 C ANISOU 1050 CB PHE A 143 6977 4929 6463 743 -536 -237 C ATOM 1051 CG PHE A 143 -10.462 19.914 -12.542 1.00 48.64 C ANISOU 1051 CG PHE A 143 6965 4964 6550 733 -532 -217 C ATOM 1052 CD1 PHE A 143 -10.726 18.880 -13.432 1.00 49.39 C ANISOU 1052 CD1 PHE A 143 7062 5025 6678 732 -563 -223 C ATOM 1053 CD2 PHE A 143 -10.718 19.707 -11.182 1.00 48.09 C ANISOU 1053 CD2 PHE A 143 6855 4923 6492 717 -497 -193 C ATOM 1054 CE1 PHE A 143 -11.210 17.642 -12.970 1.00 49.09 C ANISOU 1054 CE1 PHE A 143 6987 4977 6686 716 -560 -204 C ATOM 1055 CE2 PHE A 143 -11.227 18.490 -10.729 1.00 48.97 C ANISOU 1055 CE2 PHE A 143 6927 5031 6649 702 -495 -171 C ATOM 1056 CZ PHE A 143 -11.447 17.454 -11.624 1.00 47.11 C ANISOU 1056 CZ PHE A 143 6696 4756 6449 702 -527 -175 C ATOM 1057 N TYR A 144 -7.913 22.617 -11.103 1.00 47.75 N ANISOU 1057 N TYR A 144 6935 4937 6271 698 -456 -211 N ATOM 1058 CA TYR A 144 -7.485 22.918 -9.753 1.00 47.79 C ANISOU 1058 CA TYR A 144 6931 4986 6240 664 -417 -191 C ATOM 1059 C TYR A 144 -8.268 24.149 -9.272 1.00 52.19 C ANISOU 1059 C TYR A 144 7509 5533 6786 665 -394 -219 C ATOM 1060 O TYR A 144 -8.283 25.142 -9.981 1.00 50.70 O ANISOU 1060 O TYR A 144 7368 5317 6580 680 -406 -245 O ATOM 1061 CB TYR A 144 -5.979 23.183 -9.648 1.00 46.97 C ANISOU 1061 CB TYR A 144 6852 4923 6070 634 -408 -173 C ATOM 1062 CG TYR A 144 -5.558 23.381 -8.208 1.00 47.27 C ANISOU 1062 CG TYR A 144 6879 5016 6066 588 -374 -146 C ATOM 1063 CD1 TYR A 144 -5.301 22.289 -7.377 1.00 49.32 C ANISOU 1063 CD1 TYR A 144 7090 5309 6342 573 -368 -100 C ATOM 1064 CD2 TYR A 144 -5.439 24.658 -7.666 1.00 48.78 C ANISOU 1064 CD2 TYR A 144 7114 5222 6199 555 -349 -166 C ATOM 1065 CE1 TYR A 144 -4.943 22.469 -6.042 1.00 47.21 C ANISOU 1065 CE1 TYR A 144 6814 5097 6027 521 -342 -71 C ATOM 1066 CE2 TYR A 144 -5.063 24.848 -6.336 1.00 48.87 C ANISOU 1066 CE2 TYR A 144 7123 5286 6161 500 -318 -145 C ATOM 1067 CZ TYR A 144 -4.813 23.755 -5.534 1.00 47.96 C ANISOU 1067 CZ TYR A 144 6955 5212 6056 481 -317 -96 C ATOM 1068 OH TYR A 144 -4.437 23.963 -4.240 1.00 49.39 O ANISOU 1068 OH TYR A 144 7136 5451 6180 418 -291 -71 O ATOM 1069 N PRO A 145 -8.917 24.141 -8.083 1.00 49.82 N ANISOU 1069 N PRO A 145 7181 5254 6496 650 -357 -216 N ATOM 1070 CA PRO A 145 -9.021 23.063 -7.086 1.00 49.41 C ANISOU 1070 CA PRO A 145 7078 5236 6461 625 -339 -181 C ATOM 1071 C PRO A 145 -9.640 21.762 -7.634 1.00 54.71 C ANISOU 1071 C PRO A 145 7703 5882 7201 648 -371 -166 C ATOM 1072 O PRO A 145 -10.337 21.774 -8.654 1.00 54.75 O ANISOU 1072 O PRO A 145 7707 5848 7249 682 -401 -189 O ATOM 1073 CB PRO A 145 -9.889 23.703 -5.990 1.00 50.23 C ANISOU 1073 CB PRO A 145 7173 5352 6560 610 -290 -200 C ATOM 1074 CG PRO A 145 -9.606 25.158 -6.122 1.00 54.14 C ANISOU 1074 CG PRO A 145 7731 5833 7008 611 -273 -236 C ATOM 1075 CD PRO A 145 -9.612 25.348 -7.602 1.00 50.06 C ANISOU 1075 CD PRO A 145 7234 5269 6516 656 -322 -249 C ATOM 1076 N GLY A 146 -9.388 20.669 -6.918 1.00 49.70 N ANISOU 1076 N GLY A 146 7035 5272 6576 623 -364 -125 N ATOM 1077 CA GLY A 146 -9.861 19.323 -7.238 1.00 48.76 C ANISOU 1077 CA GLY A 146 6881 5127 6519 632 -387 -105 C ATOM 1078 C GLY A 146 -11.279 18.991 -6.832 1.00 53.23 C ANISOU 1078 C GLY A 146 7404 5688 7134 627 -378 -111 C ATOM 1079 O GLY A 146 -11.509 18.010 -6.137 1.00 53.48 O ANISOU 1079 O GLY A 146 7404 5731 7187 600 -370 -77 O ATOM 1080 N ALA A 147 -12.238 19.771 -7.279 1.00 51.64 N ANISOU 1080 N ALA A 147 7195 5470 6953 652 -381 -149 N ATOM 1081 CA ALA A 147 -13.656 19.541 -6.994 1.00 52.10 C ANISOU 1081 CA ALA A 147 7200 5531 7064 651 -372 -156 C ATOM 1082 C ALA A 147 -14.474 20.003 -8.174 1.00 53.15 C ANISOU 1082 C ALA A 147 7327 5631 7237 692 -410 -187 C ATOM 1083 O ALA A 147 -14.275 21.125 -8.640 1.00 49.74 O ANISOU 1083 O ALA A 147 6929 5185 6783 722 -413 -212 O ATOM 1084 CB ALA A 147 -14.082 20.337 -5.757 1.00 54.03 C ANISOU 1084 CB ALA A 147 7429 5814 7286 635 -311 -167 C ATOM 1085 N VAL A 148 -15.377 19.139 -8.671 1.00 50.99 N ANISOU 1085 N VAL A 148 7011 5343 7019 688 -442 -181 N ATOM 1086 CA VAL A 148 -16.281 19.468 -9.778 1.00 50.46 C ANISOU 1086 CA VAL A 148 6927 5254 6992 718 -488 -201 C ATOM 1087 C VAL A 148 -17.673 18.990 -9.444 1.00 57.31 C ANISOU 1087 C VAL A 148 7715 6143 7917 704 -486 -193 C ATOM 1088 O VAL A 148 -17.838 18.022 -8.707 1.00 59.09 O ANISOU 1088 O VAL A 148 7913 6385 8154 662 -466 -171 O ATOM 1089 CB VAL A 148 -15.844 18.910 -11.171 1.00 53.06 C ANISOU 1089 CB VAL A 148 7298 5544 7318 718 -548 -205 C ATOM 1090 CG1 VAL A 148 -14.872 19.848 -11.898 1.00 51.99 C ANISOU 1090 CG1 VAL A 148 7229 5390 7133 745 -560 -222 C ATOM 1091 CG2 VAL A 148 -15.334 17.475 -11.090 1.00 51.77 C ANISOU 1091 CG2 VAL A 148 7145 5366 7159 682 -551 -184 C ATOM 1092 N THR A 149 -18.664 19.613 -10.051 1.00 54.72 N ANISOU 1092 N THR A 149 7350 5814 7628 736 -512 -206 N ATOM 1093 CA THR A 149 -20.073 19.259 -9.947 1.00 55.12 C ANISOU 1093 CA THR A 149 7312 5891 7739 728 -520 -198 C ATOM 1094 C THR A 149 -20.458 18.971 -11.381 1.00 56.83 C ANISOU 1094 C THR A 149 7531 6085 7978 729 -601 -196 C ATOM 1095 O THR A 149 -20.209 19.798 -12.264 1.00 55.67 O ANISOU 1095 O THR A 149 7421 5914 7816 767 -637 -208 O ATOM 1096 CB THR A 149 -20.863 20.410 -9.289 1.00 67.15 C ANISOU 1096 CB THR A 149 8785 7443 9288 773 -471 -212 C ATOM 1097 OG1 THR A 149 -20.501 20.456 -7.909 1.00 74.08 O ANISOU 1097 OG1 THR A 149 9667 8346 10134 751 -393 -215 O ATOM 1098 CG2 THR A 149 -22.362 20.229 -9.384 1.00 67.08 C ANISOU 1098 CG2 THR A 149 8672 7467 9349 777 -485 -203 C ATOM 1099 N VAL A 150 -20.997 17.785 -11.619 1.00 54.15 N ANISOU 1099 N VAL A 150 7161 5749 7666 678 -633 -181 N ATOM 1100 CA VAL A 150 -21.395 17.318 -12.953 1.00 55.54 C ANISOU 1100 CA VAL A 150 7343 5906 7855 657 -712 -180 C ATOM 1101 C VAL A 150 -22.901 17.057 -12.957 1.00 62.37 C ANISOU 1101 C VAL A 150 8105 6813 8779 635 -737 -164 C ATOM 1102 O VAL A 150 -23.441 16.526 -11.980 1.00 64.17 O ANISOU 1102 O VAL A 150 8275 7073 9032 603 -696 -151 O ATOM 1103 CB VAL A 150 -20.588 16.071 -13.437 1.00 57.78 C ANISOU 1103 CB VAL A 150 7697 6146 8111 607 -733 -183 C ATOM 1104 CG1 VAL A 150 -20.978 15.653 -14.858 1.00 57.20 C ANISOU 1104 CG1 VAL A 150 7643 6051 8039 577 -811 -190 C ATOM 1105 CG2 VAL A 150 -19.082 16.308 -13.342 1.00 56.87 C ANISOU 1105 CG2 VAL A 150 7666 6001 7943 631 -702 -194 C ATOM 1106 N ALA A 151 -23.554 17.442 -14.056 1.00 56.50 N ANISOU 1106 N ALA A 151 7339 6074 8054 648 -807 -160 N ATOM 1107 CA ALA A 151 -24.964 17.289 -14.292 1.00 56.74 C ANISOU 1107 CA ALA A 151 7267 6151 8141 629 -848 -139 C ATOM 1108 C ALA A 151 -25.153 16.934 -15.752 1.00 61.02 C ANISOU 1108 C ALA A 151 7838 6677 8670 592 -944 -134 C ATOM 1109 O ALA A 151 -24.628 17.607 -16.644 1.00 59.59 O ANISOU 1109 O ALA A 151 7720 6467 8456 624 -982 -143 O ATOM 1110 CB ALA A 151 -25.692 18.593 -13.989 1.00 58.09 C ANISOU 1110 CB ALA A 151 7360 6356 8355 707 -829 -131 C ATOM 1111 N TRP A 152 -25.917 15.870 -16.002 1.00 57.50 N ANISOU 1111 N TRP A 152 7352 6252 8244 514 -983 -121 N ATOM 1112 CA TRP A 152 -26.217 15.458 -17.358 1.00 56.21 C ANISOU 1112 CA TRP A 152 7214 6081 8063 461 -1076 -118 C ATOM 1113 C TRP A 152 -27.634 15.811 -17.724 1.00 61.28 C ANISOU 1113 C TRP A 152 7737 6789 8756 457 -1137 -83 C ATOM 1114 O TRP A 152 -28.514 15.777 -16.867 1.00 61.05 O ANISOU 1114 O TRP A 152 7599 6814 8782 460 -1104 -64 O ATOM 1115 CB TRP A 152 -26.001 13.962 -17.511 1.00 53.23 C ANISOU 1115 CB TRP A 152 6892 5670 7663 365 -1083 -131 C ATOM 1116 CG TRP A 152 -24.564 13.542 -17.472 1.00 52.69 C ANISOU 1116 CG TRP A 152 6946 5530 7545 371 -1040 -162 C ATOM 1117 CD1 TRP A 152 -23.818 13.258 -16.363 1.00 55.09 C ANISOU 1117 CD1 TRP A 152 7272 5813 7846 389 -961 -165 C ATOM 1118 CD2 TRP A 152 -23.755 13.190 -18.603 1.00 52.21 C ANISOU 1118 CD2 TRP A 152 6995 5413 7429 346 -1075 -190 C ATOM 1119 NE1 TRP A 152 -22.594 12.739 -16.733 1.00 53.80 N ANISOU 1119 NE1 TRP A 152 7218 5583 7638 384 -946 -190 N ATOM 1120 CE2 TRP A 152 -22.520 12.714 -18.106 1.00 55.74 C ANISOU 1120 CE2 TRP A 152 7521 5806 7852 361 -1010 -210 C ATOM 1121 CE3 TRP A 152 -23.956 13.232 -19.996 1.00 53.57 C ANISOU 1121 CE3 TRP A 152 7207 5580 7569 310 -1154 -200 C ATOM 1122 CZ2 TRP A 152 -21.483 12.302 -18.956 1.00 54.64 C ANISOU 1122 CZ2 TRP A 152 7492 5606 7663 351 -1014 -243 C ATOM 1123 CZ3 TRP A 152 -22.927 12.835 -20.830 1.00 54.74 C ANISOU 1123 CZ3 TRP A 152 7474 5667 7659 292 -1156 -237 C ATOM 1124 CH2 TRP A 152 -21.713 12.362 -20.309 1.00 54.81 C ANISOU 1124 CH2 TRP A 152 7553 5621 7651 315 -1083 -260 C ATOM 1125 N LYS A 153 -27.854 16.149 -19.003 1.00 59.63 N ANISOU 1125 N LYS A 153 7546 6582 8530 449 -1228 -72 N ATOM 1126 CA LYS A 153 -29.175 16.420 -19.560 1.00 61.55 C ANISOU 1126 CA LYS A 153 7678 6893 8817 437 -1307 -29 C ATOM 1127 C LYS A 153 -29.397 15.625 -20.851 1.00 69.52 C ANISOU 1127 C LYS A 153 8732 7901 9783 334 -1407 -26 C ATOM 1128 O LYS A 153 -28.460 15.379 -21.611 1.00 67.68 O ANISOU 1128 O LYS A 153 8626 7609 9481 306 -1423 -57 O ATOM 1129 CB LYS A 153 -29.394 17.914 -19.811 1.00 64.23 C ANISOU 1129 CB LYS A 153 7975 7245 9185 542 -1328 -4 C ATOM 1130 CG LYS A 153 -29.534 18.738 -18.525 1.00 85.66 C ANISOU 1130 CG LYS A 153 10620 9973 11954 638 -1233 -5 C ATOM 1131 CD LYS A 153 -28.929 20.148 -18.639 1.00 98.92 C ANISOU 1131 CD LYS A 153 12349 11611 13627 744 -1216 -9 C ATOM 1132 CE LYS A 153 -29.854 21.177 -19.254 1.00115.96 C ANISOU 1132 CE LYS A 153 14422 13799 15838 810 -1284 39 C ATOM 1133 NZ LYS A 153 -29.366 22.567 -19.027 1.00126.05 N ANISOU 1133 NZ LYS A 153 15740 15031 17124 921 -1243 34 N ATOM 1134 N ALA A 154 -30.648 15.223 -21.083 1.00 70.19 N ANISOU 1134 N ALA A 154 8710 8054 9904 272 -1469 11 N ATOM 1135 CA ALA A 154 -31.106 14.551 -22.297 1.00 71.45 C ANISOU 1135 CA ALA A 154 8892 8232 10025 163 -1574 22 C ATOM 1136 C ALA A 154 -32.192 15.494 -22.809 1.00 76.57 C ANISOU 1136 C ALA A 154 9415 8958 10720 202 -1659 84 C ATOM 1137 O ALA A 154 -33.236 15.619 -22.161 1.00 75.43 O ANISOU 1137 O ALA A 154 9123 8886 10650 219 -1650 121 O ATOM 1138 CB ALA A 154 -31.691 13.183 -21.955 1.00 72.63 C ANISOU 1138 CB ALA A 154 9011 8401 10182 45 -1571 18 C ATOM 1139 N ASP A 155 -31.904 16.235 -23.900 1.00 74.91 N ANISOU 1139 N ASP A 155 9262 8733 10469 227 -1732 97 N ATOM 1140 CA ASP A 155 -32.803 17.251 -24.469 1.00 77.40 C ANISOU 1140 CA ASP A 155 9472 9110 10826 279 -1819 164 C ATOM 1141 C ASP A 155 -33.332 18.201 -23.387 1.00 84.15 C ANISOU 1141 C ASP A 155 10196 9997 11780 407 -1753 192 C ATOM 1142 O ASP A 155 -34.534 18.188 -23.080 1.00 86.16 O ANISOU 1142 O ASP A 155 10294 10334 12108 407 -1776 238 O ATOM 1143 CB ASP A 155 -33.966 16.618 -25.244 1.00 81.04 C ANISOU 1143 CB ASP A 155 9850 9653 11288 165 -1934 211 C ATOM 1144 CG ASP A 155 -33.574 16.018 -26.565 1.00 94.64 C ANISOU 1144 CG ASP A 155 11700 11350 12908 48 -2021 193 C ATOM 1145 OD1 ASP A 155 -32.782 16.656 -27.295 1.00 96.82 O ANISOU 1145 OD1 ASP A 155 12083 11578 13128 83 -2044 183 O ATOM 1146 OD2 ASP A 155 -34.102 14.946 -26.898 1.00 99.95 O ANISOU 1146 OD2 ASP A 155 12364 12056 13555 -84 -2069 191 O ATOM 1147 N SER A 156 -32.410 18.947 -22.747 1.00 79.44 N ANISOU 1147 N SER A 156 9665 9335 11182 508 -1663 158 N ATOM 1148 CA SER A 156 -32.664 19.921 -21.673 1.00 79.58 C ANISOU 1148 CA SER A 156 9596 9361 11279 634 -1579 167 C ATOM 1149 C SER A 156 -33.281 19.306 -20.390 1.00 83.32 C ANISOU 1149 C SER A 156 9964 9883 11812 620 -1493 156 C ATOM 1150 O SER A 156 -33.560 20.038 -19.439 1.00 83.83 O ANISOU 1150 O SER A 156 9953 9959 11939 716 -1414 157 O ATOM 1151 CB SER A 156 -33.496 21.105 -22.181 1.00 84.35 C ANISOU 1151 CB SER A 156 10102 10001 11945 723 -1649 232 C ATOM 1152 OG SER A 156 -34.866 20.789 -22.385 1.00 96.16 O ANISOU 1152 OG SER A 156 11441 11594 13503 687 -1718 290 O ATOM 1153 N SER A 157 -33.462 17.979 -20.343 1.00 78.34 N ANISOU 1153 N SER A 157 9336 9275 11156 499 -1503 144 N ATOM 1154 CA SER A 157 -34.042 17.353 -19.167 1.00 77.80 C ANISOU 1154 CA SER A 157 9173 9253 11135 472 -1426 138 C ATOM 1155 C SER A 157 -33.012 16.606 -18.326 1.00 79.46 C ANISOU 1155 C SER A 157 9492 9400 11297 437 -1331 83 C ATOM 1156 O SER A 157 -32.367 15.658 -18.802 1.00 77.10 O ANISOU 1156 O SER A 157 9306 9055 10935 349 -1355 57 O ATOM 1157 CB SER A 157 -35.236 16.477 -19.527 1.00 82.82 C ANISOU 1157 CB SER A 157 9699 9974 11794 363 -1500 177 C ATOM 1158 OG SER A 157 -36.355 17.284 -19.860 1.00 95.23 O ANISOU 1158 OG SER A 157 11121 11625 13438 420 -1561 238 O ATOM 1159 N PRO A 158 -32.873 17.042 -17.047 1.00 75.37 N ANISOU 1159 N PRO A 158 8941 8883 10813 508 -1220 66 N ATOM 1160 CA PRO A 158 -31.903 16.411 -16.141 1.00 74.42 C ANISOU 1160 CA PRO A 158 8915 8711 10651 481 -1130 23 C ATOM 1161 C PRO A 158 -31.977 14.893 -16.026 1.00 77.57 C ANISOU 1161 C PRO A 158 9338 9110 11024 353 -1137 19 C ATOM 1162 O PRO A 158 -33.051 14.316 -15.843 1.00 77.92 O ANISOU 1162 O PRO A 158 9276 9223 11108 288 -1155 45 O ATOM 1163 CB PRO A 158 -32.196 17.089 -14.798 1.00 76.33 C ANISOU 1163 CB PRO A 158 9076 8985 10942 558 -1023 18 C ATOM 1164 CG PRO A 158 -32.710 18.430 -15.177 1.00 80.89 C ANISOU 1164 CG PRO A 158 9582 9581 11569 666 -1047 39 C ATOM 1165 CD PRO A 158 -33.566 18.161 -16.379 1.00 77.47 C ANISOU 1165 CD PRO A 158 9087 9194 11156 618 -1169 84 C ATOM 1166 N VAL A 159 -30.814 14.253 -16.121 1.00 73.38 N ANISOU 1166 N VAL A 159 8949 8501 10431 319 -1121 -14 N ATOM 1167 CA VAL A 159 -30.700 12.804 -15.998 1.00 73.24 C ANISOU 1167 CA VAL A 159 8980 8459 10388 206 -1120 -22 C ATOM 1168 C VAL A 159 -30.566 12.482 -14.500 1.00 81.19 C ANISOU 1168 C VAL A 159 9964 9473 11410 207 -1017 -24 C ATOM 1169 O VAL A 159 -29.842 13.173 -13.777 1.00 79.68 O ANISOU 1169 O VAL A 159 9803 9262 11211 286 -946 -40 O ATOM 1170 CB VAL A 159 -29.572 12.233 -16.886 1.00 74.89 C ANISOU 1170 CB VAL A 159 9347 8578 10529 172 -1152 -54 C ATOM 1171 CG1 VAL A 159 -29.264 10.782 -16.533 1.00 74.92 C ANISOU 1171 CG1 VAL A 159 9418 8536 10514 77 -1126 -66 C ATOM 1172 CG2 VAL A 159 -29.925 12.366 -18.368 1.00 74.02 C ANISOU 1172 CG2 VAL A 159 9251 8475 10397 139 -1259 -48 C ATOM 1173 N LYS A 160 -31.338 11.488 -14.032 1.00 81.66 N ANISOU 1173 N LYS A 160 9965 9570 11490 113 -1011 -6 N ATOM 1174 CA LYS A 160 -31.412 11.084 -12.626 1.00 82.37 C ANISOU 1174 CA LYS A 160 10022 9681 11593 93 -921 1 C ATOM 1175 C LYS A 160 -30.953 9.623 -12.410 1.00 88.69 C ANISOU 1175 C LYS A 160 10915 10422 12362 -10 -914 0 C ATOM 1176 O LYS A 160 -31.092 9.106 -11.295 1.00 89.76 O ANISOU 1176 O LYS A 160 11026 10575 12504 -49 -851 15 O ATOM 1177 CB LYS A 160 -32.862 11.286 -12.120 1.00 85.76 C ANISOU 1177 CB LYS A 160 10282 10220 12084 75 -909 31 C ATOM 1178 CG LYS A 160 -33.351 12.740 -12.142 1.00 95.32 C ANISOU 1178 CG LYS A 160 11392 11485 13340 191 -898 34 C ATOM 1179 CD LYS A 160 -34.861 12.821 -11.966 1.00104.00 C ANISOU 1179 CD LYS A 160 12314 12694 14506 168 -907 68 C ATOM 1180 CE LYS A 160 -35.330 14.179 -11.501 1.00109.64 C ANISOU 1180 CE LYS A 160 12922 13460 15276 292 -852 68 C ATOM 1181 NZ LYS A 160 -36.782 14.179 -11.175 1.00112.31 N ANISOU 1181 NZ LYS A 160 13077 13912 15685 271 -844 101 N ATOM 1182 N ALA A 161 -30.409 8.956 -13.465 1.00 84.86 N ANISOU 1182 N ALA A 161 10540 9864 11841 -55 -976 -16 N ATOM 1183 CA ALA A 161 -29.976 7.559 -13.373 1.00 84.62 C ANISOU 1183 CA ALA A 161 10606 9761 11786 -147 -972 -19 C ATOM 1184 C ALA A 161 -28.796 7.179 -14.262 1.00 85.92 C ANISOU 1184 C ALA A 161 10922 9820 11904 -137 -996 -53 C ATOM 1185 O ALA A 161 -28.673 7.669 -15.395 1.00 85.59 O ANISOU 1185 O ALA A 161 10908 9770 11844 -113 -1053 -73 O ATOM 1186 CB ALA A 161 -31.147 6.625 -13.661 1.00 86.68 C ANISOU 1186 CB ALA A 161 10812 10058 12063 -274 -1023 1 C ATOM 1187 N GLY A 162 -27.979 6.253 -13.750 0.80 79.07 N ANISOU 1187 N GLY A 162 10148 8875 11021 -161 -953 -55 N ATOM 1188 CA GLY A 162 -26.823 5.704 -14.454 1.00 77.03 C ANISOU 1188 CA GLY A 162 10031 8511 10727 -152 -960 -87 C ATOM 1189 C GLY A 162 -25.568 6.554 -14.434 1.00 75.51 C ANISOU 1189 C GLY A 162 9890 8289 10511 -39 -924 -105 C ATOM 1190 O GLY A 162 -24.562 6.171 -15.046 0.80 74.82 O ANISOU 1190 O GLY A 162 9913 8121 10395 -24 -924 -133 O ATOM 1191 N VAL A 163 -25.616 7.709 -13.726 1.00 67.69 N ANISOU 1191 N VAL A 163 8823 7365 9531 37 -889 -93 N ATOM 1192 CA VAL A 163 -24.512 8.645 -13.625 1.00 64.38 C ANISOU 1192 CA VAL A 163 8443 6931 9087 136 -856 -108 C ATOM 1193 C VAL A 163 -23.555 8.246 -12.531 1.00 67.36 C ANISOU 1193 C VAL A 163 8863 7274 9455 156 -788 -92 C ATOM 1194 O VAL A 163 -23.954 8.022 -11.383 1.00 67.73 O ANISOU 1194 O VAL A 163 8857 7357 9520 131 -747 -61 O ATOM 1195 CB VAL A 163 -24.981 10.128 -13.500 1.00 66.98 C ANISOU 1195 CB VAL A 163 8686 7337 9428 208 -853 -107 C ATOM 1196 CG1 VAL A 163 -23.819 11.066 -13.173 1.00 64.90 C ANISOU 1196 CG1 VAL A 163 8466 7057 9135 298 -808 -119 C ATOM 1197 CG2 VAL A 163 -25.704 10.592 -14.769 1.00 67.11 C ANISOU 1197 CG2 VAL A 163 8674 7376 9448 203 -932 -117 C ATOM 1198 N GLU A 164 -22.276 8.182 -12.888 1.00 62.21 N ANISOU 1198 N GLU A 164 8304 6558 8774 199 -777 -109 N ATOM 1199 CA GLU A 164 -21.196 7.922 -11.945 1.00 60.53 C ANISOU 1199 CA GLU A 164 8132 6315 8549 231 -720 -89 C ATOM 1200 C GLU A 164 -20.108 8.910 -12.295 1.00 62.00 C ANISOU 1200 C GLU A 164 8357 6498 8702 314 -709 -111 C ATOM 1201 O GLU A 164 -19.828 9.096 -13.484 1.00 61.79 O ANISOU 1201 O GLU A 164 8378 6442 8657 329 -745 -145 O ATOM 1202 CB GLU A 164 -20.666 6.471 -12.036 1.00 61.77 C ANISOU 1202 CB GLU A 164 8371 6384 8714 188 -717 -79 C ATOM 1203 CG GLU A 164 -21.675 5.373 -11.720 1.00 68.93 C ANISOU 1203 CG GLU A 164 9259 7282 9651 92 -730 -56 C ATOM 1204 CD GLU A 164 -22.158 5.227 -10.287 1.00 75.84 C ANISOU 1204 CD GLU A 164 10067 8207 10541 60 -690 -7 C ATOM 1205 OE1 GLU A 164 -21.515 5.779 -9.366 1.00 59.23 O ANISOU 1205 OE1 GLU A 164 7949 6133 8422 111 -645 14 O ATOM 1206 OE2 GLU A 164 -23.203 4.564 -10.091 1.00 75.76 O ANISOU 1206 OE2 GLU A 164 10019 8212 10552 -23 -704 10 O ATOM 1207 N THR A 165 -19.515 9.562 -11.276 1.00 54.54 N ANISOU 1207 N THR A 165 7393 5588 7742 358 -660 -92 N ATOM 1208 CA THR A 165 -18.448 10.521 -11.476 1.00 52.65 C ANISOU 1208 CA THR A 165 7188 5350 7466 427 -646 -109 C ATOM 1209 C THR A 165 -17.316 10.118 -10.541 1.00 55.95 C ANISOU 1209 C THR A 165 7638 5752 7869 441 -601 -77 C ATOM 1210 O THR A 165 -17.572 9.866 -9.368 1.00 55.64 O ANISOU 1210 O THR A 165 7562 5742 7837 414 -570 -41 O ATOM 1211 CB THR A 165 -18.982 11.977 -11.302 1.00 58.64 C ANISOU 1211 CB THR A 165 7888 6174 8217 465 -641 -121 C ATOM 1212 OG1 THR A 165 -20.148 12.181 -12.122 1.00 58.23 O ANISOU 1212 OG1 THR A 165 7794 6139 8191 449 -689 -137 O ATOM 1213 CG2 THR A 165 -17.936 13.041 -11.638 1.00 52.41 C ANISOU 1213 CG2 THR A 165 7144 5384 7387 527 -632 -141 C ATOM 1214 N THR A 166 -16.075 10.009 -11.049 1.00 51.98 N ANISOU 1214 N THR A 166 7199 5208 7345 479 -598 -86 N ATOM 1215 CA THR A 166 -14.968 9.615 -10.182 1.00 50.78 C ANISOU 1215 CA THR A 166 7067 5046 7182 495 -562 -47 C ATOM 1216 C THR A 166 -14.527 10.754 -9.284 1.00 54.92 C ANISOU 1216 C THR A 166 7561 5637 7668 522 -530 -34 C ATOM 1217 O THR A 166 -14.744 11.930 -9.590 1.00 52.22 O ANISOU 1217 O THR A 166 7206 5331 7304 546 -534 -65 O ATOM 1218 CB THR A 166 -13.785 9.035 -10.967 1.00 55.70 C ANISOU 1218 CB THR A 166 7758 5605 7802 529 -563 -57 C ATOM 1219 OG1 THR A 166 -13.221 10.047 -11.788 1.00 56.47 O ANISOU 1219 OG1 THR A 166 7874 5717 7862 571 -570 -96 O ATOM 1220 CG2 THR A 166 -14.149 7.802 -11.767 1.00 54.87 C ANISOU 1220 CG2 THR A 166 7696 5419 7731 498 -584 -73 C ATOM 1221 N THR A 167 -13.853 10.404 -8.198 1.00 53.02 N ANISOU 1221 N THR A 167 7319 5411 7417 516 -501 15 N ATOM 1222 CA THR A 167 -13.326 11.419 -7.278 1.00 52.12 C ANISOU 1222 CA THR A 167 7185 5361 7256 528 -471 29 C ATOM 1223 C THR A 167 -12.071 11.984 -7.945 1.00 53.85 C ANISOU 1223 C THR A 167 7444 5573 7443 577 -474 12 C ATOM 1224 O THR A 167 -11.234 11.199 -8.370 1.00 50.90 O ANISOU 1224 O THR A 167 7102 5155 7083 596 -481 26 O ATOM 1225 CB THR A 167 -13.021 10.766 -5.885 1.00 55.76 C ANISOU 1225 CB THR A 167 7632 5845 7710 492 -446 95 C ATOM 1226 OG1 THR A 167 -14.220 10.149 -5.414 1.00 53.38 O ANISOU 1226 OG1 THR A 167 7298 5544 7439 440 -443 108 O ATOM 1227 CG2 THR A 167 -12.499 11.778 -4.853 1.00 52.72 C ANISOU 1227 CG2 THR A 167 7233 5532 7266 488 -414 111 C ATOM 1228 N PRO A 168 -11.918 13.325 -8.059 1.00 52.33 N ANISOU 1228 N PRO A 168 7251 5421 7210 597 -466 -18 N ATOM 1229 CA PRO A 168 -10.700 13.868 -8.672 1.00 51.97 C ANISOU 1229 CA PRO A 168 7243 5375 7129 633 -468 -31 C ATOM 1230 C PRO A 168 -9.402 13.299 -8.106 1.00 56.17 C ANISOU 1230 C PRO A 168 7780 5914 7646 639 -454 19 C ATOM 1231 O PRO A 168 -9.277 13.042 -6.903 1.00 55.25 O ANISOU 1231 O PRO A 168 7641 5832 7521 612 -437 68 O ATOM 1232 CB PRO A 168 -10.845 15.387 -8.446 1.00 53.78 C ANISOU 1232 CB PRO A 168 7469 5652 7314 638 -455 -58 C ATOM 1233 CG PRO A 168 -12.335 15.598 -8.426 1.00 57.13 C ANISOU 1233 CG PRO A 168 7859 6077 7771 626 -459 -81 C ATOM 1234 CD PRO A 168 -12.838 14.413 -7.651 1.00 52.62 C ANISOU 1234 CD PRO A 168 7257 5503 7234 589 -451 -42 C ATOM 1235 N SER A 169 -8.456 13.016 -9.011 1.00 54.07 N ANISOU 1235 N SER A 169 7545 5617 7382 675 -462 9 N ATOM 1236 CA SER A 169 -7.155 12.506 -8.617 1.00 54.15 C ANISOU 1236 CA SER A 169 7551 5636 7386 693 -449 58 C ATOM 1237 C SER A 169 -6.089 13.378 -9.258 1.00 55.87 C ANISOU 1237 C SER A 169 7786 5882 7559 719 -444 35 C ATOM 1238 O SER A 169 -6.276 13.889 -10.367 1.00 52.44 O ANISOU 1238 O SER A 169 7381 5427 7114 733 -454 -21 O ATOM 1239 CB SER A 169 -6.996 11.030 -8.973 1.00 58.05 C ANISOU 1239 CB SER A 169 8058 6057 7940 713 -453 78 C ATOM 1240 OG SER A 169 -6.788 10.821 -10.356 1.00 66.31 O ANISOU 1240 OG SER A 169 9143 7051 9000 745 -458 26 O ATOM 1241 N LYS A 170 -5.015 13.620 -8.504 1.00 54.58 N ANISOU 1241 N LYS A 170 7602 5774 7362 717 -432 81 N ATOM 1242 CA LYS A 170 -3.906 14.469 -8.935 1.00 54.91 C ANISOU 1242 CA LYS A 170 7652 5857 7354 730 -425 70 C ATOM 1243 C LYS A 170 -3.167 13.668 -9.980 1.00 58.53 C ANISOU 1243 C LYS A 170 8122 6269 7847 779 -421 59 C ATOM 1244 O LYS A 170 -2.934 12.483 -9.787 1.00 59.23 O ANISOU 1244 O LYS A 170 8196 6321 7987 803 -416 97 O ATOM 1245 CB LYS A 170 -3.004 14.821 -7.736 1.00 56.91 C ANISOU 1245 CB LYS A 170 7872 6189 7562 703 -417 131 C ATOM 1246 CG LYS A 170 -2.309 16.163 -7.834 1.00 80.94 C ANISOU 1246 CG LYS A 170 10928 9293 10532 682 -412 111 C ATOM 1247 CD LYS A 170 -1.275 16.341 -6.722 1.00 95.18 C ANISOU 1247 CD LYS A 170 12697 11179 12290 649 -409 178 C ATOM 1248 CE LYS A 170 -0.643 17.712 -6.749 1.00113.35 C ANISOU 1248 CE LYS A 170 15017 13540 14510 612 -403 157 C ATOM 1249 NZ LYS A 170 0.594 17.773 -5.921 1.00126.18 N ANISOU 1249 NZ LYS A 170 16603 15250 16091 580 -407 225 N ATOM 1250 N GLN A 171 -2.876 14.289 -11.104 1.00 54.64 N ANISOU 1250 N GLN A 171 7660 5772 7327 792 -419 6 N ATOM 1251 CA GLN A 171 -2.175 13.657 -12.205 1.00 55.14 C ANISOU 1251 CA GLN A 171 7742 5796 7414 834 -405 -17 C ATOM 1252 C GLN A 171 -0.707 14.087 -12.269 1.00 58.92 C ANISOU 1252 C GLN A 171 8197 6335 7854 850 -385 4 C ATOM 1253 O GLN A 171 -0.282 14.922 -11.460 1.00 56.14 O ANISOU 1253 O GLN A 171 7820 6057 7454 819 -388 36 O ATOM 1254 CB GLN A 171 -2.949 13.904 -13.526 1.00 56.35 C ANISOU 1254 CB GLN A 171 7950 5900 7562 830 -419 -92 C ATOM 1255 CG GLN A 171 -4.270 13.081 -13.618 1.00 64.76 C ANISOU 1255 CG GLN A 171 9029 6897 8678 819 -438 -107 C ATOM 1256 CD GLN A 171 -4.167 11.610 -13.198 1.00 70.59 C ANISOU 1256 CD GLN A 171 9756 7583 9481 840 -425 -70 C ATOM 1257 OE1 GLN A 171 -4.937 11.131 -12.347 1.00 58.12 O ANISOU 1257 OE1 GLN A 171 8157 5992 7933 818 -436 -37 O ATOM 1258 NE2 GLN A 171 -3.183 10.868 -13.737 1.00 61.80 N ANISOU 1258 NE2 GLN A 171 8653 6437 8391 883 -397 -71 N ATOM 1259 N SER A 172 0.067 13.524 -13.234 1.00 57.29 N ANISOU 1259 N SER A 172 7999 6101 7668 893 -361 -17 N ATOM 1260 CA SER A 172 1.506 13.807 -13.409 1.00 57.43 C ANISOU 1260 CA SER A 172 7984 6180 7658 913 -336 2 C ATOM 1261 C SER A 172 1.830 15.330 -13.542 1.00 62.98 C ANISOU 1261 C SER A 172 8698 6957 8274 865 -343 -18 C ATOM 1262 O SER A 172 2.896 15.771 -13.091 1.00 62.53 O ANISOU 1262 O SER A 172 8599 6977 8182 855 -334 23 O ATOM 1263 CB SER A 172 2.097 12.991 -14.557 1.00 58.95 C ANISOU 1263 CB SER A 172 8192 6323 7886 966 -299 -34 C ATOM 1264 OG SER A 172 2.136 13.663 -15.807 1.00 68.11 O ANISOU 1264 OG SER A 172 9400 7481 8996 951 -290 -105 O ATOM 1265 N ASN A 173 0.887 16.122 -14.104 1.00 60.11 N ANISOU 1265 N ASN A 173 8392 6569 7878 833 -364 -73 N ATOM 1266 CA ASN A 173 1.030 17.576 -14.253 1.00 58.14 C ANISOU 1266 CA ASN A 173 8169 6370 7552 788 -374 -93 C ATOM 1267 C ASN A 173 0.668 18.328 -12.983 1.00 59.75 C ANISOU 1267 C ASN A 173 8359 6616 7727 746 -389 -60 C ATOM 1268 O ASN A 173 0.692 19.541 -13.021 1.00 59.99 O ANISOU 1268 O ASN A 173 8420 6675 7697 708 -396 -79 O ATOM 1269 CB ASN A 173 0.181 18.106 -15.419 1.00 57.96 C ANISOU 1269 CB ASN A 173 8214 6298 7510 777 -392 -160 C ATOM 1270 CG ASN A 173 -1.311 18.066 -15.194 1.00 63.44 C ANISOU 1270 CG ASN A 173 8925 6942 8236 771 -422 -174 C ATOM 1271 OD1 ASN A 173 -1.838 17.576 -14.181 1.00 53.24 O ANISOU 1271 OD1 ASN A 173 7601 5645 6983 772 -425 -141 O ATOM 1272 ND2 ASN A 173 -2.023 18.484 -16.189 1.00 54.15 N ANISOU 1272 ND2 ASN A 173 7798 5729 7046 762 -444 -221 N ATOM 1273 N ASN A 174 0.250 17.624 -11.903 1.00 56.89 N ANISOU 1273 N ASN A 174 7961 6249 7406 750 -393 -17 N ATOM 1274 CA ASN A 174 -0.146 18.129 -10.567 1.00 57.78 C ANISOU 1274 CA ASN A 174 8059 6401 7494 707 -401 16 C ATOM 1275 C ASN A 174 -1.565 18.751 -10.499 1.00 62.04 C ANISOU 1275 C ASN A 174 8637 6904 8033 688 -412 -26 C ATOM 1276 O ASN A 174 -2.042 19.101 -9.412 1.00 63.17 O ANISOU 1276 O ASN A 174 8770 7070 8160 656 -409 -8 O ATOM 1277 CB ASN A 174 0.907 19.080 -9.971 1.00 59.68 C ANISOU 1277 CB ASN A 174 8287 6728 7660 661 -395 45 C ATOM 1278 CG ASN A 174 2.196 18.362 -9.682 1.00 69.13 C ANISOU 1278 CG ASN A 174 9424 7977 8867 678 -387 107 C ATOM 1279 OD1 ASN A 174 3.198 18.500 -10.399 1.00 58.24 O ANISOU 1279 OD1 ASN A 174 8033 6626 7470 690 -376 102 O ATOM 1280 ND2 ASN A 174 2.152 17.493 -8.685 1.00 61.17 N ANISOU 1280 ND2 ASN A 174 8371 6977 7895 683 -393 167 N ATOM 1281 N LYS A 175 -2.253 18.822 -11.642 1.00 56.14 N ANISOU 1281 N LYS A 175 7927 6100 7305 710 -425 -79 N ATOM 1282 CA LYS A 175 -3.644 19.270 -11.758 1.00 52.91 C ANISOU 1282 CA LYS A 175 7542 5652 6911 705 -441 -114 C ATOM 1283 C LYS A 175 -4.497 17.995 -11.639 1.00 54.28 C ANISOU 1283 C LYS A 175 7689 5779 7156 723 -448 -104 C ATOM 1284 O LYS A 175 -3.946 16.915 -11.726 1.00 53.42 O ANISOU 1284 O LYS A 175 7564 5656 7079 743 -441 -81 O ATOM 1285 CB LYS A 175 -3.864 19.993 -13.085 1.00 52.68 C ANISOU 1285 CB LYS A 175 7563 5592 6861 712 -459 -165 C ATOM 1286 CG LYS A 175 -3.098 21.309 -13.229 1.00 44.28 C ANISOU 1286 CG LYS A 175 6535 4566 5724 686 -453 -174 C ATOM 1287 CD LYS A 175 -3.221 21.864 -14.653 1.00 44.60 C ANISOU 1287 CD LYS A 175 6630 4574 5744 691 -475 -217 C ATOM 1288 CE LYS A 175 -2.714 23.283 -14.825 1.00 65.36 C ANISOU 1288 CE LYS A 175 9306 7227 8302 660 -474 -228 C ATOM 1289 NZ LYS A 175 -1.227 23.378 -14.763 1.00 76.89 N ANISOU 1289 NZ LYS A 175 10757 8745 9711 636 -451 -208 N ATOM 1290 N TYR A 176 -5.814 18.118 -11.416 1.00 50.96 N ANISOU 1290 N TYR A 176 7265 5336 6762 716 -459 -120 N ATOM 1291 CA TYR A 176 -6.742 17.012 -11.209 1.00 50.91 C ANISOU 1291 CA TYR A 176 7234 5292 6817 718 -467 -110 C ATOM 1292 C TYR A 176 -7.483 16.541 -12.455 1.00 52.79 C ANISOU 1292 C TYR A 176 7495 5473 7091 731 -496 -149 C ATOM 1293 O TYR A 176 -7.598 17.258 -13.447 1.00 53.57 O ANISOU 1293 O TYR A 176 7627 5561 7166 737 -514 -186 O ATOM 1294 CB TYR A 176 -7.769 17.362 -10.136 1.00 52.97 C ANISOU 1294 CB TYR A 176 7467 5575 7087 694 -459 -100 C ATOM 1295 CG TYR A 176 -7.222 17.363 -8.732 1.00 56.57 C ANISOU 1295 CG TYR A 176 7897 6082 7515 667 -431 -53 C ATOM 1296 CD1 TYR A 176 -6.593 18.489 -8.209 1.00 59.54 C ANISOU 1296 CD1 TYR A 176 8287 6508 7827 647 -414 -52 C ATOM 1297 CD2 TYR A 176 -7.425 16.278 -7.886 1.00 57.18 C ANISOU 1297 CD2 TYR A 176 7941 6159 7625 652 -425 -8 C ATOM 1298 CE1 TYR A 176 -6.130 18.513 -6.894 1.00 63.02 C ANISOU 1298 CE1 TYR A 176 8709 7003 8234 610 -393 -9 C ATOM 1299 CE2 TYR A 176 -6.949 16.280 -6.577 1.00 57.99 C ANISOU 1299 CE2 TYR A 176 8023 6315 7696 618 -406 42 C ATOM 1300 CZ TYR A 176 -6.311 17.403 -6.080 1.00 67.81 C ANISOU 1300 CZ TYR A 176 9280 7614 8872 595 -390 40 C ATOM 1301 OH TYR A 176 -5.890 17.429 -4.773 1.00 69.13 O ANISOU 1301 OH TYR A 176 9430 7839 8997 550 -374 88 O ATOM 1302 N ALA A 177 -7.988 15.327 -12.384 1.00 47.29 N ANISOU 1302 N ALA A 177 6783 4738 6446 728 -501 -136 N ATOM 1303 CA ALA A 177 -8.752 14.708 -13.446 1.00 46.71 C ANISOU 1303 CA ALA A 177 6732 4611 6406 726 -528 -170 C ATOM 1304 C ALA A 177 -9.846 13.852 -12.870 1.00 50.64 C ANISOU 1304 C ALA A 177 7198 5089 6955 702 -536 -152 C ATOM 1305 O ALA A 177 -9.716 13.305 -11.779 1.00 51.71 O ANISOU 1305 O ALA A 177 7305 5235 7107 693 -515 -108 O ATOM 1306 CB ALA A 177 -7.858 13.884 -14.382 1.00 46.76 C ANISOU 1306 CB ALA A 177 6777 4574 6415 745 -521 -186 C ATOM 1307 N ALA A 178 -10.916 13.711 -13.627 1.00 45.84 N ANISOU 1307 N ALA A 178 6595 4454 6368 685 -569 -181 N ATOM 1308 CA ALA A 178 -12.055 12.894 -13.267 1.00 45.40 C ANISOU 1308 CA ALA A 178 6510 4381 6359 652 -582 -169 C ATOM 1309 C ALA A 178 -12.811 12.592 -14.536 1.00 49.89 C ANISOU 1309 C ALA A 178 7104 4912 6940 631 -625 -207 C ATOM 1310 O ALA A 178 -12.641 13.259 -15.560 1.00 48.12 O ANISOU 1310 O ALA A 178 6913 4688 6684 643 -647 -240 O ATOM 1311 CB ALA A 178 -12.958 13.644 -12.292 1.00 45.87 C ANISOU 1311 CB ALA A 178 6512 4494 6424 640 -575 -153 C ATOM 1312 N SER A 179 -13.615 11.558 -14.489 1.00 47.78 N ANISOU 1312 N SER A 179 6828 4615 6713 593 -638 -201 N ATOM 1313 CA SER A 179 -14.481 11.231 -15.597 1.00 48.05 C ANISOU 1313 CA SER A 179 6880 4621 6755 557 -685 -233 C ATOM 1314 C SER A 179 -15.843 10.986 -15.037 1.00 52.53 C ANISOU 1314 C SER A 179 7386 5213 7361 514 -703 -212 C ATOM 1315 O SER A 179 -15.986 10.460 -13.932 1.00 53.69 O ANISOU 1315 O SER A 179 7500 5367 7533 500 -675 -177 O ATOM 1316 CB SER A 179 -13.963 10.035 -16.408 1.00 49.26 C ANISOU 1316 CB SER A 179 7104 4700 6912 541 -682 -257 C ATOM 1317 OG SER A 179 -13.591 8.936 -15.586 1.00 70.94 O ANISOU 1317 OG SER A 179 9854 7407 9693 538 -648 -225 O ATOM 1318 N SER A 180 -16.844 11.428 -15.765 1.00 48.99 N ANISOU 1318 N SER A 180 6915 4785 6914 493 -752 -230 N ATOM 1319 CA SER A 180 -18.230 11.167 -15.445 1.00 49.01 C ANISOU 1319 CA SER A 180 6850 4817 6955 447 -776 -213 C ATOM 1320 C SER A 180 -18.770 10.373 -16.602 1.00 56.60 C ANISOU 1320 C SER A 180 7849 5741 7918 389 -828 -237 C ATOM 1321 O SER A 180 -18.496 10.680 -17.776 1.00 53.95 O ANISOU 1321 O SER A 180 7564 5388 7547 392 -862 -268 O ATOM 1322 CB SER A 180 -19.019 12.454 -15.267 1.00 50.40 C ANISOU 1322 CB SER A 180 6954 5057 7137 476 -791 -206 C ATOM 1323 OG SER A 180 -20.378 12.133 -15.002 1.00 56.76 O ANISOU 1323 OG SER A 180 7684 5897 7984 431 -812 -189 O ATOM 1324 N TYR A 181 -19.527 9.330 -16.276 1.00 56.61 N ANISOU 1324 N TYR A 181 7829 5728 7951 326 -835 -222 N ATOM 1325 CA TYR A 181 -20.077 8.476 -17.297 1.00 57.16 C ANISOU 1325 CA TYR A 181 7939 5760 8018 254 -883 -245 C ATOM 1326 C TYR A 181 -21.536 8.142 -17.044 1.00 59.47 C ANISOU 1326 C TYR A 181 8154 6095 8346 184 -919 -222 C ATOM 1327 O TYR A 181 -22.002 8.089 -15.905 1.00 59.62 O ANISOU 1327 O TYR A 181 8104 6152 8398 179 -889 -187 O ATOM 1328 CB TYR A 181 -19.200 7.239 -17.517 1.00 60.21 C ANISOU 1328 CB TYR A 181 8424 6053 8401 236 -854 -264 C ATOM 1329 CG TYR A 181 -19.240 6.218 -16.400 1.00 64.21 C ANISOU 1329 CG TYR A 181 8921 6530 8947 210 -815 -228 C ATOM 1330 CD1 TYR A 181 -18.331 6.272 -15.347 1.00 65.55 C ANISOU 1330 CD1 TYR A 181 9087 6695 9125 268 -759 -198 C ATOM 1331 CD2 TYR A 181 -20.145 5.161 -16.430 1.00 66.53 C ANISOU 1331 CD2 TYR A 181 9218 6796 9263 121 -838 -222 C ATOM 1332 CE1 TYR A 181 -18.314 5.289 -14.357 1.00 68.21 C ANISOU 1332 CE1 TYR A 181 9424 6999 9494 241 -728 -158 C ATOM 1333 CE2 TYR A 181 -20.162 4.196 -15.429 1.00 69.02 C ANISOU 1333 CE2 TYR A 181 9534 7076 9612 93 -804 -185 C ATOM 1334 CZ TYR A 181 -19.234 4.253 -14.401 1.00 78.42 C ANISOU 1334 CZ TYR A 181 10723 8260 10811 155 -750 -151 C ATOM 1335 OH TYR A 181 -19.245 3.284 -13.428 1.00 83.13 O ANISOU 1335 OH TYR A 181 11326 8821 11439 123 -723 -107 O ATOM 1336 N LEU A 182 -22.246 7.958 -18.136 1.00 54.75 N ANISOU 1336 N LEU A 182 7566 5500 7735 124 -983 -240 N ATOM 1337 CA LEU A 182 -23.656 7.701 -18.173 1.00 55.37 C ANISOU 1337 CA LEU A 182 7568 5629 7840 49 -1032 -220 C ATOM 1338 C LEU A 182 -23.936 6.434 -19.009 1.00 59.96 C ANISOU 1338 C LEU A 182 8224 6151 8406 -56 -1070 -244 C ATOM 1339 O LEU A 182 -23.676 6.423 -20.217 1.00 59.11 O ANISOU 1339 O LEU A 182 8191 6014 8256 -77 -1109 -281 O ATOM 1340 CB LEU A 182 -24.303 8.966 -18.796 1.00 55.63 C ANISOU 1340 CB LEU A 182 7532 5736 7868 81 -1089 -213 C ATOM 1341 CG LEU A 182 -25.783 8.922 -19.194 1.00 62.56 C ANISOU 1341 CG LEU A 182 8320 6681 8768 10 -1161 -190 C ATOM 1342 CD1 LEU A 182 -26.686 8.629 -17.995 1.00 63.92 C ANISOU 1342 CD1 LEU A 182 8385 6907 8996 -15 -1131 -152 C ATOM 1343 CD2 LEU A 182 -26.191 10.205 -19.869 1.00 64.87 C ANISOU 1343 CD2 LEU A 182 8559 7033 9056 59 -1216 -178 C ATOM 1344 N SER A 183 -24.475 5.374 -18.367 1.00 60.51 N ANISOU 1344 N SER A 183 8282 6204 8507 -129 -1057 -225 N ATOM 1345 CA SER A 183 -24.854 4.114 -19.043 1.00 62.28 C ANISOU 1345 CA SER A 183 8579 6368 8718 -242 -1089 -247 C ATOM 1346 C SER A 183 -26.290 4.175 -19.509 1.00 70.14 C ANISOU 1346 C SER A 183 9493 7442 9717 -333 -1167 -230 C ATOM 1347 O SER A 183 -27.214 4.393 -18.712 1.00 71.39 O ANISOU 1347 O SER A 183 9531 7679 9915 -348 -1169 -187 O ATOM 1348 CB SER A 183 -24.639 2.895 -18.154 1.00 66.24 C ANISOU 1348 CB SER A 183 9124 6799 9248 -280 -1037 -232 C ATOM 1349 OG SER A 183 -23.280 2.813 -17.758 1.00 81.90 O ANISOU 1349 OG SER A 183 11176 8712 11229 -192 -972 -240 O ATOM 1350 N LEU A 184 -26.465 4.040 -20.815 1.00 67.87 N ANISOU 1350 N LEU A 184 9263 7140 9385 -393 -1230 -264 N ATOM 1351 CA LEU A 184 -27.760 4.074 -21.476 1.00 68.48 C ANISOU 1351 CA LEU A 184 9273 7293 9455 -490 -1318 -247 C ATOM 1352 C LEU A 184 -27.877 2.898 -22.403 1.00 71.85 C ANISOU 1352 C LEU A 184 9813 7648 9837 -618 -1354 -288 C ATOM 1353 O LEU A 184 -26.900 2.189 -22.644 1.00 70.99 O ANISOU 1353 O LEU A 184 9839 7428 9704 -615 -1307 -334 O ATOM 1354 CB LEU A 184 -27.894 5.351 -22.315 1.00 68.59 C ANISOU 1354 CB LEU A 184 9242 7376 9444 -437 -1378 -243 C ATOM 1355 CG LEU A 184 -27.823 6.679 -21.607 1.00 73.31 C ANISOU 1355 CG LEU A 184 9736 8040 10079 -310 -1351 -209 C ATOM 1356 CD1 LEU A 184 -27.362 7.754 -22.579 1.00 73.45 C ANISOU 1356 CD1 LEU A 184 9784 8068 10054 -248 -1390 -223 C ATOM 1357 CD2 LEU A 184 -29.166 7.040 -20.957 1.00 75.77 C ANISOU 1357 CD2 LEU A 184 9882 8459 10447 -326 -1378 -154 C ATOM 1358 N THR A 185 -29.072 2.695 -22.941 1.00 68.83 N ANISOU 1358 N THR A 185 9376 7331 9444 -732 -1436 -271 N ATOM 1359 CA THR A 185 -29.288 1.645 -23.916 1.00 70.03 C ANISOU 1359 CA THR A 185 9638 7425 9544 -872 -1480 -311 C ATOM 1360 C THR A 185 -29.232 2.365 -25.235 1.00 73.84 C ANISOU 1360 C THR A 185 10151 7941 9964 -876 -1550 -334 C ATOM 1361 O THR A 185 -29.502 3.570 -25.234 1.00 73.01 O ANISOU 1361 O THR A 185 9939 7928 9875 -798 -1584 -295 O ATOM 1362 CB THR A 185 -30.631 0.948 -23.682 1.00 78.68 C ANISOU 1362 CB THR A 185 10657 8579 10659 -1011 -1531 -275 C ATOM 1363 OG1 THR A 185 -31.646 1.942 -23.556 1.00 79.20 O ANISOU 1363 OG1 THR A 185 10548 8788 10755 -991 -1590 -216 O ATOM 1364 CG2 THR A 185 -30.613 0.041 -22.461 1.00 74.19 C ANISOU 1364 CG2 THR A 185 10091 7957 10139 -1030 -1458 -258 C ATOM 1365 N PRO A 186 -28.845 1.719 -26.365 1.00 71.25 N ANISOU 1365 N PRO A 186 9970 7537 9563 -959 -1570 -395 N ATOM 1366 CA PRO A 186 -28.816 2.451 -27.644 1.00 71.86 C ANISOU 1366 CA PRO A 186 10077 7656 9570 -972 -1642 -412 C ATOM 1367 C PRO A 186 -30.152 3.136 -27.970 1.00 78.43 C ANISOU 1367 C PRO A 186 10764 8629 10407 -1026 -1755 -347 C ATOM 1368 O PRO A 186 -30.138 4.191 -28.601 1.00 78.16 O ANISOU 1368 O PRO A 186 10696 8654 10346 -976 -1808 -329 O ATOM 1369 CB PRO A 186 -28.435 1.360 -28.660 1.00 74.18 C ANISOU 1369 CB PRO A 186 10550 7848 9788 -1090 -1640 -489 C ATOM 1370 CG PRO A 186 -27.662 0.384 -27.856 1.00 77.24 C ANISOU 1370 CG PRO A 186 11020 8112 10214 -1058 -1534 -522 C ATOM 1371 CD PRO A 186 -28.422 0.316 -26.562 1.00 72.99 C ANISOU 1371 CD PRO A 186 10345 7630 9759 -1047 -1526 -454 C ATOM 1372 N GLU A 187 -31.291 2.577 -27.480 1.00 77.27 N ANISOU 1372 N GLU A 187 10524 8538 10299 -1120 -1790 -306 N ATOM 1373 CA GLU A 187 -32.627 3.159 -27.656 1.00 79.12 C ANISOU 1373 CA GLU A 187 10596 8915 10552 -1168 -1892 -236 C ATOM 1374 C GLU A 187 -32.728 4.490 -26.906 1.00 82.08 C ANISOU 1374 C GLU A 187 10818 9370 10998 -1008 -1875 -178 C ATOM 1375 O GLU A 187 -33.070 5.491 -27.530 1.00 82.09 O ANISOU 1375 O GLU A 187 10753 9450 10990 -973 -1949 -143 O ATOM 1376 CB GLU A 187 -33.787 2.184 -27.309 1.00 82.36 C ANISOU 1376 CB GLU A 187 10943 9367 10984 -1317 -1927 -209 C ATOM 1377 CG GLU A 187 -33.634 1.399 -26.011 1.00 98.78 C ANISOU 1377 CG GLU A 187 13021 11388 13124 -1304 -1830 -210 C ATOM 1378 CD GLU A 187 -34.902 0.952 -25.301 1.00132.63 C ANISOU 1378 CD GLU A 187 17170 15763 17460 -1399 -1855 -154 C ATOM 1379 OE1 GLU A 187 -34.918 0.998 -24.048 1.00129.27 O ANISOU 1379 OE1 GLU A 187 16665 15348 17103 -1329 -1781 -126 O ATOM 1380 OE2 GLU A 187 -35.867 0.536 -25.984 1.00131.58 O ANISOU 1380 OE2 GLU A 187 17009 15692 17293 -1550 -1948 -138 O ATOM 1381 N GLN A 188 -32.349 4.523 -25.603 1.00 76.79 N ANISOU 1381 N GLN A 188 10108 8674 10396 -910 -1776 -171 N ATOM 1382 CA GLN A 188 -32.329 5.753 -24.796 1.00 74.63 C ANISOU 1382 CA GLN A 188 9710 8461 10186 -757 -1741 -129 C ATOM 1383 C GLN A 188 -31.489 6.845 -25.480 1.00 77.15 C ANISOU 1383 C GLN A 188 10082 8761 10468 -652 -1751 -144 C ATOM 1384 O GLN A 188 -31.997 7.940 -25.680 1.00 76.98 O ANISOU 1384 O GLN A 188 9958 8823 10470 -591 -1803 -98 O ATOM 1385 CB GLN A 188 -31.832 5.476 -23.371 1.00 74.65 C ANISOU 1385 CB GLN A 188 9704 8418 10243 -686 -1627 -133 C ATOM 1386 CG GLN A 188 -32.884 4.825 -22.481 1.00 81.36 C ANISOU 1386 CG GLN A 188 10446 9322 11143 -765 -1618 -95 C ATOM 1387 CD GLN A 188 -32.291 4.059 -21.319 1.00 95.66 C ANISOU 1387 CD GLN A 188 12308 11057 12979 -751 -1516 -110 C ATOM 1388 OE1 GLN A 188 -31.303 4.462 -20.693 1.00 83.24 O ANISOU 1388 OE1 GLN A 188 10773 9436 11419 -635 -1438 -123 O ATOM 1389 NE2 GLN A 188 -32.887 2.915 -21.009 1.00 93.78 N ANISOU 1389 NE2 GLN A 188 12075 10808 12748 -876 -1517 -102 N ATOM 1390 N TRP A 189 -30.245 6.509 -25.909 1.00 72.36 N ANISOU 1390 N TRP A 189 9639 8048 9805 -637 -1704 -207 N ATOM 1391 CA TRP A 189 -29.296 7.370 -26.639 1.00 70.15 C ANISOU 1391 CA TRP A 189 9437 7739 9477 -558 -1705 -232 C ATOM 1392 C TRP A 189 -29.864 7.901 -27.968 1.00 76.89 C ANISOU 1392 C TRP A 189 10285 8655 10274 -617 -1822 -213 C ATOM 1393 O TRP A 189 -29.619 9.055 -28.304 1.00 76.85 O ANISOU 1393 O TRP A 189 10258 8679 10261 -531 -1847 -191 O ATOM 1394 CB TRP A 189 -27.951 6.617 -26.861 1.00 67.20 C ANISOU 1394 CB TRP A 189 9237 7241 9054 -558 -1628 -307 C ATOM 1395 CG TRP A 189 -27.018 7.199 -27.893 1.00 67.19 C ANISOU 1395 CG TRP A 189 9342 7208 8980 -523 -1636 -345 C ATOM 1396 CD1 TRP A 189 -26.608 6.607 -29.051 1.00 70.47 C ANISOU 1396 CD1 TRP A 189 9895 7568 9311 -610 -1656 -402 C ATOM 1397 CD2 TRP A 189 -26.398 8.504 -27.867 1.00 65.65 C ANISOU 1397 CD2 TRP A 189 9125 7034 8785 -399 -1623 -329 C ATOM 1398 NE1 TRP A 189 -25.782 7.461 -29.757 1.00 69.37 N ANISOU 1398 NE1 TRP A 189 9816 7423 9119 -550 -1656 -421 N ATOM 1399 CE2 TRP A 189 -25.630 8.626 -29.049 1.00 69.49 C ANISOU 1399 CE2 TRP A 189 9737 7483 9185 -422 -1637 -375 C ATOM 1400 CE3 TRP A 189 -26.413 9.576 -26.957 1.00 65.49 C ANISOU 1400 CE3 TRP A 189 8997 7059 8826 -277 -1595 -284 C ATOM 1401 CZ2 TRP A 189 -24.873 9.773 -29.337 1.00 68.17 C ANISOU 1401 CZ2 TRP A 189 9588 7322 8990 -329 -1629 -372 C ATOM 1402 CZ3 TRP A 189 -25.697 10.732 -27.261 1.00 66.02 C ANISOU 1402 CZ3 TRP A 189 9087 7128 8868 -186 -1590 -282 C ATOM 1403 CH2 TRP A 189 -24.909 10.810 -28.417 1.00 66.72 C ANISOU 1403 CH2 TRP A 189 9301 7179 8872 -212 -1606 -324 C ATOM 1404 N LYS A 190 -30.626 7.072 -28.711 1.00 76.38 N ANISOU 1404 N LYS A 190 10243 8610 10168 -769 -1898 -216 N ATOM 1405 CA LYS A 190 -31.191 7.443 -30.020 1.00 77.01 C ANISOU 1405 CA LYS A 190 10326 8752 10182 -850 -2020 -195 C ATOM 1406 C LYS A 190 -32.614 8.045 -29.954 1.00 81.74 C ANISOU 1406 C LYS A 190 10739 9486 10834 -865 -2119 -105 C ATOM 1407 O LYS A 190 -33.083 8.589 -30.960 1.00 82.79 O ANISOU 1407 O LYS A 190 10851 9683 10924 -905 -2227 -68 O ATOM 1408 CB LYS A 190 -31.143 6.245 -30.990 1.00 80.53 C ANISOU 1408 CB LYS A 190 10916 9144 10537 -1017 -2051 -255 C ATOM 1409 CG LYS A 190 -29.740 5.899 -31.497 1.00 90.12 C ANISOU 1409 CG LYS A 190 12320 10239 11682 -1001 -1975 -342 C ATOM 1410 CD LYS A 190 -29.709 4.483 -32.063 1.00100.70 C ANISOU 1410 CD LYS A 190 13799 11503 12958 -1156 -1969 -411 C ATOM 1411 CE LYS A 190 -28.387 4.119 -32.691 1.00111.24 C ANISOU 1411 CE LYS A 190 15320 12724 14222 -1145 -1895 -501 C ATOM 1412 NZ LYS A 190 -28.373 2.708 -33.173 1.00120.66 N ANISOU 1412 NZ LYS A 190 16654 13830 15361 -1290 -1876 -573 N ATOM 1413 N SER A 191 -33.292 7.952 -28.786 1.00 77.39 N ANISOU 1413 N SER A 191 10050 8980 10375 -833 -2083 -67 N ATOM 1414 CA SER A 191 -34.634 8.508 -28.554 1.00 78.08 C ANISOU 1414 CA SER A 191 9941 9197 10529 -829 -2157 18 C ATOM 1415 C SER A 191 -34.593 10.039 -28.276 1.00 80.67 C ANISOU 1415 C SER A 191 10170 9568 10914 -659 -2154 68 C ATOM 1416 O SER A 191 -35.610 10.729 -28.417 1.00 80.42 O ANISOU 1416 O SER A 191 9989 9640 10928 -640 -2233 142 O ATOM 1417 CB SER A 191 -35.333 7.782 -27.406 1.00 81.53 C ANISOU 1417 CB SER A 191 10277 9664 11038 -865 -2106 34 C ATOM 1418 OG SER A 191 -34.695 7.990 -26.158 1.00 88.39 O ANISOU 1418 OG SER A 191 11137 10482 11964 -742 -1983 16 O ATOM 1419 N HIS A 192 -33.413 10.548 -27.888 1.00 75.10 N ANISOU 1419 N HIS A 192 9547 8780 10206 -538 -2063 28 N ATOM 1420 CA HIS A 192 -33.167 11.961 -27.601 1.00 73.88 C ANISOU 1420 CA HIS A 192 9334 8641 10096 -380 -2045 60 C ATOM 1421 C HIS A 192 -32.334 12.609 -28.707 1.00 76.24 C ANISOU 1421 C HIS A 192 9756 8898 10315 -358 -2086 44 C ATOM 1422 O HIS A 192 -31.434 11.962 -29.244 1.00 76.16 O ANISOU 1422 O HIS A 192 9902 8812 10226 -417 -2062 -21 O ATOM 1423 CB HIS A 192 -32.471 12.108 -26.242 1.00 73.24 C ANISOU 1423 CB HIS A 192 9252 8508 10069 -268 -1909 31 C ATOM 1424 CG HIS A 192 -33.300 11.621 -25.092 1.00 76.84 C ANISOU 1424 CG HIS A 192 9581 9013 10602 -281 -1864 53 C ATOM 1425 ND1 HIS A 192 -34.288 12.412 -24.529 1.00 78.92 N ANISOU 1425 ND1 HIS A 192 9669 9367 10951 -211 -1874 114 N ATOM 1426 CD2 HIS A 192 -33.256 10.441 -24.430 1.00 78.01 C ANISOU 1426 CD2 HIS A 192 9757 9130 10753 -356 -1806 23 C ATOM 1427 CE1 HIS A 192 -34.807 11.690 -23.547 1.00 78.40 C ANISOU 1427 CE1 HIS A 192 9529 9328 10931 -251 -1819 115 C ATOM 1428 NE2 HIS A 192 -34.224 10.494 -23.454 1.00 78.16 N ANISOU 1428 NE2 HIS A 192 9619 9226 10852 -342 -1781 64 N ATOM 1429 N ARG A 193 -32.632 13.878 -29.049 1.00 72.80 N ANISOU 1429 N ARG A 193 9251 8509 9902 -272 -2144 102 N ATOM 1430 CA ARG A 193 -31.907 14.651 -30.080 1.00 72.77 C ANISOU 1430 CA ARG A 193 9352 8472 9824 -246 -2189 99 C ATOM 1431 C ARG A 193 -30.461 14.874 -29.656 1.00 74.12 C ANISOU 1431 C ARG A 193 9646 8546 9971 -162 -2074 34 C ATOM 1432 O ARG A 193 -29.565 14.772 -30.488 1.00 74.51 O ANISOU 1432 O ARG A 193 9838 8542 9930 -200 -2077 -10 O ATOM 1433 CB ARG A 193 -32.565 16.023 -30.351 1.00 75.69 C ANISOU 1433 CB ARG A 193 9612 8905 10241 -155 -2268 185 C ATOM 1434 CG ARG A 193 -34.045 15.980 -30.712 1.00 90.92 C ANISOU 1434 CG ARG A 193 11389 10945 12210 -217 -2386 266 C ATOM 1435 CD ARG A 193 -34.613 17.383 -30.779 1.00108.47 C ANISOU 1435 CD ARG A 193 13496 13217 14501 -94 -2443 352 C ATOM 1436 NE ARG A 193 -35.978 17.401 -31.308 1.00121.00 N ANISOU 1436 NE ARG A 193 14939 14916 16121 -153 -2573 441 N ATOM 1437 CZ ARG A 193 -36.576 18.479 -31.809 1.00136.04 C ANISOU 1437 CZ ARG A 193 16754 16872 18063 -83 -2667 531 C ATOM 1438 NH1 ARG A 193 -35.934 19.640 -31.862 1.00124.09 N ANISOU 1438 NH1 ARG A 193 15290 15300 16557 45 -2644 542 N ATOM 1439 NH2 ARG A 193 -37.819 18.401 -32.266 1.00121.25 N ANISOU 1439 NH2 ARG A 193 14741 15109 16221 -142 -2788 615 N ATOM 1440 N SER A 194 -30.229 15.164 -28.360 1.00 68.15 N ANISOU 1440 N SER A 194 8832 7770 9290 -55 -1972 27 N ATOM 1441 CA SER A 194 -28.878 15.376 -27.838 1.00 66.26 C ANISOU 1441 CA SER A 194 8696 7450 9032 22 -1864 -27 C ATOM 1442 C SER A 194 -28.736 15.044 -26.362 1.00 68.93 C ANISOU 1442 C SER A 194 8983 7771 9438 76 -1753 -46 C ATOM 1443 O SER A 194 -29.723 14.964 -25.616 1.00 70.43 O ANISOU 1443 O SER A 194 9041 8016 9701 83 -1750 -10 O ATOM 1444 CB SER A 194 -28.411 16.811 -28.089 1.00 69.36 C ANISOU 1444 CB SER A 194 9104 7832 9418 128 -1873 -3 C ATOM 1445 OG SER A 194 -28.957 17.720 -27.142 1.00 80.94 O ANISOU 1445 OG SER A 194 10446 9330 10977 240 -1844 41 O ATOM 1446 N TYR A 195 -27.483 14.871 -25.945 1.00 62.04 N ANISOU 1446 N TYR A 195 8212 6825 8536 112 -1661 -99 N ATOM 1447 CA TYR A 195 -27.117 14.683 -24.550 1.00 60.10 C ANISOU 1447 CA TYR A 195 7937 6558 8341 170 -1554 -114 C ATOM 1448 C TYR A 195 -26.078 15.745 -24.167 1.00 62.21 C ANISOU 1448 C TYR A 195 8247 6789 8599 281 -1492 -126 C ATOM 1449 O TYR A 195 -25.208 16.079 -24.970 1.00 60.61 O ANISOU 1449 O TYR A 195 8147 6549 8332 286 -1504 -149 O ATOM 1450 CB TYR A 195 -26.605 13.266 -24.286 1.00 59.89 C ANISOU 1450 CB TYR A 195 7986 6477 8292 96 -1502 -161 C ATOM 1451 CG TYR A 195 -27.693 12.290 -23.891 1.00 61.23 C ANISOU 1451 CG TYR A 195 8077 6685 8504 12 -1520 -143 C ATOM 1452 CD1 TYR A 195 -28.429 11.608 -24.857 1.00 63.70 C ANISOU 1452 CD1 TYR A 195 8396 7020 8786 -105 -1608 -138 C ATOM 1453 CD2 TYR A 195 -27.937 11.989 -22.551 1.00 62.20 C ANISOU 1453 CD2 TYR A 195 8125 6820 8687 36 -1448 -131 C ATOM 1454 CE1 TYR A 195 -29.419 10.690 -24.503 1.00 63.88 C ANISOU 1454 CE1 TYR A 195 8349 7079 8843 -195 -1626 -121 C ATOM 1455 CE2 TYR A 195 -28.911 11.051 -22.183 1.00 63.88 C ANISOU 1455 CE2 TYR A 195 8269 7067 8933 -52 -1462 -114 C ATOM 1456 CZ TYR A 195 -29.662 10.417 -23.166 1.00 71.83 C ANISOU 1456 CZ TYR A 195 9280 8098 9914 -167 -1552 -108 C ATOM 1457 OH TYR A 195 -30.637 9.500 -22.837 1.00 75.22 O ANISOU 1457 OH TYR A 195 9642 8565 10372 -265 -1570 -89 O ATOM 1458 N SER A 196 -26.189 16.301 -22.958 1.00 59.54 N ANISOU 1458 N SER A 196 7834 6467 8322 363 -1425 -112 N ATOM 1459 CA SER A 196 -25.236 17.307 -22.513 1.00 58.02 C ANISOU 1459 CA SER A 196 7684 6242 8119 457 -1364 -124 C ATOM 1460 C SER A 196 -24.661 17.033 -21.123 1.00 59.29 C ANISOU 1460 C SER A 196 7841 6384 8303 491 -1256 -145 C ATOM 1461 O SER A 196 -25.340 16.510 -20.245 1.00 58.01 O ANISOU 1461 O SER A 196 7597 6252 8190 475 -1226 -133 O ATOM 1462 CB SER A 196 -25.816 18.711 -22.623 1.00 63.06 C ANISOU 1462 CB SER A 196 8256 6911 8794 539 -1399 -82 C ATOM 1463 OG SER A 196 -26.854 18.940 -21.686 1.00 77.97 O ANISOU 1463 OG SER A 196 10012 8849 10765 578 -1375 -53 O ATOM 1464 N CYS A 197 -23.369 17.327 -20.972 1.00 54.92 N ANISOU 1464 N CYS A 197 7378 5784 7705 528 -1202 -174 N ATOM 1465 CA CYS A 197 -22.616 17.224 -19.733 1.00 53.86 C ANISOU 1465 CA CYS A 197 7253 5632 7578 562 -1106 -189 C ATOM 1466 C CYS A 197 -22.319 18.708 -19.357 1.00 55.61 C ANISOU 1466 C CYS A 197 7469 5857 7802 650 -1077 -182 C ATOM 1467 O CYS A 197 -21.741 19.440 -20.143 1.00 52.91 O ANISOU 1467 O CYS A 197 7193 5492 7417 673 -1104 -188 O ATOM 1468 CB CYS A 197 -21.333 16.429 -19.965 1.00 54.29 C ANISOU 1468 CB CYS A 197 7416 5634 7578 531 -1075 -224 C ATOM 1469 SG CYS A 197 -20.294 16.210 -18.492 1.00 58.79 S ANISOU 1469 SG CYS A 197 8001 6187 8151 566 -969 -233 S ATOM 1470 N GLN A 198 -22.736 19.125 -18.172 1.00 53.46 N ANISOU 1470 N GLN A 198 7125 5610 7577 694 -1020 -172 N ATOM 1471 CA GLN A 198 -22.538 20.456 -17.629 1.00 53.91 C ANISOU 1471 CA GLN A 198 7177 5665 7641 773 -979 -170 C ATOM 1472 C GLN A 198 -21.566 20.285 -16.462 1.00 55.06 C ANISOU 1472 C GLN A 198 7360 5799 7763 777 -888 -192 C ATOM 1473 O GLN A 198 -21.839 19.510 -15.554 1.00 55.49 O ANISOU 1473 O GLN A 198 7369 5874 7841 749 -846 -189 O ATOM 1474 CB GLN A 198 -23.903 21.061 -17.220 1.00 57.18 C ANISOU 1474 CB GLN A 198 7474 6122 8130 817 -983 -144 C ATOM 1475 CG GLN A 198 -23.890 22.081 -16.075 1.00 81.88 C ANISOU 1475 CG GLN A 198 10575 9251 11283 889 -901 -152 C ATOM 1476 CD GLN A 198 -25.276 22.431 -15.579 1.00102.61 C ANISOU 1476 CD GLN A 198 13073 11923 13991 929 -890 -130 C ATOM 1477 OE1 GLN A 198 -26.253 22.473 -16.338 1.00 99.79 O ANISOU 1477 OE1 GLN A 198 12647 11592 13677 933 -962 -98 O ATOM 1478 NE2 GLN A 198 -25.389 22.709 -14.288 1.00 92.14 N ANISOU 1478 NE2 GLN A 198 11710 10611 12686 957 -797 -146 N ATOM 1479 N VAL A 199 -20.376 20.909 -16.561 1.00 48.64 N ANISOU 1479 N VAL A 199 6633 4953 6895 800 -865 -209 N ATOM 1480 CA VAL A 199 -19.324 20.806 -15.555 1.00 46.46 C ANISOU 1480 CA VAL A 199 6396 4670 6585 799 -790 -223 C ATOM 1481 C VAL A 199 -19.201 22.168 -14.857 1.00 51.96 C ANISOU 1481 C VAL A 199 7097 5368 7280 855 -742 -229 C ATOM 1482 O VAL A 199 -18.946 23.169 -15.506 1.00 52.51 O ANISOU 1482 O VAL A 199 7211 5414 7328 888 -767 -232 O ATOM 1483 CB VAL A 199 -17.957 20.318 -16.150 1.00 49.82 C ANISOU 1483 CB VAL A 199 6915 5065 6948 771 -794 -239 C ATOM 1484 CG1 VAL A 199 -16.874 20.227 -15.069 1.00 48.29 C ANISOU 1484 CG1 VAL A 199 6749 4875 6723 770 -723 -243 C ATOM 1485 CG2 VAL A 199 -18.089 18.974 -16.892 1.00 49.49 C ANISOU 1485 CG2 VAL A 199 6883 5011 6909 717 -835 -241 C ATOM 1486 N THR A 200 -19.374 22.192 -13.540 1.00 50.17 N ANISOU 1486 N THR A 200 6828 5165 7069 860 -672 -231 N ATOM 1487 CA THR A 200 -19.245 23.385 -12.725 1.00 49.81 C ANISOU 1487 CA THR A 200 6793 5117 7016 903 -613 -244 C ATOM 1488 C THR A 200 -17.951 23.238 -11.915 1.00 52.73 C ANISOU 1488 C THR A 200 7223 5489 7323 872 -558 -254 C ATOM 1489 O THR A 200 -17.704 22.201 -11.287 1.00 49.44 O ANISOU 1489 O THR A 200 6790 5093 6900 829 -536 -245 O ATOM 1490 CB THR A 200 -20.494 23.604 -11.853 1.00 56.13 C ANISOU 1490 CB THR A 200 7498 5948 7879 929 -570 -243 C ATOM 1491 OG1 THR A 200 -21.624 23.676 -12.715 1.00 56.59 O ANISOU 1491 OG1 THR A 200 7494 6012 7996 956 -633 -225 O ATOM 1492 CG2 THR A 200 -20.414 24.893 -11.017 1.00 53.12 C ANISOU 1492 CG2 THR A 200 7137 5556 7490 977 -500 -265 C ATOM 1493 N HIS A 201 -17.124 24.281 -11.968 1.00 49.01 N ANISOU 1493 N HIS A 201 6823 4995 6804 891 -542 -269 N ATOM 1494 CA HIS A 201 -15.845 24.339 -11.286 1.00 47.94 C ANISOU 1494 CA HIS A 201 6746 4868 6603 861 -497 -275 C ATOM 1495 C HIS A 201 -15.703 25.739 -10.756 1.00 54.68 C ANISOU 1495 C HIS A 201 7638 5707 7431 887 -452 -296 C ATOM 1496 O HIS A 201 -15.631 26.680 -11.546 1.00 52.95 O ANISOU 1496 O HIS A 201 7465 5451 7204 919 -480 -303 O ATOM 1497 CB HIS A 201 -14.693 24.022 -12.266 1.00 47.69 C ANISOU 1497 CB HIS A 201 6778 4819 6522 840 -540 -271 C ATOM 1498 CG HIS A 201 -13.351 23.994 -11.597 1.00 50.23 C ANISOU 1498 CG HIS A 201 7144 5160 6780 807 -500 -269 C ATOM 1499 ND1 HIS A 201 -12.427 25.007 -11.792 1.00 51.44 N ANISOU 1499 ND1 HIS A 201 7366 5303 6875 806 -492 -280 N ATOM 1500 CD2 HIS A 201 -12.870 23.134 -10.670 1.00 50.46 C ANISOU 1500 CD2 HIS A 201 7153 5221 6798 772 -467 -252 C ATOM 1501 CE1 HIS A 201 -11.396 24.704 -11.020 1.00 50.19 C ANISOU 1501 CE1 HIS A 201 7222 5178 6672 769 -458 -270 C ATOM 1502 NE2 HIS A 201 -11.630 23.597 -10.304 1.00 50.05 N ANISOU 1502 NE2 HIS A 201 7151 5185 6681 750 -442 -250 N ATOM 1503 N GLU A 202 -15.688 25.890 -9.425 1.00 55.82 N ANISOU 1503 N GLU A 202 7771 5877 7561 870 -381 -305 N ATOM 1504 CA GLU A 202 -15.518 27.205 -8.769 1.00 57.88 C ANISOU 1504 CA GLU A 202 8080 6121 7790 884 -325 -333 C ATOM 1505 C GLU A 202 -16.528 28.226 -9.270 1.00 62.90 C ANISOU 1505 C GLU A 202 8705 6712 8481 955 -332 -347 C ATOM 1506 O GLU A 202 -16.125 29.340 -9.625 1.00 64.98 O ANISOU 1506 O GLU A 202 9042 6932 8717 977 -333 -361 O ATOM 1507 CB GLU A 202 -14.082 27.755 -9.032 1.00 59.13 C ANISOU 1507 CB GLU A 202 8333 6266 7866 854 -332 -337 C ATOM 1508 CG GLU A 202 -12.948 26.839 -8.592 1.00 60.91 C ANISOU 1508 CG GLU A 202 8568 6537 8039 791 -329 -315 C ATOM 1509 CD GLU A 202 -12.857 26.667 -7.093 1.00 73.29 C ANISOU 1509 CD GLU A 202 10119 8148 9578 748 -263 -316 C ATOM 1510 OE1 GLU A 202 -12.706 27.678 -6.373 1.00 62.17 O ANISOU 1510 OE1 GLU A 202 8756 6736 8129 736 -211 -342 O ATOM 1511 OE2 GLU A 202 -12.909 25.504 -6.641 1.00 83.34 O ANISOU 1511 OE2 GLU A 202 11342 9458 10867 721 -263 -289 O ATOM 1512 N GLY A 203 -17.797 27.845 -9.398 1.00 58.82 N ANISOU 1512 N GLY A 203 8100 6206 8042 991 -344 -338 N ATOM 1513 CA GLY A 203 -18.782 28.800 -9.913 1.00 60.35 C ANISOU 1513 CA GLY A 203 8271 6361 8298 1067 -357 -342 C ATOM 1514 C GLY A 203 -18.690 29.149 -11.393 1.00 64.04 C ANISOU 1514 C GLY A 203 8774 6788 8771 1095 -446 -321 C ATOM 1515 O GLY A 203 -19.435 30.006 -11.879 1.00 65.96 O ANISOU 1515 O GLY A 203 9004 6994 9064 1161 -466 -315 O ATOM 1516 N SER A 204 -17.781 28.497 -12.128 1.00 57.75 N ANISOU 1516 N SER A 204 8021 5998 7924 1046 -499 -308 N ATOM 1517 CA SER A 204 -17.659 28.640 -13.570 1.00 56.36 C ANISOU 1517 CA SER A 204 7879 5793 7741 1055 -585 -288 C ATOM 1518 C SER A 204 -18.272 27.344 -14.169 1.00 58.53 C ANISOU 1518 C SER A 204 8082 6103 8054 1032 -642 -266 C ATOM 1519 O SER A 204 -17.956 26.258 -13.709 1.00 57.62 O ANISOU 1519 O SER A 204 7946 6020 7925 984 -623 -268 O ATOM 1520 CB SER A 204 -16.200 28.849 -13.963 1.00 59.62 C ANISOU 1520 CB SER A 204 8394 6192 8067 1013 -592 -295 C ATOM 1521 OG SER A 204 -15.890 28.311 -15.239 1.00 71.20 O ANISOU 1521 OG SER A 204 9882 7657 9513 989 -667 -279 O ATOM 1522 N THR A 205 -19.207 27.470 -15.106 1.00 55.53 N ANISOU 1522 N THR A 205 7663 5715 7722 1063 -711 -243 N ATOM 1523 CA THR A 205 -19.906 26.334 -15.712 1.00 55.40 C ANISOU 1523 CA THR A 205 7580 5730 7739 1033 -770 -222 C ATOM 1524 C THR A 205 -19.676 26.307 -17.208 1.00 58.81 C ANISOU 1524 C THR A 205 8062 6143 8139 1015 -860 -206 C ATOM 1525 O THR A 205 -19.835 27.324 -17.874 1.00 56.98 O ANISOU 1525 O THR A 205 7861 5881 7909 1054 -899 -191 O ATOM 1526 CB THR A 205 -21.438 26.375 -15.414 1.00 61.74 C ANISOU 1526 CB THR A 205 8266 6561 8633 1075 -774 -204 C ATOM 1527 OG1 THR A 205 -21.658 26.189 -14.026 1.00 59.61 O ANISOU 1527 OG1 THR A 205 7948 6318 8385 1076 -686 -222 O ATOM 1528 CG2 THR A 205 -22.200 25.281 -16.122 1.00 65.84 C ANISOU 1528 CG2 THR A 205 8719 7115 9181 1034 -845 -179 C ATOM 1529 N VAL A 206 -19.393 25.119 -17.727 1.00 55.73 N ANISOU 1529 N VAL A 206 7680 5770 7725 954 -893 -208 N ATOM 1530 CA VAL A 206 -19.219 24.840 -19.148 1.00 57.69 C ANISOU 1530 CA VAL A 206 7974 6007 7936 919 -974 -199 C ATOM 1531 C VAL A 206 -20.162 23.656 -19.499 1.00 62.91 C ANISOU 1531 C VAL A 206 8566 6701 8637 877 -1022 -186 C ATOM 1532 O VAL A 206 -20.199 22.654 -18.773 1.00 62.01 O ANISOU 1532 O VAL A 206 8416 6606 8540 846 -981 -197 O ATOM 1533 CB VAL A 206 -17.719 24.536 -19.452 1.00 62.06 C ANISOU 1533 CB VAL A 206 8628 6545 8409 878 -953 -225 C ATOM 1534 CG1 VAL A 206 -17.555 23.615 -20.656 1.00 63.12 C ANISOU 1534 CG1 VAL A 206 8796 6679 8509 821 -1012 -230 C ATOM 1535 CG2 VAL A 206 -16.931 25.823 -19.650 1.00 61.59 C ANISOU 1535 CG2 VAL A 206 8645 6454 8301 905 -943 -228 C ATOM 1536 N GLU A 207 -20.925 23.795 -20.582 1.00 62.36 N ANISOU 1536 N GLU A 207 8479 6638 8579 870 -1109 -160 N ATOM 1537 CA GLU A 207 -21.819 22.755 -21.065 1.00 64.19 C ANISOU 1537 CA GLU A 207 8652 6901 8836 817 -1166 -146 C ATOM 1538 C GLU A 207 -21.376 22.319 -22.428 1.00 70.08 C ANISOU 1538 C GLU A 207 9478 7634 9516 755 -1234 -153 C ATOM 1539 O GLU A 207 -21.183 23.165 -23.298 1.00 69.87 O ANISOU 1539 O GLU A 207 9502 7592 9454 768 -1283 -138 O ATOM 1540 CB GLU A 207 -23.272 23.214 -21.124 1.00 67.05 C ANISOU 1540 CB GLU A 207 8904 7298 9273 854 -1216 -103 C ATOM 1541 CG GLU A 207 -24.227 22.051 -20.900 1.00 80.57 C ANISOU 1541 CG GLU A 207 10527 9057 11030 800 -1232 -94 C ATOM 1542 CD GLU A 207 -25.693 22.422 -20.837 1.00 97.42 C ANISOU 1542 CD GLU A 207 12530 11239 13245 835 -1274 -49 C ATOM 1543 OE1 GLU A 207 -26.223 22.925 -21.855 1.00 95.09 O ANISOU 1543 OE1 GLU A 207 12223 10954 12955 843 -1364 -10 O ATOM 1544 OE2 GLU A 207 -26.321 22.175 -19.783 1.00 85.26 O ANISOU 1544 OE2 GLU A 207 10898 9732 11764 850 -1218 -48 O ATOM 1545 N LYS A 208 -21.225 20.989 -22.613 1.00 66.74 N ANISOU 1545 N LYS A 208 9071 7213 9073 683 -1234 -176 N ATOM 1546 CA LYS A 208 -20.809 20.348 -23.859 1.00 66.21 C ANISOU 1546 CA LYS A 208 9084 7131 8940 612 -1284 -195 C ATOM 1547 C LYS A 208 -21.935 19.432 -24.365 1.00 72.87 C ANISOU 1547 C LYS A 208 9876 8005 9807 544 -1352 -180 C ATOM 1548 O LYS A 208 -22.734 18.951 -23.563 1.00 73.40 O ANISOU 1548 O LYS A 208 9853 8098 9937 542 -1336 -167 O ATOM 1549 CB LYS A 208 -19.505 19.568 -23.651 1.00 66.80 C ANISOU 1549 CB LYS A 208 9241 7172 8969 588 -1214 -242 C ATOM 1550 CG LYS A 208 -18.299 20.441 -23.348 1.00 71.46 C ANISOU 1550 CG LYS A 208 9889 7742 9522 637 -1158 -255 C ATOM 1551 CD LYS A 208 -17.571 20.875 -24.599 1.00 75.73 C ANISOU 1551 CD LYS A 208 10525 8265 9983 614 -1193 -268 C ATOM 1552 CE LYS A 208 -16.335 21.665 -24.284 1.00 71.51 C ANISOU 1552 CE LYS A 208 10047 7715 9408 650 -1135 -281 C ATOM 1553 NZ LYS A 208 -15.310 21.447 -25.330 1.00 85.99 N ANISOU 1553 NZ LYS A 208 11977 9534 11160 607 -1136 -312 N ATOM 1554 N THR A 209 -22.014 19.209 -25.681 1.00 70.35 N ANISOU 1554 N THR A 209 9612 7686 9433 480 -1429 -182 N ATOM 1555 CA THR A 209 -23.070 18.381 -26.282 1.00 71.53 C ANISOU 1555 CA THR A 209 9720 7866 9590 399 -1504 -167 C ATOM 1556 C THR A 209 -22.521 17.347 -27.256 1.00 75.67 C ANISOU 1556 C THR A 209 10351 8362 10039 303 -1520 -213 C ATOM 1557 O THR A 209 -21.480 17.576 -27.878 1.00 73.92 O ANISOU 1557 O THR A 209 10232 8108 9748 301 -1503 -244 O ATOM 1558 CB THR A 209 -24.139 19.254 -27.001 1.00 82.65 C ANISOU 1558 CB THR A 209 11066 9321 11016 407 -1610 -106 C ATOM 1559 OG1 THR A 209 -23.494 20.123 -27.927 1.00 86.28 O ANISOU 1559 OG1 THR A 209 11613 9761 11410 419 -1645 -102 O ATOM 1560 CG2 THR A 209 -25.004 20.066 -26.044 1.00 79.98 C ANISOU 1560 CG2 THR A 209 10600 9017 10772 496 -1597 -60 C ATOM 1561 N VAL A 210 -23.247 16.209 -27.374 1.00 74.69 N ANISOU 1561 N VAL A 210 10202 8250 9927 220 -1547 -219 N ATOM 1562 CA VAL A 210 -23.041 15.070 -28.283 1.00 75.93 C ANISOU 1562 CA VAL A 210 10451 8379 10020 113 -1568 -264 C ATOM 1563 C VAL A 210 -24.406 14.594 -28.797 1.00 82.59 C ANISOU 1563 C VAL A 210 11233 9273 10874 23 -1664 -232 C ATOM 1564 O VAL A 210 -25.374 14.535 -28.022 1.00 80.44 O ANISOU 1564 O VAL A 210 10841 9043 10677 36 -1674 -193 O ATOM 1565 CB VAL A 210 -22.210 13.873 -27.717 1.00 79.82 C ANISOU 1565 CB VAL A 210 11005 8809 10513 97 -1473 -321 C ATOM 1566 CG1 VAL A 210 -20.718 14.180 -27.716 1.00 79.43 C ANISOU 1566 CG1 VAL A 210 11046 8712 10422 154 -1396 -360 C ATOM 1567 CG2 VAL A 210 -22.696 13.420 -26.339 1.00 79.05 C ANISOU 1567 CG2 VAL A 210 10814 8721 10501 124 -1424 -301 C ATOM 1568 N ALA A 211 -24.474 14.245 -30.096 1.00 83.29 N ANISOU 1568 N ALA A 211 11401 9362 10883 -74 -1734 -249 N ATOM 1569 CA ALA A 211 -25.699 13.771 -30.745 1.00 85.87 C ANISOU 1569 CA ALA A 211 11683 9741 11202 -180 -1836 -220 C ATOM 1570 C ALA A 211 -25.466 12.495 -31.590 1.00 95.25 C ANISOU 1570 C ALA A 211 12991 10887 12311 -312 -1842 -283 C ATOM 1571 O ALA A 211 -24.373 12.344 -32.154 1.00 94.79 O ANISOU 1571 O ALA A 211 13061 10772 12183 -320 -1796 -341 O ATOM 1572 CB ALA A 211 -26.286 14.876 -31.612 1.00 86.92 C ANISOU 1572 CB ALA A 211 11779 9936 11312 -176 -1947 -157 C ATOM 1573 N PRO A 212 -26.474 11.583 -31.713 1.00 95.90 N ANISOU 1573 N PRO A 212 13037 10998 12403 -421 -1895 -275 N ATOM 1574 CA PRO A 212 -26.276 10.376 -32.545 1.00 97.88 C ANISOU 1574 CA PRO A 212 13415 11200 12574 -555 -1899 -341 C ATOM 1575 C PRO A 212 -26.113 10.677 -34.039 1.00107.71 C ANISOU 1575 C PRO A 212 14759 12459 13706 -634 -1975 -355 C ATOM 1576 O PRO A 212 -27.044 11.184 -34.682 1.00108.34 O ANISOU 1576 O PRO A 212 14779 12619 13766 -686 -2093 -294 O ATOM 1577 CB PRO A 212 -27.516 9.516 -32.250 1.00100.01 C ANISOU 1577 CB PRO A 212 13605 11510 12885 -653 -1948 -315 C ATOM 1578 CG PRO A 212 -28.202 10.159 -31.099 1.00103.32 C ANISOU 1578 CG PRO A 212 13856 11989 13412 -556 -1943 -245 C ATOM 1579 CD PRO A 212 -27.824 11.600 -31.113 1.00 98.04 C ANISOU 1579 CD PRO A 212 13152 11345 12753 -432 -1950 -209 C ATOM 1580 N THR A 213 -24.906 10.392 -34.582 1.00107.55 N ANISOU 1580 N THR A 213 14887 12365 13612 -640 -1906 -431 N ATOM 1581 CA THR A 213 -24.564 10.620 -35.998 1.00109.32 C ANISOU 1581 CA THR A 213 15226 12594 13715 -719 -1957 -459 C ATOM 1582 C THR A 213 -23.645 9.514 -36.550 1.00115.48 C ANISOU 1582 C THR A 213 16174 13284 14421 -791 -1875 -565 C ATOM 1583 O THR A 213 -22.747 9.044 -35.840 1.00114.30 O ANISOU 1583 O THR A 213 16057 13058 14312 -718 -1757 -614 O ATOM 1584 CB THR A 213 -24.019 12.057 -36.235 1.00119.27 C ANISOU 1584 CB THR A 213 16478 13883 14957 -622 -1971 -420 C ATOM 1585 OG1 THR A 213 -23.798 12.262 -37.635 1.00122.52 O ANISOU 1585 OG1 THR A 213 16999 14308 15245 -714 -2030 -439 O ATOM 1586 CG2 THR A 213 -22.748 12.379 -35.428 1.00115.96 C ANISOU 1586 CG2 THR A 213 16081 13404 14575 -490 -1843 -454 C ATOM 1587 N GLU A 214 -23.886 9.105 -37.823 1.00115.09 N ANISOU 1587 N GLU A 214 16226 13244 14261 -935 -1938 -599 N ATOM 1588 CA GLU A 214 -23.137 8.056 -38.540 1.00115.87 C ANISOU 1588 CA GLU A 214 16494 13258 14275 -1022 -1867 -707 C ATOM 1589 C GLU A 214 -21.856 8.577 -39.212 1.00120.03 C ANISOU 1589 C GLU A 214 17130 13755 14722 -980 -1803 -758 C ATOM 1590 O GLU A 214 -21.837 9.693 -39.738 1.00120.02 O ANISOU 1590 O GLU A 214 17111 13816 14675 -963 -1866 -711 O ATOM 1591 CB GLU A 214 -24.032 7.333 -39.572 1.00118.70 C ANISOU 1591 CB GLU A 214 16917 13641 14543 -1212 -1961 -725 C ATOM 1592 CG GLU A 214 -23.581 5.911 -39.890 1.00129.04 C ANISOU 1592 CG GLU A 214 18377 14846 15806 -1304 -1875 -836 C ATOM 1593 CD GLU A 214 -24.303 5.185 -41.012 1.00150.27 C ANISOU 1593 CD GLU A 214 21162 17549 18386 -1505 -1956 -871 C ATOM 1594 OE1 GLU A 214 -25.552 5.109 -40.972 1.00149.69 O ANISOU 1594 OE1 GLU A 214 20999 17548 18328 -1591 -2069 -806 O ATOM 1595 OE2 GLU A 214 -23.612 4.631 -41.898 1.00139.34 O ANISOU 1595 OE2 GLU A 214 19943 16100 16899 -1581 -1900 -968 O ATOM 1596 N CYS A 215 -20.798 7.743 -39.198 0.50116.06 N ANISOU 1596 N CYS A 215 16738 13155 14205 -965 -1676 -854 N ATOM 1597 CA CYS A 215 -19.495 8.015 -39.803 0.50138.29 C ANISOU 1597 CA CYS A 215 19662 15935 16948 -930 -1592 -918 C ATOM 1598 C CYS A 215 -19.591 7.938 -41.331 0.50160.57 C ANISOU 1598 C CYS A 215 22610 18778 19619 -1080 -1647 -962 C ATOM 1599 O CYS A 215 -20.132 6.975 -41.874 0.50119.55 O ANISOU 1599 O CYS A 215 17490 13558 14374 -1213 -1672 -1008 O ATOM 1600 CB CYS A 215 -18.446 7.050 -39.253 1.00138.11 C ANISOU 1600 CB CYS A 215 19703 15804 16970 -866 -1440 -1000 C ATOM 1601 SG CYS A 215 -16.868 7.064 -40.146 1.00142.10 S ANISOU 1601 SG CYS A 215 20353 16259 17379 -849 -1322 -1099 S TER 1602 CYS A 215 ATOM 1603 N SER B 2 -21.791 9.970 22.618 1.00 83.83 N ANISOU 1603 N SER B 2 10315 12535 9002 -501 -86 -263 N ATOM 1604 CA SER B 2 -23.136 10.098 22.051 1.00 81.84 C ANISOU 1604 CA SER B 2 10147 11994 8956 -527 1 -217 C ATOM 1605 C SER B 2 -24.215 9.869 23.109 1.00 84.54 C ANISOU 1605 C SER B 2 10543 12355 9223 -598 68 -204 C ATOM 1606 O SER B 2 -23.961 9.194 24.118 1.00 85.22 O ANISOU 1606 O SER B 2 10667 12621 9091 -582 22 -152 O ATOM 1607 CB SER B 2 -23.326 9.136 20.881 1.00 84.65 C ANISOU 1607 CB SER B 2 10597 12161 9407 -393 -76 -34 C ATOM 1608 OG SER B 2 -22.941 9.728 19.650 1.00 93.97 O ANISOU 1608 OG SER B 2 11734 13215 10757 -369 -74 -72 O ATOM 1609 N VAL B 3 -25.416 10.445 22.886 1.00 78.55 N ANISOU 1609 N VAL B 3 9785 11431 8628 -661 184 -250 N ATOM 1610 CA VAL B 3 -26.552 10.288 23.811 1.00 78.05 C ANISOU 1610 CA VAL B 3 9753 11391 8511 -741 268 -255 C ATOM 1611 C VAL B 3 -27.128 8.854 23.627 1.00 78.31 C ANISOU 1611 C VAL B 3 9908 11359 8486 -696 211 -65 C ATOM 1612 O VAL B 3 -27.419 8.164 24.610 1.00 78.55 O ANISOU 1612 O VAL B 3 10024 11475 8347 -741 227 -15 O ATOM 1613 CB VAL B 3 -27.603 11.424 23.639 1.00 81.20 C ANISOU 1613 CB VAL B 3 10091 11676 9086 -793 422 -375 C ATOM 1614 CG1 VAL B 3 -28.835 11.195 24.507 1.00 81.50 C ANISOU 1614 CG1 VAL B 3 10137 11759 9072 -870 511 -382 C ATOM 1615 CG2 VAL B 3 -26.985 12.783 23.946 1.00 81.68 C ANISOU 1615 CG2 VAL B 3 10101 11762 9171 -863 526 -571 C ATOM 1616 N LEU B 4 -27.239 8.413 22.362 1.00 70.23 N ANISOU 1616 N LEU B 4 8914 10179 7590 -621 160 32 N ATOM 1617 CA LEU B 4 -27.696 7.067 22.016 1.00 68.68 C ANISOU 1617 CA LEU B 4 8859 9891 7343 -609 132 188 C ATOM 1618 C LEU B 4 -26.469 6.126 21.896 1.00 70.60 C ANISOU 1618 C LEU B 4 9228 10145 7453 -474 24 320 C ATOM 1619 O LEU B 4 -25.393 6.554 21.455 1.00 67.64 O ANISOU 1619 O LEU B 4 8778 9816 7107 -380 -52 293 O ATOM 1620 CB LEU B 4 -28.502 7.060 20.703 1.00 66.86 C ANISOU 1620 CB LEU B 4 8590 9518 7298 -613 144 207 C ATOM 1621 CG LEU B 4 -29.697 8.009 20.542 1.00 70.23 C ANISOU 1621 CG LEU B 4 8866 9957 7862 -668 239 98 C ATOM 1622 CD1 LEU B 4 -30.298 7.884 19.139 1.00 68.48 C ANISOU 1622 CD1 LEU B 4 8592 9651 7775 -631 216 139 C ATOM 1623 CD2 LEU B 4 -30.764 7.757 21.586 1.00 71.82 C ANISOU 1623 CD2 LEU B 4 9067 10251 7970 -802 340 59 C ATOM 1624 N THR B 5 -26.638 4.855 22.301 1.00 67.86 N ANISOU 1624 N THR B 5 9082 9755 6944 -460 38 459 N ATOM 1625 CA THR B 5 -25.553 3.871 22.254 1.00 68.45 C ANISOU 1625 CA THR B 5 9312 9830 6865 -280 -39 610 C ATOM 1626 C THR B 5 -25.711 2.841 21.085 1.00 71.33 C ANISOU 1626 C THR B 5 9850 9958 7292 -240 -32 735 C ATOM 1627 O THR B 5 -26.645 2.026 21.071 1.00 71.96 O ANISOU 1627 O THR B 5 10104 9895 7342 -356 69 790 O ATOM 1628 CB THR B 5 -25.388 3.219 23.632 1.00 76.09 C ANISOU 1628 CB THR B 5 10430 10920 7562 -237 -12 693 C ATOM 1629 OG1 THR B 5 -25.125 4.254 24.590 1.00 79.26 O ANISOU 1629 OG1 THR B 5 10643 11566 7908 -288 -28 550 O ATOM 1630 CG2 THR B 5 -24.258 2.183 23.666 1.00 73.16 C ANISOU 1630 CG2 THR B 5 10233 10571 6992 17 -81 874 C ATOM 1631 N GLN B 6 -24.728 2.852 20.166 1.00 65.83 N ANISOU 1631 N GLN B 6 9115 9238 6658 -90 -124 768 N ATOM 1632 CA GLN B 6 -24.648 1.972 18.999 1.00 65.83 C ANISOU 1632 CA GLN B 6 9268 9030 6714 -33 -124 871 C ATOM 1633 C GLN B 6 -23.335 1.182 18.994 1.00 74.16 C ANISOU 1633 C GLN B 6 10456 10107 7614 226 -187 1010 C ATOM 1634 O GLN B 6 -22.299 1.791 19.272 1.00 75.44 O ANISOU 1634 O GLN B 6 10445 10487 7730 353 -283 966 O ATOM 1635 CB GLN B 6 -24.640 2.813 17.722 1.00 63.98 C ANISOU 1635 CB GLN B 6 8847 8752 6712 -65 -175 777 C ATOM 1636 CG GLN B 6 -25.979 3.020 17.085 1.00 69.10 C ANISOU 1636 CG GLN B 6 9448 9301 7505 -248 -109 714 C ATOM 1637 CD GLN B 6 -25.798 3.772 15.792 1.00 63.77 C ANISOU 1637 CD GLN B 6 8623 8587 7019 -217 -165 658 C ATOM 1638 OE1 GLN B 6 -25.818 5.003 15.731 1.00 55.42 O ANISOU 1638 OE1 GLN B 6 7379 7604 6072 -221 -175 552 O ATOM 1639 NE2 GLN B 6 -25.560 3.041 14.736 1.00 52.70 N ANISOU 1639 NE2 GLN B 6 7328 7051 5644 -176 -186 731 N ATOM 1640 N PRO B 7 -23.310 -0.102 18.535 1.00 71.72 N ANISOU 1640 N PRO B 7 10436 9584 7232 308 -125 1161 N ATOM 1641 CA PRO B 7 -22.018 -0.814 18.414 1.00 72.61 C ANISOU 1641 CA PRO B 7 10667 9719 7202 612 -178 1301 C ATOM 1642 C PRO B 7 -21.122 -0.155 17.349 1.00 73.70 C ANISOU 1642 C PRO B 7 10580 9932 7491 699 -293 1229 C ATOM 1643 O PRO B 7 -21.668 0.437 16.424 1.00 71.41 O ANISOU 1643 O PRO B 7 10172 9546 7415 527 -294 1124 O ATOM 1644 CB PRO B 7 -22.428 -2.238 18.021 1.00 75.54 C ANISOU 1644 CB PRO B 7 11431 9771 7498 627 -35 1451 C ATOM 1645 CG PRO B 7 -23.753 -2.088 17.374 1.00 79.00 C ANISOU 1645 CG PRO B 7 11857 10047 8113 300 47 1341 C ATOM 1646 CD PRO B 7 -24.433 -0.956 18.090 1.00 73.56 C ANISOU 1646 CD PRO B 7 10900 9558 7493 123 13 1195 C ATOM 1647 N PRO B 8 -19.775 -0.166 17.473 1.00 71.15 N ANISOU 1647 N PRO B 8 10169 9814 7051 957 -388 1270 N ATOM 1648 CA PRO B 8 -18.944 0.539 16.473 1.00 69.92 C ANISOU 1648 CA PRO B 8 9784 9745 7037 995 -479 1173 C ATOM 1649 C PRO B 8 -18.943 -0.064 15.070 1.00 74.23 C ANISOU 1649 C PRO B 8 10470 10023 7711 1023 -447 1232 C ATOM 1650 O PRO B 8 -18.845 0.682 14.090 1.00 73.33 O ANISOU 1650 O PRO B 8 10189 9889 7784 925 -485 1123 O ATOM 1651 CB PRO B 8 -17.545 0.516 17.085 1.00 73.09 C ANISOU 1651 CB PRO B 8 10054 10487 7231 1261 -576 1201 C ATOM 1652 CG PRO B 8 -17.557 -0.665 17.989 1.00 80.25 C ANISOU 1652 CG PRO B 8 11237 11371 7883 1474 -525 1399 C ATOM 1653 CD PRO B 8 -18.946 -0.778 18.532 1.00 75.22 C ANISOU 1653 CD PRO B 8 10770 10533 7279 1233 -416 1400 C ATOM 1654 N SER B 9 -19.034 -1.404 14.977 1.00 71.56 N ANISOU 1654 N SER B 9 10462 9469 7259 1153 -360 1401 N ATOM 1655 CA SER B 9 -18.997 -2.134 13.720 1.00 71.04 C ANISOU 1655 CA SER B 9 10578 9139 7277 1182 -304 1459 C ATOM 1656 C SER B 9 -19.747 -3.450 13.768 1.00 76.20 C ANISOU 1656 C SER B 9 11642 9476 7834 1147 -135 1588 C ATOM 1657 O SER B 9 -19.901 -4.036 14.838 1.00 77.33 O ANISOU 1657 O SER B 9 11983 9611 7787 1226 -63 1693 O ATOM 1658 CB SER B 9 -17.550 -2.388 13.297 1.00 75.67 C ANISOU 1658 CB SER B 9 11115 9845 7790 1499 -373 1521 C ATOM 1659 OG SER B 9 -16.877 -3.180 14.258 1.00 87.32 O ANISOU 1659 OG SER B 9 12744 11430 9004 1810 -358 1680 O ATOM 1660 N VAL B 10 -20.212 -3.905 12.588 1.00 73.01 N ANISOU 1660 N VAL B 10 11379 8813 7547 1008 -57 1571 N ATOM 1661 CA VAL B 10 -20.887 -5.183 12.312 1.00 75.00 C ANISOU 1661 CA VAL B 10 12043 8727 7725 910 139 1652 C ATOM 1662 C VAL B 10 -20.371 -5.609 10.925 1.00 78.61 C ANISOU 1662 C VAL B 10 12584 9018 8264 978 158 1660 C ATOM 1663 O VAL B 10 -20.290 -4.792 10.019 1.00 76.56 O ANISOU 1663 O VAL B 10 12054 8853 8182 889 48 1545 O ATOM 1664 CB VAL B 10 -22.451 -5.152 12.394 1.00 78.88 C ANISOU 1664 CB VAL B 10 12569 9124 8276 508 240 1545 C ATOM 1665 CG1 VAL B 10 -23.053 -6.522 12.084 1.00 80.51 C ANISOU 1665 CG1 VAL B 10 13220 8990 8382 364 473 1600 C ATOM 1666 CG2 VAL B 10 -22.939 -4.683 13.766 1.00 79.07 C ANISOU 1666 CG2 VAL B 10 12498 9321 8222 443 226 1529 C ATOM 1667 N SER B 11 -19.965 -6.861 10.789 1.00 78.46 N ANISOU 1667 N SER B 11 12957 8751 8104 1159 309 1801 N ATOM 1668 CA SER B 11 -19.406 -7.393 9.548 1.00 78.10 C ANISOU 1668 CA SER B 11 13040 8527 8107 1252 356 1819 C ATOM 1669 C SER B 11 -20.080 -8.714 9.198 1.00 81.02 C ANISOU 1669 C SER B 11 13900 8495 8388 1100 620 1865 C ATOM 1670 O SER B 11 -20.351 -9.501 10.099 1.00 81.35 O ANISOU 1670 O SER B 11 14278 8380 8251 1145 781 1976 O ATOM 1671 CB SER B 11 -17.903 -7.623 9.707 1.00 84.04 C ANISOU 1671 CB SER B 11 13788 9398 8747 1722 295 1952 C ATOM 1672 OG SER B 11 -17.249 -6.651 10.508 1.00 93.51 O ANISOU 1672 OG SER B 11 14618 10989 9923 1882 103 1933 O ATOM 1673 N ALA B 12 -20.343 -8.969 7.897 1.00 76.74 N ANISOU 1673 N ALA B 12 13422 7784 7953 907 682 1774 N ATOM 1674 CA ALA B 12 -20.939 -10.239 7.452 1.00 78.45 C ANISOU 1674 CA ALA B 12 14118 7614 8077 714 961 1782 C ATOM 1675 C ALA B 12 -20.692 -10.527 5.992 1.00 81.67 C ANISOU 1675 C ALA B 12 14581 7878 8572 653 1001 1713 C ATOM 1676 O ALA B 12 -20.564 -9.601 5.193 1.00 80.03 O ANISOU 1676 O ALA B 12 13993 7883 8532 595 810 1607 O ATOM 1677 CB ALA B 12 -22.431 -10.282 7.747 1.00 79.23 C ANISOU 1677 CB ALA B 12 14256 7680 8170 249 1066 1654 C ATOM 1678 N ALA B 13 -20.653 -11.819 5.636 1.00 81.02 N ANISOU 1678 N ALA B 13 15005 7415 8365 653 1274 1771 N ATOM 1679 CA ALA B 13 -20.458 -12.300 4.264 1.00 81.06 C ANISOU 1679 CA ALA B 13 15154 7228 8419 570 1370 1701 C ATOM 1680 C ALA B 13 -21.598 -11.782 3.342 1.00 83.56 C ANISOU 1680 C ALA B 13 15219 7666 8864 62 1315 1470 C ATOM 1681 O ALA B 13 -22.695 -11.529 3.857 1.00 81.99 O ANISOU 1681 O ALA B 13 14923 7574 8657 -254 1320 1378 O ATOM 1682 CB ALA B 13 -20.434 -13.826 4.255 1.00 85.02 C ANISOU 1682 CB ALA B 13 16314 7258 8733 598 1734 1789 C ATOM 1683 N PRO B 14 -21.393 -11.620 2.001 1.00 80.07 N ANISOU 1683 N PRO B 14 14662 7239 8522 -16 1264 1372 N ATOM 1684 CA PRO B 14 -22.515 -11.161 1.146 1.00 78.74 C ANISOU 1684 CA PRO B 14 14252 7231 8433 -472 1210 1163 C ATOM 1685 C PRO B 14 -23.699 -12.139 1.195 1.00 84.96 C ANISOU 1685 C PRO B 14 15379 7820 9082 -919 1487 1047 C ATOM 1686 O PRO B 14 -23.502 -13.365 1.292 1.00 87.03 O ANISOU 1686 O PRO B 14 16166 7701 9202 -913 1777 1101 O ATOM 1687 CB PRO B 14 -21.888 -11.043 -0.246 1.00 79.66 C ANISOU 1687 CB PRO B 14 14289 7344 8634 -412 1150 1116 C ATOM 1688 CG PRO B 14 -20.674 -11.913 -0.209 1.00 86.17 C ANISOU 1688 CG PRO B 14 15479 7878 9382 -33 1294 1271 C ATOM 1689 CD PRO B 14 -20.171 -11.859 1.205 1.00 82.03 C ANISOU 1689 CD PRO B 14 14986 7386 8795 306 1259 1444 C ATOM 1690 N GLY B 15 -24.909 -11.581 1.237 1.00 79.99 N ANISOU 1690 N GLY B 15 14459 7455 8478 -1288 1412 891 N ATOM 1691 CA GLY B 15 -26.144 -12.356 1.349 1.00 81.70 C ANISOU 1691 CA GLY B 15 14901 7586 8554 -1773 1656 738 C ATOM 1692 C GLY B 15 -26.595 -12.636 2.774 1.00 84.82 C ANISOU 1692 C GLY B 15 15469 7911 8849 -1810 1777 801 C ATOM 1693 O GLY B 15 -27.713 -13.121 2.978 1.00 86.64 O ANISOU 1693 O GLY B 15 15819 8134 8966 -2248 1966 654 O ATOM 1694 N GLN B 16 -25.737 -12.340 3.782 1.00 79.46 N ANISOU 1694 N GLN B 16 14794 7207 8190 -1370 1676 1008 N ATOM 1695 CA GLN B 16 -26.057 -12.570 5.208 1.00 79.72 C ANISOU 1695 CA GLN B 16 14996 7182 8111 -1352 1779 1094 C ATOM 1696 C GLN B 16 -26.972 -11.460 5.778 1.00 79.73 C ANISOU 1696 C GLN B 16 14511 7588 8196 -1531 1580 991 C ATOM 1697 O GLN B 16 -27.178 -10.439 5.137 1.00 75.20 O ANISOU 1697 O GLN B 16 13472 7330 7770 -1566 1344 895 O ATOM 1698 CB GLN B 16 -24.773 -12.679 6.063 1.00 80.96 C ANISOU 1698 CB GLN B 16 15323 7215 8224 -797 1739 1351 C ATOM 1699 CG GLN B 16 -24.003 -13.998 5.952 1.00 96.92 C ANISOU 1699 CG GLN B 16 17950 8783 10091 -573 2020 1498 C ATOM 1700 CD GLN B 16 -23.230 -14.311 7.228 1.00120.17 C ANISOU 1700 CD GLN B 16 21138 11626 12894 -118 2062 1748 C ATOM 1701 OE1 GLN B 16 -22.003 -14.178 7.297 1.00114.66 O ANISOU 1701 OE1 GLN B 16 20390 10977 12199 379 1937 1912 O ATOM 1702 NE2 GLN B 16 -23.930 -14.739 8.274 1.00113.01 N ANISOU 1702 NE2 GLN B 16 20491 10607 11841 -277 2241 1778 N ATOM 1703 N LYS B 17 -27.518 -11.675 6.979 1.00 78.59 N ANISOU 1703 N LYS B 17 14500 7419 7943 -1629 1695 1017 N ATOM 1704 CA LYS B 17 -28.375 -10.715 7.675 1.00 77.19 C ANISOU 1704 CA LYS B 17 13914 7593 7820 -1775 1547 930 C ATOM 1705 C LYS B 17 -27.557 -10.025 8.791 1.00 80.67 C ANISOU 1705 C LYS B 17 14223 8135 8294 -1349 1371 1108 C ATOM 1706 O LYS B 17 -27.002 -10.712 9.653 1.00 83.24 O ANISOU 1706 O LYS B 17 14916 8233 8477 -1136 1505 1273 O ATOM 1707 CB LYS B 17 -29.612 -11.432 8.259 1.00 81.17 C ANISOU 1707 CB LYS B 17 14647 8029 8165 -2230 1817 806 C ATOM 1708 CG LYS B 17 -30.624 -10.520 8.955 0.50 86.57 C ANISOU 1708 CG LYS B 17 14911 9091 8891 -2415 1697 693 C ATOM 1709 CD LYS B 17 -31.765 -11.321 9.563 0.50 93.68 C ANISOU 1709 CD LYS B 17 16063 9917 9613 -2871 1991 568 C ATOM 1710 CE LYS B 17 -32.930 -10.445 9.941 0.50101.05 C ANISOU 1710 CE LYS B 17 16522 11283 10591 -3118 1883 400 C ATOM 1711 NZ LYS B 17 -34.040 -11.230 10.539 0.50110.46 N ANISOU 1711 NZ LYS B 17 17941 12433 11597 -3592 2183 257 N ATOM 1712 N VAL B 18 -27.482 -8.684 8.762 1.00 73.22 N ANISOU 1712 N VAL B 18 12774 7534 7515 -1226 1090 1071 N ATOM 1713 CA VAL B 18 -26.791 -7.882 9.779 1.00 71.59 C ANISOU 1713 CA VAL B 18 12377 7485 7339 -893 917 1186 C ATOM 1714 C VAL B 18 -27.831 -7.139 10.616 1.00 74.80 C ANISOU 1714 C VAL B 18 12511 8144 7764 -1098 874 1084 C ATOM 1715 O VAL B 18 -28.872 -6.721 10.095 1.00 74.43 O ANISOU 1715 O VAL B 18 12216 8276 7788 -1390 853 919 O ATOM 1716 CB VAL B 18 -25.668 -6.918 9.250 1.00 73.69 C ANISOU 1716 CB VAL B 18 12332 7909 7758 -559 667 1229 C ATOM 1717 CG1 VAL B 18 -24.584 -7.664 8.484 1.00 74.49 C ANISOU 1717 CG1 VAL B 18 12690 7782 7830 -327 715 1332 C ATOM 1718 CG2 VAL B 18 -26.225 -5.780 8.406 1.00 70.80 C ANISOU 1718 CG2 VAL B 18 11533 7796 7572 -708 501 1079 C ATOM 1719 N THR B 19 -27.536 -6.967 11.904 1.00 70.65 N ANISOU 1719 N THR B 19 12021 7663 7162 -926 858 1181 N ATOM 1720 CA THR B 19 -28.393 -6.249 12.837 1.00 69.72 C ANISOU 1720 CA THR B 19 11666 7775 7051 -1076 825 1099 C ATOM 1721 C THR B 19 -27.605 -5.110 13.485 1.00 70.34 C ANISOU 1721 C THR B 19 11449 8073 7204 -773 610 1149 C ATOM 1722 O THR B 19 -26.486 -5.323 13.972 1.00 69.98 O ANISOU 1722 O THR B 19 11539 7974 7076 -461 572 1295 O ATOM 1723 CB THR B 19 -29.004 -7.242 13.852 1.00 82.68 C ANISOU 1723 CB THR B 19 13681 9247 8486 -1260 1072 1134 C ATOM 1724 OG1 THR B 19 -30.075 -7.932 13.209 1.00 86.32 O ANISOU 1724 OG1 THR B 19 14274 9615 8908 -1672 1263 993 O ATOM 1725 CG2 THR B 19 -29.530 -6.562 15.118 1.00 82.32 C ANISOU 1725 CG2 THR B 19 13447 9419 8411 -1306 1036 1101 C ATOM 1726 N ILE B 20 -28.198 -3.907 13.503 1.00 64.56 N ANISOU 1726 N ILE B 20 10319 7603 6609 -864 486 1022 N ATOM 1727 CA ILE B 20 -27.604 -2.737 14.160 1.00 62.25 C ANISOU 1727 CA ILE B 20 9753 7517 6383 -651 323 1027 C ATOM 1728 C ILE B 20 -28.615 -2.299 15.195 1.00 66.62 C ANISOU 1728 C ILE B 20 10187 8223 6902 -829 374 944 C ATOM 1729 O ILE B 20 -29.701 -1.879 14.823 1.00 64.97 O ANISOU 1729 O ILE B 20 9779 8130 6775 -1044 390 814 O ATOM 1730 CB ILE B 20 -27.230 -1.586 13.161 1.00 61.96 C ANISOU 1730 CB ILE B 20 9386 7609 6546 -553 153 956 C ATOM 1731 CG1 ILE B 20 -26.260 -2.064 12.062 1.00 61.15 C ANISOU 1731 CG1 ILE B 20 9403 7359 6474 -399 115 1028 C ATOM 1732 CG2 ILE B 20 -26.672 -0.355 13.901 1.00 60.28 C ANISOU 1732 CG2 ILE B 20 8925 7592 6387 -394 32 929 C ATOM 1733 CD1 ILE B 20 -26.326 -1.244 10.728 1.00 59.61 C ANISOU 1733 CD1 ILE B 20 8957 7233 6459 -416 10 943 C ATOM 1734 N SER B 21 -28.284 -2.431 16.490 1.00 65.86 N ANISOU 1734 N SER B 21 10209 8148 6665 -732 405 1018 N ATOM 1735 CA SER B 21 -29.184 -2.001 17.563 1.00 67.15 C ANISOU 1735 CA SER B 21 10267 8460 6785 -894 461 938 C ATOM 1736 C SER B 21 -28.749 -0.642 18.108 1.00 67.39 C ANISOU 1736 C SER B 21 9988 8717 6901 -747 316 883 C ATOM 1737 O SER B 21 -27.569 -0.317 18.032 1.00 65.84 O ANISOU 1737 O SER B 21 9746 8554 6716 -511 199 938 O ATOM 1738 CB SER B 21 -29.230 -3.041 18.686 1.00 75.63 C ANISOU 1738 CB SER B 21 11702 9411 7625 -920 619 1047 C ATOM 1739 OG SER B 21 -28.029 -3.076 19.445 1.00 91.27 O ANISOU 1739 OG SER B 21 13777 11420 9481 -611 544 1186 O ATOM 1740 N CYS B 22 -29.695 0.156 18.627 1.00 63.70 N ANISOU 1740 N CYS B 22 9306 8413 6484 -898 341 757 N ATOM 1741 CA CYS B 22 -29.424 1.464 19.233 1.00 62.70 C ANISOU 1741 CA CYS B 22 8921 8474 6427 -802 254 679 C ATOM 1742 C CYS B 22 -30.262 1.638 20.478 1.00 67.27 C ANISOU 1742 C CYS B 22 9478 9167 6913 -947 352 616 C ATOM 1743 O CYS B 22 -31.483 1.461 20.438 1.00 66.88 O ANISOU 1743 O CYS B 22 9392 9144 6874 -1160 456 540 O ATOM 1744 CB CYS B 22 -29.631 2.616 18.250 1.00 61.66 C ANISOU 1744 CB CYS B 22 8502 8414 6512 -778 176 574 C ATOM 1745 SG CYS B 22 -28.939 4.203 18.813 1.00 64.62 S ANISOU 1745 SG CYS B 22 8646 8939 6968 -642 102 482 S ATOM 1746 N SER B 23 -29.602 1.949 21.590 1.00 64.68 N ANISOU 1746 N SER B 23 9165 8937 6474 -842 324 637 N ATOM 1747 CA SER B 23 -30.262 2.146 22.875 1.00 65.38 C ANISOU 1747 CA SER B 23 9245 9143 6454 -965 416 579 C ATOM 1748 C SER B 23 -30.253 3.596 23.334 1.00 66.57 C ANISOU 1748 C SER B 23 9119 9473 6701 -944 376 436 C ATOM 1749 O SER B 23 -29.257 4.295 23.176 1.00 65.25 O ANISOU 1749 O SER B 23 8848 9361 6582 -797 273 416 O ATOM 1750 CB SER B 23 -29.631 1.252 23.935 1.00 71.86 C ANISOU 1750 CB SER B 23 10341 9944 7017 -881 448 717 C ATOM 1751 OG SER B 23 -29.943 -0.100 23.631 1.00 89.36 O ANISOU 1751 OG SER B 23 12872 11948 9134 -949 559 834 O ATOM 1752 N GLY B 24 -31.366 4.023 23.914 1.00 63.48 N ANISOU 1752 N GLY B 24 8623 9171 6324 -1104 480 325 N ATOM 1753 CA GLY B 24 -31.513 5.364 24.462 1.00 63.23 C ANISOU 1753 CA GLY B 24 8374 9282 6368 -1099 493 180 C ATOM 1754 C GLY B 24 -32.222 5.315 25.791 1.00 69.08 C ANISOU 1754 C GLY B 24 9147 10131 6968 -1242 612 125 C ATOM 1755 O GLY B 24 -31.854 4.523 26.662 1.00 70.31 O ANISOU 1755 O GLY B 24 9505 10295 6915 -1255 630 215 O ATOM 1756 N ASN B 25 -33.263 6.137 25.939 1.00 66.02 N ANISOU 1756 N ASN B 25 8569 9832 6681 -1331 704 -16 N ATOM 1757 CA ASN B 25 -34.105 6.178 27.136 1.00 67.67 C ANISOU 1757 CA ASN B 25 8776 10158 6777 -1485 838 -95 C ATOM 1758 C ASN B 25 -35.547 6.541 26.789 1.00 73.86 C ANISOU 1758 C ASN B 25 9363 11024 7676 -1589 945 -209 C ATOM 1759 O ASN B 25 -35.904 6.590 25.600 1.00 72.43 O ANISOU 1759 O ASN B 25 9067 10818 7634 -1545 906 -206 O ATOM 1760 CB ASN B 25 -33.520 7.061 28.254 1.00 67.20 C ANISOU 1760 CB ASN B 25 8680 10210 6645 -1449 848 -179 C ATOM 1761 CG ASN B 25 -33.287 8.508 27.924 1.00 78.66 C ANISOU 1761 CG ASN B 25 9938 11679 8270 -1351 842 -311 C ATOM 1762 OD1 ASN B 25 -34.131 9.206 27.355 1.00 76.94 O ANISOU 1762 OD1 ASN B 25 9561 11452 8219 -1329 908 -392 O ATOM 1763 ND2 ASN B 25 -32.157 9.014 28.359 1.00 69.78 N ANISOU 1763 ND2 ASN B 25 8831 10600 7084 -1293 786 -344 N ATOM 1764 N ASN B 26 -36.381 6.740 27.837 1.00 72.50 N ANISOU 1764 N ASN B 26 9144 10980 7422 -1724 1080 -308 N ATOM 1765 CA ASN B 26 -37.813 7.052 27.757 1.00 73.95 C ANISOU 1765 CA ASN B 26 9117 11311 7668 -1826 1203 -432 C ATOM 1766 C ASN B 26 -38.084 8.403 27.095 1.00 77.06 C ANISOU 1766 C ASN B 26 9255 11759 8267 -1634 1194 -524 C ATOM 1767 O ASN B 26 -39.154 8.572 26.519 1.00 78.39 O ANISOU 1767 O ASN B 26 9218 12058 8508 -1636 1244 -585 O ATOM 1768 CB ASN B 26 -38.456 7.024 29.169 1.00 79.18 C ANISOU 1768 CB ASN B 26 9807 12098 8179 -1997 1357 -519 C ATOM 1769 CG ASN B 26 -38.209 5.758 29.965 1.00106.95 C ANISOU 1769 CG ASN B 26 13623 15550 11464 -2167 1399 -417 C ATOM 1770 OD1 ASN B 26 -37.134 5.555 30.548 1.00 98.90 O ANISOU 1770 OD1 ASN B 26 12801 14455 10324 -2090 1332 -320 O ATOM 1771 ND2 ASN B 26 -39.210 4.894 30.032 1.00102.18 N ANISOU 1771 ND2 ASN B 26 13062 14993 10770 -2401 1528 -441 N ATOM 1772 N SER B 27 -37.133 9.365 27.208 1.00 71.08 N ANISOU 1772 N SER B 27 8514 10915 7579 -1472 1148 -539 N ATOM 1773 CA SER B 27 -37.235 10.719 26.663 1.00 70.58 C ANISOU 1773 CA SER B 27 8290 10834 7693 -1276 1179 -617 C ATOM 1774 C SER B 27 -36.978 10.804 25.156 1.00 71.65 C ANISOU 1774 C SER B 27 8373 10877 7973 -1113 1068 -536 C ATOM 1775 O SER B 27 -37.493 11.719 24.508 1.00 71.11 O ANISOU 1775 O SER B 27 8155 10828 8036 -941 1114 -578 O ATOM 1776 CB SER B 27 -36.286 11.665 27.390 1.00 74.57 C ANISOU 1776 CB SER B 27 8874 11268 8192 -1228 1211 -690 C ATOM 1777 OG SER B 27 -36.596 11.738 28.772 1.00 86.88 O ANISOU 1777 OG SER B 27 10463 12934 9615 -1369 1326 -784 O ATOM 1778 N ASN B 28 -36.156 9.895 24.612 1.00 65.15 N ANISOU 1778 N ASN B 28 7687 9951 7117 -1142 933 -416 N ATOM 1779 CA ASN B 28 -35.842 9.916 23.191 1.00 63.08 C ANISOU 1779 CA ASN B 28 7391 9599 6978 -1005 827 -340 C ATOM 1780 C ASN B 28 -36.453 8.709 22.480 1.00 66.79 C ANISOU 1780 C ASN B 28 7854 10119 7402 -1120 782 -273 C ATOM 1781 O ASN B 28 -37.624 8.813 22.110 1.00 67.75 O ANISOU 1781 O ASN B 28 7787 10405 7550 -1136 837 -329 O ATOM 1782 CB ASN B 28 -34.338 10.109 22.922 1.00 61.72 C ANISOU 1782 CB ASN B 28 7353 9264 6832 -914 724 -284 C ATOM 1783 CG ASN B 28 -33.411 9.332 23.828 1.00 77.92 C ANISOU 1783 CG ASN B 28 9584 11303 8719 -1012 674 -234 C ATOM 1784 OD1 ASN B 28 -33.397 8.102 23.831 1.00 66.43 O ANISOU 1784 OD1 ASN B 28 8253 9832 7156 -1096 632 -134 O ATOM 1785 ND2 ASN B 28 -32.596 10.037 24.593 1.00 69.40 N ANISOU 1785 ND2 ASN B 28 8532 10237 7599 -996 690 -303 N ATOM 1786 N ILE B 29 -35.725 7.558 22.339 1.00 62.76 N ANISOU 1786 N ILE B 29 7548 9494 6805 -1208 704 -166 N ATOM 1787 CA ILE B 29 -36.245 6.360 21.629 1.00 62.58 C ANISOU 1787 CA ILE B 29 7573 9478 6728 -1353 696 -117 C ATOM 1788 C ILE B 29 -37.617 5.911 22.187 1.00 68.43 C ANISOU 1788 C ILE B 29 8226 10405 7368 -1581 833 -211 C ATOM 1789 O ILE B 29 -38.555 5.725 21.413 1.00 67.73 O ANISOU 1789 O ILE B 29 7967 10467 7301 -1656 852 -266 O ATOM 1790 CB ILE B 29 -35.233 5.170 21.520 1.00 64.30 C ANISOU 1790 CB ILE B 29 8082 9502 6848 -1393 635 17 C ATOM 1791 CG1 ILE B 29 -33.966 5.588 20.716 1.00 61.92 C ANISOU 1791 CG1 ILE B 29 7808 9065 6652 -1175 496 93 C ATOM 1792 CG2 ILE B 29 -35.910 3.948 20.828 1.00 66.62 C ANISOU 1792 CG2 ILE B 29 8454 9782 7074 -1592 681 35 C ATOM 1793 CD1 ILE B 29 -32.808 4.639 20.763 1.00 59.97 C ANISOU 1793 CD1 ILE B 29 7820 8662 6304 -1136 434 223 C ATOM 1794 N GLY B 30 -37.723 5.807 23.513 1.00 66.74 N ANISOU 1794 N GLY B 30 8105 10216 7038 -1690 929 -244 N ATOM 1795 CA GLY B 30 -38.939 5.375 24.196 1.00 68.45 C ANISOU 1795 CA GLY B 30 8262 10604 7141 -1931 1081 -342 C ATOM 1796 C GLY B 30 -40.183 6.210 23.963 1.00 73.45 C ANISOU 1796 C GLY B 30 8546 11509 7854 -1905 1143 -483 C ATOM 1797 O GLY B 30 -41.293 5.711 24.174 1.00 75.55 O ANISOU 1797 O GLY B 30 8709 11970 8026 -2130 1258 -579 O ATOM 1798 N LYS B 31 -40.015 7.478 23.515 1.00 68.72 N ANISOU 1798 N LYS B 31 7769 10931 7412 -1626 1084 -498 N ATOM 1799 CA LYS B 31 -41.108 8.421 23.272 1.00 69.26 C ANISOU 1799 CA LYS B 31 7516 11248 7553 -1498 1146 -606 C ATOM 1800 C LYS B 31 -41.309 8.810 21.794 1.00 74.33 C ANISOU 1800 C LYS B 31 7969 11967 8306 -1292 1048 -572 C ATOM 1801 O LYS B 31 -42.422 8.691 21.269 1.00 76.27 O ANISOU 1801 O LYS B 31 7956 12505 8518 -1324 1073 -642 O ATOM 1802 CB LYS B 31 -40.872 9.688 24.098 1.00 70.94 C ANISOU 1802 CB LYS B 31 7714 11410 7832 -1313 1217 -655 C ATOM 1803 CG LYS B 31 -42.111 10.256 24.745 1.00 80.87 C ANISOU 1803 CG LYS B 31 8742 12922 9062 -1311 1371 -792 C ATOM 1804 CD LYS B 31 -41.866 11.659 25.294 1.00 89.77 C ANISOU 1804 CD LYS B 31 9867 13962 10279 -1079 1458 -842 C ATOM 1805 CE LYS B 31 -41.512 11.679 26.760 1.00102.04 C ANISOU 1805 CE LYS B 31 11585 15448 11739 -1240 1554 -905 C ATOM 1806 NZ LYS B 31 -42.032 12.902 27.431 1.00113.98 N ANISOU 1806 NZ LYS B 31 12993 17019 13295 -1092 1721 -1026 N ATOM 1807 N ASN B 32 -40.238 9.288 21.131 1.00 68.94 N ANISOU 1807 N ASN B 32 7403 11054 7737 -1083 940 -472 N ATOM 1808 CA ASN B 32 -40.302 9.844 19.778 1.00 67.96 C ANISOU 1808 CA ASN B 32 7137 10968 7718 -842 856 -425 C ATOM 1809 C ASN B 32 -39.931 8.874 18.615 1.00 70.14 C ANISOU 1809 C ASN B 32 7478 11193 7979 -931 727 -343 C ATOM 1810 O ASN B 32 -39.325 7.816 18.829 1.00 68.88 O ANISOU 1810 O ASN B 32 7540 10882 7750 -1142 700 -300 O ATOM 1811 CB ASN B 32 -39.453 11.114 19.725 1.00 64.11 C ANISOU 1811 CB ASN B 32 6737 10261 7361 -562 860 -387 C ATOM 1812 CG ASN B 32 -39.818 12.121 20.784 1.00 75.55 C ANISOU 1812 CG ASN B 32 8145 11737 8825 -475 1013 -480 C ATOM 1813 OD1 ASN B 32 -40.808 12.837 20.674 1.00 74.28 O ANISOU 1813 OD1 ASN B 32 7777 11763 8683 -298 1101 -531 O ATOM 1814 ND2 ASN B 32 -39.054 12.166 21.862 1.00 65.86 N ANISOU 1814 ND2 ASN B 32 7107 10350 7566 -592 1054 -510 N ATOM 1815 N TYR B 33 -40.368 9.236 17.387 1.00 66.75 N ANISOU 1815 N TYR B 33 6855 10910 7597 -754 664 -323 N ATOM 1816 CA TYR B 33 -40.124 8.484 16.150 1.00 66.29 C ANISOU 1816 CA TYR B 33 6822 10842 7525 -814 548 -263 C ATOM 1817 C TYR B 33 -38.613 8.443 15.860 1.00 65.36 C ANISOU 1817 C TYR B 33 6986 10356 7491 -740 461 -147 C ATOM 1818 O TYR B 33 -37.928 9.479 15.893 1.00 62.83 O ANISOU 1818 O TYR B 33 6724 9871 7278 -509 458 -108 O ATOM 1819 CB TYR B 33 -40.841 9.125 14.936 1.00 69.72 C ANISOU 1819 CB TYR B 33 6978 11531 7981 -574 494 -256 C ATOM 1820 CG TYR B 33 -42.347 9.245 15.054 1.00 76.34 C ANISOU 1820 CG TYR B 33 7467 12820 8719 -589 562 -373 C ATOM 1821 CD1 TYR B 33 -43.170 8.125 14.926 1.00 80.03 C ANISOU 1821 CD1 TYR B 33 7799 13571 9037 -926 577 -479 C ATOM 1822 CD2 TYR B 33 -42.956 10.486 15.225 1.00 78.90 C ANISOU 1822 CD2 TYR B 33 7593 13302 9082 -259 626 -384 C ATOM 1823 CE1 TYR B 33 -44.559 8.235 14.998 0.50 83.57 C ANISOU 1823 CE1 TYR B 33 7880 14500 9372 -956 639 -610 C ATOM 1824 CE2 TYR B 33 -44.345 10.607 15.303 0.50 82.57 C ANISOU 1824 CE2 TYR B 33 7700 14233 9439 -233 685 -491 C ATOM 1825 CZ TYR B 33 -45.142 9.479 15.187 1.00 91.11 C ANISOU 1825 CZ TYR B 33 8607 15644 10368 -591 682 -611 C ATOM 1826 OH TYR B 33 -46.509 9.593 15.266 0.50 95.68 O ANISOU 1826 OH TYR B 33 8790 16741 10821 -586 742 -740 O ATOM 1827 N VAL B 34 -38.116 7.244 15.574 1.00 59.13 N ANISOU 1827 N VAL B 34 6377 9448 6642 -945 412 -105 N ATOM 1828 CA VAL B 34 -36.715 7.023 15.264 1.00 56.08 C ANISOU 1828 CA VAL B 34 6237 8761 6309 -883 330 0 C ATOM 1829 C VAL B 34 -36.533 7.006 13.725 1.00 59.24 C ANISOU 1829 C VAL B 34 6587 9159 6763 -777 227 55 C ATOM 1830 O VAL B 34 -37.410 6.560 12.994 1.00 61.59 O ANISOU 1830 O VAL B 34 6734 9670 6998 -874 217 13 O ATOM 1831 CB VAL B 34 -36.203 5.728 15.968 1.00 57.82 C ANISOU 1831 CB VAL B 34 6727 8827 6415 -1116 360 33 C ATOM 1832 CG1 VAL B 34 -34.890 5.237 15.373 1.00 56.22 C ANISOU 1832 CG1 VAL B 34 6748 8375 6240 -1049 269 144 C ATOM 1833 CG2 VAL B 34 -36.067 5.928 17.478 1.00 56.57 C ANISOU 1833 CG2 VAL B 34 6650 8639 6205 -1154 439 7 C ATOM 1834 N SER B 35 -35.392 7.500 13.259 1.00 52.43 N ANISOU 1834 N SER B 35 5843 8080 5998 -596 158 135 N ATOM 1835 CA SER B 35 -34.966 7.518 11.864 1.00 50.26 C ANISOU 1835 CA SER B 35 5573 7748 5777 -486 65 200 C ATOM 1836 C SER B 35 -33.579 6.873 11.780 1.00 51.64 C ANISOU 1836 C SER B 35 6002 7655 5963 -520 11 274 C ATOM 1837 O SER B 35 -32.873 6.778 12.779 1.00 48.95 O ANISOU 1837 O SER B 35 5799 7195 5605 -546 36 283 O ATOM 1838 CB SER B 35 -34.964 8.944 11.300 1.00 51.39 C ANISOU 1838 CB SER B 35 5600 7899 6025 -192 62 222 C ATOM 1839 OG SER B 35 -34.513 9.918 12.228 1.00 62.80 O ANISOU 1839 OG SER B 35 7106 9220 7536 -85 137 200 O ATOM 1840 N TRP B 36 -33.235 6.351 10.621 1.00 50.98 N ANISOU 1840 N TRP B 36 5972 7514 5885 -524 -59 324 N ATOM 1841 CA TRP B 36 -31.931 5.752 10.393 1.00 50.58 C ANISOU 1841 CA TRP B 36 6143 7232 5842 -518 -107 397 C ATOM 1842 C TRP B 36 -31.321 6.421 9.190 1.00 54.58 C ANISOU 1842 C TRP B 36 6623 7669 6448 -338 -177 441 C ATOM 1843 O TRP B 36 -32.036 6.788 8.248 1.00 55.00 O ANISOU 1843 O TRP B 36 6529 7855 6516 -278 -201 435 O ATOM 1844 CB TRP B 36 -32.028 4.237 10.204 1.00 50.69 C ANISOU 1844 CB TRP B 36 6321 7196 5745 -730 -85 412 C ATOM 1845 CG TRP B 36 -32.258 3.472 11.486 1.00 53.02 C ANISOU 1845 CG TRP B 36 6749 7468 5927 -894 7 397 C ATOM 1846 CD1 TRP B 36 -33.454 3.070 12.000 1.00 57.21 C ANISOU 1846 CD1 TRP B 36 7214 8155 6366 -1103 100 316 C ATOM 1847 CD2 TRP B 36 -31.249 2.966 12.373 1.00 52.50 C ANISOU 1847 CD2 TRP B 36 6913 7228 5805 -859 23 469 C ATOM 1848 NE1 TRP B 36 -33.257 2.366 13.163 1.00 56.72 N ANISOU 1848 NE1 TRP B 36 7359 7990 6201 -1209 184 340 N ATOM 1849 CE2 TRP B 36 -31.912 2.268 13.405 1.00 57.65 C ANISOU 1849 CE2 TRP B 36 7663 7910 6330 -1044 133 443 C ATOM 1850 CE3 TRP B 36 -29.838 3.005 12.372 1.00 52.45 C ANISOU 1850 CE3 TRP B 36 7032 7073 5822 -683 -43 551 C ATOM 1851 CZ2 TRP B 36 -31.217 1.622 14.444 1.00 57.87 C ANISOU 1851 CZ2 TRP B 36 7933 7809 6247 -1028 178 519 C ATOM 1852 CZ3 TRP B 36 -29.155 2.377 13.399 1.00 54.42 C ANISOU 1852 CZ3 TRP B 36 7477 7242 5959 -659 -12 616 C ATOM 1853 CH2 TRP B 36 -29.841 1.710 14.431 1.00 57.01 C ANISOU 1853 CH2 TRP B 36 7921 7587 6155 -815 95 610 C ATOM 1854 N TYR B 37 -29.993 6.605 9.238 1.00 49.54 N ANISOU 1854 N TYR B 37 6115 6851 5858 -246 -207 484 N ATOM 1855 CA TYR B 37 -29.219 7.309 8.207 1.00 47.87 C ANISOU 1855 CA TYR B 37 5907 6542 5738 -91 -250 517 C ATOM 1856 C TYR B 37 -28.103 6.441 7.704 1.00 51.63 C ANISOU 1856 C TYR B 37 6543 6877 6196 -108 -304 571 C ATOM 1857 O TYR B 37 -27.499 5.696 8.476 1.00 49.94 O ANISOU 1857 O TYR B 37 6452 6607 5918 -159 -299 589 O ATOM 1858 CB TYR B 37 -28.619 8.610 8.787 1.00 48.24 C ANISOU 1858 CB TYR B 37 5937 6530 5860 29 -200 479 C ATOM 1859 CG TYR B 37 -29.680 9.490 9.393 1.00 49.98 C ANISOU 1859 CG TYR B 37 6032 6863 6096 72 -119 425 C ATOM 1860 CD1 TYR B 37 -30.212 9.209 10.652 1.00 51.89 C ANISOU 1860 CD1 TYR B 37 6246 7196 6274 -38 -73 375 C ATOM 1861 CD2 TYR B 37 -30.237 10.542 8.667 1.00 51.15 C ANISOU 1861 CD2 TYR B 37 6094 7035 6304 241 -78 434 C ATOM 1862 CE1 TYR B 37 -31.292 9.921 11.152 1.00 54.02 C ANISOU 1862 CE1 TYR B 37 6384 7592 6549 3 7 323 C ATOM 1863 CE2 TYR B 37 -31.276 11.306 9.192 1.00 53.11 C ANISOU 1863 CE2 TYR B 37 6226 7400 6553 322 8 395 C ATOM 1864 CZ TYR B 37 -31.805 10.983 10.429 1.00 59.85 C ANISOU 1864 CZ TYR B 37 7032 8357 7353 196 48 332 C ATOM 1865 OH TYR B 37 -32.846 11.693 10.944 1.00 64.54 O ANISOU 1865 OH TYR B 37 7499 9081 7943 279 140 286 O ATOM 1866 N GLN B 38 -27.856 6.502 6.397 1.00 49.21 N ANISOU 1866 N GLN B 38 6240 6526 5933 -47 -348 605 N ATOM 1867 CA GLN B 38 -26.757 5.774 5.790 1.00 49.23 C ANISOU 1867 CA GLN B 38 6385 6393 5927 -38 -388 651 C ATOM 1868 C GLN B 38 -25.730 6.798 5.267 1.00 54.15 C ANISOU 1868 C GLN B 38 6997 6936 6642 102 -399 650 C ATOM 1869 O GLN B 38 -26.092 7.789 4.653 1.00 53.31 O ANISOU 1869 O GLN B 38 6813 6845 6596 185 -381 644 O ATOM 1870 CB GLN B 38 -27.258 4.858 4.662 1.00 50.34 C ANISOU 1870 CB GLN B 38 6565 6542 6020 -128 -412 673 C ATOM 1871 CG GLN B 38 -26.162 4.013 4.027 1.00 49.46 C ANISOU 1871 CG GLN B 38 6626 6273 5894 -113 -432 720 C ATOM 1872 CD GLN B 38 -26.590 3.463 2.682 1.00 60.45 C ANISOU 1872 CD GLN B 38 8038 7674 7257 -190 -448 722 C ATOM 1873 OE1 GLN B 38 -26.756 4.200 1.725 1.00 54.64 O ANISOU 1873 OE1 GLN B 38 7197 6997 6566 -117 -487 723 O ATOM 1874 NE2 GLN B 38 -26.762 2.159 2.575 1.00 62.83 N ANISOU 1874 NE2 GLN B 38 8495 7912 7466 -341 -403 720 N ATOM 1875 N GLN B 39 -24.464 6.556 5.535 1.00 53.82 N ANISOU 1875 N GLN B 39 7037 6822 6592 133 -412 655 N ATOM 1876 CA GLN B 39 -23.409 7.417 5.037 1.00 54.85 C ANISOU 1876 CA GLN B 39 7157 6894 6790 216 -404 628 C ATOM 1877 C GLN B 39 -22.361 6.580 4.321 1.00 59.49 C ANISOU 1877 C GLN B 39 7836 7414 7353 246 -449 668 C ATOM 1878 O GLN B 39 -21.540 5.920 4.961 1.00 57.65 O ANISOU 1878 O GLN B 39 7649 7202 7052 269 -467 678 O ATOM 1879 CB GLN B 39 -22.779 8.263 6.162 1.00 56.25 C ANISOU 1879 CB GLN B 39 7286 7117 6969 216 -356 546 C ATOM 1880 CG GLN B 39 -21.825 9.325 5.618 1.00 52.08 C ANISOU 1880 CG GLN B 39 6750 6532 6506 248 -304 482 C ATOM 1881 CD GLN B 39 -21.245 10.186 6.709 1.00 58.28 C ANISOU 1881 CD GLN B 39 7487 7383 7276 194 -232 365 C ATOM 1882 OE1 GLN B 39 -21.330 9.875 7.890 1.00 51.27 O ANISOU 1882 OE1 GLN B 39 6563 6605 6314 154 -246 340 O ATOM 1883 NE2 GLN B 39 -20.683 11.315 6.338 1.00 60.79 N ANISOU 1883 NE2 GLN B 39 7816 7633 7648 173 -133 280 N ATOM 1884 N LEU B 40 -22.398 6.630 2.994 1.00 60.24 N ANISOU 1884 N LEU B 40 7953 7445 7490 269 -463 696 N ATOM 1885 CA LEU B 40 -21.439 5.964 2.111 1.00 61.57 C ANISOU 1885 CA LEU B 40 8206 7539 7648 303 -490 726 C ATOM 1886 C LEU B 40 -20.066 6.673 2.239 1.00 68.84 C ANISOU 1886 C LEU B 40 9089 8469 8598 358 -468 667 C ATOM 1887 O LEU B 40 -20.041 7.890 2.465 1.00 68.90 O ANISOU 1887 O LEU B 40 9031 8489 8658 348 -413 602 O ATOM 1888 CB LEU B 40 -21.958 5.975 0.662 1.00 61.25 C ANISOU 1888 CB LEU B 40 8185 7454 7633 296 -503 758 C ATOM 1889 CG LEU B 40 -23.223 5.119 0.425 1.00 66.71 C ANISOU 1889 CG LEU B 40 8892 8193 8260 197 -522 785 C ATOM 1890 CD1 LEU B 40 -23.946 5.525 -0.857 1.00 66.41 C ANISOU 1890 CD1 LEU B 40 8798 8206 8227 203 -542 799 C ATOM 1891 CD2 LEU B 40 -22.904 3.613 0.443 1.00 68.39 C ANISOU 1891 CD2 LEU B 40 9263 8328 8395 132 -515 810 C ATOM 1892 N PRO B 41 -18.923 5.930 2.201 0.90 67.60 N ANISOU 1892 N PRO B 41 8970 8324 8391 414 -493 676 N ATOM 1893 CA PRO B 41 -17.608 6.587 2.411 0.90 67.95 C ANISOU 1893 CA PRO B 41 8929 8455 8435 441 -472 590 C ATOM 1894 C PRO B 41 -17.323 7.779 1.480 1.00 71.04 C ANISOU 1894 C PRO B 41 9297 8782 8914 398 -406 525 C ATOM 1895 O PRO B 41 -17.399 7.637 0.262 1.00 72.85 O ANISOU 1895 O PRO B 41 9593 8908 9179 415 -407 569 O ATOM 1896 CB PRO B 41 -16.599 5.441 2.253 1.00 69.88 C ANISOU 1896 CB PRO B 41 9218 8736 8599 550 -512 634 C ATOM 1897 CG PRO B 41 -17.385 4.200 2.525 1.00 74.07 C ANISOU 1897 CG PRO B 41 9886 9188 9067 574 -534 741 C ATOM 1898 CD PRO B 41 -18.773 4.470 2.014 1.00 68.83 C ANISOU 1898 CD PRO B 41 9253 8429 8471 459 -521 756 C ATOM 1899 N GLY B 42 -17.072 8.944 2.083 1.00 64.67 N ANISOU 1899 N GLY B 42 8421 8024 8128 331 -330 417 N ATOM 1900 CA GLY B 42 -16.798 10.202 1.388 1.00 63.63 C ANISOU 1900 CA GLY B 42 8315 7799 8064 272 -215 343 C ATOM 1901 C GLY B 42 -18.019 11.047 1.069 1.00 65.94 C ANISOU 1901 C GLY B 42 8683 7951 8423 290 -149 389 C ATOM 1902 O GLY B 42 -17.891 12.134 0.488 1.00 65.81 O ANISOU 1902 O GLY B 42 8740 7815 8450 271 -24 350 O ATOM 1903 N ARG B 43 -19.223 10.542 1.428 1.00 61.57 N ANISOU 1903 N ARG B 43 8117 7417 7859 337 -217 474 N ATOM 1904 CA ARG B 43 -20.507 11.212 1.167 1.00 59.60 C ANISOU 1904 CA ARG B 43 7895 7103 7646 398 -173 529 C ATOM 1905 C ARG B 43 -21.187 11.688 2.458 1.00 62.16 C ANISOU 1905 C ARG B 43 8168 7483 7967 377 -126 483 C ATOM 1906 O ARG B 43 -20.655 11.483 3.559 1.00 61.76 O ANISOU 1906 O ARG B 43 8064 7521 7879 299 -134 407 O ATOM 1907 CB ARG B 43 -21.425 10.313 0.342 1.00 57.71 C ANISOU 1907 CB ARG B 43 7655 6890 7381 451 -276 642 C ATOM 1908 CG ARG B 43 -20.889 10.026 -1.067 1.00 72.04 C ANISOU 1908 CG ARG B 43 9538 8637 9196 476 -300 685 C ATOM 1909 CD ARG B 43 -21.969 9.515 -2.007 1.00 90.25 C ANISOU 1909 CD ARG B 43 11838 10990 11462 519 -370 775 C ATOM 1910 NE ARG B 43 -23.024 10.512 -2.235 1.00105.89 N ANISOU 1910 NE ARG B 43 13792 12998 13444 630 -325 819 N ATOM 1911 CZ ARG B 43 -24.238 10.473 -1.687 1.00125.21 C ANISOU 1911 CZ ARG B 43 16139 15577 15859 655 -350 835 C ATOM 1912 NH1 ARG B 43 -25.117 11.435 -1.937 1.00116.85 N ANISOU 1912 NH1 ARG B 43 15050 14558 14789 809 -299 883 N ATOM 1913 NH2 ARG B 43 -24.580 9.470 -0.881 1.00106.16 N ANISOU 1913 NH2 ARG B 43 13663 13259 13413 539 -411 806 N ATOM 1914 N THR B 44 -22.321 12.377 2.320 1.00 58.04 N ANISOU 1914 N THR B 44 7655 6927 7469 465 -71 526 N ATOM 1915 CA THR B 44 -23.047 12.896 3.474 1.00 58.00 C ANISOU 1915 CA THR B 44 7606 6967 7464 463 -8 481 C ATOM 1916 C THR B 44 -24.100 11.890 3.946 1.00 58.63 C ANISOU 1916 C THR B 44 7585 7197 7496 453 -118 535 C ATOM 1917 O THR B 44 -24.533 11.071 3.126 1.00 57.09 O ANISOU 1917 O THR B 44 7369 7049 7272 472 -214 613 O ATOM 1918 CB THR B 44 -23.629 14.297 3.201 1.00 65.06 C ANISOU 1918 CB THR B 44 8581 7738 8400 587 153 487 C ATOM 1919 OG1 THR B 44 -24.635 14.218 2.179 1.00 63.13 O ANISOU 1919 OG1 THR B 44 8320 7526 8142 754 105 614 O ATOM 1920 CG2 THR B 44 -22.535 15.350 2.896 1.00 60.39 C ANISOU 1920 CG2 THR B 44 8139 6962 7843 539 319 404 C ATOM 1921 N PRO B 45 -24.544 11.938 5.232 1.00 53.34 N ANISOU 1921 N PRO B 45 6858 6607 6803 401 -91 481 N ATOM 1922 CA PRO B 45 -25.591 10.996 5.665 1.00 53.94 C ANISOU 1922 CA PRO B 45 6851 6821 6822 363 -169 521 C ATOM 1923 C PRO B 45 -26.921 11.249 4.943 1.00 59.95 C ANISOU 1923 C PRO B 45 7536 7659 7581 471 -169 580 C ATOM 1924 O PRO B 45 -27.314 12.405 4.727 1.00 60.90 O ANISOU 1924 O PRO B 45 7659 7740 7740 614 -74 585 O ATOM 1925 CB PRO B 45 -25.694 11.219 7.188 1.00 55.05 C ANISOU 1925 CB PRO B 45 6959 7021 6936 290 -114 441 C ATOM 1926 CG PRO B 45 -24.546 12.103 7.555 1.00 57.95 C ANISOU 1926 CG PRO B 45 7383 7304 7332 264 -27 348 C ATOM 1927 CD PRO B 45 -24.169 12.861 6.326 1.00 53.26 C ANISOU 1927 CD PRO B 45 6862 6569 6804 350 29 369 C ATOM 1928 N LYS B 46 -27.585 10.154 4.535 1.00 56.36 N ANISOU 1928 N LYS B 46 7023 7327 7065 408 -263 622 N ATOM 1929 CA LYS B 46 -28.889 10.205 3.860 1.00 57.40 C ANISOU 1929 CA LYS B 46 7027 7631 7153 481 -286 659 C ATOM 1930 C LYS B 46 -29.917 9.424 4.711 1.00 61.13 C ANISOU 1930 C LYS B 46 7388 8290 7549 339 -299 614 C ATOM 1931 O LYS B 46 -29.631 8.290 5.107 1.00 60.50 O ANISOU 1931 O LYS B 46 7377 8187 7424 161 -332 598 O ATOM 1932 CB LYS B 46 -28.782 9.598 2.443 1.00 59.67 C ANISOU 1932 CB LYS B 46 7330 7936 7404 478 -370 715 C ATOM 1933 CG LYS B 46 -29.993 9.889 1.552 1.00 87.08 C ANISOU 1933 CG LYS B 46 10649 11631 10807 598 -398 754 C ATOM 1934 CD LYS B 46 -30.298 8.743 0.579 1.00 96.53 C ANISOU 1934 CD LYS B 46 11806 12962 11908 459 -493 755 C ATOM 1935 CE LYS B 46 -31.678 8.851 -0.025 1.00104.89 C ANISOU 1935 CE LYS B 46 12642 14359 12851 524 -533 757 C ATOM 1936 NZ LYS B 46 -32.750 8.487 0.945 1.00110.50 N ANISOU 1936 NZ LYS B 46 13190 15296 13500 398 -512 676 N ATOM 1937 N LEU B 47 -31.106 10.011 4.966 1.00 57.86 N ANISOU 1937 N LEU B 47 6814 8059 7108 426 -258 597 N ATOM 1938 CA LEU B 47 -32.164 9.337 5.718 1.00 58.28 C ANISOU 1938 CA LEU B 47 6738 8325 7080 275 -254 537 C ATOM 1939 C LEU B 47 -32.677 8.128 4.906 1.00 61.30 C ANISOU 1939 C LEU B 47 7066 8866 7360 102 -329 528 C ATOM 1940 O LEU B 47 -33.010 8.278 3.724 1.00 61.50 O ANISOU 1940 O LEU B 47 7005 9013 7351 194 -382 561 O ATOM 1941 CB LEU B 47 -33.297 10.307 6.087 1.00 59.82 C ANISOU 1941 CB LEU B 47 6752 8713 7264 439 -186 515 C ATOM 1942 CG LEU B 47 -34.342 9.784 7.098 1.00 65.00 C ANISOU 1942 CG LEU B 47 7265 9592 7842 276 -152 430 C ATOM 1943 CD1 LEU B 47 -34.708 10.851 8.098 1.00 65.23 C ANISOU 1943 CD1 LEU B 47 7245 9627 7914 416 -42 396 C ATOM 1944 CD2 LEU B 47 -35.611 9.376 6.385 1.00 70.15 C ANISOU 1944 CD2 LEU B 47 7675 10603 8376 248 -198 403 C ATOM 1945 N ILE B 48 -32.692 6.930 5.534 1.00 55.27 N ANISOU 1945 N ILE B 48 6381 8086 6532 -154 -316 480 N ATOM 1946 CA ILE B 48 -33.139 5.697 4.864 1.00 55.10 C ANISOU 1946 CA ILE B 48 6362 8172 6400 -380 -341 444 C ATOM 1947 C ILE B 48 -34.435 5.121 5.492 1.00 59.16 C ANISOU 1947 C ILE B 48 6735 8948 6797 -603 -281 340 C ATOM 1948 O ILE B 48 -35.192 4.433 4.809 1.00 59.27 O ANISOU 1948 O ILE B 48 6653 9172 6696 -786 -286 272 O ATOM 1949 CB ILE B 48 -32.007 4.637 4.731 1.00 57.08 C ANISOU 1949 CB ILE B 48 6888 8147 6651 -500 -342 480 C ATOM 1950 CG1 ILE B 48 -31.391 4.226 6.096 1.00 56.44 C ANISOU 1950 CG1 ILE B 48 6985 7883 6574 -559 -282 491 C ATOM 1951 CG2 ILE B 48 -30.918 5.115 3.738 1.00 57.09 C ANISOU 1951 CG2 ILE B 48 6970 7981 6740 -314 -406 558 C ATOM 1952 CD1 ILE B 48 -30.980 2.807 6.127 1.00 58.85 C ANISOU 1952 CD1 ILE B 48 7534 8030 6795 -740 -237 504 C ATOM 1953 N MET B 49 -34.670 5.417 6.780 1.00 56.03 N ANISOU 1953 N MET B 49 6322 8552 6416 -610 -214 312 N ATOM 1954 CA MET B 49 -35.803 4.992 7.594 1.00 57.44 C ANISOU 1954 CA MET B 49 6379 8953 6491 -817 -134 208 C ATOM 1955 C MET B 49 -36.294 6.148 8.424 1.00 58.73 C ANISOU 1955 C MET B 49 6375 9233 6707 -632 -98 193 C ATOM 1956 O MET B 49 -35.494 6.905 8.969 1.00 55.99 O ANISOU 1956 O MET B 49 6135 8674 6464 -457 -89 248 O ATOM 1957 CB MET B 49 -35.401 3.872 8.565 1.00 60.90 C ANISOU 1957 CB MET B 49 7080 9183 6874 -1061 -49 197 C ATOM 1958 CG MET B 49 -34.993 2.570 7.898 1.00 66.35 C ANISOU 1958 CG MET B 49 7996 9721 7492 -1267 -32 204 C ATOM 1959 SD MET B 49 -36.367 1.532 7.339 1.00 73.87 S ANISOU 1959 SD MET B 49 8834 10969 8263 -1654 50 46 S ATOM 1960 CE MET B 49 -37.278 1.556 8.664 1.00 72.40 C ANISOU 1960 CE MET B 49 8551 10948 8012 -1801 160 -42 C ATOM 1961 N TYR B 50 -37.605 6.261 8.562 1.00 57.02 N ANISOU 1961 N TYR B 50 5895 9367 6403 -687 -61 101 N ATOM 1962 CA TYR B 50 -38.272 7.283 9.376 1.00 56.76 C ANISOU 1962 CA TYR B 50 5683 9488 6397 -517 0 70 C ATOM 1963 C TYR B 50 -39.456 6.636 10.090 1.00 61.68 C ANISOU 1963 C TYR B 50 6144 10405 6888 -789 85 -66 C ATOM 1964 O TYR B 50 -39.849 5.526 9.714 1.00 62.33 O ANISOU 1964 O TYR B 50 6222 10608 6851 -1092 95 -140 O ATOM 1965 CB TYR B 50 -38.689 8.511 8.524 1.00 57.68 C ANISOU 1965 CB TYR B 50 5584 9785 6546 -152 -44 121 C ATOM 1966 CG TYR B 50 -39.822 8.255 7.551 1.00 59.92 C ANISOU 1966 CG TYR B 50 5563 10515 6688 -171 -99 67 C ATOM 1967 CD1 TYR B 50 -39.574 7.749 6.277 1.00 61.54 C ANISOU 1967 CD1 TYR B 50 5782 10756 6844 -219 -196 97 C ATOM 1968 CD2 TYR B 50 -41.132 8.581 7.878 1.00 62.59 C ANISOU 1968 CD2 TYR B 50 5577 11277 6928 -120 -54 -21 C ATOM 1969 CE1 TYR B 50 -40.615 7.518 5.374 1.00 63.56 C ANISOU 1969 CE1 TYR B 50 5732 11479 6939 -251 -252 30 C ATOM 1970 CE2 TYR B 50 -42.182 8.332 6.997 1.00 65.50 C ANISOU 1970 CE2 TYR B 50 5618 12137 7133 -143 -111 -90 C ATOM 1971 CZ TYR B 50 -41.918 7.807 5.743 1.00 70.37 C ANISOU 1971 CZ TYR B 50 6249 12800 7688 -215 -214 -67 C ATOM 1972 OH TYR B 50 -42.959 7.585 4.877 1.00 72.22 O ANISOU 1972 OH TYR B 50 6134 13573 7733 -248 -276 -151 O ATOM 1973 N GLU B 51 -40.001 7.306 11.136 1.00 58.75 N ANISOU 1973 N GLU B 51 5658 10136 6529 -710 169 -112 N ATOM 1974 CA GLU B 51 -41.148 6.831 11.916 1.00 60.76 C ANISOU 1974 CA GLU B 51 5739 10687 6659 -956 270 -252 C ATOM 1975 C GLU B 51 -40.982 5.352 12.309 1.00 64.91 C ANISOU 1975 C GLU B 51 6494 11084 7085 -1385 333 -307 C ATOM 1976 O GLU B 51 -41.905 4.543 12.153 1.00 66.59 O ANISOU 1976 O GLU B 51 6575 11574 7153 -1688 392 -435 O ATOM 1977 CB GLU B 51 -42.471 7.093 11.159 1.00 64.91 C ANISOU 1977 CB GLU B 51 5853 11735 7076 -891 247 -339 C ATOM 1978 CG GLU B 51 -42.868 8.559 11.152 1.00 74.63 C ANISOU 1978 CG GLU B 51 6871 13113 8370 -445 247 -290 C ATOM 1979 CD GLU B 51 -43.856 9.007 10.093 1.00 90.60 C ANISOU 1979 CD GLU B 51 8519 15615 10290 -220 181 -304 C ATOM 1980 OE1 GLU B 51 -44.812 8.257 9.790 1.00 82.86 O ANISOU 1980 OE1 GLU B 51 7274 15067 9140 -473 174 -439 O ATOM 1981 OE2 GLU B 51 -43.695 10.146 9.600 1.00 86.18 O ANISOU 1981 OE2 GLU B 51 7928 15016 9801 218 152 -185 O ATOM 1982 N ASN B 52 -39.762 5.017 12.785 1.00 58.33 N ANISOU 1982 N ASN B 52 6015 9831 6316 -1399 332 -209 N ATOM 1983 CA ASN B 52 -39.269 3.717 13.271 1.00 58.24 C ANISOU 1983 CA ASN B 52 6330 9576 6224 -1696 405 -199 C ATOM 1984 C ASN B 52 -39.084 2.636 12.199 1.00 63.94 C ANISOU 1984 C ASN B 52 7184 10233 6878 -1890 388 -200 C ATOM 1985 O ASN B 52 -37.999 2.068 12.116 1.00 62.30 O ANISOU 1985 O ASN B 52 7290 9688 6695 -1877 372 -97 O ATOM 1986 CB ASN B 52 -40.119 3.171 14.414 1.00 59.52 C ANISOU 1986 CB ASN B 52 6493 9864 6258 -1983 561 -310 C ATOM 1987 CG ASN B 52 -40.594 4.220 15.398 1.00 86.01 C ANISOU 1987 CG ASN B 52 9658 13367 9656 -1829 599 -350 C ATOM 1988 OD1 ASN B 52 -39.807 4.982 15.971 1.00 81.63 O ANISOU 1988 OD1 ASN B 52 9199 12614 9202 -1596 567 -268 O ATOM 1989 ND2 ASN B 52 -41.902 4.292 15.598 1.00 79.28 N ANISOU 1989 ND2 ASN B 52 8520 12889 8715 -1966 681 -494 N ATOM 1990 N ASN B 53 -40.128 2.341 11.402 1.00 63.11 N ANISOU 1990 N ASN B 53 6836 10470 6673 -2071 400 -324 N ATOM 1991 CA ASN B 53 -40.154 1.259 10.408 1.00 63.44 C ANISOU 1991 CA ASN B 53 6985 10502 6616 -2334 419 -374 C ATOM 1992 C ASN B 53 -40.495 1.666 8.967 1.00 67.59 C ANISOU 1992 C ASN B 53 7230 11314 7137 -2219 290 -400 C ATOM 1993 O ASN B 53 -40.647 0.781 8.115 1.00 68.24 O ANISOU 1993 O ASN B 53 7365 11449 7114 -2477 316 -475 O ATOM 1994 CB ASN B 53 -41.132 0.164 10.870 1.00 66.34 C ANISOU 1994 CB ASN B 53 7385 11027 6795 -2809 608 -548 C ATOM 1995 CG ASN B 53 -42.463 0.685 11.381 1.00 85.32 C ANISOU 1995 CG ASN B 53 9395 13899 9124 -2885 656 -700 C ATOM 1996 OD1 ASN B 53 -43.100 1.554 10.772 1.00 74.88 O ANISOU 1996 OD1 ASN B 53 7672 12967 7813 -2684 548 -739 O ATOM 1997 ND2 ASN B 53 -42.886 0.194 12.543 1.00 77.18 N ANISOU 1997 ND2 ASN B 53 8478 12841 8006 -3145 826 -777 N ATOM 1998 N LYS B 54 -40.557 2.978 8.666 1.00 62.22 N ANISOU 1998 N LYS B 54 6292 10793 6558 -1831 168 -333 N ATOM 1999 CA LYS B 54 -40.890 3.393 7.299 1.00 61.41 C ANISOU 1999 CA LYS B 54 5933 10976 6423 -1680 47 -335 C ATOM 2000 C LYS B 54 -39.674 3.740 6.461 0.50 58.44 C ANISOU 2000 C LYS B 54 5751 10279 6176 -1418 -66 -175 C ATOM 2001 O LYS B 54 -38.905 4.622 6.810 0.50 51.68 O ANISOU 2001 O LYS B 54 4996 9172 5469 -1115 -102 -51 O ATOM 2002 CB LYS B 54 -41.923 4.534 7.266 1.00 65.40 C ANISOU 2002 CB LYS B 54 6014 11932 6902 -1409 3 -366 C ATOM 2003 CG LYS B 54 -43.277 4.165 7.832 1.00 76.46 C ANISOU 2003 CG LYS B 54 7130 13783 8139 -1683 103 -557 C ATOM 2004 CD LYS B 54 -44.295 5.269 7.578 1.00 86.45 C ANISOU 2004 CD LYS B 54 7943 15550 9354 -1354 46 -577 C ATOM 2005 CE LYS B 54 -45.528 5.152 8.452 0.50 87.99 C ANISOU 2005 CE LYS B 54 7852 16157 9423 -1549 161 -753 C ATOM 2006 NZ LYS B 54 -46.233 3.852 8.276 0.50 92.86 N ANISOU 2006 NZ LYS B 54 8384 17062 9836 -2098 244 -968 N ATOM 2007 N ARG B 55 -39.526 3.056 5.331 1.00 57.07 N ANISOU 2007 N ARG B 55 5621 10131 5930 -1558 -109 -197 N ATOM 2008 CA ARG B 55 -38.438 3.307 4.394 1.00 55.72 C ANISOU 2008 CA ARG B 55 5615 9697 5860 -1340 -209 -63 C ATOM 2009 C ARG B 55 -38.667 4.614 3.606 1.00 60.34 C ANISOU 2009 C ARG B 55 5940 10505 6481 -942 -326 17 C ATOM 2010 O ARG B 55 -39.776 4.909 3.177 1.00 62.39 O ANISOU 2010 O ARG B 55 5861 11228 6615 -905 -360 -55 O ATOM 2011 CB ARG B 55 -38.291 2.142 3.414 1.00 57.34 C ANISOU 2011 CB ARG B 55 5953 9874 5960 -1631 -198 -127 C ATOM 2012 CG ARG B 55 -37.746 0.863 4.028 1.00 67.87 C ANISOU 2012 CG ARG B 55 7665 10850 7273 -1944 -61 -154 C ATOM 2013 CD ARG B 55 -37.406 -0.122 2.932 1.00 83.10 C ANISOU 2013 CD ARG B 55 9772 12678 9123 -2156 -40 -193 C ATOM 2014 NE ARG B 55 -38.591 -0.482 2.158 1.00 96.36 N ANISOU 2014 NE ARG B 55 11179 14820 10614 -2433 -28 -373 N ATOM 2015 CZ ARG B 55 -39.298 -1.590 2.332 1.00106.27 C ANISOU 2015 CZ ARG B 55 12494 16181 11700 -2895 133 -555 C ATOM 2016 NH1 ARG B 55 -38.917 -2.497 3.223 1.00 91.72 N ANISOU 2016 NH1 ARG B 55 11031 13962 9856 -3110 308 -556 N ATOM 2017 NH2 ARG B 55 -40.376 -1.815 1.599 1.00 93.92 N ANISOU 2017 NH2 ARG B 55 10626 15112 9949 -3151 134 -743 N ATOM 2018 N SER B 56 -37.616 5.396 3.443 1.00 56.80 N ANISOU 2018 N SER B 56 5656 9738 6186 -641 -374 163 N ATOM 2019 CA SER B 56 -37.615 6.622 2.646 1.00 57.29 C ANISOU 2019 CA SER B 56 5584 9895 6287 -249 -451 267 C ATOM 2020 C SER B 56 -37.690 6.238 1.142 1.00 62.11 C ANISOU 2020 C SER B 56 6127 10682 6790 -280 -543 270 C ATOM 2021 O SER B 56 -37.511 5.069 0.795 1.00 62.65 O ANISOU 2021 O SER B 56 6310 10703 6792 -603 -535 195 O ATOM 2022 CB SER B 56 -36.340 7.415 2.919 1.00 59.35 C ANISOU 2022 CB SER B 56 6101 9717 6733 -11 -438 394 C ATOM 2023 OG SER B 56 -36.310 8.582 2.116 1.00 73.77 O ANISOU 2023 OG SER B 56 7860 11583 8588 352 -474 498 O ATOM 2024 N SER B 57 -37.985 7.214 0.271 1.00 58.99 N ANISOU 2024 N SER B 57 5563 10491 6360 59 -614 356 N ATOM 2025 CA SER B 57 -38.114 7.035 -1.168 1.00 59.72 C ANISOU 2025 CA SER B 57 5562 10802 6327 89 -710 372 C ATOM 2026 C SER B 57 -36.965 6.250 -1.811 1.00 63.18 C ANISOU 2026 C SER B 57 6299 10887 6820 -97 -727 391 C ATOM 2027 O SER B 57 -35.788 6.551 -1.573 1.00 59.25 O ANISOU 2027 O SER B 57 6076 9944 6491 11 -700 487 O ATOM 2028 CB SER B 57 -38.300 8.382 -1.857 1.00 63.04 C ANISOU 2028 CB SER B 57 5865 11354 6733 572 -759 519 C ATOM 2029 OG SER B 57 -39.535 8.972 -1.488 1.00 73.45 O ANISOU 2029 OG SER B 57 6857 13104 7945 759 -750 491 O ATOM 2030 N GLY B 58 -37.338 5.226 -2.585 1.00 62.49 N ANISOU 2030 N GLY B 58 6146 11023 6576 -394 -756 280 N ATOM 2031 CA GLY B 58 -36.414 4.357 -3.305 1.00 61.56 C ANISOU 2031 CA GLY B 58 6292 10625 6474 -592 -756 275 C ATOM 2032 C GLY B 58 -35.485 3.469 -2.490 1.00 65.40 C ANISOU 2032 C GLY B 58 7121 10650 7079 -821 -657 258 C ATOM 2033 O GLY B 58 -34.611 2.823 -3.074 1.00 63.43 O ANISOU 2033 O GLY B 58 7111 10136 6855 -920 -646 274 O ATOM 2034 N ILE B 59 -35.659 3.404 -1.142 1.00 63.54 N ANISOU 2034 N ILE B 59 6917 10323 6902 -889 -577 230 N ATOM 2035 CA ILE B 59 -34.811 2.562 -0.279 1.00 61.99 C ANISOU 2035 CA ILE B 59 7048 9721 6787 -1064 -480 232 C ATOM 2036 C ILE B 59 -35.142 1.065 -0.475 1.00 70.31 C ANISOU 2036 C ILE B 59 8233 10788 7696 -1491 -382 94 C ATOM 2037 O ILE B 59 -36.314 0.685 -0.420 1.00 72.40 O ANISOU 2037 O ILE B 59 8298 11401 7808 -1741 -339 -51 O ATOM 2038 CB ILE B 59 -34.814 3.019 1.214 1.00 63.25 C ANISOU 2038 CB ILE B 59 7223 9771 7037 -981 -426 257 C ATOM 2039 CG1 ILE B 59 -34.264 4.468 1.370 1.00 61.54 C ANISOU 2039 CG1 ILE B 59 6960 9452 6969 -588 -483 381 C ATOM 2040 CG2 ILE B 59 -34.077 2.032 2.151 1.00 62.20 C ANISOU 2040 CG2 ILE B 59 7415 9285 6933 -1162 -323 261 C ATOM 2041 CD1 ILE B 59 -32.880 4.857 0.606 1.00 58.28 C ANISOU 2041 CD1 ILE B 59 6743 8728 6673 -387 -533 497 C ATOM 2042 N PRO B 60 -34.123 0.205 -0.752 1.00 67.98 N ANISOU 2042 N PRO B 60 8273 10126 7431 -1583 -327 127 N ATOM 2043 CA PRO B 60 -34.415 -1.230 -0.991 1.00 69.64 C ANISOU 2043 CA PRO B 60 8672 10294 7495 -1992 -189 -6 C ATOM 2044 C PRO B 60 -35.102 -1.965 0.161 1.00 75.83 C ANISOU 2044 C PRO B 60 9536 11083 8194 -2287 -32 -108 C ATOM 2045 O PRO B 60 -34.967 -1.576 1.328 1.00 75.35 O ANISOU 2045 O PRO B 60 9498 10915 8217 -2154 -19 -39 O ATOM 2046 CB PRO B 60 -33.042 -1.835 -1.314 1.00 69.62 C ANISOU 2046 CB PRO B 60 9044 9839 7570 -1923 -148 90 C ATOM 2047 CG PRO B 60 -32.185 -0.680 -1.699 1.00 71.38 C ANISOU 2047 CG PRO B 60 9182 9993 7946 -1527 -298 236 C ATOM 2048 CD PRO B 60 -32.682 0.499 -0.921 1.00 66.45 C ANISOU 2048 CD PRO B 60 8298 9559 7388 -1323 -370 273 C ATOM 2049 N ASP B 61 -35.816 -3.053 -0.194 1.00 73.91 N ANISOU 2049 N ASP B 61 9356 10955 7771 -2714 106 -284 N ATOM 2050 CA ASP B 61 -36.594 -3.964 0.660 1.00 75.65 C ANISOU 2050 CA ASP B 61 9689 11197 7859 -3109 307 -428 C ATOM 2051 C ASP B 61 -35.732 -4.667 1.719 1.00 76.29 C ANISOU 2051 C ASP B 61 10229 10760 7999 -3090 459 -318 C ATOM 2052 O ASP B 61 -36.263 -5.112 2.739 1.00 77.63 O ANISOU 2052 O ASP B 61 10490 10910 8097 -3297 606 -378 O ATOM 2053 CB ASP B 61 -37.319 -5.038 -0.209 1.00 80.67 C ANISOU 2053 CB ASP B 61 10360 12011 8278 -3600 450 -654 C ATOM 2054 CG ASP B 61 -37.911 -4.548 -1.515 1.00 95.41 C ANISOU 2054 CG ASP B 61 11837 14363 10051 -3608 296 -750 C ATOM 2055 OD1 ASP B 61 -39.146 -4.622 -1.670 1.00 98.89 O ANISOU 2055 OD1 ASP B 61 11956 15308 10312 -3897 319 -951 O ATOM 2056 OD2 ASP B 61 -37.136 -4.100 -2.390 1.00105.88 O ANISOU 2056 OD2 ASP B 61 13173 15589 11466 -3326 157 -628 O ATOM 2057 N ARG B 62 -34.416 -4.812 1.436 1.00 70.44 N ANISOU 2057 N ARG B 62 9773 9626 7364 -2842 431 -161 N ATOM 2058 CA ARG B 62 -33.366 -5.394 2.290 1.00 69.88 C ANISOU 2058 CA ARG B 62 10122 9087 7342 -2705 538 -16 C ATOM 2059 C ARG B 62 -33.338 -4.667 3.654 1.00 71.42 C ANISOU 2059 C ARG B 62 10218 9303 7617 -2497 483 76 C ATOM 2060 O ARG B 62 -32.986 -5.267 4.663 1.00 71.84 O ANISOU 2060 O ARG B 62 10572 9091 7633 -2499 613 145 O ATOM 2061 CB ARG B 62 -31.971 -5.167 1.652 1.00 69.61 C ANISOU 2061 CB ARG B 62 10217 8798 7436 -2358 429 140 C ATOM 2062 CG ARG B 62 -31.731 -5.843 0.306 1.00 84.92 C ANISOU 2062 CG ARG B 62 12294 10655 9316 -2496 478 78 C ATOM 2063 CD ARG B 62 -30.243 -5.947 -0.032 1.00 80.90 C ANISOU 2063 CD ARG B 62 12024 9806 8909 -2179 444 237 C ATOM 2064 NE ARG B 62 -29.543 -4.661 -0.152 1.00 65.72 N ANISOU 2064 NE ARG B 62 9842 7976 7151 -1798 220 353 N ATOM 2065 CZ ARG B 62 -29.625 -3.844 -1.206 1.00 88.54 C ANISOU 2065 CZ ARG B 62 12463 11083 10094 -1715 69 333 C ATOM 2066 NH1 ARG B 62 -30.427 -4.137 -2.223 1.00 93.35 N ANISOU 2066 NH1 ARG B 62 12973 11901 10595 -1972 85 199 N ATOM 2067 NH2 ARG B 62 -28.918 -2.719 -1.240 1.00 67.42 N ANISOU 2067 NH2 ARG B 62 9623 8431 7561 -1386 -86 439 N ATOM 2068 N PHE B 63 -33.646 -3.361 3.650 1.00 65.42 N ANISOU 2068 N PHE B 63 9060 8841 6956 -2290 300 87 N ATOM 2069 CA PHE B 63 -33.669 -2.519 4.831 1.00 64.48 C ANISOU 2069 CA PHE B 63 8808 8775 6915 -2096 245 151 C ATOM 2070 C PHE B 63 -35.004 -2.571 5.502 1.00 69.60 C ANISOU 2070 C PHE B 63 9279 9706 7460 -2358 332 13 C ATOM 2071 O PHE B 63 -36.044 -2.442 4.854 1.00 71.62 O ANISOU 2071 O PHE B 63 9253 10320 7639 -2537 315 -127 O ATOM 2072 CB PHE B 63 -33.274 -1.078 4.494 1.00 64.46 C ANISOU 2072 CB PHE B 63 8527 8897 7069 -1735 48 231 C ATOM 2073 CG PHE B 63 -31.852 -0.994 4.012 1.00 64.63 C ANISOU 2073 CG PHE B 63 8728 8637 7192 -1484 -22 361 C ATOM 2074 CD1 PHE B 63 -30.805 -0.834 4.913 1.00 66.13 C ANISOU 2074 CD1 PHE B 63 9076 8601 7449 -1274 -30 474 C ATOM 2075 CD2 PHE B 63 -31.549 -1.142 2.660 1.00 66.76 C ANISOU 2075 CD2 PHE B 63 9005 8896 7467 -1476 -72 357 C ATOM 2076 CE1 PHE B 63 -29.488 -0.760 4.466 1.00 66.19 C ANISOU 2076 CE1 PHE B 63 9210 8406 7533 -1052 -91 574 C ATOM 2077 CE2 PHE B 63 -30.227 -1.100 2.218 1.00 68.28 C ANISOU 2077 CE2 PHE B 63 9357 8841 7745 -1258 -122 464 C ATOM 2078 CZ PHE B 63 -29.205 -0.905 3.122 1.00 65.18 C ANISOU 2078 CZ PHE B 63 9091 8252 7422 -1047 -130 568 C ATOM 2079 N SER B 64 -34.964 -2.809 6.804 1.00 64.96 N ANISOU 2079 N SER B 64 8855 8979 6848 -2387 433 48 N ATOM 2080 CA SER B 64 -36.125 -2.908 7.670 1.00 65.54 C ANISOU 2080 CA SER B 64 8807 9275 6821 -2639 544 -76 C ATOM 2081 C SER B 64 -35.752 -2.313 9.017 1.00 67.16 C ANISOU 2081 C SER B 64 9036 9387 7094 -2421 524 26 C ATOM 2082 O SER B 64 -34.592 -2.368 9.414 1.00 64.52 O ANISOU 2082 O SER B 64 8944 8754 6817 -2194 497 175 O ATOM 2083 CB SER B 64 -36.542 -4.365 7.822 1.00 69.35 C ANISOU 2083 CB SER B 64 9618 9610 7123 -3064 791 -177 C ATOM 2084 OG SER B 64 -37.765 -4.423 8.533 1.00 82.99 O ANISOU 2084 OG SER B 64 11182 11610 8742 -3351 905 -328 O ATOM 2085 N GLY B 65 -36.728 -1.736 9.696 1.00 65.93 N ANISOU 2085 N GLY B 65 8613 9519 6919 -2486 537 -65 N ATOM 2086 CA GLY B 65 -36.514 -1.108 10.993 1.00 65.78 C ANISOU 2086 CA GLY B 65 8588 9455 6951 -2313 529 2 C ATOM 2087 C GLY B 65 -37.571 -1.480 12.002 1.00 73.02 C ANISOU 2087 C GLY B 65 9482 10522 7739 -2602 692 -115 C ATOM 2088 O GLY B 65 -38.713 -1.760 11.636 1.00 74.52 O ANISOU 2088 O GLY B 65 9483 11001 7832 -2890 766 -280 O ATOM 2089 N SER B 66 -37.184 -1.521 13.277 1.00 70.76 N ANISOU 2089 N SER B 66 9387 10065 7433 -2542 754 -38 N ATOM 2090 CA SER B 66 -38.093 -1.837 14.375 1.00 72.88 C ANISOU 2090 CA SER B 66 9669 10444 7576 -2799 920 -134 C ATOM 2091 C SER B 66 -37.758 -1.032 15.620 1.00 74.94 C ANISOU 2091 C SER B 66 9896 10689 7889 -2576 880 -62 C ATOM 2092 O SER B 66 -36.659 -0.509 15.728 1.00 72.31 O ANISOU 2092 O SER B 66 9628 10193 7653 -2265 755 70 O ATOM 2093 CB SER B 66 -38.123 -3.341 14.658 1.00 79.88 C ANISOU 2093 CB SER B 66 10994 11072 8283 -3126 1149 -140 C ATOM 2094 OG SER B 66 -36.889 -3.860 15.128 1.00 87.88 O ANISOU 2094 OG SER B 66 12423 11691 9276 -2931 1168 52 O ATOM 2095 N LYS B 67 -38.723 -0.886 16.532 1.00 73.52 N ANISOU 2095 N LYS B 67 9589 10710 7634 -2749 989 -170 N ATOM 2096 CA LYS B 67 -38.542 -0.169 17.792 1.00 72.17 C ANISOU 2096 CA LYS B 67 9389 10547 7486 -2590 981 -131 C ATOM 2097 C LYS B 67 -39.241 -0.944 18.922 1.00 77.46 C ANISOU 2097 C LYS B 67 10237 11220 7975 -2904 1197 -197 C ATOM 2098 O LYS B 67 -40.397 -1.357 18.762 1.00 78.25 O ANISOU 2098 O LYS B 67 10211 11536 7985 -3229 1327 -359 O ATOM 2099 CB LYS B 67 -39.055 1.288 17.697 1.00 73.55 C ANISOU 2099 CB LYS B 67 9126 11021 7797 -2385 871 -206 C ATOM 2100 CG LYS B 67 -38.807 2.121 18.973 1.00 77.35 C ANISOU 2100 CG LYS B 67 9586 11496 8307 -2223 875 -183 C ATOM 2101 CD LYS B 67 -39.118 3.610 18.814 1.00 84.70 C ANISOU 2101 CD LYS B 67 10162 12636 9383 -1968 791 -236 C ATOM 2102 CE LYS B 67 -40.525 3.977 19.234 1.00 88.74 C ANISOU 2102 CE LYS B 67 10381 13489 9848 -2091 896 -391 C ATOM 2103 NZ LYS B 67 -40.695 5.434 19.469 1.00 87.30 N ANISOU 2103 NZ LYS B 67 9951 13434 9785 -1802 863 -419 N ATOM 2104 N SER B 68 -38.527 -1.143 20.047 1.00 72.97 N ANISOU 2104 N SER B 68 9954 10435 7336 -2811 1239 -77 N ATOM 2105 CA SER B 68 -39.028 -1.829 21.246 1.00 75.51 C ANISOU 2105 CA SER B 68 10502 10716 7473 -3062 1448 -104 C ATOM 2106 C SER B 68 -38.507 -1.088 22.482 1.00 77.76 C ANISOU 2106 C SER B 68 10785 11003 7759 -2836 1393 -30 C ATOM 2107 O SER B 68 -37.298 -0.913 22.622 1.00 75.89 O ANISOU 2107 O SER B 68 10690 10596 7549 -2550 1272 122 O ATOM 2108 CB SER B 68 -38.571 -3.291 21.274 1.00 81.73 C ANISOU 2108 CB SER B 68 11807 11157 8091 -3214 1611 3 C ATOM 2109 OG SER B 68 -38.324 -3.834 19.984 1.00 94.68 O ANISOU 2109 OG SER B 68 13523 12680 9773 -3250 1586 12 O ATOM 2110 N GLY B 69 -39.417 -0.630 23.338 1.00 75.94 N ANISOU 2110 N GLY B 69 10369 10995 7489 -2971 1483 -154 N ATOM 2111 CA GLY B 69 -39.083 0.112 24.550 1.00 75.46 C ANISOU 2111 CA GLY B 69 10283 10974 7414 -2808 1457 -123 C ATOM 2112 C GLY B 69 -38.155 1.271 24.257 1.00 78.43 C ANISOU 2112 C GLY B 69 10476 11358 7965 -2443 1243 -68 C ATOM 2113 O GLY B 69 -38.469 2.108 23.406 1.00 78.02 O ANISOU 2113 O GLY B 69 10110 11452 8081 -2341 1150 -145 O ATOM 2114 N ASN B 70 -36.960 1.266 24.881 1.00 73.10 N ANISOU 2114 N ASN B 70 10015 10529 7233 -2244 1172 69 N ATOM 2115 CA ASN B 70 -35.949 2.304 24.684 1.00 70.35 C ANISOU 2115 CA ASN B 70 9525 10186 7018 -1943 994 105 C ATOM 2116 C ASN B 70 -34.888 1.933 23.644 1.00 71.26 C ANISOU 2116 C ASN B 70 9758 10124 7193 -1769 864 230 C ATOM 2117 O ASN B 70 -33.833 2.573 23.578 1.00 68.20 O ANISOU 2117 O ASN B 70 9323 9721 6870 -1538 731 275 O ATOM 2118 CB ASN B 70 -35.319 2.706 26.023 1.00 70.07 C ANISOU 2118 CB ASN B 70 9565 10187 6871 -1847 988 132 C ATOM 2119 CG ASN B 70 -36.321 3.267 26.994 1.00 85.45 C ANISOU 2119 CG ASN B 70 11365 12318 8786 -1994 1111 -8 C ATOM 2120 OD1 ASN B 70 -37.346 3.851 26.608 1.00 78.80 O ANISOU 2120 OD1 ASN B 70 10256 11619 8064 -2069 1157 -143 O ATOM 2121 ND2 ASN B 70 -36.043 3.113 28.280 1.00 77.00 N ANISOU 2121 ND2 ASN B 70 10455 11268 7536 -2018 1168 24 N ATOM 2122 N SER B 71 -35.185 0.931 22.806 1.00 68.19 N ANISOU 2122 N SER B 71 9512 9618 6780 -1902 916 263 N ATOM 2123 CA SER B 71 -34.251 0.485 21.782 1.00 66.94 C ANISOU 2123 CA SER B 71 9482 9282 6669 -1754 817 374 C ATOM 2124 C SER B 71 -34.860 0.450 20.382 1.00 67.67 C ANISOU 2124 C SER B 71 9416 9407 6888 -1849 796 300 C ATOM 2125 O SER B 71 -36.065 0.261 20.224 1.00 67.86 O ANISOU 2125 O SER B 71 9328 9565 6892 -2097 901 180 O ATOM 2126 CB SER B 71 -33.647 -0.866 22.157 1.00 74.39 C ANISOU 2126 CB SER B 71 10861 9989 7416 -1758 908 531 C ATOM 2127 OG SER B 71 -32.865 -1.388 21.093 1.00 86.56 O ANISOU 2127 OG SER B 71 12534 11354 9001 -1629 840 628 O ATOM 2128 N ALA B 72 -34.011 0.665 19.374 1.00 62.57 N ANISOU 2128 N ALA B 72 8741 8675 6356 -1654 659 363 N ATOM 2129 CA ALA B 72 -34.358 0.624 17.958 1.00 61.56 C ANISOU 2129 CA ALA B 72 8487 8569 6334 -1699 614 318 C ATOM 2130 C ALA B 72 -33.318 -0.232 17.224 1.00 65.76 C ANISOU 2130 C ALA B 72 9289 8853 6843 -1604 578 446 C ATOM 2131 O ALA B 72 -32.142 -0.211 17.600 1.00 64.05 O ANISOU 2131 O ALA B 72 9209 8522 6606 -1380 510 562 O ATOM 2132 CB ALA B 72 -34.384 2.036 17.379 1.00 60.74 C ANISOU 2132 CB ALA B 72 8039 8626 6415 -1512 483 259 C ATOM 2133 N THR B 73 -33.748 -1.013 16.204 1.00 63.88 N ANISOU 2133 N THR B 73 9126 8557 6590 -1778 635 414 N ATOM 2134 CA THR B 73 -32.839 -1.841 15.409 1.00 63.68 C ANISOU 2134 CA THR B 73 9363 8286 6546 -1697 625 521 C ATOM 2135 C THR B 73 -33.031 -1.671 13.918 1.00 67.21 C ANISOU 2135 C THR B 73 9642 8791 7103 -1726 549 459 C ATOM 2136 O THR B 73 -34.164 -1.601 13.426 1.00 68.34 O ANISOU 2136 O THR B 73 9588 9132 7248 -1949 587 324 O ATOM 2137 CB THR B 73 -32.889 -3.345 15.751 1.00 71.83 C ANISOU 2137 CB THR B 73 10836 9071 7387 -1879 831 580 C ATOM 2138 OG1 THR B 73 -34.205 -3.841 15.541 1.00 87.36 O ANISOU 2138 OG1 THR B 73 12781 11129 9283 -2265 989 427 O ATOM 2139 CG2 THR B 73 -32.416 -3.672 17.138 1.00 63.30 C ANISOU 2139 CG2 THR B 73 10005 7883 6162 -1773 902 696 C ATOM 2140 N LEU B 74 -31.909 -1.654 13.194 1.00 62.63 N ANISOU 2140 N LEU B 74 9137 8065 6594 -1502 445 556 N ATOM 2141 CA LEU B 74 -31.862 -1.614 11.732 1.00 61.13 C ANISOU 2141 CA LEU B 74 8853 7884 6491 -1502 374 525 C ATOM 2142 C LEU B 74 -31.351 -2.991 11.257 1.00 66.19 C ANISOU 2142 C LEU B 74 9878 8243 7030 -1573 487 593 C ATOM 2143 O LEU B 74 -30.357 -3.518 11.788 1.00 64.34 O ANISOU 2143 O LEU B 74 9921 7793 6732 -1395 516 729 O ATOM 2144 CB LEU B 74 -30.990 -0.460 11.220 1.00 58.04 C ANISOU 2144 CB LEU B 74 8254 7538 6260 -1202 192 570 C ATOM 2145 CG LEU B 74 -30.944 -0.221 9.697 1.00 61.24 C ANISOU 2145 CG LEU B 74 8534 7976 6756 -1172 107 544 C ATOM 2146 CD1 LEU B 74 -32.315 0.213 9.122 1.00 60.32 C ANISOU 2146 CD1 LEU B 74 8133 8137 6650 -1338 105 415 C ATOM 2147 CD2 LEU B 74 -29.877 0.824 9.356 1.00 61.79 C ANISOU 2147 CD2 LEU B 74 8487 8028 6964 -880 -33 602 C ATOM 2148 N THR B 75 -32.116 -3.621 10.347 1.00 65.12 N ANISOU 2148 N THR B 75 9768 8126 6847 -1848 576 490 N ATOM 2149 CA THR B 75 -31.760 -4.933 9.815 1.00 66.54 C ANISOU 2149 CA THR B 75 10337 8020 6924 -1963 725 524 C ATOM 2150 C THR B 75 -31.659 -4.877 8.305 1.00 70.46 C ANISOU 2150 C THR B 75 10725 8553 7492 -1982 648 472 C ATOM 2151 O THR B 75 -32.585 -4.415 7.637 1.00 71.18 O ANISOU 2151 O THR B 75 10513 8924 7609 -2153 596 334 O ATOM 2152 CB THR B 75 -32.673 -6.080 10.346 1.00 80.59 C ANISOU 2152 CB THR B 75 12401 9701 8517 -2345 991 442 C ATOM 2153 OG1 THR B 75 -34.029 -5.868 9.967 1.00 86.32 O ANISOU 2153 OG1 THR B 75 12838 10740 9221 -2686 1020 239 O ATOM 2154 CG2 THR B 75 -32.595 -6.252 11.858 1.00 80.01 C ANISOU 2154 CG2 THR B 75 12515 9535 8348 -2289 1084 530 C ATOM 2155 N ILE B 76 -30.479 -5.272 7.786 1.00 65.58 N ANISOU 2155 N ILE B 76 10332 7686 6900 -1768 628 589 N ATOM 2156 CA ILE B 76 -30.181 -5.404 6.365 1.00 64.13 C ANISOU 2156 CA ILE B 76 10132 7469 6764 -1773 583 558 C ATOM 2157 C ILE B 76 -30.208 -6.910 6.094 1.00 70.21 C ANISOU 2157 C ILE B 76 11351 7941 7383 -2001 829 541 C ATOM 2158 O ILE B 76 -29.319 -7.628 6.553 1.00 69.33 O ANISOU 2158 O ILE B 76 11608 7523 7212 -1821 931 681 O ATOM 2159 CB ILE B 76 -28.815 -4.791 5.910 1.00 64.72 C ANISOU 2159 CB ILE B 76 10147 7474 6971 -1387 412 683 C ATOM 2160 CG1 ILE B 76 -28.530 -3.415 6.576 1.00 63.04 C ANISOU 2160 CG1 ILE B 76 9618 7457 6879 -1143 233 722 C ATOM 2161 CG2 ILE B 76 -28.745 -4.733 4.365 1.00 62.84 C ANISOU 2161 CG2 ILE B 76 9817 7272 6786 -1432 352 623 C ATOM 2162 CD1 ILE B 76 -27.110 -2.807 6.391 1.00 67.59 C ANISOU 2162 CD1 ILE B 76 10148 7976 7557 -795 97 826 C ATOM 2163 N THR B 77 -31.243 -7.386 5.393 1.00 70.04 N ANISOU 2163 N THR B 77 11309 8024 7279 -2395 941 365 N ATOM 2164 CA THR B 77 -31.360 -8.799 5.015 1.00 73.53 C ANISOU 2164 CA THR B 77 12193 8179 7567 -2682 1213 306 C ATOM 2165 C THR B 77 -30.683 -8.924 3.652 1.00 79.68 C ANISOU 2165 C THR B 77 13004 8870 8400 -2592 1155 310 C ATOM 2166 O THR B 77 -30.818 -8.020 2.818 1.00 79.54 O ANISOU 2166 O THR B 77 12597 9142 8484 -2537 947 257 O ATOM 2167 CB THR B 77 -32.832 -9.224 4.927 1.00 84.00 C ANISOU 2167 CB THR B 77 13449 9714 8754 -3211 1376 72 C ATOM 2168 OG1 THR B 77 -33.469 -8.465 3.894 1.00 92.40 O ANISOU 2168 OG1 THR B 77 14049 11189 9869 -3312 1197 -70 O ATOM 2169 CG2 THR B 77 -33.576 -9.058 6.233 1.00 76.76 C ANISOU 2169 CG2 THR B 77 12469 8917 7780 -3327 1440 47 C ATOM 2170 N GLY B 78 -29.949 -10.009 3.442 1.00 77.76 N ANISOU 2170 N GLY B 78 13235 8228 8083 -2551 1346 383 N ATOM 2171 CA GLY B 78 -29.259 -10.273 2.184 1.00 77.17 C ANISOU 2171 CA GLY B 78 13254 8025 8043 -2473 1333 385 C ATOM 2172 C GLY B 78 -28.272 -9.190 1.806 1.00 79.21 C ANISOU 2172 C GLY B 78 13206 8407 8481 -2044 1045 508 C ATOM 2173 O GLY B 78 -28.392 -8.569 0.740 1.00 78.87 O ANISOU 2173 O GLY B 78 12869 8585 8514 -2073 892 431 O ATOM 2174 N LEU B 79 -27.305 -8.942 2.706 1.00 74.18 N ANISOU 2174 N LEU B 79 12634 7654 7895 -1655 978 693 N ATOM 2175 CA LEU B 79 -26.252 -7.934 2.570 1.00 70.64 C ANISOU 2175 CA LEU B 79 11924 7317 7599 -1257 737 803 C ATOM 2176 C LEU B 79 -25.607 -7.894 1.177 1.00 74.20 C ANISOU 2176 C LEU B 79 12345 7732 8118 -1178 676 786 C ATOM 2177 O LEU B 79 -25.393 -8.933 0.552 1.00 76.21 O ANISOU 2177 O LEU B 79 12933 7734 8290 -1266 852 771 O ATOM 2178 CB LEU B 79 -25.193 -8.156 3.667 1.00 70.56 C ANISOU 2178 CB LEU B 79 12112 7140 7556 -893 754 989 C ATOM 2179 CG LEU B 79 -24.228 -7.008 3.986 1.00 72.55 C ANISOU 2179 CG LEU B 79 12051 7582 7933 -531 517 1076 C ATOM 2180 CD1 LEU B 79 -24.957 -5.786 4.522 1.00 69.79 C ANISOU 2180 CD1 LEU B 79 11309 7538 7671 -613 363 1005 C ATOM 2181 CD2 LEU B 79 -23.177 -7.462 4.980 1.00 76.95 C ANISOU 2181 CD2 LEU B 79 12829 8008 8399 -188 558 1246 C ATOM 2182 N GLN B 80 -25.335 -6.676 0.692 1.00 68.29 N ANISOU 2182 N GLN B 80 11214 7224 7510 -1028 447 783 N ATOM 2183 CA GLN B 80 -24.702 -6.398 -0.594 1.00 67.17 C ANISOU 2183 CA GLN B 80 10990 7090 7443 -932 362 772 C ATOM 2184 C GLN B 80 -23.448 -5.571 -0.343 1.00 71.70 C ANISOU 2184 C GLN B 80 11417 7696 8130 -551 211 887 C ATOM 2185 O GLN B 80 -23.313 -4.978 0.737 1.00 71.51 O ANISOU 2185 O GLN B 80 11265 7771 8137 -411 138 941 O ATOM 2186 CB GLN B 80 -25.655 -5.619 -1.509 1.00 67.02 C ANISOU 2186 CB GLN B 80 10644 7361 7460 -1138 247 646 C ATOM 2187 CG GLN B 80 -26.778 -6.466 -2.069 1.00 77.04 C ANISOU 2187 CG GLN B 80 12019 8661 8591 -1544 391 495 C ATOM 2188 CD GLN B 80 -27.626 -5.739 -3.085 1.00 83.11 C ANISOU 2188 CD GLN B 80 12444 9773 9359 -1698 262 380 C ATOM 2189 OE1 GLN B 80 -27.288 -4.645 -3.582 1.00 73.64 O ANISOU 2189 OE1 GLN B 80 10985 8728 8268 -1480 81 429 O ATOM 2190 NE2 GLN B 80 -28.771 -6.334 -3.388 1.00 67.84 N ANISOU 2190 NE2 GLN B 80 10509 7983 7282 -2082 368 219 N ATOM 2191 N THR B 81 -22.542 -5.499 -1.343 1.00 67.55 N ANISOU 2191 N THR B 81 10895 7113 7657 -406 171 905 N ATOM 2192 CA THR B 81 -21.300 -4.727 -1.194 1.00 66.23 C ANISOU 2192 CA THR B 81 10574 7007 7583 -82 46 983 C ATOM 2193 C THR B 81 -21.581 -3.217 -1.218 1.00 68.62 C ANISOU 2193 C THR B 81 10501 7568 8004 -78 -126 940 C ATOM 2194 O THR B 81 -20.791 -2.457 -0.676 1.00 68.90 O ANISOU 2194 O THR B 81 10389 7688 8100 123 -211 979 O ATOM 2195 CB THR B 81 -20.199 -5.182 -2.174 1.00 73.01 C ANISOU 2195 CB THR B 81 11568 7724 8447 73 83 1011 C ATOM 2196 OG1 THR B 81 -20.597 -4.923 -3.509 1.00 69.10 O ANISOU 2196 OG1 THR B 81 10987 7277 7990 -101 53 923 O ATOM 2197 CG2 THR B 81 -19.861 -6.664 -2.018 1.00 76.16 C ANISOU 2197 CG2 THR B 81 12384 7833 8719 128 285 1073 C ATOM 2198 N GLY B 82 -22.717 -2.810 -1.790 1.00 63.49 N ANISOU 2198 N GLY B 82 9706 7052 7365 -297 -159 857 N ATOM 2199 CA GLY B 82 -23.147 -1.415 -1.831 1.00 60.71 C ANISOU 2199 CA GLY B 82 9041 6921 7104 -273 -288 829 C ATOM 2200 C GLY B 82 -23.717 -0.947 -0.499 1.00 61.85 C ANISOU 2200 C GLY B 82 9075 7174 7254 -277 -305 831 C ATOM 2201 O GLY B 82 -23.911 0.254 -0.303 1.00 60.30 O ANISOU 2201 O GLY B 82 8652 7124 7135 -209 -387 819 O ATOM 2202 N ASP B 83 -23.996 -1.894 0.430 1.00 59.54 N ANISOU 2202 N ASP B 83 8966 6788 6868 -358 -205 847 N ATOM 2203 CA ASP B 83 -24.529 -1.600 1.771 1.00 59.06 C ANISOU 2203 CA ASP B 83 8834 6817 6790 -378 -202 849 C ATOM 2204 C ASP B 83 -23.440 -1.196 2.754 1.00 64.38 C ANISOU 2204 C ASP B 83 9493 7478 7490 -136 -245 921 C ATOM 2205 O ASP B 83 -23.749 -0.685 3.830 1.00 64.80 O ANISOU 2205 O ASP B 83 9443 7635 7543 -128 -264 915 O ATOM 2206 CB ASP B 83 -25.348 -2.771 2.325 1.00 61.46 C ANISOU 2206 CB ASP B 83 9358 7034 6961 -597 -56 828 C ATOM 2207 CG ASP B 83 -26.525 -3.179 1.473 1.00 63.95 C ANISOU 2207 CG ASP B 83 9652 7428 7216 -899 1 715 C ATOM 2208 OD1 ASP B 83 -27.122 -2.296 0.827 1.00 62.63 O ANISOU 2208 OD1 ASP B 83 9206 7488 7103 -933 -102 655 O ATOM 2209 OD2 ASP B 83 -26.880 -4.376 1.491 1.00 66.17 O ANISOU 2209 OD2 ASP B 83 10202 7561 7377 -1104 163 683 O ATOM 2210 N GLU B 84 -22.170 -1.443 2.386 1.00 61.35 N ANISOU 2210 N GLU B 84 9199 6998 7114 55 -257 977 N ATOM 2211 CA GLU B 84 -20.968 -1.096 3.135 1.00 61.22 C ANISOU 2211 CA GLU B 84 9130 7034 7096 292 -307 1027 C ATOM 2212 C GLU B 84 -20.988 0.405 3.377 1.00 62.87 C ANISOU 2212 C GLU B 84 9052 7427 7410 301 -401 960 C ATOM 2213 O GLU B 84 -20.860 1.182 2.436 1.00 64.05 O ANISOU 2213 O GLU B 84 9076 7606 7655 295 -445 917 O ATOM 2214 CB GLU B 84 -19.739 -1.524 2.322 1.00 62.94 C ANISOU 2214 CB GLU B 84 9437 7166 7311 465 -304 1067 C ATOM 2215 CG GLU B 84 -18.491 -1.790 3.137 1.00 74.17 C ANISOU 2215 CG GLU B 84 10889 8641 8651 729 -315 1138 C ATOM 2216 CD GLU B 84 -17.547 -2.764 2.468 1.00 95.19 C ANISOU 2216 CD GLU B 84 13745 11169 11254 908 -255 1205 C ATOM 2217 OE1 GLU B 84 -17.204 -2.542 1.284 1.00 90.30 O ANISOU 2217 OE1 GLU B 84 13075 10520 10715 889 -272 1160 O ATOM 2218 OE2 GLU B 84 -17.160 -3.757 3.126 1.00 87.77 O ANISOU 2218 OE2 GLU B 84 13025 10146 10177 1084 -177 1309 O ATOM 2219 N ALA B 85 -21.282 0.818 4.621 1.00 57.31 N ANISOU 2219 N ALA B 85 8268 6828 6679 295 -409 949 N ATOM 2220 CA ALA B 85 -21.442 2.238 4.973 1.00 55.14 C ANISOU 2220 CA ALA B 85 7759 6698 6492 279 -457 874 C ATOM 2221 C ALA B 85 -21.424 2.415 6.481 1.00 55.92 C ANISOU 2221 C ALA B 85 7820 6905 6522 301 -452 868 C ATOM 2222 O ALA B 85 -21.365 1.436 7.216 1.00 53.51 O ANISOU 2222 O ALA B 85 7671 6566 6095 336 -417 937 O ATOM 2223 CB ALA B 85 -22.784 2.740 4.430 1.00 54.72 C ANISOU 2223 CB ALA B 85 7618 6667 6504 131 -450 828 C ATOM 2224 N ASP B 86 -21.543 3.669 6.931 1.00 54.66 N ANISOU 2224 N ASP B 86 7480 6861 6428 276 -467 787 N ATOM 2225 CA ASP B 86 -21.713 4.006 8.350 1.00 56.16 C ANISOU 2225 CA ASP B 86 7612 7170 6557 258 -454 755 C ATOM 2226 C ASP B 86 -23.210 4.243 8.543 1.00 56.43 C ANISOU 2226 C ASP B 86 7611 7202 6625 117 -410 728 C ATOM 2227 O ASP B 86 -23.817 4.939 7.744 1.00 54.55 O ANISOU 2227 O ASP B 86 7285 6954 6489 81 -407 690 O ATOM 2228 CB ASP B 86 -20.955 5.288 8.718 1.00 58.66 C ANISOU 2228 CB ASP B 86 7762 7611 6917 284 -464 652 C ATOM 2229 CG ASP B 86 -19.479 5.113 8.943 1.00 67.44 C ANISOU 2229 CG ASP B 86 8843 8836 7944 402 -506 645 C ATOM 2230 OD1 ASP B 86 -19.064 3.996 9.267 1.00 67.15 O ANISOU 2230 OD1 ASP B 86 8917 8812 7785 514 -530 741 O ATOM 2231 OD2 ASP B 86 -18.754 6.119 8.882 1.00 78.74 O ANISOU 2231 OD2 ASP B 86 10140 10362 9415 384 -499 537 O ATOM 2232 N TYR B 87 -23.794 3.655 9.578 1.00 53.61 N ANISOU 2232 N TYR B 87 7325 6874 6170 53 -371 749 N ATOM 2233 CA TYR B 87 -25.224 3.782 9.863 1.00 52.78 C ANISOU 2233 CA TYR B 87 7170 6810 6075 -92 -320 710 C ATOM 2234 C TYR B 87 -25.451 4.482 11.192 1.00 57.09 C ANISOU 2234 C TYR B 87 7625 7474 6593 -112 -291 652 C ATOM 2235 O TYR B 87 -24.817 4.142 12.188 1.00 57.57 O ANISOU 2235 O TYR B 87 7754 7574 6544 -68 -293 679 O ATOM 2236 CB TYR B 87 -25.916 2.403 9.824 1.00 53.18 C ANISOU 2236 CB TYR B 87 7405 6778 6023 -218 -259 762 C ATOM 2237 CG TYR B 87 -25.963 1.816 8.430 1.00 54.17 C ANISOU 2237 CG TYR B 87 7603 6800 6178 -253 -264 784 C ATOM 2238 CD1 TYR B 87 -24.910 1.053 7.936 1.00 55.28 C ANISOU 2238 CD1 TYR B 87 7917 6804 6284 -146 -273 858 C ATOM 2239 CD2 TYR B 87 -27.039 2.067 7.583 1.00 54.94 C ANISOU 2239 CD2 TYR B 87 7579 6969 6325 -376 -262 724 C ATOM 2240 CE1 TYR B 87 -24.938 0.535 6.645 1.00 55.13 C ANISOU 2240 CE1 TYR B 87 7973 6687 6288 -190 -267 865 C ATOM 2241 CE2 TYR B 87 -27.096 1.521 6.307 1.00 54.94 C ANISOU 2241 CE2 TYR B 87 7639 6908 6329 -429 -267 730 C ATOM 2242 CZ TYR B 87 -26.035 0.771 5.833 1.00 61.21 C ANISOU 2242 CZ TYR B 87 8627 7530 7099 -347 -265 796 C ATOM 2243 OH TYR B 87 -26.080 0.267 4.549 1.00 60.08 O ANISOU 2243 OH TYR B 87 8548 7322 6957 -410 -260 789 O ATOM 2244 N TYR B 88 -26.343 5.470 11.204 1.00 52.54 N ANISOU 2244 N TYR B 88 6895 6967 6099 -158 -260 576 N ATOM 2245 CA TYR B 88 -26.627 6.237 12.419 1.00 52.96 C ANISOU 2245 CA TYR B 88 6864 7122 6136 -183 -212 504 C ATOM 2246 C TYR B 88 -28.098 6.186 12.716 1.00 54.50 C ANISOU 2246 C TYR B 88 6996 7391 6320 -296 -149 472 C ATOM 2247 O TYR B 88 -28.925 6.273 11.818 1.00 51.32 O ANISOU 2247 O TYR B 88 6514 7013 5974 -314 -148 466 O ATOM 2248 CB TYR B 88 -26.212 7.733 12.284 1.00 54.24 C ANISOU 2248 CB TYR B 88 6907 7295 6406 -110 -191 418 C ATOM 2249 CG TYR B 88 -24.782 7.968 11.857 1.00 56.97 C ANISOU 2249 CG TYR B 88 7275 7601 6769 -33 -236 412 C ATOM 2250 CD1 TYR B 88 -24.426 7.965 10.509 1.00 57.56 C ANISOU 2250 CD1 TYR B 88 7368 7580 6922 28 -272 451 C ATOM 2251 CD2 TYR B 88 -23.786 8.230 12.797 1.00 59.06 C ANISOU 2251 CD2 TYR B 88 7523 7963 6956 -34 -237 352 C ATOM 2252 CE1 TYR B 88 -23.101 8.156 10.110 1.00 57.92 C ANISOU 2252 CE1 TYR B 88 7422 7609 6975 82 -301 433 C ATOM 2253 CE2 TYR B 88 -22.452 8.403 12.411 1.00 59.98 C ANISOU 2253 CE2 TYR B 88 7623 8103 7066 19 -275 326 C ATOM 2254 CZ TYR B 88 -22.117 8.387 11.066 1.00 71.11 C ANISOU 2254 CZ TYR B 88 9056 9399 8565 74 -301 363 C ATOM 2255 OH TYR B 88 -20.808 8.609 10.675 1.00 79.32 O ANISOU 2255 OH TYR B 88 10064 10479 9597 109 -324 319 O ATOM 2256 N CYS B 89 -28.410 6.146 13.997 1.00 53.11 N ANISOU 2256 N CYS B 89 6827 7291 6062 -364 -96 439 N ATOM 2257 CA CYS B 89 -29.762 6.205 14.505 1.00 54.37 C ANISOU 2257 CA CYS B 89 6903 7556 6199 -479 -19 385 C ATOM 2258 C CYS B 89 -29.962 7.639 15.001 1.00 56.68 C ANISOU 2258 C CYS B 89 7048 7917 6569 -410 32 291 C ATOM 2259 O CYS B 89 -29.055 8.189 15.626 1.00 54.01 O ANISOU 2259 O CYS B 89 6736 7563 6223 -366 33 258 O ATOM 2260 CB CYS B 89 -29.918 5.209 15.644 1.00 57.10 C ANISOU 2260 CB CYS B 89 7393 7916 6388 -603 32 412 C ATOM 2261 SG CYS B 89 -31.575 5.163 16.351 1.00 63.57 S ANISOU 2261 SG CYS B 89 8110 8887 7156 -788 147 326 S ATOM 2262 N GLY B 90 -31.125 8.223 14.689 1.00 53.09 N ANISOU 2262 N GLY B 90 6444 7555 6174 -397 83 244 N ATOM 2263 CA GLY B 90 -31.513 9.563 15.109 1.00 53.12 C ANISOU 2263 CA GLY B 90 6334 7602 6245 -307 169 161 C ATOM 2264 C GLY B 90 -32.901 9.584 15.715 1.00 58.99 C ANISOU 2264 C GLY B 90 6950 8517 6947 -374 252 103 C ATOM 2265 O GLY B 90 -33.769 8.790 15.329 1.00 56.82 O ANISOU 2265 O GLY B 90 6609 8359 6620 -469 236 116 O ATOM 2266 N VAL B 91 -33.121 10.506 16.671 1.00 58.43 N ANISOU 2266 N VAL B 91 6837 8478 6888 -342 355 19 N ATOM 2267 CA VAL B 91 -34.397 10.694 17.389 1.00 60.10 C ANISOU 2267 CA VAL B 91 6913 8863 7059 -386 457 -55 C ATOM 2268 C VAL B 91 -34.394 12.032 18.160 1.00 65.77 C ANISOU 2268 C VAL B 91 7615 9548 7826 -284 588 -147 C ATOM 2269 O VAL B 91 -33.333 12.558 18.514 1.00 64.69 O ANISOU 2269 O VAL B 91 7599 9271 7709 -278 606 -177 O ATOM 2270 CB VAL B 91 -34.724 9.477 18.329 1.00 64.04 C ANISOU 2270 CB VAL B 91 7470 9449 7414 -626 465 -62 C ATOM 2271 CG1 VAL B 91 -33.752 9.385 19.501 1.00 63.28 C ANISOU 2271 CG1 VAL B 91 7534 9268 7241 -696 475 -72 C ATOM 2272 CG2 VAL B 91 -36.176 9.491 18.811 1.00 65.52 C ANISOU 2272 CG2 VAL B 91 7485 9857 7552 -705 565 -144 C ATOM 2273 N TRP B 92 -35.582 12.555 18.436 1.00 64.22 N ANISOU 2273 N TRP B 92 7268 9497 7634 -219 694 -206 N ATOM 2274 CA TRP B 92 -35.738 13.767 19.215 1.00 65.07 C ANISOU 2274 CA TRP B 92 7380 9567 7778 -124 854 -302 C ATOM 2275 C TRP B 92 -35.739 13.366 20.680 1.00 67.56 C ANISOU 2275 C TRP B 92 7737 9948 7983 -339 905 -382 C ATOM 2276 O TRP B 92 -36.393 12.404 21.058 1.00 66.90 O ANISOU 2276 O TRP B 92 7593 10019 7806 -494 879 -377 O ATOM 2277 CB TRP B 92 -37.054 14.480 18.833 1.00 65.79 C ANISOU 2277 CB TRP B 92 7282 9809 7906 91 952 -317 C ATOM 2278 CG TRP B 92 -37.329 15.733 19.605 1.00 68.60 C ANISOU 2278 CG TRP B 92 7663 10106 8296 219 1153 -413 C ATOM 2279 CD1 TRP B 92 -38.096 15.852 20.725 1.00 73.03 C ANISOU 2279 CD1 TRP B 92 8144 10806 8797 149 1272 -514 C ATOM 2280 CD2 TRP B 92 -36.846 17.049 19.306 1.00 69.36 C ANISOU 2280 CD2 TRP B 92 7901 9967 8486 430 1287 -426 C ATOM 2281 NE1 TRP B 92 -38.137 17.165 21.135 1.00 73.92 N ANISOU 2281 NE1 TRP B 92 8335 10786 8965 317 1472 -589 N ATOM 2282 CE2 TRP B 92 -37.369 17.921 20.288 1.00 75.15 C ANISOU 2282 CE2 TRP B 92 8644 10697 9212 485 1495 -538 C ATOM 2283 CE3 TRP B 92 -36.020 17.580 18.301 1.00 70.21 C ANISOU 2283 CE3 TRP B 92 8151 9852 8675 565 1275 -359 C ATOM 2284 CZ2 TRP B 92 -37.120 19.298 20.276 1.00 75.88 C ANISOU 2284 CZ2 TRP B 92 8907 10549 9376 674 1708 -586 C ATOM 2285 CZ3 TRP B 92 -35.778 18.949 18.289 1.00 73.07 C ANISOU 2285 CZ3 TRP B 92 8680 9981 9103 742 1486 -404 C ATOM 2286 CH2 TRP B 92 -36.314 19.788 19.276 1.00 75.59 C ANISOU 2286 CH2 TRP B 92 9030 10277 9412 792 1707 -518 C ATOM 2287 N ASP B 93 -34.985 14.081 21.495 1.00 64.32 N ANISOU 2287 N ASP B 93 7443 9427 7569 -369 987 -463 N ATOM 2288 CA ASP B 93 -34.952 13.865 22.933 1.00 64.71 C ANISOU 2288 CA ASP B 93 7535 9555 7498 -554 1046 -549 C ATOM 2289 C ASP B 93 -35.914 14.920 23.517 1.00 72.30 C ANISOU 2289 C ASP B 93 8414 10565 8492 -469 1245 -665 C ATOM 2290 O ASP B 93 -35.721 16.113 23.293 1.00 72.22 O ANISOU 2290 O ASP B 93 8453 10414 8574 -318 1367 -720 O ATOM 2291 CB ASP B 93 -33.512 14.003 23.486 1.00 64.45 C ANISOU 2291 CB ASP B 93 7651 9430 7405 -650 1014 -588 C ATOM 2292 CG ASP B 93 -33.330 13.507 24.910 1.00 69.02 C ANISOU 2292 CG ASP B 93 8280 10132 7811 -840 1026 -642 C ATOM 2293 OD1 ASP B 93 -34.135 13.890 25.781 1.00 70.74 O ANISOU 2293 OD1 ASP B 93 8452 10432 7993 -891 1162 -738 O ATOM 2294 OD2 ASP B 93 -32.374 12.758 25.156 1.00 72.04 O ANISOU 2294 OD2 ASP B 93 8749 10541 8082 -918 905 -585 O ATOM 2295 N SER B 94 -36.998 14.475 24.177 1.00 71.26 N ANISOU 2295 N SER B 94 8166 10624 8284 -554 1296 -699 N ATOM 2296 CA SER B 94 -37.989 15.379 24.778 1.00 73.14 C ANISOU 2296 CA SER B 94 8306 10943 8540 -464 1490 -811 C ATOM 2297 C SER B 94 -37.460 16.021 26.063 1.00 79.05 C ANISOU 2297 C SER B 94 9187 11619 9230 -580 1624 -944 C ATOM 2298 O SER B 94 -37.949 17.087 26.445 1.00 80.78 O ANISOU 2298 O SER B 94 9394 11806 9491 -467 1819 -1049 O ATOM 2299 CB SER B 94 -39.307 14.659 25.033 1.00 76.78 C ANISOU 2299 CB SER B 94 8575 11671 8926 -542 1506 -823 C ATOM 2300 OG SER B 94 -39.879 14.195 23.821 1.00 82.14 O ANISOU 2300 OG SER B 94 9102 12465 9644 -443 1404 -735 O ATOM 2301 N SER B 95 -36.437 15.399 26.704 1.00 75.10 N ANISOU 2301 N SER B 95 8815 11103 8618 -789 1528 -942 N ATOM 2302 CA SER B 95 -35.809 15.909 27.936 1.00 75.57 C ANISOU 2302 CA SER B 95 8983 11150 8578 -934 1627 -1077 C ATOM 2303 C SER B 95 -34.839 17.030 27.617 1.00 77.85 C ANISOU 2303 C SER B 95 9384 11249 8947 -870 1701 -1157 C ATOM 2304 O SER B 95 -34.864 18.058 28.281 1.00 78.83 O ANISOU 2304 O SER B 95 9568 11313 9070 -894 1900 -1313 O ATOM 2305 CB SER B 95 -35.100 14.795 28.706 1.00 78.83 C ANISOU 2305 CB SER B 95 9474 11672 8805 -1141 1489 -1030 C ATOM 2306 OG SER B 95 -34.573 15.251 29.943 1.00 92.60 O ANISOU 2306 OG SER B 95 11292 13474 10418 -1285 1575 -1168 O ATOM 2307 N LEU B 96 -33.988 16.837 26.600 1.00 72.28 N ANISOU 2307 N LEU B 96 8720 10438 8304 -810 1565 -1064 N ATOM 2308 CA LEU B 96 -33.031 17.853 26.179 1.00 71.27 C ANISOU 2308 CA LEU B 96 8707 10125 8248 -779 1646 -1144 C ATOM 2309 C LEU B 96 -33.692 18.884 25.258 1.00 74.99 C ANISOU 2309 C LEU B 96 9200 10406 8888 -528 1805 -1133 C ATOM 2310 O LEU B 96 -33.129 19.962 25.086 1.00 74.76 O ANISOU 2310 O LEU B 96 9314 10179 8914 -506 1968 -1232 O ATOM 2311 CB LEU B 96 -31.820 17.216 25.460 1.00 69.47 C ANISOU 2311 CB LEU B 96 8510 9879 8005 -815 1444 -1053 C ATOM 2312 CG LEU B 96 -30.940 16.228 26.247 1.00 73.49 C ANISOU 2312 CG LEU B 96 9019 10577 8326 -996 1281 -1038 C ATOM 2313 CD1 LEU B 96 -29.973 15.521 25.313 1.00 71.73 C ANISOU 2313 CD1 LEU B 96 8807 10335 8113 -950 1085 -911 C ATOM 2314 CD2 LEU B 96 -30.148 16.922 27.366 1.00 76.27 C ANISOU 2314 CD2 LEU B 96 9419 11013 8545 -1184 1386 -1237 C ATOM 2315 N SER B 97 -34.884 18.564 24.678 1.00 71.73 N ANISOU 2315 N SER B 97 8650 10067 8536 -338 1773 -1019 N ATOM 2316 CA SER B 97 -35.602 19.387 23.683 1.00 73.05 C ANISOU 2316 CA SER B 97 8804 10119 8834 -28 1887 -962 C ATOM 2317 C SER B 97 -34.686 19.711 22.450 1.00 77.08 C ANISOU 2317 C SER B 97 9436 10416 9434 74 1836 -885 C ATOM 2318 O SER B 97 -34.568 20.861 22.006 1.00 78.85 O ANISOU 2318 O SER B 97 9811 10412 9738 240 2027 -915 O ATOM 2319 CB SER B 97 -36.253 20.623 24.302 1.00 78.00 C ANISOU 2319 CB SER B 97 9496 10654 9484 97 2179 -1088 C ATOM 2320 OG SER B 97 -37.629 20.383 24.548 1.00 86.35 O ANISOU 2320 OG SER B 97 10356 11932 10522 220 2206 -1065 O ATOM 2321 N GLY B 98 -34.057 18.650 21.939 1.00 70.66 N ANISOU 2321 N GLY B 98 8578 9673 8597 -32 1597 -785 N ATOM 2322 CA GLY B 98 -33.157 18.647 20.791 1.00 69.10 C ANISOU 2322 CA GLY B 98 8462 9328 8464 23 1504 -704 C ATOM 2323 C GLY B 98 -33.064 17.274 20.142 1.00 70.68 C ANISOU 2323 C GLY B 98 8554 9663 8637 -20 1244 -561 C ATOM 2324 O GLY B 98 -33.521 16.290 20.714 1.00 68.67 O ANISOU 2324 O GLY B 98 8199 9594 8297 -140 1147 -539 O ATOM 2325 N GLY B 99 -32.485 17.210 18.944 1.00 67.36 N ANISOU 2325 N GLY B 99 8179 9133 8283 70 1155 -468 N ATOM 2326 CA GLY B 99 -32.284 15.963 18.212 1.00 65.33 C ANISOU 2326 CA GLY B 99 7857 8961 8004 30 932 -341 C ATOM 2327 C GLY B 99 -30.960 15.316 18.565 1.00 67.85 C ANISOU 2327 C GLY B 99 8254 9273 8253 -159 819 -357 C ATOM 2328 O GLY B 99 -29.917 15.976 18.528 1.00 67.85 O ANISOU 2328 O GLY B 99 8354 9155 8270 -196 874 -430 O ATOM 2329 N VAL B 100 -31.002 14.019 18.925 1.00 62.79 N ANISOU 2329 N VAL B 100 7574 8770 7514 -276 678 -295 N ATOM 2330 CA VAL B 100 -29.849 13.199 19.331 1.00 60.92 C ANISOU 2330 CA VAL B 100 7403 8572 7172 -402 559 -277 C ATOM 2331 C VAL B 100 -29.597 12.042 18.354 1.00 65.43 C ANISOU 2331 C VAL B 100 7994 9127 7741 -371 398 -132 C ATOM 2332 O VAL B 100 -30.524 11.555 17.701 1.00 65.61 O ANISOU 2332 O VAL B 100 7964 9169 7797 -334 369 -59 O ATOM 2333 CB VAL B 100 -29.945 12.705 20.811 1.00 64.11 C ANISOU 2333 CB VAL B 100 7814 9126 7419 -550 571 -324 C ATOM 2334 CG1 VAL B 100 -29.998 13.876 21.793 1.00 64.72 C ANISOU 2334 CG1 VAL B 100 7888 9219 7483 -607 737 -491 C ATOM 2335 CG2 VAL B 100 -31.134 11.763 21.021 1.00 63.90 C ANISOU 2335 CG2 VAL B 100 7747 9190 7342 -594 555 -254 C ATOM 2336 N PHE B 101 -28.338 11.599 18.279 1.00 62.65 N ANISOU 2336 N PHE B 101 7707 8763 7333 -393 303 -105 N ATOM 2337 CA PHE B 101 -27.866 10.521 17.415 1.00 61.66 C ANISOU 2337 CA PHE B 101 7633 8600 7194 -355 169 23 C ATOM 2338 C PHE B 101 -26.979 9.541 18.160 1.00 66.28 C ANISOU 2338 C PHE B 101 8296 9272 7616 -395 86 71 C ATOM 2339 O PHE B 101 -26.444 9.853 19.239 1.00 67.12 O ANISOU 2339 O PHE B 101 8391 9495 7617 -446 109 -8 O ATOM 2340 CB PHE B 101 -27.092 11.102 16.209 1.00 62.95 C ANISOU 2340 CB PHE B 101 7802 8645 7471 -263 147 26 C ATOM 2341 CG PHE B 101 -27.958 11.821 15.196 1.00 64.72 C ANISOU 2341 CG PHE B 101 7984 8774 7832 -162 207 38 C ATOM 2342 CD1 PHE B 101 -28.400 13.121 15.428 1.00 69.31 C ANISOU 2342 CD1 PHE B 101 8544 9309 8480 -115 356 -54 C ATOM 2343 CD2 PHE B 101 -28.350 11.191 14.023 1.00 65.56 C ANISOU 2343 CD2 PHE B 101 8081 8848 7979 -99 127 144 C ATOM 2344 CE1 PHE B 101 -29.218 13.777 14.504 1.00 70.69 C ANISOU 2344 CE1 PHE B 101 8690 9416 8754 40 416 -17 C ATOM 2345 CE2 PHE B 101 -29.158 11.851 13.098 1.00 68.83 C ANISOU 2345 CE2 PHE B 101 8437 9231 8485 25 171 166 C ATOM 2346 CZ PHE B 101 -29.592 13.139 13.346 1.00 68.51 C ANISOU 2346 CZ PHE B 101 8375 9153 8503 116 312 97 C ATOM 2347 N GLY B 102 -26.841 8.354 17.576 1.00 60.87 N ANISOU 2347 N GLY B 102 7698 8538 6893 -360 0 200 N ATOM 2348 CA GLY B 102 -25.924 7.327 18.034 1.00 60.84 C ANISOU 2348 CA GLY B 102 7803 8584 6729 -322 -76 288 C ATOM 2349 C GLY B 102 -24.567 7.639 17.433 1.00 65.30 C ANISOU 2349 C GLY B 102 8332 9162 7316 -225 -148 274 C ATOM 2350 O GLY B 102 -24.464 8.470 16.527 1.00 63.93 O ANISOU 2350 O GLY B 102 8090 8911 7290 -212 -132 216 O ATOM 2351 N GLY B 103 -23.532 6.976 17.924 1.00 64.44 N ANISOU 2351 N GLY B 103 8271 9168 7047 -145 -219 329 N ATOM 2352 CA GLY B 103 -22.166 7.180 17.449 1.00 64.20 C ANISOU 2352 CA GLY B 103 8174 9218 7002 -53 -290 304 C ATOM 2353 C GLY B 103 -21.808 6.590 16.094 1.00 65.95 C ANISOU 2353 C GLY B 103 8459 9289 7309 48 -343 402 C ATOM 2354 O GLY B 103 -20.712 6.851 15.590 1.00 65.36 O ANISOU 2354 O GLY B 103 8311 9281 7242 112 -389 364 O ATOM 2355 N GLY B 104 -22.707 5.796 15.510 1.00 61.51 N ANISOU 2355 N GLY B 104 8025 8548 6798 40 -327 508 N ATOM 2356 CA GLY B 104 -22.497 5.176 14.200 1.00 59.37 C ANISOU 2356 CA GLY B 104 7835 8124 6600 109 -362 592 C ATOM 2357 C GLY B 104 -21.943 3.765 14.230 1.00 62.95 C ANISOU 2357 C GLY B 104 8472 8536 6909 240 -392 738 C ATOM 2358 O GLY B 104 -21.144 3.415 15.109 1.00 62.38 O ANISOU 2358 O GLY B 104 8421 8612 6669 358 -424 778 O ATOM 2359 N THR B 105 -22.378 2.939 13.258 1.00 57.94 N ANISOU 2359 N THR B 105 7984 7708 6322 229 -369 819 N ATOM 2360 CA THR B 105 -21.924 1.565 13.096 1.00 58.33 C ANISOU 2360 CA THR B 105 8268 7645 6248 353 -355 960 C ATOM 2361 C THR B 105 -21.350 1.391 11.691 1.00 63.13 C ANISOU 2361 C THR B 105 8892 8144 6953 424 -387 978 C ATOM 2362 O THR B 105 -22.049 1.613 10.702 1.00 60.42 O ANISOU 2362 O THR B 105 8522 7694 6742 298 -371 936 O ATOM 2363 CB THR B 105 -23.056 0.562 13.367 1.00 63.96 C ANISOU 2363 CB THR B 105 9209 8201 6890 222 -246 1024 C ATOM 2364 OG1 THR B 105 -23.672 0.847 14.627 1.00 60.35 O ANISOU 2364 OG1 THR B 105 8718 7854 6358 132 -208 991 O ATOM 2365 CG2 THR B 105 -22.574 -0.904 13.326 1.00 61.36 C ANISOU 2365 CG2 THR B 105 9202 7704 6407 360 -180 1179 C ATOM 2366 N LYS B 106 -20.086 0.969 11.600 1.00 62.98 N ANISOU 2366 N LYS B 106 8907 8175 6848 637 -431 1042 N ATOM 2367 CA LYS B 106 -19.490 0.737 10.293 1.00 63.12 C ANISOU 2367 CA LYS B 106 8951 8090 6944 712 -449 1059 C ATOM 2368 C LYS B 106 -19.879 -0.683 9.851 1.00 68.98 C ANISOU 2368 C LYS B 106 10008 8581 7620 727 -356 1179 C ATOM 2369 O LYS B 106 -19.572 -1.640 10.553 1.00 70.22 O ANISOU 2369 O LYS B 106 10374 8698 7607 876 -303 1297 O ATOM 2370 CB LYS B 106 -17.955 0.925 10.347 1.00 65.93 C ANISOU 2370 CB LYS B 106 9179 8641 7229 932 -524 1056 C ATOM 2371 CG LYS B 106 -17.281 0.990 8.971 1.00 74.26 C ANISOU 2371 CG LYS B 106 10197 9628 8389 981 -545 1034 C ATOM 2372 CD LYS B 106 -16.143 -0.015 8.860 1.00 81.33 C ANISOU 2372 CD LYS B 106 11202 10554 9146 1262 -549 1144 C ATOM 2373 CE LYS B 106 -14.863 0.595 8.334 0.50 86.19 C ANISOU 2373 CE LYS B 106 11588 11377 9783 1362 -616 1058 C ATOM 2374 NZ LYS B 106 -14.104 1.306 9.396 0.50 92.03 N ANISOU 2374 NZ LYS B 106 12079 12480 10407 1416 -683 974 N ATOM 2375 N VAL B 107 -20.575 -0.814 8.715 1.00 67.10 N ANISOU 2375 N VAL B 107 9820 8178 7496 569 -319 1146 N ATOM 2376 CA VAL B 107 -20.974 -2.136 8.195 1.00 68.70 C ANISOU 2376 CA VAL B 107 10334 8134 7633 522 -201 1222 C ATOM 2377 C VAL B 107 -19.964 -2.632 7.161 1.00 73.05 C ANISOU 2377 C VAL B 107 10977 8585 8193 692 -203 1270 C ATOM 2378 O VAL B 107 -19.832 -2.031 6.094 1.00 70.99 O ANISOU 2378 O VAL B 107 10563 8347 8064 642 -262 1197 O ATOM 2379 CB VAL B 107 -22.446 -2.208 7.691 1.00 71.51 C ANISOU 2379 CB VAL B 107 10712 8407 8051 212 -134 1144 C ATOM 2380 CG1 VAL B 107 -22.720 -3.513 6.934 1.00 72.34 C ANISOU 2380 CG1 VAL B 107 11132 8264 8089 118 4 1182 C ATOM 2381 CG2 VAL B 107 -23.414 -2.068 8.855 1.00 71.22 C ANISOU 2381 CG2 VAL B 107 10654 8448 7959 68 -91 1118 C ATOM 2382 N THR B 108 -19.256 -3.728 7.488 1.00 71.84 N ANISOU 2382 N THR B 108 11086 8321 7888 913 -126 1399 N ATOM 2383 CA THR B 108 -18.242 -4.330 6.617 1.00 72.53 C ANISOU 2383 CA THR B 108 11291 8310 7957 1122 -103 1458 C ATOM 2384 C THR B 108 -18.774 -5.588 5.905 1.00 76.87 C ANISOU 2384 C THR B 108 12222 8523 8460 1020 77 1503 C ATOM 2385 O THR B 108 -19.383 -6.439 6.532 1.00 77.87 O ANISOU 2385 O THR B 108 12640 8480 8465 956 220 1566 O ATOM 2386 CB THR B 108 -16.966 -4.648 7.421 1.00 86.34 C ANISOU 2386 CB THR B 108 13054 10204 9546 1503 -134 1574 C ATOM 2387 OG1 THR B 108 -16.774 -3.673 8.452 1.00 90.32 O ANISOU 2387 OG1 THR B 108 13269 11016 10031 1522 -256 1524 O ATOM 2388 CG2 THR B 108 -15.726 -4.753 6.539 1.00 86.10 C ANISOU 2388 CG2 THR B 108 12962 10221 9530 1740 -169 1587 C ATOM 2389 N VAL B 109 -18.551 -5.695 4.601 1.00 73.96 N ANISOU 2389 N VAL B 109 11868 8056 8179 979 88 1457 N ATOM 2390 CA VAL B 109 -18.942 -6.883 3.840 1.00 75.00 C ANISOU 2390 CA VAL B 109 12367 7873 8257 865 274 1474 C ATOM 2391 C VAL B 109 -17.659 -7.714 3.790 1.00 80.05 C ANISOU 2391 C VAL B 109 13229 8398 8787 1247 347 1608 C ATOM 2392 O VAL B 109 -16.660 -7.257 3.236 1.00 78.74 O ANISOU 2392 O VAL B 109 12864 8370 8684 1438 242 1597 O ATOM 2393 CB VAL B 109 -19.531 -6.566 2.431 1.00 77.44 C ANISOU 2393 CB VAL B 109 12571 8157 8696 584 255 1338 C ATOM 2394 CG1 VAL B 109 -20.337 -7.743 1.891 1.00 78.72 C ANISOU 2394 CG1 VAL B 109 13098 8036 8776 332 468 1306 C ATOM 2395 CG2 VAL B 109 -20.396 -5.309 2.455 1.00 75.13 C ANISOU 2395 CG2 VAL B 109 11915 8104 8526 364 109 1224 C ATOM 2396 N LEU B 110 -17.652 -8.868 4.491 1.00 79.53 N ANISOU 2396 N LEU B 110 13565 8110 8544 1389 530 1742 N ATOM 2397 CA LEU B 110 -16.499 -9.763 4.608 1.00 81.83 C ANISOU 2397 CA LEU B 110 14116 8285 8689 1820 629 1904 C ATOM 2398 C LEU B 110 -16.380 -10.653 3.393 1.00 88.16 C ANISOU 2398 C LEU B 110 15231 8769 9497 1788 808 1892 C ATOM 2399 O LEU B 110 -17.396 -10.958 2.763 1.00 87.81 O ANISOU 2399 O LEU B 110 15346 8520 9497 1398 927 1783 O ATOM 2400 CB LEU B 110 -16.635 -10.664 5.843 1.00 84.78 C ANISOU 2400 CB LEU B 110 14860 8506 8847 1998 789 2070 C ATOM 2401 CG LEU B 110 -16.698 -10.010 7.210 1.00 89.09 C ANISOU 2401 CG LEU B 110 15178 9344 9330 2072 650 2109 C ATOM 2402 CD1 LEU B 110 -17.235 -10.983 8.223 1.00 91.36 C ANISOU 2402 CD1 LEU B 110 15907 9390 9415 2099 860 2244 C ATOM 2403 CD2 LEU B 110 -15.337 -9.479 7.645 1.00 92.70 C ANISOU 2403 CD2 LEU B 110 15321 10171 9727 2501 462 2177 C ATOM 2404 N GLY B 111 -15.155 -11.107 3.114 1.00 87.27 N ANISOU 2404 N GLY B 111 15207 8635 9315 2197 840 1997 N ATOM 2405 CA GLY B 111 -14.844 -12.017 2.012 1.00 88.99 C ANISOU 2405 CA GLY B 111 15752 8542 9518 2245 1031 2003 C ATOM 2406 C GLY B 111 -15.466 -11.564 0.713 1.00 90.57 C ANISOU 2406 C GLY B 111 15801 8719 9893 1825 990 1808 C ATOM 2407 O GLY B 111 -16.179 -12.316 0.045 1.00 91.34 O ANISOU 2407 O GLY B 111 16224 8509 9971 1542 1191 1741 O ATOM 2408 N GLN B 112 -15.269 -10.291 0.420 1.00 85.24 N ANISOU 2408 N GLN B 112 14630 8385 9370 1760 737 1709 N ATOM 2409 CA GLN B 112 -15.796 -9.618 -0.741 1.00 83.00 C ANISOU 2409 CA GLN B 112 14130 8161 9244 1417 652 1542 C ATOM 2410 C GLN B 112 -15.237 -10.248 -2.017 1.00 87.36 C ANISOU 2410 C GLN B 112 14874 8519 9801 1471 772 1518 C ATOM 2411 O GLN B 112 -14.007 -10.352 -2.150 1.00 87.51 O ANISOU 2411 O GLN B 112 14859 8596 9796 1839 758 1591 O ATOM 2412 CB GLN B 112 -15.467 -8.126 -0.659 1.00 81.61 C ANISOU 2412 CB GLN B 112 13437 8366 9203 1431 388 1476 C ATOM 2413 CG GLN B 112 -16.382 -7.269 -1.512 1.00 86.56 C ANISOU 2413 CG GLN B 112 13840 9077 9971 1057 294 1327 C ATOM 2414 CD GLN B 112 -16.402 -5.821 -1.078 1.00 98.79 C ANISOU 2414 CD GLN B 112 14969 10940 11627 1031 88 1275 C ATOM 2415 OE1 GLN B 112 -16.126 -4.923 -1.868 1.00 96.62 O ANISOU 2415 OE1 GLN B 112 14450 10799 11463 987 -17 1200 O ATOM 2416 NE2 GLN B 112 -16.770 -5.549 0.171 1.00 84.07 N ANISOU 2416 NE2 GLN B 112 13036 9180 9725 1040 47 1309 N ATOM 2417 N PRO B 113 -16.136 -10.718 -2.928 1.00 83.21 N ANISOU 2417 N PRO B 113 14549 7781 9284 1104 904 1407 N ATOM 2418 CA PRO B 113 -15.662 -11.349 -4.174 1.00 84.27 C ANISOU 2418 CA PRO B 113 14889 7718 9412 1118 1037 1366 C ATOM 2419 C PRO B 113 -14.920 -10.391 -5.099 1.00 84.28 C ANISOU 2419 C PRO B 113 14516 7963 9545 1192 849 1303 C ATOM 2420 O PRO B 113 -15.339 -9.247 -5.261 1.00 81.90 O ANISOU 2420 O PRO B 113 13844 7918 9355 1009 651 1222 O ATOM 2421 CB PRO B 113 -16.955 -11.829 -4.846 1.00 86.67 C ANISOU 2421 CB PRO B 113 15396 7847 9688 625 1180 1222 C ATOM 2422 CG PRO B 113 -18.036 -10.985 -4.266 1.00 88.70 C ANISOU 2422 CG PRO B 113 15359 8346 9996 351 1023 1157 C ATOM 2423 CD PRO B 113 -17.614 -10.692 -2.863 1.00 83.66 C ANISOU 2423 CD PRO B 113 14633 7815 9341 650 939 1297 C ATOM 2424 N LYS B 114 -13.843 -10.872 -5.738 1.00 80.35 N ANISOU 2424 N LYS B 114 14139 7367 9023 1458 934 1339 N ATOM 2425 CA LYS B 114 -13.091 -10.084 -6.721 1.00 77.03 C ANISOU 2425 CA LYS B 114 13414 7144 8710 1509 799 1269 C ATOM 2426 C LYS B 114 -14.029 -9.752 -7.883 1.00 77.29 C ANISOU 2426 C LYS B 114 13394 7164 8810 1077 776 1118 C ATOM 2427 O LYS B 114 -14.867 -10.577 -8.258 1.00 76.63 O ANISOU 2427 O LYS B 114 13614 6848 8655 811 944 1061 O ATOM 2428 CB LYS B 114 -11.821 -10.821 -7.223 1.00 80.17 C ANISOU 2428 CB LYS B 114 13987 7426 9049 1871 931 1328 C ATOM 2429 CG LYS B 114 -10.886 -11.375 -6.125 1.00 97.00 C ANISOU 2429 CG LYS B 114 16222 9575 11060 2362 987 1497 C ATOM 2430 CD LYS B 114 -10.194 -10.329 -5.229 1.00 99.38 C ANISOU 2430 CD LYS B 114 16069 10303 11389 2585 750 1530 C ATOM 2431 CE LYS B 114 -10.774 -10.279 -3.829 1.00101.05 C ANISOU 2431 CE LYS B 114 16290 10568 11536 2593 704 1614 C ATOM 2432 NZ LYS B 114 -10.179 -9.195 -2.998 1.00 99.97 N ANISOU 2432 NZ LYS B 114 15700 10862 11420 2739 478 1610 N ATOM 2433 N ALA B 115 -13.955 -8.514 -8.383 1.00 71.38 N ANISOU 2433 N ALA B 115 12261 6681 8177 993 576 1050 N ATOM 2434 CA ALA B 115 -14.801 -8.099 -9.493 1.00 70.36 C ANISOU 2434 CA ALA B 115 12051 6596 8089 640 534 929 C ATOM 2435 C ALA B 115 -13.911 -7.570 -10.616 1.00 72.01 C ANISOU 2435 C ALA B 115 12106 6893 8360 723 480 886 C ATOM 2436 O ALA B 115 -13.172 -6.606 -10.418 1.00 70.18 O ANISOU 2436 O ALA B 115 11589 6870 8209 888 345 904 O ATOM 2437 CB ALA B 115 -15.805 -7.047 -9.032 1.00 69.44 C ANISOU 2437 CB ALA B 115 11648 6704 8031 441 363 898 C ATOM 2438 N ALA B 116 -13.913 -8.275 -11.754 1.00 67.96 N ANISOU 2438 N ALA B 116 11814 6212 7797 606 614 821 N ATOM 2439 CA ALA B 116 -13.110 -7.928 -12.916 1.00 66.00 C ANISOU 2439 CA ALA B 116 11473 6016 7588 660 597 773 C ATOM 2440 C ALA B 116 -13.598 -6.586 -13.514 1.00 66.70 C ANISOU 2440 C ALA B 116 11241 6351 7752 467 411 716 C ATOM 2441 O ALA B 116 -14.812 -6.346 -13.571 1.00 65.56 O ANISOU 2441 O ALA B 116 11052 6274 7583 205 354 676 O ATOM 2442 CB ALA B 116 -13.202 -9.025 -13.956 1.00 68.12 C ANISOU 2442 CB ALA B 116 12076 6040 7767 527 797 703 C ATOM 2443 N PRO B 117 -12.674 -5.698 -13.953 1.00 60.66 N ANISOU 2443 N PRO B 117 10256 5730 7060 600 329 711 N ATOM 2444 CA PRO B 117 -13.121 -4.416 -14.511 1.00 57.59 C ANISOU 2444 CA PRO B 117 9623 5532 6727 447 187 676 C ATOM 2445 C PRO B 117 -13.832 -4.558 -15.838 1.00 58.77 C ANISOU 2445 C PRO B 117 9858 5663 6808 200 209 607 C ATOM 2446 O PRO B 117 -13.522 -5.441 -16.633 1.00 56.16 O ANISOU 2446 O PRO B 117 9737 5187 6414 164 338 560 O ATOM 2447 CB PRO B 117 -11.826 -3.623 -14.667 1.00 58.62 C ANISOU 2447 CB PRO B 117 9569 5775 6930 637 155 674 C ATOM 2448 CG PRO B 117 -10.764 -4.620 -14.777 1.00 65.84 C ANISOU 2448 CG PRO B 117 10639 6572 7806 840 287 676 C ATOM 2449 CD PRO B 117 -11.197 -5.810 -13.967 1.00 62.68 C ANISOU 2449 CD PRO B 117 10480 5998 7337 895 378 731 C ATOM 2450 N SER B 118 -14.816 -3.682 -16.058 1.00 55.88 N ANISOU 2450 N SER B 118 9328 5463 6440 40 88 600 N ATOM 2451 CA SER B 118 -15.495 -3.566 -17.330 1.00 56.41 C ANISOU 2451 CA SER B 118 9403 5609 6420 -166 70 544 C ATOM 2452 C SER B 118 -14.588 -2.544 -18.057 1.00 57.94 C ANISOU 2452 C SER B 118 9474 5867 6673 -45 31 562 C ATOM 2453 O SER B 118 -14.176 -1.565 -17.441 1.00 56.90 O ANISOU 2453 O SER B 118 9176 5806 6637 90 -34 610 O ATOM 2454 CB SER B 118 -16.910 -3.043 -17.119 1.00 62.21 C ANISOU 2454 CB SER B 118 9991 6538 7107 -323 -44 547 C ATOM 2455 OG SER B 118 -17.473 -2.530 -18.313 1.00 75.66 O ANISOU 2455 OG SER B 118 11618 8410 8720 -445 -106 520 O ATOM 2456 N VAL B 119 -14.144 -2.830 -19.279 1.00 54.87 N ANISOU 2456 N VAL B 119 9189 5431 6227 -96 101 512 N ATOM 2457 CA VAL B 119 -13.213 -1.897 -19.959 1.00 53.04 C ANISOU 2457 CA VAL B 119 8865 5244 6044 2 93 521 C ATOM 2458 C VAL B 119 -13.808 -1.397 -21.257 1.00 54.52 C ANISOU 2458 C VAL B 119 9046 5539 6128 -142 53 509 C ATOM 2459 O VAL B 119 -14.091 -2.191 -22.143 1.00 55.11 O ANISOU 2459 O VAL B 119 9260 5588 6090 -286 111 446 O ATOM 2460 CB VAL B 119 -11.789 -2.511 -20.116 1.00 57.05 C ANISOU 2460 CB VAL B 119 9464 5623 6588 149 221 484 C ATOM 2461 CG1 VAL B 119 -10.859 -1.618 -20.944 1.00 55.61 C ANISOU 2461 CG1 VAL B 119 9193 5500 6435 195 238 464 C ATOM 2462 CG2 VAL B 119 -11.175 -2.809 -18.742 1.00 56.52 C ANISOU 2462 CG2 VAL B 119 9354 5523 6600 350 235 518 C ATOM 2463 N THR B 120 -14.017 -0.078 -21.365 1.00 50.48 N ANISOU 2463 N THR B 120 8391 5151 5638 -97 -32 573 N ATOM 2464 CA THR B 120 -14.621 0.553 -22.562 1.00 49.80 C ANISOU 2464 CA THR B 120 8296 5197 5430 -174 -79 597 C ATOM 2465 C THR B 120 -13.666 1.605 -23.128 1.00 51.38 C ANISOU 2465 C THR B 120 8488 5363 5673 -77 -31 628 C ATOM 2466 O THR B 120 -13.441 2.625 -22.496 1.00 49.82 O ANISOU 2466 O THR B 120 8202 5164 5565 25 -44 679 O ATOM 2467 CB THR B 120 -16.003 1.149 -22.203 1.00 56.67 C ANISOU 2467 CB THR B 120 9036 6256 6240 -192 -207 663 C ATOM 2468 OG1 THR B 120 -16.740 0.211 -21.401 1.00 57.42 O ANISOU 2468 OG1 THR B 120 9126 6368 6322 -294 -227 617 O ATOM 2469 CG2 THR B 120 -16.813 1.609 -23.447 1.00 54.74 C ANISOU 2469 CG2 THR B 120 8772 6214 5814 -246 -269 696 C ATOM 2470 N LEU B 121 -13.140 1.377 -24.338 1.00 49.90 N ANISOU 2470 N LEU B 121 8407 5144 5407 -133 42 586 N ATOM 2471 CA LEU B 121 -12.196 2.299 -24.979 1.00 50.45 C ANISOU 2471 CA LEU B 121 8498 5172 5499 -77 119 599 C ATOM 2472 C LEU B 121 -12.838 3.219 -26.065 1.00 52.81 C ANISOU 2472 C LEU B 121 8836 5575 5653 -91 85 683 C ATOM 2473 O LEU B 121 -13.518 2.754 -26.975 1.00 52.97 O ANISOU 2473 O LEU B 121 8909 5704 5513 -182 44 678 O ATOM 2474 CB LEU B 121 -11.028 1.451 -25.534 1.00 51.85 C ANISOU 2474 CB LEU B 121 8770 5243 5689 -101 246 497 C ATOM 2475 CG LEU B 121 -9.852 2.150 -26.225 1.00 56.05 C ANISOU 2475 CG LEU B 121 9323 5734 6240 -79 361 466 C ATOM 2476 CD1 LEU B 121 -9.157 3.083 -25.275 1.00 53.97 C ANISOU 2476 CD1 LEU B 121 8935 5464 6108 5 391 468 C ATOM 2477 CD2 LEU B 121 -8.862 1.091 -26.756 1.00 56.22 C ANISOU 2477 CD2 LEU B 121 9426 5678 6256 -90 481 358 C ATOM 2478 N PHE B 122 -12.620 4.534 -25.938 1.00 49.21 N ANISOU 2478 N PHE B 122 8368 5093 5238 4 115 759 N ATOM 2479 CA PHE B 122 -13.168 5.541 -26.834 1.00 49.78 C ANISOU 2479 CA PHE B 122 8511 5232 5169 57 108 872 C ATOM 2480 C PHE B 122 -12.089 6.206 -27.679 1.00 56.00 C ANISOU 2480 C PHE B 122 9433 5900 5944 45 264 861 C ATOM 2481 O PHE B 122 -11.070 6.633 -27.123 1.00 56.05 O ANISOU 2481 O PHE B 122 9427 5781 6088 41 376 801 O ATOM 2482 CB PHE B 122 -13.924 6.641 -26.051 1.00 50.57 C ANISOU 2482 CB PHE B 122 8553 5364 5299 195 59 989 C ATOM 2483 CG PHE B 122 -15.037 6.182 -25.144 1.00 50.55 C ANISOU 2483 CG PHE B 122 8402 5498 5307 212 -84 1003 C ATOM 2484 CD1 PHE B 122 -14.756 5.537 -23.942 1.00 51.60 C ANISOU 2484 CD1 PHE B 122 8444 5568 5593 170 -97 921 C ATOM 2485 CD2 PHE B 122 -16.360 6.450 -25.457 1.00 52.67 C ANISOU 2485 CD2 PHE B 122 8615 5979 5417 285 -199 1102 C ATOM 2486 CE1 PHE B 122 -15.779 5.115 -23.106 1.00 52.07 C ANISOU 2486 CE1 PHE B 122 8386 5743 5655 166 -209 930 C ATOM 2487 CE2 PHE B 122 -17.388 6.060 -24.600 1.00 55.11 C ANISOU 2487 CE2 PHE B 122 8769 6439 5731 281 -317 1099 C ATOM 2488 CZ PHE B 122 -17.092 5.385 -23.433 1.00 52.50 C ANISOU 2488 CZ PHE B 122 8376 6009 5562 205 -315 1009 C ATOM 2489 N PRO B 123 -12.331 6.347 -29.012 1.00 52.91 N ANISOU 2489 N PRO B 123 9164 5572 5369 29 277 913 N ATOM 2490 CA PRO B 123 -11.374 7.061 -29.872 1.00 53.37 C ANISOU 2490 CA PRO B 123 9378 5508 5391 9 444 914 C ATOM 2491 C PRO B 123 -11.594 8.595 -29.768 1.00 59.20 C ANISOU 2491 C PRO B 123 10222 6167 6104 139 519 1054 C ATOM 2492 O PRO B 123 -12.639 8.986 -29.237 1.00 57.89 O ANISOU 2492 O PRO B 123 10001 6084 5912 270 413 1164 O ATOM 2493 CB PRO B 123 -11.774 6.580 -31.289 1.00 55.74 C ANISOU 2493 CB PRO B 123 9774 5934 5471 -45 410 934 C ATOM 2494 CG PRO B 123 -13.246 6.422 -31.229 1.00 59.56 C ANISOU 2494 CG PRO B 123 10168 6643 5820 22 227 1026 C ATOM 2495 CD PRO B 123 -13.509 5.889 -29.790 1.00 55.06 C ANISOU 2495 CD PRO B 123 9428 6062 5432 16 146 967 C ATOM 2496 N PRO B 124 -10.715 9.488 -30.320 1.00 57.93 N ANISOU 2496 N PRO B 124 10239 5847 5926 111 717 1057 N ATOM 2497 CA PRO B 124 -11.040 10.932 -30.299 1.00 59.86 C ANISOU 2497 CA PRO B 124 10655 5975 6113 244 823 1206 C ATOM 2498 C PRO B 124 -12.233 11.200 -31.208 1.00 68.29 C ANISOU 2498 C PRO B 124 11820 7191 6937 424 722 1401 C ATOM 2499 O PRO B 124 -12.283 10.648 -32.306 1.00 69.18 O ANISOU 2499 O PRO B 124 11972 7422 6892 379 681 1402 O ATOM 2500 CB PRO B 124 -9.778 11.600 -30.854 1.00 61.36 C ANISOU 2500 CB PRO B 124 11035 5969 6310 116 1082 1135 C ATOM 2501 CG PRO B 124 -9.113 10.563 -31.651 1.00 65.30 C ANISOU 2501 CG PRO B 124 11489 6543 6781 -25 1073 1013 C ATOM 2502 CD PRO B 124 -9.438 9.241 -31.021 1.00 59.08 C ANISOU 2502 CD PRO B 124 10457 5907 6085 -42 875 928 C ATOM 2503 N SER B 125 -13.225 11.957 -30.734 1.00 68.51 N ANISOU 2503 N SER B 125 11858 7252 6919 636 670 1557 N ATOM 2504 CA SER B 125 -14.405 12.268 -31.558 1.00 72.07 C ANISOU 2504 CA SER B 125 12367 7909 7108 863 565 1756 C ATOM 2505 C SER B 125 -14.049 13.270 -32.645 1.00 81.12 C ANISOU 2505 C SER B 125 13840 8903 8078 963 760 1892 C ATOM 2506 O SER B 125 -13.073 14.009 -32.497 1.00 81.13 O ANISOU 2506 O SER B 125 14042 8601 8182 881 1001 1852 O ATOM 2507 CB SER B 125 -15.548 12.820 -30.709 1.00 75.70 C ANISOU 2507 CB SER B 125 12737 8463 7564 1100 469 1887 C ATOM 2508 OG SER B 125 -15.575 14.236 -30.756 1.00 80.93 O ANISOU 2508 OG SER B 125 13669 8914 8167 1316 658 2055 O ATOM 2509 N SER B 126 -14.860 13.305 -33.721 1.00 81.44 N ANISOU 2509 N SER B 126 13936 9175 7833 1134 664 2049 N ATOM 2510 CA SER B 126 -14.714 14.225 -34.853 1.00 84.31 C ANISOU 2510 CA SER B 126 14630 9438 7967 1286 830 2222 C ATOM 2511 C SER B 126 -14.550 15.684 -34.383 1.00 87.01 C ANISOU 2511 C SER B 126 15267 9441 8351 1468 1078 2360 C ATOM 2512 O SER B 126 -13.626 16.365 -34.834 1.00 87.48 O ANISOU 2512 O SER B 126 15634 9199 8404 1381 1347 2358 O ATOM 2513 CB SER B 126 -15.890 14.084 -35.825 1.00 92.06 C ANISOU 2513 CB SER B 126 15560 10810 8608 1520 641 2397 C ATOM 2514 OG SER B 126 -17.136 14.022 -35.146 1.00104.73 O ANISOU 2514 OG SER B 126 16922 12694 10175 1727 435 2475 O ATOM 2515 N GLU B 127 -15.408 16.118 -33.432 1.00 81.95 N ANISOU 2515 N GLU B 127 14534 8839 7763 1685 1008 2452 N ATOM 2516 CA GLU B 127 -15.424 17.447 -32.816 1.00 83.30 C ANISOU 2516 CA GLU B 127 14973 8695 7982 1873 1239 2574 C ATOM 2517 C GLU B 127 -14.041 17.792 -32.227 1.00 84.45 C ANISOU 2517 C GLU B 127 15261 8450 8376 1552 1510 2374 C ATOM 2518 O GLU B 127 -13.540 18.885 -32.455 1.00 85.48 O ANISOU 2518 O GLU B 127 15770 8247 8463 1578 1818 2441 O ATOM 2519 CB GLU B 127 -16.508 17.486 -31.716 1.00 84.45 C ANISOU 2519 CB GLU B 127 14885 9004 8196 2080 1073 2629 C ATOM 2520 CG GLU B 127 -16.989 18.877 -31.348 1.00 98.65 C ANISOU 2520 CG GLU B 127 16974 10574 9935 2417 1273 2836 C ATOM 2521 CD GLU B 127 -18.463 18.984 -30.994 1.00133.83 C ANISOU 2521 CD GLU B 127 21240 15347 14264 2802 1072 3011 C ATOM 2522 OE1 GLU B 127 -18.967 18.115 -30.245 1.00139.39 O ANISOU 2522 OE1 GLU B 127 21550 16327 15084 2702 825 2888 O ATOM 2523 OE2 GLU B 127 -19.108 19.960 -31.444 1.00131.69 O ANISOU 2523 OE2 GLU B 127 21224 15047 13766 3214 1178 3274 O ATOM 2524 N GLU B 128 -13.424 16.848 -31.495 1.00 76.87 N ANISOU 2524 N GLU B 128 14004 7550 7654 1248 1408 2123 N ATOM 2525 CA GLU B 128 -12.098 17.010 -30.889 1.00 75.39 C ANISOU 2525 CA GLU B 128 13853 7108 7685 932 1621 1900 C ATOM 2526 C GLU B 128 -10.999 17.179 -31.952 1.00 79.77 C ANISOU 2526 C GLU B 128 14640 7507 8160 736 1842 1834 C ATOM 2527 O GLU B 128 -10.125 18.038 -31.805 1.00 79.83 O ANISOU 2527 O GLU B 128 14886 7226 8222 579 2147 1755 O ATOM 2528 CB GLU B 128 -11.767 15.804 -29.997 1.00 73.68 C ANISOU 2528 CB GLU B 128 13242 7068 7687 721 1424 1678 C ATOM 2529 CG GLU B 128 -10.980 16.220 -28.774 1.00 81.81 C ANISOU 2529 CG GLU B 128 14229 7919 8936 537 1579 1504 C ATOM 2530 CD GLU B 128 -10.026 15.217 -28.165 1.00 90.43 C ANISOU 2530 CD GLU B 128 15027 9119 10214 277 1506 1254 C ATOM 2531 OE1 GLU B 128 -9.141 15.678 -27.414 1.00 74.28 O ANISOU 2531 OE1 GLU B 128 12974 6951 8298 94 1680 1092 O ATOM 2532 OE2 GLU B 128 -10.166 13.992 -28.396 1.00 78.70 O ANISOU 2532 OE2 GLU B 128 13324 7847 8732 262 1290 1214 O ATOM 2533 N LEU B 129 -11.055 16.347 -33.013 1.00 75.50 N ANISOU 2533 N LEU B 129 14033 7171 7483 722 1702 1849 N ATOM 2534 CA LEU B 129 -10.097 16.333 -34.120 1.00 76.14 C ANISOU 2534 CA LEU B 129 14302 7158 7470 542 1877 1786 C ATOM 2535 C LEU B 129 -10.214 17.580 -34.986 1.00 84.33 C ANISOU 2535 C LEU B 129 15793 7967 8281 707 2130 1996 C ATOM 2536 O LEU B 129 -9.212 18.046 -35.541 1.00 83.89 O ANISOU 2536 O LEU B 129 15986 7690 8197 510 2408 1921 O ATOM 2537 CB LEU B 129 -10.259 15.058 -34.955 1.00 75.10 C ANISOU 2537 CB LEU B 129 13972 7318 7244 495 1648 1745 C ATOM 2538 CG LEU B 129 -9.904 13.751 -34.259 1.00 76.65 C ANISOU 2538 CG LEU B 129 13799 7674 7649 303 1470 1521 C ATOM 2539 CD1 LEU B 129 -10.810 12.642 -34.721 1.00 77.35 C ANISOU 2539 CD1 LEU B 129 13695 8075 7620 373 1190 1556 C ATOM 2540 CD2 LEU B 129 -8.435 13.393 -34.464 1.00 76.41 C ANISOU 2540 CD2 LEU B 129 13755 7543 7733 14 1642 1293 C ATOM 2541 N GLN B 130 -11.436 18.144 -35.066 1.00 84.22 N ANISOU 2541 N GLN B 130 15894 8009 8098 1079 2051 2261 N ATOM 2542 CA GLN B 130 -11.711 19.373 -35.806 1.00 88.05 C ANISOU 2542 CA GLN B 130 16844 8272 8340 1333 2292 2513 C ATOM 2543 C GLN B 130 -11.048 20.530 -35.063 1.00 95.36 C ANISOU 2543 C GLN B 130 18072 8760 9401 1220 2659 2455 C ATOM 2544 O GLN B 130 -10.562 21.456 -35.709 1.00 99.21 O ANISOU 2544 O GLN B 130 19004 8937 9753 1206 2992 2533 O ATOM 2545 CB GLN B 130 -13.219 19.601 -35.934 1.00 90.84 C ANISOU 2545 CB GLN B 130 17178 8858 8479 1802 2090 2802 C ATOM 2546 CG GLN B 130 -13.866 18.911 -37.136 1.00108.54 C ANISOU 2546 CG GLN B 130 19310 11491 10439 1955 1848 2925 C ATOM 2547 CD GLN B 130 -15.273 18.405 -36.859 1.00131.40 C ANISOU 2547 CD GLN B 130 21864 14828 13234 2239 1499 3037 C ATOM 2548 OE1 GLN B 130 -16.037 18.961 -36.051 1.00125.42 O ANISOU 2548 OE1 GLN B 130 21083 14064 12508 2503 1477 3155 O ATOM 2549 NE2 GLN B 130 -15.652 17.331 -37.540 1.00126.54 N ANISOU 2549 NE2 GLN B 130 20975 14623 12481 2175 1231 2987 N ATOM 2550 N ALA B 131 -10.963 20.434 -33.712 1.00 89.50 N ANISOU 2550 N ALA B 131 17094 7995 8918 1098 2615 2294 N ATOM 2551 CA ALA B 131 -10.305 21.415 -32.849 1.00 89.97 C ANISOU 2551 CA ALA B 131 17373 7690 9122 922 2948 2177 C ATOM 2552 C ALA B 131 -8.780 21.139 -32.712 1.00 95.35 C ANISOU 2552 C ALA B 131 17970 8291 9967 426 3122 1846 C ATOM 2553 O ALA B 131 -8.132 21.653 -31.794 1.00 95.80 O ANISOU 2553 O ALA B 131 18052 8166 10181 186 3333 1659 O ATOM 2554 CB ALA B 131 -10.980 21.447 -31.486 1.00 88.53 C ANISOU 2554 CB ALA B 131 16965 7564 9107 1035 2810 2162 C ATOM 2555 N ASN B 132 -8.215 20.350 -33.661 1.00 91.91 N ANISOU 2555 N ASN B 132 17433 8016 9473 278 3046 1770 N ATOM 2556 CA ASN B 132 -6.804 19.950 -33.774 1.00 91.45 C ANISOU 2556 CA ASN B 132 17260 7963 9525 -141 3182 1475 C ATOM 2557 C ASN B 132 -6.286 19.209 -32.518 1.00 92.23 C ANISOU 2557 C ASN B 132 16904 8249 9892 -355 3032 1206 C ATOM 2558 O ASN B 132 -5.102 19.302 -32.179 1.00 92.67 O ANISOU 2558 O ASN B 132 16889 8267 10055 -693 3226 945 O ATOM 2559 CB ASN B 132 -5.902 21.151 -34.172 1.00 97.86 C ANISOU 2559 CB ASN B 132 18525 8404 10254 -370 3658 1413 C ATOM 2560 CG ASN B 132 -4.599 20.775 -34.857 1.00117.96 C ANISOU 2560 CG ASN B 132 21029 10993 12799 -735 3809 1181 C ATOM 2561 OD1 ASN B 132 -3.511 21.143 -34.404 1.00111.43 O ANISOU 2561 OD1 ASN B 132 20192 10074 12074 -1099 4070 916 O ATOM 2562 ND2 ASN B 132 -4.672 20.045 -35.968 1.00108.11 N ANISOU 2562 ND2 ASN B 132 19745 9911 11421 -657 3661 1260 N ATOM 2563 N LYS B 133 -7.170 18.422 -31.863 1.00 85.17 N ANISOU 2563 N LYS B 133 15687 7590 9082 -156 2685 1267 N ATOM 2564 CA LYS B 133 -6.819 17.632 -30.675 1.00 81.74 C ANISOU 2564 CA LYS B 133 14836 7347 8874 -294 2513 1057 C ATOM 2565 C LYS B 133 -7.247 16.161 -30.796 1.00 81.29 C ANISOU 2565 C LYS B 133 14437 7603 8846 -198 2153 1061 C ATOM 2566 O LYS B 133 -8.133 15.841 -31.589 1.00 82.14 O ANISOU 2566 O LYS B 133 14601 7806 8803 7 1995 1246 O ATOM 2567 CB LYS B 133 -7.369 18.279 -29.387 1.00 84.01 C ANISOU 2567 CB LYS B 133 15107 7545 9269 -210 2525 1080 C ATOM 2568 CG LYS B 133 -6.629 19.565 -29.003 0.50 93.59 C ANISOU 2568 CG LYS B 133 16599 8460 10500 -428 2918 963 C ATOM 2569 CD LYS B 133 -6.730 19.897 -27.528 0.50100.02 C ANISOU 2569 CD LYS B 133 17273 9260 11471 -480 2925 857 C ATOM 2570 CE LYS B 133 -5.839 21.059 -27.155 0.50114.11 C ANISOU 2570 CE LYS B 133 19303 10785 13267 -789 3335 672 C ATOM 2571 NZ LYS B 133 -5.952 21.410 -25.715 0.50120.64 N ANISOU 2571 NZ LYS B 133 19999 11611 14228 -856 3351 555 N ATOM 2572 N ALA B 134 -6.574 15.260 -30.062 1.00 72.81 N ANISOU 2572 N ALA B 134 13026 6696 7942 -355 2047 849 N ATOM 2573 CA ALA B 134 -6.907 13.834 -30.050 1.00 69.43 C ANISOU 2573 CA ALA B 134 12312 6516 7554 -285 1753 832 C ATOM 2574 C ALA B 134 -6.667 13.246 -28.672 1.00 69.61 C ANISOU 2574 C ALA B 134 12019 6661 7769 -331 1633 688 C ATOM 2575 O ALA B 134 -5.544 13.280 -28.174 1.00 70.54 O ANISOU 2575 O ALA B 134 12016 6801 7986 -515 1758 487 O ATOM 2576 CB ALA B 134 -6.117 13.059 -31.106 1.00 69.67 C ANISOU 2576 CB ALA B 134 12326 6622 7523 -410 1782 733 C ATOM 2577 N THR B 135 -7.726 12.736 -28.045 1.00 62.15 N ANISOU 2577 N THR B 135 10935 5821 6859 -163 1397 786 N ATOM 2578 CA THR B 135 -7.636 12.087 -26.742 1.00 58.70 C ANISOU 2578 CA THR B 135 10217 5503 6582 -175 1265 679 C ATOM 2579 C THR B 135 -8.350 10.768 -26.814 1.00 59.81 C ANISOU 2579 C THR B 135 10209 5806 6711 -76 1016 725 C ATOM 2580 O THR B 135 -9.508 10.720 -27.212 1.00 60.31 O ANISOU 2580 O THR B 135 10334 5911 6669 54 891 880 O ATOM 2581 CB THR B 135 -8.233 12.952 -25.596 1.00 58.12 C ANISOU 2581 CB THR B 135 10146 5359 6578 -106 1275 730 C ATOM 2582 OG1 THR B 135 -7.735 14.275 -25.661 1.00 62.61 O ANISOU 2582 OG1 THR B 135 10934 5730 7125 -206 1547 702 O ATOM 2583 CG2 THR B 135 -7.922 12.388 -24.222 1.00 50.39 C ANISOU 2583 CG2 THR B 135 8888 4507 5753 -149 1176 597 C ATOM 2584 N LEU B 136 -7.659 9.704 -26.420 1.00 55.50 N ANISOU 2584 N LEU B 136 9471 5363 6255 -136 960 585 N ATOM 2585 CA LEU B 136 -8.212 8.347 -26.276 1.00 55.11 C ANISOU 2585 CA LEU B 136 9300 5429 6210 -72 766 595 C ATOM 2586 C LEU B 136 -8.497 8.185 -24.784 1.00 54.85 C ANISOU 2586 C LEU B 136 9092 5446 6302 -16 666 578 C ATOM 2587 O LEU B 136 -7.653 8.546 -23.976 1.00 51.83 O ANISOU 2587 O LEU B 136 8607 5070 6015 -63 749 472 O ATOM 2588 CB LEU B 136 -7.196 7.254 -26.695 1.00 55.28 C ANISOU 2588 CB LEU B 136 9259 5497 6247 -134 805 460 C ATOM 2589 CG LEU B 136 -6.624 7.308 -28.120 1.00 61.92 C ANISOU 2589 CG LEU B 136 10250 6298 6978 -218 931 432 C ATOM 2590 CD1 LEU B 136 -5.448 6.391 -28.244 1.00 63.13 C ANISOU 2590 CD1 LEU B 136 10306 6502 7176 -258 1002 275 C ATOM 2591 CD2 LEU B 136 -7.639 6.906 -29.129 1.00 63.23 C ANISOU 2591 CD2 LEU B 136 10545 6486 6993 -192 833 544 C ATOM 2592 N VAL B 137 -9.693 7.715 -24.431 1.00 51.62 N ANISOU 2592 N VAL B 137 8645 5095 5872 67 499 673 N ATOM 2593 CA VAL B 137 -10.101 7.434 -23.048 1.00 50.81 C ANISOU 2593 CA VAL B 137 8392 5043 5870 120 396 667 C ATOM 2594 C VAL B 137 -10.486 5.959 -22.958 1.00 51.99 C ANISOU 2594 C VAL B 137 8487 5260 6006 128 274 650 C ATOM 2595 O VAL B 137 -11.273 5.455 -23.771 1.00 50.35 O ANISOU 2595 O VAL B 137 8352 5092 5686 108 208 701 O ATOM 2596 CB VAL B 137 -11.191 8.380 -22.462 1.00 54.73 C ANISOU 2596 CB VAL B 137 8897 5533 6363 201 346 782 C ATOM 2597 CG1 VAL B 137 -11.671 7.925 -21.085 1.00 54.00 C ANISOU 2597 CG1 VAL B 137 8649 5508 6361 240 232 770 C ATOM 2598 CG2 VAL B 137 -10.645 9.780 -22.351 1.00 56.43 C ANISOU 2598 CG2 VAL B 137 9203 5630 6607 178 518 772 C ATOM 2599 N CYS B 138 -9.878 5.289 -21.996 1.00 49.40 N ANISOU 2599 N CYS B 138 8047 4951 5772 152 267 571 N ATOM 2600 CA CYS B 138 -10.092 3.894 -21.622 1.00 49.42 C ANISOU 2600 CA CYS B 138 8033 4968 5775 178 198 551 C ATOM 2601 C CYS B 138 -10.916 4.003 -20.308 1.00 49.46 C ANISOU 2601 C CYS B 138 7943 5014 5836 224 97 600 C ATOM 2602 O CYS B 138 -10.376 4.394 -19.266 1.00 45.23 O ANISOU 2602 O CYS B 138 7294 4505 5387 272 112 566 O ATOM 2603 CB CYS B 138 -8.726 3.236 -21.386 1.00 51.75 C ANISOU 2603 CB CYS B 138 8276 5265 6121 231 283 448 C ATOM 2604 SG CYS B 138 -8.730 1.422 -21.218 1.00 57.42 S ANISOU 2604 SG CYS B 138 9074 5931 6813 301 275 429 S ATOM 2605 N LEU B 139 -12.238 3.765 -20.381 1.00 46.72 N ANISOU 2605 N LEU B 139 7625 4703 5425 195 -1 670 N ATOM 2606 CA LEU B 139 -13.060 3.784 -19.162 1.00 47.29 C ANISOU 2606 CA LEU B 139 7605 4821 5540 226 -87 708 C ATOM 2607 C LEU B 139 -12.965 2.383 -18.461 1.00 51.51 C ANISOU 2607 C LEU B 139 8158 5323 6089 229 -97 667 C ATOM 2608 O LEU B 139 -13.138 1.353 -19.117 1.00 50.22 O ANISOU 2608 O LEU B 139 8110 5120 5851 162 -76 641 O ATOM 2609 CB LEU B 139 -14.522 4.213 -19.458 1.00 48.02 C ANISOU 2609 CB LEU B 139 7688 5013 5544 204 -179 792 C ATOM 2610 CG LEU B 139 -15.544 4.026 -18.290 1.00 52.86 C ANISOU 2610 CG LEU B 139 8204 5702 6179 211 -268 818 C ATOM 2611 CD1 LEU B 139 -15.254 4.985 -17.097 1.00 51.48 C ANISOU 2611 CD1 LEU B 139 7938 5500 6122 299 -252 832 C ATOM 2612 CD2 LEU B 139 -16.972 4.179 -18.787 1.00 56.99 C ANISOU 2612 CD2 LEU B 139 8691 6388 6575 181 -357 876 C ATOM 2613 N ILE B 140 -12.634 2.366 -17.149 1.00 49.93 N ANISOU 2613 N ILE B 140 7869 5131 5970 309 -108 660 N ATOM 2614 CA ILE B 140 -12.418 1.136 -16.331 1.00 49.70 C ANISOU 2614 CA ILE B 140 7881 5056 5945 367 -96 646 C ATOM 2615 C ILE B 140 -13.400 1.178 -15.141 1.00 53.74 C ANISOU 2615 C ILE B 140 8334 5612 6474 358 -174 690 C ATOM 2616 O ILE B 140 -13.194 1.945 -14.197 1.00 50.34 O ANISOU 2616 O ILE B 140 7774 5244 6109 420 -201 696 O ATOM 2617 CB ILE B 140 -10.924 1.008 -15.850 1.00 52.20 C ANISOU 2617 CB ILE B 140 8132 5392 6311 514 -32 598 C ATOM 2618 CG1 ILE B 140 -9.882 1.305 -16.982 1.00 52.08 C ANISOU 2618 CG1 ILE B 140 8123 5377 6289 509 53 536 C ATOM 2619 CG2 ILE B 140 -10.669 -0.369 -15.234 1.00 53.92 C ANISOU 2619 CG2 ILE B 140 8449 5543 6496 631 4 610 C ATOM 2620 CD1 ILE B 140 -8.538 1.874 -16.442 1.00 49.82 C ANISOU 2620 CD1 ILE B 140 7662 5217 6050 601 100 464 C ATOM 2621 N SER B 141 -14.469 0.365 -15.199 1.00 54.34 N ANISOU 2621 N SER B 141 8503 5664 6479 254 -194 702 N ATOM 2622 CA SER B 141 -15.515 0.396 -14.177 1.00 55.51 C ANISOU 2622 CA SER B 141 8592 5871 6628 214 -258 733 C ATOM 2623 C SER B 141 -15.820 -0.951 -13.497 1.00 60.13 C ANISOU 2623 C SER B 141 9320 6362 7166 177 -208 726 C ATOM 2624 O SER B 141 -15.404 -1.982 -13.989 1.00 60.48 O ANISOU 2624 O SER B 141 9541 6278 7159 166 -115 699 O ATOM 2625 CB SER B 141 -16.788 0.993 -14.768 1.00 60.52 C ANISOU 2625 CB SER B 141 9160 6633 7202 100 -330 750 C ATOM 2626 OG SER B 141 -17.127 0.362 -15.992 1.00 70.16 O ANISOU 2626 OG SER B 141 10484 7861 8314 -30 -307 713 O ATOM 2627 N ASP B 142 -16.548 -0.917 -12.356 1.00 58.63 N ANISOU 2627 N ASP B 142 9074 6219 6985 160 -249 751 N ATOM 2628 CA ASP B 142 -17.049 -2.062 -11.577 1.00 60.69 C ANISOU 2628 CA ASP B 142 9482 6389 7188 98 -189 751 C ATOM 2629 C ASP B 142 -15.985 -3.070 -11.081 1.00 64.01 C ANISOU 2629 C ASP B 142 10084 6640 7598 265 -83 778 C ATOM 2630 O ASP B 142 -16.275 -4.261 -10.993 1.00 66.54 O ANISOU 2630 O ASP B 142 10641 6804 7838 198 30 771 O ATOM 2631 CB ASP B 142 -18.139 -2.809 -12.387 1.00 64.73 C ANISOU 2631 CB ASP B 142 10111 6899 7584 -155 -146 689 C ATOM 2632 CG ASP B 142 -19.398 -1.999 -12.565 1.00 86.76 C ANISOU 2632 CG ASP B 142 12704 9917 10343 -289 -254 673 C ATOM 2633 OD1 ASP B 142 -20.150 -1.839 -11.566 1.00 90.76 O ANISOU 2633 OD1 ASP B 142 13126 10503 10855 -323 -288 684 O ATOM 2634 OD2 ASP B 142 -19.632 -1.511 -13.694 1.00 93.25 O ANISOU 2634 OD2 ASP B 142 13453 10855 11122 -340 -302 655 O ATOM 2635 N PHE B 143 -14.777 -2.612 -10.756 1.00 58.50 N ANISOU 2635 N PHE B 143 9283 5982 6962 482 -102 803 N ATOM 2636 CA PHE B 143 -13.765 -3.553 -10.302 1.00 58.36 C ANISOU 2636 CA PHE B 143 9407 5860 6907 696 -9 840 C ATOM 2637 C PHE B 143 -13.637 -3.596 -8.777 1.00 63.99 C ANISOU 2637 C PHE B 143 10071 6632 7610 847 -37 902 C ATOM 2638 O PHE B 143 -14.101 -2.700 -8.078 1.00 60.28 O ANISOU 2638 O PHE B 143 9415 6301 7188 792 -135 899 O ATOM 2639 CB PHE B 143 -12.393 -3.351 -10.994 1.00 59.16 C ANISOU 2639 CB PHE B 143 9443 6000 7034 861 15 815 C ATOM 2640 CG PHE B 143 -11.735 -1.991 -10.938 1.00 58.35 C ANISOU 2640 CG PHE B 143 9057 6103 7012 901 -75 777 C ATOM 2641 CD1 PHE B 143 -12.102 -0.980 -11.832 1.00 58.59 C ANISOU 2641 CD1 PHE B 143 8991 6179 7091 737 -119 733 C ATOM 2642 CD2 PHE B 143 -10.661 -1.756 -10.087 1.00 58.34 C ANISOU 2642 CD2 PHE B 143 8901 6253 7013 1105 -91 776 C ATOM 2643 CE1 PHE B 143 -11.459 0.266 -11.811 1.00 57.36 C ANISOU 2643 CE1 PHE B 143 8631 6164 6998 752 -153 690 C ATOM 2644 CE2 PHE B 143 -10.035 -0.502 -10.054 1.00 59.55 C ANISOU 2644 CE2 PHE B 143 8806 6595 7224 1084 -139 707 C ATOM 2645 CZ PHE B 143 -10.421 0.491 -10.938 1.00 56.03 C ANISOU 2645 CZ PHE B 143 8314 6136 6838 899 -154 662 C ATOM 2646 N TYR B 144 -13.041 -4.681 -8.275 1.00 66.70 N ANISOU 2646 N TYR B 144 10608 6860 7875 1049 64 964 N ATOM 2647 CA TYR B 144 -12.758 -4.889 -6.860 1.00 68.46 C ANISOU 2647 CA TYR B 144 10818 7146 8049 1249 51 1042 C ATOM 2648 C TYR B 144 -11.693 -5.976 -6.665 1.00 72.08 C ANISOU 2648 C TYR B 144 11469 7513 8406 1575 169 1120 C ATOM 2649 O TYR B 144 -11.875 -7.073 -7.186 1.00 71.74 O ANISOU 2649 O TYR B 144 11750 7209 8300 1565 325 1143 O ATOM 2650 CB TYR B 144 -14.021 -5.173 -6.000 1.00 71.51 C ANISOU 2650 CB TYR B 144 11317 7455 8398 1085 63 1072 C ATOM 2651 CG TYR B 144 -13.647 -5.380 -4.545 1.00 75.63 C ANISOU 2651 CG TYR B 144 11836 8049 8850 1312 54 1162 C ATOM 2652 CD1 TYR B 144 -13.483 -4.294 -3.686 1.00 77.01 C ANISOU 2652 CD1 TYR B 144 11710 8482 9070 1346 -84 1145 C ATOM 2653 CD2 TYR B 144 -13.325 -6.648 -4.062 1.00 77.89 C ANISOU 2653 CD2 TYR B 144 12432 8155 9008 1523 197 1266 C ATOM 2654 CE1 TYR B 144 -13.026 -4.467 -2.380 1.00 79.30 C ANISOU 2654 CE1 TYR B 144 11972 8889 9270 1568 -103 1220 C ATOM 2655 CE2 TYR B 144 -12.856 -6.830 -2.761 1.00 79.89 C ANISOU 2655 CE2 TYR B 144 12676 8512 9167 1788 181 1366 C ATOM 2656 CZ TYR B 144 -12.732 -5.740 -1.916 1.00 85.25 C ANISOU 2656 CZ TYR B 144 13019 9488 9884 1798 20 1338 C ATOM 2657 OH TYR B 144 -12.283 -5.916 -0.633 1.00 87.27 O ANISOU 2657 OH TYR B 144 13251 9885 10023 2049 -2 1429 O ATOM 2658 N PRO B 145 -10.608 -5.727 -5.882 1.00 69.51 N ANISOU 2658 N PRO B 145 10959 7409 8041 1872 113 1160 N ATOM 2659 CA PRO B 145 -10.248 -4.467 -5.192 1.00 68.18 C ANISOU 2659 CA PRO B 145 10416 7566 7922 1875 -42 1108 C ATOM 2660 C PRO B 145 -9.894 -3.309 -6.144 1.00 70.54 C ANISOU 2660 C PRO B 145 10465 8002 8336 1715 -109 983 C ATOM 2661 O PRO B 145 -9.814 -3.483 -7.372 1.00 69.57 O ANISOU 2661 O PRO B 145 10432 7752 8248 1636 -51 946 O ATOM 2662 CB PRO B 145 -9.107 -4.887 -4.248 1.00 71.78 C ANISOU 2662 CB PRO B 145 10804 8221 8249 2258 -43 1181 C ATOM 2663 CG PRO B 145 -8.507 -6.097 -4.873 1.00 78.31 C ANISOU 2663 CG PRO B 145 11897 8864 8995 2501 104 1250 C ATOM 2664 CD PRO B 145 -9.608 -6.787 -5.638 1.00 73.33 C ANISOU 2664 CD PRO B 145 11616 7847 8400 2252 224 1256 C ATOM 2665 N GLY B 146 -9.708 -2.127 -5.560 1.00 65.88 N ANISOU 2665 N GLY B 146 9585 7655 7790 1652 -210 916 N ATOM 2666 CA GLY B 146 -9.456 -0.883 -6.284 1.00 64.07 C ANISOU 2666 CA GLY B 146 9149 7536 7659 1477 -246 799 C ATOM 2667 C GLY B 146 -8.043 -0.607 -6.717 1.00 67.26 C ANISOU 2667 C GLY B 146 9372 8141 8043 1596 -224 715 C ATOM 2668 O GLY B 146 -7.538 0.501 -6.512 1.00 66.35 O ANISOU 2668 O GLY B 146 9012 8241 7955 1505 -255 606 O ATOM 2669 N ALA B 147 -7.408 -1.608 -7.328 1.00 64.06 N ANISOU 2669 N ALA B 147 9096 7664 7581 1783 -149 753 N ATOM 2670 CA ALA B 147 -6.050 -1.478 -7.849 1.00 63.68 C ANISOU 2670 CA ALA B 147 8875 7819 7501 1912 -113 669 C ATOM 2671 C ALA B 147 -6.005 -1.997 -9.285 1.00 64.45 C ANISOU 2671 C ALA B 147 9165 7694 7631 1875 -19 666 C ATOM 2672 O ALA B 147 -6.453 -3.106 -9.549 1.00 63.35 O ANISOU 2672 O ALA B 147 9311 7303 7456 1954 50 757 O ATOM 2673 CB ALA B 147 -5.075 -2.257 -6.970 1.00 66.16 C ANISOU 2673 CB ALA B 147 9112 8358 7669 2283 -110 724 C ATOM 2674 N VAL B 148 -5.539 -1.167 -10.220 1.00 60.17 N ANISOU 2674 N VAL B 148 8493 7222 7147 1719 1 552 N ATOM 2675 CA VAL B 148 -5.358 -1.562 -11.622 1.00 59.13 C ANISOU 2675 CA VAL B 148 8513 6922 7033 1679 92 531 C ATOM 2676 C VAL B 148 -4.004 -1.053 -12.099 1.00 64.15 C ANISOU 2676 C VAL B 148 8914 7809 7652 1723 138 405 C ATOM 2677 O VAL B 148 -3.469 -0.112 -11.510 1.00 63.39 O ANISOU 2677 O VAL B 148 8546 7984 7555 1665 98 309 O ATOM 2678 CB VAL B 148 -6.515 -1.200 -12.606 1.00 59.11 C ANISOU 2678 CB VAL B 148 8682 6673 7104 1388 91 537 C ATOM 2679 CG1 VAL B 148 -7.752 -2.056 -12.379 1.00 56.79 C ANISOU 2679 CG1 VAL B 148 8642 6144 6791 1348 85 639 C ATOM 2680 CG2 VAL B 148 -6.853 0.284 -12.567 1.00 58.11 C ANISOU 2680 CG2 VAL B 148 8391 6638 7051 1164 32 476 C ATOM 2681 N THR B 149 -3.436 -1.716 -13.121 1.00 60.34 N ANISOU 2681 N THR B 149 8536 7248 7144 1816 237 390 N ATOM 2682 CA THR B 149 -2.190 -1.354 -13.811 1.00 60.96 C ANISOU 2682 CA THR B 149 8420 7541 7202 1838 308 260 C ATOM 2683 C THR B 149 -2.611 -1.135 -15.266 1.00 61.67 C ANISOU 2683 C THR B 149 8692 7388 7351 1601 374 232 C ATOM 2684 O THR B 149 -3.397 -1.921 -15.801 1.00 57.62 O ANISOU 2684 O THR B 149 8464 6589 6839 1585 403 316 O ATOM 2685 CB THR B 149 -1.133 -2.478 -13.701 1.00 77.70 C ANISOU 2685 CB THR B 149 10515 9795 9213 2222 378 283 C ATOM 2686 OG1 THR B 149 -0.936 -2.812 -12.333 1.00 86.28 O ANISOU 2686 OG1 THR B 149 11486 11079 10216 2478 308 351 O ATOM 2687 CG2 THR B 149 0.199 -2.085 -14.297 1.00 79.81 C ANISOU 2687 CG2 THR B 149 10521 10360 9444 2253 448 130 C ATOM 2688 N VAL B 150 -2.161 -0.038 -15.887 1.00 59.83 N ANISOU 2688 N VAL B 150 8313 7266 7152 1392 408 111 N ATOM 2689 CA VAL B 150 -2.570 0.251 -17.268 1.00 58.07 C ANISOU 2689 CA VAL B 150 8270 6830 6963 1179 469 98 C ATOM 2690 C VAL B 150 -1.370 0.441 -18.161 1.00 63.22 C ANISOU 2690 C VAL B 150 8815 7621 7586 1166 588 -31 C ATOM 2691 O VAL B 150 -0.423 1.141 -17.809 1.00 65.18 O ANISOU 2691 O VAL B 150 8797 8150 7817 1139 619 -157 O ATOM 2692 CB VAL B 150 -3.606 1.420 -17.399 1.00 58.92 C ANISOU 2692 CB VAL B 150 8431 6824 7133 905 416 120 C ATOM 2693 CG1 VAL B 150 -4.041 1.630 -18.854 1.00 57.41 C ANISOU 2693 CG1 VAL B 150 8433 6442 6938 734 472 130 C ATOM 2694 CG2 VAL B 150 -4.826 1.187 -16.510 1.00 57.23 C ANISOU 2694 CG2 VAL B 150 8303 6499 6941 921 302 238 C ATOM 2695 N ALA B 151 -1.411 -0.209 -19.317 1.00 58.80 N ANISOU 2695 N ALA B 151 8456 6879 7006 1166 667 -16 N ATOM 2696 CA ALA B 151 -0.387 -0.082 -20.330 1.00 58.38 C ANISOU 2696 CA ALA B 151 8342 6919 6922 1134 794 -134 C ATOM 2697 C ALA B 151 -1.069 0.198 -21.666 1.00 60.21 C ANISOU 2697 C ALA B 151 8812 6906 7161 898 836 -114 C ATOM 2698 O ALA B 151 -2.112 -0.370 -21.974 1.00 58.52 O ANISOU 2698 O ALA B 151 8833 6461 6941 867 793 -13 O ATOM 2699 CB ALA B 151 0.438 -1.347 -20.393 1.00 60.61 C ANISOU 2699 CB ALA B 151 8632 7257 7141 1442 871 -138 C ATOM 2700 N TRP B 152 -0.494 1.096 -22.443 1.00 57.05 N ANISOU 2700 N TRP B 152 8347 6578 6754 719 927 -217 N ATOM 2701 CA TRP B 152 -0.995 1.433 -23.762 1.00 56.57 C ANISOU 2701 CA TRP B 152 8500 6325 6668 518 979 -198 C ATOM 2702 C TRP B 152 0.030 1.017 -24.827 1.00 63.14 C ANISOU 2702 C TRP B 152 9343 7200 7447 536 1130 -304 C ATOM 2703 O TRP B 152 1.240 1.016 -24.565 1.00 63.81 O ANISOU 2703 O TRP B 152 9202 7522 7521 628 1209 -425 O ATOM 2704 CB TRP B 152 -1.262 2.955 -23.858 1.00 54.53 C ANISOU 2704 CB TRP B 152 8224 6066 6430 282 992 -213 C ATOM 2705 CG TRP B 152 -2.469 3.465 -23.116 1.00 52.37 C ANISOU 2705 CG TRP B 152 8001 5700 6198 243 863 -95 C ATOM 2706 CD1 TRP B 152 -2.551 3.784 -21.786 1.00 54.40 C ANISOU 2706 CD1 TRP B 152 8098 6065 6508 293 788 -95 C ATOM 2707 CD2 TRP B 152 -3.738 3.808 -23.694 1.00 50.74 C ANISOU 2707 CD2 TRP B 152 8001 5310 5966 147 802 29 C ATOM 2708 NE1 TRP B 152 -3.818 4.244 -21.487 1.00 52.04 N ANISOU 2708 NE1 TRP B 152 7908 5634 6233 240 690 25 N ATOM 2709 CE2 TRP B 152 -4.543 4.338 -22.656 1.00 53.30 C ANISOU 2709 CE2 TRP B 152 8279 5633 6341 154 699 101 C ATOM 2710 CE3 TRP B 152 -4.269 3.738 -24.997 1.00 51.94 C ANISOU 2710 CE3 TRP B 152 8360 5335 6039 62 825 83 C ATOM 2711 CZ2 TRP B 152 -5.848 4.794 -22.883 1.00 51.01 C ANISOU 2711 CZ2 TRP B 152 8127 5228 6027 104 620 227 C ATOM 2712 CZ3 TRP B 152 -5.561 4.200 -25.217 1.00 52.07 C ANISOU 2712 CZ3 TRP B 152 8503 5264 6017 11 735 210 C ATOM 2713 CH2 TRP B 152 -6.341 4.696 -24.161 1.00 51.19 C ANISOU 2713 CH2 TRP B 152 8328 5162 5960 44 633 282 C ATOM 2714 N LYS B 153 -0.468 0.664 -26.032 1.00 60.35 N ANISOU 2714 N LYS B 153 9236 6651 7045 443 1170 -266 N ATOM 2715 CA LYS B 153 0.331 0.306 -27.213 1.00 60.92 C ANISOU 2715 CA LYS B 153 9367 6722 7056 422 1322 -360 C ATOM 2716 C LYS B 153 -0.162 1.092 -28.429 1.00 65.34 C ANISOU 2716 C LYS B 153 10106 7160 7560 168 1362 -342 C ATOM 2717 O LYS B 153 -1.365 1.307 -28.576 1.00 62.09 O ANISOU 2717 O LYS B 153 9850 6614 7129 79 1259 -225 O ATOM 2718 CB LYS B 153 0.233 -1.198 -27.536 1.00 63.00 C ANISOU 2718 CB LYS B 153 9805 6850 7281 594 1359 -336 C ATOM 2719 CG LYS B 153 0.962 -2.109 -26.564 1.00 69.81 C ANISOU 2719 CG LYS B 153 10536 7827 8163 912 1377 -349 C ATOM 2720 CD LYS B 153 0.943 -3.543 -27.077 1.00 76.46 C ANISOU 2720 CD LYS B 153 11623 8477 8951 1071 1480 -334 C ATOM 2721 CE LYS B 153 1.666 -4.493 -26.160 1.00 94.00 C ANISOU 2721 CE LYS B 153 13764 10784 11166 1449 1524 -319 C ATOM 2722 NZ LYS B 153 1.681 -5.881 -26.699 1.00110.54 N ANISOU 2722 NZ LYS B 153 16158 12642 13201 1612 1673 -304 N ATOM 2723 N ALA B 154 0.774 1.540 -29.285 1.00 67.29 N ANISOU 2723 N ALA B 154 10322 7481 7764 63 1516 -456 N ATOM 2724 CA ALA B 154 0.529 2.212 -30.572 1.00 68.14 C ANISOU 2724 CA ALA B 154 10620 7482 7788 -153 1595 -446 C ATOM 2725 C ALA B 154 0.955 1.121 -31.560 1.00 74.41 C ANISOU 2725 C ALA B 154 11525 8231 8515 -101 1695 -508 C ATOM 2726 O ALA B 154 2.129 0.741 -31.601 1.00 75.61 O ANISOU 2726 O ALA B 154 11536 8518 8675 -10 1818 -638 O ATOM 2727 CB ALA B 154 1.398 3.451 -30.698 1.00 69.96 C ANISOU 2727 CB ALA B 154 10741 7826 8016 -319 1736 -553 C ATOM 2728 N ASP B 155 -0.034 0.518 -32.243 1.00 72.25 N ANISOU 2728 N ASP B 155 11490 7793 8169 -141 1637 -422 N ATOM 2729 CA ASP B 155 0.087 -0.710 -33.043 1.00 74.23 C ANISOU 2729 CA ASP B 155 11899 7955 8352 -96 1721 -472 C ATOM 2730 C ASP B 155 0.440 -1.788 -31.989 1.00 80.19 C ANISOU 2730 C ASP B 155 12559 8722 9186 167 1712 -488 C ATOM 2731 O ASP B 155 -0.350 -1.969 -31.058 1.00 80.12 O ANISOU 2731 O ASP B 155 12548 8669 9226 230 1577 -394 O ATOM 2732 CB ASP B 155 1.091 -0.600 -34.233 1.00 77.87 C ANISOU 2732 CB ASP B 155 12391 8457 8739 -182 1912 -596 C ATOM 2733 CG ASP B 155 0.635 0.289 -35.383 1.00 86.77 C ANISOU 2733 CG ASP B 155 13683 9537 9750 -421 1934 -556 C ATOM 2734 OD1 ASP B 155 -0.589 0.355 -35.640 1.00 86.50 O ANISOU 2734 OD1 ASP B 155 13802 9421 9642 -499 1807 -437 O ATOM 2735 OD2 ASP B 155 1.507 0.889 -36.054 1.00 94.06 O ANISOU 2735 OD2 ASP B 155 14581 10522 10634 -523 2085 -644 O ATOM 2736 N SER B 156 1.634 -2.388 -32.027 1.00 78.94 N ANISOU 2736 N SER B 156 12307 8650 9038 340 1854 -596 N ATOM 2737 CA SER B 156 2.027 -3.360 -30.999 1.00 79.86 C ANISOU 2737 CA SER B 156 12343 8795 9205 651 1857 -588 C ATOM 2738 C SER B 156 3.221 -2.863 -30.152 1.00 84.50 C ANISOU 2738 C SER B 156 12572 9689 9845 814 1874 -664 C ATOM 2739 O SER B 156 3.813 -3.648 -29.402 1.00 86.14 O ANISOU 2739 O SER B 156 12673 9994 10063 1126 1899 -668 O ATOM 2740 CB SER B 156 2.328 -4.713 -31.633 1.00 86.55 C ANISOU 2740 CB SER B 156 13402 9493 9991 797 2018 -633 C ATOM 2741 OG SER B 156 3.230 -4.529 -32.711 1.00101.99 O ANISOU 2741 OG SER B 156 15326 11531 11894 730 2175 -758 O ATOM 2742 N SER B 157 3.549 -1.555 -30.253 1.00 79.48 N ANISOU 2742 N SER B 157 11761 9216 9222 604 1870 -727 N ATOM 2743 CA SER B 157 4.663 -0.934 -29.541 1.00 80.33 C ANISOU 2743 CA SER B 157 11511 9657 9353 664 1904 -844 C ATOM 2744 C SER B 157 4.201 -0.156 -28.322 1.00 83.73 C ANISOU 2744 C SER B 157 11794 10173 9849 623 1753 -787 C ATOM 2745 O SER B 157 3.294 0.671 -28.444 1.00 82.27 O ANISOU 2745 O SER B 157 11741 9833 9683 397 1683 -711 O ATOM 2746 CB SER B 157 5.465 -0.024 -30.467 1.00 85.31 C ANISOU 2746 CB SER B 157 12060 10415 9939 417 2058 -994 C ATOM 2747 OG SER B 157 6.135 -0.768 -31.474 1.00 95.93 O ANISOU 2747 OG SER B 157 13475 11753 11221 489 2215 -1078 O ATOM 2748 N PRO B 158 4.832 -0.370 -27.144 1.00 81.22 N ANISOU 2748 N PRO B 158 11195 10119 9545 851 1708 -823 N ATOM 2749 CA PRO B 158 4.415 0.363 -25.937 1.00 80.15 C ANISOU 2749 CA PRO B 158 10914 10078 9461 801 1571 -783 C ATOM 2750 C PRO B 158 4.452 1.884 -26.046 1.00 84.42 C ANISOU 2750 C PRO B 158 11378 10681 10015 454 1611 -869 C ATOM 2751 O PRO B 158 5.293 2.448 -26.754 1.00 84.56 O ANISOU 2751 O PRO B 158 11311 10827 9990 281 1766 -1021 O ATOM 2752 CB PRO B 158 5.383 -0.144 -24.866 1.00 83.62 C ANISOU 2752 CB PRO B 158 11028 10874 9868 1111 1553 -845 C ATOM 2753 CG PRO B 158 5.796 -1.491 -25.352 1.00 89.28 C ANISOU 2753 CG PRO B 158 11851 11535 10537 1418 1637 -819 C ATOM 2754 CD PRO B 158 5.908 -1.333 -26.834 1.00 85.02 C ANISOU 2754 CD PRO B 158 11486 10838 9979 1197 1778 -889 C ATOM 2755 N VAL B 159 3.493 2.533 -25.370 1.00 80.97 N ANISOU 2755 N VAL B 159 11008 10126 9632 350 1492 -771 N ATOM 2756 CA VAL B 159 3.368 3.989 -25.313 1.00 81.78 C ANISOU 2756 CA VAL B 159 11099 10226 9749 48 1542 -826 C ATOM 2757 C VAL B 159 3.971 4.393 -23.958 1.00 90.12 C ANISOU 2757 C VAL B 159 11822 11604 10814 73 1510 -937 C ATOM 2758 O VAL B 159 3.322 4.229 -22.924 1.00 89.00 O ANISOU 2758 O VAL B 159 11654 11447 10714 194 1360 -837 O ATOM 2759 CB VAL B 159 1.894 4.474 -25.481 1.00 83.30 C ANISOU 2759 CB VAL B 159 11586 10089 9976 -60 1448 -644 C ATOM 2760 CG1 VAL B 159 1.795 5.993 -25.371 1.00 83.08 C ANISOU 2760 CG1 VAL B 159 11587 10028 9953 -327 1535 -689 C ATOM 2761 CG2 VAL B 159 1.293 3.996 -26.800 1.00 82.40 C ANISOU 2761 CG2 VAL B 159 11764 9728 9816 -79 1464 -546 C ATOM 2762 N LYS B 160 5.232 4.870 -23.964 1.00 90.72 N ANISOU 2762 N LYS B 160 11629 12008 10833 -46 1653 -1158 N ATOM 2763 CA LYS B 160 5.934 5.250 -22.729 1.00 92.19 C ANISOU 2763 CA LYS B 160 11449 12589 10989 -50 1635 -1307 C ATOM 2764 C LYS B 160 5.832 6.756 -22.381 1.00 93.36 C ANISOU 2764 C LYS B 160 11597 12731 11144 -429 1733 -1421 C ATOM 2765 O LYS B 160 6.600 7.232 -21.540 1.00 95.26 O ANISOU 2765 O LYS B 160 11520 13344 11332 -534 1776 -1613 O ATOM 2766 CB LYS B 160 7.407 4.780 -22.784 1.00 98.82 C ANISOU 2766 CB LYS B 160 11929 13887 11731 69 1727 -1507 C ATOM 2767 CG LYS B 160 7.736 3.644 -21.804 1.00113.95 C ANISOU 2767 CG LYS B 160 13603 16086 13606 504 1579 -1452 C ATOM 2768 CD LYS B 160 9.241 3.464 -21.600 1.00125.52 C ANISOU 2768 CD LYS B 160 14618 18130 14942 615 1663 -1677 C ATOM 2769 CE LYS B 160 9.816 4.386 -20.545 1.00133.62 C ANISOU 2769 CE LYS B 160 15266 19608 15894 414 1665 -1883 C ATOM 2770 NZ LYS B 160 11.300 4.394 -20.568 1.00140.72 N ANISOU 2770 NZ LYS B 160 15707 21116 16646 424 1780 -2151 N ATOM 2771 N ALA B 161 4.867 7.493 -23.001 1.00 85.75 N ANISOU 2771 N ALA B 161 10995 11356 10229 -621 1777 -1301 N ATOM 2772 CA ALA B 161 4.652 8.934 -22.790 1.00 84.21 C ANISOU 2772 CA ALA B 161 10904 11053 10037 -955 1911 -1375 C ATOM 2773 C ALA B 161 3.244 9.415 -23.182 1.00 81.33 C ANISOU 2773 C ALA B 161 10944 10231 9728 -976 1868 -1143 C ATOM 2774 O ALA B 161 2.693 8.964 -24.187 1.00 79.54 O ANISOU 2774 O ALA B 161 10955 9767 9499 -882 1833 -990 O ATOM 2775 CB ALA B 161 5.704 9.742 -23.552 1.00 87.42 C ANISOU 2775 CB ALA B 161 11282 11568 10364 -1284 2188 -1606 C ATOM 2776 N GLY B 162 2.714 10.366 -22.408 1.00 74.62 N ANISOU 2776 N GLY B 162 10156 9288 8908 -1107 1887 -1135 N ATOM 2777 CA GLY B 162 1.406 10.986 -22.631 1.00 71.94 C ANISOU 2777 CA GLY B 162 10166 8565 8604 -1108 1863 -928 C ATOM 2778 C GLY B 162 0.233 10.327 -21.922 1.00 71.03 C ANISOU 2778 C GLY B 162 10066 8366 8557 -845 1605 -721 C ATOM 2779 O GLY B 162 -0.909 10.783 -22.061 1.00 68.44 O ANISOU 2779 O GLY B 162 9986 7771 8247 -814 1567 -547 O ATOM 2780 N VAL B 163 0.524 9.251 -21.147 1.00 65.36 N ANISOU 2780 N VAL B 163 9081 7891 7861 -644 1441 -741 N ATOM 2781 CA VAL B 163 -0.439 8.427 -20.423 1.00 62.64 C ANISOU 2781 CA VAL B 163 8732 7499 7568 -400 1212 -570 C ATOM 2782 C VAL B 163 -0.699 8.986 -19.039 1.00 64.59 C ANISOU 2782 C VAL B 163 8853 7837 7850 -432 1162 -601 C ATOM 2783 O VAL B 163 0.235 9.315 -18.300 1.00 66.29 O ANISOU 2783 O VAL B 163 8817 8334 8037 -531 1228 -790 O ATOM 2784 CB VAL B 163 0.004 6.922 -20.347 1.00 66.70 C ANISOU 2784 CB VAL B 163 9094 8179 8069 -142 1097 -556 C ATOM 2785 CG1 VAL B 163 -0.970 6.079 -19.516 1.00 64.40 C ANISOU 2785 CG1 VAL B 163 8826 7824 7818 80 897 -393 C ATOM 2786 CG2 VAL B 163 0.201 6.318 -21.739 1.00 66.89 C ANISOU 2786 CG2 VAL B 163 9270 8088 8056 -115 1157 -529 C ATOM 2787 N GLU B 164 -1.982 9.034 -18.688 1.00 56.05 N ANISOU 2787 N GLU B 164 7928 6552 6818 -347 1042 -425 N ATOM 2788 CA GLU B 164 -2.478 9.461 -17.398 1.00 54.80 C ANISOU 2788 CA GLU B 164 7690 6436 6697 -346 974 -417 C ATOM 2789 C GLU B 164 -3.561 8.498 -17.005 1.00 56.25 C ANISOU 2789 C GLU B 164 7920 6536 6916 -120 765 -229 C ATOM 2790 O GLU B 164 -4.448 8.208 -17.812 1.00 54.40 O ANISOU 2790 O GLU B 164 7889 6096 6683 -61 714 -80 O ATOM 2791 CB GLU B 164 -3.096 10.875 -17.454 1.00 55.37 C ANISOU 2791 CB GLU B 164 7972 6282 6784 -525 1108 -399 C ATOM 2792 CG GLU B 164 -2.135 12.022 -17.680 1.00 59.57 C ANISOU 2792 CG GLU B 164 8516 6844 7274 -810 1367 -601 C ATOM 2793 CD GLU B 164 -1.011 12.143 -16.674 1.00 64.05 C ANISOU 2793 CD GLU B 164 8762 7766 7810 -946 1418 -846 C ATOM 2794 OE1 GLU B 164 -1.233 11.861 -15.475 1.00 52.51 O ANISOU 2794 OE1 GLU B 164 7123 6462 6367 -852 1281 -846 O ATOM 2795 OE2 GLU B 164 0.107 12.494 -17.104 1.00 66.31 O ANISOU 2795 OE2 GLU B 164 8956 8203 8034 -1149 1596 -1046 O ATOM 2796 N THR B 165 -3.513 8.024 -15.767 1.00 51.92 N ANISOU 2796 N THR B 165 7185 6166 6378 -10 654 -244 N ATOM 2797 CA THR B 165 -4.554 7.147 -15.244 1.00 50.08 C ANISOU 2797 CA THR B 165 7007 5852 6170 174 480 -80 C ATOM 2798 C THR B 165 -4.954 7.691 -13.920 1.00 52.30 C ANISOU 2798 C THR B 165 7192 6204 6476 149 434 -94 C ATOM 2799 O THR B 165 -4.089 8.000 -13.095 1.00 53.76 O ANISOU 2799 O THR B 165 7164 6632 6632 100 470 -239 O ATOM 2800 CB THR B 165 -4.080 5.660 -15.174 1.00 58.18 C ANISOU 2800 CB THR B 165 7955 6991 7159 394 401 -54 C ATOM 2801 OG1 THR B 165 -3.661 5.258 -16.480 1.00 57.55 O ANISOU 2801 OG1 THR B 165 7976 6836 7054 392 475 -64 O ATOM 2802 CG2 THR B 165 -5.172 4.700 -14.633 1.00 48.29 C ANISOU 2802 CG2 THR B 165 6806 5624 5919 550 260 104 C ATOM 2803 N THR B 166 -6.267 7.805 -13.703 1.00 47.00 N ANISOU 2803 N THR B 166 6659 5354 5843 178 354 45 N ATOM 2804 CA THR B 166 -6.796 8.305 -12.461 1.00 45.76 C ANISOU 2804 CA THR B 166 6435 5239 5713 160 312 45 C ATOM 2805 C THR B 166 -6.709 7.214 -11.371 1.00 53.30 C ANISOU 2805 C THR B 166 7243 6364 6643 328 178 70 C ATOM 2806 O THR B 166 -6.736 6.014 -11.664 1.00 51.80 O ANISOU 2806 O THR B 166 7095 6156 6429 480 108 149 O ATOM 2807 CB THR B 166 -8.210 8.935 -12.647 1.00 51.98 C ANISOU 2807 CB THR B 166 7409 5801 6538 142 297 175 C ATOM 2808 OG1 THR B 166 -9.189 7.902 -12.854 1.00 50.35 O ANISOU 2808 OG1 THR B 166 7278 5526 6327 272 157 322 O ATOM 2809 CG2 THR B 166 -8.257 10.031 -13.776 1.00 43.62 C ANISOU 2809 CG2 THR B 166 6537 4564 5474 28 450 178 C ATOM 2810 N THR B 167 -6.621 7.659 -10.106 1.00 52.36 N ANISOU 2810 N THR B 167 6979 6397 6516 297 162 3 N ATOM 2811 CA THR B 167 -6.573 6.819 -8.917 1.00 52.15 C ANISOU 2811 CA THR B 167 6822 6546 6445 456 46 32 C ATOM 2812 C THR B 167 -7.964 6.216 -8.769 1.00 55.96 C ANISOU 2812 C THR B 167 7474 6824 6963 540 -54 206 C ATOM 2813 O THR B 167 -8.920 6.959 -8.807 1.00 53.88 O ANISOU 2813 O THR B 167 7305 6414 6752 443 -43 246 O ATOM 2814 CB THR B 167 -6.154 7.692 -7.740 1.00 55.03 C ANISOU 2814 CB THR B 167 6997 7131 6779 344 78 -110 C ATOM 2815 OG1 THR B 167 -4.831 8.188 -8.010 1.00 52.44 O ANISOU 2815 OG1 THR B 167 6501 7026 6398 226 189 -299 O ATOM 2816 CG2 THR B 167 -6.238 6.962 -6.373 1.00 55.39 C ANISOU 2816 CG2 THR B 167 6916 7369 6759 509 -46 -66 C ATOM 2817 N PRO B 168 -8.127 4.881 -8.701 1.00 55.72 N ANISOU 2817 N PRO B 168 7506 6769 6896 715 -130 308 N ATOM 2818 CA PRO B 168 -9.486 4.318 -8.564 1.00 55.48 C ANISOU 2818 CA PRO B 168 7637 6559 6884 736 -200 443 C ATOM 2819 C PRO B 168 -10.267 4.925 -7.396 1.00 60.45 C ANISOU 2819 C PRO B 168 8211 7223 7535 683 -244 452 C ATOM 2820 O PRO B 168 -9.710 5.240 -6.348 1.00 62.33 O ANISOU 2820 O PRO B 168 8294 7646 7742 700 -250 382 O ATOM 2821 CB PRO B 168 -9.231 2.814 -8.379 1.00 56.94 C ANISOU 2821 CB PRO B 168 7895 6740 6999 927 -228 515 C ATOM 2822 CG PRO B 168 -7.900 2.595 -9.027 1.00 62.18 C ANISOU 2822 CG PRO B 168 8486 7510 7628 1012 -167 443 C ATOM 2823 CD PRO B 168 -7.107 3.815 -8.662 1.00 57.90 C ANISOU 2823 CD PRO B 168 7719 7184 7095 907 -135 301 C ATOM 2824 N SER B 169 -11.551 5.105 -7.599 1.00 55.53 N ANISOU 2824 N SER B 169 7698 6452 6949 617 -271 529 N ATOM 2825 CA SER B 169 -12.422 5.747 -6.638 1.00 54.49 C ANISOU 2825 CA SER B 169 7526 6335 6843 566 -297 540 C ATOM 2826 C SER B 169 -13.674 4.891 -6.521 1.00 60.36 C ANISOU 2826 C SER B 169 8374 6991 7568 583 -364 646 C ATOM 2827 O SER B 169 -14.102 4.302 -7.528 1.00 56.55 O ANISOU 2827 O SER B 169 8009 6408 7070 567 -369 696 O ATOM 2828 CB SER B 169 -12.737 7.182 -7.108 1.00 55.07 C ANISOU 2828 CB SER B 169 7613 6339 6973 458 -223 503 C ATOM 2829 OG SER B 169 -13.996 7.334 -7.753 1.00 56.29 O ANISOU 2829 OG SER B 169 7873 6374 7141 449 -246 598 O ATOM 2830 N LYS B 170 -14.247 4.804 -5.282 1.00 62.05 N ANISOU 2830 N LYS B 170 8546 7261 7770 591 -403 665 N ATOM 2831 CA LYS B 170 -15.450 4.015 -5.003 1.00 63.90 C ANISOU 2831 CA LYS B 170 8868 7436 7974 570 -446 742 C ATOM 2832 C LYS B 170 -16.671 4.638 -5.670 1.00 70.06 C ANISOU 2832 C LYS B 170 9661 8174 8783 481 -456 768 C ATOM 2833 O LYS B 170 -16.978 5.793 -5.414 1.00 69.97 O ANISOU 2833 O LYS B 170 9576 8193 8818 466 -440 747 O ATOM 2834 CB LYS B 170 -15.711 3.874 -3.486 1.00 66.51 C ANISOU 2834 CB LYS B 170 9145 7850 8274 595 -472 749 C ATOM 2835 CG LYS B 170 -14.828 2.879 -2.764 1.00 83.03 C ANISOU 2835 CG LYS B 170 11265 9997 10286 729 -475 771 C ATOM 2836 CD LYS B 170 -15.483 2.437 -1.452 1.00 92.37 C ANISOU 2836 CD LYS B 170 12474 11212 11412 740 -495 815 C ATOM 2837 CE LYS B 170 -14.490 1.950 -0.420 1.00 98.84 C ANISOU 2837 CE LYS B 170 13256 12166 12133 909 -505 829 C ATOM 2838 NZ LYS B 170 -13.920 3.079 0.367 1.00102.03 N ANISOU 2838 NZ LYS B 170 13441 12783 12545 891 -529 732 N ATOM 2839 N GLN B 171 -17.360 3.871 -6.519 1.00 69.58 N ANISOU 2839 N GLN B 171 9697 8061 8679 430 -472 808 N ATOM 2840 CA GLN B 171 -18.604 4.264 -7.182 1.00 70.62 C ANISOU 2840 CA GLN B 171 9812 8227 8794 363 -499 834 C ATOM 2841 C GLN B 171 -19.740 4.102 -6.140 1.00 77.92 C ANISOU 2841 C GLN B 171 10681 9229 9695 313 -529 844 C ATOM 2842 O GLN B 171 -19.493 3.647 -5.013 1.00 77.31 O ANISOU 2842 O GLN B 171 10615 9145 9616 324 -521 838 O ATOM 2843 CB GLN B 171 -18.929 3.356 -8.396 1.00 72.46 C ANISOU 2843 CB GLN B 171 10149 8430 8954 286 -503 843 C ATOM 2844 CG GLN B 171 -17.813 3.061 -9.393 1.00 88.40 C ANISOU 2844 CG GLN B 171 12257 10358 10974 317 -463 828 C ATOM 2845 CD GLN B 171 -18.151 1.945 -10.388 1.00104.40 C ANISOU 2845 CD GLN B 171 14412 12341 12912 215 -447 819 C ATOM 2846 OE1 GLN B 171 -17.613 1.887 -11.498 1.00 96.15 O ANISOU 2846 OE1 GLN B 171 13432 11251 11852 216 -420 807 O ATOM 2847 NE2 GLN B 171 -19.009 1.000 -10.014 1.00 97.40 N ANISOU 2847 NE2 GLN B 171 13586 11466 11958 100 -443 808 N ATOM 2848 N SER B 172 -20.992 4.401 -6.553 1.00 77.20 N ANISOU 2848 N SER B 172 10529 9238 9567 264 -561 860 N ATOM 2849 CA SER B 172 -22.215 4.309 -5.740 1.00 77.85 C ANISOU 2849 CA SER B 172 10527 9439 9613 201 -584 856 C ATOM 2850 C SER B 172 -22.350 2.957 -5.004 1.00 80.87 C ANISOU 2850 C SER B 172 11006 9779 9939 84 -560 834 C ATOM 2851 O SER B 172 -22.767 2.933 -3.842 1.00 80.92 O ANISOU 2851 O SER B 172 10976 9825 9947 64 -552 828 O ATOM 2852 CB SER B 172 -23.444 4.554 -6.618 1.00 81.52 C ANISOU 2852 CB SER B 172 10900 10074 10001 166 -625 865 C ATOM 2853 OG SER B 172 -23.586 3.527 -7.587 1.00 86.86 O ANISOU 2853 OG SER B 172 11653 10765 10586 35 -631 839 O ATOM 2854 N ASN B 173 -21.947 1.855 -5.691 1.00 75.91 N ANISOU 2854 N ASN B 173 10534 9050 9257 15 -526 825 N ATOM 2855 CA ASN B 173 -22.018 0.445 -5.278 1.00 75.05 C ANISOU 2855 CA ASN B 173 10605 8839 9073 -94 -456 812 C ATOM 2856 C ASN B 173 -20.756 -0.096 -4.576 1.00 76.40 C ANISOU 2856 C ASN B 173 10913 8853 9262 49 -409 853 C ATOM 2857 O ASN B 173 -20.545 -1.319 -4.540 1.00 76.51 O ANISOU 2857 O ASN B 173 11143 8723 9203 17 -322 864 O ATOM 2858 CB ASN B 173 -22.342 -0.415 -6.512 1.00 75.05 C ANISOU 2858 CB ASN B 173 10721 8809 8984 -251 -415 769 C ATOM 2859 CG ASN B 173 -21.262 -0.448 -7.584 1.00 87.76 C ANISOU 2859 CG ASN B 173 12412 10312 10621 -158 -406 781 C ATOM 2860 OD1 ASN B 173 -20.231 0.244 -7.516 1.00 77.12 O ANISOU 2860 OD1 ASN B 173 11014 8928 9359 20 -431 817 O ATOM 2861 ND2 ASN B 173 -21.484 -1.260 -8.611 1.00 80.33 N ANISOU 2861 ND2 ASN B 173 11595 9332 9593 -303 -355 734 N ATOM 2862 N ASN B 174 -19.900 0.822 -4.079 1.00 71.21 N ANISOU 2862 N ASN B 174 10136 8237 8683 211 -451 869 N ATOM 2863 CA ASN B 174 -18.643 0.569 -3.362 1.00 71.44 C ANISOU 2863 CA ASN B 174 10207 8226 8712 378 -434 896 C ATOM 2864 C ASN B 174 -17.604 -0.221 -4.192 1.00 75.47 C ANISOU 2864 C ASN B 174 10857 8622 9194 471 -385 911 C ATOM 2865 O ASN B 174 -16.554 -0.609 -3.657 1.00 76.98 O ANISOU 2865 O ASN B 174 11084 8810 9356 645 -365 941 O ATOM 2866 CB ASN B 174 -18.883 -0.063 -1.954 1.00 74.27 C ANISOU 2866 CB ASN B 174 10639 8579 9003 399 -406 933 C ATOM 2867 CG ASN B 174 -19.476 0.938 -0.967 1.00 83.99 C ANISOU 2867 CG ASN B 174 11691 9949 10272 365 -455 908 C ATOM 2868 OD1 ASN B 174 -18.873 1.971 -0.649 1.00 80.47 O ANISOU 2868 OD1 ASN B 174 11090 9600 9886 442 -493 877 O ATOM 2869 ND2 ASN B 174 -20.685 0.683 -0.488 1.00 65.76 N ANISOU 2869 ND2 ASN B 174 9402 7658 7926 228 -436 904 N ATOM 2870 N LYS B 175 -17.872 -0.403 -5.508 1.00 69.47 N ANISOU 2870 N LYS B 175 10159 7802 8434 373 -368 887 N ATOM 2871 CA LYS B 175 -16.936 -0.989 -6.467 1.00 68.85 C ANISOU 2871 CA LYS B 175 10201 7620 8339 444 -315 886 C ATOM 2872 C LYS B 175 -16.145 0.191 -7.045 1.00 68.02 C ANISOU 2872 C LYS B 175 9922 7608 8315 512 -363 853 C ATOM 2873 O LYS B 175 -16.497 1.341 -6.784 1.00 66.99 O ANISOU 2873 O LYS B 175 9632 7580 8242 480 -416 836 O ATOM 2874 CB LYS B 175 -17.649 -1.800 -7.568 1.00 72.45 C ANISOU 2874 CB LYS B 175 10821 7974 8732 269 -256 858 C ATOM 2875 CG LYS B 175 -18.010 -3.212 -7.132 1.00 80.73 C ANISOU 2875 CG LYS B 175 12131 8861 9682 205 -139 873 C ATOM 2876 CD LYS B 175 -18.629 -4.006 -8.269 1.00 91.20 C ANISOU 2876 CD LYS B 175 13627 10095 10930 -13 -55 809 C ATOM 2877 CE LYS B 175 -19.855 -4.795 -7.863 1.00101.62 C ANISOU 2877 CE LYS B 175 15085 11375 12151 -258 30 766 C ATOM 2878 NZ LYS B 175 -19.534 -5.896 -6.921 1.00115.49 N ANISOU 2878 NZ LYS B 175 17126 12912 13844 -177 176 821 N ATOM 2879 N TYR B 176 -15.090 -0.071 -7.808 1.00 62.24 N ANISOU 2879 N TYR B 176 9237 6830 7582 600 -322 840 N ATOM 2880 CA TYR B 176 -14.245 1.001 -8.295 1.00 60.26 C ANISOU 2880 CA TYR B 176 8838 6664 7394 640 -337 794 C ATOM 2881 C TYR B 176 -14.392 1.349 -9.792 1.00 60.03 C ANISOU 2881 C TYR B 176 8844 6589 7376 545 -323 772 C ATOM 2882 O TYR B 176 -14.899 0.563 -10.601 1.00 58.14 O ANISOU 2882 O TYR B 176 8745 6263 7083 465 -298 781 O ATOM 2883 CB TYR B 176 -12.782 0.709 -7.947 1.00 62.30 C ANISOU 2883 CB TYR B 176 9053 6984 7634 821 -304 775 C ATOM 2884 CG TYR B 176 -12.473 0.783 -6.468 1.00 66.80 C ANISOU 2884 CG TYR B 176 9517 7686 8180 931 -337 784 C ATOM 2885 CD1 TYR B 176 -12.664 -0.321 -5.637 1.00 71.04 C ANISOU 2885 CD1 TYR B 176 10185 8170 8636 1039 -321 860 C ATOM 2886 CD2 TYR B 176 -11.897 1.923 -5.913 1.00 67.34 C ANISOU 2886 CD2 TYR B 176 9370 7934 8282 926 -364 711 C ATOM 2887 CE1 TYR B 176 -12.330 -0.274 -4.282 1.00 72.88 C ANISOU 2887 CE1 TYR B 176 10321 8550 8818 1162 -355 878 C ATOM 2888 CE2 TYR B 176 -11.573 1.987 -4.561 1.00 68.31 C ANISOU 2888 CE2 TYR B 176 9377 8220 8357 1015 -397 705 C ATOM 2889 CZ TYR B 176 -11.777 0.881 -3.750 1.00 79.16 C ANISOU 2889 CZ TYR B 176 10867 9564 9645 1149 -404 796 C ATOM 2890 OH TYR B 176 -11.438 0.939 -2.418 1.00 80.67 O ANISOU 2890 OH TYR B 176 10946 9942 9765 1255 -442 799 O ATOM 2891 N ALA B 177 -14.018 2.608 -10.103 1.00 55.13 N ANISOU 2891 N ALA B 177 8104 6032 6812 536 -326 739 N ATOM 2892 CA ALA B 177 -13.933 3.203 -11.436 1.00 52.35 C ANISOU 2892 CA ALA B 177 7778 5648 6464 480 -299 726 C ATOM 2893 C ALA B 177 -12.683 4.063 -11.505 1.00 54.80 C ANISOU 2893 C ALA B 177 8000 6003 6818 515 -239 659 C ATOM 2894 O ALA B 177 -12.266 4.662 -10.510 1.00 52.94 O ANISOU 2894 O ALA B 177 7645 5852 6616 537 -233 616 O ATOM 2895 CB ALA B 177 -15.163 4.038 -11.749 1.00 52.09 C ANISOU 2895 CB ALA B 177 7727 5639 6426 411 -340 769 C ATOM 2896 N ALA B 178 -12.054 4.070 -12.679 1.00 51.97 N ANISOU 2896 N ALA B 178 7699 5602 6444 497 -182 632 N ATOM 2897 CA ALA B 178 -10.897 4.909 -13.017 1.00 50.89 C ANISOU 2897 CA ALA B 178 7496 5506 6333 480 -96 549 C ATOM 2898 C ALA B 178 -10.948 5.157 -14.519 1.00 53.09 C ANISOU 2898 C ALA B 178 7893 5696 6582 418 -46 563 C ATOM 2899 O ALA B 178 -11.849 4.669 -15.196 1.00 52.36 O ANISOU 2899 O ALA B 178 7905 5547 6442 397 -93 631 O ATOM 2900 CB ALA B 178 -9.600 4.224 -12.636 1.00 51.78 C ANISOU 2900 CB ALA B 178 7520 5723 6430 575 -66 477 C ATOM 2901 N SER B 179 -10.021 5.926 -15.035 1.00 49.58 N ANISOU 2901 N SER B 179 7432 5259 6148 369 56 491 N ATOM 2902 CA SER B 179 -9.950 6.124 -16.476 1.00 50.10 C ANISOU 2902 CA SER B 179 7624 5241 6169 316 118 505 C ATOM 2903 C SER B 179 -8.523 6.419 -16.863 1.00 53.35 C ANISOU 2903 C SER B 179 7987 5697 6584 271 242 386 C ATOM 2904 O SER B 179 -7.815 7.109 -16.138 1.00 51.91 O ANISOU 2904 O SER B 179 7686 5603 6436 226 306 291 O ATOM 2905 CB SER B 179 -10.916 7.211 -16.969 1.00 50.54 C ANISOU 2905 CB SER B 179 7782 5219 6202 283 130 591 C ATOM 2906 OG SER B 179 -10.290 8.476 -16.908 1.00 68.44 O ANISOU 2906 OG SER B 179 10060 7448 8497 220 265 532 O ATOM 2907 N SER B 180 -8.091 5.847 -17.983 1.00 50.83 N ANISOU 2907 N SER B 180 7748 5345 6221 266 283 373 N ATOM 2908 CA SER B 180 -6.768 6.119 -18.531 1.00 49.87 C ANISOU 2908 CA SER B 180 7582 5277 6088 210 415 253 C ATOM 2909 C SER B 180 -6.992 6.920 -19.805 1.00 53.27 C ANISOU 2909 C SER B 180 8187 5582 6473 105 505 288 C ATOM 2910 O SER B 180 -7.922 6.635 -20.562 1.00 52.89 O ANISOU 2910 O SER B 180 8277 5447 6371 126 443 396 O ATOM 2911 CB SER B 180 -6.011 4.817 -18.790 1.00 51.02 C ANISOU 2911 CB SER B 180 7690 5486 6209 313 414 210 C ATOM 2912 OG SER B 180 -4.628 5.072 -18.973 1.00 57.11 O ANISOU 2912 OG SER B 180 8336 6393 6971 282 533 69 O ATOM 2913 N TYR B 181 -6.200 7.961 -20.010 1.00 50.39 N ANISOU 2913 N TYR B 181 7821 5218 6108 -15 660 194 N ATOM 2914 CA TYR B 181 -6.369 8.791 -21.179 1.00 50.52 C ANISOU 2914 CA TYR B 181 8040 5091 6063 -100 774 239 C ATOM 2915 C TYR B 181 -5.033 9.082 -21.818 1.00 56.50 C ANISOU 2915 C TYR B 181 8784 5887 6795 -233 954 91 C ATOM 2916 O TYR B 181 -4.012 9.202 -21.136 1.00 57.65 O ANISOU 2916 O TYR B 181 8744 6186 6974 -303 1026 -68 O ATOM 2917 CB TYR B 181 -7.243 10.046 -20.921 1.00 52.20 C ANISOU 2917 CB TYR B 181 8386 5175 6275 -113 815 332 C ATOM 2918 CG TYR B 181 -6.799 10.954 -19.796 1.00 55.76 C ANISOU 2918 CG TYR B 181 8751 5649 6787 -206 916 224 C ATOM 2919 CD1 TYR B 181 -7.103 10.653 -18.466 1.00 57.03 C ANISOU 2919 CD1 TYR B 181 8739 5916 7013 -145 796 211 C ATOM 2920 CD2 TYR B 181 -6.079 12.113 -20.055 1.00 58.96 C ANISOU 2920 CD2 TYR B 181 9262 5969 7170 -379 1150 122 C ATOM 2921 CE1 TYR B 181 -6.696 11.486 -17.426 1.00 55.19 C ANISOU 2921 CE1 TYR B 181 8422 5727 6819 -252 892 94 C ATOM 2922 CE2 TYR B 181 -5.701 12.978 -19.024 1.00 60.79 C ANISOU 2922 CE2 TYR B 181 9432 6223 7442 -509 1269 -4 C ATOM 2923 CZ TYR B 181 -5.994 12.648 -17.713 1.00 64.17 C ANISOU 2923 CZ TYR B 181 9665 6784 7932 -445 1131 -23 C ATOM 2924 OH TYR B 181 -5.562 13.469 -16.706 1.00 70.74 O ANISOU 2924 OH TYR B 181 10423 7669 8786 -598 1253 -171 O ATOM 2925 N LEU B 182 -5.015 9.016 -23.143 1.00 54.34 N ANISOU 2925 N LEU B 182 8677 5524 6446 -261 1014 132 N ATOM 2926 CA LEU B 182 -3.799 9.228 -23.903 1.00 57.52 C ANISOU 2926 CA LEU B 182 9085 5959 6810 -396 1196 -6 C ATOM 2927 C LEU B 182 -4.011 10.367 -24.896 1.00 65.92 C ANISOU 2927 C LEU B 182 10421 6832 7791 -506 1360 55 C ATOM 2928 O LEU B 182 -4.781 10.242 -25.852 1.00 66.86 O ANISOU 2928 O LEU B 182 10727 6849 7828 -436 1311 201 O ATOM 2929 CB LEU B 182 -3.317 7.911 -24.576 1.00 57.17 C ANISOU 2929 CB LEU B 182 8985 5998 6739 -322 1148 -41 C ATOM 2930 CG LEU B 182 -2.231 7.977 -25.687 1.00 63.17 C ANISOU 2930 CG LEU B 182 9786 6781 7437 -442 1328 -160 C ATOM 2931 CD1 LEU B 182 -0.931 8.622 -25.202 1.00 64.27 C ANISOU 2931 CD1 LEU B 182 9742 7082 7598 -593 1497 -368 C ATOM 2932 CD2 LEU B 182 -1.951 6.581 -26.249 1.00 63.55 C ANISOU 2932 CD2 LEU B 182 9800 6886 7462 -328 1270 -175 C ATOM 2933 N SER B 183 -3.353 11.482 -24.639 1.00 64.23 N ANISOU 2933 N SER B 183 10240 6582 7583 -680 1565 -59 N ATOM 2934 CA SER B 183 -3.440 12.647 -25.501 1.00 66.34 C ANISOU 2934 CA SER B 183 10812 6632 7761 -790 1778 -8 C ATOM 2935 C SER B 183 -2.393 12.517 -26.621 1.00 72.90 C ANISOU 2935 C SER B 183 11691 7489 8520 -937 1942 -123 C ATOM 2936 O SER B 183 -1.230 12.201 -26.354 1.00 72.91 O ANISOU 2936 O SER B 183 11467 7682 8555 -1063 2014 -333 O ATOM 2937 CB SER B 183 -3.254 13.924 -24.684 1.00 71.63 C ANISOU 2937 CB SER B 183 11547 7209 8460 -942 1968 -91 C ATOM 2938 OG SER B 183 -3.925 15.005 -25.312 1.00 83.64 O ANISOU 2938 OG SER B 183 13436 8448 9895 -924 2121 62 O ATOM 2939 N LEU B 184 -2.841 12.671 -27.876 1.00 71.62 N ANISOU 2939 N LEU B 184 11797 7172 8243 -897 1984 19 N ATOM 2940 CA LEU B 184 -2.031 12.576 -29.095 1.00 73.99 C ANISOU 2940 CA LEU B 184 12198 7463 8451 -1023 2141 -55 C ATOM 2941 C LEU B 184 -2.394 13.726 -30.012 1.00 79.84 C ANISOU 2941 C LEU B 184 13332 7948 9057 -1069 2338 76 C ATOM 2942 O LEU B 184 -3.357 14.456 -29.758 1.00 78.97 O ANISOU 2942 O LEU B 184 13406 7681 8920 -948 2324 247 O ATOM 2943 CB LEU B 184 -2.336 11.288 -29.895 1.00 73.72 C ANISOU 2943 CB LEU B 184 12121 7514 8373 -882 1955 18 C ATOM 2944 CG LEU B 184 -2.185 9.937 -29.259 1.00 78.41 C ANISOU 2944 CG LEU B 184 12423 8304 9064 -770 1759 -51 C ATOM 2945 CD1 LEU B 184 -3.110 8.938 -29.943 1.00 77.62 C ANISOU 2945 CD1 LEU B 184 12399 8195 8898 -623 1574 90 C ATOM 2946 CD2 LEU B 184 -0.725 9.470 -29.284 1.00 82.76 C ANISOU 2946 CD2 LEU B 184 12767 9031 9647 -876 1880 -280 C ATOM 2947 N THR B 185 -1.659 13.842 -31.119 1.00 78.97 N ANISOU 2947 N THR B 185 13363 7796 8845 -1212 2524 12 N ATOM 2948 CA THR B 185 -1.950 14.833 -32.156 1.00 81.15 C ANISOU 2948 CA THR B 185 14052 7824 8959 -1236 2727 155 C ATOM 2949 C THR B 185 -2.858 14.141 -33.188 1.00 85.73 C ANISOU 2949 C THR B 185 14730 8431 9412 -1018 2527 363 C ATOM 2950 O THR B 185 -2.773 12.912 -33.309 1.00 84.26 O ANISOU 2950 O THR B 185 14314 8436 9267 -973 2338 306 O ATOM 2951 CB THR B 185 -0.649 15.375 -32.801 1.00 85.87 C ANISOU 2951 CB THR B 185 14765 8368 9494 -1542 3063 -41 C ATOM 2952 OG1 THR B 185 0.100 14.295 -33.361 1.00 87.07 O ANISOU 2952 OG1 THR B 185 14701 8732 9651 -1593 2999 -174 O ATOM 2953 CG2 THR B 185 0.206 16.194 -31.828 1.00 80.03 C ANISOU 2953 CG2 THR B 185 13945 7625 8839 -1810 3295 -271 C ATOM 2954 N PRO B 186 -3.717 14.866 -33.952 1.00 84.91 N ANISOU 2954 N PRO B 186 14967 8158 9137 -876 2573 598 N ATOM 2955 CA PRO B 186 -4.524 14.186 -34.983 1.00 84.98 C ANISOU 2955 CA PRO B 186 15032 8268 8990 -698 2381 768 C ATOM 2956 C PRO B 186 -3.691 13.311 -35.942 1.00 89.86 C ANISOU 2956 C PRO B 186 15585 8996 9562 -846 2411 629 C ATOM 2957 O PRO B 186 -4.198 12.289 -36.408 1.00 87.80 O ANISOU 2957 O PRO B 186 15219 8894 9246 -752 2199 671 O ATOM 2958 CB PRO B 186 -5.202 15.353 -35.725 1.00 88.58 C ANISOU 2958 CB PRO B 186 15898 8524 9235 -552 2522 1012 C ATOM 2959 CG PRO B 186 -5.265 16.443 -34.726 1.00 93.21 C ANISOU 2959 CG PRO B 186 16594 8911 9910 -549 2678 1025 C ATOM 2960 CD PRO B 186 -3.977 16.324 -33.958 1.00 88.22 C ANISOU 2960 CD PRO B 186 15751 8299 9469 -859 2818 722 C ATOM 2961 N GLU B 187 -2.407 13.694 -36.199 1.00 88.84 N ANISOU 2961 N GLU B 187 15511 8794 9452 -1095 2688 443 N ATOM 2962 CA GLU B 187 -1.466 12.990 -37.091 1.00 89.55 C ANISOU 2962 CA GLU B 187 15545 8982 9500 -1250 2769 287 C ATOM 2963 C GLU B 187 -0.992 11.670 -36.502 1.00 90.47 C ANISOU 2963 C GLU B 187 15272 9324 9777 -1250 2598 109 C ATOM 2964 O GLU B 187 -0.938 10.679 -37.227 1.00 89.92 O ANISOU 2964 O GLU B 187 15154 9358 9655 -1223 2511 85 O ATOM 2965 CB GLU B 187 -0.254 13.873 -37.479 1.00 93.48 C ANISOU 2965 CB GLU B 187 16204 9356 9958 -1531 3137 128 C ATOM 2966 CG GLU B 187 -0.614 15.209 -38.110 1.00108.55 C ANISOU 2966 CG GLU B 187 18572 10985 11686 -1537 3371 306 C ATOM 2967 CD GLU B 187 0.370 16.326 -37.821 1.00140.48 C ANISOU 2967 CD GLU B 187 22767 14858 15751 -1832 3748 137 C ATOM 2968 OE1 GLU B 187 0.595 16.631 -36.626 1.00139.46 O ANISOU 2968 OE1 GLU B 187 22466 14745 15776 -1914 3773 13 O ATOM 2969 OE2 GLU B 187 0.897 16.915 -38.793 1.00138.79 O ANISOU 2969 OE2 GLU B 187 22856 14496 15383 -2000 4033 121 O ATOM 2970 N GLN B 188 -0.644 11.654 -35.196 1.00 86.18 N ANISOU 2970 N GLN B 188 14473 8855 9415 -1271 2565 -13 N ATOM 2971 CA GLN B 188 -0.216 10.451 -34.454 1.00 83.64 C ANISOU 2971 CA GLN B 188 13792 8746 9239 -1216 2408 -158 C ATOM 2972 C GLN B 188 -1.327 9.390 -34.450 1.00 82.88 C ANISOU 2972 C GLN B 188 13653 8699 9139 -1001 2121 -14 C ATOM 2973 O GLN B 188 -1.047 8.197 -34.617 1.00 82.70 O ANISOU 2973 O GLN B 188 13492 8787 9141 -956 2041 -94 O ATOM 2974 CB GLN B 188 0.171 10.810 -33.009 1.00 84.66 C ANISOU 2974 CB GLN B 188 13688 8955 9524 -1252 2414 -274 C ATOM 2975 CG GLN B 188 1.529 11.500 -32.872 1.00 97.89 C ANISOU 2975 CG GLN B 188 15282 10699 11214 -1513 2692 -513 C ATOM 2976 CD GLN B 188 1.756 12.050 -31.485 1.00109.98 C ANISOU 2976 CD GLN B 188 16622 12310 12856 -1579 2709 -619 C ATOM 2977 OE1 GLN B 188 0.908 12.733 -30.901 1.00104.83 O ANISOU 2977 OE1 GLN B 188 16097 11508 12227 -1526 2666 -490 O ATOM 2978 NE2 GLN B 188 2.929 11.795 -30.938 1.00101.26 N ANISOU 2978 NE2 GLN B 188 15201 11469 11806 -1696 2783 -867 N ATOM 2979 N TRP B 189 -2.588 9.839 -34.280 1.00 75.76 N ANISOU 2979 N TRP B 189 12881 7715 8189 -874 1989 191 N ATOM 2980 CA TRP B 189 -3.785 8.997 -34.288 1.00 72.32 C ANISOU 2980 CA TRP B 189 12412 7349 7716 -709 1732 323 C ATOM 2981 C TRP B 189 -3.996 8.346 -35.663 1.00 78.99 C ANISOU 2981 C TRP B 189 13392 8233 8388 -727 1713 355 C ATOM 2982 O TRP B 189 -4.108 7.118 -35.735 1.00 79.07 O ANISOU 2982 O TRP B 189 13294 8337 8414 -706 1598 294 O ATOM 2983 CB TRP B 189 -5.015 9.816 -33.830 1.00 69.18 C ANISOU 2983 CB TRP B 189 12107 6895 7284 -572 1628 523 C ATOM 2984 CG TRP B 189 -6.362 9.203 -34.109 1.00 68.52 C ANISOU 2984 CG TRP B 189 12023 6921 7092 -429 1393 670 C ATOM 2985 CD1 TRP B 189 -7.359 9.740 -34.872 1.00 72.15 C ANISOU 2985 CD1 TRP B 189 12662 7399 7352 -319 1342 862 C ATOM 2986 CD2 TRP B 189 -6.889 7.967 -33.566 1.00 66.37 C ANISOU 2986 CD2 TRP B 189 11552 6779 6886 -386 1187 630 C ATOM 2987 NE1 TRP B 189 -8.459 8.903 -34.873 1.00 70.91 N ANISOU 2987 NE1 TRP B 189 12394 7423 7127 -236 1109 921 N ATOM 2988 CE2 TRP B 189 -8.198 7.812 -34.072 1.00 70.21 C ANISOU 2988 CE2 TRP B 189 12092 7380 7205 -296 1024 776 C ATOM 2989 CE3 TRP B 189 -6.377 6.979 -32.709 1.00 66.19 C ANISOU 2989 CE3 TRP B 189 11325 6794 7028 -407 1141 488 C ATOM 2990 CZ2 TRP B 189 -9.016 6.734 -33.712 1.00 68.16 C ANISOU 2990 CZ2 TRP B 189 11690 7259 6947 -279 832 759 C ATOM 2991 CZ3 TRP B 189 -7.159 5.861 -32.425 1.00 67.06 C ANISOU 2991 CZ3 TRP B 189 11345 6996 7138 -364 965 493 C ATOM 2992 CH2 TRP B 189 -8.467 5.754 -32.914 1.00 67.89 C ANISOU 2992 CH2 TRP B 189 11509 7202 7084 -328 821 615 C ATOM 2993 N LYS B 190 -4.012 9.163 -36.746 1.00 78.72 N ANISOU 2993 N LYS B 190 13616 8117 8178 -772 1850 444 N ATOM 2994 CA LYS B 190 -4.224 8.725 -38.141 1.00 80.18 C ANISOU 2994 CA LYS B 190 13956 8352 8157 -799 1848 485 C ATOM 2995 C LYS B 190 -3.094 7.847 -38.706 1.00 87.05 C ANISOU 2995 C LYS B 190 14763 9257 9054 -941 1965 281 C ATOM 2996 O LYS B 190 -3.362 6.998 -39.566 1.00 87.99 O ANISOU 2996 O LYS B 190 14928 9455 9051 -958 1904 270 O ATOM 2997 CB LYS B 190 -4.491 9.927 -39.065 1.00 84.03 C ANISOU 2997 CB LYS B 190 14757 8736 8435 -779 1982 652 C ATOM 2998 CG LYS B 190 -5.832 10.614 -38.829 1.00 95.93 C ANISOU 2998 CG LYS B 190 16355 10255 9839 -566 1841 893 C ATOM 2999 CD LYS B 190 -5.836 12.031 -39.392 0.50105.71 C ANISOU 2999 CD LYS B 190 17931 11313 10919 -514 2049 1054 C ATOM 3000 CE LYS B 190 -7.018 12.841 -38.913 0.50112.59 C ANISOU 3000 CE LYS B 190 18885 12167 11726 -260 1952 1285 C ATOM 3001 NZ LYS B 190 -6.929 14.259 -39.354 0.50121.03 N ANISOU 3001 NZ LYS B 190 20336 12999 12651 -188 2208 1445 N ATOM 3002 N SER B 191 -1.843 8.055 -38.228 1.00 84.73 N ANISOU 3002 N SER B 191 14355 8933 8906 -1046 2141 108 N ATOM 3003 CA SER B 191 -0.634 7.338 -38.665 1.00 85.52 C ANISOU 3003 CA SER B 191 14361 9093 9038 -1155 2281 -98 C ATOM 3004 C SER B 191 -0.673 5.836 -38.377 1.00 88.39 C ANISOU 3004 C SER B 191 14548 9556 9480 -1061 2140 -181 C ATOM 3005 O SER B 191 -0.307 5.040 -39.238 1.00 90.15 O ANISOU 3005 O SER B 191 14819 9806 9630 -1104 2200 -266 O ATOM 3006 CB SER B 191 0.616 7.956 -38.038 1.00 89.21 C ANISOU 3006 CB SER B 191 14688 9578 9630 -1274 2480 -269 C ATOM 3007 OG SER B 191 0.831 7.463 -36.724 1.00 93.68 O ANISOU 3007 OG SER B 191 14963 10251 10381 -1179 2370 -352 O ATOM 3008 N HIS B 192 -1.102 5.458 -37.160 1.00 82.16 N ANISOU 3008 N HIS B 192 13582 8801 8833 -935 1977 -159 N ATOM 3009 CA HIS B 192 -1.176 4.070 -36.694 1.00 79.22 C ANISOU 3009 CA HIS B 192 13078 8481 8541 -826 1866 -222 C ATOM 3010 C HIS B 192 -2.409 3.322 -37.172 1.00 79.92 C ANISOU 3010 C HIS B 192 13294 8559 8513 -805 1708 -123 C ATOM 3011 O HIS B 192 -3.452 3.932 -37.422 1.00 78.06 O ANISOU 3011 O HIS B 192 13165 8327 8167 -811 1604 27 O ATOM 3012 CB HIS B 192 -1.082 4.019 -35.165 1.00 78.18 C ANISOU 3012 CB HIS B 192 12719 8395 8590 -708 1778 -239 C ATOM 3013 CG HIS B 192 0.266 4.399 -34.648 1.00 81.96 C ANISOU 3013 CG HIS B 192 13005 8967 9168 -733 1929 -394 C ATOM 3014 ND1 HIS B 192 0.535 5.686 -34.209 1.00 84.04 N ANISOU 3014 ND1 HIS B 192 13234 9234 9463 -833 2009 -401 N ATOM 3015 CD2 HIS B 192 1.388 3.654 -34.539 1.00 84.21 C ANISOU 3015 CD2 HIS B 192 13123 9368 9505 -673 2025 -555 C ATOM 3016 CE1 HIS B 192 1.798 5.674 -33.820 1.00 84.24 C ANISOU 3016 CE1 HIS B 192 13043 9410 9554 -866 2139 -584 C ATOM 3017 NE2 HIS B 192 2.355 4.475 -34.009 1.00 85.02 N ANISOU 3017 NE2 HIS B 192 13041 9599 9664 -750 2145 -675 N ATOM 3018 N ARG B 193 -2.288 1.990 -37.282 1.00 77.06 N ANISOU 3018 N ARG B 193 12923 8197 8160 -776 1706 -216 N ATOM 3019 CA ARG B 193 -3.390 1.118 -37.691 1.00 77.85 C ANISOU 3019 CA ARG B 193 13138 8298 8142 -808 1588 -176 C ATOM 3020 C ARG B 193 -4.406 1.013 -36.546 1.00 80.32 C ANISOU 3020 C ARG B 193 13357 8629 8532 -725 1399 -82 C ATOM 3021 O ARG B 193 -5.616 0.982 -36.798 1.00 80.01 O ANISOU 3021 O ARG B 193 13378 8654 8367 -775 1263 4 O ATOM 3022 CB ARG B 193 -2.878 -0.275 -38.086 1.00 80.28 C ANISOU 3022 CB ARG B 193 13508 8554 8442 -816 1697 -323 C ATOM 3023 CG ARG B 193 -2.464 -0.387 -39.562 1.00 98.93 C ANISOU 3023 CG ARG B 193 16033 10917 10638 -953 1840 -398 C ATOM 3024 CD ARG B 193 -1.001 -0.051 -39.816 1.00108.88 C ANISOU 3024 CD ARG B 193 17231 12174 11963 -937 2040 -507 C ATOM 3025 NE ARG B 193 -0.105 -1.084 -39.291 1.00115.58 N ANISOU 3025 NE ARG B 193 17986 12991 12940 -796 2143 -638 N ATOM 3026 CZ ARG B 193 1.179 -0.892 -39.004 1.00130.27 C ANISOU 3026 CZ ARG B 193 19682 14915 14901 -710 2280 -740 C ATOM 3027 NH1 ARG B 193 1.738 0.300 -39.185 1.00121.19 N ANISOU 3027 NH1 ARG B 193 18457 13841 13747 -805 2350 -749 N ATOM 3028 NH2 ARG B 193 1.912 -1.886 -38.520 1.00112.88 N ANISOU 3028 NH2 ARG B 193 17391 12712 12786 -524 2362 -837 N ATOM 3029 N SER B 194 -3.904 0.990 -35.285 1.00 74.08 N ANISOU 3029 N SER B 194 12398 7817 7932 -598 1391 -106 N ATOM 3030 CA SER B 194 -4.721 0.901 -34.070 1.00 70.49 C ANISOU 3030 CA SER B 194 11844 7372 7567 -512 1232 -28 C ATOM 3031 C SER B 194 -3.976 1.298 -32.790 1.00 70.92 C ANISOU 3031 C SER B 194 11703 7441 7804 -386 1243 -48 C ATOM 3032 O SER B 194 -2.756 1.446 -32.779 1.00 70.01 O ANISOU 3032 O SER B 194 11500 7353 7747 -359 1377 -148 O ATOM 3033 CB SER B 194 -5.289 -0.506 -33.921 1.00 70.84 C ANISOU 3033 CB SER B 194 11958 7371 7587 -513 1192 -69 C ATOM 3034 OG SER B 194 -4.266 -1.394 -33.516 1.00 76.86 O ANISOU 3034 OG SER B 194 12693 8060 8450 -396 1314 -173 O ATOM 3035 N TYR B 195 -4.739 1.451 -31.705 1.00 66.29 N ANISOU 3035 N TYR B 195 11030 6869 7289 -320 1102 35 N ATOM 3036 CA TYR B 195 -4.252 1.723 -30.359 1.00 64.50 C ANISOU 3036 CA TYR B 195 10613 6680 7215 -205 1081 21 C ATOM 3037 C TYR B 195 -4.909 0.735 -29.414 1.00 63.09 C ANISOU 3037 C TYR B 195 10412 6474 7084 -107 971 53 C ATOM 3038 O TYR B 195 -6.070 0.380 -29.599 1.00 61.31 O ANISOU 3038 O TYR B 195 10288 6223 6786 -171 874 117 O ATOM 3039 CB TYR B 195 -4.562 3.168 -29.938 1.00 65.02 C ANISOU 3039 CB TYR B 195 10624 6770 7309 -241 1043 98 C ATOM 3040 CG TYR B 195 -3.585 4.184 -30.481 1.00 68.05 C ANISOU 3040 CG TYR B 195 11013 7163 7679 -333 1208 34 C ATOM 3041 CD1 TYR B 195 -3.758 4.742 -31.743 1.00 70.62 C ANISOU 3041 CD1 TYR B 195 11525 7435 7871 -439 1281 78 C ATOM 3042 CD2 TYR B 195 -2.510 4.624 -29.715 1.00 69.98 C ANISOU 3042 CD2 TYR B 195 11078 7488 8023 -330 1299 -77 C ATOM 3043 CE1 TYR B 195 -2.865 5.688 -32.246 1.00 72.04 C ANISOU 3043 CE1 TYR B 195 11748 7597 8026 -549 1465 15 C ATOM 3044 CE2 TYR B 195 -1.624 5.588 -30.197 1.00 72.07 C ANISOU 3044 CE2 TYR B 195 11353 7768 8262 -467 1480 -164 C ATOM 3045 CZ TYR B 195 -1.788 6.096 -31.475 1.00 80.23 C ANISOU 3045 CZ TYR B 195 12608 8703 9172 -581 1573 -117 C ATOM 3046 OH TYR B 195 -0.904 7.038 -31.951 1.00 83.00 O ANISOU 3046 OH TYR B 195 13003 9045 9487 -738 1782 -208 O ATOM 3047 N SER B 196 -4.156 0.269 -28.426 1.00 58.65 N ANISOU 3047 N SER B 196 9718 5941 6625 43 996 3 N ATOM 3048 CA SER B 196 -4.631 -0.677 -27.420 1.00 57.00 C ANISOU 3048 CA SER B 196 9510 5688 6459 163 923 39 C ATOM 3049 C SER B 196 -4.422 -0.133 -26.022 1.00 58.61 C ANISOU 3049 C SER B 196 9508 5991 6770 275 851 64 C ATOM 3050 O SER B 196 -3.452 0.590 -25.788 1.00 56.92 O ANISOU 3050 O SER B 196 9127 5898 6601 300 906 0 O ATOM 3051 CB SER B 196 -3.911 -2.011 -27.544 1.00 57.94 C ANISOU 3051 CB SER B 196 9714 5736 6565 299 1043 -31 C ATOM 3052 OG SER B 196 -4.335 -2.651 -28.729 1.00 67.40 O ANISOU 3052 OG SER B 196 11136 6821 7654 166 1108 -60 O ATOM 3053 N CYS B 197 -5.319 -0.526 -25.099 1.00 54.79 N ANISOU 3053 N CYS B 197 9037 5469 6311 319 741 140 N ATOM 3054 CA CYS B 197 -5.315 -0.219 -23.669 1.00 53.88 C ANISOU 3054 CA CYS B 197 8755 5436 6280 428 660 174 C ATOM 3055 C CYS B 197 -5.428 -1.584 -22.946 1.00 54.19 C ANISOU 3055 C CYS B 197 8878 5396 6316 589 665 199 C ATOM 3056 O CYS B 197 -6.426 -2.290 -23.111 1.00 52.49 O ANISOU 3056 O CYS B 197 8844 5050 6051 511 643 240 O ATOM 3057 CB CYS B 197 -6.465 0.726 -23.304 1.00 53.88 C ANISOU 3057 CB CYS B 197 8730 5445 6296 316 537 258 C ATOM 3058 SG CYS B 197 -6.688 0.997 -21.519 1.00 58.35 S ANISOU 3058 SG CYS B 197 9124 6093 6953 424 435 301 S ATOM 3059 N GLN B 198 -4.376 -1.959 -22.207 1.00 50.09 N ANISOU 3059 N GLN B 198 8237 4969 5825 810 712 168 N ATOM 3060 CA GLN B 198 -4.254 -3.189 -21.449 1.00 51.10 C ANISOU 3060 CA GLN B 198 8456 5027 5934 1034 747 209 C ATOM 3061 C GLN B 198 -4.421 -2.881 -19.971 1.00 55.55 C ANISOU 3061 C GLN B 198 8859 5707 6542 1141 637 267 C ATOM 3062 O GLN B 198 -3.593 -2.177 -19.388 1.00 57.01 O ANISOU 3062 O GLN B 198 8788 6119 6756 1223 611 221 O ATOM 3063 CB GLN B 198 -2.896 -3.859 -21.722 1.00 54.56 C ANISOU 3063 CB GLN B 198 8867 5526 6339 1271 885 146 C ATOM 3064 CG GLN B 198 -2.702 -5.211 -21.006 1.00 78.15 C ANISOU 3064 CG GLN B 198 12006 8408 9280 1568 959 211 C ATOM 3065 CD GLN B 198 -1.257 -5.490 -20.622 1.00104.95 C ANISOU 3065 CD GLN B 198 15215 12019 12644 1911 1031 177 C ATOM 3066 OE1 GLN B 198 -0.325 -5.422 -21.436 1.00100.81 O ANISOU 3066 OE1 GLN B 198 14612 11594 12100 1950 1128 83 O ATOM 3067 NE2 GLN B 198 -1.040 -5.854 -19.373 1.00104.71 N ANISOU 3067 NE2 GLN B 198 15106 12091 12588 2182 990 253 N ATOM 3068 N VAL B 199 -5.497 -3.396 -19.371 1.00 49.34 N ANISOU 3068 N VAL B 199 8218 4783 5747 1112 584 350 N ATOM 3069 CA VAL B 199 -5.789 -3.198 -17.960 1.00 47.80 C ANISOU 3069 CA VAL B 199 7907 4673 5581 1202 485 412 C ATOM 3070 C VAL B 199 -5.447 -4.497 -17.205 1.00 54.08 C ANISOU 3070 C VAL B 199 8841 5389 6319 1483 561 474 C ATOM 3071 O VAL B 199 -5.967 -5.552 -17.544 1.00 57.44 O ANISOU 3071 O VAL B 199 9560 5573 6693 1468 655 505 O ATOM 3072 CB VAL B 199 -7.261 -2.736 -17.719 1.00 48.74 C ANISOU 3072 CB VAL B 199 8070 4724 5723 976 376 463 C ATOM 3073 CG1 VAL B 199 -7.559 -2.540 -16.224 1.00 47.32 C ANISOU 3073 CG1 VAL B 199 7776 4631 5572 1065 285 522 C ATOM 3074 CG2 VAL B 199 -7.596 -1.471 -18.521 1.00 46.67 C ANISOU 3074 CG2 VAL B 199 7712 4527 5493 762 323 430 C ATOM 3075 N THR B 200 -4.547 -4.422 -16.221 1.00 51.91 N ANISOU 3075 N THR B 200 8366 5324 6031 1740 536 487 N ATOM 3076 CA THR B 200 -4.178 -5.558 -15.371 1.00 54.61 C ANISOU 3076 CA THR B 200 8828 5627 6295 2074 601 575 C ATOM 3077 C THR B 200 -4.838 -5.392 -13.997 1.00 62.13 C ANISOU 3077 C THR B 200 9731 6627 7247 2094 492 657 C ATOM 3078 O THR B 200 -4.621 -4.379 -13.329 1.00 60.29 O ANISOU 3078 O THR B 200 9203 6655 7050 2058 373 621 O ATOM 3079 CB THR B 200 -2.664 -5.723 -15.266 1.00 59.49 C ANISOU 3079 CB THR B 200 9250 6499 6854 2406 655 540 C ATOM 3080 OG1 THR B 200 -2.123 -5.680 -16.563 1.00 56.70 O ANISOU 3080 OG1 THR B 200 8910 6121 6513 2332 749 445 O ATOM 3081 CG2 THR B 200 -2.252 -7.046 -14.565 1.00 62.37 C ANISOU 3081 CG2 THR B 200 9803 6790 7104 2828 758 659 C ATOM 3082 N HIS B 201 -5.646 -6.393 -13.588 1.00 62.00 N ANISOU 3082 N HIS B 201 10023 6351 7182 2127 555 754 N ATOM 3083 CA HIS B 201 -6.353 -6.395 -12.307 1.00 62.31 C ANISOU 3083 CA HIS B 201 10071 6397 7206 2138 478 838 C ATOM 3084 C HIS B 201 -6.315 -7.789 -11.670 1.00 66.87 C ANISOU 3084 C HIS B 201 10970 6768 7668 2421 618 960 C ATOM 3085 O HIS B 201 -6.861 -8.743 -12.227 1.00 65.31 O ANISOU 3085 O HIS B 201 11138 6243 7433 2338 772 976 O ATOM 3086 CB HIS B 201 -7.798 -5.873 -12.465 1.00 61.47 C ANISOU 3086 CB HIS B 201 10010 6177 7167 1754 402 816 C ATOM 3087 CG HIS B 201 -8.630 -5.954 -11.218 1.00 64.82 C ANISOU 3087 CG HIS B 201 10469 6585 7573 1736 345 892 C ATOM 3088 ND1 HIS B 201 -9.506 -7.004 -11.002 1.00 67.77 N ANISOU 3088 ND1 HIS B 201 11178 6690 7882 1671 451 949 N ATOM 3089 CD2 HIS B 201 -8.671 -5.128 -10.147 1.00 65.76 C ANISOU 3089 CD2 HIS B 201 10342 6923 7720 1759 214 906 C ATOM 3090 CE1 HIS B 201 -10.057 -6.776 -9.820 1.00 66.84 C ANISOU 3090 CE1 HIS B 201 10997 6640 7759 1666 374 1004 C ATOM 3091 NE2 HIS B 201 -9.590 -5.657 -9.270 1.00 65.87 N ANISOU 3091 NE2 HIS B 201 10526 6809 7691 1723 226 982 N ATOM 3092 N GLU B 202 -5.685 -7.886 -10.485 1.00 66.28 N ANISOU 3092 N GLU B 202 10773 6893 7520 2747 576 1043 N ATOM 3093 CA GLU B 202 -5.538 -9.131 -9.708 1.00 68.09 C ANISOU 3093 CA GLU B 202 11302 6960 7611 3096 709 1192 C ATOM 3094 C GLU B 202 -4.944 -10.220 -10.590 1.00 75.45 C ANISOU 3094 C GLU B 202 12534 7658 8475 3313 925 1212 C ATOM 3095 O GLU B 202 -5.575 -11.266 -10.799 1.00 76.32 O ANISOU 3095 O GLU B 202 13094 7370 8535 3269 1113 1265 O ATOM 3096 CB GLU B 202 -6.886 -9.578 -9.085 1.00 68.64 C ANISOU 3096 CB GLU B 202 11667 6750 7665 2892 748 1261 C ATOM 3097 CG GLU B 202 -7.400 -8.678 -7.973 1.00 73.67 C ANISOU 3097 CG GLU B 202 12040 7615 8336 2775 562 1269 C ATOM 3098 CD GLU B 202 -6.509 -8.579 -6.750 1.00 96.29 C ANISOU 3098 CD GLU B 202 14696 10792 11097 3161 484 1354 C ATOM 3099 OE1 GLU B 202 -6.373 -9.591 -6.026 1.00107.03 O ANISOU 3099 OE1 GLU B 202 16323 12029 12313 3479 598 1501 O ATOM 3100 OE2 GLU B 202 -5.920 -7.495 -6.536 1.00 83.69 O ANISOU 3100 OE2 GLU B 202 12678 9575 9544 3147 324 1269 O ATOM 3101 N GLY B 203 -3.798 -9.895 -11.200 1.00 73.46 N ANISOU 3101 N GLY B 203 12033 7647 8231 3480 910 1141 N ATOM 3102 CA GLY B 203 -3.052 -10.767 -12.104 1.00 75.41 C ANISOU 3102 CA GLY B 203 12489 7740 8421 3710 1106 1139 C ATOM 3103 C GLY B 203 -3.743 -11.243 -13.373 1.00 79.83 C ANISOU 3103 C GLY B 203 13391 7908 9031 3388 1258 1064 C ATOM 3104 O GLY B 203 -3.339 -12.258 -13.949 1.00 82.86 O ANISOU 3104 O GLY B 203 14089 8051 9344 3586 1477 1087 O ATOM 3105 N SER B 204 -4.780 -10.529 -13.822 1.00 73.84 N ANISOU 3105 N SER B 204 12578 7100 8378 2904 1153 972 N ATOM 3106 CA SER B 204 -5.523 -10.845 -15.052 1.00 72.59 C ANISOU 3106 CA SER B 204 12681 6654 8246 2545 1263 879 C ATOM 3107 C SER B 204 -5.557 -9.604 -15.921 1.00 70.45 C ANISOU 3107 C SER B 204 12081 6605 8081 2243 1104 753 C ATOM 3108 O SER B 204 -5.733 -8.512 -15.407 1.00 66.59 O ANISOU 3108 O SER B 204 11274 6365 7661 2140 912 743 O ATOM 3109 CB SER B 204 -6.943 -11.292 -14.726 1.00 76.30 C ANISOU 3109 CB SER B 204 13441 6856 8692 2246 1308 899 C ATOM 3110 OG SER B 204 -6.899 -12.390 -13.830 1.00 94.94 O ANISOU 3110 OG SER B 204 16137 8993 10945 2527 1475 1026 O ATOM 3111 N THR B 205 -5.388 -9.773 -17.226 1.00 67.78 N ANISOU 3111 N THR B 205 11848 6161 7743 2107 1204 660 N ATOM 3112 CA THR B 205 -5.382 -8.663 -18.164 1.00 65.91 C ANISOU 3112 CA THR B 205 11358 6104 7582 1842 1086 553 C ATOM 3113 C THR B 205 -6.595 -8.627 -19.062 1.00 66.56 C ANISOU 3113 C THR B 205 11603 6029 7657 1425 1086 488 C ATOM 3114 O THR B 205 -7.065 -9.653 -19.539 1.00 66.44 O ANISOU 3114 O THR B 205 11932 5745 7567 1322 1250 464 O ATOM 3115 CB THR B 205 -4.103 -8.625 -18.988 1.00 78.60 C ANISOU 3115 CB THR B 205 12860 7821 9183 2016 1168 485 C ATOM 3116 OG1 THR B 205 -4.031 -9.825 -19.768 1.00 89.78 O ANISOU 3116 OG1 THR B 205 14647 8943 10524 2065 1392 465 O ATOM 3117 CG2 THR B 205 -2.857 -8.450 -18.128 1.00 76.45 C ANISOU 3117 CG2 THR B 205 12313 7835 8899 2409 1134 521 C ATOM 3118 N VAL B 206 -7.095 -7.419 -19.284 1.00 61.45 N ANISOU 3118 N VAL B 206 10707 5568 7073 1188 912 456 N ATOM 3119 CA VAL B 206 -8.188 -7.136 -20.202 1.00 59.35 C ANISOU 3119 CA VAL B 206 10505 5263 6781 824 872 398 C ATOM 3120 C VAL B 206 -7.624 -6.130 -21.199 1.00 61.07 C ANISOU 3120 C VAL B 206 10526 5646 7033 758 818 340 C ATOM 3121 O VAL B 206 -7.212 -5.041 -20.808 1.00 59.94 O ANISOU 3121 O VAL B 206 10112 5701 6963 815 705 356 O ATOM 3122 CB VAL B 206 -9.487 -6.630 -19.500 1.00 60.53 C ANISOU 3122 CB VAL B 206 10571 5481 6946 629 724 438 C ATOM 3123 CG1 VAL B 206 -10.532 -6.187 -20.525 1.00 59.75 C ANISOU 3123 CG1 VAL B 206 10465 5442 6797 298 660 379 C ATOM 3124 CG2 VAL B 206 -10.066 -7.695 -18.574 1.00 60.91 C ANISOU 3124 CG2 VAL B 206 10853 5346 6944 656 811 483 C ATOM 3125 N GLU B 207 -7.561 -6.511 -22.477 1.00 56.70 N ANISOU 3125 N GLU B 207 10129 5001 6414 628 922 264 N ATOM 3126 CA GLU B 207 -7.118 -5.593 -23.508 1.00 54.59 C ANISOU 3126 CA GLU B 207 9719 4868 6155 538 889 212 C ATOM 3127 C GLU B 207 -8.274 -5.235 -24.468 1.00 58.84 C ANISOU 3127 C GLU B 207 10312 5430 6613 221 823 187 C ATOM 3128 O GLU B 207 -9.028 -6.120 -24.870 1.00 59.44 O ANISOU 3128 O GLU B 207 10606 5386 6593 56 891 144 O ATOM 3129 CB GLU B 207 -5.916 -6.178 -24.274 1.00 56.32 C ANISOU 3129 CB GLU B 207 10027 5024 6349 681 1061 143 C ATOM 3130 CG GLU B 207 -5.324 -5.197 -25.280 1.00 58.90 C ANISOU 3130 CG GLU B 207 10202 5494 6682 593 1048 85 C ATOM 3131 CD GLU B 207 -4.112 -5.716 -26.017 1.00 85.77 C ANISOU 3131 CD GLU B 207 13660 8869 10060 731 1219 5 C ATOM 3132 OE1 GLU B 207 -4.274 -6.585 -26.904 1.00 78.45 O ANISOU 3132 OE1 GLU B 207 12985 7772 9049 647 1351 -50 O ATOM 3133 OE2 GLU B 207 -2.991 -5.272 -25.684 1.00 91.60 O ANISOU 3133 OE2 GLU B 207 14180 9773 10851 918 1233 -18 O ATOM 3134 N LYS B 208 -8.365 -3.950 -24.861 1.00 55.40 N ANISOU 3134 N LYS B 208 9690 5160 6197 143 711 206 N ATOM 3135 CA LYS B 208 -9.295 -3.391 -25.863 1.00 54.33 C ANISOU 3135 CA LYS B 208 9568 5111 5963 -86 638 204 C ATOM 3136 C LYS B 208 -8.469 -2.634 -26.899 1.00 58.95 C ANISOU 3136 C LYS B 208 10108 5754 6534 -89 683 177 C ATOM 3137 O LYS B 208 -7.391 -2.137 -26.580 1.00 57.51 O ANISOU 3137 O LYS B 208 9805 5601 6445 54 722 169 O ATOM 3138 CB LYS B 208 -10.373 -2.473 -25.233 1.00 53.92 C ANISOU 3138 CB LYS B 208 9364 5197 5927 -139 466 290 C ATOM 3139 CG LYS B 208 -11.352 -3.202 -24.290 1.00 60.54 C ANISOU 3139 CG LYS B 208 10245 6002 6757 -187 424 305 C ATOM 3140 CD LYS B 208 -12.372 -4.058 -25.045 1.00 65.64 C ANISOU 3140 CD LYS B 208 11052 6645 7244 -433 456 234 C ATOM 3141 CE LYS B 208 -13.060 -5.031 -24.115 1.00 64.56 C ANISOU 3141 CE LYS B 208 11021 6414 7096 -498 491 215 C ATOM 3142 NZ LYS B 208 -14.371 -4.520 -23.640 1.00 74.22 N ANISOU 3142 NZ LYS B 208 12094 7826 8280 -619 342 249 N ATOM 3143 N THR B 209 -8.985 -2.545 -28.126 1.00 57.41 N ANISOU 3143 N THR B 209 10005 5600 6206 -265 683 153 N ATOM 3144 CA THR B 209 -8.338 -1.948 -29.283 1.00 58.51 C ANISOU 3144 CA THR B 209 10160 5777 6293 -302 745 127 C ATOM 3145 C THR B 209 -9.320 -1.059 -30.047 1.00 62.74 C ANISOU 3145 C THR B 209 10683 6457 6699 -431 636 195 C ATOM 3146 O THR B 209 -10.501 -1.410 -30.170 1.00 62.61 O ANISOU 3146 O THR B 209 10694 6523 6570 -551 549 206 O ATOM 3147 CB THR B 209 -7.789 -3.086 -30.194 1.00 63.53 C ANISOU 3147 CB THR B 209 10987 6298 6852 -355 909 13 C ATOM 3148 OG1 THR B 209 -6.947 -3.940 -29.431 1.00 71.28 O ANISOU 3148 OG1 THR B 209 11996 7153 7936 -176 1015 -26 O ATOM 3149 CG2 THR B 209 -6.998 -2.579 -31.384 1.00 59.71 C ANISOU 3149 CG2 THR B 209 10528 5846 6314 -393 998 -30 C ATOM 3150 N VAL B 210 -8.833 0.110 -30.511 1.00 59.54 N ANISOU 3150 N VAL B 210 10232 6095 6295 -397 652 242 N ATOM 3151 CA VAL B 210 -9.558 1.083 -31.352 1.00 60.56 C ANISOU 3151 CA VAL B 210 10384 6345 6280 -453 583 333 C ATOM 3152 C VAL B 210 -8.672 1.500 -32.506 1.00 69.14 C ANISOU 3152 C VAL B 210 11570 7401 7301 -490 713 302 C ATOM 3153 O VAL B 210 -7.460 1.657 -32.334 1.00 68.75 O ANISOU 3153 O VAL B 210 11494 7265 7365 -442 837 239 O ATOM 3154 CB VAL B 210 -10.182 2.322 -30.650 1.00 62.18 C ANISOU 3154 CB VAL B 210 10482 6616 6525 -355 477 467 C ATOM 3155 CG1 VAL B 210 -11.364 1.924 -29.767 1.00 62.19 C ANISOU 3155 CG1 VAL B 210 10392 6704 6532 -352 332 504 C ATOM 3156 CG2 VAL B 210 -9.142 3.140 -29.883 1.00 59.64 C ANISOU 3156 CG2 VAL B 210 10086 6198 6375 -260 561 463 C ATOM 3157 N ALA B 211 -9.290 1.690 -33.678 1.00 69.55 N ANISOU 3157 N ALA B 211 11721 7557 7148 -578 686 341 N ATOM 3158 CA ALA B 211 -8.631 2.086 -34.910 1.00 70.07 C ANISOU 3158 CA ALA B 211 11911 7609 7104 -631 804 326 C ATOM 3159 C ALA B 211 -9.339 3.309 -35.534 1.00 76.83 C ANISOU 3159 C ALA B 211 12821 8576 7795 -586 743 487 C ATOM 3160 O ALA B 211 -10.566 3.388 -35.424 1.00 77.18 O ANISOU 3160 O ALA B 211 12811 8783 7729 -556 587 576 O ATOM 3161 CB ALA B 211 -8.673 0.927 -35.882 1.00 71.77 C ANISOU 3161 CB ALA B 211 12240 7850 7179 -778 853 210 C ATOM 3162 N PRO B 212 -8.611 4.242 -36.218 1.00 74.23 N ANISOU 3162 N PRO B 212 12606 8176 7423 -573 876 526 N ATOM 3163 CA PRO B 212 -9.298 5.363 -36.897 1.00 76.16 C ANISOU 3163 CA PRO B 212 12960 8502 7474 -493 844 703 C ATOM 3164 C PRO B 212 -10.309 4.897 -37.956 1.00 86.36 C ANISOU 3164 C PRO B 212 14295 10030 8487 -539 727 742 C ATOM 3165 O PRO B 212 -10.056 3.916 -38.663 1.00 86.44 O ANISOU 3165 O PRO B 212 14345 10076 8422 -693 764 609 O ATOM 3166 CB PRO B 212 -8.154 6.146 -37.561 1.00 78.13 C ANISOU 3166 CB PRO B 212 13371 8598 7717 -529 1061 691 C ATOM 3167 CG PRO B 212 -6.910 5.691 -36.915 1.00 80.81 C ANISOU 3167 CG PRO B 212 13614 8807 8284 -601 1184 517 C ATOM 3168 CD PRO B 212 -7.148 4.296 -36.434 1.00 75.70 C ANISOU 3168 CD PRO B 212 12835 8216 7711 -628 1077 410 C ATOM 3169 N THR B 213 -11.458 5.592 -38.050 0.80 87.17 N ANISOU 3169 N THR B 213 14381 10316 8423 -400 592 915 N ATOM 3170 CA THR B 213 -12.530 5.285 -39.012 0.80 90.11 C ANISOU 3170 CA THR B 213 14745 11006 8486 -420 455 961 C ATOM 3171 C THR B 213 -12.433 6.135 -40.287 0.80 98.91 C ANISOU 3171 C THR B 213 16058 12177 9348 -338 528 1097 C ATOM 3172 O THR B 213 -11.824 7.211 -40.272 0.80 99.27 O ANISOU 3172 O THR B 213 16259 12010 9450 -219 670 1206 O ATOM 3173 CB THR B 213 -13.910 5.368 -38.344 0.80 96.84 C ANISOU 3173 CB THR B 213 15411 12112 9274 -305 248 1052 C ATOM 3174 OG1 THR B 213 -13.956 6.500 -37.469 0.80 93.58 O ANISOU 3174 OG1 THR B 213 14997 11563 8996 -82 262 1206 O ATOM 3175 CG2 THR B 213 -14.258 4.099 -37.581 0.80 93.08 C ANISOU 3175 CG2 THR B 213 14766 11684 8914 -481 166 879 C ATOM 3176 N GLU B 214 -13.038 5.646 -41.390 0.50 98.85 N ANISOU 3176 N GLU B 214 16059 12458 9041 -418 445 1081 N ATOM 3177 CA GLU B 214 -13.024 6.289 -42.708 0.50101.47 C ANISOU 3177 CA GLU B 214 16579 12898 9077 -346 498 1206 C ATOM 3178 C GLU B 214 -13.977 7.501 -42.828 0.50108.15 C ANISOU 3178 C GLU B 214 17458 13928 9707 -22 403 1485 C ATOM 3179 O GLU B 214 -14.865 7.511 -43.687 0.50110.38 O ANISOU 3179 O GLU B 214 17708 14586 9643 55 273 1574 O ATOM 3180 CB GLU B 214 -13.288 5.251 -43.815 0.50104.43 C ANISOU 3180 CB GLU B 214 16938 13543 9198 -569 446 1064 C ATOM 3181 N CYS B 215 -13.761 8.533 -41.975 0.50104.32 N ANISOU 3181 N CYS B 215 17045 13185 9408 176 486 1619 N ATOM 3182 CA CYS B 215 -14.500 9.809 -41.939 0.50150.82 C ANISOU 3182 CA CYS B 215 23029 19138 15140 530 462 1898 C ATOM 3183 C CYS B 215 -13.757 10.874 -41.130 0.50165.77 C ANISOU 3183 C CYS B 215 25103 20599 17283 632 670 1971 C ATOM 3184 O CYS B 215 -13.198 10.579 -40.074 0.50120.12 O ANISOU 3184 O CYS B 215 19211 14607 11821 493 711 1823 O ATOM 3185 CB CYS B 215 -15.939 9.636 -41.456 1.00151.98 C ANISOU 3185 CB CYS B 215 22901 19675 15168 690 205 1968 C ATOM 3186 SG CYS B 215 -16.096 8.915 -39.801 1.00152.69 S ANISOU 3186 SG CYS B 215 22706 19680 15628 552 110 1793 S TER 3187 CYS B 215 HETATM 3188 C1 GOL A 301 -8.772 19.984 12.697 1.00 69.38 C HETATM 3189 O1 GOL A 301 -9.901 20.831 12.554 1.00 75.18 O HETATM 3190 C2 GOL A 301 -7.757 20.304 11.624 1.00 62.22 C HETATM 3191 O2 GOL A 301 -8.360 20.144 10.348 1.00 58.50 O HETATM 3192 C3 GOL A 301 -7.216 21.709 11.756 1.00 57.56 C HETATM 3193 O3 GOL A 301 -6.136 21.939 10.851 1.00 56.23 O HETATM 3194 H11 GOL A 301 -8.339 20.087 13.691 1.00 69.41 H HETATM 3195 H12 GOL A 301 -9.085 18.943 12.622 1.00 68.99 H HETATM 3196 HO1 GOL A 301 -9.761 21.580 13.191 1.00 75.57 H HETATM 3197 H2 GOL A 301 -6.962 19.561 11.586 1.00 62.55 H HETATM 3198 HO2 GOL A 301 -8.892 20.959 10.149 1.00 58.48 H HETATM 3199 H31 GOL A 301 -8.001 22.447 11.601 1.00 57.08 H HETATM 3200 H32 GOL A 301 -6.870 21.865 12.776 1.00 57.81 H HETATM 3201 HO3 GOL A 301 -6.251 22.865 10.513 1.00 55.40 H HETATM 3202 C1 GOL A 302 -2.159 17.027 -20.239 1.00113.36 C HETATM 3203 O1 GOL A 302 -1.370 15.850 -20.096 1.00113.03 O HETATM 3204 C2 GOL A 302 -1.288 18.251 -20.423 1.00112.65 C HETATM 3205 O2 GOL A 302 -2.013 19.251 -21.151 1.00112.58 O HETATM 3206 C3 GOL A 302 -0.848 18.815 -19.091 1.00110.65 C HETATM 3207 O3 GOL A 302 0.230 19.730 -19.236 1.00108.41 O HETATM 3208 H11 GOL A 302 -2.852 16.919 -21.072 1.00113.44 H HETATM 3209 H12 GOL A 302 -2.786 17.146 -19.356 1.00113.34 H HETATM 3210 HO1 GOL A 302 -1.874 15.125 -20.551 1.00112.80 H HETATM 3211 H2 GOL A 302 -0.442 18.057 -21.082 1.00112.84 H HETATM 3212 HO2 GOL A 302 -2.864 19.438 -20.674 1.00112.56 H HETATM 3213 H31 GOL A 302 -1.684 19.315 -18.606 1.00110.78 H HETATM 3214 H32 GOL A 302 -0.551 18.005 -18.427 1.00110.76 H HETATM 3215 HO3 GOL A 302 0.336 20.165 -18.350 1.00108.20 H HETATM 3216 C1 GOL A 303 -1.358 32.036 -8.540 1.00 85.61 C HETATM 3217 O1 GOL A 303 -1.534 33.361 -8.997 1.00 90.17 O HETATM 3218 C2 GOL A 303 -1.326 31.997 -7.030 1.00 87.27 C HETATM 3219 O2 GOL A 303 -0.672 33.170 -6.522 1.00 87.13 O HETATM 3220 C3 GOL A 303 -0.605 30.757 -6.550 1.00 86.97 C HETATM 3221 O3 GOL A 303 -1.339 30.068 -5.552 1.00 86.53 O HETATM 3222 H11 GOL A 303 -2.157 31.403 -8.920 1.00 85.07 H HETATM 3223 H12 GOL A 303 -0.438 31.641 -8.966 1.00 85.07 H HETATM 3224 HO1 GOL A 303 -0.626 33.760 -9.027 1.00 90.57 H HETATM 3225 H2 GOL A 303 -2.322 32.089 -6.601 1.00 87.74 H HETATM 3226 HO2 GOL A 303 -1.314 33.926 -6.562 1.00 86.77 H HETATM 3227 H31 GOL A 303 -0.434 30.072 -7.379 1.00 87.14 H HETATM 3228 H32 GOL A 303 0.375 31.023 -6.156 1.00 86.79 H HETATM 3229 HO3 GOL A 303 -1.082 30.478 -4.684 1.00 86.32 H HETATM 3230 C1 GOL B 301 -3.235 -5.196 -30.367 1.00105.80 C HETATM 3231 O1 GOL B 301 -1.921 -5.508 -29.916 1.00103.45 O HETATM 3232 C2 GOL B 301 -3.542 -5.831 -31.706 1.00107.43 C HETATM 3233 O2 GOL B 301 -4.960 -5.823 -31.915 1.00107.43 O HETATM 3234 C3 GOL B 301 -2.871 -5.093 -32.843 1.00107.91 C HETATM 3235 O3 GOL B 301 -1.452 -5.132 -32.724 1.00107.68 O HETATM 3236 H11 GOL B 301 -3.972 -5.486 -29.620 1.00105.83 H HETATM 3237 H12 GOL B 301 -3.323 -4.116 -30.469 1.00106.03 H HETATM 3238 HO1 GOL B 301 -1.901 -5.278 -28.950 1.00103.10 H HETATM 3239 H2 GOL B 301 -3.314 -6.896 -31.718 1.00107.60 H HETATM 3240 HO2 GOL B 301 -5.372 -6.479 -31.294 1.00107.49 H HETATM 3241 H31 GOL B 301 -3.179 -5.505 -33.803 1.00107.94 H HETATM 3242 H32 GOL B 301 -3.205 -4.056 -32.856 1.00107.98 H HETATM 3243 HO3 GOL B 301 -1.141 -5.803 -33.385 1.00107.77 H HETATM 3244 C1 GOL B 302 -6.708 17.209 -22.173 1.00104.00 C HETATM 3245 O1 GOL B 302 -6.128 16.056 -21.569 1.00102.49 O HETATM 3246 C2 GOL B 302 -7.405 16.857 -23.469 1.00104.46 C HETATM 3247 O2 GOL B 302 -8.229 15.700 -23.279 1.00103.27 O HETATM 3248 C3 GOL B 302 -8.253 18.007 -23.964 1.00105.16 C HETATM 3249 O3 GOL B 302 -8.317 18.027 -25.384 1.00106.80 O HETATM 3250 H11 GOL B 302 -7.401 17.696 -21.489 1.00104.31 H HETATM 3251 H12 GOL B 302 -5.928 17.944 -22.364 1.00104.02 H HETATM 3252 HO1 GOL B 302 -5.983 16.289 -20.615 1.00102.46 H HETATM 3253 H2 GOL B 302 -6.703 16.514 -24.227 1.00104.59 H HETATM 3254 HO2 GOL B 302 -8.823 15.855 -22.499 1.00103.23 H HETATM 3255 H31 GOL B 302 -9.264 17.928 -23.569 1.00104.96 H HETATM 3256 H32 GOL B 302 -7.861 18.957 -23.603 1.00104.90 H HETATM 3257 HO3 GOL B 302 -8.937 18.767 -25.619 1.00106.87 H HETATM 3258 O HOH A 401 -24.122 -6.242 -33.899 1.00 48.15 O HETATM 3259 O HOH A 402 -1.834 30.529 -3.038 1.00 70.23 O HETATM 3260 O HOH A 403 0.083 32.295 2.016 1.00 50.64 O HETATM 3261 O HOH A 404 -10.592 10.597 -10.847 1.00 54.48 O HETATM 3262 O HOH A 405 -25.686 0.071 -21.642 1.00 60.21 O HETATM 3263 O HOH A 406 -12.229 23.154 -2.994 1.00 57.14 O HETATM 3264 O HOH A 407 0.076 21.983 -12.170 1.00 56.59 O HETATM 3265 O HOH A 408 -1.652 29.072 7.288 1.00 48.74 O HETATM 3266 O HOH A 409 -10.862 16.663 -20.853 1.00 57.02 O HETATM 3267 O HOH A 410 -19.259 31.329 10.837 1.00 62.38 O HETATM 3268 O HOH A 411 -21.833 28.707 -13.070 1.00 65.18 O HETATM 3269 O HOH A 412 -27.022 -0.201 -31.615 1.00 67.20 O HETATM 3270 O HOH A 413 -22.677 21.175 -1.805 1.00 58.90 O HETATM 3271 O HOH A 414 -26.641 26.379 23.447 1.00 73.59 O HETATM 3272 O HOH A 415 -17.575 29.407 17.092 1.00 61.44 O HETATM 3273 O HOH A 416 -2.325 24.829 -11.600 1.00 44.26 O HETATM 3274 O HOH A 417 -13.261 31.869 12.321 1.00 50.67 O HETATM 3275 O HOH A 418 -11.558 8.990 -13.768 1.00 49.04 O HETATM 3276 O HOH A 419 -19.522 11.126 13.062 1.00 70.74 O HETATM 3277 O HOH A 420 -18.533 -4.958 -29.545 1.00 56.67 O HETATM 3278 O HOH A 421 -23.379 27.191 12.627 1.00 55.43 O HETATM 3279 O HOH A 422 -10.822 31.391 -4.062 1.00 59.68 O HETATM 3280 O HOH A 423 -5.945 17.913 5.216 1.00 61.87 O HETATM 3281 O HOH A 424 -5.934 17.467 9.286 1.00 51.63 O HETATM 3282 O HOH A 425 -18.263 26.370 -5.305 1.00 60.07 O HETATM 3283 O HOH A 426 -16.448 -1.762 -34.778 1.00 71.91 O HETATM 3284 O HOH A 427 -12.522 12.993 9.229 1.00 60.53 O HETATM 3285 O HOH A 428 -30.796 28.770 17.828 1.00 81.37 O HETATM 3286 O HOH A 429 -9.785 9.238 -6.978 1.00 47.17 O HETATM 3287 O HOH A 430 -12.068 32.207 -8.073 1.00 63.82 O HETATM 3288 O HOH A 431 -15.359 23.619 -7.790 1.00 61.94 O HETATM 3289 O HOH A 432 -8.230 20.619 -4.340 1.00 56.09 O HETATM 3290 O HOH A 433 -6.155 23.914 -17.232 1.00 62.10 O HETATM 3291 O HOH A 434 -40.449 25.741 6.745 1.00 77.62 O HETATM 3292 O HOH A 435 -4.417 26.845 14.746 1.00 63.05 O HETATM 3293 O HOH A 436 -18.709 15.321 -8.983 1.00 59.58 O HETATM 3294 O HOH A 437 -1.657 22.156 8.458 1.00 57.03 O HETATM 3295 O HOH A 438 -19.792 30.066 1.233 1.00 60.68 O HETATM 3296 O HOH A 439 -18.322 18.396 -5.809 1.00 65.91 O HETATM 3297 O HOH A 440 -16.259 17.815 -26.070 1.00 58.23 O HETATM 3298 O HOH A 441 -12.806 22.481 -22.301 1.00 64.10 O HETATM 3299 O HOH A 442 0.075 25.675 12.801 1.00 72.18 O HETATM 3300 O HOH A 443 -26.891 14.216 -13.710 1.00 59.08 O HETATM 3301 O HOH A 444 -28.533 18.410 -0.419 1.00 76.84 O HETATM 3302 O HOH A 445 -7.254 34.940 7.971 1.00 62.33 O HETATM 3303 O HOH A 446 -25.225 21.248 -0.857 1.00 73.97 O HETATM 3304 O HOH A 447 -6.272 32.905 12.529 1.00 61.29 O HETATM 3305 O HOH A 448 -30.165 15.247 4.317 1.00 70.21 O HETATM 3306 O HOH A 449 -12.184 27.929 -12.683 1.00 58.16 O HETATM 3307 O HOH A 450 -23.674 7.571 -32.006 1.00 68.74 O HETATM 3308 O HOH A 451 -31.913 13.534 5.502 1.00 65.21 O HETATM 3309 O HOH A 452 -16.632 7.070 -29.233 1.00 52.24 O HETATM 3310 O HOH A 453 -39.364 16.983 15.759 1.00 77.42 O HETATM 3311 O HOH A 454 -19.459 18.416 -2.341 1.00 73.81 O HETATM 3312 O HOH A 455 -21.838 14.532 -31.791 1.00 72.13 O HETATM 3313 O HOH A 456 -4.834 16.542 -15.033 1.00 52.64 O HETATM 3314 O HOH A 457 -3.878 24.180 13.623 1.00 62.47 O HETATM 3315 O HOH A 458 -18.731 25.272 -7.593 1.00 61.58 O HETATM 3316 O HOH A 459 -15.333 31.875 1.044 1.00 57.76 O HETATM 3317 O HOH A 460 -24.555 32.666 9.393 1.00 72.39 O HETATM 3318 O HOH A 461 -1.966 30.938 9.239 1.00 62.49 O HETATM 3319 O HOH A 462 -27.742 17.748 13.972 1.00 71.87 O HETATM 3320 O HOH A 463 -2.273 21.980 -18.414 1.00 84.39 O HETATM 3321 O HOH A 464 -18.510 12.748 16.339 1.00 75.15 O HETATM 3322 O HOH A 465 -15.370 30.170 -6.236 1.00 73.62 O HETATM 3323 O HOH A 466 -31.984 25.742 19.358 1.00 85.24 O HETATM 3324 O HOH A 467 -19.370 15.746 1.058 1.00 73.35 O HETATM 3325 O HOH A 468 -14.699 5.833 7.256 1.00 75.72 O HETATM 3326 O HOH A 469 -11.069 6.806 11.408 1.00 85.76 O HETATM 3327 O HOH A 470 -11.439 21.818 -24.450 1.00 80.04 O HETATM 3328 O HOH A 471 -5.523 21.923 15.055 1.00 74.41 O HETATM 3329 O HOH B 401 -12.470 4.354 -33.855 1.00 85.38 O HETATM 3330 O HOH B 402 1.986 2.618 -21.299 1.00 66.99 O HETATM 3331 O HOH B 403 -7.666 -14.907 -13.355 1.00 66.92 O HETATM 3332 O HOH B 404 -14.679 14.855 -28.312 1.00 62.89 O HETATM 3333 O HOH B 405 -2.999 -1.532 -31.143 1.00 66.56 O HETATM 3334 O HOH B 406 -12.675 13.042 -28.237 1.00 65.45 O HETATM 3335 O HOH B 407 -34.905 -4.051 12.598 1.00 64.34 O HETATM 3336 O HOH B 408 -40.812 2.432 22.122 1.00 66.99 O HETATM 3337 O HOH B 409 -24.460 8.704 1.825 1.00 53.81 O HETATM 3338 O HOH B 410 -38.759 1.450 -1.284 1.00 63.08 O HETATM 3339 O HOH B 411 -36.161 -3.022 23.886 1.00 64.64 O HETATM 3340 O HOH B 412 -3.756 15.402 -17.301 1.00 69.23 O HETATM 3341 O HOH B 413 -10.828 7.385 -10.696 1.00 54.03 O HETATM 3342 O HOH B 414 -36.087 1.555 13.983 1.00 65.81 O HETATM 3343 O HOH B 415 -15.309 9.360 -29.617 1.00 50.30 O HETATM 3344 O HOH B 416 -18.633 18.202 -27.538 1.00 60.18 O HETATM 3345 O HOH B 417 -0.963 4.851 -16.248 1.00 66.77 O HETATM 3346 O HOH B 418 -38.200 12.084 16.711 1.00 67.45 O HETATM 3347 O HOH B 419 -26.458 6.956 1.573 1.00 65.03 O HETATM 3348 O HOH B 420 -13.143 6.099 -3.072 1.00 67.43 O HETATM 3349 O HOH B 421 -2.003 -3.995 -10.033 1.00 74.28 O HETATM 3350 O HOH B 422 -0.978 -3.479 -17.891 1.00 58.88 O HETATM 3351 O HOH B 423 -16.616 6.756 -8.608 1.00 49.07 O HETATM 3352 O HOH B 424 -28.846 -3.301 -5.508 1.00 71.19 O HETATM 3353 O HOH B 425 -27.371 0.531 0.346 1.00 58.45 O HETATM 3354 O HOH B 426 -30.130 8.243 25.413 1.00 73.10 O HETATM 3355 O HOH B 427 -14.971 -5.090 -20.772 1.00 49.46 O HETATM 3356 O HOH B 428 -15.928 0.649 -18.699 1.00 47.46 O HETATM 3357 O HOH B 429 -22.622 4.800 19.803 1.00 70.79 O HETATM 3358 O HOH B 430 -25.089 2.043 -2.351 1.00 57.44 O HETATM 3359 O HOH B 431 -14.297 -0.817 -25.894 1.00 57.08 O HETATM 3360 O HOH B 432 -1.230 8.242 -13.932 1.00 65.60 O HETATM 3361 O HOH B 433 -26.205 -4.458 17.275 1.00 72.25 O HETATM 3362 O HOH B 434 -4.217 4.574 -10.806 1.00 64.93 O HETATM 3363 O HOH B 435 -1.037 15.317 -16.967 1.00 59.74 O HETATM 3364 O HOH B 436 -37.974 11.068 0.114 1.00 73.58 O HETATM 3365 O HOH B 437 -41.776 1.174 4.023 1.00 69.50 O HETATM 3366 O HOH B 438 -19.812 -8.696 13.421 1.00 70.40 O HETATM 3367 O HOH B 439 -20.981 22.223 -30.092 1.00168.02 O HETATM 3368 O HOH B 440 -17.928 3.793 14.525 1.00 80.87 O HETATM 3369 O HOH B 441 -14.922 21.726 -34.672 1.00 71.99 O HETATM 3370 O HOH B 442 -10.227 -2.325 -2.268 1.00 68.75 O HETATM 3371 O HOH B 443 -19.444 4.971 12.488 1.00 65.73 O HETATM 3372 O HOH B 444 -0.876 -3.035 -35.364 1.00 75.78 O HETATM 3373 O HOH B 445 -35.177 -3.006 18.898 1.00 67.96 O HETATM 3374 O HOH B 446 -12.729 0.981 -33.816 1.00 64.57 O HETATM 3375 O HOH B 447 4.463 11.108 -19.409 1.00 73.07 O HETATM 3376 O HOH B 448 -33.518 -4.109 23.292 1.00 66.04 O HETATM 3377 O HOH B 449 5.777 6.938 -26.900 1.00 73.08 O HETATM 3378 O HOH B 450 -40.257 17.792 18.195 1.00 86.17 O HETATM 3379 O HOH B 451 -16.616 -2.176 -25.458 1.00 85.78 O HETATM 3380 O HOH B 452 -16.598 3.489 12.155 1.00 84.33 O HETATM 3381 O HOH B 453 -0.397 16.087 -27.835 1.00 73.93 O HETATM 3382 O HOH B 454 -3.726 9.482 -42.667 1.00 62.16 O HETATM 3383 O HOH B 455 -36.247 -0.806 -4.481 1.00 88.45 O CONECT 1015 1469 CONECT 1469 1015 CONECT 1601 3186 CONECT 2604 3058 CONECT 3058 2604 CONECT 3186 1601 CONECT 3188 3189 3190 3194 3195 CONECT 3189 3188 3196 CONECT 3190 3188 3191 3192 3197 CONECT 3191 3190 3198 CONECT 3192 3190 3193 3199 3200 CONECT 3193 3192 3201 CONECT 3194 3188 CONECT 3195 3188 CONECT 3196 3189 CONECT 3197 3190 CONECT 3198 3191 CONECT 3199 3192 CONECT 3200 3192 CONECT 3201 3193 CONECT 3202 3203 3204 3208 3209 CONECT 3203 3202 3210 CONECT 3204 3202 3205 3206 3211 CONECT 3205 3204 3212 CONECT 3206 3204 3207 3213 3214 CONECT 3207 3206 3215 CONECT 3208 3202 CONECT 3209 3202 CONECT 3210 3203 CONECT 3211 3204 CONECT 3212 3205 CONECT 3213 3206 CONECT 3214 3206 CONECT 3215 3207 CONECT 3216 3217 3218 3222 3223 CONECT 3217 3216 3224 CONECT 3218 3216 3219 3220 3225 CONECT 3219 3218 3226 CONECT 3220 3218 3221 3227 3228 CONECT 3221 3220 3229 CONECT 3222 3216 CONECT 3223 3216 CONECT 3224 3217 CONECT 3225 3218 CONECT 3226 3219 CONECT 3227 3220 CONECT 3228 3220 CONECT 3229 3221 CONECT 3230 3231 3232 3236 3237 CONECT 3231 3230 3238 CONECT 3232 3230 3233 3234 3239 CONECT 3233 3232 3240 CONECT 3234 3232 3235 3241 3242 CONECT 3235 3234 3243 CONECT 3236 3230 CONECT 3237 3230 CONECT 3238 3231 CONECT 3239 3232 CONECT 3240 3233 CONECT 3241 3234 CONECT 3242 3234 CONECT 3243 3235 CONECT 3244 3245 3246 3250 3251 CONECT 3245 3244 3252 CONECT 3246 3244 3247 3248 3253 CONECT 3247 3246 3254 CONECT 3248 3246 3249 3255 3256 CONECT 3249 3248 3257 CONECT 3250 3244 CONECT 3251 3244 CONECT 3252 3245 CONECT 3253 3246 CONECT 3254 3247 CONECT 3255 3248 CONECT 3256 3248 CONECT 3257 3249 MASTER 328 0 5 6 50 0 8 6 3335 2 76 34 END