 |
| home | start a new run | job status | references&downloads | examples | help |
Should you encounter any unexpected behaviour,
|
*** AAG protein ***elNémo ID: 240110225737593311Job options:ID = 240110225737593311 JOBID = AAG protein USERID = unknown PRIVAT = 0 NMODES = 5 DQMIN = -100 DQMAX = 100 DQSTEP = 20 DOGRAPHS = on DOPROJMODS = 0 DORMSD = 0 NRBL = 0 CUTOFF = 0 CAONLY = 0 Input data for this run:HEADER AAG protein HEADER TRANSPORT PROTEIN 21-OCT-10 3APU TITLE CRYSTAL STRUCTURE OF THE A VARIANT OF HUMAN ALPHA1-ACID GLYCOPROTEIN COMPND MOL_ID: 1; COMPND 2 MOLECULE: ALPHA-1-ACID GLYCOPROTEIN 2; COMPND 3 CHAIN: A, B; COMPND 4 SYNONYM: AGP 2, OROSOMUCOID-2, OMD 2; COMPND 5 ENGINEERED: YES; COMPND 6 MUTATION: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606; SOURCE 5 GENE: AGP2, ORM2; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 8 EXPRESSION_SYSTEM_STRAIN: ORIGAMI B (DE3); SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET3C KEYWDS BETA BARREL, PLASMA PROTEIN, TRANSPORT PROTEIN EXPDTA X-RAY DIFFRACTION AUTHOR K.NISHI,T.ONO,T.NAKAMURA,N.FUKUNAGA,M.IZUMI,H.WATANABE,A.SUENAGA, AUTHOR 2 T.MARUYAMA,Y.YAMAGATA,S.CURRY,M.OTAGIRI REVDAT 3 01-NOV-23 3APU 1 REMARK SEQADV REVDAT 2 07-NOV-18 3APU 1 JRNL REMARK REVDAT 1 23-FEB-11 3APU 0 JRNL AUTH K.NISHI,T.ONO,T.NAKAMURA,N.FUKUNAGA,M.IZUMI,H.WATANABE, JRNL AUTH 2 A.SUENAGA,T.MARUYAMA,Y.YAMAGATA,S.CURRY,M.OTAGIRI JRNL TITL STRUCTURAL INSIGHTS INTO DIFFERENCES IN DRUG-BINDING JRNL TITL 2 SELECTIVITY BETWEEN TWO FORMS OF HUMAN ALPHA1-ACID JRNL TITL 3 GLYCOPROTEIN GENETIC VARIANTS, THE A AND F1*S FORMS. JRNL REF J. BIOL. CHEM. V. 286 14427 2011 JRNL REFN ESSN 1083-351X JRNL PMID 21349832 JRNL DOI 10.1074/JBC.M110.208926 REMARK 2 REMARK 2 RESOLUTION. 2.10 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC 5.2.0019 REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER, REMARK 3 : NICHOLLS,WINN,LONG,VAGIN REMARK 3 REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 31.99 REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9 REMARK 3 NUMBER OF REFLECTIONS : 20189 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) : 0.201 REMARK 3 R VALUE (WORKING SET) : 0.200 REMARK 3 FREE R VALUE : 0.232 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900 REMARK 3 FREE R VALUE TEST SET COUNT : 1038 REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : 20 REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.10 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.16 REMARK 3 REFLECTION IN BIN (WORKING SET) : 1464 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.97 REMARK 3 BIN R VALUE (WORKING SET) : 0.2460 REMARK 3 BIN FREE R VALUE SET COUNT : 73 REMARK 3 BIN FREE R VALUE : 0.2820 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 2903 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 26 REMARK 3 SOLVENT ATOMS : 83 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 51.51 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 0.40000 REMARK 3 B22 (A**2) : 0.68000 REMARK 3 B33 (A**2) : -1.08000 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : -0.10000 REMARK 3 B23 (A**2) : 0.00000 REMARK 3 REMARK 3 ESTIMATED OVERALL COORDINATE ERROR. REMARK 3 ESU BASED ON R VALUE (A): 0.257 REMARK 3 ESU BASED ON FREE R VALUE (A): 0.191 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.173 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 14.626 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.959 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.947 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2984 ; 0.012 ; 0.022 REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4035 ; 1.336 ; 1.950 REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 345 ; 6.357 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 164 ;38.022 ;24.146 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 498 ;17.119 ;15.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 20 ;14.928 ;15.000 REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 416 ; 0.095 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2322 ; 0.006 ; 0.021 REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1187 ; 0.209 ; 0.200 REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 1969 ; 0.310 ; 0.200 REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 135 ; 0.156 ; 0.200 REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 38 ; 0.234 ; 0.200 REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 6 ; 0.147 ; 0.200 REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL REMARK 3 REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 1732 ; 0.681 ; 1.500 REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2803 ; 1.273 ; 2.000 REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1252 ; 1.780 ; 3.000 REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1232 ; 2.866 ; 4.500 REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 REMARK 3 NCS RESTRAINTS STATISTICS REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 2 REMARK 3 REMARK 3 TLS GROUP : 1 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : A 1 A 175 REMARK 3 ORIGIN FOR THE GROUP (A): 11.9830 0.1210 13.9280 REMARK 3 T TENSOR REMARK 3 T11: 0.1478 T22: 0.0466 REMARK 3 T33: 0.5598 T12: 0.0278 REMARK 3 T13: 0.0188 T23: -0.0192 REMARK 3 L TENSOR REMARK 3 L11: 2.7593 L22: 2.0731 REMARK 3 L33: 7.2819 L12: -0.1719 REMARK 3 L13: 0.2821 L23: 0.5966 REMARK 3 S TENSOR REMARK 3 S11: -0.0654 S12: -0.0026 S13: -0.0430 REMARK 3 S21: -0.0278 S22: -0.1961 S23: 0.0023 REMARK 3 S31: 0.3912 S32: -0.2662 S33: 0.2615 REMARK 3 REMARK 3 TLS GROUP : 2 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : B 2 B 173 REMARK 3 ORIGIN FOR THE GROUP (A): 10.5140 2.7350 45.9250 REMARK 3 T TENSOR REMARK 3 T11: 0.0923 T22: 0.1729 REMARK 3 T33: 0.4334 T12: -0.0913 REMARK 3 T13: 0.0490 T23: -0.0425 REMARK 3 L TENSOR REMARK 3 L11: 3.1791 L22: 2.4758 REMARK 3 L33: 11.1295 L12: 0.1729 REMARK 3 L13: 1.1364 L23: 2.0621 REMARK 3 S TENSOR REMARK 3 S11: 0.0131 S12: -0.4285 S13: 0.1457 REMARK 3 S21: 0.1418 S22: -0.2882 S23: -0.0320 REMARK 3 S31: -0.0511 S32: -0.6158 S33: 0.2750 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : MASK REMARK 3 PARAMETERS FOR MASK CALCULATION REMARK 3 VDW PROBE RADIUS : 1.40 REMARK 3 ION PROBE RADIUS : 0.80 REMARK 3 SHRINKAGE RADIUS : 0.80 REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING REMARK 3 POSITIONS REMARK 4 REMARK 4 3APU COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 09-NOV-10. REMARK 100 THE DEPOSITION ID IS D_1000029545. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 20-JUN-08 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 4.6 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : SPRING-8 REMARK 200 BEAMLINE : BL44XU REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.9 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : BRUKER DIP-6040 REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000 REMARK 200 DATA SCALING SOFTWARE : SCALEPACK REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 21258 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100 REMARK 200 RESOLUTION RANGE LOW (A) : 50.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9 REMARK 200 DATA REDUNDANCY : NULL REMARK 200 R MERGE (I) : 0.04400 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 56.8000 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) : 2.18 REMARK 200 COMPLETENESS FOR SHELL (%) : 99.3 REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : 0.32600 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 6.700 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: MOLREP REMARK 200 STARTING MODEL: PDB ENTRY 3BX6 REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 38.56 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.00 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 30% PEG 4000, 0.2M AMMONIUM ACETATE, REMARK 280 0.1M SODIUM ACETATE, PH 4.6, VAPOR DIFFUSION, HANGING DROP, REMARK 280 TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 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 REMARK 290 4555 -X+1/2,Y+1/2,-Z REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 33.55350 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 22.43100 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 33.55350 REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 22.43100 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1, 2 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 APPLY THE FOLLOWING TO CHAINS: A REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 350 REMARK 350 BIOMOLECULE: 2 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 MET A 0 REMARK 465 ARG A 176 REMARK 465 LYS A 177 REMARK 465 GLN A 178 REMARK 465 GLU A 179 REMARK 465 GLU A 180 REMARK 465 GLY A 181 REMARK 465 GLU A 182 REMARK 465 SER A 183 REMARK 465 HIS A 184 REMARK 465 HIS A 185 REMARK 465 HIS A 186 REMARK 465 HIS A 187 REMARK 465 HIS A 188 REMARK 465 HIS A 189 REMARK 465 MET B 0 REMARK 465 GLN B 1 REMARK 465 LYS B 174 REMARK 465 GLU B 175 REMARK 465 ARG B 176 REMARK 465 LYS B 177 REMARK 465 GLN B 178 REMARK 465 GLU B 179 REMARK 465 GLU B 180 REMARK 465 GLY B 181 REMARK 465 GLU B 182 REMARK 465 SER B 183 REMARK 465 HIS B 184 REMARK 465 HIS B 185 REMARK 465 HIS B 186 REMARK 465 HIS B 187 REMARK 465 HIS B 188 REMARK 465 HIS B 189 REMARK 480 REMARK 480 ZERO OCCUPANCY ATOM REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME; REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE): REMARK 480 M RES C SSEQI ATOMS REMARK 480 LYS A 170 CG CD CE NZ REMARK 480 GLN A 171 CG CD OE1 NE2 REMARK 480 LYS A 174 CB CG CD CE NZ REMARK 480 LYS B 170 CB CG CD CE NZ REMARK 480 GLN B 171 CB CG CD OE1 NE2 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT REMARK 500 REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT. REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE REMARK 500 OG SER B 125 OH TYR B 127 2.18 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 PG4 A 190 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PG4 B 190 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 3APV RELATED DB: PDB REMARK 900 RELATED ID: 3APW RELATED DB: PDB REMARK 900 RELATED ID: 3APX RELATED DB: PDB DBREF 3APU A 1 183 UNP P19652 A1AG2_HUMAN 19 201 DBREF 3APU B 1 183 UNP P19652 A1AG2_HUMAN 19 201 SEQADV 3APU MET A 0 UNP P19652 EXPRESSION TAG SEQADV 3APU ARG A 149 UNP P19652 CYS 167 ENGINEERED MUTATION SEQADV 3APU HIS A 184 UNP P19652 EXPRESSION TAG SEQADV 3APU HIS A 185 UNP P19652 EXPRESSION TAG SEQADV 3APU HIS A 186 UNP P19652 EXPRESSION TAG SEQADV 3APU HIS A 187 UNP P19652 EXPRESSION TAG SEQADV 3APU HIS A 188 UNP P19652 EXPRESSION TAG SEQADV 3APU HIS A 189 UNP P19652 EXPRESSION TAG SEQADV 3APU MET B 0 UNP P19652 EXPRESSION TAG SEQADV 3APU ARG B 149 UNP P19652 CYS 167 ENGINEERED MUTATION SEQADV 3APU HIS B 184 UNP P19652 EXPRESSION TAG SEQADV 3APU HIS B 185 UNP P19652 EXPRESSION TAG SEQADV 3APU HIS B 186 UNP P19652 EXPRESSION TAG SEQADV 3APU HIS B 187 UNP P19652 EXPRESSION TAG SEQADV 3APU HIS B 188 UNP P19652 EXPRESSION TAG SEQADV 3APU HIS B 189 UNP P19652 EXPRESSION TAG SEQRES 1 A 190 MET GLN ILE PRO LEU CYS ALA ASN LEU VAL PRO VAL PRO SEQRES 2 A 190 ILE THR ASN ALA THR LEU ASP ARG ILE THR GLY LYS TRP SEQRES 3 A 190 PHE TYR ILE ALA SER ALA PHE ARG ASN GLU GLU TYR ASN SEQRES 4 A 190 LYS SER VAL GLN GLU ILE GLN ALA THR PHE PHE TYR PHE SEQRES 5 A 190 THR PRO ASN LYS THR GLU ASP THR ILE PHE LEU ARG GLU SEQRES 6 A 190 TYR GLN THR ARG GLN ASN GLN CYS PHE TYR ASN SER SER SEQRES 7 A 190 TYR LEU ASN VAL GLN ARG GLU ASN GLY THR VAL SER ARG SEQRES 8 A 190 TYR GLU GLY GLY ARG GLU HIS VAL ALA HIS LEU LEU PHE SEQRES 9 A 190 LEU ARG ASP THR LYS THR LEU MET PHE GLY SER TYR LEU SEQRES 10 A 190 ASP ASP GLU LYS ASN TRP GLY LEU SER PHE TYR ALA ASP SEQRES 11 A 190 LYS PRO GLU THR THR LYS GLU GLN LEU GLY GLU PHE TYR SEQRES 12 A 190 GLU ALA LEU ASP CYS LEU ARG ILE PRO ARG SER ASP VAL SEQRES 13 A 190 MET TYR THR ASP TRP LYS LYS ASP LYS CYS GLU PRO LEU SEQRES 14 A 190 GLU LYS GLN HIS GLU LYS GLU ARG LYS GLN GLU GLU GLY SEQRES 15 A 190 GLU SER HIS HIS HIS HIS HIS HIS SEQRES 1 B 190 MET GLN ILE PRO LEU CYS ALA ASN LEU VAL PRO VAL PRO SEQRES 2 B 190 ILE THR ASN ALA THR LEU ASP ARG ILE THR GLY LYS TRP SEQRES 3 B 190 PHE TYR ILE ALA SER ALA PHE ARG ASN GLU GLU TYR ASN SEQRES 4 B 190 LYS SER VAL GLN GLU ILE GLN ALA THR PHE PHE TYR PHE SEQRES 5 B 190 THR PRO ASN LYS THR GLU ASP THR ILE PHE LEU ARG GLU SEQRES 6 B 190 TYR GLN THR ARG GLN ASN GLN CYS PHE TYR ASN SER SER SEQRES 7 B 190 TYR LEU ASN VAL GLN ARG GLU ASN GLY THR VAL SER ARG SEQRES 8 B 190 TYR GLU GLY GLY ARG GLU HIS VAL ALA HIS LEU LEU PHE SEQRES 9 B 190 LEU ARG ASP THR LYS THR LEU MET PHE GLY SER TYR LEU SEQRES 10 B 190 ASP ASP GLU LYS ASN TRP GLY LEU SER PHE TYR ALA ASP SEQRES 11 B 190 LYS PRO GLU THR THR LYS GLU GLN LEU GLY GLU PHE TYR SEQRES 12 B 190 GLU ALA LEU ASP CYS LEU ARG ILE PRO ARG SER ASP VAL SEQRES 13 B 190 MET TYR THR ASP TRP LYS LYS ASP LYS CYS GLU PRO LEU SEQRES 14 B 190 GLU LYS GLN HIS GLU LYS GLU ARG LYS GLN GLU GLU GLY SEQRES 15 B 190 GLU SER HIS HIS HIS HIS HIS HIS HET PG4 A 190 13 HET PG4 B 190 13 HETNAM PG4 TETRAETHYLENE GLYCOL FORMUL 3 PG4 2(C8 H18 O5) FORMUL 5 HOH *83(H2 O) HELIX 1 1 CYS A 5 VAL A 9 5 5 HELIX 2 2 THR A 14 THR A 22 1 9 HELIX 3 3 ASN A 34 GLU A 43 1 10 HELIX 4 4 THR A 134 LEU A 148 1 15 HELIX 5 5 PRO A 151 VAL A 155 5 5 HELIX 6 6 ASP A 159 ASP A 163 5 5 HELIX 7 7 CYS A 165 LYS A 174 1 10 HELIX 8 8 CYS B 5 VAL B 9 5 5 HELIX 9 9 THR B 14 THR B 22 1 9 HELIX 10 10 ASN B 34 GLN B 42 1 9 HELIX 11 11 THR B 134 LEU B 148 1 15 HELIX 12 12 PRO B 151 VAL B 155 5 5 HELIX 13 13 ASP B 159 ASP B 163 5 5 HELIX 14 14 CYS B 165 GLU B 173 1 9 SHEET 1 A14 MET A 156 TYR A 157 0 SHEET 2 A14 GLY A 23 PHE A 32 -1 N SER A 30 O MET A 156 SHEET 3 A14 GLY A 123 ALA A 128 -1 O PHE A 126 N ALA A 29 SHEET 4 A14 THR A 109 SER A 114 -1 N PHE A 112 O SER A 125 SHEET 5 A14 ARG A 95 LEU A 102 -1 N LEU A 102 O MET A 111 SHEET 6 A14 THR A 87 GLU A 92 -1 N ARG A 90 O HIS A 97 SHEET 7 A14 GLN A 71 GLN A 82 -1 N GLN A 82 O THR A 87 SHEET 8 A14 GLN B 71 GLN B 82 -1 O SER B 76 N SER A 76 SHEET 9 A14 THR B 87 GLU B 92 -1 O THR B 87 N GLN B 82 SHEET 10 A14 ARG B 95 LEU B 102 -1 O HIS B 97 N ARG B 90 SHEET 11 A14 THR B 109 SER B 114 -1 O MET B 111 N LEU B 102 SHEET 12 A14 GLY B 123 ALA B 128 -1 O GLY B 123 N SER B 114 SHEET 13 A14 GLY B 23 PHE B 32 -1 N ALA B 29 O PHE B 126 SHEET 14 A14 MET B 156 TYR B 157 -1 O MET B 156 N SER B 30 SHEET 1 B 8 GLY B 23 PHE B 32 0 SHEET 2 B 8 ILE B 44 ASN B 54 -1 O THR B 47 N TYR B 27 SHEET 3 B 8 THR B 59 ARG B 68 -1 O THR B 59 N ASN B 54 SHEET 4 B 8 GLN B 71 GLN B 82 -1 O SER B 77 N LEU B 62 SHEET 5 B 8 THR B 87 GLU B 92 -1 O THR B 87 N GLN B 82 SHEET 6 B 8 ARG B 95 LEU B 102 -1 O HIS B 97 N ARG B 90 SHEET 7 B 8 THR B 109 SER B 114 -1 O MET B 111 N LEU B 102 SHEET 8 B 8 GLY B 123 ALA B 128 -1 O GLY B 123 N SER B 114 SHEET 1 C10 MET B 156 TYR B 157 0 SHEET 2 C10 GLY B 23 PHE B 32 -1 N SER B 30 O MET B 156 SHEET 3 C10 ILE B 44 ASN B 54 -1 O THR B 47 N TYR B 27 SHEET 4 C10 THR B 59 ARG B 68 -1 O THR B 59 N ASN B 54 SHEET 5 C10 GLN B 71 GLN B 82 -1 O SER B 77 N LEU B 62 SHEET 6 C10 GLN A 71 GLN A 82 -1 N SER A 76 O SER B 76 SHEET 7 C10 THR A 59 ARG A 68 -1 N LEU A 62 O SER A 77 SHEET 8 C10 ILE A 44 ASN A 54 -1 N PHE A 48 O TYR A 65 SHEET 9 C10 GLY A 23 PHE A 32 -1 N GLY A 23 O PHE A 51 SHEET 10 C10 MET A 156 TYR A 157 -1 O MET A 156 N SER A 30 SHEET 1 D 8 GLY A 23 PHE A 32 0 SHEET 2 D 8 ILE A 44 ASN A 54 -1 O PHE A 51 N GLY A 23 SHEET 3 D 8 THR A 59 ARG A 68 -1 O TYR A 65 N PHE A 48 SHEET 4 D 8 GLN A 71 GLN A 82 -1 O SER A 77 N LEU A 62 SHEET 5 D 8 THR A 87 GLU A 92 -1 O THR A 87 N GLN A 82 SHEET 6 D 8 ARG A 95 LEU A 102 -1 O HIS A 97 N ARG A 90 SHEET 7 D 8 THR A 109 SER A 114 -1 O MET A 111 N LEU A 102 SHEET 8 D 8 GLY A 123 ALA A 128 -1 O SER A 125 N PHE A 112 SSBOND 1 CYS A 5 CYS A 147 1555 1555 2.06 SSBOND 2 CYS A 72 CYS A 165 1555 1555 2.03 SSBOND 3 CYS B 5 CYS B 147 1555 1555 2.04 SSBOND 4 CYS B 72 CYS B 165 1555 1555 2.04 SITE 1 AC1 5 VAL A 41 GLU A 64 ARG A 90 TYR A 127 SITE 2 AC1 5 HOH A 229 SITE 1 AC2 6 TYR B 27 VAL B 41 GLU B 64 ARG B 90 SITE 2 AC2 6 SER B 125 TYR B 127 CRYST1 67.107 44.862 120.784 90.00 91.88 90.00 C 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 0.014902 0.000000 0.000489 0.00000 SCALE2 0.000000 0.022291 0.000000 0.00000 SCALE3 0.000000 0.000000 0.008284 0.00000 ATOM 1 N GLN A 1 16.609 4.238 -12.023 1.00 66.38 N ANISOU 1 N GLN A 1 8468 8638 8114 998 799 919 N ATOM 2 CA GLN A 1 15.903 5.538 -12.206 1.00 67.10 C ANISOU 2 CA GLN A 1 8740 8605 8149 973 622 1156 C ATOM 3 C GLN A 1 15.999 6.402 -10.938 1.00 64.50 C ANISOU 3 C GLN A 1 8389 7976 8140 860 563 1297 C ATOM 4 O GLN A 1 16.358 7.574 -11.016 1.00 65.73 O ANISOU 4 O GLN A 1 8690 8029 8255 737 572 1580 O ATOM 5 CB GLN A 1 14.432 5.339 -12.657 1.00 67.95 C ANISOU 5 CB GLN A 1 8937 8742 8140 1144 375 1002 C ATOM 6 CG GLN A 1 13.413 4.913 -11.561 1.00 67.19 C ANISOU 6 CG GLN A 1 8722 8474 8333 1197 198 777 C ATOM 7 CD GLN A 1 13.499 3.427 -11.185 1.00 69.31 C ANISOU 7 CD GLN A 1 8851 8773 8712 1187 280 457 C ATOM 8 OE1 GLN A 1 13.236 2.543 -12.013 1.00 72.38 O ANISOU 8 OE1 GLN A 1 9273 9339 8889 1240 284 257 O ATOM 9 NE2 GLN A 1 13.857 3.149 -9.928 1.00 67.43 N ANISOU 9 NE2 GLN A 1 8489 8342 8790 1120 337 406 N ATOM 10 N ILE A 2 15.708 5.809 -9.778 1.00 60.37 N ANISOU 10 N ILE A 2 7713 7307 7917 886 511 1098 N ATOM 11 CA ILE A 2 15.624 6.552 -8.525 1.00 57.22 C ANISOU 11 CA ILE A 2 7298 6633 7809 810 429 1180 C ATOM 12 C ILE A 2 16.878 6.323 -7.689 1.00 54.99 C ANISOU 12 C ILE A 2 6840 6340 7715 658 610 1199 C ATOM 13 O ILE A 2 17.271 5.183 -7.474 1.00 54.27 O ANISOU 13 O ILE A 2 6587 6358 7675 710 714 1010 O ATOM 14 CB ILE A 2 14.323 6.210 -7.754 1.00 55.11 C ANISOU 14 CB ILE A 2 6980 6241 7718 940 227 968 C ATOM 15 CG1 ILE A 2 13.717 7.454 -7.107 1.00 54.77 C ANISOU 15 CG1 ILE A 2 7053 5959 7796 968 58 1106 C ATOM 16 CG2 ILE A 2 14.480 4.997 -6.799 1.00 54.05 C ANISOU 16 CG2 ILE A 2 6650 6082 7804 922 295 725 C ATOM 17 CD1 ILE A 2 12.541 7.987 -7.911 1.00 55.99 C ANISOU 17 CD1 ILE A 2 7362 6169 7744 1163 -145 1139 C ATOM 18 N PRO A 3 17.523 7.407 -7.228 1.00 54.06 N ANISOU 18 N PRO A 3 6767 6091 7681 471 639 1424 N ATOM 19 CA PRO A 3 18.804 7.237 -6.555 1.00 52.88 C ANISOU 19 CA PRO A 3 6413 6018 7662 306 810 1451 C ATOM 20 C PRO A 3 18.692 6.387 -5.300 1.00 49.21 C ANISOU 20 C PRO A 3 5765 5465 7469 389 776 1231 C ATOM 21 O PRO A 3 17.697 6.463 -4.576 1.00 46.37 O ANISOU 21 O PRO A 3 5460 4890 7268 468 607 1136 O ATOM 22 CB PRO A 3 19.215 8.674 -6.196 1.00 54.45 C ANISOU 22 CB PRO A 3 6749 6027 7911 56 786 1712 C ATOM 23 CG PRO A 3 18.446 9.526 -7.139 1.00 56.31 C ANISOU 23 CG PRO A 3 7300 6155 7940 104 672 1875 C ATOM 24 CD PRO A 3 17.128 8.822 -7.286 1.00 55.39 C ANISOU 24 CD PRO A 3 7194 6032 7820 404 510 1655 C ATOM 25 N LEU A 4 19.732 5.593 -5.067 1.00 48.84 N ANISOU 25 N LEU A 4 5500 5610 7449 386 941 1160 N ATOM 26 CA LEU A 4 19.794 4.661 -3.957 1.00 46.82 C ANISOU 26 CA LEU A 4 5091 5293 7406 488 931 971 C ATOM 27 C LEU A 4 19.405 5.339 -2.637 1.00 44.29 C ANISOU 27 C LEU A 4 4784 4708 7338 392 788 998 C ATOM 28 O LEU A 4 18.627 4.801 -1.858 1.00 42.80 O ANISOU 28 O LEU A 4 4599 4367 7297 496 686 841 O ATOM 29 CB LEU A 4 21.212 4.044 -3.878 1.00 48.24 C ANISOU 29 CB LEU A 4 5030 5746 7554 501 1129 959 C ATOM 30 CG LEU A 4 21.388 2.642 -3.246 1.00 49.38 C ANISOU 30 CG LEU A 4 5067 5901 7795 727 1163 737 C ATOM 31 CD1 LEU A 4 20.323 1.626 -3.711 1.00 50.42 C ANISOU 31 CD1 LEU A 4 5380 5911 7865 914 1099 526 C ATOM 32 CD2 LEU A 4 22.810 2.091 -3.454 1.00 50.24 C ANISOU 32 CD2 LEU A 4 4940 6351 7799 819 1363 733 C ATOM 33 N CYS A 5 19.929 6.533 -2.409 1.00 44.07 N ANISOU 33 N CYS A 5 4783 4623 7337 175 786 1195 N ATOM 34 CA CYS A 5 19.797 7.197 -1.139 1.00 42.13 C ANISOU 34 CA CYS A 5 4548 4150 7309 71 673 1210 C ATOM 35 C CYS A 5 18.474 8.012 -1.006 1.00 40.58 C ANISOU 35 C CYS A 5 4600 3662 7155 132 477 1220 C ATOM 36 O CYS A 5 18.258 8.652 0.023 1.00 39.97 O ANISOU 36 O CYS A 5 4572 3376 7239 74 374 1218 O ATOM 37 CB CYS A 5 21.019 8.126 -0.931 1.00 44.39 C ANISOU 37 CB CYS A 5 4770 4504 7594 -229 756 1399 C ATOM 38 SG CYS A 5 22.604 7.293 -0.413 1.00 48.55 S ANISOU 38 SG CYS A 5 4895 5403 8150 -283 935 1350 S ATOM 39 N ALA A 6 17.615 8.026 -2.025 1.00 39.63 N ANISOU 39 N ALA A 6 4632 3552 6874 268 419 1222 N ATOM 40 CA ALA A 6 16.446 8.932 -1.987 1.00 39.15 C ANISOU 40 CA ALA A 6 4795 3264 6816 366 227 1255 C ATOM 41 C ALA A 6 15.618 8.756 -0.711 1.00 36.44 C ANISOU 41 C ALA A 6 4384 2777 6685 472 102 1078 C ATOM 42 O ALA A 6 15.285 9.717 -0.051 1.00 34.91 O ANISOU 42 O ALA A 6 4321 2363 6581 469 -9 1122 O ATOM 43 CB ALA A 6 15.584 8.813 -3.245 1.00 40.25 C ANISOU 43 CB ALA A 6 5055 3505 6731 539 163 1253 C ATOM 44 N ASN A 7 15.356 7.519 -0.303 1.00 35.09 N ANISOU 44 N ASN A 7 4026 2721 6587 552 133 878 N ATOM 45 CA ASN A 7 14.500 7.337 0.870 1.00 34.29 C ANISOU 45 CA ASN A 7 3860 2517 6651 629 28 721 C ATOM 46 C ASN A 7 15.266 7.303 2.203 1.00 32.28 C ANISOU 46 C ASN A 7 3499 2181 6584 510 75 708 C ATOM 47 O ASN A 7 14.687 7.020 3.253 1.00 31.22 O ANISOU 47 O ASN A 7 3298 1990 6574 557 17 578 O ATOM 48 CB ASN A 7 13.562 6.124 0.682 1.00 34.92 C ANISOU 48 CB ASN A 7 3842 2732 6694 742 8 515 C ATOM 49 CG ASN A 7 14.323 4.847 0.471 1.00 35.17 C ANISOU 49 CG ASN A 7 3780 2880 6705 702 157 442 C ATOM 50 OD1 ASN A 7 13.800 3.757 0.686 1.00 40.45 O ANISOU 50 OD1 ASN A 7 4395 3583 7391 733 162 269 O ATOM 51 ND2 ASN A 7 15.569 4.967 0.042 1.00 40.42 N ANISOU 51 ND2 ASN A 7 4431 3609 7316 632 284 571 N ATOM 52 N LEU A 8 16.556 7.639 2.170 1.00 32.22 N ANISOU 52 N LEU A 8 3466 2201 6577 344 176 844 N ATOM 53 CA LEU A 8 17.298 7.921 3.411 1.00 31.61 C ANISOU 53 CA LEU A 8 3303 2057 6652 210 184 853 C ATOM 54 C LEU A 8 17.286 9.412 3.821 1.00 31.71 C ANISOU 54 C LEU A 8 3506 1836 6707 85 83 960 C ATOM 55 O LEU A 8 17.857 9.777 4.852 1.00 31.28 O ANISOU 55 O LEU A 8 3408 1715 6763 -52 67 955 O ATOM 56 CB LEU A 8 18.749 7.418 3.325 1.00 33.75 C ANISOU 56 CB LEU A 8 3385 2540 6900 88 338 913 C ATOM 57 CG LEU A 8 19.029 5.900 3.288 1.00 33.41 C ANISOU 57 CG LEU A 8 3170 2682 6842 237 439 789 C ATOM 58 CD1 LEU A 8 18.837 5.370 4.688 1.00 34.96 C ANISOU 58 CD1 LEU A 8 3289 2801 7192 291 385 670 C ATOM 59 CD2 LEU A 8 18.099 5.192 2.274 1.00 32.69 C ANISOU 59 CD2 LEU A 8 3174 2613 6634 400 439 700 C ATOM 60 N VAL A 9 16.639 10.262 3.021 1.00 32.84 N ANISOU 60 N VAL A 9 3887 1845 6746 144 4 1051 N ATOM 61 CA VAL A 9 16.489 11.688 3.363 1.00 34.51 C ANISOU 61 CA VAL A 9 4371 1761 6981 75 -110 1143 C ATOM 62 C VAL A 9 15.362 11.925 4.355 1.00 33.49 C ANISOU 62 C VAL A 9 4292 1476 6956 283 -257 981 C ATOM 63 O VAL A 9 14.240 11.500 4.128 1.00 32.74 O ANISOU 63 O VAL A 9 4157 1459 6826 529 -321 871 O ATOM 64 CB VAL A 9 16.233 12.572 2.117 1.00 37.13 C ANISOU 64 CB VAL A 9 5000 1973 7134 98 -150 1328 C ATOM 65 CG1 VAL A 9 16.244 14.041 2.513 1.00 39.42 C ANISOU 65 CG1 VAL A 9 5640 1895 7444 4 -258 1435 C ATOM 66 CG2 VAL A 9 17.295 12.286 1.070 1.00 38.40 C ANISOU 66 CG2 VAL A 9 5090 2347 7154 -106 18 1485 C ATOM 67 N PRO A 10 15.661 12.605 5.466 1.00 33.77 N ANISOU 67 N PRO A 10 4402 1325 7104 174 -308 952 N ATOM 68 CA PRO A 10 14.579 12.898 6.399 1.00 33.50 C ANISOU 68 CA PRO A 10 4423 1165 7141 396 -438 788 C ATOM 69 C PRO A 10 13.323 13.497 5.724 1.00 35.46 C ANISOU 69 C PRO A 10 4877 1312 7283 702 -566 788 C ATOM 70 O PRO A 10 13.389 14.300 4.791 1.00 36.98 O ANISOU 70 O PRO A 10 5341 1348 7361 708 -605 955 O ATOM 71 CB PRO A 10 15.204 13.897 7.388 1.00 35.60 C ANISOU 71 CB PRO A 10 4860 1179 7488 210 -487 798 C ATOM 72 CG PRO A 10 16.724 14.037 6.966 1.00 37.65 C ANISOU 72 CG PRO A 10 5099 1482 7724 -174 -373 976 C ATOM 73 CD PRO A 10 16.998 12.877 6.044 1.00 34.77 C ANISOU 73 CD PRO A 10 4478 1439 7294 -152 -240 1019 C ATOM 74 N VAL A 11 12.172 13.053 6.179 1.00 34.51 N ANISOU 74 N VAL A 11 4610 1319 7182 957 -630 604 N ATOM 75 CA VAL A 11 10.937 13.612 5.673 1.00 36.61 C ANISOU 75 CA VAL A 11 5010 1560 7340 1291 -768 574 C ATOM 76 C VAL A 11 10.064 14.075 6.835 1.00 35.63 C ANISOU 76 C VAL A 11 4891 1372 7275 1517 -870 390 C ATOM 77 O VAL A 11 9.863 13.336 7.806 1.00 33.73 O ANISOU 77 O VAL A 11 4391 1303 7122 1482 -819 228 O ATOM 78 CB VAL A 11 10.229 12.644 4.706 1.00 35.73 C ANISOU 78 CB VAL A 11 4687 1770 7120 1413 -755 531 C ATOM 79 CG1 VAL A 11 10.114 11.295 5.304 1.00 37.83 C ANISOU 79 CG1 VAL A 11 4612 2293 7468 1315 -659 366 C ATOM 80 CG2 VAL A 11 8.861 13.208 4.263 1.00 38.97 C ANISOU 80 CG2 VAL A 11 5172 2235 7401 1795 -923 475 C ATOM 81 N PRO A 12 9.587 15.324 6.760 1.00 38.50 N ANISOU 81 N PRO A 12 5581 1474 7575 1757 -1010 421 N ATOM 82 CA PRO A 12 8.741 15.842 7.841 1.00 39.32 C ANISOU 82 CA PRO A 12 5708 1526 7708 2030 -1107 227 C ATOM 83 C PRO A 12 7.518 14.948 8.088 1.00 38.21 C ANISOU 83 C PRO A 12 5170 1813 7537 2255 -1111 22 C ATOM 84 O PRO A 12 6.986 14.354 7.156 1.00 38.09 O ANISOU 84 O PRO A 12 4987 2059 7428 2333 -1118 37 O ATOM 85 CB PRO A 12 8.316 17.241 7.342 1.00 43.34 C ANISOU 85 CB PRO A 12 6665 1698 8103 2336 -1269 315 C ATOM 86 CG PRO A 12 8.772 17.330 5.912 1.00 44.31 C ANISOU 86 CG PRO A 12 6960 1759 8116 2229 -1258 563 C ATOM 87 CD PRO A 12 9.872 16.341 5.730 1.00 41.31 C ANISOU 87 CD PRO A 12 6339 1542 7813 1787 -1079 642 C ATOM 88 N ILE A 13 7.083 14.888 9.343 1.00 37.84 N ANISOU 88 N ILE A 13 4982 1847 7549 2333 -1105 -173 N ATOM 89 CA ILE A 13 6.006 14.000 9.759 1.00 36.96 C ANISOU 89 CA ILE A 13 4469 2167 7406 2455 -1078 -370 C ATOM 90 C ILE A 13 4.733 14.796 9.802 1.00 40.09 C ANISOU 90 C ILE A 13 4887 2662 7683 2930 -1222 -502 C ATOM 91 O ILE A 13 4.655 15.827 10.489 1.00 42.28 O ANISOU 91 O ILE A 13 5411 2692 7962 3144 -1297 -566 O ATOM 92 CB ILE A 13 6.307 13.391 11.140 1.00 34.99 C ANISOU 92 CB ILE A 13 4036 1997 7261 2242 -967 -493 C ATOM 93 CG1 ILE A 13 7.472 12.413 11.010 1.00 32.28 C ANISOU 93 CG1 ILE A 13 3617 1636 7011 1835 -831 -370 C ATOM 94 CG2 ILE A 13 5.094 12.648 11.736 1.00 35.17 C ANISOU 94 CG2 ILE A 13 3682 2454 7226 2360 -934 -702 C ATOM 95 CD1 ILE A 13 8.070 12.031 12.310 1.00 30.80 C ANISOU 95 CD1 ILE A 13 3354 1432 6916 1631 -748 -431 C ATOM 96 N THR A 14 3.744 14.354 9.036 1.00 41.68 N ANISOU 96 N THR A 14 4844 3230 7764 3116 -1271 -553 N ATOM 97 CA THR A 14 2.436 15.024 9.022 1.00 45.55 C ANISOU 97 CA THR A 14 5269 3927 8110 3621 -1418 -696 C ATOM 98 C THR A 14 1.434 14.221 9.834 1.00 45.24 C ANISOU 98 C THR A 14 4745 4404 8040 3643 -1353 -939 C ATOM 99 O THR A 14 1.758 13.139 10.347 1.00 41.68 O ANISOU 99 O THR A 14 4064 4096 7675 3252 -1200 -973 O ATOM 100 CB THR A 14 1.844 15.166 7.590 1.00 48.06 C ANISOU 100 CB THR A 14 5596 4400 8262 3869 -1550 -606 C ATOM 101 OG1 THR A 14 1.684 13.865 7.012 1.00 46.74 O ANISOU 101 OG1 THR A 14 5071 4614 8074 3584 -1469 -626 O ATOM 102 CG2 THR A 14 2.713 16.043 6.699 1.00 50.12 C ANISOU 102 CG2 THR A 14 6366 4172 8506 3874 -1617 -345 C ATOM 103 N ASN A 15 0.210 14.756 9.941 1.00 48.30 N ANISOU 103 N ASN A 15 4983 5085 8284 4111 -1469 -1103 N ATOM 104 CA ASN A 15 -0.913 13.933 10.352 1.00 49.22 C ANISOU 104 CA ASN A 15 4564 5824 8314 4120 -1417 -1320 C ATOM 105 C ASN A 15 -1.091 12.650 9.532 1.00 47.34 C ANISOU 105 C ASN A 15 4012 5930 8045 3769 -1359 -1294 C ATOM 106 O ASN A 15 -1.351 11.619 10.117 1.00 46.62 O ANISOU 106 O ASN A 15 3593 6145 7974 3452 -1224 -1404 O ATOM 107 CB ASN A 15 -2.204 14.719 10.372 1.00 53.54 C ANISOU 107 CB ASN A 15 4957 6707 8678 4716 -1566 -1492 C ATOM 108 CG ASN A 15 -2.293 15.641 11.574 1.00 56.71 C ANISOU 108 CG ASN A 15 5526 6933 9089 5025 -1570 -1628 C ATOM 109 OD1 ASN A 15 -1.354 15.736 12.390 1.00 58.19 O ANISOU 109 OD1 ASN A 15 5963 6726 9421 4765 -1473 -1587 O ATOM 110 ND2 ASN A 15 -3.413 16.287 11.711 1.00 57.76 N ANISOU 110 ND2 ASN A 15 5504 7388 9054 5583 -1684 -1807 N ATOM 111 N ALA A 16 -0.955 12.715 8.207 1.00 47.62 N ANISOU 111 N ALA A 16 4177 5900 8015 3814 -1458 -1152 N ATOM 112 CA ALA A 16 -1.025 11.508 7.353 1.00 46.43 C ANISOU 112 CA ALA A 16 3793 6024 7826 3468 -1409 -1136 C ATOM 113 C ALA A 16 0.079 10.531 7.679 1.00 43.17 C ANISOU 113 C ALA A 16 3457 5364 7581 2940 -1220 -1051 C ATOM 114 O ALA A 16 -0.137 9.314 7.612 1.00 42.72 O ANISOU 114 O ALA A 16 3145 5572 7514 2603 -1126 -1127 O ATOM 115 CB ALA A 16 -0.978 11.861 5.875 1.00 47.07 C ANISOU 115 CB ALA A 16 4055 6046 7783 3640 -1553 -989 C ATOM 116 N THR A 17 1.272 11.041 8.010 1.00 41.94 N ANISOU 116 N THR A 17 3665 4705 7566 2862 -1171 -896 N ATOM 117 CA THR A 17 2.387 10.147 8.307 1.00 38.50 C ANISOU 117 CA THR A 17 3291 4062 7275 2417 -1005 -810 C ATOM 118 C THR A 17 2.018 9.383 9.565 1.00 37.70 C ANISOU 118 C THR A 17 2927 4178 7220 2229 -885 -968 C ATOM 119 O THR A 17 2.271 8.174 9.649 1.00 36.00 O ANISOU 119 O THR A 17 2598 4038 7043 1877 -763 -974 O ATOM 120 CB THR A 17 3.691 10.890 8.637 1.00 38.26 C ANISOU 120 CB THR A 17 3631 3532 7374 2359 -978 -645 C ATOM 121 OG1 THR A 17 3.943 11.931 7.687 1.00 40.93 O ANISOU 121 OG1 THR A 17 4276 3625 7650 2575 -1098 -492 O ATOM 122 CG2 THR A 17 4.853 9.917 8.684 1.00 34.38 C ANISOU 122 CG2 THR A 17 3164 2902 6995 1954 -826 -546 C ATOM 123 N LEU A 18 1.476 10.108 10.552 1.00 38.04 N ANISOU 123 N LEU A 18 2919 4288 7247 2471 -917 -1087 N ATOM 124 CA LEU A 18 1.071 9.511 11.837 1.00 38.53 C ANISOU 124 CA LEU A 18 2738 4584 7319 2317 -797 -1235 C ATOM 125 C LEU A 18 -0.053 8.473 11.640 1.00 40.55 C ANISOU 125 C LEU A 18 2586 5369 7454 2163 -754 -1378 C ATOM 126 O LEU A 18 0.006 7.375 12.214 1.00 38.94 O ANISOU 126 O LEU A 18 2253 5267 7274 1792 -611 -1407 O ATOM 127 CB LEU A 18 0.665 10.591 12.877 1.00 39.45 C ANISOU 127 CB LEU A 18 2887 4697 7406 2657 -844 -1357 C ATOM 128 CG LEU A 18 1.826 11.458 13.398 1.00 38.40 C ANISOU 128 CG LEU A 18 3157 4038 7394 2682 -859 -1251 C ATOM 129 CD1 LEU A 18 1.387 12.711 14.146 1.00 40.24 C ANISOU 129 CD1 LEU A 18 3516 4199 7572 3092 -947 -1383 C ATOM 130 CD2 LEU A 18 2.852 10.663 14.239 1.00 34.81 C ANISOU 130 CD2 LEU A 18 2743 3423 7060 2270 -712 -1184 C ATOM 131 N ASP A 19 -1.069 8.817 10.841 1.00 43.75 N ANISOU 131 N ASP A 19 2799 6109 7714 2434 -884 -1464 N ATOM 132 CA ASP A 19 -2.093 7.827 10.443 1.00 46.42 C ANISOU 132 CA ASP A 19 2741 6974 7921 2233 -865 -1599 C ATOM 133 C ASP A 19 -1.496 6.561 9.822 1.00 45.00 C ANISOU 133 C ASP A 19 2637 6668 7794 1763 -776 -1514 C ATOM 134 O ASP A 19 -1.852 5.435 10.188 1.00 46.04 O ANISOU 134 O ASP A 19 2575 7022 7898 1381 -658 -1599 O ATOM 135 CB ASP A 19 -3.099 8.440 9.464 1.00 49.96 C ANISOU 135 CB ASP A 19 3004 7784 8195 2621 -1055 -1678 C ATOM 136 CG ASP A 19 -4.195 9.224 10.168 1.00 54.63 C ANISOU 136 CG ASP A 19 3316 8779 8662 3037 -1116 -1863 C ATOM 137 OD1 ASP A 19 -4.951 9.935 9.473 1.00 58.73 O ANISOU 137 OD1 ASP A 19 3725 9557 9034 3476 -1294 -1919 O ATOM 138 OD2 ASP A 19 -4.308 9.123 11.412 1.00 56.02 O ANISOU 138 OD2 ASP A 19 3381 9035 8867 2953 -989 -1956 O ATOM 139 N ARG A 20 -0.581 6.759 8.883 1.00 43.53 N ANISOU 139 N ARG A 20 2759 6114 7667 1793 -826 -1347 N ATOM 140 CA ARG A 20 0.097 5.679 8.202 1.00 41.77 C ANISOU 140 CA ARG A 20 2658 5733 7482 1434 -749 -1269 C ATOM 141 C ARG A 20 0.849 4.698 9.152 1.00 39.57 C ANISOU 141 C ARG A 20 2473 5232 7329 1060 -564 -1233 C ATOM 142 O ARG A 20 0.865 3.493 8.889 1.00 38.63 O ANISOU 142 O ARG A 20 2337 5150 7190 723 -483 -1263 O ATOM 143 CB ARG A 20 1.035 6.282 7.152 1.00 40.68 C ANISOU 143 CB ARG A 20 2838 5247 7372 1591 -821 -1084 C ATOM 144 CG ARG A 20 1.984 5.298 6.519 1.00 40.23 C ANISOU 144 CG ARG A 20 2954 4971 7362 1284 -724 -991 C ATOM 145 CD ARG A 20 2.731 5.985 5.428 1.00 39.78 C ANISOU 145 CD ARG A 20 3152 4681 7282 1454 -794 -822 C ATOM 146 NE ARG A 20 3.609 5.068 4.739 1.00 38.38 N ANISOU 146 NE ARG A 20 3114 4350 7117 1210 -697 -753 N ATOM 147 CZ ARG A 20 4.285 5.381 3.643 1.00 41.17 C ANISOU 147 CZ ARG A 20 3663 4564 7414 1283 -723 -616 C ATOM 148 NH1 ARG A 20 4.159 6.606 3.121 1.00 40.59 N ANISOU 148 NH1 ARG A 20 3699 4454 7270 1572 -850 -511 N ATOM 149 NH2 ARG A 20 5.084 4.477 3.074 1.00 38.59 N ANISOU 149 NH2 ARG A 20 3444 4133 7085 1081 -617 -581 N ATOM 150 N ILE A 21 1.442 5.190 10.252 1.00 37.29 N ANISOU 150 N ILE A 21 2304 4714 7152 1124 -508 -1175 N ATOM 151 CA ILE A 21 2.184 4.294 11.178 1.00 34.37 C ANISOU 151 CA ILE A 21 2035 4146 6878 816 -352 -1125 C ATOM 152 C ILE A 21 1.365 3.788 12.366 1.00 35.40 C ANISOU 152 C ILE A 21 1941 4558 6950 649 -257 -1252 C ATOM 153 O ILE A 21 1.882 3.074 13.231 1.00 33.24 O ANISOU 153 O ILE A 21 1764 4138 6727 414 -135 -1203 O ATOM 154 CB ILE A 21 3.479 4.934 11.690 1.00 32.68 C ANISOU 154 CB ILE A 21 2087 3528 6801 908 -338 -976 C ATOM 155 CG1 ILE A 21 3.158 6.161 12.575 1.00 35.05 C ANISOU 155 CG1 ILE A 21 2363 3853 7103 1185 -399 -1035 C ATOM 156 CG2 ILE A 21 4.330 5.323 10.503 1.00 32.58 C ANISOU 156 CG2 ILE A 21 2283 3270 6825 997 -399 -836 C ATOM 157 CD1 ILE A 21 4.390 6.865 13.098 1.00 36.12 C ANISOU 157 CD1 ILE A 21 2760 3606 7357 1235 -403 -913 C ATOM 158 N THR A 22 0.081 4.150 12.399 1.00 37.55 N ANISOU 158 N THR A 22 1906 5267 7094 780 -313 -1412 N ATOM 159 CA THR A 22 -0.802 3.712 13.460 1.00 39.38 C ANISOU 159 CA THR A 22 1872 5857 7233 611 -211 -1544 C ATOM 160 C THR A 22 -1.013 2.191 13.378 1.00 40.85 C ANISOU 160 C THR A 22 2021 6129 7371 108 -90 -1559 C ATOM 161 O THR A 22 -1.262 1.641 12.304 1.00 42.23 O ANISOU 161 O THR A 22 2170 6379 7499 -34 -137 -1590 O ATOM 162 CB THR A 22 -2.147 4.493 13.389 1.00 42.53 C ANISOU 162 CB THR A 22 1901 6777 7481 911 -306 -1727 C ATOM 163 OG1 THR A 22 -1.853 5.892 13.507 1.00 41.65 O ANISOU 163 OG1 THR A 22 1932 6478 7417 1391 -418 -1702 O ATOM 164 CG2 THR A 22 -3.110 4.085 14.504 1.00 43.07 C ANISOU 164 CG2 THR A 22 1638 7304 7423 732 -180 -1875 C ATOM 165 N GLY A 23 -0.888 1.519 14.517 1.00 40.78 N ANISOU 165 N GLY A 23 2052 6081 7359 -163 59 -1536 N ATOM 166 CA GLY A 23 -1.298 0.122 14.630 1.00 41.73 C ANISOU 166 CA GLY A 23 2149 6309 7398 -661 183 -1563 C ATOM 167 C GLY A 23 -0.126 -0.755 15.033 1.00 38.95 C ANISOU 167 C GLY A 23 2195 5458 7144 -874 283 -1393 C ATOM 168 O GLY A 23 0.789 -0.310 15.738 1.00 36.26 O ANISOU 168 O GLY A 23 2037 4840 6902 -690 296 -1279 O ATOM 169 N LYS A 24 -0.196 -2.006 14.605 1.00 39.46 N ANISOU 169 N LYS A 24 2395 5431 7166 -1258 347 -1390 N ATOM 170 CA LYS A 24 0.691 -3.067 15.062 1.00 38.26 C ANISOU 170 CA LYS A 24 2625 4854 7059 -1491 455 -1248 C ATOM 171 C LYS A 24 1.830 -3.244 14.072 1.00 36.74 C ANISOU 171 C LYS A 24 2734 4243 6983 -1336 393 -1154 C ATOM 172 O LYS A 24 1.613 -3.288 12.855 1.00 36.12 O ANISOU 172 O LYS A 24 2620 4219 6885 -1324 314 -1229 O ATOM 173 CB LYS A 24 -0.084 -4.387 15.231 1.00 41.53 C ANISOU 173 CB LYS A 24 3075 5371 7334 -2024 571 -1304 C ATOM 174 CG LYS A 24 0.687 -5.473 15.980 1.00 41.04 C ANISOU 174 CG LYS A 24 3438 4877 7279 -2251 694 -1145 C ATOM 175 CD LYS A 24 -0.110 -6.791 16.061 1.00 44.82 C ANISOU 175 CD LYS A 24 4025 5399 7605 -2829 806 -1195 C ATOM 176 CE LYS A 24 0.658 -7.862 16.849 1.00 43.68 C ANISOU 176 CE LYS A 24 4373 4776 7448 -3014 920 -1013 C ATOM 177 NZ LYS A 24 -0.102 -9.155 16.952 1.00 49.84 N ANISOU 177 NZ LYS A 24 5341 5528 8067 -3619 1035 -1045 N ATOM 178 N TRP A 25 3.050 -3.296 14.610 1.00 35.29 N ANISOU 178 N TRP A 25 2818 3690 6900 -1196 425 -995 N ATOM 179 CA TRP A 25 4.243 -3.549 13.812 1.00 34.29 C ANISOU 179 CA TRP A 25 2964 3199 6867 -1046 394 -898 C ATOM 180 C TRP A 25 5.103 -4.682 14.392 1.00 34.72 C ANISOU 180 C TRP A 25 3376 2889 6929 -1166 490 -773 C ATOM 181 O TRP A 25 5.075 -4.985 15.595 1.00 35.50 O ANISOU 181 O TRP A 25 3537 2962 6989 -1278 565 -708 O ATOM 182 CB TRP A 25 5.061 -2.268 13.619 1.00 30.73 C ANISOU 182 CB TRP A 25 2455 2692 6530 -661 302 -826 C ATOM 183 CG TRP A 25 4.286 -1.170 12.922 1.00 32.23 C ANISOU 183 CG TRP A 25 2380 3167 6700 -489 191 -928 C ATOM 184 CD1 TRP A 25 3.516 -0.204 13.519 1.00 34.36 C ANISOU 184 CD1 TRP A 25 2403 3712 6940 -360 148 -1002 C ATOM 185 CD2 TRP A 25 4.172 -0.953 11.508 1.00 32.47 C ANISOU 185 CD2 TRP A 25 2385 3244 6708 -396 104 -969 C ATOM 186 NE1 TRP A 25 2.940 0.605 12.566 1.00 34.80 N ANISOU 186 NE1 TRP A 25 2296 3965 6963 -166 30 -1078 N ATOM 187 CE2 TRP A 25 3.326 0.170 11.322 1.00 34.89 C ANISOU 187 CE2 TRP A 25 2437 3845 6974 -197 -1 -1050 C ATOM 188 CE3 TRP A 25 4.688 -1.611 10.375 1.00 33.96 C ANISOU 188 CE3 TRP A 25 2754 3264 6886 -441 103 -952 C ATOM 189 CZ2 TRP A 25 2.987 0.659 10.050 1.00 34.78 C ANISOU 189 CZ2 TRP A 25 2350 3959 6905 -46 -116 -1092 C ATOM 190 CZ3 TRP A 25 4.375 -1.113 9.109 1.00 34.71 C ANISOU 190 CZ3 TRP A 25 2765 3498 6924 -313 1 -1002 C ATOM 191 CH2 TRP A 25 3.522 0.016 8.959 1.00 35.80 C ANISOU 191 CH2 TRP A 25 2654 3930 7018 -121 -113 -1061 C ATOM 192 N PHE A 26 5.859 -5.311 13.512 1.00 34.17 N ANISOU 192 N PHE A 26 3553 2545 6886 -1114 486 -742 N ATOM 193 CA PHE A 26 6.777 -6.349 13.914 1.00 34.75 C ANISOU 193 CA PHE A 26 3992 2252 6959 -1125 557 -626 C ATOM 194 C PHE A 26 8.176 -5.868 13.549 1.00 32.01 C ANISOU 194 C PHE A 26 3697 1749 6717 -753 511 -523 C ATOM 195 O PHE A 26 8.394 -5.397 12.444 1.00 31.63 O ANISOU 195 O PHE A 26 3564 1752 6700 -611 457 -565 O ATOM 196 CB PHE A 26 6.446 -7.656 13.178 1.00 36.13 C ANISOU 196 CB PHE A 26 4449 2235 7044 -1387 602 -706 C ATOM 197 CG PHE A 26 5.094 -8.245 13.545 1.00 40.41 C ANISOU 197 CG PHE A 26 4951 2940 7463 -1843 658 -806 C ATOM 198 CD1 PHE A 26 3.918 -7.791 12.938 1.00 39.85 C ANISOU 198 CD1 PHE A 26 4544 3261 7336 -2011 608 -973 C ATOM 199 CD2 PHE A 26 5.001 -9.267 14.491 1.00 40.03 C ANISOU 199 CD2 PHE A 26 5201 2676 7332 -2113 761 -727 C ATOM 200 CE1 PHE A 26 2.665 -8.346 13.284 1.00 43.16 C ANISOU 200 CE1 PHE A 26 4870 3906 7622 -2471 667 -1076 C ATOM 201 CE2 PHE A 26 3.753 -9.809 14.848 1.00 43.97 C ANISOU 201 CE2 PHE A 26 5652 3356 7697 -2600 831 -810 C ATOM 202 CZ PHE A 26 2.595 -9.352 14.238 1.00 43.46 C ANISOU 202 CZ PHE A 26 5201 3730 7582 -2791 787 -993 C ATOM 203 N TYR A 27 9.118 -6.008 14.474 1.00 31.62 N ANISOU 203 N TYR A 27 3776 1539 6698 -610 535 -385 N ATOM 204 CA TYR A 27 10.510 -5.681 14.226 1.00 29.96 C ANISOU 204 CA TYR A 27 3593 1225 6564 -291 502 -287 C ATOM 205 C TYR A 27 11.109 -6.823 13.427 1.00 30.99 C ANISOU 205 C TYR A 27 4023 1098 6653 -224 545 -288 C ATOM 206 O TYR A 27 11.026 -7.983 13.833 1.00 33.63 O ANISOU 206 O TYR A 27 4665 1201 6912 -333 602 -267 O ATOM 207 CB TYR A 27 11.246 -5.418 15.557 1.00 29.86 C ANISOU 207 CB TYR A 27 3574 1198 6573 -166 494 -157 C ATOM 208 CG TYR A 27 12.770 -5.454 15.498 1.00 30.57 C ANISOU 208 CG TYR A 27 3723 1189 6704 130 473 -47 C ATOM 209 CD1 TYR A 27 13.491 -6.365 16.287 1.00 30.81 C ANISOU 209 CD1 TYR A 27 3988 1042 6675 239 498 63 C ATOM 210 CD2 TYR A 27 13.480 -4.622 14.634 1.00 26.04 C ANISOU 210 CD2 TYR A 27 2973 719 6203 301 429 -48 C ATOM 211 CE1 TYR A 27 14.878 -6.428 16.235 1.00 32.86 C ANISOU 211 CE1 TYR A 27 4254 1282 6951 541 471 152 C ATOM 212 CE2 TYR A 27 14.887 -4.679 14.575 1.00 26.51 C ANISOU 212 CE2 TYR A 27 3031 763 6279 549 421 45 C ATOM 213 CZ TYR A 27 15.569 -5.562 15.379 1.00 30.44 C ANISOU 213 CZ TYR A 27 3709 1137 6721 681 437 134 C ATOM 214 OH TYR A 27 16.946 -5.620 15.313 1.00 33.29 O ANISOU 214 OH TYR A 27 4017 1554 7080 957 421 211 O ATOM 215 N ILE A 28 11.646 -6.495 12.250 1.00 29.45 N ANISOU 215 N ILE A 28 3764 939 6486 -52 520 -320 N ATOM 216 CA ILE A 28 12.107 -7.509 11.295 1.00 30.00 C ANISOU 216 CA ILE A 28 4100 804 6493 33 563 -368 C ATOM 217 C ILE A 28 13.613 -7.674 11.386 1.00 29.98 C ANISOU 217 C ILE A 28 4166 715 6510 380 580 -257 C ATOM 218 O ILE A 28 14.102 -8.799 11.497 1.00 32.66 O ANISOU 218 O ILE A 28 4821 802 6785 495 625 -241 O ATOM 219 CB ILE A 28 11.651 -7.216 9.834 1.00 29.66 C ANISOU 219 CB ILE A 28 3964 887 6417 -9 537 -497 C ATOM 220 CG1 ILE A 28 10.118 -7.173 9.737 1.00 30.25 C ANISOU 220 CG1 ILE A 28 3948 1100 6446 -345 507 -625 C ATOM 221 CG2 ILE A 28 12.293 -8.211 8.815 1.00 33.63 C ANISOU 221 CG2 ILE A 28 4749 1190 6837 133 586 -561 C ATOM 222 CD1 ILE A 28 9.350 -8.498 10.209 1.00 32.77 C ANISOU 222 CD1 ILE A 28 4563 1214 6675 -668 564 -694 C ATOM 223 N ALA A 29 14.355 -6.570 11.401 1.00 28.09 N ANISOU 223 N ALA A 29 3641 685 6345 546 542 -181 N ATOM 224 CA ALA A 29 15.816 -6.649 11.263 1.00 28.54 C ANISOU 224 CA ALA A 29 3678 764 6401 862 560 -98 C ATOM 225 C ALA A 29 16.456 -5.272 11.498 1.00 26.88 C ANISOU 225 C ALA A 29 3126 814 6274 918 509 -12 C ATOM 226 O ALA A 29 15.769 -4.252 11.431 1.00 25.47 O ANISOU 226 O ALA A 29 2777 752 6148 753 462 -33 O ATOM 227 CB ALA A 29 16.155 -7.131 9.889 1.00 29.69 C ANISOU 227 CB ALA A 29 3924 880 6477 992 611 -181 C ATOM 228 N SER A 30 17.754 -5.255 11.782 1.00 27.48 N ANISOU 228 N SER A 30 3114 980 6348 1149 513 78 N ATOM 229 CA SER A 30 18.490 -3.992 11.864 1.00 26.65 C ANISOU 229 CA SER A 30 2698 1125 6303 1157 471 150 C ATOM 230 C SER A 30 19.964 -4.231 11.579 1.00 28.32 C ANISOU 230 C SER A 30 2797 1497 6466 1422 508 208 C ATOM 231 O SER A 30 20.452 -5.419 11.548 1.00 29.93 O ANISOU 231 O SER A 30 3180 1603 6589 1672 553 198 O ATOM 232 CB SER A 30 18.296 -3.315 13.246 1.00 25.65 C ANISOU 232 CB SER A 30 2474 1038 6236 1041 391 200 C ATOM 233 OG SER A 30 19.012 -4.067 14.228 1.00 32.10 O ANISOU 233 OG SER A 30 3363 1828 7006 1212 380 268 O ATOM 234 N ALA A 31 20.681 -3.132 11.343 1.00 27.79 N ANISOU 234 N ALA A 31 2447 1682 6430 1377 492 264 N ATOM 235 CA ALA A 31 22.163 -3.167 11.241 1.00 29.58 C ANISOU 235 CA ALA A 31 2460 2177 6603 1586 522 326 C ATOM 236 C ALA A 31 22.647 -1.780 11.540 1.00 29.09 C ANISOU 236 C ALA A 31 2114 2340 6599 1383 466 394 C ATOM 237 O ALA A 31 22.038 -0.794 11.040 1.00 27.86 O ANISOU 237 O ALA A 31 1946 2145 6493 1146 452 391 O ATOM 238 CB ALA A 31 22.601 -3.561 9.845 1.00 30.93 C ANISOU 238 CB ALA A 31 2625 2444 6683 1735 631 285 C ATOM 239 N PHE A 32 23.696 -1.643 12.356 1.00 30.34 N ANISOU 239 N PHE A 32 2062 2725 6739 1460 419 452 N ATOM 240 CA PHE A 32 24.187 -0.271 12.656 1.00 30.32 C ANISOU 240 CA PHE A 32 1809 2928 6784 1201 358 503 C ATOM 241 C PHE A 32 25.680 -0.307 12.637 1.00 33.15 C ANISOU 241 C PHE A 32 1849 3685 7061 1322 379 551 C ATOM 242 O PHE A 32 26.276 -1.370 12.796 1.00 34.49 O ANISOU 242 O PHE A 32 1997 3960 7149 1656 403 547 O ATOM 243 CB PHE A 32 23.767 0.250 14.039 1.00 29.30 C ANISOU 243 CB PHE A 32 1713 2703 6719 1055 232 498 C ATOM 244 CG PHE A 32 22.317 0.124 14.308 1.00 30.36 C ANISOU 244 CG PHE A 32 2117 2512 6906 982 213 440 C ATOM 245 CD1 PHE A 32 21.772 -1.091 14.753 1.00 33.65 C ANISOU 245 CD1 PHE A 32 2750 2749 7287 1149 232 417 C ATOM 246 CD2 PHE A 32 21.475 1.216 14.108 1.00 32.33 C ANISOU 246 CD2 PHE A 32 2415 2643 7226 746 179 410 C ATOM 247 CE1 PHE A 32 20.384 -1.185 14.981 1.00 32.91 C ANISOU 247 CE1 PHE A 32 2864 2414 7227 1026 227 357 C ATOM 248 CE2 PHE A 32 20.098 1.095 14.324 1.00 31.65 C ANISOU 248 CE2 PHE A 32 2523 2330 7170 699 165 341 C ATOM 249 CZ PHE A 32 19.584 -0.081 14.762 1.00 32.10 C ANISOU 249 CZ PHE A 32 2736 2269 7191 814 194 313 C ATOM 250 N ARG A 33 26.284 0.857 12.455 1.00 33.92 N ANISOU 250 N ARG A 33 1708 4013 7169 1051 367 597 N ATOM 251 CA ARG A 33 27.730 0.952 12.642 1.00 38.77 C ANISOU 251 CA ARG A 33 1945 5089 7697 1094 368 636 C ATOM 252 C ARG A 33 28.042 1.283 14.110 1.00 39.11 C ANISOU 252 C ARG A 33 1879 5222 7759 1016 214 636 C ATOM 253 O ARG A 33 29.152 1.054 14.569 1.00 41.11 O ANISOU 253 O ARG A 33 1833 5863 7924 1144 177 651 O ATOM 254 CB ARG A 33 28.332 1.959 11.662 1.00 40.27 C ANISOU 254 CB ARG A 33 1920 5529 7853 797 449 691 C ATOM 255 CG ARG A 33 28.401 1.384 10.238 1.00 42.70 C ANISOU 255 CG ARG A 33 2248 5904 8072 975 615 690 C ATOM 256 CD ARG A 33 29.084 2.331 9.305 1.00 45.88 C ANISOU 256 CD ARG A 33 2427 6601 8404 674 712 767 C ATOM 257 NE ARG A 33 29.281 1.794 7.962 1.00 46.82 N ANISOU 257 NE ARG A 33 2527 6864 8399 854 881 763 N ATOM 258 CZ ARG A 33 29.711 2.528 6.944 1.00 49.71 C ANISOU 258 CZ ARG A 33 2762 7454 8673 599 997 842 C ATOM 259 NH1 ARG A 33 29.967 3.817 7.137 1.00 51.39 N ANISOU 259 NH1 ARG A 33 2886 7722 8916 139 955 936 N ATOM 260 NH2 ARG A 33 29.881 1.989 5.743 1.00 49.96 N ANISOU 260 NH2 ARG A 33 2780 7638 8565 788 1156 827 N ATOM 261 N ASN A 34 27.049 1.818 14.826 1.00 36.50 N ANISOU 261 N ASN A 34 1780 4564 7524 824 122 607 N ATOM 262 CA ASN A 34 27.151 2.068 16.265 1.00 37.49 C ANISOU 262 CA ASN A 34 1869 4725 7650 767 -24 587 C ATOM 263 C ASN A 34 27.151 0.763 17.073 1.00 39.01 C ANISOU 263 C ASN A 34 2155 4895 7774 1149 -59 591 C ATOM 264 O ASN A 34 26.185 -0.008 17.018 1.00 36.92 O ANISOU 264 O ASN A 34 2198 4298 7530 1296 -15 578 O ATOM 265 CB ASN A 34 25.995 2.930 16.743 1.00 34.84 C ANISOU 265 CB ASN A 34 1784 4041 7413 510 -92 537 C ATOM 266 CG ASN A 34 26.111 3.280 18.212 1.00 36.09 C ANISOU 266 CG ASN A 34 1911 4253 7548 433 -239 497 C ATOM 267 OD1 ASN A 34 25.460 2.666 19.056 1.00 34.95 O ANISOU 267 OD1 ASN A 34 1943 3950 7387 589 -276 475 O ATOM 268 ND2 ASN A 34 26.969 4.256 18.529 1.00 36.78 N ANISOU 268 ND2 ASN A 34 1777 4584 7616 166 -321 487 N ATOM 269 N GLU A 35 28.216 0.540 17.841 1.00 42.45 N ANISOU 269 N GLU A 35 2336 5685 8110 1290 -145 614 N ATOM 270 CA GLU A 35 28.377 -0.732 18.543 1.00 45.34 C ANISOU 270 CA GLU A 35 2804 6047 8376 1708 -184 646 C ATOM 271 C GLU A 35 27.456 -0.966 19.751 1.00 43.75 C ANISOU 271 C GLU A 35 2903 5545 8176 1700 -270 645 C ATOM 272 O GLU A 35 27.022 -2.093 19.974 1.00 43.47 O ANISOU 272 O GLU A 35 3147 5279 8091 1975 -242 681 O ATOM 273 CB GLU A 35 29.846 -1.029 18.861 1.00 49.66 C ANISOU 273 CB GLU A 35 2967 7118 8782 1955 -250 677 C ATOM 274 CG GLU A 35 30.692 -1.498 17.634 1.00 56.62 C ANISOU 274 CG GLU A 35 3624 8286 9603 2196 -119 683 C ATOM 275 CD GLU A 35 30.036 -2.613 16.742 1.00 61.05 C ANISOU 275 CD GLU A 35 4546 8478 10172 2504 20 676 C ATOM 276 OE1 GLU A 35 30.484 -2.801 15.586 1.00 64.24 O ANISOU 276 OE1 GLU A 35 4821 9047 10539 2620 148 656 O ATOM 277 OE2 GLU A 35 29.096 -3.313 17.175 1.00 59.74 O ANISOU 277 OE2 GLU A 35 4792 7876 10030 2613 6 683 O ATOM 278 N GLU A 36 27.147 0.092 20.499 1.00 43.06 N ANISOU 278 N GLU A 36 2783 5447 8130 1375 -364 600 N ATOM 279 CA GLU A 36 26.178 0.035 21.603 1.00 42.80 C ANISOU 279 CA GLU A 36 3017 5159 8086 1323 -425 581 C ATOM 280 C GLU A 36 24.792 -0.407 21.118 1.00 39.69 C ANISOU 280 C GLU A 36 2969 4340 7769 1305 -309 565 C ATOM 281 O GLU A 36 24.135 -1.244 21.757 1.00 39.41 O ANISOU 281 O GLU A 36 3192 4107 7676 1429 -299 596 O ATOM 282 CB GLU A 36 26.056 1.399 22.308 1.00 43.16 C ANISOU 282 CB GLU A 36 2976 5260 8164 968 -532 498 C ATOM 283 CG GLU A 36 27.262 1.771 23.212 1.00 50.34 C ANISOU 283 CG GLU A 36 3584 6586 8956 943 -689 492 C ATOM 284 CD GLU A 36 28.563 2.097 22.448 1.00 57.49 C ANISOU 284 CD GLU A 36 4102 7891 9851 890 -686 509 C ATOM 285 OE1 GLU A 36 28.499 2.663 21.329 1.00 59.33 O ANISOU 285 OE1 GLU A 36 4299 8058 10187 691 -585 500 O ATOM 286 OE2 GLU A 36 29.664 1.798 22.981 1.00 61.33 O ANISOU 286 OE2 GLU A 36 4303 8796 10204 1046 -786 534 O ATOM 287 N TYR A 37 24.357 0.153 19.990 1.00 37.13 N ANISOU 287 N TYR A 37 2649 3901 7558 1133 -224 523 N ATOM 288 CA TYR A 37 23.097 -0.270 19.354 1.00 34.91 C ANISOU 288 CA TYR A 37 2641 3287 7337 1114 -121 495 C ATOM 289 C TYR A 37 23.179 -1.739 18.905 1.00 35.49 C ANISOU 289 C TYR A 37 2883 3255 7348 1411 -37 544 C ATOM 290 O TYR A 37 22.275 -2.521 19.179 1.00 34.30 O ANISOU 290 O TYR A 37 3012 2848 7173 1442 1 543 O ATOM 291 CB TYR A 37 22.777 0.661 18.182 1.00 33.66 C ANISOU 291 CB TYR A 37 2430 3079 7281 909 -70 452 C ATOM 292 CG TYR A 37 21.965 1.863 18.575 1.00 33.77 C ANISOU 292 CG TYR A 37 2493 2978 7360 651 -129 381 C ATOM 293 CD1 TYR A 37 22.013 2.382 19.872 1.00 36.01 C ANISOU 293 CD1 TYR A 37 2752 3318 7611 568 -237 345 C ATOM 294 CD2 TYR A 37 21.156 2.508 17.632 1.00 34.18 C ANISOU 294 CD2 TYR A 37 2628 2872 7488 521 -86 341 C ATOM 295 CE1 TYR A 37 21.224 3.515 20.231 1.00 35.48 C ANISOU 295 CE1 TYR A 37 2765 3124 7592 372 -290 253 C ATOM 296 CE2 TYR A 37 20.385 3.612 17.966 1.00 35.67 C ANISOU 296 CE2 TYR A 37 2890 2940 7724 353 -148 269 C ATOM 297 CZ TYR A 37 20.415 4.119 19.256 1.00 36.43 C ANISOU 297 CZ TYR A 37 2979 3068 7793 285 -244 217 C ATOM 298 OH TYR A 37 19.631 5.229 19.541 1.00 37.75 O ANISOU 298 OH TYR A 37 3250 3099 7995 162 -302 123 O ATOM 299 N ASN A 38 24.281 -2.135 18.267 1.00 36.33 N ANISOU 299 N ASN A 38 2829 3567 7409 1628 -9 580 N ATOM 300 CA ASN A 38 24.434 -3.555 17.912 1.00 38.69 C ANISOU 300 CA ASN A 38 3334 3739 7628 1968 59 610 C ATOM 301 C ASN A 38 24.353 -4.468 19.133 1.00 39.93 C ANISOU 301 C ASN A 38 3719 3772 7681 2160 -3 677 C ATOM 302 O ASN A 38 23.686 -5.496 19.092 1.00 38.89 O ANISOU 302 O ASN A 38 3946 3319 7512 2255 54 691 O ATOM 303 CB ASN A 38 25.722 -3.813 17.088 1.00 41.29 C ANISOU 303 CB ASN A 38 3420 4373 7896 2234 101 623 C ATOM 304 CG ASN A 38 25.604 -3.275 15.668 1.00 41.04 C ANISOU 304 CG ASN A 38 3291 4372 7928 2076 208 571 C ATOM 305 OD1 ASN A 38 24.491 -3.129 15.141 1.00 40.31 O ANISOU 305 OD1 ASN A 38 3407 4000 7910 1880 258 524 O ATOM 306 ND2 ASN A 38 26.728 -2.954 15.052 1.00 41.00 N ANISOU 306 ND2 ASN A 38 2958 4743 7878 2150 242 582 N ATOM 307 N LYS A 39 24.992 -4.052 20.222 1.00 42.61 N ANISOU 307 N LYS A 39 3870 4360 7960 2180 -125 720 N ATOM 308 CA LYS A 39 25.003 -4.809 21.473 1.00 46.65 C ANISOU 308 CA LYS A 39 4582 4803 8340 2366 -203 805 C ATOM 309 C LYS A 39 23.582 -4.985 22.007 1.00 45.46 C ANISOU 309 C LYS A 39 4770 4300 8205 2131 -161 800 C ATOM 310 O LYS A 39 23.159 -6.098 22.288 1.00 46.58 O ANISOU 310 O LYS A 39 5271 4169 8260 2265 -122 868 O ATOM 311 CB LYS A 39 25.913 -4.147 22.532 1.00 48.16 C ANISOU 311 CB LYS A 39 4465 5383 8450 2378 -359 829 C ATOM 312 CG LYS A 39 27.198 -4.874 22.832 1.00 54.48 C ANISOU 312 CG LYS A 39 5132 6472 9096 2817 -441 909 C ATOM 313 CD LYS A 39 27.053 -5.916 23.968 1.00 59.14 C ANISOU 313 CD LYS A 39 6063 6892 9514 3091 -511 1029 C ATOM 314 CE LYS A 39 27.699 -7.282 23.641 1.00 61.73 C ANISOU 314 CE LYS A 39 6590 7147 9718 3631 -494 1115 C ATOM 315 NZ LYS A 39 29.102 -7.497 24.126 1.00 67.33 N ANISOU 315 NZ LYS A 39 7005 8319 10260 4058 -639 1172 N ATOM 316 N SER A 40 22.826 -3.900 22.115 1.00 45.12 N ANISOU 316 N SER A 40 4625 4260 8258 1780 -163 717 N ATOM 317 CA SER A 40 21.487 -4.017 22.675 1.00 45.25 C ANISOU 317 CA SER A 40 4893 4035 8266 1567 -118 697 C ATOM 318 C SER A 40 20.576 -4.849 21.767 1.00 44.98 C ANISOU 318 C SER A 40 5133 3688 8269 1523 13 677 C ATOM 319 O SER A 40 19.736 -5.623 22.243 1.00 45.89 O ANISOU 319 O SER A 40 5546 3579 8311 1451 65 713 O ATOM 320 CB SER A 40 20.893 -2.646 22.935 1.00 44.24 C ANISOU 320 CB SER A 40 4589 3999 8220 1266 -152 591 C ATOM 321 OG SER A 40 20.503 -2.055 21.714 1.00 47.23 O ANISOU 321 OG SER A 40 4885 4323 8738 1130 -91 508 O ATOM 322 N VAL A 41 20.791 -4.734 20.464 1.00 43.78 N ANISOU 322 N VAL A 41 4888 3537 8209 1553 65 622 N ATOM 323 CA VAL A 41 19.890 -5.308 19.489 1.00 43.17 C ANISOU 323 CA VAL A 41 5024 3207 8171 1461 173 564 C ATOM 324 C VAL A 41 20.156 -6.823 19.316 1.00 45.99 C ANISOU 324 C VAL A 41 5725 3323 8425 1712 223 626 C ATOM 325 O VAL A 41 19.231 -7.598 19.038 1.00 45.59 O ANISOU 325 O VAL A 41 5982 2988 8351 1586 300 597 O ATOM 326 CB VAL A 41 19.976 -4.490 18.185 1.00 41.99 C ANISOU 326 CB VAL A 41 4653 3167 8133 1384 202 480 C ATOM 327 CG1 VAL A 41 19.723 -5.325 16.974 1.00 44.27 C ANISOU 327 CG1 VAL A 41 5128 3275 8416 1452 295 434 C ATOM 328 CG2 VAL A 41 19.014 -3.228 18.258 1.00 38.88 C ANISOU 328 CG2 VAL A 41 4119 2824 7830 1079 178 400 C ATOM 329 N GLN A 42 21.412 -7.220 19.510 1.00 48.12 N ANISOU 329 N GLN A 42 5946 3717 8621 2065 172 702 N ATOM 330 CA GLN A 42 21.839 -8.617 19.473 1.00 52.20 C ANISOU 330 CA GLN A 42 6812 4005 9017 2403 195 769 C ATOM 331 C GLN A 42 20.905 -9.532 20.234 1.00 53.21 C ANISOU 331 C GLN A 42 7396 3767 9053 2276 225 836 C ATOM 332 O GLN A 42 20.570 -10.608 19.760 1.00 55.66 O ANISOU 332 O GLN A 42 8105 3732 9312 2331 294 829 O ATOM 333 CB GLN A 42 23.199 -8.763 20.135 1.00 54.54 C ANISOU 333 CB GLN A 42 6958 4557 9209 2799 92 867 C ATOM 334 CG GLN A 42 24.392 -8.525 19.267 1.00 57.79 C ANISOU 334 CG GLN A 42 7039 5286 9633 3077 90 825 C ATOM 335 CD GLN A 42 25.674 -8.743 20.050 1.00 63.18 C ANISOU 335 CD GLN A 42 7550 6273 10182 3478 -26 919 C ATOM 336 OE1 GLN A 42 25.697 -8.594 21.277 1.00 64.28 O ANISOU 336 OE1 GLN A 42 7689 6484 10252 3449 -131 1004 O ATOM 337 NE2 GLN A 42 26.742 -9.113 19.352 1.00 67.86 N ANISOU 337 NE2 GLN A 42 7986 7082 10715 3874 -12 898 N ATOM 338 N GLU A 43 20.512 -9.093 21.423 1.00 52.19 N ANISOU 338 N GLU A 43 7219 3723 8887 2091 175 897 N ATOM 339 CA GLU A 43 19.796 -9.914 22.385 1.00 54.21 C ANISOU 339 CA GLU A 43 7879 3708 9011 1976 200 1001 C ATOM 340 C GLU A 43 18.327 -10.175 22.037 1.00 52.01 C ANISOU 340 C GLU A 43 7816 3181 8765 1553 319 926 C ATOM 341 O GLU A 43 17.705 -11.092 22.600 1.00 53.94 O ANISOU 341 O GLU A 43 8469 3142 8884 1419 372 1012 O ATOM 342 CB GLU A 43 19.884 -9.241 23.756 1.00 55.19 C ANISOU 342 CB GLU A 43 7827 4081 9063 1912 112 1073 C ATOM 343 CG GLU A 43 21.317 -8.977 24.220 1.00 60.13 C ANISOU 343 CG GLU A 43 8209 5009 9627 2291 -27 1140 C ATOM 344 CD GLU A 43 21.393 -8.538 25.670 1.00 63.91 C ANISOU 344 CD GLU A 43 8607 5693 9982 2243 -125 1218 C ATOM 345 OE1 GLU A 43 22.303 -9.021 26.378 1.00 67.54 O ANISOU 345 OE1 GLU A 43 9134 6244 10285 2583 -230 1345 O ATOM 346 OE2 GLU A 43 20.539 -7.721 26.095 1.00 63.82 O ANISOU 346 OE2 GLU A 43 8471 5765 10012 1893 -100 1143 O ATOM 347 N ILE A 44 17.797 -9.376 21.110 1.00 47.08 N ANISOU 347 N ILE A 44 6918 2683 8288 1339 355 773 N ATOM 348 CA ILE A 44 16.389 -9.421 20.700 1.00 44.06 C ANISOU 348 CA ILE A 44 6617 2185 7939 936 447 671 C ATOM 349 C ILE A 44 16.096 -10.618 19.795 1.00 45.85 C ANISOU 349 C ILE A 44 7236 2056 8130 913 524 634 C ATOM 350 O ILE A 44 16.654 -10.769 18.697 1.00 45.93 O ANISOU 350 O ILE A 44 7234 2026 8192 1118 526 563 O ATOM 351 CB ILE A 44 15.926 -8.067 20.061 1.00 41.46 C ANISOU 351 CB ILE A 44 5857 2138 7759 763 434 526 C ATOM 352 CG1 ILE A 44 16.282 -6.908 20.980 1.00 37.55 C ANISOU 352 CG1 ILE A 44 5046 1935 7287 793 350 549 C ATOM 353 CG2 ILE A 44 14.405 -8.041 19.794 1.00 38.41 C ANISOU 353 CG2 ILE A 44 5489 1725 7379 371 510 417 C ATOM 354 CD1 ILE A 44 15.969 -5.512 20.369 1.00 36.90 C ANISOU 354 CD1 ILE A 44 4601 2077 7341 677 320 421 C ATOM 355 N GLN A 45 15.235 -11.492 20.311 1.00 46.38 N ANISOU 355 N GLN A 45 7674 1865 8084 648 592 681 N ATOM 356 CA GLN A 45 14.763 -12.663 19.601 1.00 46.75 C ANISOU 356 CA GLN A 45 8161 1528 8073 516 667 635 C ATOM 357 C GLN A 45 13.534 -12.321 18.762 1.00 44.25 C ANISOU 357 C GLN A 45 7677 1310 7827 98 723 454 C ATOM 358 O GLN A 45 13.384 -12.799 17.635 1.00 44.05 O ANISOU 358 O GLN A 45 7801 1120 7818 66 749 334 O ATOM 359 CB GLN A 45 14.467 -13.780 20.611 1.00 50.50 C ANISOU 359 CB GLN A 45 9155 1662 8369 389 711 794 C ATOM 360 CG GLN A 45 15.762 -14.284 21.307 1.00 53.06 C ANISOU 360 CG GLN A 45 9712 1854 8594 894 633 978 C ATOM 361 CD GLN A 45 15.526 -15.350 22.365 1.00 59.50 C ANISOU 361 CD GLN A 45 11087 2315 9206 804 666 1173 C ATOM 362 OE1 GLN A 45 14.811 -15.123 23.345 1.00 60.59 O ANISOU 362 OE1 GLN A 45 11186 2571 9265 476 704 1253 O ATOM 363 NE2 GLN A 45 16.166 -16.514 22.190 1.00 61.05 N ANISOU 363 NE2 GLN A 45 11826 2075 9296 1126 650 1257 N ATOM 364 N ALA A 46 12.660 -11.480 19.316 1.00 41.06 N ANISOU 364 N ALA A 46 6953 1203 7445 -195 735 424 N ATOM 365 CA ALA A 46 11.467 -11.053 18.608 1.00 39.56 C ANISOU 365 CA ALA A 46 6536 1192 7303 -549 771 252 C ATOM 366 C ALA A 46 10.903 -9.795 19.263 1.00 37.58 C ANISOU 366 C ALA A 46 5835 1348 7094 -657 750 221 C ATOM 367 O ALA A 46 11.197 -9.500 20.441 1.00 37.17 O ANISOU 367 O ALA A 46 5740 1386 6995 -580 735 333 O ATOM 368 CB ALA A 46 10.407 -12.180 18.578 1.00 42.53 C ANISOU 368 CB ALA A 46 7276 1328 7554 -988 865 219 C ATOM 369 N THR A 47 10.130 -9.028 18.497 1.00 35.56 N ANISOU 369 N THR A 47 5257 1342 6913 -794 737 63 N ATOM 370 CA THR A 47 9.424 -7.888 19.060 1.00 34.33 C ANISOU 370 CA THR A 47 4715 1552 6777 -886 721 4 C ATOM 371 C THR A 47 8.266 -7.507 18.182 1.00 34.31 C ANISOU 371 C THR A 47 4472 1772 6793 -1103 725 -173 C ATOM 372 O THR A 47 8.438 -7.264 16.979 1.00 33.52 O ANISOU 372 O THR A 47 4300 1666 6770 -992 674 -254 O ATOM 373 CB THR A 47 10.342 -6.621 19.216 1.00 32.30 C ANISOU 373 CB THR A 47 4184 1455 6633 -545 621 28 C ATOM 374 OG1 THR A 47 11.403 -6.880 20.150 1.00 31.32 O ANISOU 374 OG1 THR A 47 4213 1214 6471 -343 598 182 O ATOM 375 CG2 THR A 47 9.537 -5.446 19.718 1.00 30.61 C ANISOU 375 CG2 THR A 47 3631 1571 6429 -618 601 -62 C ATOM 376 N PHE A 48 7.089 -7.411 18.787 1.00 35.45 N ANISOU 376 N PHE A 48 4463 2159 6845 -1397 784 -235 N ATOM 377 CA PHE A 48 6.001 -6.671 18.165 1.00 35.00 C ANISOU 377 CA PHE A 48 4045 2453 6801 -1505 758 -410 C ATOM 378 C PHE A 48 5.542 -5.520 19.061 1.00 34.58 C ANISOU 378 C PHE A 48 3656 2748 6735 -1418 743 -449 C ATOM 379 O PHE A 48 5.826 -5.523 20.267 1.00 34.72 O ANISOU 379 O PHE A 48 3742 2754 6696 -1401 784 -352 O ATOM 380 CB PHE A 48 4.861 -7.605 17.757 1.00 38.53 C ANISOU 380 CB PHE A 48 4551 2957 7130 -1942 832 -511 C ATOM 381 CG PHE A 48 4.150 -8.265 18.910 1.00 41.81 C ANISOU 381 CG PHE A 48 5054 3446 7388 -2311 958 -460 C ATOM 382 CD1 PHE A 48 4.534 -9.530 19.345 1.00 45.58 C ANISOU 382 CD1 PHE A 48 6007 3532 7779 -2500 1037 -321 C ATOM 383 CD2 PHE A 48 3.079 -7.636 19.539 1.00 44.42 C ANISOU 383 CD2 PHE A 48 5007 4240 7632 -2462 1002 -550 C ATOM 384 CE1 PHE A 48 3.851 -10.179 20.399 1.00 48.75 C ANISOU 384 CE1 PHE A 48 6532 3987 8006 -2892 1167 -249 C ATOM 385 CE2 PHE A 48 2.382 -8.270 20.589 1.00 47.47 C ANISOU 385 CE2 PHE A 48 5454 4742 7840 -2847 1142 -500 C ATOM 386 CZ PHE A 48 2.777 -9.546 21.020 1.00 49.79 C ANISOU 386 CZ PHE A 48 6249 4623 8045 -3087 1227 -337 C ATOM 387 N PHE A 49 4.873 -4.523 18.477 1.00 33.18 N ANISOU 387 N PHE A 49 3141 2869 6596 -1326 677 -593 N ATOM 388 CA PHE A 49 4.467 -3.357 19.232 1.00 33.63 C ANISOU 388 CA PHE A 49 2912 3225 6640 -1171 651 -655 C ATOM 389 C PHE A 49 3.316 -2.584 18.569 1.00 34.11 C ANISOU 389 C PHE A 49 2619 3664 6678 -1138 599 -838 C ATOM 390 O PHE A 49 3.010 -2.781 17.389 1.00 34.68 O ANISOU 390 O PHE A 49 2653 3756 6768 -1185 553 -905 O ATOM 391 CB PHE A 49 5.680 -2.436 19.489 1.00 31.21 C ANISOU 391 CB PHE A 49 2655 2748 6454 -815 558 -573 C ATOM 392 CG PHE A 49 6.264 -1.852 18.240 1.00 30.88 C ANISOU 392 CG PHE A 49 2601 2587 6544 -595 452 -581 C ATOM 393 CD1 PHE A 49 7.367 -2.443 17.636 1.00 28.43 C ANISOU 393 CD1 PHE A 49 2520 1977 6303 -536 442 -471 C ATOM 394 CD2 PHE A 49 5.696 -0.717 17.653 1.00 28.70 C ANISOU 394 CD2 PHE A 49 2094 2510 6300 -430 365 -695 C ATOM 395 CE1 PHE A 49 7.907 -1.896 16.480 1.00 27.22 C ANISOU 395 CE1 PHE A 49 2344 1753 6244 -355 364 -472 C ATOM 396 CE2 PHE A 49 6.222 -0.190 16.504 1.00 28.08 C ANISOU 396 CE2 PHE A 49 2038 2316 6315 -253 276 -677 C ATOM 397 CZ PHE A 49 7.323 -0.785 15.911 1.00 25.98 C ANISOU 397 CZ PHE A 49 1980 1780 6112 -237 284 -565 C ATOM 398 N TYR A 50 2.676 -1.718 19.344 1.00 34.80 N ANISOU 398 N TYR A 50 2451 4068 6704 -1031 602 -927 N ATOM 399 CA TYR A 50 1.548 -0.932 18.863 1.00 35.50 C ANISOU 399 CA TYR A 50 2184 4562 6744 -925 546 -1106 C ATOM 400 C TYR A 50 1.913 0.538 18.895 1.00 34.59 C ANISOU 400 C TYR A 50 2002 4426 6715 -487 424 -1138 C ATOM 401 O TYR A 50 2.474 1.007 19.880 1.00 33.81 O ANISOU 401 O TYR A 50 1991 4226 6631 -359 432 -1094 O ATOM 402 CB TYR A 50 0.328 -1.171 19.752 1.00 39.01 C ANISOU 402 CB TYR A 50 2364 5457 7002 -1157 666 -1214 C ATOM 403 CG TYR A 50 -0.264 -2.541 19.607 1.00 40.61 C ANISOU 403 CG TYR A 50 2606 5731 7093 -1657 783 -1208 C ATOM 404 CD1 TYR A 50 0.320 -3.639 20.245 1.00 42.31 C ANISOU 404 CD1 TYR A 50 3172 5625 7278 -1943 894 -1046 C ATOM 405 CD2 TYR A 50 -1.391 -2.748 18.825 1.00 43.28 C ANISOU 405 CD2 TYR A 50 2658 6446 7342 -1850 772 -1362 C ATOM 406 CE1 TYR A 50 -0.214 -4.915 20.115 1.00 43.93 C ANISOU 406 CE1 TYR A 50 3493 5826 7370 -2436 1001 -1034 C ATOM 407 CE2 TYR A 50 -1.960 -4.033 18.696 1.00 46.52 C ANISOU 407 CE2 TYR A 50 3127 6913 7634 -2387 880 -1370 C ATOM 408 CZ TYR A 50 -1.353 -5.105 19.343 1.00 47.20 C ANISOU 408 CZ TYR A 50 3621 6613 7700 -2685 998 -1202 C ATOM 409 OH TYR A 50 -1.862 -6.374 19.222 1.00 50.41 O ANISOU 409 OH TYR A 50 4173 6993 7988 -3233 1102 -1199 O ATOM 410 N PHE A 51 1.633 1.254 17.810 1.00 34.69 N ANISOU 410 N PHE A 51 1900 4510 6771 -266 304 -1211 N ATOM 411 CA PHE A 51 1.748 2.712 17.813 1.00 34.92 C ANISOU 411 CA PHE A 51 1887 4532 6850 143 184 -1259 C ATOM 412 C PHE A 51 0.331 3.281 17.943 1.00 37.40 C ANISOU 412 C PHE A 51 1846 5341 7024 289 166 -1455 C ATOM 413 O PHE A 51 -0.525 2.917 17.151 1.00 38.34 O ANISOU 413 O PHE A 51 1756 5743 7068 196 149 -1537 O ATOM 414 CB PHE A 51 2.363 3.206 16.493 1.00 33.57 C ANISOU 414 CB PHE A 51 1854 4111 6791 330 56 -1190 C ATOM 415 CG PHE A 51 3.886 3.239 16.463 1.00 31.65 C ANISOU 415 CG PHE A 51 1915 3424 6687 345 43 -1018 C ATOM 416 CD1 PHE A 51 4.554 3.327 15.235 1.00 29.94 C ANISOU 416 CD1 PHE A 51 1834 2995 6548 405 -23 -928 C ATOM 417 CD2 PHE A 51 4.647 3.209 17.633 1.00 28.86 C ANISOU 417 CD2 PHE A 51 1686 2916 6363 306 94 -951 C ATOM 418 CE1 PHE A 51 5.977 3.398 15.172 1.00 27.92 C ANISOU 418 CE1 PHE A 51 1803 2402 6402 419 -28 -777 C ATOM 419 CE2 PHE A 51 6.020 3.264 17.583 1.00 25.90 C ANISOU 419 CE2 PHE A 51 1528 2215 6097 326 70 -808 C ATOM 420 CZ PHE A 51 6.700 3.382 16.351 1.00 25.94 C ANISOU 420 CZ PHE A 51 1637 2033 6185 382 14 -723 C ATOM 421 N THR A 52 0.077 4.143 18.933 1.00 38.82 N ANISOU 421 N THR A 52 1945 5655 7149 522 168 -1544 N ATOM 422 CA THR A 52 -1.191 4.936 18.986 1.00 41.80 C ANISOU 422 CA THR A 52 1988 6504 7390 807 124 -1748 C ATOM 423 C THR A 52 -0.806 6.410 19.127 1.00 42.12 C ANISOU 423 C THR A 52 2192 6323 7489 1284 -8 -1784 C ATOM 424 O THR A 52 -0.525 6.888 20.240 1.00 40.79 O ANISOU 424 O THR A 52 2114 6084 7300 1386 27 -1822 O ATOM 425 CB THR A 52 -2.122 4.533 20.151 1.00 44.42 C ANISOU 425 CB THR A 52 2030 7310 7536 643 280 -1874 C ATOM 426 OG1 THR A 52 -2.246 3.111 20.197 1.00 45.91 O ANISOU 426 OG1 THR A 52 2191 7573 7678 121 419 -1798 O ATOM 427 CG2 THR A 52 -3.564 5.146 19.992 1.00 48.33 C ANISOU 427 CG2 THR A 52 2083 8418 7861 919 244 -2104 C ATOM 428 N PRO A 53 -0.730 7.122 17.990 1.00 42.61 N ANISOU 428 N PRO A 53 2342 6235 7614 1556 -164 -1762 N ATOM 429 CA PRO A 53 -0.342 8.538 18.014 1.00 43.33 C ANISOU 429 CA PRO A 53 2669 6040 7756 1982 -300 -1778 C ATOM 430 C PRO A 53 -1.370 9.430 18.711 1.00 46.71 C ANISOU 430 C PRO A 53 2905 6808 8033 2381 -326 -1999 C ATOM 431 O PRO A 53 -2.551 9.121 18.697 1.00 49.20 O ANISOU 431 O PRO A 53 2833 7663 8198 2419 -286 -2142 O ATOM 432 CB PRO A 53 -0.259 8.884 16.522 1.00 43.71 C ANISOU 432 CB PRO A 53 2816 5938 7852 2135 -443 -1693 C ATOM 433 CG PRO A 53 0.178 7.550 15.876 1.00 40.29 C ANISOU 433 CG PRO A 53 2371 5458 7479 1691 -362 -1562 C ATOM 434 CD PRO A 53 -0.746 6.587 16.613 1.00 42.18 C ANISOU 434 CD PRO A 53 2273 6159 7594 1430 -220 -1685 C ATOM 435 N ASN A 54 -0.887 10.487 19.361 1.00 47.07 N ANISOU 435 N ASN A 54 3221 6555 8108 2653 -386 -2036 N ATOM 436 CA ASN A 54 -1.708 11.571 19.844 1.00 50.74 C ANISOU 436 CA ASN A 54 3621 7216 8440 3147 -451 -2249 C ATOM 437 C ASN A 54 -1.286 12.800 19.058 1.00 51.00 C ANISOU 437 C ASN A 54 4037 6792 8550 3522 -646 -2195 C ATOM 438 O ASN A 54 -0.318 13.505 19.413 1.00 49.51 O ANISOU 438 O ASN A 54 4255 6100 8457 3543 -699 -2138 O ATOM 439 CB ASN A 54 -1.542 11.784 21.350 1.00 51.39 C ANISOU 439 CB ASN A 54 3754 7313 8457 3147 -355 -2365 C ATOM 440 CG ASN A 54 -2.631 12.691 21.936 1.00 58.51 C ANISOU 440 CG ASN A 54 4490 8571 9168 3664 -380 -2636 C ATOM 441 OD1 ASN A 54 -3.378 13.348 21.206 1.00 63.46 O ANISOU 441 OD1 ASN A 54 5038 9343 9731 4092 -502 -2725 O ATOM 442 ND2 ASN A 54 -2.719 12.729 23.262 1.00 62.09 N ANISOU 442 ND2 ASN A 54 4896 9185 9509 3656 -267 -2772 N ATOM 443 N LYS A 55 -2.010 13.035 17.970 1.00 52.56 N ANISOU 443 N LYS A 55 4111 7171 8688 3789 -757 -2206 N ATOM 444 CA LYS A 55 -1.660 14.072 17.022 1.00 53.87 C ANISOU 444 CA LYS A 55 4655 6910 8903 4111 -942 -2107 C ATOM 445 C LYS A 55 -1.681 15.451 17.664 1.00 56.95 C ANISOU 445 C LYS A 55 5373 7018 9246 4582 -1042 -2236 C ATOM 446 O LYS A 55 -0.912 16.333 17.283 1.00 58.27 O ANISOU 446 O LYS A 55 6027 6616 9497 4685 -1159 -2121 O ATOM 447 CB LYS A 55 -2.595 14.029 15.827 1.00 55.60 C ANISOU 447 CB LYS A 55 4637 7473 9015 4357 -1049 -2117 C ATOM 448 CG LYS A 55 -2.450 12.768 15.004 1.00 56.40 C ANISOU 448 CG LYS A 55 4523 7742 9165 3889 -981 -1984 C ATOM 449 CD LYS A 55 -3.008 12.992 13.611 1.00 60.48 C ANISOU 449 CD LYS A 55 4982 8404 9594 4145 -1140 -1940 C ATOM 450 CE LYS A 55 -3.527 11.701 12.996 1.00 60.01 C ANISOU 450 CE LYS A 55 4511 8811 9480 3780 -1076 -1952 C ATOM 451 NZ LYS A 55 -5.002 11.598 13.245 1.00 58.03 N ANISOU 451 NZ LYS A 55 3733 9289 9027 4006 -1086 -2191 N ATOM 452 N THR A 56 -2.528 15.637 18.661 1.00 58.77 N ANISOU 452 N THR A 56 5365 7633 9331 4844 -987 -2480 N ATOM 453 CA THR A 56 -2.614 16.945 19.277 1.00 61.73 C ANISOU 453 CA THR A 56 6074 7741 9638 5339 -1084 -2639 C ATOM 454 C THR A 56 -1.434 17.238 20.208 1.00 60.17 C ANISOU 454 C THR A 56 6279 7030 9553 5068 -1045 -2608 C ATOM 455 O THR A 56 -1.107 18.395 20.442 1.00 62.46 O ANISOU 455 O THR A 56 7031 6861 9841 5360 -1161 -2670 O ATOM 456 CB THR A 56 -3.986 17.181 19.956 1.00 65.83 C ANISOU 456 CB THR A 56 6202 8883 9927 5818 -1052 -2942 C ATOM 457 OG1 THR A 56 -4.075 16.425 21.165 1.00 64.05 O ANISOU 457 OG1 THR A 56 5672 9017 9647 5499 -849 -3052 O ATOM 458 CG2 THR A 56 -5.107 16.765 19.024 1.00 66.81 C ANISOU 458 CG2 THR A 56 5852 9601 9932 6006 -1092 -2969 C ATOM 459 N GLU A 57 -0.789 16.186 20.706 1.00 56.21 N ANISOU 459 N GLU A 57 5623 6598 9137 4509 -893 -2511 N ATOM 460 CA GLU A 57 0.346 16.313 21.638 1.00 54.93 C ANISOU 460 CA GLU A 57 5764 6047 9060 4215 -856 -2481 C ATOM 461 C GLU A 57 1.706 15.988 21.006 1.00 49.97 C ANISOU 461 C GLU A 57 5386 4967 8631 3760 -876 -2205 C ATOM 462 O GLU A 57 2.730 16.134 21.652 1.00 48.07 O ANISOU 462 O GLU A 57 5389 4414 8463 3508 -870 -2166 O ATOM 463 CB GLU A 57 0.134 15.408 22.866 1.00 54.70 C ANISOU 463 CB GLU A 57 5397 6445 8941 3960 -671 -2582 C ATOM 464 CG GLU A 57 -1.221 15.657 23.568 1.00 61.45 C ANISOU 464 CG GLU A 57 5936 7846 9567 4375 -613 -2867 C ATOM 465 CD GLU A 57 -1.206 16.857 24.482 1.00 67.02 C ANISOU 465 CD GLU A 57 6960 8331 10175 4768 -682 -3092 C ATOM 466 OE1 GLU A 57 -0.257 16.987 25.283 1.00 69.25 O ANISOU 466 OE1 GLU A 57 7520 8287 10503 4525 -671 -3079 O ATOM 467 OE2 GLU A 57 -2.145 17.671 24.418 1.00 74.31 O ANISOU 467 OE2 GLU A 57 7859 9417 10957 5336 -753 -3295 O ATOM 468 N ASP A 58 1.703 15.604 19.734 1.00 48.33 N ANISOU 468 N ASP A 58 5113 4758 8491 3680 -908 -2030 N ATOM 469 CA ASP A 58 2.906 15.145 19.029 1.00 45.78 C ANISOU 469 CA ASP A 58 4946 4116 8331 3260 -901 -1772 C ATOM 470 C ASP A 58 3.626 14.085 19.852 1.00 42.03 C ANISOU 470 C ASP A 58 4320 3737 7913 2809 -757 -1718 C ATOM 471 O ASP A 58 4.823 14.213 20.124 1.00 40.86 O ANISOU 471 O ASP A 58 4406 3256 7862 2555 -768 -1614 O ATOM 472 CB ASP A 58 3.880 16.297 18.766 1.00 47.08 C ANISOU 472 CB ASP A 58 5628 3682 8577 3282 -1029 -1680 C ATOM 473 CG ASP A 58 3.434 17.217 17.641 1.00 51.41 C ANISOU 473 CG ASP A 58 6420 4028 9086 3650 -1177 -1630 C ATOM 474 OD1 ASP A 58 2.402 16.942 16.979 1.00 53.62 O ANISOU 474 OD1 ASP A 58 6436 4660 9278 3906 -1195 -1663 O ATOM 475 OD2 ASP A 58 4.134 18.233 17.433 1.00 51.51 O ANISOU 475 OD2 ASP A 58 6905 3526 9140 3668 -1282 -1554 O ATOM 476 N THR A 59 2.891 13.085 20.312 1.00 41.22 N ANISOU 476 N THR A 59 3836 4098 7727 2715 -629 -1793 N ATOM 477 CA THR A 59 3.506 11.933 21.001 1.00 39.36 C ANISOU 477 CA THR A 59 3479 3953 7524 2297 -491 -1709 C ATOM 478 C THR A 59 2.928 10.693 20.361 1.00 38.35 C ANISOU 478 C THR A 59 3039 4154 7377 2102 -394 -1644 C ATOM 479 O THR A 59 1.883 10.778 19.705 1.00 39.85 O ANISOU 479 O THR A 59 3034 4614 7493 2304 -424 -1725 O ATOM 480 CB THR A 59 3.153 11.888 22.500 1.00 40.78 C ANISOU 480 CB THR A 59 3553 4368 7572 2318 -405 -1878 C ATOM 481 OG1 THR A 59 1.725 11.853 22.650 1.00 45.08 O ANISOU 481 OG1 THR A 59 3785 5387 7958 2558 -353 -2059 O ATOM 482 CG2 THR A 59 3.697 13.137 23.240 1.00 43.15 C ANISOU 482 CG2 THR A 59 4187 4341 7866 2506 -509 -1986 C ATOM 483 N ILE A 60 3.595 9.547 20.546 1.00 36.58 N ANISOU 483 N ILE A 60 2782 3910 7206 1722 -290 -1508 N ATOM 484 CA ILE A 60 3.021 8.264 20.157 1.00 36.30 C ANISOU 484 CA ILE A 60 2496 4167 7130 1483 -181 -1471 C ATOM 485 C ILE A 60 3.071 7.331 21.358 1.00 36.80 C ANISOU 485 C ILE A 60 2477 4389 7117 1215 -35 -1467 C ATOM 486 O ILE A 60 4.155 7.080 21.943 1.00 34.69 O ANISOU 486 O ILE A 60 2397 3878 6907 1060 -17 -1354 O ATOM 487 CB ILE A 60 3.809 7.593 18.992 1.00 34.58 C ANISOU 487 CB ILE A 60 2388 3716 7037 1277 -193 -1281 C ATOM 488 CG1 ILE A 60 3.949 8.550 17.802 1.00 33.23 C ANISOU 488 CG1 ILE A 60 2357 3343 6927 1514 -335 -1242 C ATOM 489 CG2 ILE A 60 3.137 6.289 18.579 1.00 33.73 C ANISOU 489 CG2 ILE A 60 2067 3881 6870 1026 -92 -1275 C ATOM 490 CD1 ILE A 60 5.034 8.160 16.783 1.00 29.27 C ANISOU 490 CD1 ILE A 60 2023 2557 6541 1339 -347 -1048 C ATOM 491 N PHE A 61 1.911 6.796 21.718 1.00 38.05 N ANISOU 491 N PHE A 61 2350 4980 7127 1148 69 -1579 N ATOM 492 CA PHE A 61 1.878 5.802 22.771 1.00 38.26 C ANISOU 492 CA PHE A 61 2320 5165 7053 845 224 -1546 C ATOM 493 C PHE A 61 2.401 4.475 22.220 1.00 36.59 C ANISOU 493 C PHE A 61 2202 4790 6911 485 287 -1362 C ATOM 494 O PHE A 61 1.883 3.974 21.225 1.00 36.50 O ANISOU 494 O PHE A 61 2078 4881 6910 382 289 -1362 O ATOM 495 CB PHE A 61 0.473 5.681 23.391 1.00 41.47 C ANISOU 495 CB PHE A 61 2385 6121 7251 848 336 -1724 C ATOM 496 CG PHE A 61 0.442 4.819 24.609 1.00 43.55 C ANISOU 496 CG PHE A 61 2629 6542 7375 546 503 -1682 C ATOM 497 CD1 PHE A 61 -0.465 3.769 24.712 1.00 46.83 C ANISOU 497 CD1 PHE A 61 2814 7330 7649 209 657 -1688 C ATOM 498 CD2 PHE A 61 1.363 5.021 25.633 1.00 43.05 C ANISOU 498 CD2 PHE A 61 2802 6247 7309 563 501 -1621 C ATOM 499 CE1 PHE A 61 -0.484 2.953 25.840 1.00 48.82 C ANISOU 499 CE1 PHE A 61 3099 7702 7749 -97 820 -1618 C ATOM 500 CE2 PHE A 61 1.369 4.209 26.759 1.00 46.54 C ANISOU 500 CE2 PHE A 61 3260 6826 7597 297 648 -1557 C ATOM 501 CZ PHE A 61 0.434 3.171 26.866 1.00 49.17 C ANISOU 501 CZ PHE A 61 3392 7509 7781 -33 814 -1545 C ATOM 502 N LEU A 62 3.436 3.923 22.861 1.00 34.14 N ANISOU 502 N LEU A 62 2110 4228 6634 320 326 -1216 N ATOM 503 CA LEU A 62 4.065 2.686 22.400 1.00 33.79 C ANISOU 503 CA LEU A 62 2218 3971 6648 48 376 -1041 C ATOM 504 C LEU A 62 3.803 1.561 23.382 1.00 35.07 C ANISOU 504 C LEU A 62 2404 4257 6664 -250 528 -981 C ATOM 505 O LEU A 62 4.119 1.695 24.563 1.00 36.38 O ANISOU 505 O LEU A 62 2636 4440 6747 -232 559 -961 O ATOM 506 CB LEU A 62 5.596 2.880 22.248 1.00 30.13 C ANISOU 506 CB LEU A 62 2008 3110 6330 130 288 -895 C ATOM 507 CG LEU A 62 6.490 1.652 22.033 1.00 30.03 C ANISOU 507 CG LEU A 62 2191 2861 6360 -60 335 -714 C ATOM 508 CD1 LEU A 62 6.255 1.036 20.670 1.00 27.51 C ANISOU 508 CD1 LEU A 62 1872 2482 6099 -149 341 -695 C ATOM 509 CD2 LEU A 62 7.990 2.002 22.238 1.00 26.03 C ANISOU 509 CD2 LEU A 62 1852 2089 5949 59 249 -599 C ATOM 510 N ARG A 63 3.239 0.459 22.898 1.00 36.14 N ANISOU 510 N ARG A 63 2516 4465 6752 -540 618 -949 N ATOM 511 CA ARG A 63 3.083 -0.739 23.701 1.00 37.84 C ANISOU 511 CA ARG A 63 2845 4705 6827 -878 765 -850 C ATOM 512 C ARG A 63 3.928 -1.807 23.040 1.00 36.78 C ANISOU 512 C ARG A 63 3015 4178 6782 -1019 760 -685 C ATOM 513 O ARG A 63 3.639 -2.213 21.919 1.00 36.69 O ANISOU 513 O ARG A 63 2991 4124 6826 -1118 745 -716 O ATOM 514 CB ARG A 63 1.617 -1.198 23.740 1.00 41.62 C ANISOU 514 CB ARG A 63 3062 5611 7139 -1164 889 -967 C ATOM 515 CG ARG A 63 0.652 -0.144 24.253 1.00 45.28 C ANISOU 515 CG ARG A 63 3168 6542 7495 -969 898 -1166 C ATOM 516 CD ARG A 63 -0.700 -0.728 24.621 1.00 54.62 C ANISOU 516 CD ARG A 63 4069 8224 8461 -1305 1059 -1260 C ATOM 517 NE ARG A 63 -1.424 -1.301 23.478 1.00 59.44 N ANISOU 517 NE ARG A 63 4529 8974 9082 -1541 1056 -1320 N ATOM 518 CZ ARG A 63 -2.095 -0.593 22.564 1.00 61.80 C ANISOU 518 CZ ARG A 63 4524 9542 9414 -1324 953 -1488 C ATOM 519 NH1 ARG A 63 -2.129 0.737 22.629 1.00 62.13 N ANISOU 519 NH1 ARG A 63 4420 9693 9495 -842 844 -1604 N ATOM 520 NH2 ARG A 63 -2.730 -1.215 21.572 1.00 62.06 N ANISOU 520 NH2 ARG A 63 4428 9723 9429 -1582 946 -1541 N ATOM 521 N GLU A 64 4.951 -2.277 23.747 1.00 35.62 N ANISOU 521 N GLU A 64 3143 3765 6628 -1007 769 -520 N ATOM 522 CA GLU A 64 5.984 -3.090 23.144 1.00 34.77 C ANISOU 522 CA GLU A 64 3329 3268 6615 -1000 737 -372 C ATOM 523 C GLU A 64 6.098 -4.447 23.810 1.00 36.28 C ANISOU 523 C GLU A 64 3827 3288 6671 -1251 846 -216 C ATOM 524 O GLU A 64 6.121 -4.537 25.039 1.00 37.53 O ANISOU 524 O GLU A 64 4045 3523 6691 -1296 899 -145 O ATOM 525 CB GLU A 64 7.330 -2.346 23.219 1.00 31.89 C ANISOU 525 CB GLU A 64 3023 2721 6373 -674 611 -307 C ATOM 526 CG GLU A 64 8.526 -3.151 22.748 1.00 33.79 C ANISOU 526 CG GLU A 64 3530 2624 6685 -602 580 -154 C ATOM 527 CD GLU A 64 9.819 -2.400 23.021 1.00 40.38 C ANISOU 527 CD GLU A 64 4356 3384 7602 -328 466 -96 C ATOM 528 OE1 GLU A 64 10.284 -1.706 22.103 1.00 42.47 O ANISOU 528 OE1 GLU A 64 4525 3608 8003 -181 386 -135 O ATOM 529 OE2 GLU A 64 10.331 -2.447 24.164 1.00 42.49 O ANISOU 529 OE2 GLU A 64 4699 3665 7781 -280 453 -17 O ATOM 530 N TYR A 65 6.159 -5.494 22.992 1.00 36.97 N ANISOU 530 N TYR A 65 4139 3128 6779 -1409 876 -165 N ATOM 531 CA TYR A 65 6.290 -6.866 23.477 1.00 39.16 C ANISOU 531 CA TYR A 65 4804 3146 6928 -1644 971 -7 C ATOM 532 C TYR A 65 7.592 -7.469 22.924 1.00 38.47 C ANISOU 532 C TYR A 65 5043 2637 6935 -1407 900 116 C ATOM 533 O TYR A 65 7.633 -7.931 21.779 1.00 38.05 O ANISOU 533 O TYR A 65 5092 2407 6957 -1433 886 68 O ATOM 534 CB TYR A 65 5.094 -7.695 23.041 1.00 41.92 C ANISOU 534 CB TYR A 65 5185 3563 7181 -2090 1083 -79 C ATOM 535 CG TYR A 65 3.767 -7.256 23.612 1.00 43.40 C ANISOU 535 CG TYR A 65 5023 4233 7235 -2348 1176 -201 C ATOM 536 CD1 TYR A 65 3.108 -6.133 23.117 1.00 42.42 C ANISOU 536 CD1 TYR A 65 4448 4491 7179 -2213 1118 -399 C ATOM 537 CD2 TYR A 65 3.162 -7.972 24.640 1.00 47.13 C ANISOU 537 CD2 TYR A 65 5620 4797 7492 -2714 1327 -114 C ATOM 538 CE1 TYR A 65 1.878 -5.734 23.636 1.00 44.72 C ANISOU 538 CE1 TYR A 65 4385 5279 7329 -2396 1204 -529 C ATOM 539 CE2 TYR A 65 1.930 -7.583 25.162 1.00 49.25 C ANISOU 539 CE2 TYR A 65 5522 5579 7612 -2954 1432 -238 C ATOM 540 CZ TYR A 65 1.298 -6.462 24.653 1.00 47.70 C ANISOU 540 CZ TYR A 65 4843 5791 7490 -2771 1367 -456 C ATOM 541 OH TYR A 65 0.088 -6.053 25.173 1.00 50.71 O ANISOU 541 OH TYR A 65 4826 6731 7709 -2943 1469 -595 O ATOM 542 N GLN A 66 8.644 -7.460 23.744 1.00 37.74 N ANISOU 542 N GLN A 66 5096 2423 6819 -1161 851 263 N ATOM 543 CA GLN A 66 9.967 -7.882 23.324 1.00 37.62 C ANISOU 543 CA GLN A 66 5310 2105 6879 -857 772 370 C ATOM 544 C GLN A 66 10.391 -9.230 23.938 1.00 41.15 C ANISOU 544 C GLN A 66 6240 2219 7176 -881 819 563 C ATOM 545 O GLN A 66 10.280 -9.434 25.149 1.00 42.97 O ANISOU 545 O GLN A 66 6587 2493 7248 -960 857 680 O ATOM 546 CB GLN A 66 10.963 -6.788 23.681 1.00 36.12 C ANISOU 546 CB GLN A 66 4886 2064 6772 -518 651 379 C ATOM 547 CG GLN A 66 12.391 -7.129 23.376 1.00 37.55 C ANISOU 547 CG GLN A 66 5216 2045 7007 -186 568 486 C ATOM 548 CD GLN A 66 13.266 -5.899 23.338 1.00 36.45 C ANISOU 548 CD GLN A 66 4766 2103 6982 62 450 444 C ATOM 549 OE1 GLN A 66 14.119 -5.729 24.186 1.00 41.74 O ANISOU 549 OE1 GLN A 66 5429 2835 7597 238 377 532 O ATOM 550 NE2 GLN A 66 13.038 -5.029 22.370 1.00 31.68 N ANISOU 550 NE2 GLN A 66 3915 1603 6518 55 424 312 N ATOM 551 N THR A 67 10.864 -10.153 23.103 1.00 41.69 N ANISOU 551 N THR A 67 6622 1946 7275 -796 817 597 N ATOM 552 CA THR A 67 11.398 -11.409 23.622 1.00 45.43 C ANISOU 552 CA THR A 67 7614 2043 7605 -726 839 787 C ATOM 553 C THR A 67 12.916 -11.354 23.660 1.00 45.59 C ANISOU 553 C THR A 67 7672 1985 7667 -206 720 884 C ATOM 554 O THR A 67 13.564 -11.087 22.649 1.00 43.93 O ANISOU 554 O THR A 67 7322 1774 7594 40 663 799 O ATOM 555 CB THR A 67 10.909 -12.624 22.823 1.00 47.05 C ANISOU 555 CB THR A 67 8237 1871 7767 -968 919 762 C ATOM 556 OG1 THR A 67 9.477 -12.634 22.803 1.00 45.92 O ANISOU 556 OG1 THR A 67 7991 1886 7571 -1494 1025 659 O ATOM 557 CG2 THR A 67 11.422 -13.946 23.455 1.00 52.02 C ANISOU 557 CG2 THR A 67 9496 2045 8223 -884 940 977 C ATOM 558 N ARG A 68 13.463 -11.586 24.849 1.00 48.20 N ANISOU 558 N ARG A 68 8163 2296 7855 -48 683 1061 N ATOM 559 CA ARG A 68 14.909 -11.694 25.052 1.00 49.65 C ANISOU 559 CA ARG A 68 8400 2440 8026 453 561 1173 C ATOM 560 C ARG A 68 15.150 -12.822 26.043 1.00 53.85 C ANISOU 560 C ARG A 68 9450 2682 8328 537 568 1402 C ATOM 561 O ARG A 68 14.332 -13.044 26.940 1.00 55.71 O ANISOU 561 O ARG A 68 9845 2911 8412 213 647 1487 O ATOM 562 CB ARG A 68 15.512 -10.416 25.640 1.00 47.41 C ANISOU 562 CB ARG A 68 7647 2573 7793 628 452 1144 C ATOM 563 CG ARG A 68 15.396 -9.178 24.783 1.00 45.32 C ANISOU 563 CG ARG A 68 6905 2577 7736 577 426 947 C ATOM 564 CD ARG A 68 16.156 -8.012 25.407 1.00 48.22 C ANISOU 564 CD ARG A 68 6902 3286 8133 752 305 930 C ATOM 565 NE ARG A 68 15.869 -7.851 26.835 1.00 52.24 N ANISOU 565 NE ARG A 68 7442 3930 8476 655 293 1003 N ATOM 566 CZ ARG A 68 14.897 -7.086 27.340 1.00 54.87 C ANISOU 566 CZ ARG A 68 7593 4462 8794 384 340 903 C ATOM 567 NH1 ARG A 68 14.095 -6.389 26.532 1.00 51.38 N ANISOU 567 NH1 ARG A 68 6920 4104 8498 198 388 730 N ATOM 568 NH2 ARG A 68 14.728 -7.013 28.663 1.00 56.79 N ANISOU 568 NH2 ARG A 68 7885 4841 8852 329 335 973 N ATOM 569 N GLN A 69 16.291 -13.499 25.902 1.00 56.00 N ANISOU 569 N GLN A 69 9976 2746 8555 996 484 1508 N ATOM 570 CA GLN A 69 16.656 -14.636 26.772 1.00 60.88 C ANISOU 570 CA GLN A 69 11156 3037 8938 1180 466 1747 C ATOM 571 C GLN A 69 15.435 -15.517 27.047 1.00 62.78 C ANISOU 571 C GLN A 69 11882 2929 9043 681 615 1822 C ATOM 572 O GLN A 69 15.160 -15.898 28.188 1.00 65.80 O ANISOU 572 O GLN A 69 12542 3247 9211 547 644 2010 O ATOM 573 CB GLN A 69 17.336 -14.145 28.066 1.00 61.56 C ANISOU 573 CB GLN A 69 11066 3435 8887 1421 348 1886 C ATOM 574 CG GLN A 69 18.784 -13.610 27.866 1.00 63.79 C ANISOU 574 CG GLN A 69 10988 4008 9243 1967 180 1857 C ATOM 575 CD GLN A 69 18.874 -12.103 27.666 1.00 65.44 C ANISOU 575 CD GLN A 69 10522 4706 9635 1862 133 1670 C ATOM 576 OE1 GLN A 69 18.394 -11.328 28.499 1.00 67.14 O ANISOU 576 OE1 GLN A 69 10517 5181 9811 1617 130 1650 O ATOM 577 NE2 GLN A 69 19.510 -11.675 26.567 1.00 64.39 N ANISOU 577 NE2 GLN A 69 10084 4695 9684 2053 99 1534 N ATOM 578 N ASN A 70 14.696 -15.811 25.974 1.00 62.09 N ANISOU 578 N ASN A 70 11878 2648 9066 377 712 1668 N ATOM 579 CA ASN A 70 13.500 -16.679 25.997 1.00 64.88 C ANISOU 579 CA ASN A 70 12669 2677 9306 -174 860 1696 C ATOM 580 C ASN A 70 12.379 -16.264 26.949 1.00 64.80 C ANISOU 580 C ASN A 70 12482 2952 9186 -695 967 1729 C ATOM 581 O ASN A 70 11.676 -17.110 27.498 1.00 68.37 O ANISOU 581 O ASN A 70 13383 3149 9444 -1083 1078 1865 O ATOM 582 CB ASN A 70 13.896 -18.154 26.238 1.00 70.07 C ANISOU 582 CB ASN A 70 14140 2717 9768 -17 863 1903 C ATOM 583 CG ASN A 70 15.033 -18.593 25.348 1.00 70.58 C ANISOU 583 CG ASN A 70 14382 2526 9910 570 762 1858 C ATOM 584 OD1 ASN A 70 16.060 -19.058 25.830 1.00 77.08 O ANISOU 584 OD1 ASN A 70 15482 3191 10615 1094 662 2028 O ATOM 585 ND2 ASN A 70 14.866 -18.420 24.038 1.00 67.49 N ANISOU 585 ND2 ASN A 70 13804 2140 9700 514 785 1622 N ATOM 586 N GLN A 71 12.207 -14.962 27.147 1.00 60.96 N ANISOU 586 N GLN A 71 11358 2996 8807 -709 939 1603 N ATOM 587 CA GLN A 71 11.058 -14.495 27.922 1.00 60.95 C ANISOU 587 CA GLN A 71 11128 3323 8705 -1180 1053 1582 C ATOM 588 C GLN A 71 10.523 -13.150 27.453 1.00 56.38 C ANISOU 588 C GLN A 71 9874 3233 8313 -1271 1046 1331 C ATOM 589 O GLN A 71 11.236 -12.371 26.805 1.00 52.75 O ANISOU 589 O GLN A 71 9088 2906 8047 -923 930 1215 O ATOM 590 CB GLN A 71 11.333 -14.523 29.437 1.00 63.46 C ANISOU 590 CB GLN A 71 11582 3743 8787 -1099 1042 1801 C ATOM 591 CG GLN A 71 12.390 -13.549 29.939 1.00 61.00 C ANISOU 591 CG GLN A 71 10905 3746 8525 -613 879 1798 C ATOM 592 CD GLN A 71 12.933 -13.933 31.310 1.00 64.81 C ANISOU 592 CD GLN A 71 11684 4203 8738 -432 831 2052 C ATOM 593 OE1 GLN A 71 12.895 -13.141 32.253 1.00 64.80 O ANISOU 593 OE1 GLN A 71 11392 4586 8643 -429 805 2046 O ATOM 594 NE2 GLN A 71 13.438 -15.154 31.422 1.00 67.51 N ANISOU 594 NE2 GLN A 71 12633 4081 8936 -262 812 2272 N ATOM 595 N CYS A 72 9.256 -12.908 27.775 1.00 56.59 N ANISOU 595 N CYS A 72 9710 3528 8262 -1741 1175 1253 N ATOM 596 CA CYS A 72 8.562 -11.710 27.353 1.00 53.24 C ANISOU 596 CA CYS A 72 8692 3558 7979 -1835 1178 1013 C ATOM 597 C CYS A 72 8.809 -10.547 28.301 1.00 51.23 C ANISOU 597 C CYS A 72 8067 3698 7702 -1620 1119 991 C ATOM 598 O CYS A 72 8.632 -10.667 29.518 1.00 53.04 O ANISOU 598 O CYS A 72 8395 4041 7717 -1722 1177 1114 O ATOM 599 CB CYS A 72 7.064 -11.973 27.226 1.00 55.42 C ANISOU 599 CB CYS A 72 8883 4008 8165 -2407 1339 914 C ATOM 600 SG CYS A 72 6.163 -10.638 26.406 1.00 53.13 S ANISOU 600 SG CYS A 72 7900 4238 8051 -2459 1322 600 S ATOM 601 N PHE A 73 9.213 -9.423 27.715 1.00 47.41 N ANISOU 601 N PHE A 73 7184 3407 7422 -1339 1004 829 N ATOM 602 CA PHE A 73 9.339 -8.149 28.407 1.00 45.49 C ANISOU 602 CA PHE A 73 6565 3530 7188 -1165 938 742 C ATOM 603 C PHE A 73 8.389 -7.155 27.781 1.00 43.00 C ANISOU 603 C PHE A 73 5819 3527 6994 -1278 960 500 C ATOM 604 O PHE A 73 8.552 -6.765 26.625 1.00 41.19 O ANISOU 604 O PHE A 73 5443 3247 6962 -1160 892 389 O ATOM 605 CB PHE A 73 10.782 -7.630 28.333 1.00 43.77 C ANISOU 605 CB PHE A 73 6295 3246 7089 -718 763 777 C ATOM 606 CG PHE A 73 11.750 -8.486 29.080 1.00 47.52 C ANISOU 606 CG PHE A 73 7137 3502 7416 -526 715 1007 C ATOM 607 CD1 PHE A 73 11.861 -8.375 30.465 1.00 49.79 C ANISOU 607 CD1 PHE A 73 7474 3952 7491 -507 705 1109 C ATOM 608 CD2 PHE A 73 12.518 -9.440 28.411 1.00 49.42 C ANISOU 608 CD2 PHE A 73 7694 3381 7701 -342 678 1119 C ATOM 609 CE1 PHE A 73 12.740 -9.185 31.167 1.00 52.53 C ANISOU 609 CE1 PHE A 73 8174 4112 7673 -298 644 1337 C ATOM 610 CE2 PHE A 73 13.404 -10.262 29.105 1.00 52.39 C ANISOU 610 CE2 PHE A 73 8431 3556 7920 -102 620 1337 C ATOM 611 CZ PHE A 73 13.520 -10.143 30.477 1.00 54.08 C ANISOU 611 CZ PHE A 73 8690 3936 7921 -78 597 1456 C ATOM 612 N TYR A 74 7.387 -6.758 28.549 1.00 43.38 N ANISOU 612 N TYR A 74 5669 3915 6897 -1487 1058 423 N ATOM 613 CA TYR A 74 6.429 -5.777 28.094 1.00 41.58 C ANISOU 613 CA TYR A 74 5020 4033 6744 -1535 1073 189 C ATOM 614 C TYR A 74 6.743 -4.436 28.716 1.00 40.41 C ANISOU 614 C TYR A 74 4617 4120 6617 -1243 979 80 C ATOM 615 O TYR A 74 6.986 -4.346 29.918 1.00 41.32 O ANISOU 615 O TYR A 74 4798 4334 6566 -1204 990 147 O ATOM 616 CB TYR A 74 4.992 -6.200 28.460 1.00 44.26 C ANISOU 616 CB TYR A 74 5258 4667 6893 -1958 1256 136 C ATOM 617 CG TYR A 74 3.970 -5.091 28.261 1.00 42.87 C ANISOU 617 CG TYR A 74 4601 4951 6739 -1930 1269 -115 C ATOM 618 CD1 TYR A 74 3.665 -4.205 29.294 1.00 43.48 C ANISOU 618 CD1 TYR A 74 4454 5378 6688 -1806 1292 -208 C ATOM 619 CD2 TYR A 74 3.333 -4.909 27.030 1.00 41.35 C ANISOU 619 CD2 TYR A 74 4189 4845 6677 -1983 1246 -268 C ATOM 620 CE1 TYR A 74 2.733 -3.185 29.117 1.00 43.20 C ANISOU 620 CE1 TYR A 74 4002 5756 6657 -1710 1298 -449 C ATOM 621 CE2 TYR A 74 2.402 -3.900 26.838 1.00 41.32 C ANISOU 621 CE2 TYR A 74 3755 5271 6675 -1894 1241 -491 C ATOM 622 CZ TYR A 74 2.100 -3.043 27.887 1.00 44.20 C ANISOU 622 CZ TYR A 74 3915 5965 6914 -1743 1269 -582 C ATOM 623 OH TYR A 74 1.170 -2.041 27.711 1.00 46.16 O ANISOU 623 OH TYR A 74 3757 6635 7147 -1591 1260 -815 O ATOM 624 N ASN A 75 6.715 -3.402 27.885 1.00 38.69 N ANISOU 624 N ASN A 75 4139 3978 6585 -1050 882 -89 N ATOM 625 CA ASN A 75 6.900 -2.008 28.303 1.00 39.25 C ANISOU 625 CA ASN A 75 3991 4232 6691 -787 784 -231 C ATOM 626 C ASN A 75 5.943 -1.105 27.523 1.00 38.61 C ANISOU 626 C ASN A 75 3602 4370 6699 -733 774 -449 C ATOM 627 O ASN A 75 5.727 -1.330 26.337 1.00 39.32 O ANISOU 627 O ASN A 75 3656 4370 6915 -777 760 -469 O ATOM 628 CB ASN A 75 8.347 -1.551 28.044 1.00 36.82 C ANISOU 628 CB ASN A 75 3776 3673 6540 -514 617 -169 C ATOM 629 CG ASN A 75 9.348 -2.166 29.028 1.00 41.04 C ANISOU 629 CG ASN A 75 4551 4089 6955 -469 588 16 C ATOM 630 OD1 ASN A 75 10.124 -3.080 28.672 1.00 42.91 O ANISOU 630 OD1 ASN A 75 5009 4068 7227 -443 567 181 O ATOM 631 ND2 ASN A 75 9.317 -1.697 30.276 1.00 42.98 N ANISOU 631 ND2 ASN A 75 4764 4535 7032 -434 582 -18 N ATOM 632 N SER A 76 5.341 -0.118 28.175 1.00 39.07 N ANISOU 632 N SER A 76 3449 4725 6669 -616 777 -616 N ATOM 633 CA SER A 76 4.681 0.957 27.435 1.00 38.69 C ANISOU 633 CA SER A 76 3150 4833 6718 -429 716 -820 C ATOM 634 C SER A 76 5.307 2.287 27.829 1.00 38.49 C ANISOU 634 C SER A 76 3134 4743 6748 -115 578 -920 C ATOM 635 O SER A 76 5.943 2.392 28.886 1.00 39.29 O ANISOU 635 O SER A 76 3356 4816 6758 -84 559 -880 O ATOM 636 CB SER A 76 3.164 0.968 27.644 1.00 41.21 C ANISOU 636 CB SER A 76 3183 5604 6873 -544 846 -976 C ATOM 637 OG SER A 76 2.812 1.532 28.885 1.00 44.17 O ANISOU 637 OG SER A 76 3464 6257 7062 -451 899 -1083 O ATOM 638 N SER A 77 5.167 3.281 26.958 1.00 37.19 N ANISOU 638 N SER A 77 2876 4533 6723 103 471 -1043 N ATOM 639 CA SER A 77 5.768 4.602 27.163 1.00 37.25 C ANISOU 639 CA SER A 77 2951 4404 6797 371 328 -1141 C ATOM 640 C SER A 77 5.267 5.493 26.046 1.00 36.57 C ANISOU 640 C SER A 77 2775 4293 6829 578 243 -1258 C ATOM 641 O SER A 77 4.519 5.024 25.167 1.00 36.81 O ANISOU 641 O SER A 77 2663 4445 6879 512 290 -1258 O ATOM 642 CB SER A 77 7.313 4.544 27.123 1.00 34.93 C ANISOU 642 CB SER A 77 2875 3773 6624 351 223 -984 C ATOM 643 OG SER A 77 7.765 4.050 25.871 1.00 33.34 O ANISOU 643 OG SER A 77 2716 3367 6585 291 198 -856 O ATOM 644 N TYR A 78 5.682 6.759 26.087 1.00 35.78 N ANISOU 644 N TYR A 78 2779 4026 6789 814 111 -1353 N ATOM 645 CA TYR A 78 5.333 7.744 25.061 1.00 35.36 C ANISOU 645 CA TYR A 78 2724 3876 6836 1052 6 -1442 C ATOM 646 C TYR A 78 6.601 8.121 24.296 1.00 33.17 C ANISOU 646 C TYR A 78 2663 3199 6739 1027 -115 -1305 C ATOM 647 O TYR A 78 7.644 8.380 24.875 1.00 33.46 O ANISOU 647 O TYR A 78 2855 3056 6802 965 -171 -1260 O ATOM 648 CB TYR A 78 4.644 8.975 25.674 1.00 37.07 C ANISOU 648 CB TYR A 78 2932 4206 6947 1366 -44 -1677 C ATOM 649 CG TYR A 78 3.219 8.701 26.127 1.00 39.51 C ANISOU 649 CG TYR A 78 2948 4997 7069 1441 81 -1832 C ATOM 650 CD1 TYR A 78 2.954 8.278 27.428 1.00 40.08 C ANISOU 650 CD1 TYR A 78 2933 5341 6953 1335 205 -1889 C ATOM 651 CD2 TYR A 78 2.140 8.853 25.251 1.00 38.39 C ANISOU 651 CD2 TYR A 78 2591 5083 6911 1609 77 -1920 C ATOM 652 CE1 TYR A 78 1.658 8.008 27.847 1.00 41.46 C ANISOU 652 CE1 TYR A 78 2806 6014 6934 1363 342 -2027 C ATOM 653 CE2 TYR A 78 0.839 8.585 25.665 1.00 42.10 C ANISOU 653 CE2 TYR A 78 2731 6074 7192 1654 197 -2071 C ATOM 654 CZ TYR A 78 0.611 8.167 26.960 1.00 42.90 C ANISOU 654 CZ TYR A 78 2741 6446 7112 1517 338 -2124 C ATOM 655 OH TYR A 78 -0.667 7.904 27.374 1.00 47.82 O ANISOU 655 OH TYR A 78 3009 7635 7527 1528 476 -2271 O ATOM 656 N LEU A 79 6.514 8.068 22.977 1.00 32.25 N ANISOU 656 N LEU A 79 2533 2990 6729 1046 -147 -1235 N ATOM 657 CA LEU A 79 7.534 8.581 22.093 1.00 30.32 C ANISOU 657 CA LEU A 79 2471 2419 6632 1044 -250 -1120 C ATOM 658 C LEU A 79 7.215 10.037 21.766 1.00 32.42 C ANISOU 658 C LEU A 79 2871 2538 6911 1314 -373 -1234 C ATOM 659 O LEU A 79 6.035 10.361 21.583 1.00 31.85 O ANISOU 659 O LEU A 79 2688 2652 6761 1539 -376 -1366 O ATOM 660 CB LEU A 79 7.486 7.746 20.826 1.00 29.68 C ANISOU 660 CB LEU A 79 2318 2342 6617 942 -210 -995 C ATOM 661 CG LEU A 79 7.702 6.219 21.029 1.00 30.00 C ANISOU 661 CG LEU A 79 2287 2477 6635 694 -88 -887 C ATOM 662 CD1 LEU A 79 7.941 5.571 19.710 1.00 30.42 C ANISOU 662 CD1 LEU A 79 2349 2446 6765 614 -75 -775 C ATOM 663 CD2 LEU A 79 8.887 6.002 21.926 1.00 30.09 C ANISOU 663 CD2 LEU A 79 2409 2366 6656 590 -90 -797 C ATOM 664 N ASN A 80 8.221 10.920 21.707 1.00 32.13 N ANISOU 664 N ASN A 80 3077 2181 6951 1297 -476 -1190 N ATOM 665 CA ASN A 80 7.922 12.298 21.275 1.00 35.51 C ANISOU 665 CA ASN A 80 3717 2390 7386 1547 -599 -1276 C ATOM 666 C ASN A 80 8.108 12.423 19.776 1.00 34.36 C ANISOU 666 C ASN A 80 3646 2084 7326 1547 -642 -1124 C ATOM 667 O ASN A 80 8.926 11.732 19.216 1.00 31.56 O ANISOU 667 O ASN A 80 3252 1692 7049 1313 -598 -957 O ATOM 668 CB ASN A 80 8.769 13.357 22.006 1.00 37.04 C ANISOU 668 CB ASN A 80 4196 2288 7589 1512 -699 -1335 C ATOM 669 CG ASN A 80 8.341 13.543 23.448 1.00 41.21 C ANISOU 669 CG ASN A 80 4699 2971 7989 1614 -683 -1540 C ATOM 670 OD1 ASN A 80 7.171 13.369 23.795 1.00 43.64 O ANISOU 670 OD1 ASN A 80 4833 3563 8185 1831 -623 -1679 O ATOM 671 ND2 ASN A 80 9.293 13.887 24.302 1.00 44.65 N ANISOU 671 ND2 ASN A 80 5285 3262 8417 1447 -735 -1566 N ATOM 672 N VAL A 81 7.377 13.333 19.139 1.00 35.77 N ANISOU 672 N VAL A 81 3948 2171 7473 1838 -731 -1184 N ATOM 673 CA VAL A 81 7.505 13.494 17.696 1.00 34.99 C ANISOU 673 CA VAL A 81 3942 1932 7421 1856 -778 -1030 C ATOM 674 C VAL A 81 8.073 14.891 17.421 1.00 37.55 C ANISOU 674 C VAL A 81 4678 1819 7771 1924 -905 -989 C ATOM 675 O VAL A 81 7.557 15.883 17.939 1.00 39.67 O ANISOU 675 O VAL A 81 5142 1954 7976 2195 -992 -1140 O ATOM 676 CB VAL A 81 6.134 13.308 16.989 1.00 36.67 C ANISOU 676 CB VAL A 81 3962 2425 7546 2139 -789 -1101 C ATOM 677 CG1 VAL A 81 6.252 13.580 15.498 1.00 35.37 C ANISOU 677 CG1 VAL A 81 3929 2112 7397 2190 -857 -943 C ATOM 678 CG2 VAL A 81 5.603 11.879 17.238 1.00 33.33 C ANISOU 678 CG2 VAL A 81 3158 2416 7090 1978 -655 -1137 C ATOM 679 N GLN A 82 9.126 14.960 16.615 1.00 36.14 N ANISOU 679 N GLN A 82 4643 1421 7667 1676 -910 -789 N ATOM 680 CA GLN A 82 9.630 16.217 16.133 1.00 40.35 C ANISOU 680 CA GLN A 82 5585 1537 8209 1679 -1018 -709 C ATOM 681 C GLN A 82 9.252 16.273 14.652 1.00 40.32 C ANISOU 681 C GLN A 82 5634 1514 8172 1811 -1044 -561 C ATOM 682 O GLN A 82 9.893 15.661 13.805 1.00 38.04 O ANISOU 682 O GLN A 82 5249 1285 7918 1579 -976 -387 O ATOM 683 CB GLN A 82 11.143 16.325 16.368 1.00 40.61 C ANISOU 683 CB GLN A 82 5727 1383 8320 1253 -998 -592 C ATOM 684 CG GLN A 82 11.606 16.108 17.835 1.00 42.45 C ANISOU 684 CG GLN A 82 5861 1704 8566 1099 -978 -730 C ATOM 685 CD GLN A 82 11.515 14.647 18.353 1.00 41.26 C ANISOU 685 CD GLN A 82 5295 1959 8421 1032 -856 -748 C ATOM 686 OE1 GLN A 82 11.846 13.650 17.649 1.00 37.97 O ANISOU 686 OE1 GLN A 82 4671 1712 8044 903 -767 -606 O ATOM 687 NE2 GLN A 82 11.084 14.521 19.610 1.00 40.61 N ANISOU 687 NE2 GLN A 82 5129 2019 8284 1121 -848 -925 N ATOM 688 N ARG A 83 8.184 17.010 14.355 1.00 42.35 N ANISOU 688 N ARG A 83 6040 1714 8339 2220 -1149 -641 N ATOM 689 CA ARG A 83 7.535 16.941 13.049 1.00 42.73 C ANISOU 689 CA ARG A 83 6065 1858 8314 2430 -1190 -540 C ATOM 690 C ARG A 83 8.405 17.416 11.899 1.00 43.13 C ANISOU 690 C ARG A 83 6421 1599 8368 2241 -1214 -286 C ATOM 691 O ARG A 83 8.556 16.726 10.906 1.00 41.89 O ANISOU 691 O ARG A 83 6108 1613 8195 2127 -1157 -150 O ATOM 692 CB ARG A 83 6.217 17.735 13.059 1.00 45.88 C ANISOU 692 CB ARG A 83 6564 2277 8590 2972 -1320 -689 C ATOM 693 CG ARG A 83 5.073 16.990 13.721 1.00 44.98 C ANISOU 693 CG ARG A 83 6002 2665 8422 3180 -1272 -912 C ATOM 694 CD ARG A 83 3.779 17.804 13.588 1.00 50.64 C ANISOU 694 CD ARG A 83 6778 3469 8993 3765 -1408 -1056 C ATOM 695 NE ARG A 83 2.703 17.170 14.343 1.00 50.59 N ANISOU 695 NE ARG A 83 6314 3992 8916 3936 -1346 -1288 N ATOM 696 CZ ARG A 83 1.558 16.738 13.823 1.00 53.81 C ANISOU 696 CZ ARG A 83 6367 4869 9209 4184 -1369 -1365 C ATOM 697 NH1 ARG A 83 1.290 16.899 12.525 1.00 54.45 N ANISOU 697 NH1 ARG A 83 6512 4954 9224 4347 -1472 -1236 N ATOM 698 NH2 ARG A 83 0.666 16.163 14.620 1.00 54.66 N ANISOU 698 NH2 ARG A 83 6049 5473 9245 4257 -1289 -1576 N ATOM 699 N GLU A 84 8.951 18.614 12.027 1.00 45.87 N ANISOU 699 N GLU A 84 7226 1488 8715 2199 -1296 -229 N ATOM 700 CA GLU A 84 9.731 19.222 10.952 1.00 46.86 C ANISOU 700 CA GLU A 84 7700 1294 8813 2002 -1318 25 C ATOM 701 C GLU A 84 11.021 18.443 10.671 1.00 43.84 C ANISOU 701 C GLU A 84 7114 1033 8509 1489 -1172 182 C ATOM 702 O GLU A 84 11.431 18.315 9.527 1.00 43.89 O ANISOU 702 O GLU A 84 7161 1047 8468 1355 -1131 385 O ATOM 703 CB GLU A 84 10.042 20.684 11.293 1.00 50.31 C ANISOU 703 CB GLU A 84 8715 1176 9226 2013 -1436 35 C ATOM 704 CG GLU A 84 8.758 21.555 11.438 1.00 56.34 C ANISOU 704 CG GLU A 84 9746 1780 9881 2616 -1595 -112 C ATOM 705 CD GLU A 84 8.091 21.473 12.838 1.00 59.78 C ANISOU 705 CD GLU A 84 9994 2381 10337 2861 -1607 -426 C ATOM 706 OE1 GLU A 84 7.119 22.241 13.080 1.00 63.09 O ANISOU 706 OE1 GLU A 84 10632 2681 10659 3371 -1730 -577 O ATOM 707 OE2 GLU A 84 8.529 20.640 13.683 1.00 57.43 O ANISOU 707 OE2 GLU A 84 9337 2351 10133 2570 -1493 -520 O ATOM 708 N ASN A 85 11.661 17.951 11.716 1.00 41.75 N ANISOU 708 N ASN A 85 6637 882 8343 1232 -1099 84 N ATOM 709 CA ASN A 85 12.890 17.154 11.567 1.00 40.45 C ANISOU 709 CA ASN A 85 6234 890 8244 807 -967 206 C ATOM 710 C ASN A 85 12.628 15.724 11.100 1.00 37.67 C ANISOU 710 C ASN A 85 5460 957 7896 851 -857 211 C ATOM 711 O ASN A 85 13.558 14.995 10.698 1.00 36.22 O ANISOU 711 O ASN A 85 5091 933 7738 586 -745 325 O ATOM 712 CB ASN A 85 13.649 17.123 12.899 1.00 40.50 C ANISOU 712 CB ASN A 85 6162 897 8331 559 -951 93 C ATOM 713 CG ASN A 85 14.284 18.479 13.258 1.00 45.03 C ANISOU 713 CG ASN A 85 7168 1043 8898 353 -1045 109 C ATOM 714 OD1 ASN A 85 14.800 18.648 14.357 1.00 49.98 O ANISOU 714 OD1 ASN A 85 7788 1638 9565 173 -1067 -9 O ATOM 715 ND2 ASN A 85 14.248 19.431 12.337 1.00 45.16 N ANISOU 715 ND2 ASN A 85 7585 725 8848 364 -1105 257 N ATOM 716 N GLY A 86 11.363 15.311 11.152 1.00 36.39 N ANISOU 716 N GLY A 86 5145 985 7696 1185 -887 75 N ATOM 717 CA GLY A 86 10.989 13.972 10.736 1.00 34.19 C ANISOU 717 CA GLY A 86 4511 1070 7408 1205 -795 55 C ATOM 718 C GLY A 86 11.569 12.913 11.649 1.00 31.44 C ANISOU 718 C GLY A 86 3888 914 7143 993 -686 -8 C ATOM 719 O GLY A 86 11.990 11.859 11.179 1.00 29.87 O ANISOU 719 O GLY A 86 3497 900 6954 861 -584 54 O ATOM 720 N THR A 87 11.606 13.195 12.951 1.00 31.63 N ANISOU 720 N THR A 87 3922 887 7211 982 -712 -133 N ATOM 721 CA THR A 87 12.157 12.234 13.929 1.00 29.85 C ANISOU 721 CA THR A 87 3466 838 7039 806 -625 -182 C ATOM 722 C THR A 87 11.148 11.916 15.026 1.00 30.51 C ANISOU 722 C THR A 87 3414 1082 7095 972 -627 -374 C ATOM 723 O THR A 87 10.163 12.663 15.256 1.00 30.30 O ANISOU 723 O THR A 87 3480 1016 7018 1223 -706 -497 O ATOM 724 CB THR A 87 13.399 12.789 14.647 1.00 30.39 C ANISOU 724 CB THR A 87 3640 751 7156 559 -644 -145 C ATOM 725 OG1 THR A 87 13.052 14.012 15.323 1.00 32.75 O ANISOU 725 OG1 THR A 87 4194 811 7437 656 -757 -255 O ATOM 726 CG2 THR A 87 14.562 13.032 13.664 1.00 30.12 C ANISOU 726 CG2 THR A 87 3681 629 7133 317 -613 52 C ATOM 727 N VAL A 88 11.420 10.814 15.712 1.00 29.02 N ANISOU 727 N VAL A 88 3017 1085 6924 845 -537 -394 N ATOM 728 CA VAL A 88 10.658 10.360 16.853 1.00 30.83 C ANISOU 728 CA VAL A 88 3109 1496 7110 921 -507 -545 C ATOM 729 C VAL A 88 11.711 10.122 17.933 1.00 31.24 C ANISOU 729 C VAL A 88 3148 1534 7187 734 -487 -527 C ATOM 730 O VAL A 88 12.847 9.728 17.626 1.00 32.32 O ANISOU 730 O VAL A 88 3264 1645 7372 558 -457 -394 O ATOM 731 CB VAL A 88 9.915 9.036 16.502 1.00 30.97 C ANISOU 731 CB VAL A 88 2907 1770 7091 915 -410 -556 C ATOM 732 CG1 VAL A 88 9.362 8.329 17.754 1.00 31.42 C ANISOU 732 CG1 VAL A 88 2817 2030 7089 887 -342 -666 C ATOM 733 CG2 VAL A 88 8.795 9.282 15.465 1.00 30.04 C ANISOU 733 CG2 VAL A 88 2757 1737 6921 1103 -451 -599 C ATOM 734 N SER A 89 11.378 10.314 19.195 1.00 31.98 N ANISOU 734 N SER A 89 3234 1688 7229 782 -503 -661 N ATOM 735 CA SER A 89 12.374 10.041 20.213 1.00 33.97 C ANISOU 735 CA SER A 89 3465 1963 7478 615 -499 -640 C ATOM 736 C SER A 89 11.791 9.227 21.352 1.00 35.30 C ANISOU 736 C SER A 89 3502 2355 7555 642 -430 -725 C ATOM 737 O SER A 89 10.605 9.348 21.682 1.00 34.98 O ANISOU 737 O SER A 89 3417 2433 7441 791 -408 -858 O ATOM 738 CB SER A 89 12.997 11.333 20.736 1.00 34.72 C ANISOU 738 CB SER A 89 3760 1854 7579 563 -615 -702 C ATOM 739 OG SER A 89 12.010 12.091 21.402 1.00 38.97 O ANISOU 739 OG SER A 89 4399 2362 8045 765 -662 -891 O ATOM 740 N ARG A 90 12.659 8.430 21.957 1.00 36.73 N ANISOU 740 N ARG A 90 3621 2612 7721 503 -398 -641 N ATOM 741 CA ARG A 90 12.318 7.497 23.034 1.00 40.34 C ANISOU 741 CA ARG A 90 3993 3261 8072 488 -324 -664 C ATOM 742 C ARG A 90 13.311 7.715 24.171 1.00 43.89 C ANISOU 742 C ARG A 90 4479 3728 8468 410 -393 -668 C ATOM 743 O ARG A 90 14.507 7.835 23.932 1.00 44.36 O ANISOU 743 O ARG A 90 4543 3724 8585 313 -451 -576 O ATOM 744 CB ARG A 90 12.401 6.057 22.515 1.00 38.31 C ANISOU 744 CB ARG A 90 3662 3069 7825 420 -220 -525 C ATOM 745 CG ARG A 90 12.205 4.987 23.573 1.00 39.43 C ANISOU 745 CG ARG A 90 3782 3354 7845 368 -141 -499 C ATOM 746 CD ARG A 90 11.935 3.637 22.929 1.00 42.78 C ANISOU 746 CD ARG A 90 4203 3782 8271 305 -34 -396 C ATOM 747 NE ARG A 90 11.284 2.725 23.869 1.00 45.52 N ANISOU 747 NE ARG A 90 4566 4253 8477 226 61 -391 N ATOM 748 CZ ARG A 90 11.078 1.433 23.648 1.00 45.91 C ANISOU 748 CZ ARG A 90 4682 4275 8486 126 158 -297 C ATOM 749 NH1 ARG A 90 11.475 0.878 22.503 1.00 46.29 N ANISOU 749 NH1 ARG A 90 4777 4184 8625 127 169 -222 N ATOM 750 NH2 ARG A 90 10.460 0.688 24.573 1.00 48.19 N ANISOU 750 NH2 ARG A 90 5016 4667 8625 12 250 -281 N ATOM 751 N TYR A 91 12.818 7.780 25.401 1.00 48.66 N ANISOU 751 N TYR A 91 5089 4459 8941 449 -386 -782 N ATOM 752 CA TYR A 91 13.675 7.963 26.568 1.00 53.04 C ANISOU 752 CA TYR A 91 5676 5069 9407 383 -462 -804 C ATOM 753 C TYR A 91 13.854 6.620 27.291 1.00 54.69 C ANISOU 753 C TYR A 91 5823 5453 9502 346 -386 -684 C ATOM 754 O TYR A 91 12.902 6.079 27.839 1.00 54.40 O ANISOU 754 O TYR A 91 5770 5549 9350 374 -287 -717 O ATOM 755 CB TYR A 91 13.072 9.012 27.507 1.00 55.20 C ANISOU 755 CB TYR A 91 6041 5358 9575 468 -515 -1023 C ATOM 756 CG TYR A 91 13.017 10.409 26.910 1.00 59.09 C ANISOU 756 CG TYR A 91 6683 5609 10160 522 -615 -1139 C ATOM 757 CD1 TYR A 91 12.068 10.743 25.926 1.00 61.21 C ANISOU 757 CD1 TYR A 91 6971 5788 10499 670 -581 -1171 C ATOM 758 CD2 TYR A 91 13.905 11.396 27.324 1.00 61.95 C ANISOU 758 CD2 TYR A 91 7192 5825 10521 417 -752 -1214 C ATOM 759 CE1 TYR A 91 12.021 12.016 25.369 1.00 63.03 C ANISOU 759 CE1 TYR A 91 7398 5757 10794 748 -681 -1252 C ATOM 760 CE2 TYR A 91 13.857 12.671 26.783 1.00 65.46 C ANISOU 760 CE2 TYR A 91 7848 5987 11037 443 -843 -1306 C ATOM 761 CZ TYR A 91 12.915 12.973 25.807 1.00 65.90 C ANISOU 761 CZ TYR A 91 7956 5924 11159 627 -806 -1315 C ATOM 762 OH TYR A 91 12.881 14.239 25.271 1.00 69.15 O ANISOU 762 OH TYR A 91 8635 6018 11622 679 -905 -1383 O ATOM 763 N GLU A 92 15.075 6.085 27.253 1.00 57.02 N ANISOU 763 N GLU A 92 6089 5758 9818 289 -431 -539 N ATOM 764 CA GLU A 92 15.451 4.876 28.006 1.00 60.10 C ANISOU 764 CA GLU A 92 6475 6278 10080 299 -394 -407 C ATOM 765 C GLU A 92 16.691 5.212 28.818 1.00 62.22 C ANISOU 765 C GLU A 92 6712 6651 10275 273 -535 -400 C ATOM 766 O GLU A 92 17.555 5.959 28.339 1.00 63.02 O ANISOU 766 O GLU A 92 6757 6712 10477 206 -634 -419 O ATOM 767 CB GLU A 92 15.755 3.699 27.077 1.00 59.66 C ANISOU 767 CB GLU A 92 6412 6156 10098 323 -317 -229 C ATOM 768 CG GLU A 92 14.525 2.952 26.560 1.00 61.67 C ANISOU 768 CG GLU A 92 6713 6359 10358 308 -171 -218 C ATOM 769 CD GLU A 92 14.856 2.020 25.401 1.00 64.74 C ANISOU 769 CD GLU A 92 7127 6630 10843 327 -115 -88 C ATOM 770 OE1 GLU A 92 15.574 2.454 24.463 1.00 65.66 O ANISOU 770 OE1 GLU A 92 7178 6685 11085 353 -165 -70 O ATOM 771 OE2 GLU A 92 14.387 0.855 25.420 1.00 65.48 O ANISOU 771 OE2 GLU A 92 7324 6686 10870 301 -14 -8 O ATOM 772 N GLY A 93 16.785 4.662 30.033 1.00 64.45 N ANISOU 772 N GLY A 93 7030 7092 10366 305 -546 -368 N ATOM 773 CA GLY A 93 17.865 5.016 30.973 1.00 66.37 C ANISOU 773 CA GLY A 93 7230 7495 10493 285 -701 -388 C ATOM 774 C GLY A 93 17.869 6.522 31.171 1.00 67.79 C ANISOU 774 C GLY A 93 7424 7630 10702 183 -807 -607 C ATOM 775 O GLY A 93 16.803 7.155 31.269 1.00 67.87 O ANISOU 775 O GLY A 93 7524 7555 10708 200 -756 -762 O ATOM 776 N GLY A 94 19.063 7.106 31.203 1.00 68.87 N ANISOU 776 N GLY A 94 7480 7829 10861 77 -957 -627 N ATOM 777 CA GLY A 94 19.196 8.559 31.185 1.00 69.83 C ANISOU 777 CA GLY A 94 7666 7832 11033 -74 -1064 -821 C ATOM 778 C GLY A 94 19.559 9.017 29.785 1.00 68.79 C ANISOU 778 C GLY A 94 7501 7517 11117 -177 -1054 -767 C ATOM 779 O GLY A 94 20.583 9.682 29.582 1.00 70.51 O ANISOU 779 O GLY A 94 7658 7756 11375 -370 -1167 -784 O ATOM 780 N ARG A 95 18.725 8.663 28.809 1.00 66.16 N ANISOU 780 N ARG A 95 7202 7030 10905 -74 -919 -700 N ATOM 781 CA ARG A 95 19.080 8.909 27.418 1.00 64.43 C ANISOU 781 CA ARG A 95 6948 6671 10862 -149 -893 -612 C ATOM 782 C ARG A 95 17.873 9.051 26.486 1.00 61.04 C ANISOU 782 C ARG A 95 6627 6031 10536 -45 -787 -630 C ATOM 783 O ARG A 95 17.059 8.133 26.367 1.00 59.64 O ANISOU 783 O ARG A 95 6426 5893 10342 92 -672 -579 O ATOM 784 CB ARG A 95 20.058 7.823 26.919 1.00 64.48 C ANISOU 784 CB ARG A 95 6757 6851 10891 -124 -860 -414 C ATOM 785 CG ARG A 95 20.581 8.055 25.503 1.00 66.97 C ANISOU 785 CG ARG A 95 7005 7087 11353 -214 -825 -322 C ATOM 786 CD ARG A 95 22.067 7.756 25.363 1.00 72.03 C ANISOU 786 CD ARG A 95 7412 7982 11974 -295 -878 -217 C ATOM 787 NE ARG A 95 22.720 8.882 24.691 1.00 77.36 N ANISOU 787 NE ARG A 95 8063 8605 12724 -562 -930 -239 N ATOM 788 CZ ARG A 95 24.034 9.041 24.553 1.00 80.38 C ANISOU 788 CZ ARG A 95 8221 9237 13084 -739 -989 -189 C ATOM 789 NH1 ARG A 95 24.882 8.137 25.029 1.00 82.69 N ANISOU 789 NH1 ARG A 95 8268 9870 13279 -615 -1020 -118 N ATOM 790 NH2 ARG A 95 24.501 10.114 23.928 1.00 83.36 N ANISOU 790 NH2 ARG A 95 8621 9534 13519 -1040 -1019 -204 N ATOM 791 N GLU A 96 17.775 10.216 25.842 1.00 59.10 N ANISOU 791 N GLU A 96 6511 5564 10379 -123 -835 -702 N ATOM 792 CA GLU A 96 16.832 10.443 24.747 1.00 55.63 C ANISOU 792 CA GLU A 96 6161 4941 10036 -16 -763 -694 C ATOM 793 C GLU A 96 17.384 9.924 23.415 1.00 52.05 C ANISOU 793 C GLU A 96 5605 4484 9689 -69 -700 -510 C ATOM 794 O GLU A 96 18.310 10.509 22.855 1.00 53.80 O ANISOU 794 O GLU A 96 5832 4646 9965 -245 -749 -450 O ATOM 795 CB GLU A 96 16.528 11.929 24.602 1.00 57.64 C ANISOU 795 CB GLU A 96 6657 4927 10317 -41 -854 -830 C ATOM 796 CG GLU A 96 15.346 12.205 23.678 1.00 59.14 C ANISOU 796 CG GLU A 96 6949 4961 10560 156 -802 -849 C ATOM 797 CD GLU A 96 15.490 13.495 22.909 1.00 62.40 C ANISOU 797 CD GLU A 96 7616 5056 11036 96 -885 -859 C ATOM 798 OE1 GLU A 96 16.644 13.975 22.777 1.00 64.77 O ANISOU 798 OE1 GLU A 96 7970 5273 11367 -173 -949 -796 O ATOM 799 OE2 GLU A 96 14.456 14.016 22.427 1.00 62.70 O ANISOU 799 OE2 GLU A 96 7801 4944 11078 314 -887 -922 O ATOM 800 N HIS A 97 16.816 8.842 22.900 1.00 46.43 N ANISOU 800 N HIS A 97 4807 3842 8991 62 -586 -429 N ATOM 801 CA HIS A 97 17.264 8.294 21.623 1.00 42.13 C ANISOU 801 CA HIS A 97 4184 3298 8523 44 -518 -280 C ATOM 802 C HIS A 97 16.395 8.858 20.525 1.00 38.60 C ANISOU 802 C HIS A 97 3849 2679 8138 105 -496 -296 C ATOM 803 O HIS A 97 15.214 8.785 20.619 1.00 37.50 O ANISOU 803 O HIS A 97 3749 2525 7974 240 -468 -381 O ATOM 804 CB HIS A 97 17.135 6.779 21.648 1.00 41.55 C ANISOU 804 CB HIS A 97 4011 3360 8414 150 -418 -197 C ATOM 805 CG HIS A 97 17.924 6.144 22.740 1.00 45.75 C ANISOU 805 CG HIS A 97 4464 4059 8860 150 -448 -161 C ATOM 806 ND1 HIS A 97 19.154 5.563 22.521 1.00 48.96 N ANISOU 806 ND1 HIS A 97 4742 4600 9262 149 -452 -42 N ATOM 807 CD2 HIS A 97 17.674 6.020 24.064 1.00 49.02 C ANISOU 807 CD2 HIS A 97 4904 4556 9164 175 -481 -227 C ATOM 808 CE1 HIS A 97 19.619 5.084 23.663 1.00 52.33 C ANISOU 808 CE1 HIS A 97 5125 5177 9582 193 -501 -30 C ATOM 809 NE2 HIS A 97 18.739 5.348 24.615 1.00 51.92 N ANISOU 809 NE2 HIS A 97 5178 5089 9462 194 -518 -134 N ATOM 810 N VAL A 98 17.001 9.417 19.491 1.00 35.42 N ANISOU 810 N VAL A 98 3484 2180 7793 2 -509 -209 N ATOM 811 CA VAL A 98 16.279 10.028 18.401 1.00 32.25 C ANISOU 811 CA VAL A 98 3218 1610 7426 69 -506 -199 C ATOM 812 C VAL A 98 16.441 9.178 17.145 1.00 28.97 C ANISOU 812 C VAL A 98 2703 1272 7030 91 -409 -70 C ATOM 813 O VAL A 98 17.542 8.639 16.867 1.00 27.88 O ANISOU 813 O VAL A 98 2437 1260 6898 -8 -362 36 O ATOM 814 CB VAL A 98 16.807 11.479 18.131 1.00 34.21 C ANISOU 814 CB VAL A 98 3669 1634 7695 -89 -599 -187 C ATOM 815 CG1 VAL A 98 15.982 12.160 17.062 1.00 33.45 C ANISOU 815 CG1 VAL A 98 3767 1336 7607 31 -614 -166 C ATOM 816 CG2 VAL A 98 16.781 12.320 19.411 1.00 36.43 C ANISOU 816 CG2 VAL A 98 4081 1817 7943 -130 -705 -341 C ATOM 817 N ALA A 99 15.364 9.029 16.389 1.00 25.50 N ANISOU 817 N ALA A 99 2309 796 6584 236 -380 -91 N ATOM 818 CA ALA A 99 15.476 8.282 15.119 1.00 24.95 C ANISOU 818 CA ALA A 99 2177 792 6513 253 -297 11 C ATOM 819 C ALA A 99 14.682 8.946 14.032 1.00 24.61 C ANISOU 819 C ALA A 99 2260 640 6452 343 -328 20 C ATOM 820 O ALA A 99 13.625 9.494 14.298 1.00 25.30 O ANISOU 820 O ALA A 99 2425 668 6521 480 -392 -83 O ATOM 821 CB ALA A 99 15.037 6.771 15.274 1.00 22.70 C ANISOU 821 CB ALA A 99 1771 653 6202 330 -208 -18 C ATOM 822 N HIS A 100 15.155 8.862 12.801 1.00 24.75 N ANISOU 822 N HIS A 100 2287 664 6452 297 -283 139 N ATOM 823 CA HIS A 100 14.391 9.414 11.670 1.00 25.97 C ANISOU 823 CA HIS A 100 2572 738 6559 404 -320 167 C ATOM 824 C HIS A 100 13.381 8.389 11.194 1.00 24.87 C ANISOU 824 C HIS A 100 2325 750 6376 541 -280 94 C ATOM 825 O HIS A 100 13.751 7.238 10.972 1.00 23.68 O ANISOU 825 O HIS A 100 2060 721 6218 495 -187 109 O ATOM 826 CB HIS A 100 15.346 9.779 10.541 1.00 26.88 C ANISOU 826 CB HIS A 100 2754 819 6641 270 -280 335 C ATOM 827 CG HIS A 100 16.022 11.091 10.759 1.00 29.65 C ANISOU 827 CG HIS A 100 3287 973 7008 105 -343 409 C ATOM 828 ND1 HIS A 100 17.170 11.223 11.514 1.00 28.84 N ANISOU 828 ND1 HIS A 100 3107 902 6947 -117 -329 432 N ATOM 829 CD2 HIS A 100 15.670 12.345 10.384 1.00 30.42 C ANISOU 829 CD2 HIS A 100 3666 821 7072 124 -434 455 C ATOM 830 CE1 HIS A 100 17.512 12.495 11.562 1.00 30.97 C ANISOU 830 CE1 HIS A 100 3603 951 7213 -279 -401 482 C ATOM 831 NE2 HIS A 100 16.618 13.195 10.892 1.00 31.90 N ANISOU 831 NE2 HIS A 100 3969 864 7287 -128 -464 504 N ATOM 832 N LEU A 101 12.122 8.806 11.030 1.00 25.26 N ANISOU 832 N LEU A 101 2416 801 6382 712 -355 6 N ATOM 833 CA LEU A 101 11.086 7.935 10.487 1.00 24.69 C ANISOU 833 CA LEU A 101 2225 912 6246 803 -334 -76 C ATOM 834 C LEU A 101 11.270 7.907 8.974 1.00 25.79 C ANISOU 834 C LEU A 101 2426 1062 6312 813 -326 27 C ATOM 835 O LEU A 101 11.206 8.948 8.336 1.00 26.61 O ANISOU 835 O LEU A 101 2685 1055 6371 897 -403 106 O ATOM 836 CB LEU A 101 9.682 8.397 10.870 1.00 25.62 C ANISOU 836 CB LEU A 101 2301 1114 6318 994 -421 -219 C ATOM 837 CG LEU A 101 8.495 7.643 10.260 1.00 26.58 C ANISOU 837 CG LEU A 101 2264 1485 6350 1062 -422 -321 C ATOM 838 CD1 LEU A 101 8.619 6.071 10.437 1.00 24.65 C ANISOU 838 CD1 LEU A 101 1890 1362 6113 858 -299 -359 C ATOM 839 CD2 LEU A 101 7.240 8.125 10.884 1.00 31.62 C ANISOU 839 CD2 LEU A 101 2801 2274 6941 1248 -495 -474 C ATOM 840 N LEU A 102 11.529 6.716 8.409 1.00 24.48 N ANISOU 840 N LEU A 102 2174 1013 6116 735 -232 29 N ATOM 841 CA LEU A 102 11.764 6.630 6.968 1.00 25.18 C ANISOU 841 CA LEU A 102 2320 1139 6109 745 -212 114 C ATOM 842 C LEU A 102 10.873 5.584 6.324 1.00 25.85 C ANISOU 842 C LEU A 102 2320 1397 6105 774 -200 -3 C ATOM 843 O LEU A 102 10.488 4.611 6.952 1.00 25.42 O ANISOU 843 O LEU A 102 2171 1409 6078 710 -157 -118 O ATOM 844 CB LEU A 102 13.239 6.291 6.676 1.00 24.96 C ANISOU 844 CB LEU A 102 2298 1089 6096 617 -99 236 C ATOM 845 CG LEU A 102 14.303 7.217 7.271 1.00 25.34 C ANISOU 845 CG LEU A 102 2395 1016 6217 507 -99 350 C ATOM 846 CD1 LEU A 102 15.706 6.633 7.064 1.00 25.57 C ANISOU 846 CD1 LEU A 102 2333 1139 6244 393 24 436 C ATOM 847 CD2 LEU A 102 14.180 8.603 6.681 1.00 27.37 C ANISOU 847 CD2 LEU A 102 2842 1133 6425 520 -183 458 C ATOM 848 N PHE A 103 10.621 5.750 5.037 1.00 28.37 N ANISOU 848 N PHE A 103 2695 1785 6300 840 -235 34 N ATOM 849 CA PHE A 103 9.721 4.859 4.311 1.00 30.60 C ANISOU 849 CA PHE A 103 2904 2253 6471 850 -249 -94 C ATOM 850 C PHE A 103 10.354 4.167 3.117 1.00 32.14 C ANISOU 850 C PHE A 103 3163 2491 6559 803 -169 -57 C ATOM 851 O PHE A 103 11.319 4.659 2.537 1.00 33.15 O ANISOU 851 O PHE A 103 3384 2556 6654 808 -123 95 O ATOM 852 CB PHE A 103 8.448 5.600 3.901 1.00 31.54 C ANISOU 852 CB PHE A 103 2987 2507 6489 1020 -402 -148 C ATOM 853 CG PHE A 103 7.629 6.029 5.070 1.00 34.44 C ANISOU 853 CG PHE A 103 3248 2907 6930 1094 -467 -246 C ATOM 854 CD1 PHE A 103 6.962 5.080 5.848 1.00 33.03 C ANISOU 854 CD1 PHE A 103 2895 2875 6779 976 -424 -408 C ATOM 855 CD2 PHE A 103 7.560 7.372 5.427 1.00 35.91 C ANISOU 855 CD2 PHE A 103 3535 2964 7143 1272 -559 -177 C ATOM 856 CE1 PHE A 103 6.235 5.445 6.944 1.00 34.10 C ANISOU 856 CE1 PHE A 103 2911 3088 6958 1038 -460 -501 C ATOM 857 CE2 PHE A 103 6.819 7.759 6.525 1.00 37.95 C ANISOU 857 CE2 PHE A 103 3698 3271 7450 1374 -609 -291 C ATOM 858 CZ PHE A 103 6.141 6.812 7.278 1.00 37.38 C ANISOU 858 CZ PHE A 103 3404 3406 7394 1264 -556 -454 C ATOM 859 N LEU A 104 9.804 3.003 2.778 1.00 33.75 N ANISOU 859 N LEU A 104 3321 2809 6692 739 -147 -208 N ATOM 860 CA LEU A 104 10.189 2.246 1.603 1.00 36.20 C ANISOU 860 CA LEU A 104 3708 3178 6868 717 -84 -229 C ATOM 861 C LEU A 104 9.017 2.286 0.619 1.00 39.16 C ANISOU 861 C LEU A 104 4052 3759 7070 762 -205 -330 C ATOM 862 O LEU A 104 7.960 2.838 0.952 1.00 40.05 O ANISOU 862 O LEU A 104 4056 3980 7181 821 -329 -382 O ATOM 863 CB LEU A 104 10.519 0.812 2.043 1.00 36.19 C ANISOU 863 CB LEU A 104 3737 3102 6911 602 29 -343 C ATOM 864 CG LEU A 104 11.654 0.878 3.079 1.00 35.33 C ANISOU 864 CG LEU A 104 3630 2836 6956 605 120 -233 C ATOM 865 CD1 LEU A 104 11.871 -0.441 3.774 1.00 40.99 C ANISOU 865 CD1 LEU A 104 4404 3446 7723 536 205 -325 C ATOM 866 CD2 LEU A 104 12.947 1.326 2.416 1.00 35.37 C ANISOU 866 CD2 LEU A 104 3671 2846 6924 674 198 -80 C ATOM 867 N ARG A 105 9.181 1.755 -0.590 1.00 41.16 N ANISOU 867 N ARG A 105 4383 4100 7154 760 -180 -366 N ATOM 868 CA ARG A 105 8.090 1.822 -1.563 1.00 45.01 C ANISOU 868 CA ARG A 105 4831 4822 7448 804 -316 -463 C ATOM 869 C ARG A 105 6.872 1.102 -1.024 1.00 45.55 C ANISOU 869 C ARG A 105 4750 5029 7530 671 -384 -681 C ATOM 870 O ARG A 105 5.742 1.554 -1.179 1.00 46.74 O ANISOU 870 O ARG A 105 4754 5412 7595 734 -532 -750 O ATOM 871 CB ARG A 105 8.492 1.238 -2.921 1.00 47.52 C ANISOU 871 CB ARG A 105 5271 5224 7561 802 -269 -496 C ATOM 872 CG ARG A 105 9.077 2.259 -3.894 1.00 53.55 C ANISOU 872 CG ARG A 105 6138 6021 8187 951 -278 -286 C ATOM 873 CD ARG A 105 10.602 2.096 -4.005 1.00 60.68 C ANISOU 873 CD ARG A 105 7140 6793 9123 928 -85 -159 C ATOM 874 NE ARG A 105 11.335 3.360 -4.197 1.00 66.10 N ANISOU 874 NE ARG A 105 7894 7422 9800 987 -63 103 N ATOM 875 CZ ARG A 105 11.722 4.177 -3.210 1.00 67.59 C ANISOU 875 CZ ARG A 105 8065 7440 10177 966 -59 238 C ATOM 876 NH1 ARG A 105 11.429 3.896 -1.940 1.00 66.86 N ANISOU 876 NH1 ARG A 105 7871 7242 10292 921 -77 139 N ATOM 877 NH2 ARG A 105 12.407 5.288 -3.488 1.00 69.73 N ANISOU 877 NH2 ARG A 105 8441 7642 10413 964 -37 471 N ATOM 878 N ASP A 106 7.113 -0.024 -0.369 1.00 45.28 N ANISOU 878 N ASP A 106 4753 4863 7587 485 -273 -785 N ATOM 879 CA ASP A 106 6.039 -0.797 0.217 1.00 45.97 C ANISOU 879 CA ASP A 106 4725 5059 7681 279 -306 -977 C ATOM 880 C ASP A 106 5.423 -0.082 1.421 1.00 44.96 C ANISOU 880 C ASP A 106 4408 4994 7681 310 -354 -951 C ATOM 881 O ASP A 106 6.106 0.284 2.377 1.00 43.90 O ANISOU 881 O ASP A 106 4309 4663 7709 361 -284 -832 O ATOM 882 CB ASP A 106 6.509 -2.217 0.577 1.00 46.35 C ANISOU 882 CB ASP A 106 4949 4888 7774 70 -170 -1073 C ATOM 883 CG ASP A 106 5.349 -3.137 0.897 1.00 48.70 C ANISOU 883 CG ASP A 106 5181 5304 8020 -226 -202 -1282 C ATOM 884 OD1 ASP A 106 4.465 -2.696 1.649 1.00 48.56 O ANISOU 884 OD1 ASP A 106 4937 5469 8045 -279 -262 -1307 O ATOM 885 OD2 ASP A 106 5.305 -4.278 0.392 1.00 51.44 O ANISOU 885 OD2 ASP A 106 5704 5572 8268 -414 -164 -1429 O ATOM 886 N THR A 107 4.111 0.096 1.357 1.00 45.84 N ANISOU 886 N THR A 107 4301 5420 7697 285 -479 -1082 N ATOM 887 CA THR A 107 3.365 0.787 2.393 1.00 45.06 C ANISOU 887 CA THR A 107 3987 5461 7671 355 -531 -1095 C ATOM 888 C THR A 107 3.218 0.009 3.712 1.00 43.19 C ANISOU 888 C THR A 107 3704 5155 7549 104 -417 -1164 C ATOM 889 O THR A 107 2.858 0.589 4.737 1.00 43.07 O ANISOU 889 O THR A 107 3547 5208 7611 174 -422 -1153 O ATOM 890 CB THR A 107 1.974 1.199 1.873 1.00 48.00 C ANISOU 890 CB THR A 107 4091 6274 7874 443 -703 -1228 C ATOM 891 OG1 THR A 107 1.204 1.711 2.963 1.00 51.71 O ANISOU 891 OG1 THR A 107 4326 6922 8399 509 -730 -1277 O ATOM 892 CG2 THR A 107 1.245 0.017 1.277 1.00 49.21 C ANISOU 892 CG2 THR A 107 4160 6661 7876 136 -720 -1435 C ATOM 893 N LYS A 108 3.520 -1.286 3.680 1.00 41.78 N ANISOU 893 N LYS A 108 3683 4824 7366 -170 -312 -1231 N ATOM 894 CA LYS A 108 3.329 -2.194 4.822 1.00 40.73 C ANISOU 894 CA LYS A 108 3569 4606 7300 -452 -202 -1288 C ATOM 895 C LYS A 108 4.619 -2.313 5.630 1.00 37.28 C ANISOU 895 C LYS A 108 3354 3790 7022 -382 -81 -1126 C ATOM 896 O LYS A 108 4.738 -3.182 6.498 1.00 37.04 O ANISOU 896 O LYS A 108 3436 3602 7035 -584 20 -1134 O ATOM 897 CB LYS A 108 2.929 -3.591 4.332 1.00 42.43 C ANISOU 897 CB LYS A 108 3907 4813 7401 -802 -166 -1451 C ATOM 898 CG LYS A 108 1.494 -3.738 3.863 1.00 48.40 C ANISOU 898 CG LYS A 108 4394 6005 7990 -1007 -273 -1651 C ATOM 899 CD LYS A 108 1.285 -5.149 3.255 1.00 53.60 C ANISOU 899 CD LYS A 108 5260 6578 8528 -1389 -239 -1816 C ATOM 900 CE LYS A 108 -0.182 -5.561 3.253 1.00 58.74 C ANISOU 900 CE LYS A 108 5630 7661 9028 -1758 -305 -2029 C ATOM 901 NZ LYS A 108 -0.669 -5.964 4.610 1.00 61.02 N ANISOU 901 NZ LYS A 108 5833 7981 9372 -2055 -196 -2033 N ATOM 902 N THR A 109 5.584 -1.450 5.330 1.00 34.10 N ANISOU 902 N THR A 109 3016 3255 6684 -108 -95 -975 N ATOM 903 CA THR A 109 6.854 -1.436 6.047 1.00 31.07 C ANISOU 903 CA THR A 109 2784 2587 6436 -25 0 -825 C ATOM 904 C THR A 109 7.228 -0.016 6.462 1.00 30.12 C ANISOU 904 C THR A 109 2574 2466 6404 198 -54 -696 C ATOM 905 O THR A 109 6.649 0.973 5.957 1.00 30.99 O ANISOU 905 O THR A 109 2574 2739 6463 341 -164 -699 O ATOM 906 CB THR A 109 7.993 -2.000 5.195 1.00 30.00 C ANISOU 906 CB THR A 109 2863 2260 6277 38 68 -771 C ATOM 907 OG1 THR A 109 8.139 -1.209 4.009 1.00 28.51 O ANISOU 907 OG1 THR A 109 2643 2178 6009 199 1 -726 O ATOM 908 CG2 THR A 109 7.714 -3.457 4.792 1.00 31.73 C ANISOU 908 CG2 THR A 109 3254 2400 6400 -167 121 -915 C ATOM 909 N LEU A 110 8.164 0.073 7.407 1.00 27.66 N ANISOU 909 N LEU A 110 2331 1969 6210 228 12 -588 N ATOM 910 CA LEU A 110 8.817 1.324 7.734 1.00 27.05 C ANISOU 910 CA LEU A 110 2236 1827 6215 393 -27 -461 C ATOM 911 C LEU A 110 10.182 1.080 8.318 1.00 24.81 C ANISOU 911 C LEU A 110 2049 1356 6021 396 57 -346 C ATOM 912 O LEU A 110 10.515 -0.054 8.728 1.00 25.24 O ANISOU 912 O LEU A 110 2185 1324 6081 311 141 -364 O ATOM 913 CB LEU A 110 7.937 2.209 8.663 1.00 28.00 C ANISOU 913 CB LEU A 110 2218 2059 6363 450 -101 -511 C ATOM 914 CG LEU A 110 7.640 1.643 10.060 1.00 29.87 C ANISOU 914 CG LEU A 110 2402 2308 6637 320 -38 -568 C ATOM 915 CD1 LEU A 110 8.711 2.038 11.013 1.00 29.94 C ANISOU 915 CD1 LEU A 110 2484 2144 6748 366 -10 -459 C ATOM 916 CD2 LEU A 110 6.340 2.152 10.593 1.00 31.98 C ANISOU 916 CD2 LEU A 110 2479 2815 6856 352 -96 -689 C ATOM 917 N MET A 111 11.009 2.121 8.309 1.00 24.06 N ANISOU 917 N MET A 111 1961 1201 5979 493 31 -225 N ATOM 918 CA MET A 111 12.350 2.032 8.890 1.00 23.60 C ANISOU 918 CA MET A 111 1935 1039 5994 493 94 -119 C ATOM 919 C MET A 111 12.530 3.144 9.884 1.00 23.24 C ANISOU 919 C MET A 111 1849 953 6027 505 32 -75 C ATOM 920 O MET A 111 11.921 4.193 9.730 1.00 24.21 O ANISOU 920 O MET A 111 1971 1083 6143 559 -54 -87 O ATOM 921 CB MET A 111 13.431 2.215 7.828 1.00 23.62 C ANISOU 921 CB MET A 111 1972 1042 5961 539 137 -12 C ATOM 922 CG MET A 111 13.486 1.162 6.772 1.00 28.94 C ANISOU 922 CG MET A 111 2711 1750 6537 559 207 -61 C ATOM 923 SD MET A 111 14.942 1.437 5.733 1.00 29.31 S ANISOU 923 SD MET A 111 2753 1858 6524 624 288 73 S ATOM 924 CE MET A 111 14.725 3.098 5.143 1.00 27.02 C ANISOU 924 CE MET A 111 2465 1590 6211 597 201 186 C ATOM 925 N PHE A 112 13.391 2.933 10.873 1.00 21.92 N ANISOU 925 N PHE A 112 1669 742 5918 476 65 -29 N ATOM 926 CA PHE A 112 13.918 4.037 11.673 1.00 22.24 C ANISOU 926 CA PHE A 112 1691 739 6020 463 6 20 C ATOM 927 C PHE A 112 15.425 4.098 11.414 1.00 22.89 C ANISOU 927 C PHE A 112 1746 834 6117 431 48 141 C ATOM 928 O PHE A 112 16.101 3.063 11.355 1.00 23.02 O ANISOU 928 O PHE A 112 1732 901 6113 464 125 165 O ATOM 929 CB PHE A 112 13.557 3.860 13.152 1.00 21.37 C ANISOU 929 CB PHE A 112 1553 634 5933 442 -10 -48 C ATOM 930 CG PHE A 112 12.109 4.196 13.442 1.00 23.08 C ANISOU 930 CG PHE A 112 1748 901 6121 474 -56 -170 C ATOM 931 CD1 PHE A 112 11.708 5.545 13.483 1.00 24.30 C ANISOU 931 CD1 PHE A 112 1929 1019 6287 553 -150 -201 C ATOM 932 CD2 PHE A 112 11.145 3.198 13.601 1.00 21.74 C ANISOU 932 CD2 PHE A 112 1539 823 5897 428 -6 -258 C ATOM 933 CE1 PHE A 112 10.380 5.901 13.722 1.00 25.95 C ANISOU 933 CE1 PHE A 112 2087 1323 6451 647 -197 -327 C ATOM 934 CE2 PHE A 112 9.781 3.553 13.833 1.00 24.01 C ANISOU 934 CE2 PHE A 112 1740 1245 6137 457 -44 -383 C ATOM 935 CZ PHE A 112 9.414 4.895 13.890 1.00 24.46 C ANISOU 935 CZ PHE A 112 1786 1304 6202 597 -139 -421 C ATOM 936 N GLY A 113 15.906 5.301 11.145 1.00 23.91 N ANISOU 936 N GLY A 113 1896 926 6263 371 1 215 N ATOM 937 CA GLY A 113 17.295 5.572 10.924 1.00 23.69 C ANISOU 937 CA GLY A 113 1803 964 6235 282 38 327 C ATOM 938 C GLY A 113 17.881 6.201 12.160 1.00 25.32 C ANISOU 938 C GLY A 113 1968 1156 6494 182 -26 327 C ATOM 939 O GLY A 113 17.317 7.115 12.707 1.00 24.55 O ANISOU 939 O GLY A 113 1968 932 6426 149 -114 277 O ATOM 940 N SER A 114 19.049 5.722 12.578 1.00 25.72 N ANISOU 940 N SER A 114 1873 1359 6540 151 11 372 N ATOM 941 CA SER A 114 19.725 6.224 13.772 1.00 27.90 C ANISOU 941 CA SER A 114 2078 1680 6843 43 -61 363 C ATOM 942 C SER A 114 21.082 6.748 13.355 1.00 29.73 C ANISOU 942 C SER A 114 2173 2072 7050 -130 -39 464 C ATOM 943 O SER A 114 21.697 6.210 12.427 1.00 28.39 O ANISOU 943 O SER A 114 1893 2061 6831 -87 60 534 O ATOM 944 CB SER A 114 19.927 5.065 14.763 1.00 27.62 C ANISOU 944 CB SER A 114 1953 1750 6789 176 -49 328 C ATOM 945 OG SER A 114 18.651 4.585 15.166 1.00 31.27 O ANISOU 945 OG SER A 114 2539 2084 7256 273 -52 242 O ATOM 946 N TYR A 115 21.542 7.798 14.041 1.00 31.95 N ANISOU 946 N TYR A 115 2460 2330 7351 -340 -128 458 N ATOM 947 CA TYR A 115 22.837 8.428 13.775 1.00 34.91 C ANISOU 947 CA TYR A 115 2690 2883 7692 -596 -118 545 C ATOM 948 C TYR A 115 23.117 8.639 12.298 1.00 35.70 C ANISOU 948 C TYR A 115 2798 3024 7744 -676 -13 664 C ATOM 949 O TYR A 115 24.279 8.545 11.842 1.00 37.99 O ANISOU 949 O TYR A 115 2861 3603 7969 -801 65 746 O ATOM 950 CB TYR A 115 23.983 7.619 14.402 1.00 36.43 C ANISOU 950 CB TYR A 115 2574 3427 7841 -547 -104 550 C ATOM 951 CG TYR A 115 23.783 7.322 15.852 1.00 37.74 C ANISOU 951 CG TYR A 115 2734 3587 8019 -455 -206 453 C ATOM 952 CD1 TYR A 115 23.672 6.009 16.295 1.00 35.52 C ANISOU 952 CD1 TYR A 115 2389 3396 7711 -166 -177 436 C ATOM 953 CD2 TYR A 115 23.700 8.356 16.790 1.00 43.03 C ANISOU 953 CD2 TYR A 115 3501 4141 8708 -660 -331 379 C ATOM 954 CE1 TYR A 115 23.492 5.726 17.621 1.00 39.09 C ANISOU 954 CE1 TYR A 115 2856 3851 8144 -89 -263 371 C ATOM 955 CE2 TYR A 115 23.502 8.078 18.138 1.00 45.72 C ANISOU 955 CE2 TYR A 115 3840 4503 9030 -569 -420 287 C ATOM 956 CZ TYR A 115 23.399 6.756 18.542 1.00 43.11 C ANISOU 956 CZ TYR A 115 3428 4290 8663 -287 -382 295 C ATOM 957 OH TYR A 115 23.202 6.460 19.872 1.00 46.90 O ANISOU 957 OH TYR A 115 3927 4798 9096 -203 -463 227 O ATOM 958 N LEU A 116 22.058 8.954 11.565 1.00 34.59 N ANISOU 958 N LEU A 116 2900 2631 7611 -602 -12 671 N ATOM 959 CA LEU A 116 22.114 9.077 10.119 1.00 36.33 C ANISOU 959 CA LEU A 116 3173 2873 7759 -632 82 783 C ATOM 960 C LEU A 116 23.052 10.140 9.592 1.00 40.28 C ANISOU 960 C LEU A 116 3684 3420 8201 -976 109 918 C ATOM 961 O LEU A 116 23.430 10.091 8.420 1.00 42.21 O ANISOU 961 O LEU A 116 3893 3794 8349 -1029 221 1031 O ATOM 962 CB LEU A 116 20.731 9.407 9.578 1.00 35.77 C ANISOU 962 CB LEU A 116 3379 2519 7692 -490 34 760 C ATOM 963 CG LEU A 116 19.792 8.329 9.138 1.00 32.38 C ANISOU 963 CG LEU A 116 2947 2107 7248 -210 71 686 C ATOM 964 CD1 LEU A 116 18.719 9.014 8.262 1.00 33.82 C ANISOU 964 CD1 LEU A 116 3372 2090 7386 -144 19 712 C ATOM 965 CD2 LEU A 116 20.516 7.153 8.393 1.00 33.71 C ANISOU 965 CD2 LEU A 116 2923 2541 7343 -121 211 716 C ATOM 966 N ASP A 117 23.415 11.099 10.442 1.00 41.45 N ANISOU 966 N ASP A 117 3896 3464 8388 -1235 12 903 N ATOM 967 CA ASP A 117 24.330 12.153 10.050 1.00 45.92 C ANISOU 967 CA ASP A 117 4498 4055 8893 -1646 32 1028 C ATOM 968 C ASP A 117 25.792 11.728 10.248 1.00 47.06 C ANISOU 968 C ASP A 117 4223 4676 8982 -1833 110 1055 C ATOM 969 O ASP A 117 26.685 12.480 9.925 1.00 50.09 O ANISOU 969 O ASP A 117 4555 5183 9296 -2224 149 1157 O ATOM 970 CB ASP A 117 24.010 13.481 10.805 1.00 48.03 C ANISOU 970 CB ASP A 117 5098 3942 9211 -1872 -119 985 C ATOM 971 CG ASP A 117 24.233 13.386 12.340 1.00 50.08 C ANISOU 971 CG ASP A 117 5229 4261 9537 -1890 -232 823 C ATOM 972 OD1 ASP A 117 24.103 12.290 12.923 1.00 54.51 O ANISOU 972 OD1 ASP A 117 5558 5023 10129 -1610 -224 732 O ATOM 973 OD2 ASP A 117 24.518 14.419 12.983 1.00 56.06 O ANISOU 973 OD2 ASP A 117 6154 4844 10302 -2189 -335 784 O ATOM 974 N ASP A 118 26.026 10.506 10.740 1.00 44.74 N ANISOU 974 N ASP A 118 3635 4663 8703 -1547 135 970 N ATOM 975 CA ASP A 118 27.369 10.088 11.188 1.00 45.48 C ANISOU 975 CA ASP A 118 3307 5234 8740 -1644 167 965 C ATOM 976 C ASP A 118 27.806 8.748 10.583 1.00 44.50 C ANISOU 976 C ASP A 118 2896 5468 8543 -1308 305 976 C ATOM 977 O ASP A 118 27.379 7.671 11.021 1.00 42.45 O ANISOU 977 O ASP A 118 2623 5188 8320 -928 287 890 O ATOM 978 CB ASP A 118 27.387 10.031 12.726 1.00 45.00 C ANISOU 978 CB ASP A 118 3191 5164 8744 -1612 13 835 C ATOM 979 CG ASP A 118 28.720 9.559 13.299 1.00 47.86 C ANISOU 979 CG ASP A 118 3101 6051 9032 -1654 11 818 C ATOM 980 OD1 ASP A 118 28.846 9.513 14.540 1.00 48.12 O ANISOU 980 OD1 ASP A 118 3066 6131 9085 -1637 -122 721 O ATOM 981 OD2 ASP A 118 29.636 9.208 12.534 1.00 48.87 O ANISOU 981 OD2 ASP A 118 2926 6581 9063 -1676 137 894 O ATOM 982 N GLU A 119 28.668 8.814 9.584 1.00 46.48 N ANISOU 982 N GLU A 119 2941 6045 8674 -1451 447 1078 N ATOM 983 CA GLU A 119 29.139 7.618 8.894 1.00 46.75 C ANISOU 983 CA GLU A 119 2721 6431 8611 -1117 592 1075 C ATOM 984 C GLU A 119 29.851 6.581 9.784 1.00 46.29 C ANISOU 984 C GLU A 119 2331 6719 8538 -816 560 984 C ATOM 985 O GLU A 119 30.001 5.427 9.377 1.00 46.67 O ANISOU 985 O GLU A 119 2273 6936 8523 -421 651 949 O ATOM 986 CB GLU A 119 30.021 8.003 7.696 1.00 50.00 C ANISOU 986 CB GLU A 119 2938 7195 8865 -1362 764 1201 C ATOM 987 CG GLU A 119 31.456 8.309 8.008 1.00 55.38 C ANISOU 987 CG GLU A 119 3168 8422 9451 -1646 798 1231 C ATOM 988 CD GLU A 119 32.168 8.902 6.812 1.00 62.98 C ANISOU 988 CD GLU A 119 3996 9685 10247 -1993 978 1375 C ATOM 989 OE1 GLU A 119 33.402 9.117 6.889 1.00 67.40 O ANISOU 989 OE1 GLU A 119 4125 10791 10694 -2258 1042 1405 O ATOM 990 OE2 GLU A 119 31.486 9.164 5.793 1.00 64.03 O ANISOU 990 OE2 GLU A 119 4446 9538 10346 -2014 1054 1463 O ATOM 991 N LYS A 120 30.269 6.980 10.984 1.00 45.51 N ANISOU 991 N LYS A 120 2103 6708 8480 -980 422 942 N ATOM 992 CA LYS A 120 30.871 6.040 11.928 1.00 45.77 C ANISOU 992 CA LYS A 120 1860 7047 8484 -668 359 866 C ATOM 993 C LYS A 120 29.822 5.302 12.760 1.00 42.75 C ANISOU 993 C LYS A 120 1769 6275 8199 -329 258 785 C ATOM 994 O LYS A 120 30.134 4.296 13.403 1.00 42.95 O ANISOU 994 O LYS A 120 1668 6464 8186 23 222 742 O ATOM 995 CB LYS A 120 31.843 6.760 12.858 1.00 49.19 C ANISOU 995 CB LYS A 120 1993 7815 8882 -1002 245 851 C ATOM 996 CG LYS A 120 33.056 7.315 12.131 1.00 52.38 C ANISOU 996 CG LYS A 120 2013 8734 9156 -1349 356 926 C ATOM 997 CD LYS A 120 34.076 6.204 11.900 1.00 57.02 C ANISOU 997 CD LYS A 120 2136 9927 9601 -956 449 910 C ATOM 998 CE LYS A 120 35.166 6.588 10.890 1.00 61.63 C ANISOU 998 CE LYS A 120 2321 11069 10024 -1235 622 988 C ATOM 999 NZ LYS A 120 35.683 7.958 11.052 1.00 64.47 N ANISOU 999 NZ LYS A 120 2578 11553 10365 -1933 582 1040 N ATOM 1000 N ASN A 121 28.591 5.810 12.741 1.00 39.27 N ANISOU 1000 N ASN A 121 1717 5339 7865 -433 215 770 N ATOM 1001 CA ASN A 121 27.590 5.370 13.683 1.00 36.94 C ANISOU 1001 CA ASN A 121 1669 4714 7651 -232 114 691 C ATOM 1002 C ASN A 121 26.229 4.966 13.114 1.00 33.84 C ANISOU 1002 C ASN A 121 1617 3922 7318 -61 161 667 C ATOM 1003 O ASN A 121 25.462 4.293 13.803 1.00 32.37 O ANISOU 1003 O ASN A 121 1590 3539 7170 144 113 605 O ATOM 1004 CB ASN A 121 27.454 6.389 14.816 1.00 36.81 C ANISOU 1004 CB ASN A 121 1723 4575 7688 -516 -41 642 C ATOM 1005 CG ASN A 121 28.582 6.255 15.815 1.00 39.78 C ANISOU 1005 CG ASN A 121 1774 5350 7992 -537 -132 618 C ATOM 1006 OD1 ASN A 121 28.649 5.266 16.540 1.00 38.76 O ANISOU 1006 OD1 ASN A 121 1585 5317 7827 -212 -172 590 O ATOM 1007 ND2 ASN A 121 29.502 7.219 15.824 1.00 41.93 N ANISOU 1007 ND2 ASN A 121 1835 5874 8223 -924 -165 637 N ATOM 1008 N TRP A 122 25.973 5.321 11.853 1.00 33.83 N ANISOU 1008 N TRP A 122 1708 3845 7301 -151 256 720 N ATOM 1009 CA TRP A 122 24.640 5.229 11.275 1.00 31.60 C ANISOU 1009 CA TRP A 122 1732 3211 7063 -63 271 693 C ATOM 1010 C TRP A 122 24.124 3.796 11.140 1.00 30.76 C ANISOU 1010 C TRP A 122 1704 3044 6940 285 325 630 C ATOM 1011 O TRP A 122 24.893 2.851 11.114 1.00 31.38 O ANISOU 1011 O TRP A 122 1629 3343 6952 500 385 628 O ATOM 1012 CB TRP A 122 24.539 5.984 9.937 1.00 32.70 C ANISOU 1012 CB TRP A 122 1959 3308 7157 -237 346 778 C ATOM 1013 CG TRP A 122 25.463 5.571 8.781 1.00 34.30 C ANISOU 1013 CG TRP A 122 1965 3835 7233 -197 501 849 C ATOM 1014 CD1 TRP A 122 25.904 4.329 8.475 1.00 35.83 C ANISOU 1014 CD1 TRP A 122 2017 4243 7354 107 596 808 C ATOM 1015 CD2 TRP A 122 25.951 6.433 7.740 1.00 37.02 C ANISOU 1015 CD2 TRP A 122 2281 4298 7488 -460 585 969 C ATOM 1016 NE1 TRP A 122 26.676 4.361 7.332 1.00 36.89 N ANISOU 1016 NE1 TRP A 122 1991 4669 7356 69 739 877 N ATOM 1017 CE2 TRP A 122 26.703 5.641 6.855 1.00 37.89 C ANISOU 1017 CE2 TRP A 122 2180 4751 7466 -298 741 987 C ATOM 1018 CE3 TRP A 122 25.811 7.805 7.470 1.00 37.40 C ANISOU 1018 CE3 TRP A 122 2498 4174 7540 -813 546 1068 C ATOM 1019 CZ2 TRP A 122 27.345 6.168 5.733 1.00 42.13 C ANISOU 1019 CZ2 TRP A 122 2622 5522 7865 -502 873 1104 C ATOM 1020 CZ3 TRP A 122 26.455 8.335 6.350 1.00 42.45 C ANISOU 1020 CZ3 TRP A 122 3084 5000 8046 -1039 670 1206 C ATOM 1021 CH2 TRP A 122 27.212 7.514 5.495 1.00 43.62 C ANISOU 1021 CH2 TRP A 122 2975 5543 8054 -893 838 1224 C ATOM 1022 N GLY A 123 22.812 3.657 11.079 1.00 28.69 N ANISOU 1022 N GLY A 123 1692 2484 6726 337 297 571 N ATOM 1023 CA GLY A 123 22.227 2.335 10.970 1.00 27.63 C ANISOU 1023 CA GLY A 123 1678 2251 6570 589 342 503 C ATOM 1024 C GLY A 123 20.737 2.444 10.803 1.00 25.98 C ANISOU 1024 C GLY A 123 1694 1774 6402 553 306 436 C ATOM 1025 O GLY A 123 20.160 3.545 10.883 1.00 25.14 O ANISOU 1025 O GLY A 123 1650 1561 6343 394 235 440 O ATOM 1026 N LEU A 124 20.098 1.299 10.571 1.00 25.47 N ANISOU 1026 N LEU A 124 1762 1608 6308 704 349 367 N ATOM 1027 CA LEU A 124 18.682 1.274 10.226 1.00 24.00 C ANISOU 1027 CA LEU A 124 1741 1247 6131 661 325 289 C ATOM 1028 C LEU A 124 18.008 0.104 10.871 1.00 23.61 C ANISOU 1028 C LEU A 124 1822 1072 6076 732 333 210 C ATOM 1029 O LEU A 124 18.582 -1.012 10.948 1.00 24.56 O ANISOU 1029 O LEU A 124 1996 1187 6150 882 391 210 O ATOM 1030 CB LEU A 124 18.474 1.146 8.721 1.00 24.48 C ANISOU 1030 CB LEU A 124 1856 1332 6113 688 386 279 C ATOM 1031 CG LEU A 124 18.929 2.276 7.788 1.00 25.58 C ANISOU 1031 CG LEU A 124 1930 1573 6217 591 396 375 C ATOM 1032 CD1 LEU A 124 19.111 1.746 6.349 1.00 26.50 C ANISOU 1032 CD1 LEU A 124 2079 1783 6207 678 493 369 C ATOM 1033 CD2 LEU A 124 17.932 3.465 7.840 1.00 24.66 C ANISOU 1033 CD2 LEU A 124 1899 1329 6144 473 290 379 C ATOM 1034 N SER A 125 16.753 0.295 11.249 1.00 22.72 N ANISOU 1034 N SER A 125 1781 861 5990 635 283 139 N ATOM 1035 CA SER A 125 15.971 -0.851 11.718 1.00 22.81 C ANISOU 1035 CA SER A 125 1935 761 5972 630 309 65 C ATOM 1036 C SER A 125 14.690 -0.934 10.874 1.00 22.67 C ANISOU 1036 C SER A 125 1977 720 5918 540 304 -37 C ATOM 1037 O SER A 125 14.171 0.088 10.403 1.00 22.28 O ANISOU 1037 O SER A 125 1848 737 5880 501 248 -49 O ATOM 1038 CB SER A 125 15.753 -0.791 13.240 1.00 22.45 C ANISOU 1038 CB SER A 125 1882 692 5955 581 267 72 C ATOM 1039 OG SER A 125 15.091 0.397 13.639 1.00 29.91 O ANISOU 1039 OG SER A 125 2736 1684 6944 489 194 38 O ATOM 1040 N PHE A 126 14.191 -2.149 10.677 1.00 23.42 N ANISOU 1040 N PHE A 126 2227 720 5952 508 355 -110 N ATOM 1041 CA PHE A 126 13.222 -2.432 9.638 1.00 23.93 C ANISOU 1041 CA PHE A 126 2343 798 5950 421 354 -219 C ATOM 1042 C PHE A 126 12.032 -3.121 10.318 1.00 24.50 C ANISOU 1042 C PHE A 126 2488 828 5994 233 357 -312 C ATOM 1043 O PHE A 126 12.222 -4.033 11.140 1.00 25.10 O ANISOU 1043 O PHE A 126 2715 762 6058 200 407 -290 O ATOM 1044 CB PHE A 126 13.889 -3.409 8.623 1.00 25.33 C ANISOU 1044 CB PHE A 126 2677 898 6050 527 428 -242 C ATOM 1045 CG PHE A 126 13.013 -3.797 7.444 1.00 27.90 C ANISOU 1045 CG PHE A 126 3080 1243 6278 436 422 -372 C ATOM 1046 CD1 PHE A 126 12.310 -2.833 6.716 1.00 27.47 C ANISOU 1046 CD1 PHE A 126 2881 1358 6200 390 350 -398 C ATOM 1047 CD2 PHE A 126 12.935 -5.136 7.037 1.00 29.45 C ANISOU 1047 CD2 PHE A 126 3523 1281 6388 411 479 -472 C ATOM 1048 CE1 PHE A 126 11.493 -3.212 5.623 1.00 30.60 C ANISOU 1048 CE1 PHE A 126 3330 1817 6480 310 326 -526 C ATOM 1049 CE2 PHE A 126 12.150 -5.524 5.935 1.00 31.22 C ANISOU 1049 CE2 PHE A 126 3825 1535 6502 300 463 -615 C ATOM 1050 CZ PHE A 126 11.429 -4.588 5.232 1.00 32.41 C ANISOU 1050 CZ PHE A 126 3787 1905 6621 246 384 -644 C ATOM 1051 N TYR A 127 10.829 -2.690 9.954 1.00 24.58 N ANISOU 1051 N TYR A 127 2388 977 5973 114 305 -409 N ATOM 1052 CA TYR A 127 9.579 -3.141 10.579 1.00 25.43 C ANISOU 1052 CA TYR A 127 2476 1148 6036 -105 310 -507 C ATOM 1053 C TYR A 127 8.586 -3.426 9.499 1.00 26.66 C ANISOU 1053 C TYR A 127 2604 1426 6099 -234 280 -646 C ATOM 1054 O TYR A 127 8.653 -2.781 8.460 1.00 26.42 O ANISOU 1054 O TYR A 127 2499 1490 6048 -111 222 -652 O ATOM 1055 CB TYR A 127 9.032 -2.064 11.521 1.00 24.70 C ANISOU 1055 CB TYR A 127 2176 1221 5988 -93 257 -503 C ATOM 1056 CG TYR A 127 10.064 -1.631 12.541 1.00 25.55 C ANISOU 1056 CG TYR A 127 2299 1233 6175 31 263 -381 C ATOM 1057 CD1 TYR A 127 11.026 -0.679 12.218 1.00 24.02 C ANISOU 1057 CD1 TYR A 127 2057 1021 6048 203 218 -294 C ATOM 1058 CD2 TYR A 127 10.122 -2.227 13.807 1.00 27.45 C ANISOU 1058 CD2 TYR A 127 2616 1411 6403 -52 315 -346 C ATOM 1059 CE1 TYR A 127 11.966 -0.285 13.137 1.00 25.21 C ANISOU 1059 CE1 TYR A 127 2199 1123 6256 277 210 -202 C ATOM 1060 CE2 TYR A 127 11.088 -1.835 14.737 1.00 26.41 C ANISOU 1060 CE2 TYR A 127 2486 1228 6321 66 301 -243 C ATOM 1061 CZ TYR A 127 11.986 -0.867 14.388 1.00 25.32 C ANISOU 1061 CZ TYR A 127 2266 1101 6254 222 244 -184 C ATOM 1062 OH TYR A 127 12.952 -0.461 15.277 1.00 27.82 O ANISOU 1062 OH TYR A 127 2559 1404 6607 301 217 -100 O ATOM 1063 N ALA A 128 7.679 -4.377 9.745 1.00 28.29 N ANISOU 1063 N ALA A 128 2877 1642 6230 -501 316 -750 N ATOM 1064 CA ALA A 128 6.593 -4.713 8.817 1.00 30.87 C ANISOU 1064 CA ALA A 128 3143 2141 6444 -691 276 -911 C ATOM 1065 C ALA A 128 5.269 -4.990 9.534 1.00 33.64 C ANISOU 1065 C ALA A 128 3347 2707 6729 -996 287 -1016 C ATOM 1066 O ALA A 128 5.257 -5.264 10.737 1.00 34.36 O ANISOU 1066 O ALA A 128 3481 2732 6843 -1103 358 -958 O ATOM 1067 CB ALA A 128 6.974 -5.923 7.970 1.00 31.72 C ANISOU 1067 CB ALA A 128 3554 2018 6479 -777 322 -972 C ATOM 1068 N ASP A 129 4.159 -4.976 8.798 1.00 36.39 N ANISOU 1068 N ASP A 129 3515 3342 6971 -1151 222 -1171 N ATOM 1069 CA ASP A 129 2.867 -5.284 9.414 1.00 40.19 C ANISOU 1069 CA ASP A 129 3802 4107 7362 -1479 242 -1287 C ATOM 1070 C ASP A 129 2.661 -6.798 9.636 1.00 42.83 C ANISOU 1070 C ASP A 129 4424 4231 7617 -1905 344 -1339 C ATOM 1071 O ASP A 129 1.631 -7.217 10.162 1.00 44.62 O ANISOU 1071 O ASP A 129 4525 4678 7750 -2267 386 -1426 O ATOM 1072 CB ASP A 129 1.711 -4.653 8.624 1.00 42.25 C ANISOU 1072 CB ASP A 129 3703 4830 7518 -1476 121 -1441 C ATOM 1073 CG ASP A 129 1.492 -5.302 7.269 1.00 46.61 C ANISOU 1073 CG ASP A 129 4353 5398 7959 -1619 62 -1569 C ATOM 1074 OD1 ASP A 129 2.342 -6.084 6.781 1.00 50.84 O ANISOU 1074 OD1 ASP A 129 5245 5563 8507 -1642 110 -1539 O ATOM 1075 OD2 ASP A 129 0.433 -5.032 6.680 1.00 54.84 O ANISOU 1075 OD2 ASP A 129 5103 6855 8878 -1693 -40 -1716 O ATOM 1076 N LYS A 130 3.660 -7.590 9.237 1.00 42.80 N ANISOU 1076 N LYS A 130 4817 3804 7639 -1851 386 -1284 N ATOM 1077 CA LYS A 130 3.701 -9.032 9.454 1.00 45.51 C ANISOU 1077 CA LYS A 130 5563 3814 7915 -2179 479 -1306 C ATOM 1078 C LYS A 130 5.068 -9.428 10.002 1.00 44.77 C ANISOU 1078 C LYS A 130 5828 3273 7909 -1923 548 -1129 C ATOM 1079 O LYS A 130 6.068 -8.753 9.714 1.00 41.28 O ANISOU 1079 O LYS A 130 5342 2782 7562 -1520 515 -1038 O ATOM 1080 CB LYS A 130 3.420 -9.794 8.143 1.00 47.69 C ANISOU 1080 CB LYS A 130 6018 4025 8078 -2362 437 -1483 C ATOM 1081 CG LYS A 130 2.003 -9.572 7.599 1.00 50.64 C ANISOU 1081 CG LYS A 130 6033 4881 8328 -2667 354 -1679 C ATOM 1082 CD LYS A 130 1.760 -10.232 6.252 1.00 53.36 C ANISOU 1082 CD LYS A 130 6535 5196 8542 -2832 289 -1870 C ATOM 1083 CE LYS A 130 0.269 -10.174 5.912 1.00 57.18 C ANISOU 1083 CE LYS A 130 6649 6201 8877 -3217 207 -2072 C ATOM 1084 NZ LYS A 130 -0.073 -10.952 4.680 1.00 59.01 N ANISOU 1084 NZ LYS A 130 7055 6417 8950 -3474 137 -2288 N ATOM 1085 N PRO A 131 5.128 -10.518 10.792 1.00 47.12 N ANISOU 1085 N PRO A 131 6484 3260 8159 -2158 643 -1073 N ATOM 1086 CA PRO A 131 6.415 -10.975 11.324 1.00 47.11 C ANISOU 1086 CA PRO A 131 6836 2850 8213 -1874 693 -905 C ATOM 1087 C PRO A 131 7.351 -11.522 10.254 1.00 47.89 C ANISOU 1087 C PRO A 131 7238 2651 8306 -1617 680 -945 C ATOM 1088 O PRO A 131 8.534 -11.685 10.501 1.00 46.62 O ANISOU 1088 O PRO A 131 7268 2252 8193 -1269 702 -821 O ATOM 1089 CB PRO A 131 6.014 -12.102 12.296 1.00 50.01 C ANISOU 1089 CB PRO A 131 7562 2956 8485 -2242 788 -850 C ATOM 1090 CG PRO A 131 4.656 -12.515 11.878 1.00 52.96 C ANISOU 1090 CG PRO A 131 7867 3514 8741 -2764 795 -1031 C ATOM 1091 CD PRO A 131 4.005 -11.242 11.417 1.00 50.54 C ANISOU 1091 CD PRO A 131 6973 3754 8475 -2684 709 -1131 C ATOM 1092 N GLU A 132 6.800 -11.850 9.087 1.00 51.27 N ANISOU 1092 N GLU A 132 7706 3123 8651 -1790 645 -1133 N ATOM 1093 CA GLU A 132 7.577 -12.368 7.952 1.00 53.20 C ANISOU 1093 CA GLU A 132 8230 3130 8855 -1557 637 -1212 C ATOM 1094 C GLU A 132 7.496 -11.361 6.824 1.00 51.54 C ANISOU 1094 C GLU A 132 7650 3281 8651 -1388 555 -1293 C ATOM 1095 O GLU A 132 6.408 -10.861 6.521 1.00 52.92 O ANISOU 1095 O GLU A 132 7520 3801 8785 -1628 489 -1397 O ATOM 1096 CB GLU A 132 7.016 -13.704 7.460 1.00 56.70 C ANISOU 1096 CB GLU A 132 9116 3274 9152 -1922 661 -1385 C ATOM 1097 CG GLU A 132 6.583 -14.663 8.555 1.00 62.10 C ANISOU 1097 CG GLU A 132 10149 3660 9787 -2290 736 -1324 C ATOM 1098 CD GLU A 132 5.096 -14.546 8.949 1.00 63.91 C ANISOU 1098 CD GLU A 132 10110 4220 9955 -2863 733 -1404 C ATOM 1099 OE1 GLU A 132 4.371 -13.614 8.492 1.00 61.74 O ANISOU 1099 OE1 GLU A 132 9322 4447 9688 -2920 660 -1499 O ATOM 1100 OE2 GLU A 132 4.667 -15.394 9.754 1.00 66.20 O ANISOU 1100 OE2 GLU A 132 10705 4277 10171 -3245 809 -1361 O ATOM 1101 N THR A 133 8.624 -11.031 6.207 1.00 50.07 N ANISOU 1101 N THR A 133 7472 3052 8498 -972 557 -1239 N ATOM 1102 CA THR A 133 8.558 -10.140 5.043 1.00 48.16 C ANISOU 1102 CA THR A 133 6946 3126 8229 -834 487 -1301 C ATOM 1103 C THR A 133 8.615 -10.898 3.721 1.00 49.64 C ANISOU 1103 C THR A 133 7392 3206 8265 -840 483 -1485 C ATOM 1104 O THR A 133 9.063 -12.053 3.642 1.00 50.85 O ANISOU 1104 O THR A 133 7976 2990 8355 -823 546 -1550 O ATOM 1105 CB THR A 133 9.596 -9.000 5.071 1.00 45.77 C ANISOU 1105 CB THR A 133 6393 2965 8031 -441 486 -1127 C ATOM 1106 OG1 THR A 133 10.913 -9.531 5.172 1.00 48.14 O ANISOU 1106 OG1 THR A 133 6928 3015 8348 -143 565 -1047 O ATOM 1107 CG2 THR A 133 9.320 -8.075 6.250 1.00 44.64 C ANISOU 1107 CG2 THR A 133 5964 2983 8015 -471 459 -992 C ATOM 1108 N THR A 134 8.110 -10.242 2.688 1.00 48.16 N ANISOU 1108 N THR A 134 6962 3339 7999 -856 401 -1576 N ATOM 1109 CA THR A 134 8.255 -10.739 1.347 1.00 49.19 C ANISOU 1109 CA THR A 134 7284 3441 7967 -806 389 -1743 C ATOM 1110 C THR A 134 9.681 -10.419 0.901 1.00 46.70 C ANISOU 1110 C THR A 134 6997 3077 7668 -348 460 -1627 C ATOM 1111 O THR A 134 10.376 -9.620 1.535 1.00 44.44 O ANISOU 1111 O THR A 134 6507 2860 7518 -128 489 -1425 O ATOM 1112 CB THR A 134 7.232 -10.073 0.413 1.00 50.03 C ANISOU 1112 CB THR A 134 7095 3957 7958 -955 262 -1859 C ATOM 1113 OG1 THR A 134 7.665 -8.746 0.108 1.00 46.70 O ANISOU 1113 OG1 THR A 134 6359 3802 7584 -649 228 -1699 O ATOM 1114 CG2 THR A 134 5.860 -10.020 1.071 1.00 51.26 C ANISOU 1114 CG2 THR A 134 7041 4311 8123 -1353 191 -1925 C ATOM 1115 N LYS A 135 10.120 -11.054 -0.177 1.00 47.06 N ANISOU 1115 N LYS A 135 7292 3028 7558 -221 493 -1769 N ATOM 1116 CA LYS A 135 11.449 -10.814 -0.721 1.00 45.04 C ANISOU 1116 CA LYS A 135 7039 2799 7276 203 578 -1686 C ATOM 1117 C LYS A 135 11.582 -9.413 -1.331 1.00 42.09 C ANISOU 1117 C LYS A 135 6271 2825 6895 329 538 -1557 C ATOM 1118 O LYS A 135 12.661 -8.833 -1.308 1.00 40.57 O ANISOU 1118 O LYS A 135 5947 2718 6752 611 610 -1395 O ATOM 1119 CB LYS A 135 11.851 -11.931 -1.716 1.00 47.74 C ANISOU 1119 CB LYS A 135 7778 2938 7422 325 635 -1899 C ATOM 1120 CG LYS A 135 11.225 -11.870 -3.099 1.00 48.35 C ANISOU 1120 CG LYS A 135 7846 3236 7288 207 566 -2091 C ATOM 1121 CD LYS A 135 11.259 -13.252 -3.763 1.00 52.04 C ANISOU 1121 CD LYS A 135 8813 3391 7569 187 600 -2364 C ATOM 1122 CE LYS A 135 11.162 -13.219 -5.281 1.00 54.00 C ANISOU 1122 CE LYS A 135 9086 3867 7564 240 571 -2550 C ATOM 1123 NZ LYS A 135 10.653 -11.956 -5.872 1.00 52.15 N ANISOU 1123 NZ LYS A 135 8415 4114 7288 180 475 -2454 N ATOM 1124 N GLU A 136 10.492 -8.884 -1.879 1.00 41.88 N ANISOU 1124 N GLU A 136 6070 3049 6794 117 420 -1627 N ATOM 1125 CA GLU A 136 10.444 -7.475 -2.313 1.00 40.87 C ANISOU 1125 CA GLU A 136 5607 3258 6662 221 357 -1478 C ATOM 1126 C GLU A 136 10.672 -6.492 -1.160 1.00 37.76 C ANISOU 1126 C GLU A 136 4971 2891 6485 274 354 -1252 C ATOM 1127 O GLU A 136 11.414 -5.539 -1.326 1.00 36.61 O ANISOU 1127 O GLU A 136 4677 2865 6370 465 380 -1077 O ATOM 1128 CB GLU A 136 9.139 -7.124 -3.040 1.00 41.81 C ANISOU 1128 CB GLU A 136 5589 3653 6645 22 204 -1599 C ATOM 1129 CG GLU A 136 8.981 -7.819 -4.407 1.00 46.43 C ANISOU 1129 CG GLU A 136 6372 4299 6971 -5 184 -1814 C ATOM 1130 CD GLU A 136 8.626 -9.313 -4.332 1.00 49.92 C ANISOU 1130 CD GLU A 136 7153 4465 7351 -241 206 -2066 C ATOM 1131 OE1 GLU A 136 8.212 -9.798 -3.248 1.00 50.30 O ANISOU 1131 OE1 GLU A 136 7257 4317 7538 -459 214 -2077 O ATOM 1132 OE2 GLU A 136 8.768 -10.007 -5.372 1.00 51.12 O ANISOU 1132 OE2 GLU A 136 7547 4582 7295 -218 219 -2255 O ATOM 1133 N GLN A 137 10.048 -6.718 -0.003 1.00 37.18 N ANISOU 1133 N GLN A 137 4873 2710 6542 85 327 -1258 N ATOM 1134 CA GLN A 137 10.216 -5.787 1.128 1.00 34.58 C ANISOU 1134 CA GLN A 137 4329 2412 6398 135 318 -1071 C ATOM 1135 C GLN A 137 11.623 -5.857 1.661 1.00 33.28 C ANISOU 1135 C GLN A 137 4228 2087 6330 358 429 -927 C ATOM 1136 O GLN A 137 12.234 -4.839 1.940 1.00 31.04 O ANISOU 1136 O GLN A 137 3762 1900 6131 487 432 -759 O ATOM 1137 CB GLN A 137 9.205 -6.038 2.265 1.00 35.07 C ANISOU 1137 CB GLN A 137 4339 2440 6546 -119 278 -1119 C ATOM 1138 CG GLN A 137 7.736 -5.831 1.919 1.00 38.47 C ANISOU 1138 CG GLN A 137 4600 3130 6885 -345 158 -1257 C ATOM 1139 CD GLN A 137 6.776 -6.517 2.922 1.00 44.00 C ANISOU 1139 CD GLN A 137 5304 3797 7616 -671 162 -1351 C ATOM 1140 OE1 GLN A 137 7.155 -7.462 3.615 1.00 43.89 O ANISOU 1140 OE1 GLN A 137 5538 3492 7646 -767 255 -1346 O ATOM 1141 NE2 GLN A 137 5.531 -6.032 2.992 1.00 46.09 N ANISOU 1141 NE2 GLN A 137 5293 4382 7837 -831 62 -1431 N ATOM 1142 N LEU A 138 12.163 -7.078 1.765 1.00 34.84 N ANISOU 1142 N LEU A 138 4701 2042 6496 411 516 -1002 N ATOM 1143 CA LEU A 138 13.524 -7.291 2.233 1.00 33.88 C ANISOU 1143 CA LEU A 138 4632 1806 6434 673 614 -887 C ATOM 1144 C LEU A 138 14.585 -6.635 1.317 1.00 34.37 C ANISOU 1144 C LEU A 138 4553 2079 6428 916 672 -802 C ATOM 1145 O LEU A 138 15.575 -6.058 1.799 1.00 33.70 O ANISOU 1145 O LEU A 138 4301 2077 6425 1068 716 -643 O ATOM 1146 CB LEU A 138 13.758 -8.819 2.374 1.00 37.21 C ANISOU 1146 CB LEU A 138 5439 1905 6793 721 680 -1010 C ATOM 1147 CG LEU A 138 14.844 -9.384 3.289 1.00 37.89 C ANISOU 1147 CG LEU A 138 5653 1799 6944 969 752 -911 C ATOM 1148 CD1 LEU A 138 14.656 -8.881 4.713 1.00 37.21 C ANISOU 1148 CD1 LEU A 138 5413 1708 7016 857 710 -762 C ATOM 1149 CD2 LEU A 138 14.896 -10.964 3.238 1.00 39.67 C ANISOU 1149 CD2 LEU A 138 6365 1641 7068 1027 801 -1057 C ATOM 1150 N GLY A 139 14.400 -6.753 -0.001 1.00 35.27 N ANISOU 1150 N GLY A 139 4730 2300 6369 933 678 -912 N ATOM 1151 CA GLY A 139 15.231 -6.071 -0.978 1.00 35.63 C ANISOU 1151 CA GLY A 139 4640 2589 6309 1106 739 -828 C ATOM 1152 C GLY A 139 15.213 -4.548 -0.800 1.00 33.71 C ANISOU 1152 C GLY A 139 4115 2542 6152 1039 682 -627 C ATOM 1153 O GLY A 139 16.242 -3.921 -0.947 1.00 33.67 O ANISOU 1153 O GLY A 139 3969 2681 6142 1155 757 -482 O ATOM 1154 N GLU A 140 14.056 -3.967 -0.464 1.00 32.54 N ANISOU 1154 N GLU A 140 3894 2401 6070 851 553 -627 N ATOM 1155 CA GLU A 140 13.964 -2.505 -0.230 1.00 31.32 C ANISOU 1155 CA GLU A 140 3538 2369 5993 816 484 -448 C ATOM 1156 C GLU A 140 14.858 -2.072 0.942 1.00 29.74 C ANISOU 1156 C GLU A 140 3225 2105 5968 854 527 -299 C ATOM 1157 O GLU A 140 15.642 -1.156 0.831 1.00 29.58 O ANISOU 1157 O GLU A 140 3091 2189 5961 888 557 -141 O ATOM 1158 CB GLU A 140 12.487 -2.059 -0.071 1.00 30.65 C ANISOU 1158 CB GLU A 140 3397 2325 5924 671 332 -510 C ATOM 1159 CG GLU A 140 11.755 -2.029 -1.421 1.00 34.98 C ANISOU 1159 CG GLU A 140 3985 3043 6264 660 261 -603 C ATOM 1160 CD GLU A 140 10.220 -1.888 -1.334 1.00 42.25 C ANISOU 1160 CD GLU A 140 4822 4069 7160 531 105 -721 C ATOM 1161 OE1 GLU A 140 9.685 -1.327 -0.346 1.00 40.60 O ANISOU 1161 OE1 GLU A 140 4484 3852 7088 490 40 -680 O ATOM 1162 OE2 GLU A 140 9.527 -2.333 -2.297 1.00 46.91 O ANISOU 1162 OE2 GLU A 140 5460 4795 7570 477 43 -870 O ATOM 1163 N PHE A 141 14.766 -2.796 2.044 1.00 29.14 N ANISOU 1163 N PHE A 141 3200 1866 6005 827 532 -353 N ATOM 1164 CA PHE A 141 15.646 -2.601 3.171 1.00 29.03 C ANISOU 1164 CA PHE A 141 3096 1807 6126 883 566 -237 C ATOM 1165 C PHE A 141 17.139 -2.764 2.829 1.00 30.26 C ANISOU 1165 C PHE A 141 3197 2071 6231 1067 684 -162 C ATOM 1166 O PHE A 141 17.948 -1.920 3.207 1.00 29.75 O ANISOU 1166 O PHE A 141 2955 2123 6227 1068 696 -21 O ATOM 1167 CB PHE A 141 15.276 -3.568 4.282 1.00 29.66 C ANISOU 1167 CB PHE A 141 3296 1689 6282 843 559 -312 C ATOM 1168 CG PHE A 141 16.096 -3.405 5.515 1.00 30.51 C ANISOU 1168 CG PHE A 141 3318 1768 6506 908 572 -199 C ATOM 1169 CD1 PHE A 141 16.690 -4.492 6.103 1.00 32.50 C ANISOU 1169 CD1 PHE A 141 3707 1886 6755 1041 627 -216 C ATOM 1170 CD2 PHE A 141 16.213 -2.152 6.126 1.00 31.64 C ANISOU 1170 CD2 PHE A 141 3271 2004 6748 840 512 -84 C ATOM 1171 CE1 PHE A 141 17.442 -4.350 7.257 1.00 32.17 C ANISOU 1171 CE1 PHE A 141 3574 1855 6796 1119 620 -111 C ATOM 1172 CE2 PHE A 141 16.974 -2.020 7.279 1.00 31.04 C ANISOU 1172 CE2 PHE A 141 3111 1925 6758 883 510 1 C ATOM 1173 CZ PHE A 141 17.575 -3.123 7.833 1.00 28.49 C ANISOU 1173 CZ PHE A 141 2888 1517 6421 1025 561 -10 C ATOM 1174 N TYR A 142 17.485 -3.814 2.096 1.00 32.35 N ANISOU 1174 N TYR A 142 3604 2320 6367 1216 769 -270 N ATOM 1175 CA TYR A 142 18.876 -4.036 1.649 1.00 34.37 C ANISOU 1175 CA TYR A 142 3780 2746 6535 1440 895 -227 C ATOM 1176 C TYR A 142 19.387 -2.860 0.816 1.00 35.44 C ANISOU 1176 C TYR A 142 3714 3155 6596 1381 934 -94 C ATOM 1177 O TYR A 142 20.533 -2.426 0.996 1.00 35.42 O ANISOU 1177 O TYR A 142 3507 3352 6598 1437 1005 25 O ATOM 1178 CB TYR A 142 18.983 -5.317 0.819 1.00 36.57 C ANISOU 1178 CB TYR A 142 4290 2952 6652 1631 975 -402 C ATOM 1179 CG TYR A 142 18.854 -6.625 1.571 1.00 36.55 C ANISOU 1179 CG TYR A 142 4550 2653 6686 1741 970 -515 C ATOM 1180 CD1 TYR A 142 18.689 -7.810 0.876 1.00 38.54 C ANISOU 1180 CD1 TYR A 142 5109 2738 6795 1864 1016 -702 C ATOM 1181 CD2 TYR A 142 18.891 -6.683 2.964 1.00 34.68 C ANISOU 1181 CD2 TYR A 142 4294 2279 6602 1716 919 -434 C ATOM 1182 CE1 TYR A 142 18.602 -9.031 1.539 1.00 40.78 C ANISOU 1182 CE1 TYR A 142 5710 2690 7094 1960 1014 -794 C ATOM 1183 CE2 TYR A 142 18.769 -7.886 3.644 1.00 35.70 C ANISOU 1183 CE2 TYR A 142 4715 2110 6739 1809 917 -509 C ATOM 1184 CZ TYR A 142 18.621 -9.062 2.922 1.00 39.40 C ANISOU 1184 CZ TYR A 142 5524 2377 7070 1925 965 -684 C ATOM 1185 OH TYR A 142 18.495 -10.278 3.567 1.00 39.76 O ANISOU 1185 OH TYR A 142 5937 2064 7108 2004 962 -750 O ATOM 1186 N GLU A 143 18.515 -2.297 -0.043 1.00 35.16 N ANISOU 1186 N GLU A 143 3734 3141 6482 1246 877 -101 N ATOM 1187 CA GLU A 143 18.903 -1.140 -0.856 1.00 36.60 C ANISOU 1187 CA GLU A 143 3795 3538 6572 1168 907 53 C ATOM 1188 C GLU A 143 19.188 0.070 0.025 1.00 34.94 C ANISOU 1188 C GLU A 143 3433 3328 6516 1013 852 231 C ATOM 1189 O GLU A 143 20.150 0.817 -0.220 1.00 35.19 O ANISOU 1189 O GLU A 143 3322 3546 6504 951 927 381 O ATOM 1190 CB GLU A 143 17.841 -0.795 -1.910 1.00 37.91 C ANISOU 1190 CB GLU A 143 4086 3715 6604 1091 830 17 C ATOM 1191 CG GLU A 143 17.700 -1.866 -2.999 1.00 44.00 C ANISOU 1191 CG GLU A 143 5008 4539 7171 1217 892 -163 C ATOM 1192 CD GLU A 143 16.520 -1.620 -3.969 1.00 48.83 C ANISOU 1192 CD GLU A 143 5734 5185 7636 1138 782 -227 C ATOM 1193 OE1 GLU A 143 15.663 -0.742 -3.721 1.00 49.36 O ANISOU 1193 OE1 GLU A 143 5770 5213 7771 1021 644 -151 O ATOM 1194 OE2 GLU A 143 16.455 -2.327 -4.996 1.00 54.17 O ANISOU 1194 OE2 GLU A 143 6532 5943 8106 1218 827 -366 O ATOM 1195 N ALA A 144 18.367 0.257 1.058 1.00 32.36 N ANISOU 1195 N ALA A 144 3141 2803 6353 931 727 206 N ATOM 1196 CA ALA A 144 18.594 1.352 2.017 1.00 31.60 C ANISOU 1196 CA ALA A 144 2938 2668 6401 797 663 338 C ATOM 1197 C ALA A 144 19.952 1.117 2.725 1.00 32.83 C ANISOU 1197 C ALA A 144 2920 2947 6609 842 749 392 C ATOM 1198 O ALA A 144 20.754 2.048 2.865 1.00 33.02 O ANISOU 1198 O ALA A 144 2806 3094 6648 713 768 529 O ATOM 1199 CB ALA A 144 17.456 1.438 3.012 1.00 28.68 C ANISOU 1199 CB ALA A 144 2630 2099 6168 744 531 267 C ATOM 1200 N LEU A 145 20.222 -0.133 3.112 1.00 33.32 N ANISOU 1200 N LEU A 145 3000 2985 6674 1024 796 284 N ATOM 1201 CA LEU A 145 21.537 -0.469 3.665 1.00 35.72 C ANISOU 1201 CA LEU A 145 3123 3462 6987 1144 869 324 C ATOM 1202 C LEU A 145 22.658 -0.253 2.675 1.00 38.21 C ANISOU 1202 C LEU A 145 3265 4102 7151 1187 1006 393 C ATOM 1203 O LEU A 145 23.671 0.341 3.030 1.00 39.19 O ANISOU 1203 O LEU A 145 3149 4453 7287 1107 1038 501 O ATOM 1204 CB LEU A 145 21.591 -1.899 4.189 1.00 35.90 C ANISOU 1204 CB LEU A 145 3262 3365 7013 1390 888 203 C ATOM 1205 CG LEU A 145 20.781 -2.074 5.468 1.00 36.21 C ANISOU 1205 CG LEU A 145 3414 3150 7196 1316 774 174 C ATOM 1206 CD1 LEU A 145 20.742 -3.536 5.766 1.00 36.40 C ANISOU 1206 CD1 LEU A 145 3641 3005 7184 1534 802 68 C ATOM 1207 CD2 LEU A 145 21.379 -1.278 6.631 1.00 36.44 C ANISOU 1207 CD2 LEU A 145 3243 3270 7332 1225 713 283 C ATOM 1208 N ASP A 146 22.480 -0.752 1.450 1.00 40.00 N ANISOU 1208 N ASP A 146 3601 4379 7217 1295 1088 322 N ATOM 1209 CA ASP A 146 23.403 -0.460 0.354 1.00 42.82 C ANISOU 1209 CA ASP A 146 3805 5074 7391 1309 1234 391 C ATOM 1210 C ASP A 146 23.788 1.058 0.351 1.00 42.78 C ANISOU 1210 C ASP A 146 3644 5205 7406 986 1225 596 C ATOM 1211 O ASP A 146 24.965 1.379 0.285 1.00 44.84 O ANISOU 1211 O ASP A 146 3647 5791 7599 933 1330 687 O ATOM 1212 CB ASP A 146 22.837 -0.943 -1.017 1.00 44.13 C ANISOU 1212 CB ASP A 146 4167 5234 7367 1403 1289 291 C ATOM 1213 CG ASP A 146 22.726 -2.516 -1.166 1.00 47.88 C ANISOU 1213 CG ASP A 146 4821 5596 7775 1721 1330 70 C ATOM 1214 OD1 ASP A 146 21.969 -2.968 -2.068 1.00 51.21 O ANISOU 1214 OD1 ASP A 146 5463 5921 8074 1752 1325 -52 O ATOM 1215 OD2 ASP A 146 23.362 -3.324 -0.435 1.00 47.68 O ANISOU 1215 OD2 ASP A 146 4754 5563 7797 1946 1359 11 O ATOM 1216 N CYS A 147 22.819 1.978 0.481 1.00 40.99 N ANISOU 1216 N CYS A 147 3576 4734 7265 773 1096 662 N ATOM 1217 CA CYS A 147 23.112 3.455 0.514 1.00 41.44 C ANISOU 1217 CA CYS A 147 3584 4821 7339 460 1070 856 C ATOM 1218 C CYS A 147 24.013 3.883 1.669 1.00 39.98 C ANISOU 1218 C CYS A 147 3181 4731 7280 321 1052 916 C ATOM 1219 O CYS A 147 24.773 4.826 1.545 1.00 41.14 O ANISOU 1219 O CYS A 147 3209 5039 7382 60 1098 1062 O ATOM 1220 CB CYS A 147 21.830 4.321 0.531 1.00 40.58 C ANISOU 1220 CB CYS A 147 3730 4391 7297 340 913 894 C ATOM 1221 SG CYS A 147 22.012 6.105 1.159 1.00 47.07 S ANISOU 1221 SG CYS A 147 4605 5063 8218 -12 817 1089 S ATOM 1222 N LEU A 148 23.916 3.188 2.792 1.00 36.90 N ANISOU 1222 N LEU A 148 2751 4244 7026 472 982 806 N ATOM 1223 CA LEU A 148 24.729 3.510 3.952 1.00 36.35 C ANISOU 1223 CA LEU A 148 2470 4283 7057 367 942 842 C ATOM 1224 C LEU A 148 26.042 2.701 3.935 1.00 38.14 C ANISOU 1224 C LEU A 148 2391 4912 7186 556 1066 817 C ATOM 1225 O LEU A 148 26.825 2.787 4.873 1.00 38.55 O ANISOU 1225 O LEU A 148 2218 5138 7292 522 1031 831 O ATOM 1226 CB LEU A 148 23.950 3.215 5.247 1.00 33.35 C ANISOU 1226 CB LEU A 148 2208 3617 6848 443 795 749 C ATOM 1227 CG LEU A 148 22.671 4.035 5.503 1.00 31.69 C ANISOU 1227 CG LEU A 148 2243 3061 6735 299 662 749 C ATOM 1228 CD1 LEU A 148 22.227 3.834 6.953 1.00 29.54 C ANISOU 1228 CD1 LEU A 148 1999 2621 6606 339 545 669 C ATOM 1229 CD2 LEU A 148 22.916 5.525 5.203 1.00 32.51 C ANISOU 1229 CD2 LEU A 148 2378 3151 6824 -10 639 893 C ATOM 1230 N ARG A 149 26.240 1.918 2.871 1.00 39.09 N ANISOU 1230 N ARG A 149 2509 5192 7150 779 1200 765 N ATOM 1231 CA ARG A 149 27.387 1.026 2.721 1.00 42.24 C ANISOU 1231 CA ARG A 149 2647 5976 7428 1062 1327 710 C ATOM 1232 C ARG A 149 27.521 0.070 3.898 1.00 40.97 C ANISOU 1232 C ARG A 149 2469 5735 7363 1353 1245 612 C ATOM 1233 O ARG A 149 28.619 -0.226 4.343 1.00 43.11 O ANISOU 1233 O ARG A 149 2442 6350 7586 1506 1279 613 O ATOM 1234 CB ARG A 149 28.691 1.813 2.507 1.00 45.28 C ANISOU 1234 CB ARG A 149 2647 6852 7708 836 1432 836 C ATOM 1235 CG ARG A 149 28.688 2.669 1.261 1.00 49.65 C ANISOU 1235 CG ARG A 149 3236 7513 8116 554 1544 958 C ATOM 1236 CD ARG A 149 30.022 3.401 1.109 1.00 59.51 C ANISOU 1236 CD ARG A 149 4087 9278 9245 272 1664 1085 C ATOM 1237 NE ARG A 149 30.345 4.304 2.227 1.00 62.68 N ANISOU 1237 NE ARG A 149 4365 9662 9791 -71 1541 1162 N ATOM 1238 CZ ARG A 149 29.758 5.479 2.464 1.00 61.79 C ANISOU 1238 CZ ARG A 149 4489 9209 9781 -465 1431 1270 C ATOM 1239 NH1 ARG A 149 28.780 5.907 1.685 1.00 61.65 N ANISOU 1239 NH1 ARG A 149 4834 8847 9743 -539 1418 1329 N ATOM 1240 NH2 ARG A 149 30.154 6.232 3.487 1.00 62.44 N ANISOU 1240 NH2 ARG A 149 4457 9298 9970 -765 1325 1309 N ATOM 1241 N ILE A 150 26.385 -0.394 4.399 1.00 38.37 N ANISOU 1241 N ILE A 150 2456 4972 7152 1422 1134 534 N ATOM 1242 CA ILE A 150 26.382 -1.429 5.398 1.00 38.04 C ANISOU 1242 CA ILE A 150 2490 4795 7169 1705 1069 452 C ATOM 1243 C ILE A 150 26.148 -2.760 4.667 1.00 39.12 C ANISOU 1243 C ILE A 150 2861 4809 7195 2057 1151 316 C ATOM 1244 O ILE A 150 25.099 -2.926 4.002 1.00 38.51 O ANISOU 1244 O ILE A 150 3062 4459 7109 1986 1147 250 O ATOM 1245 CB ILE A 150 25.288 -1.189 6.455 1.00 35.15 C ANISOU 1245 CB ILE A 150 2338 4043 6974 1540 914 448 C ATOM 1246 CG1 ILE A 150 25.500 0.159 7.152 1.00 34.56 C ANISOU 1246 CG1 ILE A 150 2083 4053 6994 1203 828 555 C ATOM 1247 CG2 ILE A 150 25.292 -2.305 7.480 1.00 35.20 C ANISOU 1247 CG2 ILE A 150 2461 3903 7011 1817 858 388 C ATOM 1248 CD1 ILE A 150 24.255 0.628 7.988 1.00 31.82 C ANISOU 1248 CD1 ILE A 150 1959 3336 6794 1020 689 539 C ATOM 1249 N PRO A 151 27.104 -3.704 4.786 1.00 41.55 N ANISOU 1249 N PRO A 151 3068 5318 7403 2447 1213 262 N ATOM 1250 CA PRO A 151 26.950 -4.981 4.080 1.00 43.09 C ANISOU 1250 CA PRO A 151 3536 5362 7474 2808 1291 114 C ATOM 1251 C PRO A 151 25.679 -5.726 4.508 1.00 41.12 C ANISOU 1251 C PRO A 151 3740 4567 7316 2792 1195 29 C ATOM 1252 O PRO A 151 25.284 -5.659 5.680 1.00 39.72 O ANISOU 1252 O PRO A 151 3627 4190 7274 2688 1078 80 O ATOM 1253 CB PRO A 151 28.209 -5.770 4.490 1.00 46.30 C ANISOU 1253 CB PRO A 151 3758 6055 7781 3264 1333 88 C ATOM 1254 CG PRO A 151 29.200 -4.737 4.878 1.00 47.78 C ANISOU 1254 CG PRO A 151 3448 6728 7978 3087 1334 219 C ATOM 1255 CD PRO A 151 28.366 -3.658 5.553 1.00 43.65 C ANISOU 1255 CD PRO A 151 2973 5968 7645 2600 1205 320 C ATOM 1256 N ARG A 152 25.021 -6.395 3.563 1.00 41.53 N ANISOU 1256 N ARG A 152 4096 4404 7280 2855 1246 -104 N ATOM 1257 CA ARG A 152 23.815 -7.175 3.896 1.00 40.45 C ANISOU 1257 CA ARG A 152 4387 3777 7204 2791 1166 -200 C ATOM 1258 C ARG A 152 24.128 -8.263 4.950 1.00 41.74 C ANISOU 1258 C ARG A 152 4758 3719 7383 3090 1125 -217 C ATOM 1259 O ARG A 152 23.253 -8.659 5.731 1.00 40.55 O ANISOU 1259 O ARG A 152 4882 3206 7320 2951 1040 -222 O ATOM 1260 CB ARG A 152 23.235 -7.817 2.637 1.00 42.23 C ANISOU 1260 CB ARG A 152 4897 3857 7292 2829 1230 -368 C ATOM 1261 CG ARG A 152 22.460 -6.843 1.748 1.00 39.77 C ANISOU 1261 CG ARG A 152 4505 3636 6972 2485 1218 -352 C ATOM 1262 CD ARG A 152 22.401 -7.375 0.327 1.00 42.99 C ANISOU 1262 CD ARG A 152 5073 4087 7173 2611 1312 -506 C ATOM 1263 NE ARG A 152 21.918 -6.385 -0.632 1.00 46.46 N ANISOU 1263 NE ARG A 152 5396 4704 7554 2350 1312 -460 N ATOM 1264 CZ ARG A 152 21.497 -6.686 -1.859 1.00 48.42 C ANISOU 1264 CZ ARG A 152 5809 4966 7623 2358 1351 -592 C ATOM 1265 NH1 ARG A 152 21.455 -7.958 -2.266 1.00 51.90 N ANISOU 1265 NH1 ARG A 152 6559 5221 7939 2588 1393 -801 N ATOM 1266 NH2 ARG A 152 21.096 -5.722 -2.669 1.00 46.87 N ANISOU 1266 NH2 ARG A 152 5505 4945 7357 2141 1337 -519 N ATOM 1267 N SER A 153 25.380 -8.715 4.988 1.00 44.58 N ANISOU 1267 N SER A 153 4974 4325 7639 3504 1186 -214 N ATOM 1268 CA SER A 153 25.799 -9.707 5.986 1.00 46.46 C ANISOU 1268 CA SER A 153 5408 4381 7863 3859 1135 -206 C ATOM 1269 C SER A 153 25.822 -9.193 7.445 1.00 44.96 C ANISOU 1269 C SER A 153 5063 4210 7810 3708 1010 -50 C ATOM 1270 O SER A 153 25.857 -9.991 8.374 1.00 45.88 O ANISOU 1270 O SER A 153 5425 4087 7920 3919 944 -23 O ATOM 1271 CB SER A 153 27.136 -10.374 5.594 1.00 50.57 C ANISOU 1271 CB SER A 153 5809 5198 8206 4425 1225 -262 C ATOM 1272 OG SER A 153 28.063 -9.381 5.222 1.00 51.58 O ANISOU 1272 OG SER A 153 5381 5918 8300 4379 1290 -192 O ATOM 1273 N ASP A 154 25.755 -7.876 7.658 1.00 43.22 N ANISOU 1273 N ASP A 154 4487 4238 7698 3340 973 49 N ATOM 1274 CA ASP A 154 25.734 -7.352 9.034 1.00 42.66 C ANISOU 1274 CA ASP A 154 4288 4180 7740 3183 850 169 C ATOM 1275 C ASP A 154 24.350 -7.306 9.648 1.00 40.42 C ANISOU 1275 C ASP A 154 4297 3490 7572 2853 773 171 C ATOM 1276 O ASP A 154 24.186 -6.888 10.797 1.00 40.21 O ANISOU 1276 O ASP A 154 4205 3448 7625 2709 678 254 O ATOM 1277 CB ASP A 154 26.344 -5.949 9.110 1.00 41.84 C ANISOU 1277 CB ASP A 154 3701 4506 7689 2932 834 263 C ATOM 1278 CG ASP A 154 27.861 -5.960 9.079 1.00 47.03 C ANISOU 1278 CG ASP A 154 3972 5663 8233 3230 874 294 C ATOM 1279 OD1 ASP A 154 28.496 -7.036 9.282 1.00 46.63 O ANISOU 1279 OD1 ASP A 154 4004 5641 8073 3701 883 259 O ATOM 1280 OD2 ASP A 154 28.413 -4.864 8.842 1.00 50.29 O ANISOU 1280 OD2 ASP A 154 3999 6453 8656 2985 894 354 O ATOM 1281 N VAL A 155 23.338 -7.704 8.888 1.00 39.49 N ANISOU 1281 N VAL A 155 4475 3082 7446 2719 814 69 N ATOM 1282 CA VAL A 155 21.977 -7.523 9.353 1.00 36.01 C ANISOU 1282 CA VAL A 155 4222 2358 7101 2362 752 58 C ATOM 1283 C VAL A 155 21.689 -8.517 10.466 1.00 37.43 C ANISOU 1283 C VAL A 155 4729 2225 7270 2449 707 84 C ATOM 1284 O VAL A 155 22.088 -9.685 10.392 1.00 38.79 O ANISOU 1284 O VAL A 155 5191 2209 7340 2762 740 50 O ATOM 1285 CB VAL A 155 20.965 -7.641 8.199 1.00 35.91 C ANISOU 1285 CB VAL A 155 4388 2193 7063 2170 795 -67 C ATOM 1286 CG1 VAL A 155 19.545 -7.711 8.720 1.00 33.15 C ANISOU 1286 CG1 VAL A 155 4238 1579 6780 1841 736 -100 C ATOM 1287 CG2 VAL A 155 21.117 -6.460 7.254 1.00 33.54 C ANISOU 1287 CG2 VAL A 155 3777 2194 6771 2032 821 -50 C ATOM 1288 N MET A 156 20.982 -8.061 11.498 1.00 35.11 N ANISOU 1288 N MET A 156 4418 1861 7060 2181 634 146 N ATOM 1289 CA MET A 156 20.572 -8.956 12.575 1.00 37.13 C ANISOU 1289 CA MET A 156 5005 1818 7284 2193 601 190 C ATOM 1290 C MET A 156 19.078 -9.069 12.458 1.00 35.48 C ANISOU 1290 C MET A 156 5001 1374 7105 1809 614 112 C ATOM 1291 O MET A 156 18.379 -8.063 12.375 1.00 31.91 O ANISOU 1291 O MET A 156 4319 1068 6735 1525 589 90 O ATOM 1292 CB MET A 156 20.955 -8.416 13.955 1.00 37.85 C ANISOU 1292 CB MET A 156 4908 2065 7407 2193 515 318 C ATOM 1293 CG MET A 156 22.456 -8.374 14.229 1.00 43.18 C ANISOU 1293 CG MET A 156 5351 3027 8029 2569 481 395 C ATOM 1294 SD MET A 156 22.716 -7.199 15.572 1.00 50.87 S ANISOU 1294 SD MET A 156 5979 4286 9063 2399 364 496 S ATOM 1295 CE MET A 156 24.469 -6.880 15.433 1.00 50.97 C ANISOU 1295 CE MET A 156 5578 4771 9017 2736 334 540 C ATOM 1296 N TYR A 157 18.591 -10.297 12.444 1.00 36.21 N ANISOU 1296 N TYR A 157 5534 1108 7118 1803 649 66 N ATOM 1297 CA TYR A 157 17.192 -10.544 12.194 1.00 36.28 C ANISOU 1297 CA TYR A 157 5730 927 7127 1411 670 -32 C ATOM 1298 C TYR A 157 16.522 -11.070 13.444 1.00 37.75 C ANISOU 1298 C TYR A 157 6162 898 7283 1207 659 47 C ATOM 1299 O TYR A 157 17.153 -11.807 14.209 1.00 39.64 O ANISOU 1299 O TYR A 157 6653 957 7453 1438 652 154 O ATOM 1300 CB TYR A 157 17.056 -11.629 11.121 1.00 38.28 C ANISOU 1300 CB TYR A 157 6355 907 7284 1471 728 -170 C ATOM 1301 CG TYR A 157 17.636 -11.245 9.792 1.00 38.02 C ANISOU 1301 CG TYR A 157 6126 1083 7238 1662 758 -262 C ATOM 1302 CD1 TYR A 157 18.941 -11.614 9.446 1.00 41.62 C ANISOU 1302 CD1 TYR A 157 6594 1592 7626 2120 792 -248 C ATOM 1303 CD2 TYR A 157 16.868 -10.556 8.855 1.00 36.44 C ANISOU 1303 CD2 TYR A 157 5733 1049 7062 1403 754 -365 C ATOM 1304 CE1 TYR A 157 19.465 -11.284 8.192 1.00 40.90 C ANISOU 1304 CE1 TYR A 157 6319 1730 7493 2278 843 -335 C ATOM 1305 CE2 TYR A 157 17.362 -10.229 7.632 1.00 36.50 C ANISOU 1305 CE2 TYR A 157 5595 1247 7027 1558 789 -435 C ATOM 1306 CZ TYR A 157 18.662 -10.546 7.307 1.00 38.14 C ANISOU 1306 CZ TYR A 157 5796 1527 7170 1973 841 -416 C ATOM 1307 OH TYR A 157 19.138 -10.218 6.059 1.00 38.51 O ANISOU 1307 OH TYR A 157 5686 1800 7145 2107 896 -486 O ATOM 1308 N THR A 158 15.238 -10.757 13.610 1.00 36.45 N ANISOU 1308 N THR A 158 5942 763 7145 789 663 -8 N ATOM 1309 CA THR A 158 14.408 -11.495 14.561 1.00 38.29 C ANISOU 1309 CA THR A 158 6474 766 7306 511 690 38 C ATOM 1310 C THR A 158 14.032 -12.866 13.975 1.00 42.76 C ANISOU 1310 C THR A 158 7553 927 7766 403 745 -47 C ATOM 1311 O THR A 158 14.119 -13.072 12.767 1.00 42.74 O ANISOU 1311 O THR A 158 7602 881 7754 472 757 -184 O ATOM 1312 CB THR A 158 13.122 -10.762 14.885 1.00 37.36 C ANISOU 1312 CB THR A 158 6099 869 7225 97 689 -15 C ATOM 1313 OG1 THR A 158 12.439 -10.414 13.673 1.00 37.61 O ANISOU 1313 OG1 THR A 158 5973 1030 7287 -66 686 -180 O ATOM 1314 CG2 THR A 158 13.422 -9.459 15.676 1.00 33.05 C ANISOU 1314 CG2 THR A 158 5138 654 6764 189 631 64 C ATOM 1315 N ASP A 159 13.586 -13.762 14.854 1.00 44.70 N ANISOU 1315 N ASP A 159 8190 877 7916 207 780 33 N ATOM 1316 CA ASP A 159 13.077 -15.063 14.495 1.00 49.90 C ANISOU 1316 CA ASP A 159 9400 1100 8460 -3 832 -38 C ATOM 1317 C ASP A 159 11.680 -15.206 15.138 1.00 50.99 C ANISOU 1317 C ASP A 159 9583 1246 8544 -601 880 -40 C ATOM 1318 O ASP A 159 11.577 -15.430 16.354 1.00 52.47 O ANISOU 1318 O ASP A 159 9912 1356 8667 -699 904 124 O ATOM 1319 CB ASP A 159 14.077 -16.101 15.020 1.00 51.44 C ANISOU 1319 CB ASP A 159 10103 887 8555 385 831 101 C ATOM 1320 CG ASP A 159 13.666 -17.522 14.748 1.00 58.18 C ANISOU 1320 CG ASP A 159 11649 1185 9273 204 881 47 C ATOM 1321 OD1 ASP A 159 14.425 -18.405 15.207 1.00 57.16 O ANISOU 1321 OD1 ASP A 159 11999 675 9043 544 873 169 O ATOM 1322 OD2 ASP A 159 12.614 -17.760 14.113 1.00 60.05 O ANISOU 1322 OD2 ASP A 159 11967 1361 9489 -266 917 -115 O ATOM 1323 N TRP A 160 10.618 -15.063 14.334 1.00 51.35 N ANISOU 1323 N TRP A 160 9482 1434 8595 -996 894 -225 N ATOM 1324 CA TRP A 160 9.237 -15.172 14.846 1.00 53.49 C ANISOU 1324 CA TRP A 160 9713 1813 8799 -1589 946 -256 C ATOM 1325 C TRP A 160 8.916 -16.457 15.634 1.00 58.13 C ANISOU 1325 C TRP A 160 10901 1953 9231 -1901 1024 -150 C ATOM 1326 O TRP A 160 8.087 -16.411 16.546 1.00 58.94 O ANISOU 1326 O TRP A 160 10929 2198 9266 -2297 1083 -79 O ATOM 1327 CB TRP A 160 8.167 -14.942 13.756 1.00 54.02 C ANISOU 1327 CB TRP A 160 9539 2122 8865 -1950 933 -490 C ATOM 1328 CG TRP A 160 6.740 -14.872 14.328 1.00 57.39 C ANISOU 1328 CG TRP A 160 9776 2813 9218 -2538 984 -532 C ATOM 1329 CD1 TRP A 160 5.676 -15.716 14.054 1.00 62.78 C ANISOU 1329 CD1 TRP A 160 10678 3404 9773 -3110 1033 -657 C ATOM 1330 CD2 TRP A 160 6.260 -13.935 15.308 1.00 57.50 C ANISOU 1330 CD2 TRP A 160 9342 3248 9259 -2612 999 -456 C ATOM 1331 NE1 TRP A 160 4.564 -15.337 14.788 1.00 62.87 N ANISOU 1331 NE1 TRP A 160 10350 3810 9728 -3533 1085 -658 N ATOM 1332 CE2 TRP A 160 4.896 -14.248 15.563 1.00 60.67 C ANISOU 1332 CE2 TRP A 160 9668 3844 9540 -3210 1067 -540 C ATOM 1333 CE3 TRP A 160 6.850 -12.855 15.993 1.00 54.44 C ANISOU 1333 CE3 TRP A 160 8610 3104 8969 -2240 962 -341 C ATOM 1334 CZ2 TRP A 160 4.113 -13.514 16.473 1.00 60.42 C ANISOU 1334 CZ2 TRP A 160 9211 4267 9480 -3394 1109 -514 C ATOM 1335 CZ3 TRP A 160 6.066 -12.118 16.899 1.00 56.14 C ANISOU 1335 CZ3 TRP A 160 8450 3718 9161 -2427 992 -323 C ATOM 1336 CH2 TRP A 160 4.712 -12.460 17.132 1.00 58.37 C ANISOU 1336 CH2 TRP A 160 8651 4208 9317 -2977 1070 -410 C ATOM 1337 N LYS A 161 9.580 -17.570 15.304 1.00 60.84 N ANISOU 1337 N LYS A 161 11849 1766 9503 -1708 1028 -133 N ATOM 1338 CA LYS A 161 9.416 -18.846 16.043 1.00 66.67 C ANISOU 1338 CA LYS A 161 13278 1976 10078 -1949 1093 -3 C ATOM 1339 C LYS A 161 9.694 -18.646 17.519 1.00 66.01 C ANISOU 1339 C LYS A 161 13177 1953 9952 -1851 1112 259 C ATOM 1340 O LYS A 161 9.172 -19.387 18.349 1.00 68.16 O ANISOU 1340 O LYS A 161 13854 1969 10076 -2224 1185 390 O ATOM 1341 CB LYS A 161 10.390 -19.914 15.533 1.00 69.42 C ANISOU 1341 CB LYS A 161 14275 1738 10363 -1537 1070 -4 C ATOM 1342 CG LYS A 161 10.104 -20.437 14.134 1.00 74.40 C ANISOU 1342 CG LYS A 161 15124 2170 10973 -1671 1064 -269 C ATOM 1343 CD LYS A 161 11.391 -20.739 13.315 1.00 77.87 C ANISOU 1343 CD LYS A 161 15785 2375 11428 -980 1015 -332 C ATOM 1344 CE LYS A 161 12.546 -21.264 14.160 1.00 78.92 C ANISOU 1344 CE LYS A 161 16310 2173 11503 -419 998 -105 C ATOM 1345 NZ LYS A 161 12.510 -22.740 14.266 1.00 84.07 N ANISOU 1345 NZ LYS A 161 17877 2083 11982 -495 1027 -83 N ATOM 1346 N LYS A 162 10.513 -17.632 17.831 1.00 62.10 N ANISOU 1346 N LYS A 162 12218 1806 9570 -1377 1044 332 N ATOM 1347 CA LYS A 162 11.031 -17.446 19.190 1.00 62.15 C ANISOU 1347 CA LYS A 162 12226 1864 9523 -1168 1033 572 C ATOM 1348 C LYS A 162 10.160 -16.589 20.087 1.00 60.20 C ANISOU 1348 C LYS A 162 11528 2074 9271 -1528 1075 607 C ATOM 1349 O LYS A 162 10.458 -16.450 21.275 1.00 60.44 O ANISOU 1349 O LYS A 162 11572 2167 9226 -1421 1073 796 O ATOM 1350 CB LYS A 162 12.470 -16.915 19.181 1.00 59.49 C ANISOU 1350 CB LYS A 162 11680 1647 9275 -474 931 637 C ATOM 1351 CG LYS A 162 13.405 -17.741 18.317 1.00 63.35 C ANISOU 1351 CG LYS A 162 12573 1748 9747 -38 897 593 C ATOM 1352 CD LYS A 162 14.701 -18.084 19.037 1.00 67.14 C ANISOU 1352 CD LYS A 162 13273 2082 10154 558 828 790 C ATOM 1353 CE LYS A 162 15.336 -19.309 18.396 1.00 72.11 C ANISOU 1353 CE LYS A 162 14531 2177 10690 910 823 764 C ATOM 1354 NZ LYS A 162 16.288 -20.029 19.300 1.00 76.96 N ANISOU 1354 NZ LYS A 162 15579 2505 11156 1401 765 991 N ATOM 1355 N ASP A 163 9.084 -16.032 19.529 1.00 59.12 N ANISOU 1355 N ASP A 163 10998 2272 9192 -1928 1109 420 N ATOM 1356 CA ASP A 163 8.225 -15.098 20.264 1.00 57.89 C ANISOU 1356 CA ASP A 163 10343 2620 9032 -2204 1146 409 C ATOM 1357 C ASP A 163 7.703 -15.692 21.562 1.00 61.02 C ANISOU 1357 C ASP A 163 11022 2929 9233 -2557 1250 587 C ATOM 1358 O ASP A 163 7.159 -16.774 21.556 1.00 63.78 O ANISOU 1358 O ASP A 163 11839 2950 9447 -2965 1334 618 O ATOM 1359 CB ASP A 163 7.024 -14.673 19.418 1.00 57.93 C ANISOU 1359 CB ASP A 163 9969 2962 9080 -2604 1170 175 C ATOM 1360 CG ASP A 163 6.049 -13.795 20.200 1.00 57.52 C ANISOU 1360 CG ASP A 163 9421 3441 8991 -2871 1220 147 C ATOM 1361 OD1 ASP A 163 6.393 -12.638 20.480 1.00 53.83 O ANISOU 1361 OD1 ASP A 163 8532 3298 8624 -2544 1156 143 O ATOM 1362 OD2 ASP A 163 4.946 -14.275 20.557 1.00 63.76 O ANISOU 1362 OD2 ASP A 163 10258 4330 9637 -3414 1328 126 O ATOM 1363 N LYS A 164 7.849 -14.979 22.672 1.00 59.58 N ANISOU 1363 N LYS A 164 10576 3043 9018 -2429 1248 702 N ATOM 1364 CA LYS A 164 7.266 -15.463 23.924 1.00 63.09 C ANISOU 1364 CA LYS A 164 11245 3479 9246 -2794 1362 870 C ATOM 1365 C LYS A 164 6.139 -14.564 24.414 1.00 62.17 C ANISOU 1365 C LYS A 164 10572 3958 9094 -3132 1440 765 C ATOM 1366 O LYS A 164 5.595 -14.775 25.501 1.00 64.63 O ANISOU 1366 O LYS A 164 10956 4389 9211 -3438 1551 887 O ATOM 1367 CB LYS A 164 8.340 -15.620 24.999 1.00 63.46 C ANISOU 1367 CB LYS A 164 11562 3347 9202 -2386 1310 1118 C ATOM 1368 CG LYS A 164 9.235 -16.823 24.801 1.00 67.36 C ANISOU 1368 CG LYS A 164 12742 3215 9636 -2129 1269 1268 C ATOM 1369 CD LYS A 164 8.696 -18.064 25.513 1.00 74.50 C ANISOU 1369 CD LYS A 164 14301 3719 10287 -2562 1389 1463 C ATOM 1370 CE LYS A 164 9.464 -19.326 25.103 1.00 80.51 C ANISOU 1370 CE LYS A 164 15821 3778 10991 -2312 1345 1571 C ATOM 1371 NZ LYS A 164 10.917 -19.027 24.838 1.00 78.57 N ANISOU 1371 NZ LYS A 164 15499 3489 10865 -1525 1185 1591 N ATOM 1372 N CYS A 165 5.775 -13.583 23.589 1.00 59.16 N ANISOU 1372 N CYS A 165 9650 3952 8877 -3064 1385 538 N ATOM 1373 CA CYS A 165 4.884 -12.496 23.999 1.00 57.47 C ANISOU 1373 CA CYS A 165 8846 4338 8653 -3196 1421 413 C ATOM 1374 C CYS A 165 3.414 -12.641 23.566 1.00 60.06 C ANISOU 1374 C CYS A 165 8934 4983 8904 -3753 1523 239 C ATOM 1375 O CYS A 165 2.554 -11.901 24.044 1.00 60.03 O ANISOU 1375 O CYS A 165 8471 5503 8836 -3894 1580 144 O ATOM 1376 CB CYS A 165 5.457 -11.156 23.537 1.00 53.46 C ANISOU 1376 CB CYS A 165 7886 4074 8351 -2702 1281 293 C ATOM 1377 SG CYS A 165 6.887 -10.616 24.508 1.00 49.12 S ANISOU 1377 SG CYS A 165 7396 3436 7831 -2161 1180 468 S ATOM 1378 N GLU A 166 3.124 -13.590 22.681 1.00 62.35 N ANISOU 1378 N GLU A 166 9524 4984 9183 -4062 1543 183 N ATOM 1379 CA GLU A 166 1.738 -13.866 22.277 1.00 65.49 C ANISOU 1379 CA GLU A 166 9716 5691 9478 -4660 1633 17 C ATOM 1380 C GLU A 166 0.772 -14.058 23.471 1.00 68.10 C ANISOU 1380 C GLU A 166 9949 6354 9570 -5153 1809 92 C ATOM 1381 O GLU A 166 -0.291 -13.425 23.510 1.00 67.80 O ANISOU 1381 O GLU A 166 9355 6929 9477 -5373 1860 -73 O ATOM 1382 CB GLU A 166 1.668 -15.071 21.327 1.00 69.01 C ANISOU 1382 CB GLU A 166 10645 5673 9901 -4984 1635 -28 C ATOM 1383 CG GLU A 166 1.902 -14.733 19.859 1.00 69.16 C ANISOU 1383 CG GLU A 166 10502 5677 10098 -4723 1495 -230 C ATOM 1384 CD GLU A 166 1.997 -15.979 18.988 1.00 73.91 C ANISOU 1384 CD GLU A 166 11671 5749 10661 -4982 1491 -276 C ATOM 1385 OE1 GLU A 166 1.582 -17.066 19.445 1.00 79.80 O ANISOU 1385 OE1 GLU A 166 12877 6208 11234 -5492 1603 -190 O ATOM 1386 OE2 GLU A 166 2.499 -15.874 17.848 1.00 74.12 O ANISOU 1386 OE2 GLU A 166 11716 5631 10815 -4680 1380 -400 O ATOM 1387 N PRO A 167 1.145 -14.914 24.449 1.00 70.47 N ANISOU 1387 N PRO A 167 10784 6281 9711 -5300 1902 344 N ATOM 1388 CA PRO A 167 0.292 -15.094 25.623 1.00 73.93 C ANISOU 1388 CA PRO A 167 11152 7043 9895 -5770 2085 440 C ATOM 1389 C PRO A 167 0.020 -13.821 26.430 1.00 71.63 C ANISOU 1389 C PRO A 167 10247 7388 9583 -5511 2102 379 C ATOM 1390 O PRO A 167 -1.126 -13.595 26.831 1.00 73.18 O ANISOU 1390 O PRO A 167 10042 8146 9618 -5910 2238 282 O ATOM 1391 CB PRO A 167 1.073 -16.105 26.467 1.00 76.79 C ANISOU 1391 CB PRO A 167 12259 6803 10115 -5775 2132 756 C ATOM 1392 CG PRO A 167 1.832 -16.901 25.466 1.00 77.09 C ANISOU 1392 CG PRO A 167 12827 6181 10284 -5614 2022 765 C ATOM 1393 CD PRO A 167 2.260 -15.886 24.448 1.00 71.36 C ANISOU 1393 CD PRO A 167 11628 5654 9831 -5095 1855 548 C ATOM 1394 N LEU A 168 1.046 -12.994 26.667 1.00 66.93 N ANISOU 1394 N LEU A 168 9570 6728 9133 -4862 1969 419 N ATOM 1395 CA LEU A 168 0.828 -11.779 27.443 1.00 65.59 C ANISOU 1395 CA LEU A 168 8885 7103 8934 -4606 1974 342 C ATOM 1396 C LEU A 168 -0.073 -10.784 26.689 1.00 64.73 C ANISOU 1396 C LEU A 168 8115 7554 8926 -4573 1938 45 C ATOM 1397 O LEU A 168 -0.913 -10.110 27.295 1.00 65.80 O ANISOU 1397 O LEU A 168 7797 8268 8935 -4647 2025 -66 O ATOM 1398 CB LEU A 168 2.161 -11.133 27.868 1.00 61.52 C ANISOU 1398 CB LEU A 168 8461 6375 8540 -3968 1827 443 C ATOM 1399 CG LEU A 168 2.155 -9.976 28.876 1.00 59.54 C ANISOU 1399 CG LEU A 168 7831 6564 8226 -3684 1822 395 C ATOM 1400 CD1 LEU A 168 1.454 -10.309 30.186 1.00 61.11 C ANISOU 1400 CD1 LEU A 168 8060 7051 8109 -4051 2014 501 C ATOM 1401 CD2 LEU A 168 3.587 -9.517 29.149 1.00 54.82 C ANISOU 1401 CD2 LEU A 168 7395 5682 7752 -3122 1654 497 C ATOM 1402 N GLU A 169 0.092 -10.721 25.369 1.00 63.66 N ANISOU 1402 N GLU A 169 7938 7258 8992 -4444 1811 -83 N ATOM 1403 CA GLU A 169 -0.691 -9.835 24.518 1.00 64.01 C ANISOU 1403 CA GLU A 169 7414 7779 9127 -4366 1746 -347 C ATOM 1404 C GLU A 169 -2.178 -10.170 24.581 1.00 69.46 C ANISOU 1404 C GLU A 169 7784 8993 9613 -4952 1895 -477 C ATOM 1405 O GLU A 169 -3.033 -9.272 24.642 1.00 69.61 O ANISOU 1405 O GLU A 169 7227 9636 9587 -4876 1905 -665 O ATOM 1406 CB GLU A 169 -0.206 -9.954 23.084 1.00 62.24 C ANISOU 1406 CB GLU A 169 7311 7229 9109 -4194 1596 -423 C ATOM 1407 CG GLU A 169 -0.982 -9.122 22.086 1.00 63.01 C ANISOU 1407 CG GLU A 169 6880 7778 9282 -4103 1508 -676 C ATOM 1408 CD GLU A 169 -0.660 -9.503 20.662 1.00 64.49 C ANISOU 1408 CD GLU A 169 7241 7658 9606 -4072 1392 -744 C ATOM 1409 OE1 GLU A 169 -0.377 -10.691 20.396 1.00 65.94 O ANISOU 1409 OE1 GLU A 169 7902 7397 9756 -4364 1431 -659 O ATOM 1410 OE2 GLU A 169 -0.662 -8.598 19.802 1.00 66.00 O ANISOU 1410 OE2 GLU A 169 7122 8031 9924 -3731 1257 -881 O ATOM 1411 N LYS A 170 -2.474 -11.469 24.579 1.00 73.93 N ANISOU 1411 N LYS A 170 8737 9308 10043 -5534 2010 -379 N ATOM 1412 CA LYS A 170 -3.842 -11.933 24.648 1.00 80.08 C ANISOU 1412 CA LYS A 170 9251 10571 10607 -6198 2164 -486 C ATOM 1413 C LYS A 170 -4.387 -11.708 26.055 1.00 83.37 C ANISOU 1413 C LYS A 170 9452 11442 10782 -6368 2349 -414 C ATOM 1414 O LYS A 170 -5.578 -11.459 26.217 1.00 86.99 O ANISOU 1414 O LYS A 170 9387 12591 11075 -6686 2460 -574 O ATOM 1415 CB LYS A 170 -3.933 -13.406 24.238 1.00 83.26 C ANISOU 1415 CB LYS A 170 10211 10498 10926 -6811 2230 -397 C ATOM 1416 CG LYS A 170 -5.465 -13.850 24.196 0.00114.53 C ANISOU 1416 CG LYS A 170 13813 15054 14650 -7598 2386 -547 C ATOM 1417 CD LYS A 170 -6.375 -13.234 23.112 0.00116.23 C ANISOU 1417 CD LYS A 170 13368 15875 14918 -7612 2286 -866 C ATOM 1418 CE LYS A 170 -5.934 -13.589 21.688 0.00115.53 C ANISOU 1418 CE LYS A 170 13545 15337 15016 -7521 2105 -964 C ATOM 1419 NZ LYS A 170 -4.832 -12.704 21.203 0.00108.30 N ANISOU 1419 NZ LYS A 170 12650 14132 14368 -6690 1913 -955 N ATOM 1420 N GLN A 171 -3.521 -11.777 27.069 1.00 83.27 N ANISOU 1420 N GLN A 171 9814 11093 10730 -6139 2379 -184 N ATOM 1421 CA GLN A 171 -3.964 -11.542 28.451 1.00 86.57 C ANISOU 1421 CA GLN A 171 10059 11937 10894 -6266 2554 -109 C ATOM 1422 C GLN A 171 -4.153 -10.048 28.747 1.00 84.81 C ANISOU 1422 C GLN A 171 9222 12282 10720 -5723 2494 -306 C ATOM 1423 O GLN A 171 -4.751 -9.688 29.758 1.00 87.19 O ANISOU 1423 O GLN A 171 9234 13097 10796 -5806 2643 -330 O ATOM 1424 CB GLN A 171 -3.045 -12.222 29.476 1.00 86.74 C ANISOU 1424 CB GLN A 171 10725 11428 10805 -6254 2608 214 C ATOM 1425 CG GLN A 171 -3.606 -12.077 30.876 0.00113.76 C ANISOU 1425 CG GLN A 171 13982 15326 13915 -6465 2810 293 C ATOM 1426 CD GLN A 171 -5.080 -12.491 31.050 0.00120.75 C ANISOU 1426 CD GLN A 171 14528 16821 14531 -7200 3044 203 C ATOM 1427 OE1 GLN A 171 -5.448 -13.666 30.897 0.00124.18 O ANISOU 1427 OE1 GLN A 171 15330 17018 14836 -7859 3161 325 O ATOM 1428 NE2 GLN A 171 -5.921 -11.520 31.401 0.00121.62 N ANISOU 1428 NE2 GLN A 171 13941 17730 14539 -7091 3117 -16 N ATOM 1429 N HIS A 172 -3.639 -9.190 27.859 1.00 81.86 N ANISOU 1429 N HIS A 172 8684 11798 10622 -5171 2281 -445 N ATOM 1430 CA HIS A 172 -3.951 -7.748 27.853 1.00 81.04 C ANISOU 1430 CA HIS A 172 8011 12200 10582 -4671 2198 -673 C ATOM 1431 C HIS A 172 -5.243 -7.438 27.084 1.00 84.19 C ANISOU 1431 C HIS A 172 7825 13226 10936 -4845 2212 -939 C ATOM 1432 O HIS A 172 -6.063 -6.636 27.542 1.00 86.07 O ANISOU 1432 O HIS A 172 7545 14117 11040 -4712 2273 -1114 O ATOM 1433 CB HIS A 172 -2.802 -6.920 27.261 1.00 75.66 C ANISOU 1433 CB HIS A 172 7446 11106 10194 -4018 1964 -685 C ATOM 1434 CG HIS A 172 -1.698 -6.630 28.228 1.00 73.72 C ANISOU 1434 CG HIS A 172 7503 10546 9961 -3676 1927 -521 C ATOM 1435 ND1 HIS A 172 -0.423 -6.300 27.822 1.00 69.78 N ANISOU 1435 ND1 HIS A 172 7267 9553 9695 -3240 1744 -447 N ATOM 1436 CD2 HIS A 172 -1.675 -6.621 29.582 1.00 75.10 C ANISOU 1436 CD2 HIS A 172 7742 10870 9922 -3719 2046 -423 C ATOM 1437 CE1 HIS A 172 0.336 -6.098 28.883 1.00 68.45 C ANISOU 1437 CE1 HIS A 172 7293 9253 9461 -3034 1739 -319 C ATOM 1438 NE2 HIS A 172 -0.400 -6.287 29.963 1.00 71.88 N ANISOU 1438 NE2 HIS A 172 7628 10058 9624 -3306 1917 -301 N ATOM 1439 N GLU A 173 -5.402 -8.075 25.919 1.00 85.52 N ANISOU 1439 N GLU A 173 8082 13209 11203 -5112 2145 -979 N ATOM 1440 CA GLU A 173 -6.580 -7.918 25.048 1.00 88.49 C ANISOU 1440 CA GLU A 173 7929 14161 11531 -5314 2127 -1226 C ATOM 1441 C GLU A 173 -7.903 -8.185 25.762 1.00 94.23 C ANISOU 1441 C GLU A 173 8225 15634 11945 -5838 2349 -1315 C ATOM 1442 O GLU A 173 -8.860 -7.428 25.599 1.00 96.14 O ANISOU 1442 O GLU A 173 7827 16599 12102 -5699 2342 -1552 O ATOM 1443 CB GLU A 173 -6.461 -8.823 23.818 1.00 88.62 C ANISOU 1443 CB GLU A 173 8231 13785 11655 -5638 2042 -1225 C ATOM 1444 CG GLU A 173 -5.570 -8.280 22.713 1.00 84.91 C ANISOU 1444 CG GLU A 173 7899 12892 11470 -5086 1805 -1257 C ATOM 1445 CD GLU A 173 -5.492 -9.204 21.505 1.00 86.67 C ANISOU 1445 CD GLU A 173 8406 12761 11762 -5407 1733 -1279 C ATOM 1446 OE1 GLU A 173 -4.395 -9.365 20.934 1.00 84.29 O ANISOU 1446 OE1 GLU A 173 8537 11838 11651 -5127 1617 -1179 O ATOM 1447 OE2 GLU A 173 -6.530 -9.777 21.118 1.00 93.09 O ANISOU 1447 OE2 GLU A 173 9002 13943 12425 -5951 1792 -1410 O ATOM 1448 N LYS A 174 -7.946 -9.266 26.544 1.00 97.73 N ANISOU 1448 N LYS A 174 9027 15908 12199 -6432 2546 -1119 N ATOM 1449 CA LYS A 174 -9.115 -9.621 27.349 1.00103.68 C ANISOU 1449 CA LYS A 174 9429 17346 12618 -7013 2795 -1157 C ATOM 1450 C LYS A 174 -9.440 -8.546 28.388 1.00104.12 C ANISOU 1450 C LYS A 174 9026 18002 12532 -6597 2879 -1250 C ATOM 1451 O LYS A 174 -10.603 -8.340 28.742 1.00108.37 O ANISOU 1451 O LYS A 174 8978 19372 12825 -6835 3031 -1415 O ATOM 1452 CB LYS A 174 -8.950 -10.934 27.897 0.00130.24 C ANISOU 1452 CB LYS A 174 13365 20295 15826 -7679 2966 -901 C ATOM 1453 CG LYS A 174 -10.141 -11.855 27.691 0.00136.23 C ANISOU 1453 CG LYS A 174 13932 21483 16345 -8576 3137 -968 C ATOM 1454 CD LYS A 174 -10.161 -12.971 28.722 0.00140.78 C ANISOU 1454 CD LYS A 174 15014 21820 16656 -9258 3383 -686 C ATOM 1455 CE LYS A 174 -9.235 -14.109 28.324 0.00140.38 C ANISOU 1455 CE LYS A 174 15865 20743 16729 -9481 3314 -449 C ATOM 1456 NZ LYS A 174 -9.026 -15.072 29.440 0.00143.13 N ANISOU 1456 NZ LYS A 174 16823 20730 16829 -9965 3522 -123 N ATOM 1457 N GLU A 175 -8.400 -7.879 28.882 1.00100.02 N ANISOU 1457 N GLU A 175 8776 17077 12151 -5983 2780 -1154 N ATOM 1458 CA GLU A 175 -8.557 -6.711 29.739 1.00 99.78 C ANISOU 1458 CA GLU A 175 8371 17513 12027 -5468 2807 -1279 C ATOM 1459 C GLU A 175 -8.891 -5.463 28.917 1.00 97.88 C ANISOU 1459 C GLU A 175 7622 17622 11946 -4857 2616 -1569 C ATOM 1460 O GLU A 175 -9.615 -4.585 29.379 1.00 99.96 O ANISOU 1460 O GLU A 175 7370 18550 12060 -4567 2669 -1774 O ATOM 1461 CB GLU A 175 -7.278 -6.460 30.533 1.00 96.32 C ANISOU 1461 CB GLU A 175 8435 16488 11673 -5064 2747 -1082 C ATOM 1462 CG GLU A 175 -7.145 -7.279 31.793 1.00 98.93 C ANISOU 1462 CG GLU A 175 9117 16737 11735 -5487 2962 -836 C ATOM 1463 CD GLU A 175 -6.258 -6.593 32.802 1.00 96.54 C ANISOU 1463 CD GLU A 175 9020 16243 11420 -4975 2914 -759 C ATOM 1464 OE1 GLU A 175 -5.263 -5.952 32.386 1.00 92.47 O ANISOU 1464 OE1 GLU A 175 8683 15271 11179 -4423 2686 -770 O ATOM 1465 OE2 GLU A 175 -6.558 -6.685 34.010 1.00 99.81 O ANISOU 1465 OE2 GLU A 175 9407 16985 11531 -5145 3107 -692 O TER 1466 GLU A 175 ATOM 1467 N ILE B 2 14.394 -3.047 70.447 1.00 89.10 N ANISOU 1467 N ILE B 2 12680 13435 7741 -2308 -528 1016 N ATOM 1468 CA ILE B 2 14.452 -3.412 69.000 1.00 85.90 C ANISOU 1468 CA ILE B 2 12249 12601 7788 -2202 -498 1075 C ATOM 1469 C ILE B 2 15.702 -2.806 68.345 1.00 83.17 C ANISOU 1469 C ILE B 2 11557 12173 7872 -1723 -740 925 C ATOM 1470 O ILE B 2 15.809 -1.581 68.233 1.00 81.03 O ANISOU 1470 O ILE B 2 10802 12137 7847 -1676 -718 590 O ATOM 1471 CB ILE B 2 13.162 -2.973 68.237 1.00 83.29 C ANISOU 1471 CB ILE B 2 11604 12366 7677 -2543 -160 863 C ATOM 1472 CG1 ILE B 2 11.903 -3.357 69.032 1.00 87.33 C ANISOU 1472 CG1 ILE B 2 12294 13183 7705 -3075 107 918 C ATOM 1473 CG2 ILE B 2 13.130 -3.573 66.828 1.00 80.27 C ANISOU 1473 CG2 ILE B 2 11306 11538 7657 -2497 -126 978 C ATOM 1474 CD1 ILE B 2 10.606 -2.757 68.499 1.00 86.36 C ANISOU 1474 CD1 ILE B 2 11729 13370 7712 -3359 424 621 C ATOM 1475 N PRO B 3 16.652 -3.660 67.903 1.00 83.87 N ANISOU 1475 N PRO B 3 11911 11937 8018 -1374 -972 1157 N ATOM 1476 CA PRO B 3 17.893 -3.161 67.305 1.00 81.99 C ANISOU 1476 CA PRO B 3 11298 11733 8122 -948 -1192 1009 C ATOM 1477 C PRO B 3 17.624 -2.477 65.965 1.00 77.14 C ANISOU 1477 C PRO B 3 10277 11008 8025 -1012 -1016 795 C ATOM 1478 O PRO B 3 16.577 -2.709 65.359 1.00 75.73 O ANISOU 1478 O PRO B 3 10190 10640 7943 -1280 -774 825 O ATOM 1479 CB PRO B 3 18.721 -4.433 67.109 1.00 84.67 C ANISOU 1479 CB PRO B 3 12079 11761 8330 -546 -1442 1314 C ATOM 1480 CG PRO B 3 17.714 -5.501 66.924 1.00 85.84 C ANISOU 1480 CG PRO B 3 12811 11501 8304 -837 -1268 1588 C ATOM 1481 CD PRO B 3 16.555 -5.130 67.811 1.00 86.87 C ANISOU 1481 CD PRO B 3 12964 11890 8152 -1370 -1023 1543 C ATOM 1482 N LEU B 4 18.568 -1.655 65.514 1.00 75.41 N ANISOU 1482 N LEU B 4 9624 10932 8095 -797 -1142 583 N ATOM 1483 CA LEU B 4 18.377 -0.782 64.343 1.00 71.29 C ANISOU 1483 CA LEU B 4 8728 10337 8023 -885 -990 362 C ATOM 1484 C LEU B 4 18.208 -1.525 63.036 1.00 68.89 C ANISOU 1484 C LEU B 4 8539 9671 7965 -808 -901 505 C ATOM 1485 O LEU B 4 17.581 -1.027 62.102 1.00 66.14 O ANISOU 1485 O LEU B 4 8017 9208 7906 -960 -714 383 O ATOM 1486 CB LEU B 4 19.545 0.207 64.195 1.00 71.08 C ANISOU 1486 CB LEU B 4 8273 10552 8184 -751 -1154 130 C ATOM 1487 CG LEU B 4 19.926 1.117 65.370 1.00 73.89 C ANISOU 1487 CG LEU B 4 8460 11280 8334 -836 -1279 -81 C ATOM 1488 CD1 LEU B 4 21.050 2.072 64.955 1.00 73.42 C ANISOU 1488 CD1 LEU B 4 7983 11419 8493 -817 -1411 -317 C ATOM 1489 CD2 LEU B 4 18.712 1.881 65.931 1.00 74.24 C ANISOU 1489 CD2 LEU B 4 8546 11369 8294 -1132 -1078 -259 C ATOM 1490 N CYS B 5 18.783 -2.714 62.965 1.00 70.64 N ANISOU 1490 N CYS B 5 9083 9706 8051 -530 -1058 750 N ATOM 1491 CA CYS B 5 18.791 -3.466 61.723 1.00 69.03 C ANISOU 1491 CA CYS B 5 9016 9152 8060 -393 -1013 860 C ATOM 1492 C CYS B 5 17.584 -4.381 61.549 1.00 68.89 C ANISOU 1492 C CYS B 5 9471 8787 7919 -676 -830 1052 C ATOM 1493 O CYS B 5 17.513 -5.130 60.579 1.00 68.45 O ANISOU 1493 O CYS B 5 9622 8396 7988 -593 -800 1150 O ATOM 1494 CB CYS B 5 20.111 -4.224 61.587 1.00 71.78 C ANISOU 1494 CB CYS B 5 9452 9483 8338 132 -1295 965 C ATOM 1495 SG CYS B 5 21.497 -3.087 61.299 1.00 72.04 S ANISOU 1495 SG CYS B 5 8767 10008 8597 349 -1441 676 S ATOM 1496 N ALA B 6 16.637 -4.301 62.484 1.00 69.44 N ANISOU 1496 N ALA B 6 9691 8978 7716 -1045 -700 1079 N ATOM 1497 CA ALA B 6 15.434 -5.132 62.466 1.00 69.91 C ANISOU 1497 CA ALA B 6 10165 8820 7579 -1443 -504 1243 C ATOM 1498 C ALA B 6 14.689 -5.042 61.137 1.00 66.18 C ANISOU 1498 C ALA B 6 9516 8195 7433 -1618 -297 1137 C ATOM 1499 O ALA B 6 14.439 -6.063 60.498 1.00 67.08 O ANISOU 1499 O ALA B 6 10018 7942 7526 -1686 -270 1304 O ATOM 1500 CB ALA B 6 14.510 -4.770 63.634 1.00 71.67 C ANISOU 1500 CB ALA B 6 10384 9381 7468 -1851 -352 1199 C ATOM 1501 N ASN B 7 14.366 -3.824 60.713 1.00 62.07 N ANISOU 1501 N ASN B 7 8458 7933 7192 -1667 -176 857 N ATOM 1502 CA ASN B 7 13.616 -3.610 59.467 1.00 58.82 C ANISOU 1502 CA ASN B 7 7846 7437 7067 -1798 3 736 C ATOM 1503 C ASN B 7 14.415 -3.875 58.196 1.00 55.84 C ANISOU 1503 C ASN B 7 7446 6766 7004 -1489 -90 767 C ATOM 1504 O ASN B 7 13.864 -3.823 57.100 1.00 53.26 O ANISOU 1504 O ASN B 7 7008 6339 6890 -1575 37 693 O ATOM 1505 CB ASN B 7 13.037 -2.188 59.414 1.00 56.91 C ANISOU 1505 CB ASN B 7 7111 7526 6987 -1865 124 426 C ATOM 1506 CG ASN B 7 11.967 -1.956 60.456 1.00 60.76 C ANISOU 1506 CG ASN B 7 7561 8368 7156 -2178 273 334 C ATOM 1507 OD1 ASN B 7 11.823 -0.844 60.970 1.00 64.04 O ANISOU 1507 OD1 ASN B 7 7685 9076 7572 -2124 287 94 O ATOM 1508 ND2 ASN B 7 11.216 -3.002 60.785 1.00 62.06 N ANISOU 1508 ND2 ASN B 7 8045 8521 7014 -2527 389 509 N ATOM 1509 N LEU B 8 15.710 -4.148 58.345 1.00 55.86 N ANISOU 1509 N LEU B 8 7522 6695 7005 -1112 -314 853 N ATOM 1510 CA LEU B 8 16.570 -4.379 57.190 1.00 54.15 C ANISOU 1510 CA LEU B 8 7226 6305 7044 -779 -400 848 C ATOM 1511 C LEU B 8 16.689 -5.841 56.759 1.00 56.06 C ANISOU 1511 C LEU B 8 7998 6134 7168 -627 -472 1060 C ATOM 1512 O LEU B 8 17.326 -6.154 55.750 1.00 55.53 O ANISOU 1512 O LEU B 8 7898 5922 7280 -326 -532 1039 O ATOM 1513 CB LEU B 8 17.923 -3.704 57.397 1.00 54.47 C ANISOU 1513 CB LEU B 8 6915 6612 7168 -448 -586 743 C ATOM 1514 CG LEU B 8 17.609 -2.212 57.216 1.00 52.44 C ANISOU 1514 CG LEU B 8 6202 6595 7130 -669 -461 501 C ATOM 1515 CD1 LEU B 8 18.725 -1.307 57.596 1.00 54.38 C ANISOU 1515 CD1 LEU B 8 6097 7146 7417 -542 -606 357 C ATOM 1516 CD2 LEU B 8 17.244 -1.978 55.778 1.00 51.18 C ANISOU 1516 CD2 LEU B 8 5902 6279 7266 -718 -317 429 C ATOM 1517 N VAL B 9 16.033 -6.716 57.509 1.00 58.21 N ANISOU 1517 N VAL B 9 8791 6213 7113 -867 -456 1252 N ATOM 1518 CA VAL B 9 15.979 -8.137 57.199 1.00 60.97 C ANISOU 1518 CA VAL B 9 9807 6071 7288 -813 -523 1465 C ATOM 1519 C VAL B 9 14.878 -8.375 56.167 1.00 59.64 C ANISOU 1519 C VAL B 9 9684 5722 7254 -1209 -296 1412 C ATOM 1520 O VAL B 9 13.728 -7.989 56.398 1.00 58.87 O ANISOU 1520 O VAL B 9 9435 5832 7100 -1712 -85 1348 O ATOM 1521 CB VAL B 9 15.698 -8.977 58.479 1.00 65.31 C ANISOU 1521 CB VAL B 9 10996 6454 7366 -1003 -598 1720 C ATOM 1522 CG1 VAL B 9 15.596 -10.474 58.152 1.00 68.90 C ANISOU 1522 CG1 VAL B 9 12292 6286 7602 -993 -680 1954 C ATOM 1523 CG2 VAL B 9 16.764 -8.723 59.533 1.00 66.35 C ANISOU 1523 CG2 VAL B 9 11065 6817 7329 -591 -845 1762 C ATOM 1524 N PRO B 10 15.220 -9.014 55.031 1.00 59.75 N ANISOU 1524 N PRO B 10 9880 5404 7418 -967 -345 1413 N ATOM 1525 CA PRO B 10 14.230 -9.380 54.014 1.00 58.97 C ANISOU 1525 CA PRO B 10 9885 5111 7409 -1332 -163 1363 C ATOM 1526 C PRO B 10 12.964 -10.014 54.610 1.00 61.57 C ANISOU 1526 C PRO B 10 10644 5336 7413 -1992 -14 1486 C ATOM 1527 O PRO B 10 13.036 -10.753 55.594 1.00 65.25 O ANISOU 1527 O PRO B 10 11676 5589 7525 -2088 -106 1704 O ATOM 1528 CB PRO B 10 14.976 -10.412 53.163 1.00 60.96 C ANISOU 1528 CB PRO B 10 10582 4896 7686 -912 -320 1423 C ATOM 1529 CG PRO B 10 16.394 -10.001 53.261 1.00 61.00 C ANISOU 1529 CG PRO B 10 10278 5097 7803 -262 -521 1370 C ATOM 1530 CD PRO B 10 16.567 -9.494 54.672 1.00 61.43 C ANISOU 1530 CD PRO B 10 10221 5445 7674 -310 -588 1440 C ATOM 1531 N VAL B 11 11.815 -9.692 54.019 1.00 59.95 N ANISOU 1531 N VAL B 11 10150 5333 7296 -2454 212 1339 N ATOM 1532 CA VAL B 11 10.531 -10.245 54.444 1.00 62.88 C ANISOU 1532 CA VAL B 11 10802 5742 7346 -3169 391 1401 C ATOM 1533 C VAL B 11 9.959 -11.039 53.286 1.00 63.74 C ANISOU 1533 C VAL B 11 11186 5543 7489 -3440 461 1368 C ATOM 1534 O VAL B 11 9.826 -10.512 52.183 1.00 60.41 O ANISOU 1534 O VAL B 11 10312 5267 7375 -3303 516 1168 O ATOM 1535 CB VAL B 11 9.508 -9.150 54.846 1.00 61.40 C ANISOU 1535 CB VAL B 11 9949 6223 7157 -3521 606 1195 C ATOM 1536 CG1 VAL B 11 8.305 -9.766 55.558 1.00 65.47 C ANISOU 1536 CG1 VAL B 11 10733 6901 7240 -4279 792 1268 C ATOM 1537 CG2 VAL B 11 10.159 -8.078 55.729 1.00 59.77 C ANISOU 1537 CG2 VAL B 11 9347 6342 7021 -3157 528 1137 C ATOM 1538 N PRO B 12 9.625 -12.314 53.529 1.00 68.61 N ANISOU 1538 N PRO B 12 12600 5709 7761 -3845 448 1566 N ATOM 1539 CA PRO B 12 9.011 -13.126 52.492 1.00 70.69 C ANISOU 1539 CA PRO B 12 13193 5663 8004 -4203 514 1518 C ATOM 1540 C PRO B 12 7.808 -12.436 51.861 1.00 68.47 C ANISOU 1540 C PRO B 12 12212 5965 7839 -4655 752 1252 C ATOM 1541 O PRO B 12 7.027 -11.801 52.561 1.00 68.65 O ANISOU 1541 O PRO B 12 11791 6561 7731 -5014 914 1172 O ATOM 1542 CB PRO B 12 8.554 -14.372 53.261 1.00 76.80 C ANISOU 1542 CB PRO B 12 14894 6007 8278 -4810 519 1775 C ATOM 1543 CG PRO B 12 9.503 -14.477 54.372 1.00 78.28 C ANISOU 1543 CG PRO B 12 15442 5994 8305 -4383 326 2005 C ATOM 1544 CD PRO B 12 9.816 -13.075 54.778 1.00 73.29 C ANISOU 1544 CD PRO B 12 13899 6018 7931 -4010 357 1851 C ATOM 1545 N ILE B 13 7.660 -12.578 50.550 1.00 67.37 N ANISOU 1545 N ILE B 13 11979 5709 7909 -4598 760 1101 N ATOM 1546 CA ILE B 13 6.524 -11.991 49.859 1.00 65.88 C ANISOU 1546 CA ILE B 13 11154 6076 7801 -4966 946 840 C ATOM 1547 C ILE B 13 5.400 -13.019 49.739 1.00 71.16 C ANISOU 1547 C ILE B 13 12235 6687 8117 -5831 1078 840 C ATOM 1548 O ILE B 13 5.422 -13.923 48.900 1.00 73.27 O ANISOU 1548 O ILE B 13 13005 6474 8359 -5961 1021 847 O ATOM 1549 CB ILE B 13 6.938 -11.340 48.515 1.00 61.45 C ANISOU 1549 CB ILE B 13 10136 5559 7651 -4424 888 652 C ATOM 1550 CG1 ILE B 13 7.989 -10.259 48.789 1.00 57.34 C ANISOU 1550 CG1 ILE B 13 9207 5166 7414 -3729 787 656 C ATOM 1551 CG2 ILE B 13 5.728 -10.749 47.815 1.00 60.29 C ANISOU 1551 CG2 ILE B 13 9369 5996 7542 -4754 1045 386 C ATOM 1552 CD1 ILE B 13 8.594 -9.595 47.557 1.00 54.55 C ANISOU 1552 CD1 ILE B 13 8477 4824 7426 -3200 727 519 C ATOM 1553 N THR B 14 4.435 -12.882 50.639 1.00 73.77 N ANISOU 1553 N THR B 14 12363 7531 8136 -6450 1257 820 N ATOM 1554 CA THR B 14 3.239 -13.691 50.632 1.00 79.06 C ANISOU 1554 CA THR B 14 13264 8358 8419 -7407 1429 781 C ATOM 1555 C THR B 14 2.191 -12.875 49.893 1.00 77.19 C ANISOU 1555 C THR B 14 12098 8940 8291 -7560 1576 420 C ATOM 1556 O THR B 14 2.482 -11.766 49.422 1.00 70.89 O ANISOU 1556 O THR B 14 10647 8430 7859 -6891 1521 255 O ATOM 1557 CB THR B 14 2.759 -14.014 52.068 1.00 83.83 C ANISOU 1557 CB THR B 14 14135 9168 8548 -8046 1563 952 C ATOM 1558 OG1 THR B 14 2.020 -12.906 52.599 1.00 82.93 O ANISOU 1558 OG1 THR B 14 13100 10008 8402 -8114 1738 728 O ATOM 1559 CG2 THR B 14 3.941 -14.310 52.977 1.00 84.33 C ANISOU 1559 CG2 THR B 14 14856 8617 8568 -7589 1377 1280 C ATOM 1560 N ASN B 15 0.977 -13.410 49.803 1.00 81.52 N ANISOU 1560 N ASN B 15 12601 9881 8491 -8444 1753 295 N ATOM 1561 CA ASN B 15 -0.096 -12.722 49.095 1.00 81.26 C ANISOU 1561 CA ASN B 15 11673 10708 8496 -8592 1872 -75 C ATOM 1562 C ASN B 15 -0.699 -11.525 49.848 1.00 80.43 C ANISOU 1562 C ASN B 15 10679 11546 8336 -8451 2000 -278 C ATOM 1563 O ASN B 15 -1.122 -10.541 49.215 1.00 77.56 O ANISOU 1563 O ASN B 15 9534 11762 8174 -8044 1992 -572 O ATOM 1564 CB ASN B 15 -1.151 -13.721 48.620 1.00 87.57 C ANISOU 1564 CB ASN B 15 12677 11662 8935 -9582 1998 -187 C ATOM 1565 CG ASN B 15 -0.634 -14.608 47.496 1.00 87.95 C ANISOU 1565 CG ASN B 15 13408 10877 9132 -9520 1841 -120 C ATOM 1566 OD1 ASN B 15 0.120 -14.160 46.612 1.00 82.55 O ANISOU 1566 OD1 ASN B 15 12599 9899 8869 -8711 1678 -163 O ATOM 1567 ND2 ASN B 15 -1.026 -15.870 47.527 1.00 94.33 N ANISOU 1567 ND2 ASN B 15 14978 11295 9568 -10393 1891 -23 N ATOM 1568 N ALA B 16 -0.717 -11.599 51.185 1.00 82.99 N ANISOU 1568 N ALA B 16 11166 11999 8367 -8734 2100 -127 N ATOM 1569 CA ALA B 16 -1.040 -10.435 52.023 1.00 81.83 C ANISOU 1569 CA ALA B 16 10284 12622 8185 -8445 2188 -302 C ATOM 1570 C ALA B 16 -0.054 -9.282 51.740 1.00 75.04 C ANISOU 1570 C ALA B 16 9147 11531 7833 -7367 1993 -331 C ATOM 1571 O ALA B 16 -0.460 -8.139 51.518 1.00 73.33 O ANISOU 1571 O ALA B 16 8190 11911 7762 -6936 1999 -619 O ATOM 1572 CB ALA B 16 -1.047 -10.816 53.513 1.00 85.35 C ANISOU 1572 CB ALA B 16 11088 13125 8217 -8914 2309 -89 C ATOM 1573 N THR B 17 1.239 -9.598 51.716 1.00 71.87 N ANISOU 1573 N THR B 17 9365 10270 7673 -6941 1810 -43 N ATOM 1574 CA THR B 17 2.265 -8.627 51.374 1.00 65.66 C ANISOU 1574 CA THR B 17 8377 9232 7337 -6037 1631 -52 C ATOM 1575 C THR B 17 1.930 -7.965 50.034 1.00 62.75 C ANISOU 1575 C THR B 17 7493 9091 7258 -5699 1592 -311 C ATOM 1576 O THR B 17 1.971 -6.729 49.910 1.00 59.48 O ANISOU 1576 O THR B 17 6550 8993 7058 -5157 1546 -490 O ATOM 1577 CB THR B 17 3.675 -9.276 51.324 1.00 64.04 C ANISOU 1577 CB THR B 17 8899 8128 7307 -5683 1439 263 C ATOM 1578 OG1 THR B 17 3.870 -10.091 52.483 1.00 68.53 O ANISOU 1578 OG1 THR B 17 10066 8441 7532 -6054 1454 524 O ATOM 1579 CG2 THR B 17 4.767 -8.220 51.282 1.00 59.03 C ANISOU 1579 CG2 THR B 17 8009 7370 7051 -4867 1284 256 C ATOM 1580 N LEU B 18 1.565 -8.777 49.041 1.00 63.80 N ANISOU 1580 N LEU B 18 7824 9056 7363 -6031 1600 -337 N ATOM 1581 CA LEU B 18 1.237 -8.230 47.735 1.00 61.08 C ANISOU 1581 CA LEU B 18 7034 8926 7246 -5728 1550 -568 C ATOM 1582 C LEU B 18 -0.012 -7.342 47.815 1.00 62.98 C ANISOU 1582 C LEU B 18 6470 10127 7335 -5790 1655 -909 C ATOM 1583 O LEU B 18 -0.047 -6.273 47.188 1.00 60.06 O ANISOU 1583 O LEU B 18 5639 9986 7193 -5203 1567 -1090 O ATOM 1584 CB LEU B 18 1.131 -9.318 46.666 1.00 62.41 C ANISOU 1584 CB LEU B 18 7607 8716 7389 -6073 1524 -543 C ATOM 1585 CG LEU B 18 2.420 -10.059 46.282 1.00 59.79 C ANISOU 1585 CG LEU B 18 8010 7454 7253 -5779 1376 -283 C ATOM 1586 CD1 LEU B 18 2.093 -11.340 45.479 1.00 63.65 C ANISOU 1586 CD1 LEU B 18 9019 7583 7583 -6300 1378 -283 C ATOM 1587 CD2 LEU B 18 3.419 -9.156 45.506 1.00 54.22 C ANISOU 1587 CD2 LEU B 18 7085 6542 6973 -4930 1232 -293 C ATOM 1588 N ASP B 19 -0.991 -7.753 48.628 1.00 67.41 N ANISOU 1588 N ASP B 19 6882 11252 7480 -6468 1836 -996 N ATOM 1589 CA ASP B 19 -2.188 -6.942 48.900 1.00 70.54 C ANISOU 1589 CA ASP B 19 6463 12683 7656 -6505 1948 -1355 C ATOM 1590 C ASP B 19 -1.800 -5.627 49.589 1.00 67.67 C ANISOU 1590 C ASP B 19 5781 12477 7453 -5782 1885 -1426 C ATOM 1591 O ASP B 19 -2.284 -4.560 49.211 1.00 67.11 O ANISOU 1591 O ASP B 19 5131 12908 7461 -5274 1829 -1717 O ATOM 1592 CB ASP B 19 -3.225 -7.704 49.769 1.00 76.76 C ANISOU 1592 CB ASP B 19 7166 14094 7906 -7455 2187 -1421 C ATOM 1593 CG ASP B 19 -4.306 -8.436 48.950 1.00 82.05 C ANISOU 1593 CG ASP B 19 7623 15237 8316 -8157 2279 -1626 C ATOM 1594 OD1 ASP B 19 -4.428 -8.253 47.716 1.00 79.64 O ANISOU 1594 OD1 ASP B 19 7113 14927 8221 -7859 2157 -1775 O ATOM 1595 OD2 ASP B 19 -5.072 -9.212 49.566 1.00 88.70 O ANISOU 1595 OD2 ASP B 19 8501 16506 8696 -9076 2482 -1646 O ATOM 1596 N ARG B 20 -0.927 -5.707 50.594 1.00 67.03 N ANISOU 1596 N ARG B 20 6123 11949 7397 -5722 1875 -1171 N ATOM 1597 CA ARG B 20 -0.490 -4.528 51.349 1.00 64.98 C ANISOU 1597 CA ARG B 20 5644 11786 7259 -5117 1813 -1235 C ATOM 1598 C ARG B 20 0.171 -3.482 50.440 1.00 60.88 C ANISOU 1598 C ARG B 20 5016 10938 7179 -4308 1612 -1294 C ATOM 1599 O ARG B 20 -0.038 -2.284 50.614 1.00 60.41 O ANISOU 1599 O ARG B 20 4566 11214 7174 -3804 1561 -1520 O ATOM 1600 CB ARG B 20 0.437 -4.939 52.506 1.00 64.88 C ANISOU 1600 CB ARG B 20 6168 11299 7184 -5230 1809 -925 C ATOM 1601 CG ARG B 20 1.158 -3.778 53.215 1.00 61.82 C ANISOU 1601 CG ARG B 20 5669 10851 6971 -4600 1704 -958 C ATOM 1602 CD ARG B 20 2.020 -4.258 54.389 1.00 62.99 C ANISOU 1602 CD ARG B 20 6318 10618 6998 -4742 1687 -664 C ATOM 1603 NE ARG B 20 2.712 -3.154 55.075 1.00 61.35 N ANISOU 1603 NE ARG B 20 5994 10383 6933 -4194 1580 -723 N ATOM 1604 CZ ARG B 20 3.360 -3.259 56.238 1.00 61.74 C ANISOU 1604 CZ ARG B 20 6327 10289 6842 -4223 1552 -555 C ATOM 1605 NH1 ARG B 20 3.428 -4.420 56.870 1.00 65.94 N ANISOU 1605 NH1 ARG B 20 7325 10653 7077 -4735 1616 -287 N ATOM 1606 NH2 ARG B 20 3.938 -2.199 56.785 1.00 60.17 N ANISOU 1606 NH2 ARG B 20 5992 10101 6769 -3752 1448 -657 N ATOM 1607 N ILE B 21 0.947 -3.936 49.456 1.00 58.44 N ANISOU 1607 N ILE B 21 5082 9976 7147 -4194 1501 -1100 N ATOM 1608 CA ILE B 21 1.640 -3.012 48.561 1.00 54.55 C ANISOU 1608 CA ILE B 21 4540 9156 7029 -3522 1332 -1118 C ATOM 1609 C ILE B 21 0.827 -2.602 47.313 1.00 55.22 C ANISOU 1609 C ILE B 21 4242 9584 7156 -3337 1290 -1359 C ATOM 1610 O ILE B 21 1.274 -1.760 46.531 1.00 52.92 O ANISOU 1610 O ILE B 21 3919 9067 7122 -2798 1153 -1382 O ATOM 1611 CB ILE B 21 3.092 -3.486 48.220 1.00 51.13 C ANISOU 1611 CB ILE B 21 4653 7900 6872 -3361 1222 -805 C ATOM 1612 CG1 ILE B 21 3.106 -4.769 47.374 1.00 52.20 C ANISOU 1612 CG1 ILE B 21 5139 7710 6987 -3720 1238 -681 C ATOM 1613 CG2 ILE B 21 3.878 -3.676 49.501 1.00 51.44 C ANISOU 1613 CG2 ILE B 21 4994 7702 6849 -3408 1219 -609 C ATOM 1614 CD1 ILE B 21 4.505 -5.167 46.825 1.00 49.55 C ANISOU 1614 CD1 ILE B 21 5263 6649 6916 -3425 1114 -444 C ATOM 1615 N THR B 22 -0.370 -3.166 47.160 1.00 59.06 N ANISOU 1615 N THR B 22 4437 10652 7350 -3803 1403 -1543 N ATOM 1616 CA THR B 22 -1.239 -2.863 46.018 1.00 60.60 C ANISOU 1616 CA THR B 22 4222 11285 7519 -3654 1349 -1799 C ATOM 1617 C THR B 22 -1.773 -1.434 46.106 1.00 61.17 C ANISOU 1617 C THR B 22 3796 11870 7577 -3014 1262 -2090 C ATOM 1618 O THR B 22 -2.323 -1.034 47.139 1.00 63.78 O ANISOU 1618 O THR B 22 3819 12732 7681 -3022 1343 -2267 O ATOM 1619 CB THR B 22 -2.432 -3.852 45.935 1.00 65.82 C ANISOU 1619 CB THR B 22 4640 12558 7811 -4398 1498 -1962 C ATOM 1620 OG1 THR B 22 -1.943 -5.178 45.709 1.00 66.56 O ANISOU 1620 OG1 THR B 22 5317 12061 7910 -4960 1544 -1701 O ATOM 1621 CG2 THR B 22 -3.410 -3.475 44.817 1.00 67.50 C ANISOU 1621 CG2 THR B 22 4327 13374 7946 -4209 1422 -2278 C ATOM 1622 N GLY B 23 -1.614 -0.673 45.024 1.00 59.11 N ANISOU 1622 N GLY B 23 3498 11439 7522 -2446 1090 -2144 N ATOM 1623 CA GLY B 23 -2.151 0.687 44.958 1.00 59.97 C ANISOU 1623 CA GLY B 23 3244 11950 7592 -1765 960 -2423 C ATOM 1624 C GLY B 23 -1.121 1.755 44.613 1.00 56.28 C ANISOU 1624 C GLY B 23 3140 10804 7442 -1133 784 -2277 C ATOM 1625 O GLY B 23 -0.078 1.468 44.014 1.00 52.62 O ANISOU 1625 O GLY B 23 3097 9658 7238 -1176 748 -1994 O ATOM 1626 N LYS B 24 -1.444 2.989 44.986 1.00 57.58 N ANISOU 1626 N LYS B 24 3143 11188 7546 -557 675 -2496 N ATOM 1627 CA LYS B 24 -0.700 4.180 44.589 1.00 55.87 C ANISOU 1627 CA LYS B 24 3275 10400 7551 48 486 -2421 C ATOM 1628 C LYS B 24 0.378 4.529 45.619 1.00 53.16 C ANISOU 1628 C LYS B 24 3283 9551 7364 20 512 -2249 C ATOM 1629 O LYS B 24 0.098 4.629 46.817 1.00 54.94 O ANISOU 1629 O LYS B 24 3350 10095 7431 -48 591 -2384 O ATOM 1630 CB LYS B 24 -1.679 5.357 44.402 1.00 59.85 C ANISOU 1630 CB LYS B 24 3508 11369 7865 743 314 -2777 C ATOM 1631 CG LYS B 24 -1.070 6.602 43.746 1.00 59.51 C ANISOU 1631 CG LYS B 24 3919 10700 7991 1366 84 -2701 C ATOM 1632 CD LYS B 24 -2.153 7.644 43.475 1.00 64.58 C ANISOU 1632 CD LYS B 24 4341 11806 8389 2115 -122 -3065 C ATOM 1633 CE LYS B 24 -1.533 8.932 42.942 1.00 65.43 C ANISOU 1633 CE LYS B 24 5048 11191 8621 2705 -361 -2969 C ATOM 1634 NZ LYS B 24 -2.546 9.982 42.636 1.00 69.06 N ANISOU 1634 NZ LYS B 24 5418 12001 8818 3546 -612 -3313 N ATOM 1635 N TRP B 25 1.609 4.700 45.152 1.00 49.18 N ANISOU 1635 N TRP B 25 3224 8323 7138 49 449 -1968 N ATOM 1636 CA TRP B 25 2.708 5.090 46.033 1.00 46.73 C ANISOU 1636 CA TRP B 25 3223 7563 6967 23 447 -1820 C ATOM 1637 C TRP B 25 3.417 6.313 45.508 1.00 46.11 C ANISOU 1637 C TRP B 25 3504 6964 7051 431 277 -1768 C ATOM 1638 O TRP B 25 3.426 6.555 44.297 1.00 46.52 O ANISOU 1638 O TRP B 25 3675 6830 7170 614 189 -1709 O ATOM 1639 CB TRP B 25 3.707 3.941 46.182 1.00 43.77 C ANISOU 1639 CB TRP B 25 3044 6855 6732 -468 559 -1514 C ATOM 1640 CG TRP B 25 3.081 2.782 46.851 1.00 44.48 C ANISOU 1640 CG TRP B 25 2929 7347 6623 -922 716 -1535 C ATOM 1641 CD1 TRP B 25 2.503 1.705 46.247 1.00 43.98 C ANISOU 1641 CD1 TRP B 25 2754 7486 6470 -1266 801 -1516 C ATOM 1642 CD2 TRP B 25 2.906 2.599 48.257 1.00 45.38 C ANISOU 1642 CD2 TRP B 25 2959 7728 6555 -1133 812 -1588 C ATOM 1643 NE1 TRP B 25 2.003 0.846 47.191 1.00 45.48 N ANISOU 1643 NE1 TRP B 25 2836 8015 6428 -1729 949 -1534 N ATOM 1644 CE2 TRP B 25 2.236 1.364 48.435 1.00 47.47 C ANISOU 1644 CE2 TRP B 25 3095 8329 6612 -1649 963 -1569 C ATOM 1645 CE3 TRP B 25 3.269 3.343 49.387 1.00 46.66 C ANISOU 1645 CE3 TRP B 25 3176 7868 6683 -972 783 -1649 C ATOM 1646 CZ2 TRP B 25 1.909 0.858 49.700 1.00 50.00 C ANISOU 1646 CZ2 TRP B 25 3349 8973 6675 -2020 1098 -1584 C ATOM 1647 CZ3 TRP B 25 2.948 2.836 50.646 1.00 50.10 C ANISOU 1647 CZ3 TRP B 25 3508 8653 6875 -1291 911 -1682 C ATOM 1648 CH2 TRP B 25 2.267 1.601 50.788 1.00 51.79 C ANISOU 1648 CH2 TRP B 25 3602 9209 6867 -1818 1073 -1637 C ATOM 1649 N PHE B 26 4.013 7.080 46.419 1.00 45.60 N ANISOU 1649 N PHE B 26 3645 6663 7019 531 232 -1787 N ATOM 1650 CA PHE B 26 4.822 8.235 46.056 1.00 44.70 C ANISOU 1650 CA PHE B 26 3959 5991 7035 781 83 -1718 C ATOM 1651 C PHE B 26 6.257 7.995 46.509 1.00 41.59 C ANISOU 1651 C PHE B 26 3783 5201 6817 414 136 -1474 C ATOM 1652 O PHE B 26 6.498 7.594 47.633 1.00 41.41 O ANISOU 1652 O PHE B 26 3660 5318 6755 201 210 -1479 O ATOM 1653 CB PHE B 26 4.287 9.526 46.702 1.00 47.81 C ANISOU 1653 CB PHE B 26 4468 6421 7277 1253 -57 -2008 C ATOM 1654 CG PHE B 26 2.935 9.973 46.185 1.00 51.99 C ANISOU 1654 CG PHE B 26 4805 7346 7603 1773 -165 -2288 C ATOM 1655 CD1 PHE B 26 1.756 9.354 46.622 1.00 52.19 C ANISOU 1655 CD1 PHE B 26 4281 8138 7411 1783 -67 -2529 C ATOM 1656 CD2 PHE B 26 2.839 11.047 45.299 1.00 53.69 C ANISOU 1656 CD2 PHE B 26 5399 7201 7799 2256 -375 -2323 C ATOM 1657 CE1 PHE B 26 0.509 9.779 46.171 1.00 57.36 C ANISOU 1657 CE1 PHE B 26 4673 9279 7842 2300 -181 -2832 C ATOM 1658 CE2 PHE B 26 1.588 11.484 44.834 1.00 58.04 C ANISOU 1658 CE2 PHE B 26 5773 8154 8128 2839 -517 -2602 C ATOM 1659 CZ PHE B 26 0.417 10.850 45.275 1.00 59.39 C ANISOU 1659 CZ PHE B 26 5299 9179 8089 2884 -422 -2877 C ATOM 1660 N TYR B 27 7.206 8.239 45.622 1.00 40.05 N ANISOU 1660 N TYR B 27 3865 4570 6782 342 94 -1269 N ATOM 1661 CA TYR B 27 8.613 8.138 45.957 1.00 37.99 C ANISOU 1661 CA TYR B 27 3759 4016 6659 31 125 -1077 C ATOM 1662 C TYR B 27 9.046 9.385 46.773 1.00 40.15 C ANISOU 1662 C TYR B 27 4307 4050 6900 113 16 -1191 C ATOM 1663 O TYR B 27 8.784 10.518 46.366 1.00 42.35 O ANISOU 1663 O TYR B 27 4892 4071 7130 379 -112 -1287 O ATOM 1664 CB TYR B 27 9.434 7.943 44.669 1.00 36.17 C ANISOU 1664 CB TYR B 27 3664 3516 6561 -102 143 -851 C ATOM 1665 CG TYR B 27 10.907 8.234 44.801 1.00 34.82 C ANISOU 1665 CG TYR B 27 3660 3079 6492 -364 144 -703 C ATOM 1666 CD1 TYR B 27 11.525 9.136 43.948 1.00 34.94 C ANISOU 1666 CD1 TYR B 27 3980 2765 6531 -408 91 -617 C ATOM 1667 CD2 TYR B 27 11.685 7.597 45.773 1.00 33.56 C ANISOU 1667 CD2 TYR B 27 3349 3039 6364 -590 195 -651 C ATOM 1668 CE1 TYR B 27 12.882 9.405 44.053 1.00 37.69 C ANISOU 1668 CE1 TYR B 27 4417 2970 6932 -727 109 -505 C ATOM 1669 CE2 TYR B 27 13.043 7.869 45.897 1.00 35.52 C ANISOU 1669 CE2 TYR B 27 3668 3158 6672 -823 184 -554 C ATOM 1670 CZ TYR B 27 13.637 8.766 45.032 1.00 38.05 C ANISOU 1670 CZ TYR B 27 4227 3216 7016 -921 153 -492 C ATOM 1671 OH TYR B 27 14.980 9.067 45.150 1.00 40.07 O ANISOU 1671 OH TYR B 27 4499 3435 7291 -1229 157 -422 O ATOM 1672 N ILE B 28 9.705 9.169 47.918 1.00 39.73 N ANISOU 1672 N ILE B 28 4192 4056 6847 -110 48 -1184 N ATOM 1673 CA ILE B 28 10.017 10.269 48.851 1.00 42.24 C ANISOU 1673 CA ILE B 28 4746 4206 7098 -63 -56 -1340 C ATOM 1674 C ILE B 28 11.497 10.581 48.907 1.00 42.29 C ANISOU 1674 C ILE B 28 4936 3928 7205 -402 -84 -1195 C ATOM 1675 O ILE B 28 11.896 11.756 48.898 1.00 44.69 O ANISOU 1675 O ILE B 28 5608 3887 7486 -421 -193 -1266 O ATOM 1676 CB ILE B 28 9.529 9.987 50.312 1.00 42.92 C ANISOU 1676 CB ILE B 28 4614 4662 7032 -40 -19 -1517 C ATOM 1677 CG1 ILE B 28 8.053 9.574 50.357 1.00 42.53 C ANISOU 1677 CG1 ILE B 28 4278 5052 6831 208 44 -1687 C ATOM 1678 CG2 ILE B 28 9.819 11.178 51.240 1.00 45.04 C ANISOU 1678 CG2 ILE B 28 5158 4744 7211 37 -141 -1720 C ATOM 1679 CD1 ILE B 28 7.041 10.684 50.093 1.00 42.91 C ANISOU 1679 CD1 ILE B 28 4450 5099 6754 704 -76 -1967 C ATOM 1680 N ALA B 29 12.322 9.543 48.984 1.00 40.00 N ANISOU 1680 N ALA B 29 4410 3795 6995 -674 3 -1011 N ATOM 1681 CA ALA B 29 13.735 9.772 49.213 1.00 40.46 C ANISOU 1681 CA ALA B 29 4520 3751 7101 -986 -26 -923 C ATOM 1682 C ALA B 29 14.540 8.482 49.028 1.00 39.02 C ANISOU 1682 C ALA B 29 4050 3786 6991 -1144 57 -726 C ATOM 1683 O ALA B 29 13.991 7.381 49.111 1.00 37.38 O ANISOU 1683 O ALA B 29 3664 3768 6771 -1044 125 -669 O ATOM 1684 CB ALA B 29 13.949 10.350 50.612 1.00 41.62 C ANISOU 1684 CB ALA B 29 4728 3947 7137 -1045 -108 -1097 C ATOM 1685 N SER B 30 15.839 8.638 48.762 1.00 39.32 N ANISOU 1685 N SER B 30 4062 3805 7074 -1392 44 -639 N ATOM 1686 CA SER B 30 16.745 7.506 48.670 1.00 38.95 C ANISOU 1686 CA SER B 30 3738 4001 7058 -1459 88 -498 C ATOM 1687 C SER B 30 18.160 7.937 49.021 1.00 40.82 C ANISOU 1687 C SER B 30 3873 4376 7261 -1734 32 -514 C ATOM 1688 O SER B 30 18.502 9.129 48.980 1.00 42.50 O ANISOU 1688 O SER B 30 4274 4428 7446 -1973 -11 -596 O ATOM 1689 CB SER B 30 16.713 6.885 47.252 1.00 37.28 C ANISOU 1689 CB SER B 30 3482 3749 6935 -1394 182 -361 C ATOM 1690 OG SER B 30 17.148 7.865 46.310 1.00 41.64 O ANISOU 1690 OG SER B 30 4189 4124 7507 -1572 194 -343 O ATOM 1691 N ALA B 31 18.981 6.952 49.370 1.00 40.56 N ANISOU 1691 N ALA B 31 3561 4650 7200 -1700 19 -448 N ATOM 1692 CA ALA B 31 20.406 7.156 49.514 1.00 43.08 C ANISOU 1692 CA ALA B 31 3654 5250 7464 -1926 -29 -473 C ATOM 1693 C ALA B 31 21.062 5.819 49.255 1.00 42.71 C ANISOU 1693 C ALA B 31 3322 5498 7408 -1703 -19 -371 C ATOM 1694 O ALA B 31 20.549 4.795 49.683 1.00 41.31 O ANISOU 1694 O ALA B 31 3180 5304 7210 -1423 -39 -304 O ATOM 1695 CB ALA B 31 20.739 7.670 50.913 1.00 45.25 C ANISOU 1695 CB ALA B 31 3912 5660 7621 -2054 -156 -609 C ATOM 1696 N PHE B 32 22.167 5.816 48.518 1.00 44.65 N ANISOU 1696 N PHE B 32 3317 6011 7638 -1825 15 -366 N ATOM 1697 CA PHE B 32 22.861 4.568 48.234 1.00 45.65 C ANISOU 1697 CA PHE B 32 3173 6445 7726 -1524 5 -312 C ATOM 1698 C PHE B 32 24.350 4.777 48.375 1.00 49.40 C ANISOU 1698 C PHE B 32 3232 7463 8074 -1677 -49 -415 C ATOM 1699 O PHE B 32 24.846 5.855 48.094 1.00 51.73 O ANISOU 1699 O PHE B 32 3458 7858 8340 -2119 -3 -489 O ATOM 1700 CB PHE B 32 22.567 4.091 46.811 1.00 44.48 C ANISOU 1700 CB PHE B 32 3076 6161 7665 -1405 141 -226 C ATOM 1701 CG PHE B 32 21.104 3.875 46.526 1.00 42.16 C ANISOU 1701 CG PHE B 32 3128 5420 7472 -1284 196 -151 C ATOM 1702 CD1 PHE B 32 20.360 4.854 45.872 1.00 42.62 C ANISOU 1702 CD1 PHE B 32 3405 5189 7598 -1481 269 -150 C ATOM 1703 CD2 PHE B 32 20.474 2.689 46.900 1.00 41.18 C ANISOU 1703 CD2 PHE B 32 3124 5185 7337 -982 164 -86 C ATOM 1704 CE1 PHE B 32 18.971 4.661 45.601 1.00 40.04 C ANISOU 1704 CE1 PHE B 32 3324 4555 7333 -1336 304 -118 C ATOM 1705 CE2 PHE B 32 19.101 2.493 46.651 1.00 39.57 C ANISOU 1705 CE2 PHE B 32 3177 4667 7190 -945 224 -47 C ATOM 1706 CZ PHE B 32 18.354 3.479 45.998 1.00 38.22 C ANISOU 1706 CZ PHE B 32 3128 4304 7092 -1101 292 -78 C ATOM 1707 N ARG B 33 25.067 3.751 48.804 1.00 50.97 N ANISOU 1707 N ARG B 33 3171 8028 8166 -1317 -158 -429 N ATOM 1708 CA ARG B 33 26.513 3.823 48.736 1.00 55.50 C ANISOU 1708 CA ARG B 33 3243 9253 8591 -1388 -204 -559 C ATOM 1709 C ARG B 33 26.990 3.558 47.315 1.00 56.06 C ANISOU 1709 C ARG B 33 3100 9529 8670 -1357 -52 -560 C ATOM 1710 O ARG B 33 28.106 3.924 46.960 1.00 59.32 O ANISOU 1710 O ARG B 33 3071 10514 8952 -1588 -16 -685 O ATOM 1711 CB ARG B 33 27.167 2.907 49.762 1.00 58.10 C ANISOU 1711 CB ARG B 33 3358 9963 8755 -946 -415 -603 C ATOM 1712 CG ARG B 33 27.135 3.502 51.147 1.00 59.74 C ANISOU 1712 CG ARG B 33 3613 10209 8877 -1141 -560 -666 C ATOM 1713 CD ARG B 33 27.785 2.601 52.150 1.00 65.34 C ANISOU 1713 CD ARG B 33 4142 11301 9383 -678 -792 -693 C ATOM 1714 NE ARG B 33 28.022 3.297 53.409 1.00 69.64 N ANISOU 1714 NE ARG B 33 4617 12046 9796 -928 -936 -799 N ATOM 1715 CZ ARG B 33 28.450 2.703 54.518 1.00 74.46 C ANISOU 1715 CZ ARG B 33 5145 12951 10197 -581 -1167 -817 C ATOM 1716 NH1 ARG B 33 28.681 1.391 54.531 1.00 76.52 N ANISOU 1716 NH1 ARG B 33 5440 13285 10351 59 -1291 -721 N ATOM 1717 NH2 ARG B 33 28.643 3.415 55.619 1.00 76.80 N ANISOU 1717 NH2 ARG B 33 5379 13440 10363 -852 -1290 -933 N ATOM 1718 N ASN B 34 26.117 2.960 46.506 1.00 52.82 N ANISOU 1718 N ASN B 34 2992 8690 8387 -1120 44 -436 N ATOM 1719 CA ASN B 34 26.354 2.761 45.079 1.00 53.90 C ANISOU 1719 CA ASN B 34 3015 8931 8532 -1106 205 -430 C ATOM 1720 C ASN B 34 26.138 4.033 44.266 1.00 54.12 C ANISOU 1720 C ASN B 34 3163 8798 8604 -1685 369 -400 C ATOM 1721 O ASN B 34 25.008 4.537 44.161 1.00 51.00 O ANISOU 1721 O ASN B 34 3202 7839 8336 -1815 403 -302 O ATOM 1722 CB ASN B 34 25.456 1.646 44.518 1.00 50.52 C ANISOU 1722 CB ASN B 34 2913 8083 8201 -665 231 -324 C ATOM 1723 CG ASN B 34 25.630 1.463 43.011 1.00 51.56 C ANISOU 1723 CG ASN B 34 2957 8307 8326 -648 398 -331 C ATOM 1724 OD1 ASN B 34 24.966 2.126 42.214 1.00 51.11 O ANISOU 1724 OD1 ASN B 34 3115 7952 8351 -950 530 -257 O ATOM 1725 ND2 ASN B 34 26.532 0.568 42.620 1.00 53.41 N ANISOU 1725 ND2 ASN B 34 2885 8975 8432 -252 380 -433 N ATOM 1726 N GLU B 35 27.212 4.514 43.647 1.00 58.42 N ANISOU 1726 N GLU B 35 3333 9859 9007 -2014 469 -488 N ATOM 1727 CA GLU B 35 27.206 5.838 43.034 1.00 60.61 C ANISOU 1727 CA GLU B 35 3772 10004 9252 -2671 602 -452 C ATOM 1728 C GLU B 35 26.430 5.932 41.712 1.00 58.76 C ANISOU 1728 C GLU B 35 3878 9359 9087 -2692 756 -312 C ATOM 1729 O GLU B 35 25.835 6.972 41.429 1.00 58.45 O ANISOU 1729 O GLU B 35 4258 8875 9077 -3068 797 -223 O ATOM 1730 CB GLU B 35 28.623 6.384 42.915 1.00 66.05 C ANISOU 1730 CB GLU B 35 3955 11427 9713 -3149 666 -595 C ATOM 1731 CG GLU B 35 28.692 7.898 42.790 1.00 70.80 C ANISOU 1731 CG GLU B 35 4829 11833 10239 -3956 740 -569 C ATOM 1732 CD GLU B 35 28.745 8.367 41.335 1.00 75.13 C ANISOU 1732 CD GLU B 35 5518 12338 10692 -4336 960 -464 C ATOM 1733 OE1 GLU B 35 29.841 8.365 40.717 1.00 78.62 O ANISOU 1733 OE1 GLU B 35 5478 13484 10911 -4643 1101 -553 O ATOM 1734 OE2 GLU B 35 27.670 8.732 40.814 1.00 76.11 O ANISOU 1734 OE2 GLU B 35 6223 11760 10935 -4311 987 -299 O ATOM 1735 N GLU B 36 26.412 4.858 40.922 1.00 58.09 N ANISOU 1735 N GLU B 36 3663 9400 9009 -2257 818 -304 N ATOM 1736 CA GLU B 36 25.599 4.822 39.695 1.00 56.96 C ANISOU 1736 CA GLU B 36 3842 8882 8920 -2219 941 -184 C ATOM 1737 C GLU B 36 24.095 4.986 40.001 1.00 53.06 C ANISOU 1737 C GLU B 36 3875 7675 8609 -2087 858 -74 C ATOM 1738 O GLU B 36 23.384 5.738 39.319 1.00 52.50 O ANISOU 1738 O GLU B 36 4163 7230 8556 -2294 913 24 O ATOM 1739 CB GLU B 36 25.862 3.539 38.895 1.00 57.54 C ANISOU 1739 CB GLU B 36 3689 9224 8950 -1735 999 -237 C ATOM 1740 CG GLU B 36 27.321 3.381 38.383 1.00 64.61 C ANISOU 1740 CG GLU B 36 4003 10930 9615 -1808 1107 -386 C ATOM 1741 CD GLU B 36 28.261 2.694 39.390 1.00 70.23 C ANISOU 1741 CD GLU B 36 4261 12175 10250 -1457 959 -556 C ATOM 1742 OE1 GLU B 36 27.967 1.562 39.840 1.00 71.15 O ANISOU 1742 OE1 GLU B 36 4473 12124 10438 -843 817 -576 O ATOM 1743 OE2 GLU B 36 29.309 3.279 39.728 1.00 75.70 O ANISOU 1743 OE2 GLU B 36 4518 13466 10778 -1806 974 -673 O ATOM 1744 N TYR B 37 23.624 4.307 41.046 1.00 50.90 N ANISOU 1744 N TYR B 37 3647 7259 8436 -1744 720 -98 N ATOM 1745 CA TYR B 37 22.248 4.490 41.539 1.00 48.29 C ANISOU 1745 CA TYR B 37 3718 6396 8235 -1657 647 -37 C ATOM 1746 C TYR B 37 22.006 5.944 41.957 1.00 48.93 C ANISOU 1746 C TYR B 37 4041 6240 8312 -2051 614 -37 C ATOM 1747 O TYR B 37 21.021 6.544 41.534 1.00 47.48 O ANISOU 1747 O TYR B 37 4215 5656 8170 -2081 621 17 O ATOM 1748 CB TYR B 37 21.931 3.529 42.698 1.00 46.55 C ANISOU 1748 CB TYR B 37 3486 6143 8058 -1313 520 -62 C ATOM 1749 CG TYR B 37 21.313 2.192 42.281 1.00 46.51 C ANISOU 1749 CG TYR B 37 3592 5991 8089 -925 528 -23 C ATOM 1750 CD1 TYR B 37 21.728 1.531 41.120 1.00 48.11 C ANISOU 1750 CD1 TYR B 37 3692 6337 8252 -763 614 -32 C ATOM 1751 CD2 TYR B 37 20.345 1.578 43.071 1.00 44.55 C ANISOU 1751 CD2 TYR B 37 3567 5479 7880 -758 453 7 C ATOM 1752 CE1 TYR B 37 21.174 0.309 40.743 1.00 47.11 C ANISOU 1752 CE1 TYR B 37 3735 6025 8138 -437 606 -18 C ATOM 1753 CE2 TYR B 37 19.767 0.342 42.699 1.00 44.96 C ANISOU 1753 CE2 TYR B 37 3789 5360 7933 -499 459 41 C ATOM 1754 CZ TYR B 37 20.189 -0.277 41.536 1.00 45.83 C ANISOU 1754 CZ TYR B 37 3844 5552 8019 -335 526 24 C ATOM 1755 OH TYR B 37 19.655 -1.486 41.161 1.00 45.59 O ANISOU 1755 OH TYR B 37 4040 5311 7970 -105 518 34 O ATOM 1756 N ASN B 38 22.909 6.498 42.776 1.00 51.45 N ANISOU 1756 N ASN B 38 4182 6813 8555 -2326 561 -117 N ATOM 1757 CA ASN B 38 22.835 7.915 43.174 1.00 53.82 C ANISOU 1757 CA ASN B 38 4767 6866 8815 -2751 520 -144 C ATOM 1758 C ASN B 38 22.684 8.832 41.969 1.00 55.71 C ANISOU 1758 C ASN B 38 5331 6842 8993 -3068 620 -49 C ATOM 1759 O ASN B 38 21.761 9.653 41.913 1.00 54.37 O ANISOU 1759 O ASN B 38 5642 6170 8848 -3085 567 -15 O ATOM 1760 CB ASN B 38 24.065 8.342 43.995 1.00 56.70 C ANISOU 1760 CB ASN B 38 4836 7649 9059 -3109 469 -263 C ATOM 1761 CG ASN B 38 24.024 7.825 45.428 1.00 55.56 C ANISOU 1761 CG ASN B 38 4542 7628 8939 -2843 317 -353 C ATOM 1762 OD1 ASN B 38 22.959 7.498 45.964 1.00 51.27 O ANISOU 1762 OD1 ASN B 38 4229 6759 8493 -2520 254 -328 O ATOM 1763 ND2 ASN B 38 25.188 7.762 46.061 1.00 56.39 N ANISOU 1763 ND2 ASN B 38 4245 8259 8922 -2997 257 -465 N ATOM 1764 N LYS B 39 23.581 8.645 41.001 1.00 58.54 N ANISOU 1764 N LYS B 39 5433 7568 9241 -3271 758 -15 N ATOM 1765 CA LYS B 39 23.621 9.444 39.784 1.00 62.16 C ANISOU 1765 CA LYS B 39 6184 7857 9577 -3635 875 100 C ATOM 1766 C LYS B 39 22.279 9.433 39.039 1.00 60.12 C ANISOU 1766 C LYS B 39 6359 7082 9401 -3301 858 213 C ATOM 1767 O LYS B 39 21.707 10.486 38.798 1.00 62.11 O ANISOU 1767 O LYS B 39 7136 6862 9602 -3465 808 283 O ATOM 1768 CB LYS B 39 24.764 8.968 38.875 1.00 64.61 C ANISOU 1768 CB LYS B 39 6037 8781 9732 -3820 1050 93 C ATOM 1769 CG LYS B 39 25.338 10.020 37.958 1.00 69.76 C ANISOU 1769 CG LYS B 39 6892 9459 10153 -4481 1189 183 C ATOM 1770 CD LYS B 39 26.639 10.600 38.506 1.00 76.31 C ANISOU 1770 CD LYS B 39 7403 10791 10802 -5103 1227 68 C ATOM 1771 CE LYS B 39 27.671 10.779 37.401 1.00 80.92 C ANISOU 1771 CE LYS B 39 7714 11928 11102 -5626 1455 92 C ATOM 1772 NZ LYS B 39 29.065 10.907 37.935 1.00 87.35 N ANISOU 1772 NZ LYS B 39 7923 13542 11724 -6110 1507 -92 N ATOM 1773 N SER B 40 21.751 8.262 38.703 1.00 57.92 N ANISOU 1773 N SER B 40 5898 6884 9226 -2820 875 215 N ATOM 1774 CA SER B 40 20.492 8.229 37.952 1.00 56.45 C ANISOU 1774 CA SER B 40 6055 6309 9086 -2536 853 294 C ATOM 1775 C SER B 40 19.280 8.748 38.758 1.00 54.79 C ANISOU 1775 C SER B 40 6185 5665 8967 -2326 695 253 C ATOM 1776 O SER B 40 18.345 9.338 38.203 1.00 56.37 O ANISOU 1776 O SER B 40 6773 5512 9134 -2208 641 303 O ATOM 1777 CB SER B 40 20.219 6.840 37.421 1.00 53.68 C ANISOU 1777 CB SER B 40 5446 6152 8798 -2139 906 279 C ATOM 1778 OG SER B 40 19.445 6.133 38.361 1.00 53.91 O ANISOU 1778 OG SER B 40 5434 6083 8967 -1802 802 208 O ATOM 1779 N VAL B 41 19.315 8.557 40.065 1.00 52.69 N ANISOU 1779 N VAL B 41 5768 5470 8781 -2255 614 148 N ATOM 1780 CA VAL B 41 18.220 8.977 40.922 1.00 50.90 C ANISOU 1780 CA VAL B 41 5787 4945 8610 -2042 483 68 C ATOM 1781 C VAL B 41 18.192 10.491 41.175 1.00 52.90 C ANISOU 1781 C VAL B 41 6494 4833 8774 -2286 393 44 C ATOM 1782 O VAL B 41 17.140 11.066 41.424 1.00 52.22 O ANISOU 1782 O VAL B 41 6731 4428 8682 -2039 282 -20 O ATOM 1783 CB VAL B 41 18.245 8.147 42.209 1.00 49.48 C ANISOU 1783 CB VAL B 41 5305 4990 8505 -1881 440 -26 C ATOM 1784 CG1 VAL B 41 17.647 8.865 43.365 1.00 50.69 C ANISOU 1784 CG1 VAL B 41 5652 4953 8653 -1838 322 -143 C ATOM 1785 CG2 VAL B 41 17.534 6.831 41.964 1.00 46.43 C ANISOU 1785 CG2 VAL B 41 4752 4704 8186 -1541 475 -8 C ATOM 1786 N GLN B 42 19.346 11.137 41.068 1.00 55.49 N ANISOU 1786 N GLN B 42 6862 5220 9000 -2772 438 78 N ATOM 1787 CA GLN B 42 19.460 12.560 41.378 1.00 58.79 C ANISOU 1787 CA GLN B 42 7787 5245 9304 -3099 346 48 C ATOM 1788 C GLN B 42 18.548 13.499 40.598 1.00 59.89 C ANISOU 1788 C GLN B 42 8576 4827 9351 -2962 264 122 C ATOM 1789 O GLN B 42 18.182 14.569 41.111 1.00 62.34 O ANISOU 1789 O GLN B 42 9398 4698 9589 -2974 120 43 O ATOM 1790 CB GLN B 42 20.906 13.021 41.231 1.00 62.66 C ANISOU 1790 CB GLN B 42 8190 5961 9656 -3762 437 80 C ATOM 1791 CG GLN B 42 21.541 13.289 42.562 1.00 65.84 C ANISOU 1791 CG GLN B 42 8436 6528 10051 -4007 360 -82 C ATOM 1792 CD GLN B 42 23.043 13.327 42.498 1.00 71.01 C ANISOU 1792 CD GLN B 42 8720 7686 10573 -4607 465 -96 C ATOM 1793 OE1 GLN B 42 23.631 13.566 41.438 1.00 74.19 O ANISOU 1793 OE1 GLN B 42 9156 8196 10838 -4995 600 19 O ATOM 1794 NE2 GLN B 42 23.684 13.094 43.641 1.00 71.29 N ANISOU 1794 NE2 GLN B 42 8372 8099 10615 -4696 403 -251 N ATOM 1795 N GLU B 43 18.209 13.134 39.364 1.00 57.98 N ANISOU 1795 N GLU B 43 8356 4592 9083 -2808 334 260 N ATOM 1796 CA GLU B 43 17.426 14.039 38.505 1.00 60.16 C ANISOU 1796 CA GLU B 43 9278 4361 9221 -2660 235 353 C ATOM 1797 C GLU B 43 15.903 13.849 38.634 1.00 56.44 C ANISOU 1797 C GLU B 43 8872 3757 8817 -1969 92 248 C ATOM 1798 O GLU B 43 15.123 14.622 38.067 1.00 58.36 O ANISOU 1798 O GLU B 43 9644 3600 8929 -1704 -45 281 O ATOM 1799 CB GLU B 43 17.896 13.977 37.040 1.00 61.99 C ANISOU 1799 CB GLU B 43 9592 4653 9309 -2916 369 564 C ATOM 1800 CG GLU B 43 17.747 12.581 36.366 1.00 61.61 C ANISOU 1800 CG GLU B 43 8974 5072 9364 -2639 498 586 C ATOM 1801 CD GLU B 43 18.267 12.550 34.915 1.00 66.92 C ANISOU 1801 CD GLU B 43 9722 5849 9857 -2902 642 770 C ATOM 1802 OE1 GLU B 43 18.150 11.494 34.247 1.00 66.90 O ANISOU 1802 OE1 GLU B 43 9339 6179 9901 -2679 739 776 O ATOM 1803 OE2 GLU B 43 18.779 13.585 34.437 1.00 71.71 O ANISOU 1803 OE2 GLU B 43 10807 6192 10246 -3354 660 907 O ATOM 1804 N ILE B 44 15.499 12.834 39.398 1.00 51.43 N ANISOU 1804 N ILE B 44 7710 3484 8348 -1691 115 115 N ATOM 1805 CA ILE B 44 14.088 12.610 39.730 1.00 48.47 C ANISOU 1805 CA ILE B 44 7286 3121 8009 -1125 4 -32 C ATOM 1806 C ILE B 44 13.572 13.760 40.617 1.00 50.37 C ANISOU 1806 C ILE B 44 7956 3010 8171 -939 -177 -198 C ATOM 1807 O ILE B 44 14.005 13.941 41.758 1.00 50.41 O ANISOU 1807 O ILE B 44 7896 3042 8215 -1109 -189 -311 O ATOM 1808 CB ILE B 44 13.834 11.209 40.383 1.00 44.86 C ANISOU 1808 CB ILE B 44 6206 3135 7702 -989 94 -118 C ATOM 1809 CG1 ILE B 44 14.367 10.074 39.484 1.00 42.72 C ANISOU 1809 CG1 ILE B 44 5599 3146 7486 -1120 249 18 C ATOM 1810 CG2 ILE B 44 12.358 11.004 40.682 1.00 42.99 C ANISOU 1810 CG2 ILE B 44 5885 3000 7451 -507 5 -283 C ATOM 1811 CD1 ILE B 44 14.257 8.684 40.080 1.00 41.64 C ANISOU 1811 CD1 ILE B 44 4992 3366 7462 -1030 322 -39 C ATOM 1812 N GLN B 45 12.665 14.557 40.062 1.00 51.65 N ANISOU 1812 N GLN B 45 8586 2841 8195 -553 -336 -225 N ATOM 1813 CA GLN B 45 12.023 15.630 40.816 1.00 53.06 C ANISOU 1813 CA GLN B 45 9216 2678 8268 -222 -538 -424 C ATOM 1814 C GLN B 45 10.848 15.102 41.625 1.00 51.07 C ANISOU 1814 C GLN B 45 8533 2817 8054 296 -580 -680 C ATOM 1815 O GLN B 45 10.641 15.526 42.753 1.00 51.54 O ANISOU 1815 O GLN B 45 8646 2848 8089 424 -655 -890 O ATOM 1816 CB GLN B 45 11.563 16.731 39.877 1.00 57.26 C ANISOU 1816 CB GLN B 45 10494 2674 8588 50 -725 -355 C ATOM 1817 CG GLN B 45 12.709 17.472 39.206 1.00 58.74 C ANISOU 1817 CG GLN B 45 11251 2405 8664 -551 -690 -108 C ATOM 1818 CD GLN B 45 12.230 18.442 38.141 1.00 61.00 C ANISOU 1818 CD GLN B 45 12339 2139 8699 -284 -875 19 C ATOM 1819 OE1 GLN B 45 11.626 18.043 37.148 1.00 58.86 O ANISOU 1819 OE1 GLN B 45 11965 2023 8376 40 -890 110 O ATOM 1820 NE2 GLN B 45 12.511 19.729 38.341 1.00 67.07 N ANISOU 1820 NE2 GLN B 45 13966 2234 9283 -428 -1034 26 N ATOM 1821 N ALA B 46 10.084 14.178 41.031 1.00 48.51 N ANISOU 1821 N ALA B 46 7783 2887 7760 552 -525 -673 N ATOM 1822 CA ALA B 46 8.963 13.509 41.690 1.00 47.57 C ANISOU 1822 CA ALA B 46 7171 3260 7646 922 -521 -903 C ATOM 1823 C ALA B 46 8.643 12.178 40.984 1.00 44.93 C ANISOU 1823 C ALA B 46 6322 3365 7384 861 -382 -816 C ATOM 1824 O ALA B 46 9.024 11.959 39.819 1.00 45.40 O ANISOU 1824 O ALA B 46 6472 3323 7455 721 -340 -617 O ATOM 1825 CB ALA B 46 7.727 14.415 41.743 1.00 51.11 C ANISOU 1825 CB ALA B 46 7882 3642 7898 1586 -742 -1148 C ATOM 1826 N THR B 47 7.992 11.268 41.699 1.00 43.04 N ANISOU 1826 N THR B 47 5576 3608 7170 911 -301 -963 N ATOM 1827 CA THR B 47 7.481 10.033 41.094 1.00 40.56 C ANISOU 1827 CA THR B 47 4838 3694 6879 861 -194 -931 C ATOM 1828 C THR B 47 6.340 9.492 41.918 1.00 40.81 C ANISOU 1828 C THR B 47 4441 4244 6821 1020 -169 -1175 C ATOM 1829 O THR B 47 6.467 9.336 43.129 1.00 40.24 O ANISOU 1829 O THR B 47 4233 4296 6761 888 -110 -1256 O ATOM 1830 CB THR B 47 8.561 8.913 40.966 1.00 37.47 C ANISOU 1830 CB THR B 47 4266 3321 6651 380 -13 -717 C ATOM 1831 OG1 THR B 47 9.632 9.372 40.153 1.00 37.30 O ANISOU 1831 OG1 THR B 47 4556 2943 6675 192 -7 -513 O ATOM 1832 CG2 THR B 47 7.980 7.656 40.307 1.00 34.63 C ANISOU 1832 CG2 THR B 47 3575 3294 6288 334 75 -708 C ATOM 1833 N PHE B 48 5.222 9.229 41.255 1.00 42.64 N ANISOU 1833 N PHE B 48 4450 4824 6928 1282 -214 -1300 N ATOM 1834 CA PHE B 48 4.181 8.368 41.821 1.00 43.31 C ANISOU 1834 CA PHE B 48 4022 5528 6906 1249 -130 -1502 C ATOM 1835 C PHE B 48 3.971 7.201 40.872 1.00 42.28 C ANISOU 1835 C PHE B 48 3663 5607 6793 998 -38 -1408 C ATOM 1836 O PHE B 48 4.284 7.318 39.680 1.00 42.29 O ANISOU 1836 O PHE B 48 3870 5367 6832 1056 -91 -1266 O ATOM 1837 CB PHE B 48 2.877 9.126 42.133 1.00 47.18 C ANISOU 1837 CB PHE B 48 4347 6419 7160 1787 -271 -1843 C ATOM 1838 CG PHE B 48 2.252 9.831 40.951 1.00 50.23 C ANISOU 1838 CG PHE B 48 4890 6779 7416 2295 -473 -1910 C ATOM 1839 CD1 PHE B 48 2.644 11.118 40.604 1.00 52.41 C ANISOU 1839 CD1 PHE B 48 5749 6492 7673 2668 -666 -1854 C ATOM 1840 CD2 PHE B 48 1.234 9.219 40.211 1.00 52.97 C ANISOU 1840 CD2 PHE B 48 4832 7677 7619 2395 -488 -2039 C ATOM 1841 CE1 PHE B 48 2.038 11.793 39.528 1.00 56.01 C ANISOU 1841 CE1 PHE B 48 6429 6893 7960 3194 -884 -1900 C ATOM 1842 CE2 PHE B 48 0.630 9.877 39.125 1.00 54.13 C ANISOU 1842 CE2 PHE B 48 5116 7845 7606 2923 -706 -2110 C ATOM 1843 CZ PHE B 48 1.037 11.163 38.784 1.00 55.94 C ANISOU 1843 CZ PHE B 48 5972 7472 7810 3351 -911 -2027 C ATOM 1844 N PHE B 49 3.475 6.075 41.396 1.00 41.93 N ANISOU 1844 N PHE B 49 3247 5988 6697 681 102 -1481 N ATOM 1845 CA PHE B 49 3.259 4.877 40.588 1.00 41.22 C ANISOU 1845 CA PHE B 49 2994 6066 6603 378 190 -1416 C ATOM 1846 C PHE B 49 2.182 3.966 41.160 1.00 43.41 C ANISOU 1846 C PHE B 49 2848 6949 6695 109 294 -1609 C ATOM 1847 O PHE B 49 1.802 4.104 42.318 1.00 46.01 O ANISOU 1847 O PHE B 49 3005 7556 6922 79 342 -1746 O ATOM 1848 CB PHE B 49 4.559 4.081 40.431 1.00 37.27 C ANISOU 1848 CB PHE B 49 2730 5128 6302 9 299 -1133 C ATOM 1849 CG PHE B 49 5.160 3.627 41.732 1.00 36.25 C ANISOU 1849 CG PHE B 49 2620 4921 6230 -268 401 -1060 C ATOM 1850 CD1 PHE B 49 6.102 4.421 42.387 1.00 37.24 C ANISOU 1850 CD1 PHE B 49 2955 4732 6464 -183 364 -977 C ATOM 1851 CD2 PHE B 49 4.797 2.406 42.301 1.00 36.71 C ANISOU 1851 CD2 PHE B 49 2530 5212 6204 -643 523 -1070 C ATOM 1852 CE1 PHE B 49 6.688 4.010 43.573 1.00 36.56 C ANISOU 1852 CE1 PHE B 49 2881 4605 6405 -410 434 -912 C ATOM 1853 CE2 PHE B 49 5.365 1.992 43.499 1.00 36.46 C ANISOU 1853 CE2 PHE B 49 2577 5089 6186 -867 594 -978 C ATOM 1854 CZ PHE B 49 6.325 2.803 44.135 1.00 36.98 C ANISOU 1854 CZ PHE B 49 2804 4879 6366 -720 542 -902 C ATOM 1855 N TYR B 50 1.707 3.030 40.346 1.00 43.80 N ANISOU 1855 N TYR B 50 2748 7216 6677 -135 338 -1625 N ATOM 1856 CA TYR B 50 0.742 2.031 40.792 1.00 46.18 C ANISOU 1856 CA TYR B 50 2695 8075 6775 -551 458 -1787 C ATOM 1857 C TYR B 50 1.343 0.644 40.760 1.00 44.53 C ANISOU 1857 C TYR B 50 2706 7571 6643 -1114 595 -1580 C ATOM 1858 O TYR B 50 2.077 0.292 39.819 1.00 42.43 O ANISOU 1858 O TYR B 50 2711 6885 6526 -1122 573 -1409 O ATOM 1859 CB TYR B 50 -0.505 2.052 39.912 1.00 49.66 C ANISOU 1859 CB TYR B 50 2757 9113 6996 -416 376 -2046 C ATOM 1860 CG TYR B 50 -1.300 3.327 40.017 1.00 53.71 C ANISOU 1860 CG TYR B 50 3021 10032 7356 212 215 -2311 C ATOM 1861 CD1 TYR B 50 -0.867 4.488 39.379 1.00 55.04 C ANISOU 1861 CD1 TYR B 50 3502 9787 7624 803 24 -2241 C ATOM 1862 CD2 TYR B 50 -2.495 3.374 40.743 1.00 59.04 C ANISOU 1862 CD2 TYR B 50 3171 11516 7746 224 248 -2644 C ATOM 1863 CE1 TYR B 50 -1.589 5.666 39.460 1.00 59.49 C ANISOU 1863 CE1 TYR B 50 3945 10638 8019 1456 -161 -2488 C ATOM 1864 CE2 TYR B 50 -3.231 4.551 40.831 1.00 62.84 C ANISOU 1864 CE2 TYR B 50 3427 12393 8056 913 74 -2929 C ATOM 1865 CZ TYR B 50 -2.766 5.691 40.184 1.00 63.32 C ANISOU 1865 CZ TYR B 50 3890 11936 8233 1559 -145 -2845 C ATOM 1866 OH TYR B 50 -3.460 6.866 40.259 1.00 68.28 O ANISOU 1866 OH TYR B 50 4417 12854 8673 2310 -352 -3122 O ATOM 1867 N PHE B 51 1.044 -0.129 41.799 1.00 45.91 N ANISOU 1867 N PHE B 51 2801 7958 6685 -1562 732 -1600 N ATOM 1868 CA PHE B 51 1.427 -1.530 41.883 1.00 45.93 C ANISOU 1868 CA PHE B 51 3079 7690 6682 -2110 845 -1429 C ATOM 1869 C PHE B 51 0.190 -2.408 41.773 1.00 50.06 C ANISOU 1869 C PHE B 51 3338 8765 6915 -2621 934 -1620 C ATOM 1870 O PHE B 51 -0.687 -2.342 42.628 1.00 52.48 O ANISOU 1870 O PHE B 51 3312 9644 6984 -2829 1016 -1796 O ATOM 1871 CB PHE B 51 2.065 -1.811 43.240 1.00 45.47 C ANISOU 1871 CB PHE B 51 3238 7404 6634 -2306 927 -1269 C ATOM 1872 CG PHE B 51 3.540 -1.599 43.293 1.00 43.60 C ANISOU 1872 CG PHE B 51 3371 6533 6663 -2052 868 -1021 C ATOM 1873 CD1 PHE B 51 4.165 -1.428 44.520 1.00 43.90 C ANISOU 1873 CD1 PHE B 51 3531 6430 6718 -2051 887 -916 C ATOM 1874 CD2 PHE B 51 4.314 -1.590 42.138 1.00 42.70 C ANISOU 1874 CD2 PHE B 51 3451 6030 6743 -1836 798 -910 C ATOM 1875 CE1 PHE B 51 5.545 -1.260 44.603 1.00 42.86 C ANISOU 1875 CE1 PHE B 51 3677 5810 6798 -1843 826 -715 C ATOM 1876 CE2 PHE B 51 5.698 -1.419 42.210 1.00 41.25 C ANISOU 1876 CE2 PHE B 51 3532 5377 6762 -1641 759 -710 C ATOM 1877 CZ PHE B 51 6.308 -1.249 43.442 1.00 41.45 C ANISOU 1877 CZ PHE B 51 3641 5301 6806 -1645 767 -621 C ATOM 1878 N THR B 52 0.119 -3.235 40.733 1.00 50.70 N ANISOU 1878 N THR B 52 3560 8716 6987 -2861 925 -1604 N ATOM 1879 CA THR B 52 -0.981 -4.206 40.592 1.00 54.74 C ANISOU 1879 CA THR B 52 3890 9705 7204 -3483 1013 -1780 C ATOM 1880 C THR B 52 -0.390 -5.608 40.500 1.00 54.31 C ANISOU 1880 C THR B 52 4414 9062 7158 -3999 1080 -1574 C ATOM 1881 O THR B 52 -0.018 -6.058 39.425 1.00 52.85 O ANISOU 1881 O THR B 52 4480 8530 7071 -3956 1017 -1531 O ATOM 1882 CB THR B 52 -1.855 -3.907 39.353 1.00 56.55 C ANISOU 1882 CB THR B 52 3731 10425 7331 -3317 910 -2034 C ATOM 1883 OG1 THR B 52 -2.161 -2.507 39.329 1.00 57.88 O ANISOU 1883 OG1 THR B 52 3519 10947 7525 -2647 790 -2181 O ATOM 1884 CG2 THR B 52 -3.151 -4.720 39.374 1.00 61.86 C ANISOU 1884 CG2 THR B 52 4056 11809 7637 -3993 1004 -2290 C ATOM 1885 N PRO B 53 -0.274 -6.294 41.642 1.00 56.13 N ANISOU 1885 N PRO B 53 4910 9155 7263 -4450 1195 -1445 N ATOM 1886 CA PRO B 53 0.234 -7.661 41.645 1.00 57.51 C ANISOU 1886 CA PRO B 53 5738 8724 7391 -4916 1232 -1251 C ATOM 1887 C PRO B 53 -0.557 -8.582 40.731 1.00 60.93 C ANISOU 1887 C PRO B 53 6225 9305 7622 -5455 1251 -1410 C ATOM 1888 O PRO B 53 -1.769 -8.408 40.579 1.00 63.65 O ANISOU 1888 O PRO B 53 6041 10412 7731 -5757 1299 -1679 O ATOM 1889 CB PRO B 53 0.041 -8.093 43.097 1.00 60.25 C ANISOU 1889 CB PRO B 53 6239 9147 7508 -5391 1359 -1150 C ATOM 1890 CG PRO B 53 0.183 -6.814 43.853 1.00 58.36 C ANISOU 1890 CG PRO B 53 5586 9212 7378 -4882 1347 -1183 C ATOM 1891 CD PRO B 53 -0.581 -5.835 43.004 1.00 57.55 C ANISOU 1891 CD PRO B 53 4859 9702 7307 -4519 1284 -1470 C ATOM 1892 N ASN B 54 0.160 -9.500 40.083 1.00 61.00 N ANISOU 1892 N ASN B 54 6844 8621 7714 -5514 1197 -1274 N ATOM 1893 CA ASN B 54 -0.417 -10.728 39.557 1.00 65.24 C ANISOU 1893 CA ASN B 54 7718 9065 8006 -6204 1229 -1365 C ATOM 1894 C ASN B 54 0.104 -11.895 40.388 1.00 68.14 C ANISOU 1894 C ASN B 54 8897 8749 8242 -6638 1271 -1121 C ATOM 1895 O ASN B 54 1.169 -12.459 40.113 1.00 66.56 O ANISOU 1895 O ASN B 54 9327 7771 8193 -6342 1178 -943 O ATOM 1896 CB ASN B 54 -0.110 -10.931 38.071 1.00 64.09 C ANISOU 1896 CB ASN B 54 7706 8651 7994 -5933 1114 -1449 C ATOM 1897 CG ASN B 54 -0.812 -12.171 37.490 1.00 68.84 C ANISOU 1897 CG ASN B 54 8648 9197 8309 -6696 1136 -1598 C ATOM 1898 OD1 ASN B 54 -0.877 -13.224 38.122 1.00 71.88 O ANISOU 1898 OD1 ASN B 54 9614 9216 8481 -7322 1200 -1498 O ATOM 1899 ND2 ASN B 54 -1.333 -12.041 36.280 1.00 69.13 N ANISOU 1899 ND2 ASN B 54 8372 9578 8316 -6661 1070 -1835 N ATOM 1900 N LYS B 55 -0.669 -12.239 41.414 1.00 72.92 N ANISOU 1900 N LYS B 55 9485 9691 8531 -7323 1407 -1123 N ATOM 1901 CA LYS B 55 -0.327 -13.312 42.355 1.00 77.16 C ANISOU 1901 CA LYS B 55 10831 9630 8858 -7816 1451 -870 C ATOM 1902 C LYS B 55 0.013 -14.640 41.667 1.00 80.09 C ANISOU 1902 C LYS B 55 12090 9199 9142 -8121 1371 -803 C ATOM 1903 O LYS B 55 1.071 -15.217 41.928 1.00 80.16 O ANISOU 1903 O LYS B 55 12850 8377 9230 -7818 1269 -557 O ATOM 1904 CB LYS B 55 -1.436 -13.489 43.398 1.00 82.00 C ANISOU 1904 CB LYS B 55 11225 10873 9057 -8662 1642 -929 C ATOM 1905 CG LYS B 55 -1.587 -12.300 44.363 1.00 80.81 C ANISOU 1905 CG LYS B 55 10381 11370 8952 -8308 1716 -958 C ATOM 1906 CD LYS B 55 -2.668 -12.594 45.410 1.00 91.41 C ANISOU 1906 CD LYS B 55 11535 13374 9822 -9197 1929 -1026 C ATOM 1907 CE LYS B 55 -3.001 -11.363 46.254 1.00 90.65 C ANISOU 1907 CE LYS B 55 10646 14069 9729 -8829 2007 -1153 C ATOM 1908 NZ LYS B 55 -4.269 -10.726 45.788 1.00 94.72 N ANISOU 1908 NZ LYS B 55 10208 15693 10090 -8948 2080 -1569 N ATOM 1909 N THR B 56 -0.862 -15.098 40.777 1.00 83.30 N ANISOU 1909 N THR B 56 12407 9872 9371 -8663 1396 -1047 N ATOM 1910 CA THR B 56 -0.599 -16.279 39.951 1.00 86.33 C ANISOU 1910 CA THR B 56 13609 9519 9674 -8916 1302 -1053 C ATOM 1911 C THR B 56 0.806 -16.244 39.303 1.00 81.73 C ANISOU 1911 C THR B 56 13410 8190 9455 -7949 1127 -929 C ATOM 1912 O THR B 56 1.623 -17.145 39.508 1.00 83.46 O ANISOU 1912 O THR B 56 14533 7540 9637 -7847 1034 -739 O ATOM 1913 CB THR B 56 -1.707 -16.442 38.879 1.00 89.28 C ANISOU 1913 CB THR B 56 13588 10461 9874 -9458 1329 -1403 C ATOM 1914 OG1 THR B 56 -2.836 -17.115 39.453 1.00 97.32 O ANISOU 1914 OG1 THR B 56 14686 11857 10433 -10606 1481 -1489 O ATOM 1915 CG2 THR B 56 -1.217 -17.242 37.676 1.00 90.49 C ANISOU 1915 CG2 THR B 56 14377 9917 10088 -9324 1187 -1472 C ATOM 1916 N GLU B 57 1.090 -15.184 38.553 1.00 76.15 N ANISOU 1916 N GLU B 57 12019 7853 9063 -7227 1078 -1040 N ATOM 1917 CA GLU B 57 2.325 -15.099 37.757 1.00 72.31 C ANISOU 1917 CA GLU B 57 11765 6833 8876 -6389 942 -980 C ATOM 1918 C GLU B 57 3.630 -14.721 38.496 1.00 67.88 C ANISOU 1918 C GLU B 57 11360 5883 8550 -5670 882 -718 C ATOM 1919 O GLU B 57 4.707 -14.835 37.909 1.00 66.31 O ANISOU 1919 O GLU B 57 11416 5244 8535 -5041 777 -676 O ATOM 1920 CB GLU B 57 2.116 -14.190 36.530 1.00 69.33 C ANISOU 1920 CB GLU B 57 10684 6976 8684 -5982 914 -1195 C ATOM 1921 CG GLU B 57 1.079 -14.733 35.524 1.00 73.66 C ANISOU 1921 CG GLU B 57 11186 7799 9004 -6558 915 -1478 C ATOM 1922 CD GLU B 57 1.406 -16.142 35.007 1.00 79.52 C ANISOU 1922 CD GLU B 57 12862 7757 9593 -6840 844 -1500 C ATOM 1923 OE1 GLU B 57 2.570 -16.387 34.610 1.00 79.17 O ANISOU 1923 OE1 GLU B 57 13261 7096 9725 -6206 748 -1407 O ATOM 1924 OE2 GLU B 57 0.495 -16.999 34.979 1.00 82.82 O ANISOU 1924 OE2 GLU B 57 13575 8203 9692 -7698 882 -1636 O ATOM 1925 N ASP B 58 3.539 -14.313 39.765 1.00 66.49 N ANISOU 1925 N ASP B 58 11020 5912 8331 -5777 948 -567 N ATOM 1926 CA ASP B 58 4.694 -13.775 40.509 1.00 62.73 C ANISOU 1926 CA ASP B 58 10542 5227 8066 -5116 888 -354 C ATOM 1927 C ASP B 58 5.257 -12.513 39.835 1.00 57.34 C ANISOU 1927 C ASP B 58 9193 4870 7723 -4399 857 -425 C ATOM 1928 O ASP B 58 6.486 -12.346 39.703 1.00 54.92 O ANISOU 1928 O ASP B 58 9002 4248 7616 -3768 768 -322 O ATOM 1929 CB ASP B 58 5.808 -14.825 40.697 1.00 64.54 C ANISOU 1929 CB ASP B 58 11660 4606 8257 -4827 753 -171 C ATOM 1930 CG ASP B 58 5.417 -15.939 41.653 1.00 69.56 C ANISOU 1930 CG ASP B 58 13070 4826 8534 -5473 762 -16 C ATOM 1931 OD1 ASP B 58 4.691 -15.669 42.627 1.00 70.01 O ANISOU 1931 OD1 ASP B 58 12901 5276 8423 -5974 882 43 O ATOM 1932 OD2 ASP B 58 5.846 -17.092 41.430 1.00 70.98 O ANISOU 1932 OD2 ASP B 58 14129 4272 8570 -5474 646 45 O ATOM 1933 N THR B 59 4.349 -11.640 39.396 1.00 55.92 N ANISOU 1933 N THR B 59 8334 5343 7571 -4509 923 -610 N ATOM 1934 CA THR B 59 4.719 -10.347 38.795 1.00 52.06 C ANISOU 1934 CA THR B 59 7264 5167 7348 -3907 893 -665 C ATOM 1935 C THR B 59 3.917 -9.211 39.426 1.00 50.86 C ANISOU 1935 C THR B 59 6473 5666 7184 -3952 954 -745 C ATOM 1936 O THR B 59 2.878 -9.434 40.041 1.00 53.51 O ANISOU 1936 O THR B 59 6676 6371 7285 -4482 1038 -830 O ATOM 1937 CB THR B 59 4.467 -10.329 37.264 1.00 52.14 C ANISOU 1937 CB THR B 59 7137 5282 7393 -3805 855 -847 C ATOM 1938 OG1 THR B 59 3.115 -10.720 36.994 1.00 55.99 O ANISOU 1938 OG1 THR B 59 7478 6162 7636 -4410 902 -1047 O ATOM 1939 CG2 THR B 59 5.401 -11.290 36.531 1.00 53.33 C ANISOU 1939 CG2 THR B 59 7871 4816 7575 -3601 787 -806 C ATOM 1940 N ILE B 60 4.406 -7.992 39.266 1.00 47.40 N ANISOU 1940 N ILE B 60 5661 5380 6968 -3403 913 -732 N ATOM 1941 CA ILE B 60 3.654 -6.809 39.627 1.00 46.86 C ANISOU 1941 CA ILE B 60 5024 5892 6890 -3307 933 -854 C ATOM 1942 C ILE B 60 3.702 -5.865 38.440 1.00 44.85 C ANISOU 1942 C ILE B 60 4473 5789 6778 -2855 855 -946 C ATOM 1943 O ILE B 60 4.786 -5.405 38.017 1.00 41.78 O ANISOU 1943 O ILE B 60 4195 5082 6596 -2427 804 -822 O ATOM 1944 CB ILE B 60 4.267 -6.044 40.833 1.00 45.30 C ANISOU 1944 CB ILE B 60 4756 5659 6795 -3051 936 -724 C ATOM 1945 CG1 ILE B 60 4.430 -6.929 42.068 1.00 48.05 C ANISOU 1945 CG1 ILE B 60 5468 5795 6995 -3419 993 -580 C ATOM 1946 CG2 ILE B 60 3.421 -4.819 41.183 1.00 46.49 C ANISOU 1946 CG2 ILE B 60 4366 6393 6904 -2905 942 -896 C ATOM 1947 CD1 ILE B 60 5.318 -6.276 43.167 1.00 44.82 C ANISOU 1947 CD1 ILE B 60 5065 5265 6700 -3105 964 -432 C ATOM 1948 N PHE B 61 2.528 -5.541 37.931 1.00 46.03 N ANISOU 1948 N PHE B 61 4236 6472 6782 -2955 842 -1167 N ATOM 1949 CA PHE B 61 2.409 -4.538 36.911 1.00 45.23 C ANISOU 1949 CA PHE B 61 3865 6566 6754 -2504 744 -1254 C ATOM 1950 C PHE B 61 2.634 -3.181 37.567 1.00 44.12 C ANISOU 1950 C PHE B 61 3519 6521 6726 -2071 703 -1217 C ATOM 1951 O PHE B 61 2.031 -2.863 38.596 1.00 45.86 O ANISOU 1951 O PHE B 61 3505 7078 6843 -2159 739 -1306 O ATOM 1952 CB PHE B 61 1.034 -4.603 36.261 1.00 48.61 C ANISOU 1952 CB PHE B 61 3918 7604 6946 -2696 711 -1525 C ATOM 1953 CG PHE B 61 0.881 -3.718 35.060 1.00 47.57 C ANISOU 1953 CG PHE B 61 3594 7641 6838 -2219 578 -1605 C ATOM 1954 CD1 PHE B 61 -0.177 -2.824 34.980 1.00 50.31 C ANISOU 1954 CD1 PHE B 61 3469 8615 7030 -1972 486 -1822 C ATOM 1955 CD2 PHE B 61 1.774 -3.784 34.006 1.00 44.90 C ANISOU 1955 CD2 PHE B 61 3555 6871 6635 -1992 537 -1474 C ATOM 1956 CE1 PHE B 61 -0.339 -2.008 33.865 1.00 49.42 C ANISOU 1956 CE1 PHE B 61 3256 8627 6897 -1493 331 -1877 C ATOM 1957 CE2 PHE B 61 1.608 -2.971 32.884 1.00 45.68 C ANISOU 1957 CE2 PHE B 61 3527 7124 6704 -1586 414 -1524 C ATOM 1958 CZ PHE B 61 0.538 -2.081 32.824 1.00 46.75 C ANISOU 1958 CZ PHE B 61 3256 7825 6682 -1333 299 -1713 C ATOM 1959 N LEU B 62 3.514 -2.405 36.954 1.00 40.95 N ANISOU 1959 N LEU B 62 3233 5820 6504 -1639 634 -1097 N ATOM 1960 CA LEU B 62 3.923 -1.112 37.463 1.00 40.09 C ANISOU 1960 CA LEU B 62 3067 5659 6508 -1257 581 -1041 C ATOM 1961 C LEU B 62 3.612 -0.020 36.448 1.00 40.34 C ANISOU 1961 C LEU B 62 2997 5813 6515 -840 453 -1108 C ATOM 1962 O LEU B 62 4.057 -0.086 35.305 1.00 39.81 O ANISOU 1962 O LEU B 62 3086 5554 6485 -743 424 -1032 O ATOM 1963 CB LEU B 62 5.432 -1.140 37.761 1.00 36.84 C ANISOU 1963 CB LEU B 62 2964 4734 6299 -1187 614 -806 C ATOM 1964 CG LEU B 62 6.191 0.164 37.943 1.00 35.70 C ANISOU 1964 CG LEU B 62 2865 4413 6285 -854 557 -714 C ATOM 1965 CD1 LEU B 62 5.887 0.677 39.326 1.00 36.91 C ANISOU 1965 CD1 LEU B 62 2901 4713 6410 -853 557 -775 C ATOM 1966 CD2 LEU B 62 7.690 -0.044 37.772 1.00 34.41 C ANISOU 1966 CD2 LEU B 62 2937 3860 6276 -836 593 -518 C ATOM 1967 N ARG B 63 2.853 0.980 36.883 1.00 42.14 N ANISOU 1967 N ARG B 63 3000 6359 6651 -567 370 -1256 N ATOM 1968 CA ARG B 63 2.534 2.129 36.069 1.00 43.29 C ANISOU 1968 CA ARG B 63 3140 6571 6738 -89 209 -1313 C ATOM 1969 C ARG B 63 3.197 3.319 36.738 1.00 42.52 C ANISOU 1969 C ARG B 63 3252 6153 6752 202 158 -1218 C ATOM 1970 O ARG B 63 2.843 3.701 37.849 1.00 43.22 O ANISOU 1970 O ARG B 63 3206 6412 6802 263 160 -1333 O ATOM 1971 CB ARG B 63 1.030 2.307 35.981 1.00 47.12 C ANISOU 1971 CB ARG B 63 3210 7723 6971 66 116 -1615 C ATOM 1972 CG ARG B 63 0.367 1.297 35.053 1.00 50.86 C ANISOU 1972 CG ARG B 63 3497 8528 7301 -215 128 -1728 C ATOM 1973 CD ARG B 63 -1.165 1.166 35.216 1.00 58.92 C ANISOU 1973 CD ARG B 63 3976 10380 8031 -252 83 -2074 C ATOM 1974 NE ARG B 63 -1.825 2.232 35.975 1.00 64.46 N ANISOU 1974 NE ARG B 63 4414 11464 8615 192 -11 -2266 N ATOM 1975 CZ ARG B 63 -2.428 3.301 35.443 1.00 69.75 C ANISOU 1975 CZ ARG B 63 4973 12391 9137 837 -230 -2422 C ATOM 1976 NH1 ARG B 63 -2.428 3.495 34.122 1.00 71.50 N ANISOU 1976 NH1 ARG B 63 5339 12519 9311 1093 -379 -2373 N ATOM 1977 NH2 ARG B 63 -3.027 4.190 36.238 1.00 69.93 N ANISOU 1977 NH2 ARG B 63 4778 12760 9033 1267 -315 -2633 N ATOM 1978 N GLU B 64 4.179 3.891 36.065 1.00 40.94 N ANISOU 1978 N GLU B 64 3394 5502 6662 336 121 -1018 N ATOM 1979 CA GLU B 64 5.030 4.856 36.707 1.00 40.10 C ANISOU 1979 CA GLU B 64 3546 5024 6666 448 100 -901 C ATOM 1980 C GLU B 64 4.920 6.216 36.064 1.00 40.86 C ANISOU 1980 C GLU B 64 3923 4928 6673 866 -74 -887 C ATOM 1981 O GLU B 64 4.997 6.350 34.850 1.00 40.88 O ANISOU 1981 O GLU B 64 4089 4833 6612 964 -129 -796 O ATOM 1982 CB GLU B 64 6.469 4.375 36.688 1.00 38.03 C ANISOU 1982 CB GLU B 64 3474 4393 6583 147 226 -670 C ATOM 1983 CG GLU B 64 7.421 5.283 37.424 1.00 40.87 C ANISOU 1983 CG GLU B 64 4053 4433 7041 155 216 -567 C ATOM 1984 CD GLU B 64 8.843 4.833 37.237 1.00 45.17 C ANISOU 1984 CD GLU B 64 4705 4741 7716 -109 328 -371 C ATOM 1985 OE1 GLU B 64 9.349 4.116 38.118 1.00 45.94 O ANISOU 1985 OE1 GLU B 64 4696 4860 7897 -301 408 -349 O ATOM 1986 OE2 GLU B 64 9.439 5.175 36.194 1.00 49.16 O ANISOU 1986 OE2 GLU B 64 5391 5080 8207 -107 331 -247 O ATOM 1987 N TYR B 65 4.733 7.214 36.920 1.00 41.91 N ANISOU 1987 N TYR B 65 4160 4987 6776 1116 -167 -981 N ATOM 1988 CA TYR B 65 4.638 8.617 36.525 1.00 43.30 C ANISOU 1988 CA TYR B 65 4739 4873 6842 1547 -363 -975 C ATOM 1989 C TYR B 65 5.803 9.384 37.182 1.00 42.71 C ANISOU 1989 C TYR B 65 5056 4283 6889 1383 -340 -826 C ATOM 1990 O TYR B 65 5.733 9.800 38.346 1.00 42.05 O ANISOU 1990 O TYR B 65 4963 4194 6822 1445 -359 -953 O ATOM 1991 CB TYR B 65 3.279 9.196 36.934 1.00 46.73 C ANISOU 1991 CB TYR B 65 4992 5690 7074 2068 -535 -1285 C ATOM 1992 CG TYR B 65 2.053 8.534 36.300 1.00 47.14 C ANISOU 1992 CG TYR B 65 4591 6369 6952 2225 -580 -1482 C ATOM 1993 CD1 TYR B 65 1.606 7.280 36.732 1.00 45.69 C ANISOU 1993 CD1 TYR B 65 3888 6687 6784 1836 -411 -1598 C ATOM 1994 CD2 TYR B 65 1.334 9.173 35.288 1.00 49.05 C ANISOU 1994 CD2 TYR B 65 4950 6708 6978 2741 -805 -1558 C ATOM 1995 CE1 TYR B 65 0.483 6.674 36.160 1.00 47.85 C ANISOU 1995 CE1 TYR B 65 3734 7577 6869 1885 -448 -1802 C ATOM 1996 CE2 TYR B 65 0.206 8.574 34.712 1.00 51.20 C ANISOU 1996 CE2 TYR B 65 4751 7640 7063 2870 -861 -1771 C ATOM 1997 CZ TYR B 65 -0.212 7.328 35.160 1.00 50.22 C ANISOU 1997 CZ TYR B 65 4076 8041 6965 2406 -674 -1903 C ATOM 1998 OH TYR B 65 -1.314 6.712 34.599 1.00 53.69 O ANISOU 1998 OH TYR B 65 4037 9169 7196 2428 -720 -2132 O ATOM 1999 N GLN B 66 6.881 9.539 36.422 1.00 42.35 N ANISOU 1999 N GLN B 66 5326 3861 6903 1134 -288 -573 N ATOM 2000 CA GLN B 66 8.104 10.159 36.903 1.00 42.68 C ANISOU 2000 CA GLN B 66 5689 3489 7038 849 -242 -426 C ATOM 2001 C GLN B 66 8.273 11.534 36.289 1.00 46.57 C ANISOU 2001 C GLN B 66 6809 3506 7381 1021 -402 -326 C ATOM 2002 O GLN B 66 8.079 11.710 35.086 1.00 48.33 O ANISOU 2002 O GLN B 66 7245 3646 7470 1151 -466 -217 O ATOM 2003 CB GLN B 66 9.300 9.290 36.527 1.00 40.80 C ANISOU 2003 CB GLN B 66 5316 3255 6933 378 -44 -230 C ATOM 2004 CG GLN B 66 10.623 9.797 37.041 1.00 43.03 C ANISOU 2004 CG GLN B 66 5797 3262 7290 21 21 -107 C ATOM 2005 CD GLN B 66 11.666 8.709 37.053 1.00 43.17 C ANISOU 2005 CD GLN B 66 5497 3469 7436 -337 207 -10 C ATOM 2006 OE1 GLN B 66 12.457 8.618 36.127 1.00 45.51 O ANISOU 2006 OE1 GLN B 66 5860 3730 7702 -540 293 139 O ATOM 2007 NE2 GLN B 66 11.665 7.868 38.091 1.00 40.09 N ANISOU 2007 NE2 GLN B 66 4777 3300 7155 -388 263 -100 N ATOM 2008 N THR B 67 8.631 12.508 37.115 1.00 48.06 N ANISOU 2008 N THR B 67 7346 3352 7561 1007 -478 -360 N ATOM 2009 CA THR B 67 8.919 13.848 36.614 1.00 52.36 C ANISOU 2009 CA THR B 67 8626 3327 7940 1076 -632 -244 C ATOM 2010 C THR B 67 10.412 14.104 36.676 1.00 52.14 C ANISOU 2010 C THR B 67 8830 3003 7978 432 -493 -35 C ATOM 2011 O THR B 67 11.023 13.960 37.726 1.00 50.53 O ANISOU 2011 O THR B 67 8432 2861 7906 146 -407 -99 O ATOM 2012 CB THR B 67 8.132 14.926 37.377 1.00 55.62 C ANISOU 2012 CB THR B 67 9401 3506 8225 1581 -866 -470 C ATOM 2013 OG1 THR B 67 6.736 14.635 37.266 1.00 56.26 O ANISOU 2013 OG1 THR B 67 9153 4015 8209 2189 -986 -696 O ATOM 2014 CG2 THR B 67 8.392 16.325 36.793 1.00 61.44 C ANISOU 2014 CG2 THR B 67 11056 3539 8748 1673 -1060 -334 C ATOM 2015 N ARG B 68 10.991 14.434 35.527 1.00 54.50 N ANISOU 2015 N ARG B 68 9498 3058 8153 189 -464 205 N ATOM 2016 CA ARG B 68 12.395 14.831 35.432 1.00 56.54 C ANISOU 2016 CA ARG B 68 10008 3082 8393 -471 -332 397 C ATOM 2017 C ARG B 68 12.454 16.013 34.486 1.00 61.75 C ANISOU 2017 C ARG B 68 11501 3185 8775 -509 -462 588 C ATOM 2018 O ARG B 68 11.709 16.058 33.500 1.00 63.28 O ANISOU 2018 O ARG B 68 11887 3340 8818 -126 -569 653 O ATOM 2019 CB ARG B 68 13.267 13.716 34.857 1.00 53.74 C ANISOU 2019 CB ARG B 68 9129 3155 8135 -877 -80 524 C ATOM 2020 CG ARG B 68 13.158 12.355 35.555 1.00 50.29 C ANISOU 2020 CG ARG B 68 7940 3235 7932 -794 36 375 C ATOM 2021 CD ARG B 68 14.211 11.385 35.029 1.00 51.46 C ANISOU 2021 CD ARG B 68 7685 3727 8140 -1169 260 485 C ATOM 2022 NE ARG B 68 14.178 11.295 33.573 1.00 53.91 N ANISOU 2022 NE ARG B 68 8137 4049 8297 -1170 306 633 N ATOM 2023 CZ ARG B 68 13.505 10.378 32.879 1.00 53.70 C ANISOU 2023 CZ ARG B 68 7847 4273 8282 -887 323 597 C ATOM 2024 NH1 ARG B 68 12.800 9.431 33.507 1.00 51.27 N ANISOU 2024 NH1 ARG B 68 7129 4221 8131 -627 308 425 N ATOM 2025 NH2 ARG B 68 13.548 10.398 31.549 1.00 53.89 N ANISOU 2025 NH2 ARG B 68 8041 4302 8131 -913 359 732 N ATOM 2026 N GLN B 69 13.345 16.956 34.767 1.00 65.01 N ANISOU 2026 N GLN B 69 12438 3173 9091 -1001 -460 683 N ATOM 2027 CA GLN B 69 13.515 18.123 33.902 1.00 71.15 C ANISOU 2027 CA GLN B 69 14139 3335 9557 -1162 -575 901 C ATOM 2028 C GLN B 69 12.176 18.757 33.542 1.00 74.12 C ANISOU 2028 C GLN B 69 15056 3349 9755 -354 -885 840 C ATOM 2029 O GLN B 69 11.895 19.040 32.368 1.00 76.97 O ANISOU 2029 O GLN B 69 15853 3513 9878 -203 -968 1033 O ATOM 2030 CB GLN B 69 14.287 17.741 32.642 1.00 71.26 C ANISOU 2030 CB GLN B 69 14080 3548 9446 -1653 -366 1172 C ATOM 2031 CG GLN B 69 15.748 17.519 32.911 1.00 71.95 C ANISOU 2031 CG GLN B 69 13849 3900 9589 -2493 -101 1238 C ATOM 2032 CD GLN B 69 16.292 16.364 32.139 1.00 70.38 C ANISOU 2032 CD GLN B 69 12961 4335 9445 -2695 154 1315 C ATOM 2033 OE1 GLN B 69 16.891 16.544 31.088 1.00 74.24 O ANISOU 2033 OE1 GLN B 69 13668 4839 9702 -3110 283 1530 O ATOM 2034 NE2 GLN B 69 16.072 15.157 32.643 1.00 65.77 N ANISOU 2034 NE2 GLN B 69 11579 4271 9139 -2397 228 1134 N ATOM 2035 N ASN B 70 11.353 18.951 34.573 1.00 73.85 N ANISOU 2035 N ASN B 70 14955 3293 9811 193 -1059 554 N ATOM 2036 CA ASN B 70 10.066 19.633 34.472 1.00 77.43 C ANISOU 2036 CA ASN B 70 15874 3469 10078 1059 -1384 408 C ATOM 2037 C ASN B 70 9.081 19.032 33.466 1.00 76.61 C ANISOU 2037 C ASN B 70 15457 3757 9893 1626 -1458 414 C ATOM 2038 O ASN B 70 8.275 19.751 32.882 1.00 81.53 O ANISOU 2038 O ASN B 70 16661 4067 10249 2239 -1738 415 O ATOM 2039 CB ASN B 70 10.294 21.124 34.208 1.00 84.56 C ANISOU 2039 CB ASN B 70 18000 3460 10669 1017 -1609 550 C ATOM 2040 CG ASN B 70 11.422 21.681 35.041 1.00 86.06 C ANISOU 2040 CG ASN B 70 18510 3283 10906 266 -1506 570 C ATOM 2041 OD1 ASN B 70 11.351 21.681 36.266 1.00 84.93 O ANISOU 2041 OD1 ASN B 70 18107 3239 10923 353 -1521 304 O ATOM 2042 ND2 ASN B 70 12.481 22.143 34.382 1.00 90.16 N ANISOU 2042 ND2 ASN B 70 19564 3436 11257 -520 -1392 876 N ATOM 2043 N GLN B 71 9.144 17.715 33.264 1.00 71.43 N ANISOU 2043 N GLN B 71 13917 3780 9444 1439 -1227 405 N ATOM 2044 CA GLN B 71 8.162 17.049 32.411 1.00 70.35 C ANISOU 2044 CA GLN B 71 13404 4090 9237 1932 -1293 356 C ATOM 2045 C GLN B 71 7.870 15.611 32.834 1.00 64.14 C ANISOU 2045 C GLN B 71 11597 4058 8715 1881 -1098 174 C ATOM 2046 O GLN B 71 8.631 14.996 33.591 1.00 60.50 O ANISOU 2046 O GLN B 71 10724 3771 8493 1395 -875 161 O ATOM 2047 CB GLN B 71 8.537 17.156 30.924 1.00 72.39 C ANISOU 2047 CB GLN B 71 14059 4172 9274 1729 -1273 671 C ATOM 2048 CG GLN B 71 9.847 16.495 30.536 1.00 71.11 C ANISOU 2048 CG GLN B 71 13628 4164 9229 899 -939 893 C ATOM 2049 CD GLN B 71 10.393 17.035 29.230 1.00 76.01 C ANISOU 2049 CD GLN B 71 14888 4446 9545 601 -927 1225 C ATOM 2050 OE1 GLN B 71 10.597 16.291 28.269 1.00 76.57 O ANISOU 2050 OE1 GLN B 71 14650 4871 9574 432 -777 1339 O ATOM 2051 NE2 GLN B 71 10.624 18.328 29.186 1.00 79.07 N ANISOU 2051 NE2 GLN B 71 16217 4137 9690 521 -1086 1378 N ATOM 2052 N CYS B 72 6.751 15.088 32.348 1.00 63.44 N ANISOU 2052 N CYS B 72 11139 4416 8551 2381 -1200 28 N ATOM 2053 CA CYS B 72 6.306 13.764 32.742 1.00 58.93 C ANISOU 2053 CA CYS B 72 9693 4525 8173 2330 -1044 -163 C ATOM 2054 C CYS B 72 6.870 12.659 31.857 1.00 55.14 C ANISOU 2054 C CYS B 72 8872 4303 7773 1886 -823 3 C ATOM 2055 O CYS B 72 6.823 12.733 30.635 1.00 56.58 O ANISOU 2055 O CYS B 72 9284 4437 7778 1952 -874 150 O ATOM 2056 CB CYS B 72 4.785 13.688 32.759 1.00 60.84 C ANISOU 2056 CB CYS B 72 9620 5227 8269 3018 -1250 -460 C ATOM 2057 SG CYS B 72 4.181 12.213 33.590 1.00 58.85 S ANISOU 2057 SG CYS B 72 8376 5771 8214 2852 -1056 -729 S ATOM 2058 N PHE B 73 7.396 11.619 32.488 1.00 50.67 N ANISOU 2058 N PHE B 73 7787 4011 7452 1470 -590 -33 N ATOM 2059 CA PHE B 73 7.734 10.410 31.760 1.00 47.15 C ANISOU 2059 CA PHE B 73 6966 3872 7076 1170 -405 39 C ATOM 2060 C PHE B 73 6.910 9.270 32.323 1.00 44.89 C ANISOU 2060 C PHE B 73 6061 4097 6898 1238 -356 -199 C ATOM 2061 O PHE B 73 7.052 8.913 33.493 1.00 43.81 O ANISOU 2061 O PHE B 73 5674 4050 6923 1084 -269 -294 O ATOM 2062 CB PHE B 73 9.244 10.140 31.815 1.00 44.85 C ANISOU 2062 CB PHE B 73 6700 3421 6920 601 -177 234 C ATOM 2063 CG PHE B 73 10.061 11.242 31.196 1.00 47.97 C ANISOU 2063 CG PHE B 73 7698 3373 7156 404 -196 471 C ATOM 2064 CD1 PHE B 73 10.229 11.307 29.813 1.00 49.92 C ANISOU 2064 CD1 PHE B 73 8182 3585 7201 355 -182 647 C ATOM 2065 CD2 PHE B 73 10.610 12.250 31.987 1.00 49.05 C ANISOU 2065 CD2 PHE B 73 8212 3123 7303 241 -237 514 C ATOM 2066 CE1 PHE B 73 10.957 12.363 29.218 1.00 54.16 C ANISOU 2066 CE1 PHE B 73 9344 3703 7531 101 -191 891 C ATOM 2067 CE2 PHE B 73 11.350 13.301 31.405 1.00 52.58 C ANISOU 2067 CE2 PHE B 73 9295 3127 7557 -39 -253 742 C ATOM 2068 CZ PHE B 73 11.523 13.355 30.020 1.00 53.92 C ANISOU 2068 CZ PHE B 73 9714 3264 7509 -126 -223 942 C ATOM 2069 N TYR B 74 6.036 8.708 31.494 1.00 44.80 N ANISOU 2069 N TYR B 74 5827 4431 6762 1432 -416 -295 N ATOM 2070 CA TYR B 74 5.226 7.574 31.914 1.00 42.87 C ANISOU 2070 CA TYR B 74 5026 4691 6570 1386 -358 -519 C ATOM 2071 C TYR B 74 5.791 6.266 31.371 1.00 40.57 C ANISOU 2071 C TYR B 74 4537 4505 6373 982 -167 -447 C ATOM 2072 O TYR B 74 6.140 6.189 30.206 1.00 40.30 O ANISOU 2072 O TYR B 74 4669 4396 6249 950 -155 -324 O ATOM 2073 CB TYR B 74 3.792 7.740 31.421 1.00 45.69 C ANISOU 2073 CB TYR B 74 5205 5461 6695 1839 -563 -737 C ATOM 2074 CG TYR B 74 2.946 6.484 31.595 1.00 43.72 C ANISOU 2074 CG TYR B 74 4381 5793 6439 1660 -487 -965 C ATOM 2075 CD1 TYR B 74 2.816 5.549 30.565 1.00 41.85 C ANISOU 2075 CD1 TYR B 74 4003 5761 6137 1469 -440 -968 C ATOM 2076 CD2 TYR B 74 2.272 6.243 32.799 1.00 44.64 C ANISOU 2076 CD2 TYR B 74 4127 6256 6578 1637 -457 -1188 C ATOM 2077 CE1 TYR B 74 2.020 4.394 30.733 1.00 42.86 C ANISOU 2077 CE1 TYR B 74 3670 6389 6228 1219 -375 -1188 C ATOM 2078 CE2 TYR B 74 1.489 5.099 32.983 1.00 44.66 C ANISOU 2078 CE2 TYR B 74 3646 6792 6529 1365 -373 -1388 C ATOM 2079 CZ TYR B 74 1.370 4.178 31.954 1.00 43.37 C ANISOU 2079 CZ TYR B 74 3389 6781 6306 1136 -336 -1385 C ATOM 2080 OH TYR B 74 0.579 3.071 32.154 1.00 45.58 O ANISOU 2080 OH TYR B 74 3256 7556 6505 793 -258 -1591 O ATOM 2081 N ASN B 75 5.858 5.249 32.225 1.00 39.49 N ANISOU 2081 N ASN B 75 4090 4529 6385 699 -28 -532 N ATOM 2082 CA ASN B 75 6.270 3.897 31.840 1.00 38.96 C ANISOU 2082 CA ASN B 75 3880 4538 6386 372 125 -511 C ATOM 2083 C ASN B 75 5.461 2.848 32.560 1.00 38.78 C ANISOU 2083 C ASN B 75 3525 4839 6371 191 171 -702 C ATOM 2084 O ASN B 75 5.197 2.972 33.759 1.00 38.88 O ANISOU 2084 O ASN B 75 3411 4928 6433 161 181 -776 O ATOM 2085 CB ASN B 75 7.761 3.673 32.122 1.00 38.09 C ANISOU 2085 CB ASN B 75 3910 4119 6443 119 280 -326 C ATOM 2086 CG ASN B 75 8.639 4.363 31.106 1.00 41.18 C ANISOU 2086 CG ASN B 75 4587 4288 6770 137 294 -139 C ATOM 2087 OD1 ASN B 75 9.043 5.516 31.304 1.00 46.48 O ANISOU 2087 OD1 ASN B 75 5507 4725 7427 188 245 -28 O ATOM 2088 ND2 ASN B 75 8.892 3.694 29.982 1.00 41.16 N ANISOU 2088 ND2 ASN B 75 4587 4361 6691 71 359 -111 N ATOM 2089 N SER B 76 5.039 1.824 31.828 1.00 39.46 N ANISOU 2089 N SER B 76 3495 5124 6375 35 199 -791 N ATOM 2090 CA SER B 76 4.507 0.624 32.472 1.00 39.84 C ANISOU 2090 CA SER B 76 3337 5383 6420 -298 280 -931 C ATOM 2091 C SER B 76 5.348 -0.585 32.099 1.00 39.13 C ANISOU 2091 C SER B 76 3424 5039 6404 -571 402 -848 C ATOM 2092 O SER B 76 5.892 -0.663 30.989 1.00 39.76 O ANISOU 2092 O SER B 76 3655 4991 6462 -492 408 -780 O ATOM 2093 CB SER B 76 3.036 0.386 32.139 1.00 42.31 C ANISOU 2093 CB SER B 76 3339 6223 6514 -310 190 -1184 C ATOM 2094 OG SER B 76 2.910 -0.159 30.850 1.00 43.27 O ANISOU 2094 OG SER B 76 3506 6408 6527 -358 162 -1222 O ATOM 2095 N SER B 77 5.456 -1.513 33.040 1.00 38.42 N ANISOU 2095 N SER B 77 3350 4877 6371 -864 491 -859 N ATOM 2096 CA SER B 77 6.250 -2.710 32.877 1.00 38.00 C ANISOU 2096 CA SER B 77 3536 4533 6369 -1055 578 -798 C ATOM 2097 C SER B 77 5.821 -3.672 33.961 1.00 38.71 C ANISOU 2097 C SER B 77 3659 4626 6422 -1407 630 -850 C ATOM 2098 O SER B 77 4.942 -3.362 34.776 1.00 39.18 O ANISOU 2098 O SER B 77 3498 4978 6412 -1524 621 -936 O ATOM 2099 CB SER B 77 7.747 -2.393 33.036 1.00 36.26 C ANISOU 2099 CB SER B 77 3478 3988 6310 -877 629 -606 C ATOM 2100 OG SER B 77 7.970 -1.791 34.300 1.00 38.07 O ANISOU 2100 OG SER B 77 3645 4186 6636 -859 631 -536 O ATOM 2101 N TYR B 78 6.440 -4.844 33.955 1.00 38.71 N ANISOU 2101 N TYR B 78 3966 4309 6434 -1564 679 -804 N ATOM 2102 CA TYR B 78 6.263 -5.818 35.012 1.00 40.07 C ANISOU 2102 CA TYR B 78 4328 4347 6550 -1901 722 -793 C ATOM 2103 C TYR B 78 7.542 -6.018 35.797 1.00 38.95 C ANISOU 2103 C TYR B 78 4424 3838 6538 -1735 738 -613 C ATOM 2104 O TYR B 78 8.635 -6.132 35.221 1.00 38.73 O ANISOU 2104 O TYR B 78 4535 3585 6596 -1457 732 -547 O ATOM 2105 CB TYR B 78 5.847 -7.144 34.425 1.00 41.98 C ANISOU 2105 CB TYR B 78 4855 4458 6639 -2231 728 -902 C ATOM 2106 CG TYR B 78 4.450 -7.137 33.896 1.00 45.58 C ANISOU 2106 CG TYR B 78 5043 5365 6911 -2524 710 -1112 C ATOM 2107 CD1 TYR B 78 4.188 -6.729 32.589 1.00 46.91 C ANISOU 2107 CD1 TYR B 78 5039 5742 7041 -2329 650 -1222 C ATOM 2108 CD2 TYR B 78 3.378 -7.541 34.697 1.00 47.51 C ANISOU 2108 CD2 TYR B 78 5181 5892 6977 -3013 751 -1214 C ATOM 2109 CE1 TYR B 78 2.901 -6.736 32.085 1.00 48.28 C ANISOU 2109 CE1 TYR B 78 4925 6403 7015 -2565 605 -1441 C ATOM 2110 CE2 TYR B 78 2.087 -7.545 34.207 1.00 50.85 C ANISOU 2110 CE2 TYR B 78 5275 6851 7195 -3298 731 -1447 C ATOM 2111 CZ TYR B 78 1.854 -7.146 32.901 1.00 51.39 C ANISOU 2111 CZ TYR B 78 5158 7130 7239 -3049 645 -1568 C ATOM 2112 OH TYR B 78 0.581 -7.163 32.396 1.00 53.74 O ANISOU 2112 OH TYR B 78 5091 8022 7304 -3299 599 -1823 O ATOM 2113 N LEU B 79 7.394 -6.041 37.111 1.00 38.70 N ANISOU 2113 N LEU B 79 4399 3817 6487 -1894 756 -552 N ATOM 2114 CA LEU B 79 8.450 -6.449 37.999 1.00 39.13 C ANISOU 2114 CA LEU B 79 4713 3554 6600 -1786 747 -397 C ATOM 2115 C LEU B 79 8.315 -7.937 38.226 1.00 42.52 C ANISOU 2115 C LEU B 79 5620 3663 6874 -2072 744 -383 C ATOM 2116 O LEU B 79 7.186 -8.432 38.341 1.00 44.48 O ANISOU 2116 O LEU B 79 5914 4036 6949 -2523 781 -472 O ATOM 2117 CB LEU B 79 8.302 -5.726 39.334 1.00 38.56 C ANISOU 2117 CB LEU B 79 4453 3657 6542 -1829 757 -340 C ATOM 2118 CG LEU B 79 8.197 -4.201 39.258 1.00 36.98 C ANISOU 2118 CG LEU B 79 3859 3740 6450 -1598 744 -382 C ATOM 2119 CD1 LEU B 79 8.154 -3.604 40.648 1.00 38.64 C ANISOU 2119 CD1 LEU B 79 3954 4072 6654 -1624 746 -349 C ATOM 2120 CD2 LEU B 79 9.396 -3.631 38.493 1.00 38.11 C ANISOU 2120 CD2 LEU B 79 3995 3734 6749 -1251 717 -307 C ATOM 2121 N ASN B 80 9.437 -8.655 38.276 1.00 43.70 N ANISOU 2121 N ASN B 80 6139 3418 7048 -1819 692 -289 N ATOM 2122 CA ASN B 80 9.394 -10.059 38.694 1.00 48.29 C ANISOU 2122 CA ASN B 80 7318 3581 7450 -2040 654 -244 C ATOM 2123 C ASN B 80 9.502 -10.197 40.214 1.00 49.39 C ANISOU 2123 C ASN B 80 7627 3632 7508 -2162 637 -85 C ATOM 2124 O ASN B 80 10.203 -9.416 40.874 1.00 46.91 O ANISOU 2124 O ASN B 80 7057 3453 7312 -1870 614 1 O ATOM 2125 CB ASN B 80 10.415 -10.923 37.949 1.00 50.29 C ANISOU 2125 CB ASN B 80 7978 3426 7702 -1658 575 -260 C ATOM 2126 CG ASN B 80 9.957 -11.290 36.537 1.00 51.69 C ANISOU 2126 CG ASN B 80 8210 3595 7836 -1744 595 -439 C ATOM 2127 OD1 ASN B 80 8.810 -11.680 36.324 1.00 55.45 O ANISOU 2127 OD1 ASN B 80 8775 4121 8174 -2242 629 -535 O ATOM 2128 ND2 ASN B 80 10.860 -11.182 35.573 1.00 50.00 N ANISOU 2128 ND2 ASN B 80 7922 3368 7707 -1284 578 -501 N ATOM 2129 N VAL B 81 8.756 -11.154 40.767 1.00 52.85 N ANISOU 2129 N VAL B 81 8497 3872 7710 -2656 652 -52 N ATOM 2130 CA VAL B 81 8.674 -11.316 42.212 1.00 54.38 C ANISOU 2130 CA VAL B 81 8881 4021 7760 -2872 653 106 C ATOM 2131 C VAL B 81 9.368 -12.616 42.557 1.00 58.93 C ANISOU 2131 C VAL B 81 10265 3956 8171 -2775 532 250 C ATOM 2132 O VAL B 81 9.084 -13.657 41.971 1.00 61.40 O ANISOU 2132 O VAL B 81 11108 3886 8337 -2997 505 205 O ATOM 2133 CB VAL B 81 7.211 -11.304 42.724 1.00 56.26 C ANISOU 2133 CB VAL B 81 8971 4618 7787 -3580 784 44 C ATOM 2134 CG1 VAL B 81 7.157 -11.381 44.252 1.00 57.44 C ANISOU 2134 CG1 VAL B 81 9282 4785 7757 -3803 806 211 C ATOM 2135 CG2 VAL B 81 6.489 -10.059 42.249 1.00 52.56 C ANISOU 2135 CG2 VAL B 81 7734 4783 7452 -3556 865 -141 C ATOM 2136 N GLN B 82 10.314 -12.532 43.480 1.00 59.65 N ANISOU 2136 N GLN B 82 10470 3924 8272 -2398 435 408 N ATOM 2137 CA GLN B 82 11.005 -13.707 43.972 1.00 64.88 C ANISOU 2137 CA GLN B 82 11928 3987 8736 -2205 278 562 C ATOM 2138 C GLN B 82 10.549 -13.852 45.421 1.00 67.10 C ANISOU 2138 C GLN B 82 12448 4270 8777 -2621 299 749 C ATOM 2139 O GLN B 82 11.138 -13.259 46.331 1.00 65.63 O ANISOU 2139 O GLN B 82 12025 4280 8630 -2342 250 848 O ATOM 2140 CB GLN B 82 12.522 -13.532 43.847 1.00 64.39 C ANISOU 2140 CB GLN B 82 11778 3863 8825 -1374 124 574 C ATOM 2141 CG GLN B 82 13.044 -13.326 42.405 1.00 64.51 C ANISOU 2141 CG GLN B 82 11500 3966 9044 -966 130 381 C ATOM 2142 CD GLN B 82 12.796 -11.916 41.802 1.00 61.89 C ANISOU 2142 CD GLN B 82 10310 4234 8973 -1017 276 261 C ATOM 2143 OE1 GLN B 82 12.623 -11.782 40.585 1.00 61.00 O ANISOU 2143 OE1 GLN B 82 10014 4210 8954 -991 335 113 O ATOM 2144 NE2 GLN B 82 12.786 -10.876 42.644 1.00 60.67 N ANISOU 2144 NE2 GLN B 82 9691 4453 8905 -1073 318 324 N ATOM 2145 N ARG B 83 9.474 -14.624 45.610 1.00 70.73 N ANISOU 2145 N ARG B 83 13360 4555 8961 -3344 382 782 N ATOM 2146 CA ARG B 83 8.703 -14.644 46.860 1.00 73.23 C ANISOU 2146 CA ARG B 83 13769 5049 9006 -3948 480 918 C ATOM 2147 C ARG B 83 9.542 -14.965 48.103 1.00 75.77 C ANISOU 2147 C ARG B 83 14567 5067 9156 -3654 330 1174 C ATOM 2148 O ARG B 83 9.402 -14.307 49.140 1.00 74.38 O ANISOU 2148 O ARG B 83 14057 5282 8923 -3764 390 1245 O ATOM 2149 CB ARG B 83 7.538 -15.648 46.762 1.00 78.35 C ANISOU 2149 CB ARG B 83 14963 5489 9319 -4830 584 917 C ATOM 2150 CG ARG B 83 6.386 -15.260 45.813 1.00 77.27 C ANISOU 2150 CG ARG B 83 14242 5867 9251 -5313 759 649 C ATOM 2151 CD ARG B 83 5.283 -16.385 45.805 1.00 83.86 C ANISOU 2151 CD ARG B 83 15681 6498 9684 -6294 853 646 C ATOM 2152 NE ARG B 83 4.093 -15.981 45.050 1.00 83.57 N ANISOU 2152 NE ARG B 83 14988 7111 9653 -6804 1018 367 N ATOM 2153 CZ ARG B 83 3.015 -15.358 45.582 1.00 85.05 C ANISOU 2153 CZ ARG B 83 14521 8096 9698 -7335 1207 257 C ATOM 2154 NH1 ARG B 83 2.952 -15.048 46.887 1.00 86.39 N ANISOU 2154 NH1 ARG B 83 14608 8508 9709 -7472 1280 405 N ATOM 2155 NH2 ARG B 83 1.993 -15.018 44.806 1.00 85.79 N ANISOU 2155 NH2 ARG B 83 14004 8809 9784 -7687 1316 -26 N ATOM 2156 N GLU B 84 10.401 -15.979 47.974 1.00 79.65 N ANISOU 2156 N GLU B 84 15848 4874 9541 -3239 119 1290 N ATOM 2157 CA GLU B 84 11.203 -16.545 49.070 1.00 84.00 C ANISOU 2157 CA GLU B 84 17046 5021 9851 -2908 -82 1544 C ATOM 2158 C GLU B 84 12.241 -15.557 49.596 1.00 80.19 C ANISOU 2158 C GLU B 84 15930 4957 9581 -2216 -177 1545 C ATOM 2159 O GLU B 84 12.418 -15.427 50.813 1.00 81.22 O ANISOU 2159 O GLU B 84 16156 5178 9527 -2228 -230 1718 O ATOM 2160 CB GLU B 84 11.935 -17.823 48.607 1.00 89.09 C ANISOU 2160 CB GLU B 84 18666 4838 10345 -2457 -325 1606 C ATOM 2161 CG GLU B 84 11.426 -18.465 47.291 1.00 92.15 C ANISOU 2161 CG GLU B 84 19349 4897 10767 -2709 -273 1424 C ATOM 2162 CD GLU B 84 11.437 -17.509 46.080 1.00 87.97 C ANISOU 2162 CD GLU B 84 17847 4926 10653 -2482 -147 1136 C ATOM 2163 OE1 GLU B 84 10.576 -17.685 45.192 1.00 88.94 O ANISOU 2163 OE1 GLU B 84 17933 5069 10793 -2976 -17 978 O ATOM 2164 OE2 GLU B 84 12.281 -16.575 46.017 1.00 83.85 O ANISOU 2164 OE2 GLU B 84 16615 4835 10410 -1857 -179 1070 O ATOM 2165 N ASN B 85 12.926 -14.882 48.665 1.00 76.32 N ANISOU 2165 N ASN B 85 14818 4733 9448 -1661 -196 1347 N ATOM 2166 CA ASN B 85 13.991 -13.928 48.983 1.00 73.04 C ANISOU 2166 CA ASN B 85 13773 4738 9239 -1046 -284 1308 C ATOM 2167 C ASN B 85 13.412 -12.585 49.390 1.00 69.06 C ANISOU 2167 C ASN B 85 12461 4881 8896 -1389 -96 1230 C ATOM 2168 O ASN B 85 14.119 -11.714 49.909 1.00 66.91 O ANISOU 2168 O ASN B 85 11710 4972 8741 -1059 -150 1212 O ATOM 2169 CB ASN B 85 14.938 -13.743 47.789 1.00 70.94 C ANISOU 2169 CB ASN B 85 13178 4536 9239 -406 -353 1121 C ATOM 2170 CG ASN B 85 15.476 -15.062 47.239 1.00 75.50 C ANISOU 2170 CG ASN B 85 14541 4491 9656 14 -539 1130 C ATOM 2171 OD1 ASN B 85 15.657 -15.210 46.032 1.00 74.51 O ANISOU 2171 OD1 ASN B 85 14327 4310 9671 233 -517 953 O ATOM 2172 ND2 ASN B 85 15.738 -16.015 48.120 1.00 80.71 N ANISOU 2172 ND2 ASN B 85 16009 4666 9992 158 -735 1329 N ATOM 2173 N GLY B 86 12.115 -12.424 49.141 1.00 68.45 N ANISOU 2173 N GLY B 86 12241 4966 8800 -2045 113 1159 N ATOM 2174 CA GLY B 86 11.446 -11.160 49.360 1.00 65.00 C ANISOU 2174 CA GLY B 86 11054 5139 8503 -2308 284 1032 C ATOM 2175 C GLY B 86 11.995 -10.076 48.453 1.00 60.73 C ANISOU 2175 C GLY B 86 9843 4903 8329 -1885 292 851 C ATOM 2176 O GLY B 86 11.994 -8.912 48.828 1.00 57.99 O ANISOU 2176 O GLY B 86 8949 4974 8109 -1841 341 774 O ATOM 2177 N THR B 87 12.478 -10.461 47.270 1.00 60.65 N ANISOU 2177 N THR B 87 9923 4666 8456 -1587 242 780 N ATOM 2178 CA THR B 87 12.936 -9.481 46.286 1.00 57.05 C ANISOU 2178 CA THR B 87 8880 4497 8301 -1273 275 621 C ATOM 2179 C THR B 87 11.960 -9.270 45.135 1.00 55.92 C ANISOU 2179 C THR B 87 8525 4469 8253 -1561 413 469 C ATOM 2180 O THR B 87 11.129 -10.131 44.798 1.00 57.52 O ANISOU 2180 O THR B 87 9084 4465 8307 -1929 459 456 O ATOM 2181 CB THR B 87 14.343 -9.786 45.675 1.00 57.38 C ANISOU 2181 CB THR B 87 8979 4388 8435 -650 134 605 C ATOM 2182 OG1 THR B 87 14.294 -10.978 44.892 1.00 60.20 O ANISOU 2182 OG1 THR B 87 9865 4316 8694 -585 89 590 O ATOM 2183 CG2 THR B 87 15.409 -9.924 46.736 1.00 59.26 C ANISOU 2183 CG2 THR B 87 9331 4616 8570 -270 -36 719 C ATOM 2184 N VAL B 88 12.107 -8.100 44.532 1.00 52.79 N ANISOU 2184 N VAL B 88 7573 4405 8082 -1396 463 354 N ATOM 2185 CA VAL B 88 11.410 -7.710 43.333 1.00 51.88 C ANISOU 2185 CA VAL B 88 7202 4441 8069 -1514 555 209 C ATOM 2186 C VAL B 88 12.503 -7.356 42.305 1.00 51.03 C ANISOU 2186 C VAL B 88 6917 4332 8141 -1070 517 165 C ATOM 2187 O VAL B 88 13.592 -6.898 42.665 1.00 50.01 O ANISOU 2187 O VAL B 88 6631 4283 8089 -759 457 209 O ATOM 2188 CB VAL B 88 10.467 -6.531 43.668 1.00 50.43 C ANISOU 2188 CB VAL B 88 6561 4679 7922 -1734 643 120 C ATOM 2189 CG1 VAL B 88 10.543 -5.413 42.649 1.00 48.87 C ANISOU 2189 CG1 VAL B 88 5964 4690 7916 -1523 663 11 C ATOM 2190 CG2 VAL B 88 9.053 -7.018 43.889 1.00 51.61 C ANISOU 2190 CG2 VAL B 88 6782 4957 7871 -2239 732 58 C ATOM 2191 N SER B 89 12.241 -7.604 41.032 1.00 51.42 N ANISOU 2191 N SER B 89 6982 4334 8221 -1068 555 68 N ATOM 2192 CA SER B 89 13.239 -7.300 40.032 1.00 51.59 C ANISOU 2192 CA SER B 89 6833 4408 8362 -693 546 21 C ATOM 2193 C SER B 89 12.647 -6.491 38.886 1.00 50.93 C ANISOU 2193 C SER B 89 6445 4547 8360 -782 627 -80 C ATOM 2194 O SER B 89 11.508 -6.714 38.480 1.00 50.96 O ANISOU 2194 O SER B 89 6496 4572 8295 -1060 664 -155 O ATOM 2195 CB SER B 89 13.917 -8.578 39.535 1.00 54.14 C ANISOU 2195 CB SER B 89 7571 4407 8591 -426 476 1 C ATOM 2196 OG SER B 89 13.010 -9.383 38.811 1.00 55.71 O ANISOU 2196 OG SER B 89 8077 4398 8691 -678 503 -81 O ATOM 2197 N ARG B 90 13.435 -5.543 38.395 1.00 51.50 N ANISOU 2197 N ARG B 90 6214 4809 8543 -565 648 -80 N ATOM 2198 CA ARG B 90 13.062 -4.638 37.302 1.00 52.68 C ANISOU 2198 CA ARG B 90 6130 5144 8743 -595 705 -137 C ATOM 2199 C ARG B 90 14.134 -4.698 36.202 1.00 54.69 C ANISOU 2199 C ARG B 90 6331 5444 9003 -341 738 -160 C ATOM 2200 O ARG B 90 15.328 -4.810 36.491 1.00 55.41 O ANISOU 2200 O ARG B 90 6365 5582 9105 -125 723 -132 O ATOM 2201 CB ARG B 90 12.929 -3.198 37.840 1.00 51.37 C ANISOU 2201 CB ARG B 90 5698 5164 8656 -652 707 -99 C ATOM 2202 CG ARG B 90 12.421 -2.195 36.819 1.00 51.01 C ANISOU 2202 CG ARG B 90 5514 5248 8621 -660 730 -137 C ATOM 2203 CD ARG B 90 12.045 -0.863 37.418 1.00 51.45 C ANISOU 2203 CD ARG B 90 5436 5397 8716 -693 699 -126 C ATOM 2204 NE ARG B 90 11.317 -0.077 36.422 1.00 52.01 N ANISOU 2204 NE ARG B 90 5475 5544 8743 -649 682 -169 N ATOM 2205 CZ ARG B 90 10.898 1.171 36.592 1.00 54.95 C ANISOU 2205 CZ ARG B 90 5816 5951 9111 -591 627 -179 C ATOM 2206 NH1 ARG B 90 11.142 1.807 37.735 1.00 56.07 N ANISOU 2206 NH1 ARG B 90 5937 6064 9302 -609 599 -166 N ATOM 2207 NH2 ARG B 90 10.221 1.787 35.617 1.00 56.01 N ANISOU 2207 NH2 ARG B 90 5980 6136 9166 -483 579 -213 N ATOM 2208 N TYR B 91 13.705 -4.658 34.945 1.00 56.88 N ANISOU 2208 N TYR B 91 6604 5770 9238 -361 780 -229 N ATOM 2209 CA TYR B 91 14.643 -4.565 33.817 1.00 59.91 C ANISOU 2209 CA TYR B 91 6898 6277 9588 -161 839 -259 C ATOM 2210 C TYR B 91 14.638 -3.163 33.200 1.00 60.20 C ANISOU 2210 C TYR B 91 6715 6517 9641 -245 891 -200 C ATOM 2211 O TYR B 91 13.595 -2.674 32.761 1.00 59.69 O ANISOU 2211 O TYR B 91 6664 6464 9551 -364 872 -211 O ATOM 2212 CB TYR B 91 14.335 -5.635 32.769 1.00 61.67 C ANISOU 2212 CB TYR B 91 7346 6386 9700 -96 845 -384 C ATOM 2213 CG TYR B 91 14.529 -7.030 33.296 1.00 64.51 C ANISOU 2213 CG TYR B 91 8048 6457 10007 19 779 -437 C ATOM 2214 CD1 TYR B 91 13.610 -7.596 34.185 1.00 65.29 C ANISOU 2214 CD1 TYR B 91 8396 6323 10087 -230 719 -414 C ATOM 2215 CD2 TYR B 91 15.642 -7.787 32.921 1.00 68.06 C ANISOU 2215 CD2 TYR B 91 8602 6873 10384 389 769 -515 C ATOM 2216 CE1 TYR B 91 13.790 -8.884 34.686 1.00 68.41 C ANISOU 2216 CE1 TYR B 91 9232 6370 10392 -155 643 -431 C ATOM 2217 CE2 TYR B 91 15.836 -9.082 33.415 1.00 70.62 C ANISOU 2217 CE2 TYR B 91 9353 6853 10627 571 670 -562 C ATOM 2218 CZ TYR B 91 14.905 -9.617 34.297 1.00 71.35 C ANISOU 2218 CZ TYR B 91 9781 6629 10701 276 603 -501 C ATOM 2219 OH TYR B 91 15.079 -10.889 34.782 1.00 75.79 O ANISOU 2219 OH TYR B 91 10881 6773 11143 417 492 -517 O ATOM 2220 N GLU B 92 15.805 -2.515 33.221 1.00 62.57 N ANISOU 2220 N GLU B 92 6834 6988 9953 -191 942 -143 N ATOM 2221 CA GLU B 92 16.007 -1.174 32.646 1.00 63.76 C ANISOU 2221 CA GLU B 92 6872 7278 10075 -327 997 -60 C ATOM 2222 C GLU B 92 17.280 -1.139 31.790 1.00 66.29 C ANISOU 2222 C GLU B 92 7037 7864 10286 -274 1112 -70 C ATOM 2223 O GLU B 92 18.360 -1.589 32.231 1.00 67.52 O ANISOU 2223 O GLU B 92 7025 8193 10435 -146 1134 -116 O ATOM 2224 CB GLU B 92 16.111 -0.119 33.745 1.00 63.58 C ANISOU 2224 CB GLU B 92 6785 7232 10141 -474 954 24 C ATOM 2225 CG GLU B 92 14.782 0.525 34.164 1.00 64.32 C ANISOU 2225 CG GLU B 92 6994 7168 10275 -549 867 34 C ATOM 2226 CD GLU B 92 14.965 1.968 34.656 1.00 66.95 C ANISOU 2226 CD GLU B 92 7347 7462 10630 -679 837 110 C ATOM 2227 OE1 GLU B 92 14.165 2.406 35.511 1.00 66.47 O ANISOU 2227 OE1 GLU B 92 7334 7306 10615 -677 753 82 O ATOM 2228 OE2 GLU B 92 15.909 2.662 34.190 1.00 69.21 O ANISOU 2228 OE2 GLU B 92 7617 7820 10858 -806 901 183 O ATOM 2229 N GLY B 93 17.152 -0.595 30.574 1.00 67.14 N ANISOU 2229 N GLY B 93 7184 8056 10271 -361 1182 -35 N ATOM 2230 CA GLY B 93 18.226 -0.654 29.578 1.00 69.30 C ANISOU 2230 CA GLY B 93 7306 8647 10379 -341 1321 -65 C ATOM 2231 C GLY B 93 18.725 -2.079 29.356 1.00 70.36 C ANISOU 2231 C GLY B 93 7383 8884 10467 -15 1339 -241 C ATOM 2232 O GLY B 93 19.929 -2.348 29.460 1.00 72.48 O ANISOU 2232 O GLY B 93 7406 9466 10669 118 1404 -315 O ATOM 2233 N GLY B 94 17.790 -2.992 29.078 1.00 69.40 N ANISOU 2233 N GLY B 94 7500 8510 10357 120 1266 -329 N ATOM 2234 CA GLY B 94 18.083 -4.426 28.905 1.00 70.48 C ANISOU 2234 CA GLY B 94 7744 8595 10439 443 1243 -508 C ATOM 2235 C GLY B 94 18.663 -5.165 30.112 1.00 70.63 C ANISOU 2235 C GLY B 94 7775 8521 10540 671 1155 -549 C ATOM 2236 O GLY B 94 18.935 -6.369 30.035 1.00 72.86 O ANISOU 2236 O GLY B 94 8241 8688 10753 995 1103 -695 O ATOM 2237 N ARG B 95 18.829 -4.454 31.229 1.00 68.46 N ANISOU 2237 N ARG B 95 7361 8265 10386 524 1118 -425 N ATOM 2238 CA ARG B 95 19.572 -4.949 32.395 1.00 68.29 C ANISOU 2238 CA ARG B 95 7288 8256 10403 745 1030 -444 C ATOM 2239 C ARG B 95 18.707 -5.098 33.662 1.00 64.93 C ANISOU 2239 C ARG B 95 7094 7472 10105 615 907 -349 C ATOM 2240 O ARG B 95 17.782 -4.305 33.903 1.00 61.97 O ANISOU 2240 O ARG B 95 6737 6992 9817 300 910 -253 O ATOM 2241 CB ARG B 95 20.758 -4.017 32.665 1.00 69.99 C ANISOU 2241 CB ARG B 95 7074 8926 10592 676 1098 -413 C ATOM 2242 CG ARG B 95 21.786 -4.559 33.641 1.00 74.12 C ANISOU 2242 CG ARG B 95 7439 9635 11087 997 1004 -482 C ATOM 2243 CD ARG B 95 22.438 -3.414 34.372 1.00 77.32 C ANISOU 2243 CD ARG B 95 7493 10360 11525 723 1025 -407 C ATOM 2244 NE ARG B 95 22.324 -3.586 35.817 1.00 79.27 N ANISOU 2244 NE ARG B 95 7833 10424 11863 782 870 -350 N ATOM 2245 CZ ARG B 95 22.396 -2.594 36.702 1.00 80.03 C ANISOU 2245 CZ ARG B 95 7786 10592 12030 477 847 -264 C ATOM 2246 NH1 ARG B 95 22.589 -1.342 36.297 1.00 80.91 N ANISOU 2246 NH1 ARG B 95 7705 10901 12136 73 962 -216 N ATOM 2247 NH2 ARG B 95 22.276 -2.853 38.001 1.00 80.46 N ANISOU 2247 NH2 ARG B 95 7943 10496 12133 561 704 -224 N ATOM 2248 N GLU B 96 19.042 -6.101 34.475 1.00 64.87 N ANISOU 2248 N GLU B 96 7272 7303 10073 886 793 -384 N ATOM 2249 CA GLU B 96 18.234 -6.484 35.642 1.00 62.14 C ANISOU 2249 CA GLU B 96 7220 6608 9781 755 685 -296 C ATOM 2250 C GLU B 96 18.656 -5.839 36.967 1.00 59.82 C ANISOU 2250 C GLU B 96 6735 6444 9550 696 628 -196 C ATOM 2251 O GLU B 96 19.827 -5.901 37.340 1.00 61.80 O ANISOU 2251 O GLU B 96 6788 6942 9751 970 581 -229 O ATOM 2252 CB GLU B 96 18.253 -7.997 35.812 1.00 64.78 C ANISOU 2252 CB GLU B 96 8018 6590 10004 1042 573 -360 C ATOM 2253 CG GLU B 96 17.224 -8.460 36.802 1.00 65.32 C ANISOU 2253 CG GLU B 96 8467 6280 10073 776 496 -260 C ATOM 2254 CD GLU B 96 17.550 -9.793 37.393 1.00 69.77 C ANISOU 2254 CD GLU B 96 9539 6474 10496 1069 348 -262 C ATOM 2255 OE1 GLU B 96 18.751 -10.081 37.599 1.00 73.29 O ANISOU 2255 OE1 GLU B 96 9922 7048 10876 1555 260 -306 O ATOM 2256 OE2 GLU B 96 16.601 -10.551 37.665 1.00 70.77 O ANISOU 2256 OE2 GLU B 96 10144 6197 10547 809 311 -225 O ATOM 2257 N HIS B 97 17.687 -5.257 37.677 1.00 55.37 N ANISOU 2257 N HIS B 97 6215 5758 9067 362 624 -104 N ATOM 2258 CA HIS B 97 17.919 -4.643 38.990 1.00 52.92 C ANISOU 2258 CA HIS B 97 5771 5538 8797 274 565 -25 C ATOM 2259 C HIS B 97 17.073 -5.367 40.035 1.00 51.03 C ANISOU 2259 C HIS B 97 5875 5001 8512 173 486 39 C ATOM 2260 O HIS B 97 15.848 -5.376 39.928 1.00 48.83 O ANISOU 2260 O HIS B 97 5733 4581 8240 -102 530 42 O ATOM 2261 CB HIS B 97 17.537 -3.148 38.985 1.00 51.21 C ANISOU 2261 CB HIS B 97 5310 5470 8676 -32 634 8 C ATOM 2262 CG HIS B 97 18.250 -2.323 37.952 1.00 54.19 C ANISOU 2262 CG HIS B 97 5432 6099 9058 -61 726 -18 C ATOM 2263 ND1 HIS B 97 19.063 -1.260 38.282 1.00 58.19 N ANISOU 2263 ND1 HIS B 97 5680 6853 9577 -194 743 1 N ATOM 2264 CD2 HIS B 97 18.241 -2.378 36.597 1.00 56.89 C ANISOU 2264 CD2 HIS B 97 5766 6492 9358 -35 815 -58 C ATOM 2265 CE1 HIS B 97 19.540 -0.707 37.179 1.00 60.10 C ANISOU 2265 CE1 HIS B 97 5781 7282 9774 -282 848 -10 C ATOM 2266 NE2 HIS B 97 19.058 -1.370 36.142 1.00 59.62 N ANISOU 2266 NE2 HIS B 97 5860 7116 9678 -163 894 -42 N ATOM 2267 N VAL B 98 17.726 -5.946 41.043 1.00 50.49 N ANISOU 2267 N VAL B 98 5932 4889 8364 382 369 85 N ATOM 2268 CA VAL B 98 17.054 -6.633 42.157 1.00 49.01 C ANISOU 2268 CA VAL B 98 6117 4427 8077 257 293 179 C ATOM 2269 C VAL B 98 16.947 -5.730 43.408 1.00 46.71 C ANISOU 2269 C VAL B 98 5625 4315 7807 67 275 241 C ATOM 2270 O VAL B 98 17.880 -4.999 43.722 1.00 45.92 O ANISOU 2270 O VAL B 98 5205 4494 7750 192 240 222 O ATOM 2271 CB VAL B 98 17.796 -7.964 42.505 1.00 53.11 C ANISOU 2271 CB VAL B 98 7042 4706 8432 657 139 208 C ATOM 2272 CG1 VAL B 98 17.058 -8.746 43.571 1.00 53.77 C ANISOU 2272 CG1 VAL B 98 7630 4440 8359 459 68 338 C ATOM 2273 CG2 VAL B 98 17.974 -8.815 41.258 1.00 53.48 C ANISOU 2273 CG2 VAL B 98 7305 4575 8441 902 147 103 C ATOM 2274 N ALA B 99 15.802 -5.759 44.093 1.00 44.49 N ANISOU 2274 N ALA B 99 5511 3920 7473 -263 307 290 N ATOM 2275 CA ALA B 99 15.641 -5.053 45.366 1.00 42.89 C ANISOU 2275 CA ALA B 99 5179 3876 7242 -416 285 329 C ATOM 2276 C ALA B 99 14.792 -5.844 46.363 1.00 43.95 C ANISOU 2276 C ALA B 99 5684 3832 7183 -653 272 421 C ATOM 2277 O ALA B 99 13.826 -6.491 45.974 1.00 44.57 O ANISOU 2277 O ALA B 99 6000 3743 7189 -901 341 419 O ATOM 2278 CB ALA B 99 15.033 -3.677 45.143 1.00 40.07 C ANISOU 2278 CB ALA B 99 4478 3736 7013 -624 381 240 C ATOM 2279 N HIS B 100 15.148 -5.780 47.642 1.00 44.20 N ANISOU 2279 N HIS B 100 5762 3933 7100 -624 188 498 N ATOM 2280 CA HIS B 100 14.350 -6.377 48.705 1.00 45.67 C ANISOU 2280 CA HIS B 100 6282 4012 7058 -912 195 600 C ATOM 2281 C HIS B 100 13.238 -5.418 49.143 1.00 44.32 C ANISOU 2281 C HIS B 100 5816 4134 6891 -1271 328 506 C ATOM 2282 O HIS B 100 13.479 -4.251 49.413 1.00 42.18 O ANISOU 2282 O HIS B 100 5182 4116 6731 -1197 327 415 O ATOM 2283 CB HIS B 100 15.223 -6.746 49.916 1.00 48.30 C ANISOU 2283 CB HIS B 100 6821 4316 7216 -692 31 728 C ATOM 2284 CG HIS B 100 16.190 -7.863 49.660 1.00 50.83 C ANISOU 2284 CG HIS B 100 7524 4343 7447 -271 -134 814 C ATOM 2285 ND1 HIS B 100 15.904 -9.182 49.955 1.00 55.44 N ANISOU 2285 ND1 HIS B 100 8783 4498 7783 -315 -205 965 N ATOM 2286 CD2 HIS B 100 17.444 -7.856 49.149 1.00 51.80 C ANISOU 2286 CD2 HIS B 100 7465 4556 7659 222 -251 753 C ATOM 2287 CE1 HIS B 100 16.939 -9.937 49.629 1.00 57.80 C ANISOU 2287 CE1 HIS B 100 9338 4590 8034 213 -382 986 C ATOM 2288 NE2 HIS B 100 17.886 -9.156 49.138 1.00 56.53 N ANISOU 2288 NE2 HIS B 100 8611 4793 8073 557 -406 845 N ATOM 2289 N LEU B 101 12.012 -5.921 49.224 1.00 45.24 N ANISOU 2289 N LEU B 101 6100 4235 6854 -1664 437 506 N ATOM 2290 CA LEU B 101 10.931 -5.135 49.789 1.00 44.35 C ANISOU 2290 CA LEU B 101 5696 4484 6671 -1958 555 389 C ATOM 2291 C LEU B 101 11.099 -5.104 51.305 1.00 46.11 C ANISOU 2291 C LEU B 101 6020 4817 6683 -2030 516 474 C ATOM 2292 O LEU B 101 11.223 -6.148 51.935 1.00 48.04 O ANISOU 2292 O LEU B 101 6712 4844 6696 -2154 472 650 O ATOM 2293 CB LEU B 101 9.577 -5.712 49.389 1.00 45.14 C ANISOU 2293 CB LEU B 101 5864 4660 6626 -2391 692 330 C ATOM 2294 CG LEU B 101 8.310 -5.104 49.996 1.00 45.83 C ANISOU 2294 CG LEU B 101 5625 5230 6556 -2711 827 175 C ATOM 2295 CD1 LEU B 101 8.057 -3.669 49.560 1.00 40.61 C ANISOU 2295 CD1 LEU B 101 4457 4881 6093 -2448 835 -43 C ATOM 2296 CD2 LEU B 101 7.119 -5.978 49.607 1.00 46.25 C ANISOU 2296 CD2 LEU B 101 5789 5379 6404 -3212 952 133 C ATOM 2297 N LEU B 102 11.163 -3.899 51.882 1.00 44.87 N ANISOU 2297 N LEU B 102 5504 4960 6586 -1930 515 351 N ATOM 2298 CA LEU B 102 11.234 -3.782 53.344 1.00 46.82 C ANISOU 2298 CA LEU B 102 5811 5372 6605 -2014 486 396 C ATOM 2299 C LEU B 102 10.109 -2.935 53.913 1.00 47.68 C ANISOU 2299 C LEU B 102 5608 5907 6602 -2227 618 200 C ATOM 2300 O LEU B 102 9.649 -1.979 53.279 1.00 46.57 O ANISOU 2300 O LEU B 102 5129 5937 6630 -2125 664 -3 O ATOM 2301 CB LEU B 102 12.592 -3.250 53.809 1.00 45.42 C ANISOU 2301 CB LEU B 102 5561 5175 6524 -1661 318 422 C ATOM 2302 CG LEU B 102 13.841 -3.954 53.267 1.00 45.32 C ANISOU 2302 CG LEU B 102 5742 4874 6605 -1338 168 557 C ATOM 2303 CD1 LEU B 102 15.043 -3.007 53.305 1.00 41.58 C ANISOU 2303 CD1 LEU B 102 4949 4553 6296 -1042 47 471 C ATOM 2304 CD2 LEU B 102 14.120 -5.266 54.018 1.00 49.29 C ANISOU 2304 CD2 LEU B 102 6764 5142 6821 -1328 64 783 C ATOM 2305 N PHE B 103 9.675 -3.286 55.117 1.00 50.74 N ANISOU 2305 N PHE B 103 6131 6478 6668 -2492 670 254 N ATOM 2306 CA PHE B 103 8.638 -2.525 55.785 1.00 52.67 C ANISOU 2306 CA PHE B 103 6055 7211 6745 -2662 800 38 C ATOM 2307 C PHE B 103 9.144 -1.761 56.992 1.00 53.72 C ANISOU 2307 C PHE B 103 6111 7520 6780 -2507 724 -21 C ATOM 2308 O PHE B 103 10.188 -2.076 57.548 1.00 54.93 O ANISOU 2308 O PHE B 103 6507 7464 6898 -2380 582 151 O ATOM 2309 CB PHE B 103 7.457 -3.439 56.149 1.00 55.79 C ANISOU 2309 CB PHE B 103 6572 7841 6785 -3197 980 78 C ATOM 2310 CG PHE B 103 6.713 -3.932 54.952 1.00 55.79 C ANISOU 2310 CG PHE B 103 6526 7810 6863 -3396 1071 32 C ATOM 2311 CD1 PHE B 103 6.530 -5.295 54.738 1.00 60.24 C ANISOU 2311 CD1 PHE B 103 7538 8098 7252 -3795 1112 238 C ATOM 2312 CD2 PHE B 103 6.199 -3.036 54.025 1.00 53.03 C ANISOU 2312 CD2 PHE B 103 5736 7680 6733 -3181 1095 -220 C ATOM 2313 CE1 PHE B 103 5.830 -5.756 53.617 1.00 60.20 C ANISOU 2313 CE1 PHE B 103 7491 8081 7300 -4020 1189 167 C ATOM 2314 CE2 PHE B 103 5.515 -3.481 52.902 1.00 54.55 C ANISOU 2314 CE2 PHE B 103 5862 7890 6974 -3352 1161 -277 C ATOM 2315 CZ PHE B 103 5.327 -4.844 52.698 1.00 57.46 C ANISOU 2315 CZ PHE B 103 6630 8025 7177 -3793 1213 -95 C ATOM 2316 N LEU B 104 8.402 -0.727 57.360 1.00 54.97 N ANISOU 2316 N LEU B 104 5922 8083 6882 -2473 802 -297 N ATOM 2317 CA LEU B 104 8.670 0.070 58.550 1.00 56.17 C ANISOU 2317 CA LEU B 104 5991 8459 6893 -2360 751 -419 C ATOM 2318 C LEU B 104 7.508 -0.144 59.521 1.00 60.58 C ANISOU 2318 C LEU B 104 6453 9530 7035 -2694 933 -520 C ATOM 2319 O LEU B 104 6.588 -0.900 59.219 1.00 62.02 O ANISOU 2319 O LEU B 104 6627 9880 7057 -3040 1091 -484 O ATOM 2320 CB LEU B 104 8.799 1.532 58.149 1.00 54.18 C ANISOU 2320 CB LEU B 104 5471 8222 6892 -2001 677 -694 C ATOM 2321 CG LEU B 104 10.031 1.788 57.256 1.00 51.58 C ANISOU 2321 CG LEU B 104 5231 7447 6921 -1761 517 -589 C ATOM 2322 CD1 LEU B 104 9.880 3.052 56.467 1.00 50.66 C ANISOU 2322 CD1 LEU B 104 4941 7270 7039 -1510 483 -818 C ATOM 2323 CD2 LEU B 104 11.311 1.809 58.070 1.00 49.41 C ANISOU 2323 CD2 LEU B 104 5095 7062 6615 -1689 358 -479 C ATOM 2324 N ARG B 105 7.541 0.504 60.680 1.00 63.05 N ANISOU 2324 N ARG B 105 6684 10133 7141 -2631 921 -662 N ATOM 2325 CA ARG B 105 6.432 0.385 61.625 1.00 67.84 C ANISOU 2325 CA ARG B 105 7142 11324 7312 -2940 1116 -798 C ATOM 2326 C ARG B 105 5.114 0.849 60.988 1.00 68.70 C ANISOU 2326 C ARG B 105 6813 11881 7410 -2934 1276 -1113 C ATOM 2327 O ARG B 105 4.111 0.141 61.031 1.00 71.69 O ANISOU 2327 O ARG B 105 7083 12651 7504 -3356 1473 -1116 O ATOM 2328 CB ARG B 105 6.736 1.143 62.923 1.00 69.88 C ANISOU 2328 CB ARG B 105 7362 11831 7357 -2797 1060 -950 C ATOM 2329 CG ARG B 105 7.325 0.266 64.022 1.00 73.69 C ANISOU 2329 CG ARG B 105 8228 12253 7516 -3058 1021 -648 C ATOM 2330 CD ARG B 105 6.328 0.011 65.153 1.00 79.72 C ANISOU 2330 CD ARG B 105 8921 13633 7737 -3448 1236 -727 C ATOM 2331 NE ARG B 105 6.762 0.642 66.400 1.00 83.57 N ANISOU 2331 NE ARG B 105 9418 14337 7996 -3299 1155 -845 N ATOM 2332 CZ ARG B 105 7.229 -0.018 67.462 1.00 86.95 C ANISOU 2332 CZ ARG B 105 10204 14768 8067 -3513 1110 -589 C ATOM 2333 NH1 ARG B 105 7.313 -1.344 67.448 1.00 88.89 N ANISOU 2333 NH1 ARG B 105 10888 14759 8128 -3878 1133 -187 N ATOM 2334 NH2 ARG B 105 7.607 0.647 68.549 1.00 88.03 N ANISOU 2334 NH2 ARG B 105 10310 15140 7998 -3353 1025 -739 N ATOM 2335 N ASP B 106 5.146 2.027 60.369 1.00 66.90 N ANISOU 2335 N ASP B 106 6359 11592 7471 -2462 1176 -1377 N ATOM 2336 CA ASP B 106 3.995 2.618 59.688 1.00 67.38 C ANISOU 2336 CA ASP B 106 6015 12049 7539 -2286 1260 -1703 C ATOM 2337 C ASP B 106 3.550 1.735 58.529 1.00 65.97 C ANISOU 2337 C ASP B 106 5810 11792 7464 -2536 1333 -1560 C ATOM 2338 O ASP B 106 4.378 1.127 57.859 1.00 63.72 O ANISOU 2338 O ASP B 106 5836 10944 7431 -2595 1244 -1266 O ATOM 2339 CB ASP B 106 4.389 4.012 59.182 1.00 65.72 C ANISOU 2339 CB ASP B 106 5769 11564 7637 -1697 1076 -1929 C ATOM 2340 CG ASP B 106 3.206 4.920 58.998 1.00 68.78 C ANISOU 2340 CG ASP B 106 5775 12456 7903 -1350 1117 -2357 C ATOM 2341 OD1 ASP B 106 2.368 4.634 58.127 1.00 70.98 O ANISOU 2341 OD1 ASP B 106 5808 12978 8184 -1376 1189 -2425 O ATOM 2342 OD2 ASP B 106 3.117 5.930 59.720 1.00 71.78 O ANISOU 2342 OD2 ASP B 106 6106 13002 8166 -1016 1059 -2648 O ATOM 2343 N THR B 107 2.245 1.668 58.295 1.00 67.82 N ANISOU 2343 N THR B 107 5650 12640 7480 -2672 1490 -1798 N ATOM 2344 CA THR B 107 1.679 0.859 57.213 1.00 66.97 C ANISOU 2344 CA THR B 107 5467 12560 7418 -2958 1564 -1721 C ATOM 2345 C THR B 107 1.562 1.661 55.928 1.00 63.96 C ANISOU 2345 C THR B 107 4906 12034 7363 -2453 1431 -1892 C ATOM 2346 O THR B 107 1.489 1.099 54.837 1.00 62.38 O ANISOU 2346 O THR B 107 4751 11633 7318 -2575 1421 -1778 O ATOM 2347 CB THR B 107 0.269 0.353 57.569 1.00 72.02 C ANISOU 2347 CB THR B 107 5705 14055 7604 -3434 1806 -1919 C ATOM 2348 OG1 THR B 107 0.241 -0.059 58.940 1.00 75.21 O ANISOU 2348 OG1 THR B 107 6220 14732 7622 -3834 1942 -1839 O ATOM 2349 CG2 THR B 107 -0.133 -0.816 56.668 1.00 72.91 C ANISOU 2349 CG2 THR B 107 5897 14105 7700 -3958 1892 -1751 C ATOM 2350 N LYS B 108 1.556 2.981 56.063 1.00 63.17 N ANISOU 2350 N LYS B 108 4660 12000 7339 -1881 1316 -2165 N ATOM 2351 CA LYS B 108 1.400 3.874 54.917 1.00 61.17 C ANISOU 2351 CA LYS B 108 4310 11596 7336 -1352 1167 -2335 C ATOM 2352 C LYS B 108 2.755 4.193 54.227 1.00 56.23 C ANISOU 2352 C LYS B 108 4121 10115 7130 -1139 983 -2076 C ATOM 2353 O LYS B 108 2.828 5.057 53.342 1.00 54.58 O ANISOU 2353 O LYS B 108 3953 9661 7123 -707 841 -2172 O ATOM 2354 CB LYS B 108 0.622 5.133 55.340 1.00 64.73 C ANISOU 2354 CB LYS B 108 4456 12529 7608 -812 1118 -2781 C ATOM 2355 CG LYS B 108 -0.679 4.803 56.120 1.00 69.55 C ANISOU 2355 CG LYS B 108 4551 14127 7748 -1041 1327 -3071 C ATOM 2356 CD LYS B 108 -1.359 6.036 56.691 1.00 74.89 C ANISOU 2356 CD LYS B 108 4940 15306 8207 -431 1272 -3545 C ATOM 2357 CE LYS B 108 -2.469 6.522 55.768 1.00 77.61 C ANISOU 2357 CE LYS B 108 4856 16159 8473 34 1208 -3892 C ATOM 2358 NZ LYS B 108 -3.186 7.704 56.326 1.00 82.22 N ANISOU 2358 NZ LYS B 108 5171 17268 8801 731 1133 -4398 N ATOM 2359 N THR B 109 3.807 3.476 54.629 1.00 53.57 N ANISOU 2359 N THR B 109 4108 9367 6878 -1447 984 -1754 N ATOM 2360 CA THR B 109 5.127 3.597 53.994 1.00 50.05 C ANISOU 2360 CA THR B 109 3997 8240 6779 -1322 839 -1513 C ATOM 2361 C THR B 109 5.721 2.250 53.586 1.00 48.65 C ANISOU 2361 C THR B 109 4044 7760 6682 -1678 877 -1174 C ATOM 2362 O THR B 109 5.284 1.194 54.045 1.00 50.01 O ANISOU 2362 O THR B 109 4240 8135 6626 -2077 1001 -1075 O ATOM 2363 CB THR B 109 6.156 4.308 54.905 1.00 49.24 C ANISOU 2363 CB THR B 109 4095 7889 6724 -1184 727 -1500 C ATOM 2364 OG1 THR B 109 6.462 3.482 56.035 1.00 48.78 O ANISOU 2364 OG1 THR B 109 4131 7942 6459 -1511 792 -1345 O ATOM 2365 CG2 THR B 109 5.624 5.650 55.371 1.00 52.33 C ANISOU 2365 CG2 THR B 109 4369 8499 7017 -811 669 -1854 C ATOM 2366 N LEU B 110 6.744 2.309 52.736 1.00 46.50 N ANISOU 2366 N LEU B 110 3972 6994 6704 -1534 766 -1006 N ATOM 2367 CA LEU B 110 7.524 1.128 52.379 1.00 45.28 C ANISOU 2367 CA LEU B 110 4071 6502 6632 -1740 763 -712 C ATOM 2368 C LEU B 110 8.919 1.535 51.906 1.00 42.66 C ANISOU 2368 C LEU B 110 3890 5749 6570 -1511 626 -589 C ATOM 2369 O LEU B 110 9.160 2.704 51.547 1.00 41.51 O ANISOU 2369 O LEU B 110 3681 5521 6570 -1266 551 -712 O ATOM 2370 CB LEU B 110 6.801 0.248 51.347 1.00 45.74 C ANISOU 2370 CB LEU B 110 4109 6590 6681 -1934 847 -677 C ATOM 2371 CG LEU B 110 6.493 0.738 49.935 1.00 45.14 C ANISOU 2371 CG LEU B 110 3896 6462 6793 -1712 812 -778 C ATOM 2372 CD1 LEU B 110 7.748 0.763 49.104 1.00 45.12 C ANISOU 2372 CD1 LEU B 110 4099 5985 7060 -1535 715 -603 C ATOM 2373 CD2 LEU B 110 5.491 -0.184 49.295 1.00 49.54 C ANISOU 2373 CD2 LEU B 110 4370 7230 7221 -2003 914 -808 C ATOM 2374 N MET B 111 9.829 0.569 51.936 1.00 41.58 N ANISOU 2374 N MET B 111 3973 5366 6460 -1596 590 -357 N ATOM 2375 CA MET B 111 11.175 0.768 51.459 1.00 39.29 C ANISOU 2375 CA MET B 111 3756 4796 6378 -1408 478 -254 C ATOM 2376 C MET B 111 11.546 -0.303 50.465 1.00 39.07 C ANISOU 2376 C MET B 111 3878 4532 6435 -1410 484 -93 C ATOM 2377 O MET B 111 11.031 -1.431 50.540 1.00 40.45 O ANISOU 2377 O MET B 111 4232 4671 6465 -1598 540 -2 O ATOM 2378 CB MET B 111 12.156 0.695 52.616 1.00 40.49 C ANISOU 2378 CB MET B 111 3994 4952 6439 -1387 380 -172 C ATOM 2379 CG MET B 111 12.139 1.884 53.555 1.00 40.28 C ANISOU 2379 CG MET B 111 3847 5105 6354 -1349 338 -348 C ATOM 2380 SD MET B 111 13.528 1.793 54.685 1.00 41.20 S ANISOU 2380 SD MET B 111 4033 5241 6381 -1309 185 -254 S ATOM 2381 CE MET B 111 13.344 0.151 55.404 1.00 41.66 C ANISOU 2381 CE MET B 111 4361 5298 6170 -1430 201 -19 C ATOM 2382 N PHE B 112 12.437 0.047 49.542 1.00 37.74 N ANISOU 2382 N PHE B 112 3665 4206 6468 -1231 430 -70 N ATOM 2383 CA PHE B 112 13.153 -0.944 48.749 1.00 38.20 C ANISOU 2383 CA PHE B 112 3864 4064 6588 -1145 408 65 C ATOM 2384 C PHE B 112 14.658 -0.924 49.047 1.00 38.97 C ANISOU 2384 C PHE B 112 3938 4147 6724 -957 292 134 C ATOM 2385 O PHE B 112 15.272 0.125 49.087 1.00 38.56 O ANISOU 2385 O PHE B 112 3697 4194 6759 -921 254 60 O ATOM 2386 CB PHE B 112 12.848 -0.774 47.261 1.00 36.81 C ANISOU 2386 CB PHE B 112 3620 3811 6554 -1101 465 17 C ATOM 2387 CG PHE B 112 11.535 -1.387 46.858 1.00 37.57 C ANISOU 2387 CG PHE B 112 3776 3936 6562 -1279 553 -23 C ATOM 2388 CD1 PHE B 112 11.401 -2.773 46.777 1.00 38.70 C ANISOU 2388 CD1 PHE B 112 4186 3921 6595 -1404 571 76 C ATOM 2389 CD2 PHE B 112 10.425 -0.593 46.604 1.00 37.05 C ANISOU 2389 CD2 PHE B 112 3520 4070 6486 -1324 603 -179 C ATOM 2390 CE1 PHE B 112 10.177 -3.354 46.432 1.00 40.57 C ANISOU 2390 CE1 PHE B 112 4475 4223 6716 -1673 658 21 C ATOM 2391 CE2 PHE B 112 9.181 -1.169 46.260 1.00 37.84 C ANISOU 2391 CE2 PHE B 112 3592 4319 6465 -1522 682 -253 C ATOM 2392 CZ PHE B 112 9.068 -2.543 46.169 1.00 40.37 C ANISOU 2392 CZ PHE B 112 4155 4503 6680 -1746 719 -153 C ATOM 2393 N GLY B 113 15.238 -2.095 49.294 1.00 41.27 N ANISOU 2393 N GLY B 113 4439 4328 6914 -840 222 262 N ATOM 2394 CA GLY B 113 16.665 -2.194 49.639 1.00 42.56 C ANISOU 2394 CA GLY B 113 4534 4577 7062 -592 86 301 C ATOM 2395 C GLY B 113 17.477 -2.745 48.483 1.00 43.30 C ANISOU 2395 C GLY B 113 4604 4608 7239 -345 69 313 C ATOM 2396 O GLY B 113 17.114 -3.767 47.899 1.00 44.12 O ANISOU 2396 O GLY B 113 4977 4478 7308 -284 92 369 O ATOM 2397 N SER B 114 18.560 -2.053 48.143 1.00 43.17 N ANISOU 2397 N SER B 114 4271 4826 7307 -237 36 240 N ATOM 2398 CA SER B 114 19.417 -2.413 47.012 1.00 44.33 C ANISOU 2398 CA SER B 114 4294 5041 7506 -8 43 210 C ATOM 2399 C SER B 114 20.793 -2.826 47.503 1.00 46.93 C ANISOU 2399 C SER B 114 4473 5643 7716 323 -112 193 C ATOM 2400 O SER B 114 21.272 -2.281 48.494 1.00 48.02 O ANISOU 2400 O SER B 114 4442 6014 7789 272 -203 168 O ATOM 2401 CB SER B 114 19.561 -1.207 46.086 1.00 43.09 C ANISOU 2401 CB SER B 114 3850 5028 7494 -210 156 124 C ATOM 2402 OG SER B 114 18.323 -0.858 45.526 1.00 41.19 O ANISOU 2402 OG SER B 114 3745 4566 7338 -411 267 126 O ATOM 2403 N TYR B 115 21.425 -3.784 46.822 1.00 49.13 N ANISOU 2403 N TYR B 115 4802 5924 7939 694 -158 180 N ATOM 2404 CA TYR B 115 22.777 -4.275 47.188 1.00 53.24 C ANISOU 2404 CA TYR B 115 5142 6781 8308 1138 -332 124 C ATOM 2405 C TYR B 115 22.985 -4.517 48.687 1.00 54.80 C ANISOU 2405 C TYR B 115 5472 7019 8331 1260 -523 195 C ATOM 2406 O TYR B 115 24.054 -4.217 49.235 1.00 57.16 O ANISOU 2406 O TYR B 115 5420 7772 8528 1432 -655 111 O ATOM 2407 CB TYR B 115 23.875 -3.319 46.671 1.00 54.53 C ANISOU 2407 CB TYR B 115 4704 7505 8510 1067 -281 -30 C ATOM 2408 CG TYR B 115 23.730 -2.964 45.212 1.00 54.50 C ANISOU 2408 CG TYR B 115 4571 7504 8634 902 -85 -84 C ATOM 2409 CD1 TYR B 115 23.474 -1.655 44.812 1.00 52.57 C ANISOU 2409 CD1 TYR B 115 4134 7326 8512 413 63 -101 C ATOM 2410 CD2 TYR B 115 23.846 -3.948 44.227 1.00 58.76 C ANISOU 2410 CD2 TYR B 115 5241 7948 9138 1255 -63 -118 C ATOM 2411 CE1 TYR B 115 23.315 -1.335 43.466 1.00 53.07 C ANISOU 2411 CE1 TYR B 115 4141 7372 8652 265 231 -123 C ATOM 2412 CE2 TYR B 115 23.698 -3.639 42.879 1.00 58.88 C ANISOU 2412 CE2 TYR B 115 5149 7987 9237 1104 117 -167 C ATOM 2413 CZ TYR B 115 23.434 -2.336 42.507 1.00 55.36 C ANISOU 2413 CZ TYR B 115 4510 7623 8902 604 263 -155 C ATOM 2414 OH TYR B 115 23.300 -2.054 41.169 1.00 56.54 O ANISOU 2414 OH TYR B 115 4603 7790 9091 469 426 -181 O ATOM 2415 N LEU B 116 21.972 -5.075 49.336 1.00 53.87 N ANISOU 2415 N LEU B 116 5848 6474 8145 1147 -538 343 N ATOM 2416 CA LEU B 116 21.942 -5.220 50.801 1.00 55.48 C ANISOU 2416 CA LEU B 116 6241 6680 8157 1159 -687 439 C ATOM 2417 C LEU B 116 23.070 -6.012 51.456 1.00 59.61 C ANISOU 2417 C LEU B 116 6834 7378 8436 1720 -956 457 C ATOM 2418 O LEU B 116 23.445 -5.729 52.590 1.00 60.88 O ANISOU 2418 O LEU B 116 6905 7779 8448 1745 -1096 472 O ATOM 2419 CB LEU B 116 20.583 -5.768 51.248 1.00 54.65 C ANISOU 2419 CB LEU B 116 6677 6110 7978 871 -616 599 C ATOM 2420 CG LEU B 116 19.648 -4.789 51.969 1.00 52.45 C ANISOU 2420 CG LEU B 116 6288 5904 7737 379 -494 589 C ATOM 2421 CD1 LEU B 116 19.875 -3.326 51.582 1.00 48.05 C ANISOU 2421 CD1 LEU B 116 5200 5664 7394 175 -397 418 C ATOM 2422 CD2 LEU B 116 18.203 -5.207 51.766 1.00 50.79 C ANISOU 2422 CD2 LEU B 116 6429 5353 7517 32 -335 666 C ATOM 2423 N ASP B 117 23.597 -7.002 50.747 1.00 62.12 N ANISOU 2423 N ASP B 117 7327 7589 8688 2211 -1045 438 N ATOM 2424 CA ASP B 117 24.684 -7.838 51.268 1.00 67.58 C ANISOU 2424 CA ASP B 117 8118 8446 9113 2888 -1336 430 C ATOM 2425 C ASP B 117 26.043 -7.196 51.020 1.00 69.33 C ANISOU 2425 C ASP B 117 7573 9432 9339 3150 -1402 198 C ATOM 2426 O ASP B 117 27.042 -7.598 51.621 1.00 74.26 O ANISOU 2426 O ASP B 117 8082 10409 9724 3690 -1662 140 O ATOM 2427 CB ASP B 117 24.649 -9.213 50.610 1.00 70.29 C ANISOU 2427 CB ASP B 117 9045 8314 9346 3367 -1424 476 C ATOM 2428 CG ASP B 117 24.661 -9.134 49.099 1.00 68.93 C ANISOU 2428 CG ASP B 117 8634 8175 9379 3357 -1236 323 C ATOM 2429 OD1 ASP B 117 24.213 -8.111 48.537 1.00 67.28 O ANISOU 2429 OD1 ASP B 117 8023 8124 9415 2822 -993 266 O ATOM 2430 OD2 ASP B 117 25.114 -10.096 48.460 1.00 73.28 O ANISOU 2430 OD2 ASP B 117 9438 8582 9824 3912 -1342 252 O ATOM 2431 N ASP B 118 26.060 -6.202 50.130 1.00 66.33 N ANISOU 2431 N ASP B 118 6682 9326 9193 2748 -1172 64 N ATOM 2432 CA ASP B 118 27.277 -5.510 49.705 1.00 67.93 C ANISOU 2432 CA ASP B 118 6134 10284 9392 2821 -1167 -165 C ATOM 2433 C ASP B 118 27.475 -4.203 50.466 1.00 66.58 C ANISOU 2433 C ASP B 118 5534 10508 9257 2305 -1141 -223 C ATOM 2434 O ASP B 118 26.809 -3.201 50.203 1.00 62.86 O ANISOU 2434 O ASP B 118 5007 9889 8986 1698 -935 -208 O ATOM 2435 CB ASP B 118 27.235 -5.255 48.190 1.00 66.42 C ANISOU 2435 CB ASP B 118 5720 10137 9379 2662 -927 -265 C ATOM 2436 CG ASP B 118 28.541 -4.674 47.642 1.00 69.80 C ANISOU 2436 CG ASP B 118 5378 11402 9741 2717 -896 -507 C ATOM 2437 OD1 ASP B 118 29.476 -4.384 48.419 1.00 70.72 O ANISOU 2437 OD1 ASP B 118 5070 12111 9690 2830 -1057 -621 O ATOM 2438 OD2 ASP B 118 28.614 -4.499 46.407 1.00 71.36 O ANISOU 2438 OD2 ASP B 118 5382 11704 10028 2604 -701 -590 O ATOM 2439 N GLU B 119 28.433 -4.236 51.383 1.00 70.28 N ANISOU 2439 N GLU B 119 5715 11487 9500 2593 -1376 -310 N ATOM 2440 CA GLU B 119 28.754 -3.148 52.300 1.00 70.26 C ANISOU 2440 CA GLU B 119 5347 11892 9458 2174 -1419 -391 C ATOM 2441 C GLU B 119 29.158 -1.857 51.584 1.00 68.89 C ANISOU 2441 C GLU B 119 4609 12137 9430 1588 -1213 -565 C ATOM 2442 O GLU B 119 28.920 -0.750 52.088 1.00 67.19 O ANISOU 2442 O GLU B 119 4311 11939 9280 1017 -1152 -594 O ATOM 2443 CB GLU B 119 29.887 -3.623 53.201 1.00 76.08 C ANISOU 2443 CB GLU B 119 5818 13211 9876 2722 -1741 -492 C ATOM 2444 CG GLU B 119 29.996 -2.937 54.541 1.00 78.07 C ANISOU 2444 CG GLU B 119 5960 13701 10000 2443 -1878 -510 C ATOM 2445 CD GLU B 119 31.147 -3.487 55.361 1.00 84.96 C ANISOU 2445 CD GLU B 119 6554 15206 10522 3063 -2229 -619 C ATOM 2446 OE1 GLU B 119 32.176 -3.876 54.770 1.00 89.69 O ANISOU 2446 OE1 GLU B 119 6696 16382 11000 3533 -2320 -802 O ATOM 2447 OE2 GLU B 119 31.024 -3.534 56.598 1.00 87.38 O ANISOU 2447 OE2 GLU B 119 7082 15476 10643 3112 -2421 -536 O ATOM 2448 N LYS B 120 29.751 -2.022 50.402 1.00 69.73 N ANISOU 2448 N LYS B 120 4389 12550 9556 1728 -1108 -682 N ATOM 2449 CA LYS B 120 30.278 -0.922 49.603 1.00 69.67 C ANISOU 2449 CA LYS B 120 3859 12996 9615 1178 -908 -838 C ATOM 2450 C LYS B 120 29.219 -0.233 48.732 1.00 64.71 C ANISOU 2450 C LYS B 120 3551 11782 9254 633 -633 -717 C ATOM 2451 O LYS B 120 29.426 0.900 48.283 1.00 64.17 O ANISOU 2451 O LYS B 120 3238 11907 9239 36 -476 -790 O ATOM 2452 CB LYS B 120 31.445 -1.417 48.728 1.00 74.48 C ANISOU 2452 CB LYS B 120 3921 14315 10062 1577 -908 -1038 C ATOM 2453 CG LYS B 120 32.255 -2.581 49.338 1.00 80.01 C ANISOU 2453 CG LYS B 120 4495 15414 10491 2458 -1217 -1132 C ATOM 2454 CD LYS B 120 33.556 -2.866 48.570 1.00 87.58 C ANISOU 2454 CD LYS B 120 4740 17301 11234 2844 -1226 -1415 C ATOM 2455 CE LYS B 120 33.330 -3.104 47.057 1.00 86.91 C ANISOU 2455 CE LYS B 120 4701 17053 11266 2852 -967 -1428 C ATOM 2456 NZ LYS B 120 32.337 -4.187 46.729 1.00 82.73 N ANISOU 2456 NZ LYS B 120 4960 15610 10862 3318 -988 -1234 N ATOM 2457 N ASN B 121 28.086 -0.907 48.512 1.00 60.79 N ANISOU 2457 N ASN B 121 3627 10580 8892 822 -589 -537 N ATOM 2458 CA ASN B 121 27.060 -0.430 47.573 1.00 56.65 C ANISOU 2458 CA ASN B 121 3386 9550 8587 440 -356 -440 C ATOM 2459 C ASN B 121 25.624 -0.312 48.104 1.00 52.34 C ANISOU 2459 C ASN B 121 3379 8333 8176 252 -330 -279 C ATOM 2460 O ASN B 121 24.745 0.196 47.397 1.00 49.24 O ANISOU 2460 O ASN B 121 3183 7582 7942 -48 -164 -224 O ATOM 2461 CB ASN B 121 27.051 -1.306 46.318 1.00 56.81 C ANISOU 2461 CB ASN B 121 3470 9486 8629 785 -263 -438 C ATOM 2462 CG ASN B 121 28.299 -1.130 45.472 1.00 60.66 C ANISOU 2462 CG ASN B 121 3374 10676 8995 823 -193 -622 C ATOM 2463 OD1 ASN B 121 28.419 -0.172 44.711 1.00 61.33 O ANISOU 2463 OD1 ASN B 121 3253 10921 9129 318 -4 -656 O ATOM 2464 ND2 ASN B 121 29.218 -2.066 45.586 1.00 64.58 N ANISOU 2464 ND2 ASN B 121 3628 11609 9300 1432 -347 -746 N ATOM 2465 N TRP B 122 25.382 -0.756 49.336 1.00 52.58 N ANISOU 2465 N TRP B 122 3625 8245 8108 431 -494 -215 N ATOM 2466 CA TRP B 122 24.001 -0.822 49.846 1.00 49.58 C ANISOU 2466 CA TRP B 122 3724 7316 7799 280 -454 -79 C ATOM 2467 C TRP B 122 23.272 0.519 49.922 1.00 46.78 C ANISOU 2467 C TRP B 122 3387 6812 7576 -235 -331 -114 C ATOM 2468 O TRP B 122 23.885 1.588 50.059 1.00 47.42 O ANISOU 2468 O TRP B 122 3193 7170 7655 -531 -332 -231 O ATOM 2469 CB TRP B 122 23.896 -1.590 51.177 1.00 51.28 C ANISOU 2469 CB TRP B 122 4202 7458 7824 537 -643 12 C ATOM 2470 CG TRP B 122 24.660 -1.032 52.372 1.00 54.14 C ANISOU 2470 CG TRP B 122 4304 8237 8032 490 -808 -75 C ATOM 2471 CD1 TRP B 122 24.944 0.288 52.651 1.00 53.50 C ANISOU 2471 CD1 TRP B 122 3920 8415 7993 68 -776 -214 C ATOM 2472 CD2 TRP B 122 25.193 -1.790 53.469 1.00 57.79 C ANISOU 2472 CD2 TRP B 122 4846 8870 8239 872 -1050 -30 C ATOM 2473 NE1 TRP B 122 25.624 0.386 53.839 1.00 55.89 N ANISOU 2473 NE1 TRP B 122 4063 9081 8093 141 -974 -279 N ATOM 2474 CE2 TRP B 122 25.797 -0.871 54.361 1.00 58.72 C ANISOU 2474 CE2 TRP B 122 4632 9417 8263 655 -1150 -163 C ATOM 2475 CE3 TRP B 122 25.225 -3.159 53.782 1.00 59.33 C ANISOU 2475 CE3 TRP B 122 5424 8869 8251 1382 -1210 112 C ATOM 2476 CZ2 TRP B 122 26.419 -1.278 55.548 1.00 61.67 C ANISOU 2476 CZ2 TRP B 122 4981 10087 8362 951 -1405 -162 C ATOM 2477 CZ3 TRP B 122 25.852 -3.560 54.958 1.00 62.52 C ANISOU 2477 CZ3 TRP B 122 5861 9520 8375 1702 -1471 135 C ATOM 2478 CH2 TRP B 122 26.438 -2.622 55.826 1.00 63.80 C ANISOU 2478 CH2 TRP B 122 5624 10169 8447 1496 -1567 -2 C ATOM 2479 N GLY B 123 21.953 0.455 49.809 1.00 44.29 N ANISOU 2479 N GLY B 123 3415 6065 7350 -340 -232 -32 N ATOM 2480 CA GLY B 123 21.142 1.650 49.934 1.00 42.67 C ANISOU 2480 CA GLY B 123 3281 5697 7236 -700 -146 -86 C ATOM 2481 C GLY B 123 19.657 1.400 50.030 1.00 40.62 C ANISOU 2481 C GLY B 123 3336 5092 7006 -732 -67 -25 C ATOM 2482 O GLY B 123 19.189 0.268 49.888 1.00 40.43 O ANISOU 2482 O GLY B 123 3510 4910 6942 -565 -54 77 O ATOM 2483 N LEU B 124 18.918 2.471 50.293 1.00 40.05 N ANISOU 2483 N LEU B 124 3319 4925 6974 -954 -22 -111 N ATOM 2484 CA LEU B 124 17.478 2.369 50.511 1.00 39.32 C ANISOU 2484 CA LEU B 124 3429 4646 6864 -985 51 -110 C ATOM 2485 C LEU B 124 16.695 3.438 49.773 1.00 38.39 C ANISOU 2485 C LEU B 124 3351 4380 6857 -1091 131 -206 C ATOM 2486 O LEU B 124 17.136 4.551 49.597 1.00 38.35 O ANISOU 2486 O LEU B 124 3317 4354 6901 -1209 107 -289 O ATOM 2487 CB LEU B 124 17.115 2.398 52.001 1.00 40.26 C ANISOU 2487 CB LEU B 124 3617 4867 6814 -1027 -10 -146 C ATOM 2488 CG LEU B 124 17.629 1.277 52.916 1.00 42.35 C ANISOU 2488 CG LEU B 124 3957 5236 6898 -898 -112 -23 C ATOM 2489 CD1 LEU B 124 17.456 1.656 54.376 1.00 44.10 C ANISOU 2489 CD1 LEU B 124 4208 5614 6933 -982 -178 -86 C ATOM 2490 CD2 LEU B 124 16.920 -0.037 52.636 1.00 41.03 C ANISOU 2490 CD2 LEU B 124 4038 4884 6666 -837 -51 125 C ATOM 2491 N SER B 125 15.493 3.044 49.391 1.00 38.15 N ANISOU 2491 N SER B 125 3417 4251 6828 -1053 213 -199 N ATOM 2492 CA SER B 125 14.594 3.816 48.595 1.00 37.95 C ANISOU 2492 CA SER B 125 3435 4113 6871 -1048 268 -284 C ATOM 2493 C SER B 125 13.292 3.846 49.424 1.00 37.58 C ANISOU 2493 C SER B 125 3409 4176 6696 -1039 295 -394 C ATOM 2494 O SER B 125 12.842 2.793 49.912 1.00 36.67 O ANISOU 2494 O SER B 125 3303 4163 6468 -1091 338 -333 O ATOM 2495 CB SER B 125 14.427 3.017 47.312 1.00 37.88 C ANISOU 2495 CB SER B 125 3436 4022 6934 -994 338 -190 C ATOM 2496 OG SER B 125 13.461 3.559 46.472 1.00 42.66 O ANISOU 2496 OG SER B 125 4078 4558 7572 -950 377 -261 O ATOM 2497 N PHE B 126 12.718 5.043 49.604 1.00 37.27 N ANISOU 2497 N PHE B 126 3401 4123 6637 -977 266 -565 N ATOM 2498 CA PHE B 126 11.629 5.291 50.583 1.00 38.13 C ANISOU 2498 CA PHE B 126 3470 4438 6581 -927 282 -736 C ATOM 2499 C PHE B 126 10.358 5.820 49.917 1.00 38.23 C ANISOU 2499 C PHE B 126 3451 4506 6569 -743 306 -894 C ATOM 2500 O PHE B 126 10.425 6.734 49.097 1.00 38.53 O ANISOU 2500 O PHE B 126 3615 4327 6697 -600 243 -938 O ATOM 2501 CB PHE B 126 12.146 6.263 51.662 1.00 39.59 C ANISOU 2501 CB PHE B 126 3722 4617 6703 -934 189 -862 C ATOM 2502 CG PHE B 126 11.145 6.613 52.755 1.00 42.65 C ANISOU 2502 CG PHE B 126 4063 5254 6888 -850 204 -1075 C ATOM 2503 CD1 PHE B 126 10.475 5.625 53.477 1.00 42.92 C ANISOU 2503 CD1 PHE B 126 3967 5601 6741 -952 301 -1049 C ATOM 2504 CD2 PHE B 126 10.915 7.949 53.092 1.00 45.14 C ANISOU 2504 CD2 PHE B 126 4503 5490 7158 -684 119 -1312 C ATOM 2505 CE1 PHE B 126 9.589 5.965 54.502 1.00 45.24 C ANISOU 2505 CE1 PHE B 126 4172 6213 6805 -900 337 -1264 C ATOM 2506 CE2 PHE B 126 10.018 8.295 54.116 1.00 47.13 C ANISOU 2506 CE2 PHE B 126 4688 6025 7194 -551 133 -1552 C ATOM 2507 CZ PHE B 126 9.355 7.296 54.819 1.00 46.31 C ANISOU 2507 CZ PHE B 126 4370 6324 6903 -667 254 -1531 C ATOM 2508 N TYR B 127 9.209 5.236 50.263 1.00 38.53 N ANISOU 2508 N TYR B 127 3326 4864 6450 -758 390 -981 N ATOM 2509 CA TYR B 127 7.924 5.519 49.595 1.00 39.01 C ANISOU 2509 CA TYR B 127 3255 5123 6444 -571 411 -1152 C ATOM 2510 C TYR B 127 6.806 5.662 50.616 1.00 41.61 C ANISOU 2510 C TYR B 127 3375 5911 6523 -517 462 -1394 C ATOM 2511 O TYR B 127 6.878 5.092 51.702 1.00 42.01 O ANISOU 2511 O TYR B 127 3378 6149 6434 -743 533 -1361 O ATOM 2512 CB TYR B 127 7.548 4.413 48.582 1.00 37.98 C ANISOU 2512 CB TYR B 127 3038 5046 6346 -715 493 -1029 C ATOM 2513 CG TYR B 127 8.678 4.077 47.618 1.00 35.92 C ANISOU 2513 CG TYR B 127 2950 4406 6293 -771 468 -802 C ATOM 2514 CD1 TYR B 127 9.732 3.245 48.015 1.00 34.04 C ANISOU 2514 CD1 TYR B 127 2807 4027 6101 -956 484 -610 C ATOM 2515 CD2 TYR B 127 8.719 4.635 46.347 1.00 32.99 C ANISOU 2515 CD2 TYR B 127 2651 3853 6033 -601 417 -794 C ATOM 2516 CE1 TYR B 127 10.777 2.951 47.153 1.00 34.12 C ANISOU 2516 CE1 TYR B 127 2913 3787 6265 -956 465 -449 C ATOM 2517 CE2 TYR B 127 9.766 4.369 45.480 1.00 32.48 C ANISOU 2517 CE2 TYR B 127 2707 3517 6116 -666 416 -610 C ATOM 2518 CZ TYR B 127 10.795 3.509 45.888 1.00 33.35 C ANISOU 2518 CZ TYR B 127 2845 3555 6272 -838 447 -454 C ATOM 2519 OH TYR B 127 11.854 3.209 45.040 1.00 32.06 O ANISOU 2519 OH TYR B 127 2740 3219 6222 -858 452 -312 O ATOM 2520 N ALA B 128 5.774 6.420 50.254 1.00 43.51 N ANISOU 2520 N ALA B 128 3490 6366 6674 -194 421 -1643 N ATOM 2521 CA ALA B 128 4.650 6.689 51.137 1.00 47.07 C ANISOU 2521 CA ALA B 128 3675 7357 6853 -59 467 -1942 C ATOM 2522 C ALA B 128 3.407 6.869 50.292 1.00 49.64 C ANISOU 2522 C ALA B 128 3738 8051 7071 219 452 -2154 C ATOM 2523 O ALA B 128 3.512 7.104 49.085 1.00 48.63 O ANISOU 2523 O ALA B 128 3735 7648 7094 394 362 -2080 O ATOM 2524 CB ALA B 128 4.919 7.941 51.964 1.00 48.62 C ANISOU 2524 CB ALA B 128 4050 7420 7002 244 351 -2138 C ATOM 2525 N ASP B 129 2.234 6.779 50.924 1.00 53.63 N ANISOU 2525 N ASP B 129 3858 9236 7284 265 538 -2433 N ATOM 2526 CA ASP B 129 0.959 6.875 50.199 1.00 57.06 C ANISOU 2526 CA ASP B 129 3926 10199 7555 529 523 -2686 C ATOM 2527 C ASP B 129 0.575 8.321 49.903 1.00 59.81 C ANISOU 2527 C ASP B 129 4371 10490 7866 1269 312 -2970 C ATOM 2528 O ASP B 129 -0.366 8.589 49.155 1.00 62.42 O ANISOU 2528 O ASP B 129 4462 11180 8074 1642 230 -3180 O ATOM 2529 CB ASP B 129 -0.173 6.103 50.913 1.00 60.04 C ANISOU 2529 CB ASP B 129 3782 11445 7586 212 718 -2887 C ATOM 2530 CG ASP B 129 -0.648 6.765 52.219 1.00 64.76 C ANISOU 2530 CG ASP B 129 4187 12513 7908 439 751 -3205 C ATOM 2531 OD1 ASP B 129 -0.061 7.762 52.708 1.00 63.32 O ANISOU 2531 OD1 ASP B 129 4314 11940 7805 810 622 -3267 O ATOM 2532 OD2 ASP B 129 -1.659 6.273 52.764 1.00 71.74 O ANISOU 2532 OD2 ASP B 129 4590 14214 8455 212 918 -3418 O ATOM 2533 N LYS B 130 1.321 9.245 50.490 1.00 59.93 N ANISOU 2533 N LYS B 130 4774 10034 7962 1486 204 -2980 N ATOM 2534 CA LYS B 130 1.121 10.663 50.238 1.00 63.21 C ANISOU 2534 CA LYS B 130 5475 10201 8341 2175 -26 -3215 C ATOM 2535 C LYS B 130 2.430 11.270 49.752 1.00 61.10 C ANISOU 2535 C LYS B 130 5842 9018 8356 2125 -156 -2937 C ATOM 2536 O LYS B 130 3.498 10.703 50.000 1.00 57.03 O ANISOU 2536 O LYS B 130 5454 8192 8024 1611 -62 -2646 O ATOM 2537 CB LYS B 130 0.579 11.365 51.485 1.00 66.98 C ANISOU 2537 CB LYS B 130 5840 11057 8551 2520 -44 -3599 C ATOM 2538 CG LYS B 130 -0.949 11.247 51.616 1.00 71.56 C ANISOU 2538 CG LYS B 130 5795 12611 8781 2854 7 -4000 C ATOM 2539 CD LYS B 130 -1.450 11.807 52.934 1.00 75.37 C ANISOU 2539 CD LYS B 130 6105 13569 8964 3147 31 -4393 C ATOM 2540 CE LYS B 130 -2.920 11.485 53.153 1.00 79.79 C ANISOU 2540 CE LYS B 130 5910 15273 9134 3334 144 -4788 C ATOM 2541 NZ LYS B 130 -3.204 11.468 54.612 1.00 82.72 N ANISOU 2541 NZ LYS B 130 6009 16212 9208 3227 304 -5042 N ATOM 2542 N PRO B 131 2.350 12.398 49.019 1.00 63.74 N ANISOU 2542 N PRO B 131 6580 8944 8694 2650 -379 -3023 N ATOM 2543 CA PRO B 131 3.572 12.979 48.442 1.00 62.74 C ANISOU 2543 CA PRO B 131 7071 7973 8792 2505 -485 -2745 C ATOM 2544 C PRO B 131 4.556 13.538 49.477 1.00 63.26 C ANISOU 2544 C PRO B 131 7488 7640 8909 2290 -505 -2737 C ATOM 2545 O PRO B 131 5.766 13.538 49.233 1.00 61.05 O ANISOU 2545 O PRO B 131 7509 6863 8824 1875 -494 -2457 O ATOM 2546 CB PRO B 131 3.045 14.088 47.528 1.00 66.23 C ANISOU 2546 CB PRO B 131 7912 8120 9133 3151 -732 -2876 C ATOM 2547 CG PRO B 131 1.617 14.310 47.928 1.00 70.13 C ANISOU 2547 CG PRO B 131 8018 9295 9334 3763 -794 -3304 C ATOM 2548 CD PRO B 131 1.129 13.022 48.477 1.00 68.03 C ANISOU 2548 CD PRO B 131 7015 9818 9018 3352 -541 -3336 C ATOM 2549 N GLU B 132 4.031 14.005 50.609 1.00 66.49 N ANISOU 2549 N GLU B 132 7820 8327 9115 2567 -533 -3068 N ATOM 2550 CA GLU B 132 4.844 14.437 51.753 1.00 67.47 C ANISOU 2550 CA GLU B 132 8196 8202 9239 2349 -543 -3115 C ATOM 2551 C GLU B 132 4.621 13.466 52.927 1.00 66.70 C ANISOU 2551 C GLU B 132 7562 8752 9029 2044 -339 -3171 C ATOM 2552 O GLU B 132 3.535 12.886 53.066 1.00 68.25 O ANISOU 2552 O GLU B 132 7261 9623 9048 2178 -229 -3331 O ATOM 2553 CB GLU B 132 4.512 15.894 52.145 1.00 72.56 C ANISOU 2553 CB GLU B 132 9333 8537 9701 2934 -769 -3469 C ATOM 2554 CG GLU B 132 4.994 16.948 51.120 1.00 74.62 C ANISOU 2554 CG GLU B 132 10339 7967 10045 3112 -989 -3356 C ATOM 2555 CD GLU B 132 4.240 18.285 51.181 1.00 81.60 C ANISOU 2555 CD GLU B 132 11731 8586 10687 3907 -1253 -3732 C ATOM 2556 OE1 GLU B 132 3.993 18.804 52.295 1.00 83.40 O ANISOU 2556 OE1 GLU B 132 12023 8930 10734 4162 -1304 -4073 O ATOM 2557 OE2 GLU B 132 3.909 18.824 50.096 1.00 84.46 O ANISOU 2557 OE2 GLU B 132 12472 8602 11018 4309 -1426 -3690 O ATOM 2558 N THR B 133 5.646 13.273 53.756 1.00 65.11 N ANISOU 2558 N THR B 133 7462 8380 8896 1604 -291 -3036 N ATOM 2559 CA THR B 133 5.544 12.372 54.912 1.00 64.25 C ANISOU 2559 CA THR B 133 6951 8812 8647 1295 -118 -3046 C ATOM 2560 C THR B 133 5.630 13.132 56.220 1.00 67.12 C ANISOU 2560 C THR B 133 7463 9227 8814 1427 -179 -3333 C ATOM 2561 O THR B 133 6.090 14.269 56.251 1.00 69.07 O ANISOU 2561 O THR B 133 8187 8966 9090 1622 -359 -3462 O ATOM 2562 CB THR B 133 6.662 11.316 54.933 1.00 60.29 C ANISOU 2562 CB THR B 133 6401 8175 8329 697 -17 -2649 C ATOM 2563 OG1 THR B 133 7.938 11.960 54.821 1.00 59.81 O ANISOU 2563 OG1 THR B 133 6749 7533 8443 538 -145 -2525 O ATOM 2564 CG2 THR B 133 6.478 10.316 53.808 1.00 57.25 C ANISOU 2564 CG2 THR B 133 5815 7850 8086 535 80 -2393 C ATOM 2565 N THR B 134 5.197 12.489 57.300 1.00 67.83 N ANISOU 2565 N THR B 134 7182 9918 8674 1279 -28 -3430 N ATOM 2566 CA THR B 134 5.301 13.065 58.633 1.00 70.35 C ANISOU 2566 CA THR B 134 7595 10367 8769 1354 -63 -3696 C ATOM 2567 C THR B 134 6.720 12.909 59.189 1.00 68.25 C ANISOU 2567 C THR B 134 7569 9736 8628 884 -105 -3454 C ATOM 2568 O THR B 134 7.493 12.062 58.725 1.00 64.50 O ANISOU 2568 O THR B 134 7050 9099 8358 483 -57 -3076 O ATOM 2569 CB THR B 134 4.288 12.426 59.606 1.00 72.61 C ANISOU 2569 CB THR B 134 7380 11507 8700 1336 133 -3891 C ATOM 2570 OG1 THR B 134 4.555 11.025 59.732 1.00 69.95 O ANISOU 2570 OG1 THR B 134 6792 11402 8382 759 314 -3528 O ATOM 2571 CG2 THR B 134 2.853 12.633 59.113 1.00 75.91 C ANISOU 2571 CG2 THR B 134 7462 12439 8940 1822 169 -4202 C ATOM 2572 N LYS B 135 7.043 13.748 60.176 1.00 70.97 N ANISOU 2572 N LYS B 135 8158 9985 8822 974 -211 -3706 N ATOM 2573 CA LYS B 135 8.306 13.707 60.921 1.00 70.11 C ANISOU 2573 CA LYS B 135 8222 9670 8746 562 -273 -3569 C ATOM 2574 C LYS B 135 8.580 12.306 61.439 1.00 67.53 C ANISOU 2574 C LYS B 135 7542 9756 8359 143 -115 -3267 C ATOM 2575 O LYS B 135 9.733 11.860 61.485 1.00 64.95 O ANISOU 2575 O LYS B 135 7279 9232 8166 -214 -161 -2990 O ATOM 2576 CB LYS B 135 8.264 14.670 62.122 1.00 74.26 C ANISOU 2576 CB LYS B 135 8962 10246 9008 751 -375 -3967 C ATOM 2577 CG LYS B 135 7.958 16.130 61.808 1.00 78.57 C ANISOU 2577 CG LYS B 135 9989 10328 9538 1224 -566 -4323 C ATOM 2578 CD LYS B 135 6.460 16.458 61.911 1.00 83.69 C ANISOU 2578 CD LYS B 135 10454 11412 9932 1861 -523 -4711 C ATOM 2579 CE LYS B 135 6.244 17.908 62.348 1.00 88.24 C ANISOU 2579 CE LYS B 135 11548 11652 10326 2369 -733 -5186 C ATOM 2580 NZ LYS B 135 4.859 18.426 62.102 1.00 92.66 N ANISOU 2580 NZ LYS B 135 12024 12505 10677 3148 -764 -5580 N ATOM 2581 N GLU B 136 7.499 11.634 61.835 1.00 68.58 N ANISOU 2581 N GLU B 136 7320 10484 8252 199 63 -3338 N ATOM 2582 CA GLU B 136 7.524 10.256 62.328 1.00 67.52 C ANISOU 2582 CA GLU B 136 6931 10738 7987 -201 226 -3053 C ATOM 2583 C GLU B 136 7.970 9.268 61.232 1.00 63.05 C ANISOU 2583 C GLU B 136 6341 9910 7704 -451 263 -2640 C ATOM 2584 O GLU B 136 8.885 8.463 61.430 1.00 61.26 O ANISOU 2584 O GLU B 136 6178 9567 7531 -760 247 -2330 O ATOM 2585 CB GLU B 136 6.124 9.878 62.858 1.00 70.90 C ANISOU 2585 CB GLU B 136 6997 11886 8056 -133 428 -3261 C ATOM 2586 CG GLU B 136 6.109 9.049 64.153 1.00 74.89 C ANISOU 2586 CG GLU B 136 7384 12868 8202 -492 562 -3169 C ATOM 2587 CD GLU B 136 7.023 7.824 64.090 1.00 74.73 C ANISOU 2587 CD GLU B 136 7491 12617 8288 -940 568 -2677 C ATOM 2588 OE1 GLU B 136 8.102 7.850 64.729 1.00 75.40 O ANISOU 2588 OE1 GLU B 136 7786 12491 8373 -1050 436 -2557 O ATOM 2589 OE2 GLU B 136 6.667 6.852 63.388 1.00 74.14 O ANISOU 2589 OE2 GLU B 136 7318 12573 8278 -1151 686 -2435 O ATOM 2590 N GLN B 137 7.307 9.337 60.080 1.00 61.68 N ANISOU 2590 N GLN B 137 6084 9667 7684 -269 296 -2661 N ATOM 2591 CA GLN B 137 7.584 8.441 58.971 1.00 57.42 C ANISOU 2591 CA GLN B 137 5520 8912 7387 -465 339 -2324 C ATOM 2592 C GLN B 137 9.020 8.643 58.519 1.00 54.42 C ANISOU 2592 C GLN B 137 5404 7983 7290 -572 191 -2109 C ATOM 2593 O GLN B 137 9.759 7.678 58.362 1.00 51.55 O ANISOU 2593 O GLN B 137 5043 7527 7015 -830 208 -1802 O ATOM 2594 CB GLN B 137 6.593 8.678 57.830 1.00 57.67 C ANISOU 2594 CB GLN B 137 5420 8994 7499 -198 370 -2445 C ATOM 2595 CG GLN B 137 5.179 8.141 58.121 1.00 61.34 C ANISOU 2595 CG GLN B 137 5496 10145 7666 -207 550 -2615 C ATOM 2596 CD GLN B 137 4.105 8.603 57.127 1.00 64.05 C ANISOU 2596 CD GLN B 137 5649 10666 8022 171 538 -2841 C ATOM 2597 OE1 GLN B 137 4.309 9.523 56.327 1.00 64.84 O ANISOU 2597 OE1 GLN B 137 5976 10344 8317 535 375 -2913 O ATOM 2598 NE2 GLN B 137 2.941 7.967 57.194 1.00 65.93 N ANISOU 2598 NE2 GLN B 137 5475 11563 8011 69 706 -2961 N ATOM 2599 N LEU B 138 9.412 9.904 58.346 1.00 54.80 N ANISOU 2599 N LEU B 138 5691 7692 7439 -377 43 -2290 N ATOM 2600 CA LEU B 138 10.778 10.250 57.980 1.00 53.02 C ANISOU 2600 CA LEU B 138 5689 7026 7428 -552 -87 -2137 C ATOM 2601 C LEU B 138 11.764 9.665 59.001 1.00 52.66 C ANISOU 2601 C LEU B 138 5592 7131 7287 -834 -118 -2002 C ATOM 2602 O LEU B 138 12.772 9.053 58.621 1.00 51.14 O ANISOU 2602 O LEU B 138 5371 6823 7236 -1033 -148 -1743 O ATOM 2603 CB LEU B 138 10.920 11.769 57.849 1.00 55.80 C ANISOU 2603 CB LEU B 138 6387 7001 7812 -369 -239 -2393 C ATOM 2604 CG LEU B 138 12.153 12.384 57.174 1.00 56.00 C ANISOU 2604 CG LEU B 138 6693 6542 8042 -593 -359 -2275 C ATOM 2605 CD1 LEU B 138 12.420 11.797 55.785 1.00 53.63 C ANISOU 2605 CD1 LEU B 138 6321 6082 7974 -684 -297 -1985 C ATOM 2606 CD2 LEU B 138 11.982 13.897 57.095 1.00 61.47 C ANISOU 2606 CD2 LEU B 138 7842 6820 8692 -400 -505 -2555 C ATOM 2607 N GLY B 139 11.447 9.814 60.286 1.00 54.30 N ANISOU 2607 N GLY B 139 5769 7642 7221 -812 -116 -2188 N ATOM 2608 CA GLY B 139 12.218 9.194 61.365 1.00 54.56 C ANISOU 2608 CA GLY B 139 5754 7889 7088 -1034 -155 -2065 C ATOM 2609 C GLY B 139 12.539 7.719 61.169 1.00 52.59 C ANISOU 2609 C GLY B 139 5391 7734 6856 -1205 -88 -1697 C ATOM 2610 O GLY B 139 13.688 7.292 61.349 1.00 52.12 O ANISOU 2610 O GLY B 139 5349 7626 6829 -1327 -196 -1514 O ATOM 2611 N GLU B 140 11.520 6.949 60.794 1.00 51.59 N ANISOU 2611 N GLU B 140 5164 7756 6683 -1200 75 -1610 N ATOM 2612 CA GLU B 140 11.651 5.517 60.532 1.00 50.56 C ANISOU 2612 CA GLU B 140 5030 7638 6543 -1367 142 -1275 C ATOM 2613 C GLU B 140 12.641 5.217 59.395 1.00 47.78 C ANISOU 2613 C GLU B 140 4721 6929 6502 -1352 62 -1063 C ATOM 2614 O GLU B 140 13.501 4.342 59.519 1.00 47.73 O ANISOU 2614 O GLU B 140 4777 6877 6482 -1411 -7 -827 O ATOM 2615 CB GLU B 140 10.265 4.899 60.250 1.00 50.75 C ANISOU 2615 CB GLU B 140 4943 7895 6443 -1436 341 -1280 C ATOM 2616 CG GLU B 140 9.382 4.762 61.498 1.00 55.24 C ANISOU 2616 CG GLU B 140 5433 8947 6608 -1555 459 -1415 C ATOM 2617 CD GLU B 140 7.910 4.442 61.205 1.00 58.70 C ANISOU 2617 CD GLU B 140 5657 9756 6891 -1642 667 -1529 C ATOM 2618 OE1 GLU B 140 7.586 3.937 60.111 1.00 58.02 O ANISOU 2618 OE1 GLU B 140 5531 9539 6977 -1692 723 -1416 O ATOM 2619 OE2 GLU B 140 7.061 4.694 62.090 1.00 62.61 O ANISOU 2619 OE2 GLU B 140 5990 10740 7059 -1671 777 -1756 O ATOM 2620 N PHE B 141 12.518 5.940 58.289 1.00 46.06 N ANISOU 2620 N PHE B 141 4485 6482 6532 -1242 64 -1156 N ATOM 2621 CA PHE B 141 13.469 5.811 57.190 1.00 44.10 C ANISOU 2621 CA PHE B 141 4256 5951 6550 -1247 5 -992 C ATOM 2622 C PHE B 141 14.910 6.155 57.631 1.00 44.97 C ANISOU 2622 C PHE B 141 4369 6039 6678 -1320 -154 -976 C ATOM 2623 O PHE B 141 15.854 5.451 57.259 1.00 43.59 O ANISOU 2623 O PHE B 141 4140 5844 6579 -1337 -204 -787 O ATOM 2624 CB PHE B 141 13.018 6.670 56.000 1.00 43.66 C ANISOU 2624 CB PHE B 141 4230 5664 6694 -1134 31 -1105 C ATOM 2625 CG PHE B 141 13.994 6.705 54.849 1.00 43.13 C ANISOU 2625 CG PHE B 141 4183 5341 6862 -1179 -11 -962 C ATOM 2626 CD1 PHE B 141 14.434 7.912 54.348 1.00 46.09 C ANISOU 2626 CD1 PHE B 141 4683 5480 7350 -1202 -82 -1072 C ATOM 2627 CD2 PHE B 141 14.438 5.529 54.247 1.00 45.22 C ANISOU 2627 CD2 PHE B 141 4381 5598 7201 -1208 27 -727 C ATOM 2628 CE1 PHE B 141 15.328 7.963 53.278 1.00 47.10 C ANISOU 2628 CE1 PHE B 141 4812 5438 7647 -1307 -92 -942 C ATOM 2629 CE2 PHE B 141 15.334 5.572 53.177 1.00 45.12 C ANISOU 2629 CE2 PHE B 141 4342 5431 7370 -1233 6 -627 C ATOM 2630 CZ PHE B 141 15.773 6.787 52.696 1.00 45.94 C ANISOU 2630 CZ PHE B 141 4514 5372 7569 -1308 -40 -730 C ATOM 2631 N TYR B 142 15.068 7.214 58.429 1.00 46.27 N ANISOU 2631 N TYR B 142 4584 6249 6748 -1352 -239 -1202 N ATOM 2632 CA TYR B 142 16.398 7.629 58.862 1.00 48.85 C ANISOU 2632 CA TYR B 142 4880 6617 7062 -1487 -394 -1232 C ATOM 2633 C TYR B 142 17.032 6.569 59.737 1.00 50.37 C ANISOU 2633 C TYR B 142 4978 7090 7070 -1484 -469 -1068 C ATOM 2634 O TYR B 142 18.239 6.396 59.719 1.00 50.94 O ANISOU 2634 O TYR B 142 4930 7263 7160 -1529 -591 -1000 O ATOM 2635 CB TYR B 142 16.353 8.943 59.645 1.00 50.76 C ANISOU 2635 CB TYR B 142 5256 6837 7194 -1549 -480 -1536 C ATOM 2636 CG TYR B 142 16.126 10.188 58.820 1.00 50.89 C ANISOU 2636 CG TYR B 142 5483 6488 7366 -1558 -486 -1704 C ATOM 2637 CD1 TYR B 142 15.853 11.398 59.444 1.00 53.20 C ANISOU 2637 CD1 TYR B 142 6014 6656 7543 -1546 -566 -2007 C ATOM 2638 CD2 TYR B 142 16.176 10.164 57.424 1.00 49.42 C ANISOU 2638 CD2 TYR B 142 5321 6050 7408 -1561 -427 -1565 C ATOM 2639 CE1 TYR B 142 15.641 12.556 58.715 1.00 55.00 C ANISOU 2639 CE1 TYR B 142 6560 6465 7874 -1522 -603 -2153 C ATOM 2640 CE2 TYR B 142 15.961 11.330 56.673 1.00 50.26 C ANISOU 2640 CE2 TYR B 142 5712 5773 7610 -1564 -452 -1694 C ATOM 2641 CZ TYR B 142 15.692 12.518 57.336 1.00 53.71 C ANISOU 2641 CZ TYR B 142 6443 6040 7922 -1536 -549 -1981 C ATOM 2642 OH TYR B 142 15.477 13.686 56.640 1.00 56.43 O ANISOU 2642 OH TYR B 142 7191 5928 8321 -1507 -606 -2104 O ATOM 2643 N GLU B 143 16.198 5.881 60.514 1.00 51.48 N ANISOU 2643 N GLU B 143 5180 7387 6993 -1431 -399 -1014 N ATOM 2644 CA GLU B 143 16.655 4.837 61.421 1.00 54.14 C ANISOU 2644 CA GLU B 143 5545 7938 7089 -1410 -479 -830 C ATOM 2645 C GLU B 143 17.233 3.647 60.635 1.00 53.15 C ANISOU 2645 C GLU B 143 5430 7698 7068 -1303 -503 -547 C ATOM 2646 O GLU B 143 18.224 3.030 61.038 1.00 55.05 O ANISOU 2646 O GLU B 143 5658 8065 7195 -1195 -661 -421 O ATOM 2647 CB GLU B 143 15.479 4.384 62.284 1.00 55.33 C ANISOU 2647 CB GLU B 143 5813 8253 6957 -1455 -356 -821 C ATOM 2648 CG GLU B 143 15.798 4.213 63.751 1.00 61.13 C ANISOU 2648 CG GLU B 143 6616 9276 7336 -1488 -463 -823 C ATOM 2649 CD GLU B 143 14.641 3.614 64.536 1.00 66.20 C ANISOU 2649 CD GLU B 143 7386 10118 7650 -1600 -307 -771 C ATOM 2650 OE1 GLU B 143 13.481 3.669 64.053 1.00 66.77 O ANISOU 2650 OE1 GLU B 143 7412 10191 7767 -1663 -110 -846 O ATOM 2651 OE2 GLU B 143 14.898 3.083 65.644 1.00 70.14 O ANISOU 2651 OE2 GLU B 143 8021 10820 7810 -1641 -384 -658 O ATOM 2652 N ALA B 144 16.592 3.332 59.514 1.00 51.11 N ANISOU 2652 N ALA B 144 5201 7216 7003 -1291 -361 -472 N ATOM 2653 CA ALA B 144 17.014 2.245 58.643 1.00 50.36 C ANISOU 2653 CA ALA B 144 5156 6967 7012 -1172 -367 -245 C ATOM 2654 C ALA B 144 18.333 2.638 57.997 1.00 50.48 C ANISOU 2654 C ALA B 144 4961 7012 7206 -1090 -484 -282 C ATOM 2655 O ALA B 144 19.252 1.829 57.909 1.00 51.62 O ANISOU 2655 O ALA B 144 5078 7228 7308 -906 -600 -150 O ATOM 2656 CB ALA B 144 15.946 1.960 57.593 1.00 47.55 C ANISOU 2656 CB ALA B 144 4863 6402 6803 -1220 -185 -209 C ATOM 2657 N LEU B 145 18.436 3.905 57.592 1.00 50.22 N ANISOU 2657 N LEU B 145 4798 6952 7334 -1230 -461 -476 N ATOM 2658 CA LEU B 145 19.678 4.425 57.038 1.00 51.17 C ANISOU 2658 CA LEU B 145 4702 7166 7573 -1283 -547 -535 C ATOM 2659 C LEU B 145 20.800 4.309 58.053 1.00 54.83 C ANISOU 2659 C LEU B 145 5010 7985 7839 -1250 -742 -568 C ATOM 2660 O LEU B 145 21.933 3.999 57.684 1.00 56.27 O ANISOU 2660 O LEU B 145 4961 8386 8032 -1165 -836 -538 O ATOM 2661 CB LEU B 145 19.514 5.881 56.580 1.00 50.82 C ANISOU 2661 CB LEU B 145 4675 6967 7669 -1517 -498 -731 C ATOM 2662 CG LEU B 145 18.781 6.157 55.263 1.00 46.17 C ANISOU 2662 CG LEU B 145 4189 6065 7289 -1519 -351 -706 C ATOM 2663 CD1 LEU B 145 18.832 7.633 54.986 1.00 48.73 C ANISOU 2663 CD1 LEU B 145 4626 6208 7680 -1735 -363 -888 C ATOM 2664 CD2 LEU B 145 19.360 5.400 54.083 1.00 44.84 C ANISOU 2664 CD2 LEU B 145 3892 5893 7250 -1440 -306 -545 C ATOM 2665 N ASP B 146 20.471 4.547 59.327 1.00 56.94 N ANISOU 2665 N ASP B 146 5376 8366 7894 -1296 -806 -648 N ATOM 2666 CA ASP B 146 21.430 4.438 60.431 1.00 60.99 C ANISOU 2666 CA ASP B 146 5760 9248 8164 -1251 -1013 -688 C ATOM 2667 C ASP B 146 22.003 3.031 60.517 1.00 62.23 C ANISOU 2667 C ASP B 146 5922 9535 8187 -910 -1130 -460 C ATOM 2668 O ASP B 146 23.206 2.857 60.722 1.00 64.86 O ANISOU 2668 O ASP B 146 6008 10217 8417 -773 -1318 -488 O ATOM 2669 CB ASP B 146 20.787 4.804 61.781 1.00 62.80 C ANISOU 2669 CB ASP B 146 6154 9557 8149 -1332 -1040 -794 C ATOM 2670 CG ASP B 146 20.454 6.293 61.910 1.00 64.42 C ANISOU 2670 CG ASP B 146 6384 9672 8421 -1598 -998 -1086 C ATOM 2671 OD1 ASP B 146 19.483 6.616 62.647 1.00 66.57 O ANISOU 2671 OD1 ASP B 146 6832 9907 8556 -1616 -933 -1193 O ATOM 2672 OD2 ASP B 146 21.150 7.136 61.293 1.00 65.46 O ANISOU 2672 OD2 ASP B 146 6391 9773 8709 -1793 -1030 -1217 O ATOM 2673 N CYS B 147 21.144 2.028 60.359 1.00 61.04 N ANISOU 2673 N CYS B 147 6068 9116 8009 -769 -1033 -250 N ATOM 2674 CA CYS B 147 21.605 0.648 60.388 1.00 62.96 C ANISOU 2674 CA CYS B 147 6465 9352 8104 -419 -1156 -23 C ATOM 2675 C CYS B 147 22.633 0.401 59.282 1.00 62.76 C ANISOU 2675 C CYS B 147 6175 9418 8251 -200 -1212 -32 C ATOM 2676 O CYS B 147 23.610 -0.321 59.492 1.00 65.24 O ANISOU 2676 O CYS B 147 6419 9963 8404 161 -1416 25 O ATOM 2677 CB CYS B 147 20.434 -0.342 60.309 1.00 62.25 C ANISOU 2677 CB CYS B 147 6811 8894 7948 -420 -1019 194 C ATOM 2678 SG CYS B 147 20.879 -2.022 59.671 1.00 65.18 S ANISOU 2678 SG CYS B 147 7500 9010 8257 1 -1123 463 S ATOM 2679 N LEU B 148 22.423 1.020 58.120 1.00 59.79 N ANISOU 2679 N LEU B 148 5647 8903 8167 -391 -1039 -119 N ATOM 2680 CA LEU B 148 23.364 0.875 57.004 1.00 59.60 C ANISOU 2680 CA LEU B 148 5338 9023 8285 -242 -1052 -150 C ATOM 2681 C LEU B 148 24.538 1.861 57.045 1.00 61.40 C ANISOU 2681 C LEU B 148 5098 9723 8509 -420 -1140 -365 C ATOM 2682 O LEU B 148 25.404 1.843 56.164 1.00 62.29 O ANISOU 2682 O LEU B 148 4892 10082 8694 -359 -1136 -425 O ATOM 2683 CB LEU B 148 22.636 0.944 55.658 1.00 56.21 C ANISOU 2683 CB LEU B 148 4995 8241 8120 -359 -829 -114 C ATOM 2684 CG LEU B 148 21.528 -0.087 55.413 1.00 54.67 C ANISOU 2684 CG LEU B 148 5216 7630 7927 -243 -732 72 C ATOM 2685 CD1 LEU B 148 20.898 0.162 54.061 1.00 52.47 C ANISOU 2685 CD1 LEU B 148 4940 7099 7898 -381 -534 59 C ATOM 2686 CD2 LEU B 148 22.026 -1.533 55.505 1.00 56.81 C ANISOU 2686 CD2 LEU B 148 5699 7860 8028 190 -878 234 C ATOM 2687 N ARG B 149 24.561 2.710 58.074 1.00 62.24 N ANISOU 2687 N ARG B 149 5163 9986 8500 -675 -1214 -499 N ATOM 2688 CA ARG B 149 25.618 3.723 58.272 1.00 64.50 C ANISOU 2688 CA ARG B 149 5051 10718 8737 -963 -1308 -729 C ATOM 2689 C ARG B 149 25.720 4.709 57.098 1.00 63.03 C ANISOU 2689 C ARG B 149 4736 10431 8782 -1364 -1134 -835 C ATOM 2690 O ARG B 149 26.816 5.118 56.691 1.00 65.39 O ANISOU 2690 O ARG B 149 4642 11151 9054 -1555 -1168 -965 O ATOM 2691 CB ARG B 149 26.969 3.065 58.579 1.00 68.52 C ANISOU 2691 CB ARG B 149 5172 11832 9030 -636 -1537 -767 C ATOM 2692 CG ARG B 149 26.981 2.208 59.833 1.00 71.63 C ANISOU 2692 CG ARG B 149 5747 12335 9133 -242 -1758 -662 C ATOM 2693 CD ARG B 149 28.315 1.466 60.003 1.00 78.16 C ANISOU 2693 CD ARG B 149 6202 13766 9728 225 -2018 -702 C ATOM 2694 NE ARG B 149 28.558 0.526 58.905 1.00 80.07 N ANISOU 2694 NE ARG B 149 6420 13938 10066 641 -1977 -598 N ATOM 2695 CZ ARG B 149 29.663 0.484 58.157 1.00 84.23 C ANISOU 2695 CZ ARG B 149 6426 14993 10585 790 -2019 -748 C ATOM 2696 NH1 ARG B 149 30.679 1.316 58.392 1.00 88.26 N ANISOU 2696 NH1 ARG B 149 6359 16191 10985 505 -2106 -1003 N ATOM 2697 NH2 ARG B 149 29.764 -0.416 57.180 1.00 84.20 N ANISOU 2697 NH2 ARG B 149 6470 14872 10652 1213 -1973 -663 N ATOM 2698 N ILE B 150 24.560 5.069 56.556 1.00 59.26 N ANISOU 2698 N ILE B 150 4595 9428 8494 -1494 -950 -777 N ATOM 2699 CA ILE B 150 24.451 6.082 55.512 1.00 58.07 C ANISOU 2699 CA ILE B 150 4473 9063 8530 -1861 -798 -848 C ATOM 2700 C ILE B 150 24.058 7.381 56.208 1.00 58.52 C ANISOU 2700 C ILE B 150 4746 8937 8550 -2224 -820 -1026 C ATOM 2701 O ILE B 150 23.029 7.425 56.881 1.00 57.46 O ANISOU 2701 O ILE B 150 4899 8545 8389 -2111 -810 -1030 O ATOM 2702 CB ILE B 150 23.415 5.664 54.418 1.00 54.35 C ANISOU 2702 CB ILE B 150 4251 8142 8258 -1705 -616 -690 C ATOM 2703 CG1 ILE B 150 23.935 4.436 53.661 1.00 54.32 C ANISOU 2703 CG1 ILE B 150 4060 8308 8272 -1364 -606 -555 C ATOM 2704 CG2 ILE B 150 23.126 6.826 53.459 1.00 53.44 C ANISOU 2704 CG2 ILE B 150 4280 7732 8293 -2058 -485 -752 C ATOM 2705 CD1 ILE B 150 22.905 3.655 52.925 1.00 48.87 C ANISOU 2705 CD1 ILE B 150 3636 7225 7706 -1138 -480 -395 C ATOM 2706 N PRO B 151 24.891 8.432 56.087 1.00 61.12 N ANISOU 2706 N PRO B 151 4952 9427 8843 -2676 -852 -1195 N ATOM 2707 CA PRO B 151 24.511 9.681 56.761 1.00 62.37 C ANISOU 2707 CA PRO B 151 5420 9331 8947 -3006 -895 -1387 C ATOM 2708 C PRO B 151 23.205 10.254 56.207 1.00 59.66 C ANISOU 2708 C PRO B 151 5549 8360 8760 -2962 -765 -1363 C ATOM 2709 O PRO B 151 22.877 10.024 55.045 1.00 57.43 O ANISOU 2709 O PRO B 151 5319 7864 8637 -2880 -633 -1219 O ATOM 2710 CB PRO B 151 25.692 10.630 56.474 1.00 66.38 C ANISOU 2710 CB PRO B 151 5754 10086 9382 -3582 -932 -1546 C ATOM 2711 CG PRO B 151 26.822 9.751 56.034 1.00 67.60 C ANISOU 2711 CG PRO B 151 5348 10851 9485 -3488 -948 -1478 C ATOM 2712 CD PRO B 151 26.202 8.529 55.411 1.00 63.65 C ANISOU 2712 CD PRO B 151 4860 10199 9127 -2933 -855 -1243 C ATOM 2713 N ARG B 152 22.463 10.979 57.038 1.00 60.23 N ANISOU 2713 N ARG B 152 5945 8180 8758 -2971 -814 -1523 N ATOM 2714 CA ARG B 152 21.235 11.642 56.594 1.00 59.35 C ANISOU 2714 CA ARG B 152 6271 7534 8748 -2862 -729 -1560 C ATOM 2715 C ARG B 152 21.504 12.702 55.514 1.00 60.66 C ANISOU 2715 C ARG B 152 6715 7335 9000 -3213 -691 -1584 C ATOM 2716 O ARG B 152 20.678 12.929 54.624 1.00 58.48 O ANISOU 2716 O ARG B 152 6713 6666 8840 -3056 -605 -1512 O ATOM 2717 CB ARG B 152 20.497 12.253 57.788 1.00 60.94 C ANISOU 2717 CB ARG B 152 6735 7620 8799 -2764 -809 -1785 C ATOM 2718 CG ARG B 152 20.023 11.201 58.783 1.00 60.65 C ANISOU 2718 CG ARG B 152 6498 7907 8641 -2436 -811 -1729 C ATOM 2719 CD ARG B 152 19.459 11.820 60.052 1.00 64.32 C ANISOU 2719 CD ARG B 152 7162 8376 8899 -2381 -886 -1982 C ATOM 2720 NE ARG B 152 19.090 10.781 61.012 1.00 64.36 N ANISOU 2720 NE ARG B 152 6987 8732 8736 -2144 -877 -1898 N ATOM 2721 CZ ARG B 152 18.415 10.991 62.139 1.00 66.51 C ANISOU 2721 CZ ARG B 152 7368 9115 8788 -2031 -895 -2073 C ATOM 2722 NH1 ARG B 152 18.006 12.216 62.477 1.00 67.93 N ANISOU 2722 NH1 ARG B 152 7836 9074 8901 -2061 -939 -2380 N ATOM 2723 NH2 ARG B 152 18.149 9.959 62.932 1.00 66.30 N ANISOU 2723 NH2 ARG B 152 7204 9413 8576 -1880 -873 -1944 N ATOM 2724 N SER B 153 22.672 13.332 55.590 1.00 64.01 N ANISOU 2724 N SER B 153 7071 7919 9331 -3715 -761 -1681 N ATOM 2725 CA SER B 153 23.101 14.317 54.596 1.00 66.71 C ANISOU 2725 CA SER B 153 7700 7953 9693 -4185 -718 -1680 C ATOM 2726 C SER B 153 23.190 13.759 53.168 1.00 64.87 C ANISOU 2726 C SER B 153 7315 7732 9602 -4134 -561 -1438 C ATOM 2727 O SER B 153 23.119 14.519 52.209 1.00 66.32 O ANISOU 2727 O SER B 153 7865 7526 9806 -4392 -502 -1386 O ATOM 2728 CB SER B 153 24.444 14.909 55.002 1.00 71.41 C ANISOU 2728 CB SER B 153 8134 8881 10116 -4822 -805 -1832 C ATOM 2729 OG SER B 153 25.314 13.872 55.398 1.00 71.76 O ANISOU 2729 OG SER B 153 7509 9651 10107 -4736 -834 -1797 O ATOM 2730 N ASP B 154 23.340 12.441 53.029 1.00 62.27 N ANISOU 2730 N ASP B 154 6503 7816 9340 -3794 -506 -1293 N ATOM 2731 CA ASP B 154 23.383 11.801 51.709 1.00 60.52 C ANISOU 2731 CA ASP B 154 6128 7628 9238 -3681 -361 -1090 C ATOM 2732 C ASP B 154 22.002 11.580 51.043 1.00 56.69 C ANISOU 2732 C ASP B 154 5956 6686 8899 -3267 -279 -972 C ATOM 2733 O ASP B 154 21.921 11.063 49.921 1.00 54.83 O ANISOU 2733 O ASP B 154 5638 6440 8753 -3157 -165 -815 O ATOM 2734 CB ASP B 154 24.161 10.478 51.780 1.00 60.15 C ANISOU 2734 CB ASP B 154 5494 8186 9176 -3452 -357 -1013 C ATOM 2735 CG ASP B 154 25.662 10.684 52.003 1.00 65.94 C ANISOU 2735 CG ASP B 154 5802 9505 9746 -3869 -413 -1129 C ATOM 2736 OD1 ASP B 154 26.185 11.795 51.755 1.00 68.91 O ANISOU 2736 OD1 ASP B 154 6320 9826 10038 -4460 -398 -1225 O ATOM 2737 OD2 ASP B 154 26.330 9.710 52.416 1.00 69.28 O ANISOU 2737 OD2 ASP B 154 5757 10468 10097 -3606 -482 -1131 O ATOM 2738 N VAL B 155 20.922 11.984 51.700 1.00 55.35 N ANISOU 2738 N VAL B 155 6113 6193 8723 -3034 -339 -1073 N ATOM 2739 CA VAL B 155 19.593 11.677 51.164 1.00 52.30 C ANISOU 2739 CA VAL B 155 5906 5527 8436 -2614 -274 -1000 C ATOM 2740 C VAL B 155 19.201 12.616 50.019 1.00 53.09 C ANISOU 2740 C VAL B 155 6441 5160 8569 -2699 -245 -964 C ATOM 2741 O VAL B 155 19.468 13.818 50.070 1.00 55.53 O ANISOU 2741 O VAL B 155 7149 5158 8794 -3001 -319 -1065 O ATOM 2742 CB VAL B 155 18.499 11.614 52.269 1.00 51.45 C ANISOU 2742 CB VAL B 155 5891 5389 8271 -2275 -329 -1139 C ATOM 2743 CG1 VAL B 155 17.149 11.214 51.688 1.00 48.14 C ANISOU 2743 CG1 VAL B 155 5545 4825 7920 -1879 -252 -1088 C ATOM 2744 CG2 VAL B 155 18.887 10.596 53.325 1.00 51.33 C ANISOU 2744 CG2 VAL B 155 5505 5813 8184 -2202 -355 -1121 C ATOM 2745 N MET B 156 18.590 12.037 48.984 1.00 50.46 N ANISOU 2745 N MET B 156 6073 4767 8334 -2444 -151 -817 N ATOM 2746 CA MET B 156 18.023 12.797 47.874 1.00 51.56 C ANISOU 2746 CA MET B 156 6636 4476 8478 -2405 -143 -764 C ATOM 2747 C MET B 156 16.503 12.699 47.988 1.00 49.41 C ANISOU 2747 C MET B 156 6487 4066 8221 -1881 -176 -845 C ATOM 2748 O MET B 156 15.962 11.620 48.149 1.00 46.54 O ANISOU 2748 O MET B 156 5783 3987 7911 -1623 -114 -814 O ATOM 2749 CB MET B 156 18.521 12.256 46.526 1.00 50.64 C ANISOU 2749 CB MET B 156 6354 4469 8417 -2527 -15 -557 C ATOM 2750 CG MET B 156 20.040 12.405 46.306 1.00 55.62 C ANISOU 2750 CG MET B 156 6799 5351 8985 -3066 40 -506 C ATOM 2751 SD MET B 156 20.731 11.087 45.278 1.00 56.69 S ANISOU 2751 SD MET B 156 6407 5956 9177 -3026 201 -340 S ATOM 2752 CE MET B 156 20.160 9.615 46.132 1.00 51.25 C ANISOU 2752 CE MET B 156 5350 5534 8588 -2503 174 -364 C ATOM 2753 N TYR B 157 15.835 13.844 47.926 1.00 51.59 N ANISOU 2753 N TYR B 157 7266 3921 8416 -1734 -285 -967 N ATOM 2754 CA TYR B 157 14.405 13.950 48.200 1.00 50.46 C ANISOU 2754 CA TYR B 157 7213 3730 8229 -1200 -346 -1126 C ATOM 2755 C TYR B 157 13.673 14.372 46.941 1.00 51.19 C ANISOU 2755 C TYR B 157 7625 3522 8303 -930 -382 -1059 C ATOM 2756 O TYR B 157 14.190 15.172 46.158 1.00 52.98 O ANISOU 2756 O TYR B 157 8291 3353 8486 -1156 -424 -954 O ATOM 2757 CB TYR B 157 14.159 15.028 49.261 1.00 53.59 C ANISOU 2757 CB TYR B 157 7975 3894 8492 -1106 -493 -1390 C ATOM 2758 CG TYR B 157 14.803 14.742 50.590 1.00 52.86 C ANISOU 2758 CG TYR B 157 7615 4099 8372 -1344 -488 -1489 C ATOM 2759 CD1 TYR B 157 16.047 15.278 50.910 1.00 55.34 C ANISOU 2759 CD1 TYR B 157 8066 4309 8652 -1853 -532 -1489 C ATOM 2760 CD2 TYR B 157 14.173 13.926 51.526 1.00 50.38 C ANISOU 2760 CD2 TYR B 157 6907 4208 8027 -1096 -441 -1583 C ATOM 2761 CE1 TYR B 157 16.648 15.017 52.136 1.00 55.70 C ANISOU 2761 CE1 TYR B 157 7847 4675 8643 -2045 -554 -1593 C ATOM 2762 CE2 TYR B 157 14.760 13.655 52.750 1.00 51.18 C ANISOU 2762 CE2 TYR B 157 6798 4583 8063 -1293 -453 -1657 C ATOM 2763 CZ TYR B 157 15.997 14.199 53.046 1.00 54.68 C ANISOU 2763 CZ TYR B 157 7364 4928 8484 -1734 -521 -1666 C ATOM 2764 OH TYR B 157 16.582 13.931 54.257 1.00 57.30 O ANISOU 2764 OH TYR B 157 7471 5576 8725 -1901 -558 -1751 O ATOM 2765 N THR B 158 12.469 13.849 46.744 1.00 49.03 N ANISOU 2765 N THR B 158 7144 3460 8027 -474 -369 -1121 N ATOM 2766 CA THR B 158 11.583 14.429 45.755 1.00 50.41 C ANISOU 2766 CA THR B 158 7649 3378 8125 -89 -465 -1135 C ATOM 2767 C THR B 158 10.932 15.671 46.349 1.00 54.98 C ANISOU 2767 C THR B 158 8709 3638 8542 288 -658 -1398 C ATOM 2768 O THR B 158 10.816 15.796 47.569 1.00 55.56 O ANISOU 2768 O THR B 158 8689 3853 8568 344 -682 -1609 O ATOM 2769 CB THR B 158 10.477 13.483 45.351 1.00 47.75 C ANISOU 2769 CB THR B 158 6885 3456 7802 265 -403 -1159 C ATOM 2770 OG1 THR B 158 9.822 13.007 46.528 1.00 46.84 O ANISOU 2770 OG1 THR B 158 6400 3752 7643 425 -369 -1364 O ATOM 2771 CG2 THR B 158 11.047 12.321 44.592 1.00 44.46 C ANISOU 2771 CG2 THR B 158 6122 3252 7519 -40 -241 -916 C ATOM 2772 N ASP B 159 10.496 16.566 45.472 1.00 58.16 N ANISOU 2772 N ASP B 159 9656 3610 8833 584 -806 -1390 N ATOM 2773 CA ASP B 159 9.739 17.738 45.872 1.00 63.48 C ANISOU 2773 CA ASP B 159 10862 3941 9318 1101 -1029 -1658 C ATOM 2774 C ASP B 159 8.422 17.719 45.106 1.00 64.79 C ANISOU 2774 C ASP B 159 10983 4261 9375 1790 -1132 -1747 C ATOM 2775 O ASP B 159 8.407 17.909 43.891 1.00 65.82 O ANISOU 2775 O ASP B 159 11409 4130 9470 1845 -1187 -1553 O ATOM 2776 CB ASP B 159 10.575 18.999 45.592 1.00 67.70 C ANISOU 2776 CB ASP B 159 12266 3700 9755 799 -1165 -1571 C ATOM 2777 CG ASP B 159 9.782 20.289 45.699 1.00 73.09 C ANISOU 2777 CG ASP B 159 13708 3856 10206 1415 -1444 -1813 C ATOM 2778 OD1 ASP B 159 10.415 21.348 45.533 1.00 78.01 O ANISOU 2778 OD1 ASP B 159 15152 3772 10715 1146 -1571 -1753 O ATOM 2779 OD2 ASP B 159 8.554 20.261 45.935 1.00 73.41 O ANISOU 2779 OD2 ASP B 159 13553 4188 10149 2153 -1541 -2073 O ATOM 2780 N TRP B 160 7.323 17.482 45.822 1.00 65.57 N ANISOU 2780 N TRP B 160 10679 4849 9387 2298 -1156 -2051 N ATOM 2781 CA TRP B 160 5.997 17.388 45.200 1.00 67.66 C ANISOU 2781 CA TRP B 160 10747 5448 9514 2968 -1253 -2199 C ATOM 2782 C TRP B 160 5.572 18.575 44.313 1.00 72.52 C ANISOU 2782 C TRP B 160 12123 5499 9931 3532 -1537 -2227 C ATOM 2783 O TRP B 160 4.813 18.396 43.348 1.00 72.80 O ANISOU 2783 O TRP B 160 12047 5733 9881 3933 -1612 -2206 O ATOM 2784 CB TRP B 160 4.905 17.109 46.240 1.00 69.31 C ANISOU 2784 CB TRP B 160 10412 6330 9594 3403 -1236 -2581 C ATOM 2785 CG TRP B 160 3.580 16.711 45.603 1.00 71.42 C ANISOU 2785 CG TRP B 160 10232 7183 9720 3952 -1280 -2736 C ATOM 2786 CD1 TRP B 160 2.342 17.229 45.873 1.00 77.55 C ANISOU 2786 CD1 TRP B 160 10902 8330 10234 4736 -1445 -3133 C ATOM 2787 CD2 TRP B 160 3.385 15.719 44.584 1.00 69.76 C ANISOU 2787 CD2 TRP B 160 9604 7304 9597 3754 -1166 -2529 C ATOM 2788 NE1 TRP B 160 1.388 16.616 45.089 1.00 78.03 N ANISOU 2788 NE1 TRP B 160 10455 8985 10207 5006 -1440 -3184 N ATOM 2789 CE2 TRP B 160 2.002 15.691 44.286 1.00 72.35 C ANISOU 2789 CE2 TRP B 160 9569 8217 9704 4393 -1273 -2813 C ATOM 2790 CE3 TRP B 160 4.246 14.849 43.894 1.00 63.57 C ANISOU 2790 CE3 TRP B 160 8710 6412 9033 3119 -991 -2160 C ATOM 2791 CZ2 TRP B 160 1.460 14.826 43.327 1.00 71.58 C ANISOU 2791 CZ2 TRP B 160 9018 8575 9604 4351 -1212 -2730 C ATOM 2792 CZ3 TRP B 160 3.706 13.994 42.936 1.00 63.31 C ANISOU 2792 CZ3 TRP B 160 8278 6776 9003 3120 -931 -2080 C ATOM 2793 CH2 TRP B 160 2.326 13.989 42.660 1.00 66.11 C ANISOU 2793 CH2 TRP B 160 8293 7687 9139 3700 -1042 -2359 C ATOM 2794 N LYS B 161 6.058 19.773 44.618 1.00 76.55 N ANISOU 2794 N LYS B 161 13448 5293 10344 3559 -1709 -2273 N ATOM 2795 CA LYS B 161 5.682 20.952 43.818 1.00 82.61 C ANISOU 2795 CA LYS B 161 15101 5408 10880 4112 -2010 -2283 C ATOM 2796 C LYS B 161 6.122 20.845 42.353 1.00 81.82 C ANISOU 2796 C LYS B 161 15288 4999 10802 3825 -1997 -1882 C ATOM 2797 O LYS B 161 5.489 21.427 41.460 1.00 85.01 O ANISOU 2797 O LYS B 161 16174 5130 10996 4401 -2228 -1867 O ATOM 2798 CB LYS B 161 6.184 22.257 44.467 1.00 87.83 C ANISOU 2798 CB LYS B 161 16701 5262 11407 4106 -2200 -2405 C ATOM 2799 CG LYS B 161 5.092 23.155 45.062 1.00 94.55 C ANISOU 2799 CG LYS B 161 17905 6034 11986 5097 -2488 -2858 C ATOM 2800 CD LYS B 161 3.938 22.383 45.722 1.00 94.06 C ANISOU 2800 CD LYS B 161 16837 7005 11896 5643 -2404 -3215 C ATOM 2801 CE LYS B 161 4.321 21.780 47.069 1.00 90.67 C ANISOU 2801 CE LYS B 161 15800 7041 11608 5158 -2165 -3351 C ATOM 2802 NZ LYS B 161 4.441 22.813 48.121 1.00 94.51 N ANISOU 2802 NZ LYS B 161 16880 7093 11938 5384 -2327 -3667 N ATOM 2803 N LYS B 162 7.174 20.054 42.120 1.00 77.26 N ANISOU 2803 N LYS B 162 14374 4532 10451 2983 -1730 -1577 N ATOM 2804 CA LYS B 162 7.792 19.905 40.802 1.00 76.58 C ANISOU 2804 CA LYS B 162 14516 4200 10380 2580 -1664 -1196 C ATOM 2805 C LYS B 162 7.025 18.966 39.872 1.00 74.21 C ANISOU 2805 C LYS B 162 13630 4470 10098 2874 -1610 -1138 C ATOM 2806 O LYS B 162 7.280 18.954 38.665 1.00 74.69 O ANISOU 2806 O LYS B 162 13943 4336 10099 2731 -1610 -866 O ATOM 2807 CB LYS B 162 9.223 19.374 40.937 1.00 72.93 C ANISOU 2807 CB LYS B 162 13831 3755 10124 1617 -1396 -947 C ATOM 2808 CG LYS B 162 10.042 19.949 42.076 1.00 74.49 C ANISOU 2808 CG LYS B 162 14295 3659 10350 1193 -1389 -1048 C ATOM 2809 CD LYS B 162 11.063 20.953 41.603 1.00 80.27 C ANISOU 2809 CD LYS B 162 15896 3652 10952 631 -1442 -830 C ATOM 2810 CE LYS B 162 12.158 21.106 42.635 1.00 80.42 C ANISOU 2810 CE LYS B 162 15878 3625 11051 -53 -1342 -884 C ATOM 2811 NZ LYS B 162 12.709 22.487 42.605 1.00 88.06 N ANISOU 2811 NZ LYS B 162 17912 3748 11799 -384 -1506 -851 N ATOM 2812 N ASP B 163 6.105 18.176 40.424 1.00 72.16 N ANISOU 2812 N ASP B 163 12597 4930 9890 3226 -1557 -1396 N ATOM 2813 CA ASP B 163 5.450 17.108 39.655 1.00 69.33 C ANISOU 2813 CA ASP B 163 11585 5194 9563 3341 -1466 -1362 C ATOM 2814 C ASP B 163 4.736 17.656 38.424 1.00 73.07 C ANISOU 2814 C ASP B 163 12467 5497 9798 3915 -1705 -1320 C ATOM 2815 O ASP B 163 4.092 18.706 38.497 1.00 78.10 O ANISOU 2815 O ASP B 163 13633 5840 10203 4589 -1989 -1502 O ATOM 2816 CB ASP B 163 4.457 16.334 40.520 1.00 67.83 C ANISOU 2816 CB ASP B 163 10587 5798 9388 3615 -1395 -1687 C ATOM 2817 CG ASP B 163 3.550 15.430 39.697 1.00 68.08 C ANISOU 2817 CG ASP B 163 10038 6461 9368 3817 -1365 -1723 C ATOM 2818 OD1 ASP B 163 4.060 14.473 39.069 1.00 66.58 O ANISOU 2818 OD1 ASP B 163 9573 6395 9330 3310 -1177 -1484 O ATOM 2819 OD2 ASP B 163 2.326 15.676 39.666 1.00 72.51 O ANISOU 2819 OD2 ASP B 163 10409 7425 9715 4493 -1538 -2015 O ATOM 2820 N LYS B 164 4.860 16.948 37.302 1.00 70.43 N ANISOU 2820 N LYS B 164 11920 5342 9497 3686 -1608 -1091 N ATOM 2821 CA LYS B 164 4.228 17.376 36.050 1.00 73.94 C ANISOU 2821 CA LYS B 164 12728 5671 9693 4194 -1833 -1021 C ATOM 2822 C LYS B 164 3.290 16.311 35.491 1.00 71.98 C ANISOU 2822 C LYS B 164 11699 6224 9427 4410 -1791 -1141 C ATOM 2823 O LYS B 164 2.818 16.417 34.360 1.00 74.08 O ANISOU 2823 O LYS B 164 12122 6525 9499 4745 -1944 -1068 O ATOM 2824 CB LYS B 164 5.294 17.742 35.009 1.00 74.36 C ANISOU 2824 CB LYS B 164 13443 5103 9709 3704 -1794 -609 C ATOM 2825 CG LYS B 164 6.113 18.983 35.347 1.00 77.51 C ANISOU 2825 CG LYS B 164 14778 4646 10025 3492 -1889 -484 C ATOM 2826 CD LYS B 164 5.340 20.290 35.149 1.00 83.45 C ANISOU 2826 CD LYS B 164 16395 4868 10443 4300 -2282 -594 C ATOM 2827 CE LYS B 164 6.108 21.435 35.773 1.00 86.78 C ANISOU 2827 CE LYS B 164 17718 4451 10802 4033 -2364 -544 C ATOM 2828 NZ LYS B 164 5.431 22.748 35.604 1.00 94.20 N ANISOU 2828 NZ LYS B 164 19662 4738 11392 4833 -2771 -645 N ATOM 2829 N CYS B 165 3.003 15.305 36.309 1.00 68.75 N ANISOU 2829 N CYS B 165 10484 6454 9185 4198 -1593 -1331 N ATOM 2830 CA CYS B 165 2.388 14.066 35.836 1.00 66.83 C ANISOU 2830 CA CYS B 165 9492 6934 8968 4095 -1472 -1398 C ATOM 2831 C CYS B 165 0.900 13.934 36.145 1.00 69.77 C ANISOU 2831 C CYS B 165 9307 8061 9140 4702 -1607 -1802 C ATOM 2832 O CYS B 165 0.193 13.184 35.470 1.00 69.56 O ANISOU 2832 O CYS B 165 8793 8609 9027 4750 -1601 -1883 O ATOM 2833 CB CYS B 165 3.150 12.854 36.380 1.00 61.04 C ANISOU 2833 CB CYS B 165 8278 6393 8520 3328 -1140 -1289 C ATOM 2834 SG CYS B 165 4.717 12.498 35.542 1.00 59.17 S ANISOU 2834 SG CYS B 165 8365 5652 8465 2623 -948 -855 S ATOM 2835 N GLU B 166 0.419 14.665 37.150 1.00 73.52 N ANISOU 2835 N GLU B 166 9835 8587 9514 5157 -1729 -2083 N ATOM 2836 CA GLU B 166 -1.004 14.606 37.512 1.00 77.41 C ANISOU 2836 CA GLU B 166 9735 9909 9769 5769 -1851 -2520 C ATOM 2837 C GLU B 166 -1.953 14.786 36.320 1.00 81.13 C ANISOU 2837 C GLU B 166 10149 10719 9957 6395 -2109 -2620 C ATOM 2838 O GLU B 166 -2.948 14.057 36.222 1.00 81.99 O ANISOU 2838 O GLU B 166 9487 11729 9935 6492 -2084 -2882 O ATOM 2839 CB GLU B 166 -1.348 15.573 38.643 1.00 81.45 C ANISOU 2839 CB GLU B 166 10436 10358 10154 6309 -1990 -2826 C ATOM 2840 CG GLU B 166 -0.942 15.082 40.038 1.00 80.04 C ANISOU 2840 CG GLU B 166 9908 10342 10162 5775 -1721 -2899 C ATOM 2841 CD GLU B 166 -1.393 16.035 41.151 1.00 86.52 C ANISOU 2841 CD GLU B 166 10873 11191 10809 6368 -1866 -3263 C ATOM 2842 OE1 GLU B 166 -2.120 17.003 40.855 1.00 92.73 O ANISOU 2842 OE1 GLU B 166 11969 11942 11322 7249 -2179 -3497 O ATOM 2843 OE2 GLU B 166 -1.024 15.819 42.326 1.00 86.23 O ANISOU 2843 OE2 GLU B 166 10664 11215 10884 5994 -1681 -3327 O ATOM 2844 N PRO B 167 -1.645 15.733 35.401 1.00 83.88 N ANISOU 2844 N PRO B 167 11319 10371 10181 6776 -2359 -2408 N ATOM 2845 CA PRO B 167 -2.531 15.880 34.240 1.00 87.66 C ANISOU 2845 CA PRO B 167 11761 11186 10359 7398 -2629 -2488 C ATOM 2846 C PRO B 167 -2.552 14.622 33.363 1.00 83.87 C ANISOU 2846 C PRO B 167 10719 11188 9961 6838 -2441 -2356 C ATOM 2847 O PRO B 167 -3.631 14.173 32.968 1.00 85.56 O ANISOU 2847 O PRO B 167 10311 12234 9966 7159 -2540 -2626 O ATOM 2848 CB PRO B 167 -1.929 17.075 33.485 1.00 90.74 C ANISOU 2848 CB PRO B 167 13291 10567 10619 7716 -2882 -2185 C ATOM 2849 CG PRO B 167 -1.178 17.834 34.526 1.00 91.04 C ANISOU 2849 CG PRO B 167 13896 9904 10792 7572 -2841 -2146 C ATOM 2850 CD PRO B 167 -0.580 16.754 35.385 1.00 84.43 C ANISOU 2850 CD PRO B 167 12401 9369 10311 6684 -2434 -2115 C ATOM 2851 N LEU B 168 -1.381 14.042 33.091 1.00 78.69 N ANISOU 2851 N LEU B 168 10251 10063 9585 6013 -2176 -1982 N ATOM 2852 CA LEU B 168 -1.325 12.787 32.325 1.00 75.70 C ANISOU 2852 CA LEU B 168 9385 10086 9292 5463 -1984 -1878 C ATOM 2853 C LEU B 168 -2.023 11.624 33.050 1.00 74.15 C ANISOU 2853 C LEU B 168 8255 10759 9158 5140 -1785 -2174 C ATOM 2854 O LEU B 168 -2.691 10.809 32.411 1.00 75.13 O ANISOU 2854 O LEU B 168 7870 11505 9170 5045 -1775 -2297 O ATOM 2855 CB LEU B 168 0.114 12.422 31.928 1.00 70.69 C ANISOU 2855 CB LEU B 168 9140 8802 8916 4714 -1744 -1454 C ATOM 2856 CG LEU B 168 0.318 11.208 31.004 1.00 67.75 C ANISOU 2856 CG LEU B 168 8425 8705 8610 4203 -1567 -1329 C ATOM 2857 CD1 LEU B 168 -0.583 11.250 29.761 1.00 70.91 C ANISOU 2857 CD1 LEU B 168 8758 9485 8699 4667 -1804 -1415 C ATOM 2858 CD2 LEU B 168 1.785 11.066 30.600 1.00 62.15 C ANISOU 2858 CD2 LEU B 168 8156 7360 8099 3606 -1362 -940 C ATOM 2859 N GLU B 169 -1.884 11.567 34.373 1.00 72.77 N ANISOU 2859 N GLU B 169 7893 10630 9127 4943 -1634 -2292 N ATOM 2860 CA GLU B 169 -2.582 10.575 35.197 1.00 72.50 C ANISOU 2860 CA GLU B 169 7049 11405 9092 4622 -1446 -2570 C ATOM 2861 C GLU B 169 -4.126 10.702 35.115 1.00 78.56 C ANISOU 2861 C GLU B 169 7216 13132 9501 5231 -1643 -3018 C ATOM 2862 O GLU B 169 -4.834 9.690 34.993 1.00 78.80 O ANISOU 2862 O GLU B 169 6566 13938 9437 4893 -1530 -3200 O ATOM 2863 CB GLU B 169 -2.087 10.675 36.639 1.00 70.42 C ANISOU 2863 CB GLU B 169 6809 10947 9000 4367 -1277 -2589 C ATOM 2864 CG GLU B 169 -2.762 9.752 37.638 1.00 71.12 C ANISOU 2864 CG GLU B 169 6155 11821 9046 4007 -1072 -2853 C ATOM 2865 CD GLU B 169 -2.786 10.350 39.041 1.00 73.69 C ANISOU 2865 CD GLU B 169 6481 12162 9356 4188 -1046 -3033 C ATOM 2866 OE1 GLU B 169 -3.108 11.549 39.183 1.00 80.32 O ANISOU 2866 OE1 GLU B 169 7602 12876 10040 4928 -1285 -3209 O ATOM 2867 OE2 GLU B 169 -2.489 9.629 40.013 1.00 71.31 O ANISOU 2867 OE2 GLU B 169 5943 11981 9172 3617 -799 -3006 O ATOM 2868 N LYS B 170 -4.634 11.937 35.165 1.00 83.64 N ANISOU 2868 N LYS B 170 8129 13734 9916 6123 -1946 -3208 N ATOM 2869 CA LYS B 170 -6.064 12.200 34.989 1.00 90.58 C ANISOU 2869 CA LYS B 170 8461 15548 10407 6864 -2189 -3656 C ATOM 2870 C LYS B 170 -6.546 11.705 33.622 1.00 92.15 C ANISOU 2870 C LYS B 170 8434 16140 10439 6895 -2310 -3639 C ATOM 2871 O LYS B 170 -7.554 10.999 33.531 1.00 94.34 O ANISOU 2871 O LYS B 170 7895 17441 10511 6821 -2288 -3962 O ATOM 2872 CB LYS B 170 -6.337 13.636 35.100 0.00122.73 C ANISOU 2872 CB LYS B 170 13056 19310 14265 7881 -2534 -3802 C ATOM 2873 CG LYS B 170 -7.727 14.095 34.652 0.00131.84 C ANISOU 2873 CG LYS B 170 13792 21333 14967 8870 -2881 -4240 C ATOM 2874 CD LYS B 170 -8.849 13.758 35.651 0.00136.03 C ANISOU 2874 CD LYS B 170 13322 23083 15281 9023 -2799 -4784 C ATOM 2875 CE LYS B 170 -9.100 14.883 36.655 0.00141.09 C ANISOU 2875 CE LYS B 170 14205 23632 15772 9840 -2966 -5081 C ATOM 2876 NZ LYS B 170 -8.023 14.958 37.685 0.00135.50 N ANISOU 2876 NZ LYS B 170 13960 22115 15410 9256 -2709 -4839 N ATOM 2877 N GLN B 171 -5.803 12.064 32.574 1.00 91.19 N ANISOU 2877 N GLN B 171 9034 15230 10383 6941 -2424 -3266 N ATOM 2878 CA GLN B 171 -6.125 11.695 31.190 1.00 92.77 C ANISOU 2878 CA GLN B 171 9158 15679 10413 6996 -2558 -3203 C ATOM 2879 C GLN B 171 -6.096 10.188 30.914 1.00 89.43 C ANISOU 2879 C GLN B 171 8147 15709 10122 6083 -2265 -3180 C ATOM 2880 O GLN B 171 -6.674 9.730 29.928 1.00 91.43 O ANISOU 2880 O GLN B 171 8098 16468 10173 6114 -2372 -3274 O ATOM 2881 CB GLN B 171 -5.170 12.252 30.223 0.00119.58 C ANISOU 2881 CB GLN B 171 13458 18109 13867 7036 -2656 -2764 C ATOM 2882 CG GLN B 171 -5.522 11.957 28.774 0.00121.88 C ANISOU 2882 CG GLN B 171 13716 18662 13931 7162 -2820 -2706 C ATOM 2883 CD GLN B 171 -6.770 12.688 28.318 0.00130.36 C ANISOU 2883 CD GLN B 171 14637 20344 14551 8211 -3250 -3035 C ATOM 2884 OE1 GLN B 171 -7.011 13.831 28.706 0.00135.44 O ANISOU 2884 OE1 GLN B 171 15697 20732 15034 9012 -3511 -3133 O ATOM 2885 NE2 GLN B 171 -7.572 12.029 27.488 0.00132.56 N ANISOU 2885 NE2 GLN B 171 14331 21442 14595 8238 -3344 -3231 N ATOM 2886 N HIS B 172 -5.420 9.426 31.777 1.00 84.96 N ANISOU 2886 N HIS B 172 7473 14937 9871 5290 -1917 -3060 N ATOM 2887 CA HIS B 172 -5.396 7.961 31.673 1.00 82.20 C ANISOU 2887 CA HIS B 172 6654 14946 9633 4418 -1642 -3054 C ATOM 2888 C HIS B 172 -6.670 7.288 32.186 1.00 86.17 C ANISOU 2888 C HIS B 172 6252 16588 9899 4272 -1593 -3501 C ATOM 2889 O HIS B 172 -7.300 6.542 31.442 1.00 88.00 O ANISOU 2889 O HIS B 172 6062 17417 9956 4035 -1613 -3651 O ATOM 2890 CB HIS B 172 -4.165 7.365 32.349 1.00 75.85 C ANISOU 2890 CB HIS B 172 6142 13465 9211 3671 -1320 -2744 C ATOM 2891 CG HIS B 172 -2.973 7.271 31.448 1.00 71.94 C ANISOU 2891 CG HIS B 172 6253 12170 8912 3419 -1265 -2337 C ATOM 2892 ND1 HIS B 172 -1.681 7.406 31.905 1.00 65.72 N ANISOU 2892 ND1 HIS B 172 5947 10605 8418 3110 -1101 -2024 N ATOM 2893 CD2 HIS B 172 -2.881 7.069 30.112 1.00 71.49 C ANISOU 2893 CD2 HIS B 172 6361 12041 8761 3434 -1352 -2216 C ATOM 2894 CE1 HIS B 172 -0.844 7.292 30.891 1.00 64.18 C ANISOU 2894 CE1 HIS B 172 6159 9931 8297 2940 -1074 -1736 C ATOM 2895 NE2 HIS B 172 -1.547 7.084 29.792 1.00 67.12 N ANISOU 2895 NE2 HIS B 172 6369 10695 8437 3131 -1220 -1839 N ATOM 2896 N GLU B 173 -7.036 7.540 33.447 1.00 88.15 N ANISOU 2896 N GLU B 173 6203 17170 10119 4361 -1518 -3723 N ATOM 2897 CA GLU B 173 -8.315 7.057 33.998 1.00 93.23 C ANISOU 2897 CA GLU B 173 5944 19015 10464 4263 -1472 -4187 C ATOM 2898 C GLU B 173 -9.450 7.354 33.016 1.00 99.43 C ANISOU 2898 C GLU B 173 6295 20630 10855 4891 -1783 -4514 C ATOM 2899 O GLU B 173 -9.893 8.494 32.913 1.00103.97 O ANISOU 2899 O GLU B 173 6959 21324 11219 5876 -2091 -4688 O ATOM 2900 CB GLU B 173 -8.614 7.694 35.371 1.00 95.29 C ANISOU 2900 CB GLU B 173 6009 19536 10659 4590 -1435 -4421 C ATOM 2901 CG GLU B 173 -9.914 7.184 36.037 1.00100.58 C ANISOU 2901 CG GLU B 173 5687 21550 10980 4414 -1339 -4918 C ATOM 2902 CD GLU B 173 -10.633 8.235 36.897 1.00106.64 C ANISOU 2902 CD GLU B 173 6159 22874 11486 5269 -1489 -5316 C ATOM 2903 OE1 GLU B 173 -9.961 9.039 37.581 1.00104.68 O ANISOU 2903 OE1 GLU B 173 6464 21894 11417 5616 -1509 -5178 O ATOM 2904 OE2 GLU B 173 -11.888 8.248 36.904 1.00113.14 O ANISOU 2904 OE2 GLU B 173 6168 24923 11898 5595 -1588 -5802 O TER 2905 GLU B 173 HETATM 2906 O1 PG4 A 190 16.862 -0.706 18.072 1.00 43.00 O HETATM 2907 C1 PG4 A 190 15.933 -1.081 17.031 1.00 40.73 C HETATM 2908 C2 PG4 A 190 15.016 -2.253 17.391 1.00 39.46 C HETATM 2909 O2 PG4 A 190 14.200 -2.041 18.542 1.00 41.67 O HETATM 2910 C3 PG4 A 190 12.835 -2.517 18.394 1.00 40.60 C HETATM 2911 C4 PG4 A 190 11.844 -1.757 19.286 1.00 40.16 C HETATM 2912 O3 PG4 A 190 11.067 -0.821 18.508 1.00 42.66 O HETATM 2913 C5 PG4 A 190 10.707 0.383 19.179 1.00 40.42 C HETATM 2914 C6 PG4 A 190 9.794 1.224 18.288 1.00 41.36 C HETATM 2915 O4 PG4 A 190 10.463 2.232 17.513 1.00 41.71 O HETATM 2916 C7 PG4 A 190 10.831 3.385 18.278 1.00 41.59 C HETATM 2917 C8 PG4 A 190 11.778 4.269 17.468 1.00 42.79 C HETATM 2918 O5 PG4 A 190 12.759 4.930 18.304 1.00 46.17 O HETATM 2919 O1 PG4 B 190 12.266 -1.876 42.085 1.00 47.76 O HETATM 2920 C1 PG4 B 190 11.275 -1.268 42.926 1.00 46.00 C HETATM 2921 C2 PG4 B 190 10.295 -0.485 42.054 1.00 45.38 C HETATM 2922 O2 PG4 B 190 9.994 0.763 42.671 1.00 45.96 O HETATM 2923 C3 PG4 B 190 9.221 1.612 41.826 1.00 46.13 C HETATM 2924 C4 PG4 B 190 10.054 2.640 41.071 1.00 46.72 C HETATM 2925 O3 PG4 B 190 10.050 3.927 41.692 1.00 48.52 O HETATM 2926 C5 PG4 B 190 11.020 4.801 41.086 1.00 45.71 C HETATM 2927 C6 PG4 B 190 11.806 5.476 42.200 1.00 45.17 C HETATM 2928 O4 PG4 B 190 13.185 5.115 42.142 1.00 42.99 O HETATM 2929 C7 PG4 B 190 13.833 5.329 43.384 1.00 41.93 C HETATM 2930 C8 PG4 B 190 14.907 4.269 43.564 1.00 42.24 C HETATM 2931 O5 PG4 B 190 15.649 4.188 42.341 1.00 45.32 O HETATM 2932 O HOH A 191 -0.155 0.647 29.754 1.00 3.18 O HETATM 2933 O HOH A 192 4.336 2.541 5.839 1.00 2.17 O HETATM 2934 O HOH A 193 12.642 11.321 8.576 1.00 2.00 O HETATM 2935 O HOH A 194 17.020 2.592 14.152 1.00 14.37 O HETATM 2936 O HOH A 195 19.334 9.781 12.961 1.00 8.43 O HETATM 2937 O HOH A 196 6.805 -8.269 30.986 1.00 5.05 O HETATM 2938 O HOH A 197 -1.724 15.306 6.786 1.00 2.00 O HETATM 2939 O HOH A 198 7.287 2.464 3.869 1.00 14.71 O HETATM 2940 O HOH A 199 12.131 7.792 3.307 1.00 12.07 O HETATM 2941 O HOH A 200 8.947 10.859 8.415 1.00 6.06 O HETATM 2942 O HOH A 201 9.768 -4.358 26.032 1.00 6.43 O HETATM 2943 O HOH A 202 18.022 6.035 17.312 1.00 11.41 O HETATM 2944 O HOH A 203 29.550 -8.629 7.455 1.00 11.97 O HETATM 2945 O HOH A 204 14.879 1.239 -0.284 1.00 2.00 O HETATM 2946 O HOH A 205 20.434 -12.584 12.908 1.00 5.94 O HETATM 2947 O HOH A 206 6.912 11.726 6.791 1.00 7.52 O HETATM 2948 O HOH A 207 13.454 10.196 2.240 1.00 10.06 O HETATM 2949 O HOH A 208 18.037 -13.186 23.976 1.00 4.09 O HETATM 2950 O HOH A 209 8.259 -10.576 21.095 1.00 2.00 O HETATM 2951 O HOH A 210 14.835 15.672 15.946 1.00 5.28 O HETATM 2952 O HOH A 211 5.553 15.037 5.001 1.00 10.45 O HETATM 2953 O HOH A 212 12.635 -4.918 -3.710 1.00 3.87 O HETATM 2954 O HOH A 213 9.899 -11.702 13.925 1.00 12.32 O HETATM 2955 O HOH A 214 10.219 7.363 25.795 1.00 18.17 O HETATM 2956 O HOH A 215 13.275 -11.402 10.646 1.00 3.08 O HETATM 2957 O HOH A 216 9.616 -9.795 15.784 1.00 11.30 O HETATM 2958 O HOH A 217 26.160 -6.219 0.697 1.00 2.90 O HETATM 2959 O HOH A 218 29.021 -0.953 8.006 1.00 5.48 O HETATM 2960 O HOH A 219 19.792 9.237 15.618 1.00 17.13 O HETATM 2961 O HOH A 220 10.326 -14.735 11.324 1.00 2.75 O HETATM 2962 O HOH A 221 4.953 18.579 9.512 1.00 13.05 O HETATM 2963 O HOH A 222 18.877 2.687 -6.663 1.00 18.24 O HETATM 2964 O HOH A 223 12.307 11.018 -2.180 1.00 3.30 O HETATM 2965 O HOH A 224 12.397 1.340 -1.465 1.00 10.46 O HETATM 2966 O HOH A 225 -0.190 7.893 3.702 1.00 27.88 O HETATM 2967 O HOH A 226 6.336 5.071 0.636 1.00 13.48 O HETATM 2968 O HOH A 227 17.825 -7.726 16.305 1.00 11.54 O HETATM 2969 O HOH A 228 30.601 2.047 17.856 1.00 9.40 O HETATM 2970 O HOH A 229 18.159 0.666 20.007 1.00 50.66 O HETATM 2971 O HOH A 230 6.683 18.474 16.460 1.00 5.92 O HETATM 2972 O HOH A 231 -0.016 18.732 17.335 1.00 10.50 O HETATM 2973 O HOH A 232 0.100 19.857 14.221 1.00 25.54 O HETATM 2974 O HOH A 233 19.266 3.537 28.365 1.00 33.10 O HETATM 2975 O HOH A 234 19.931 9.684 19.607 1.00 18.58 O HETATM 2976 O HOH A 235 5.986 -7.417 -1.040 1.00 8.55 O HETATM 2977 O HOH A 236 0.042 17.429 9.771 1.00 3.04 O HETATM 2978 O HOH A 237 0.621 -2.067 10.717 1.00 24.45 O HETATM 2979 O HOH A 238 14.670 2.846 16.298 1.00 38.58 O HETATM 2980 O HOH A 239 -2.130 8.525 22.719 1.00 24.07 O HETATM 2981 O HOH A 240 11.196 18.884 14.381 1.00 23.28 O HETATM 2982 O HOH A 241 16.123 9.451 29.851 1.00 27.99 O HETATM 2983 O HOH A 242 8.241 -13.100 -1.529 1.00 2.00 O HETATM 2984 O HOH A 243 8.159 -5.739 31.683 1.00 2.73 O HETATM 2985 O HOH A 244 8.451 9.600 2.033 1.00 12.36 O HETATM 2986 O HOH A 245 15.516 4.870 -3.529 1.00 13.77 O HETATM 2987 O HOH A 246 13.670 -8.839 -3.778 1.00 3.47 O HETATM 2988 O HOH A 247 2.101 8.796 4.064 1.00 17.83 O HETATM 2989 O HOH A 248 12.108 11.801 0.545 1.00 12.28 O HETATM 2990 O HOH A 249 9.461 11.982 1.011 1.00 7.60 O HETATM 2991 O HOH B 191 6.053 12.703 38.935 1.00 5.85 O HETATM 2992 O HOH B 192 16.117 0.879 46.204 1.00 21.34 O HETATM 2993 O HOH B 193 5.745 -0.291 56.300 1.00 21.45 O HETATM 2994 O HOH B 194 8.934 6.850 34.078 1.00 18.58 O HETATM 2995 O HOH B 195 7.565 0.807 34.438 1.00 24.97 O HETATM 2996 O HOH B 196 3.040 -0.579 53.932 1.00 16.41 O HETATM 2997 O HOH B 197 15.332 16.759 36.502 1.00 13.43 O HETATM 2998 O HOH B 198 2.159 -10.982 34.326 1.00 24.42 O HETATM 2999 O HOH B 199 11.873 -5.474 56.865 1.00 28.64 O HETATM 3000 O HOH B 200 -4.733 -10.879 51.600 1.00 36.40 O HETATM 3001 O HOH B 201 -3.962 0.191 50.165 1.00 26.35 O HETATM 3002 O HOH B 202 15.990 11.099 44.201 1.00 16.24 O HETATM 3003 O HOH B 203 -2.827 0.458 37.706 1.00 27.54 O HETATM 3004 O HOH B 204 20.602 -4.488 41.811 1.00 35.33 O HETATM 3005 O HOH B 205 23.887 13.580 58.504 1.00 15.19 O HETATM 3006 O HOH B 206 1.656 18.729 41.834 1.00 8.29 O HETATM 3007 O HOH B 207 6.989 7.759 28.455 1.00 15.23 O HETATM 3008 O HOH B 208 5.256 10.382 29.283 1.00 17.94 O HETATM 3009 O HOH B 209 12.361 -8.387 51.601 1.00 16.78 O HETATM 3010 O HOH B 210 -1.170 3.314 49.002 1.00 22.38 O HETATM 3011 O HOH B 211 23.226 8.783 48.809 1.00 26.28 O HETATM 3012 O HOH B 212 19.940 15.544 52.138 1.00 16.50 O HETATM 3013 O HOH B 213 17.638 0.943 70.691 1.00 39.17 O HETATM 3014 O HOH B 214 19.947 -7.784 55.137 1.00 14.69 O CONECT 38 1221 CONECT 600 1377 CONECT 1221 38 CONECT 1377 600 CONECT 1495 2678 CONECT 2057 2834 CONECT 2678 1495 CONECT 2834 2057 CONECT 2906 2907 CONECT 2907 2906 2908 CONECT 2908 2907 2909 CONECT 2909 2908 2910 CONECT 2910 2909 2911 CONECT 2911 2910 2912 CONECT 2912 2911 2913 CONECT 2913 2912 2914 CONECT 2914 2913 2915 CONECT 2915 2914 2916 CONECT 2916 2915 2917 CONECT 2917 2916 2918 CONECT 2918 2917 CONECT 2919 2920 CONECT 2920 2919 2921 CONECT 2921 2920 2922 CONECT 2922 2921 2923 CONECT 2923 2922 2924 CONECT 2924 2923 2925 CONECT 2925 2924 2926 CONECT 2926 2925 2927 CONECT 2927 2926 2928 CONECT 2928 2927 2929 CONECT 2929 2928 2930 CONECT 2930 2929 2931 CONECT 2931 2930 MASTER 358 0 2 14 40 0 4 6 3012 2 34 30 END If you find results from this site helpful for your research, please cite one of our papers:
elNémo
is maintained by Yves-Henri Sanejouand. |