Browse entries in the PDBbind-CN Database
HEADER TRANSFERASE,TRANSCRIPTION 08-APR-11 3RGF TITLE CRYSTAL STRUCTURE OF HUMAN CDK8/CYCC COMPND MOL_ID: 1; COMPND 2 MOLECULE: CYCLIN-DEPENDENT KINASE 8; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: UNP RESIDUES 1-403; COMPND 5 SYNONYM: CDK8, CELL DIVISION PROTEIN KINASE 8, MEDIATOR COMPLEX COMPND 6 SUBUNIT CDK8, MEDIATOR OF RNA POLYMERASE II TRANSCRIPTION SUBUNIT COMPND 7 CDK8, PROTEIN KINASE K35; COMPND 8 EC: 2.7.11.22, 2.7.11.23; COMPND 9 ENGINEERED: YES; COMPND 10 MOL_ID: 2; COMPND 11 MOLECULE: CYCLIN-C; COMPND 12 CHAIN: B; COMPND 13 SYNONYM: CYCC, SRB11 HOMOLOG, HSRB11; COMPND 14 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606; SOURCE 5 GENE: CDK8; SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM; SOURCE 8 EXPRESSION_SYSTEM_TAXID: 7108; SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS; SOURCE 10 MOL_ID: 2; SOURCE 11 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 12 ORGANISM_COMMON: HUMAN; SOURCE 13 ORGANISM_TAXID: 9606; SOURCE 14 GENE: CCNC; SOURCE 15 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 16 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM; SOURCE 17 EXPRESSION_SYSTEM_TAXID: 7108; SOURCE 18 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS KEYWDS PROTEIN KINASE COMPLEX, TRANSFERASE,TRANSCRIPTION EXPDTA X-RAY DIFFRACTION AUTHOR E.V.SCHNEIDER,J.BOETTCHER,M.BLAESSE,R.HUBER,K.MASKOS REVDAT 3 03-OCT-12 3RGF 1 HETSYN REVDAT 2 07-SEP-11 3RGF 1 JRNL REVDAT 1 10-AUG-11 3RGF 0 JRNL AUTH E.V.SCHNEIDER,J.BOTTCHER,M.BLAESSE,L.NEUMANN,R.HUBER, JRNL AUTH 2 K.MASKOS JRNL TITL THE STRUCTURE OF CDK8/CYCC IMPLICATES SPECIFICITY IN THE JRNL TITL 2 CDK/CYCLIN FAMILY AND REVEALS INTERACTION WITH A DEEP POCKET JRNL TITL 3 BINDER. JRNL REF J.MOL.BIOL. V. 412 251 2011 JRNL REFN ISSN 0022-2836 JRNL PMID 21806996 JRNL DOI 10.1016/J.JMB.2011.07.020 REMARK 2 REMARK 2 RESOLUTION. 2.20 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC 5.5.0109 REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON REMARK 3 REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 37.57 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000 REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9 REMARK 3 NUMBER OF REFLECTIONS : 37691 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) : 0.183 REMARK 3 R VALUE (WORKING SET) : 0.180 REMARK 3 FREE R VALUE : 0.221 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000 REMARK 3 FREE R VALUE TEST SET COUNT : 1885 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) : 2.20 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.26 REMARK 3 REFLECTION IN BIN (WORKING SET) : 2630 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.82 REMARK 3 BIN R VALUE (WORKING SET) : 0.2200 REMARK 3 BIN FREE R VALUE SET COUNT : 139 REMARK 3 BIN FREE R VALUE : 0.2730 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 4869 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 82 REMARK 3 SOLVENT ATOMS : 175 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 44.54 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : -0.51000 REMARK 3 B22 (A**2) : 0.86000 REMARK 3 B33 (A**2) : -0.25000 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : 0.17000 REMARK 3 B23 (A**2) : 0.00000 REMARK 3 REMARK 3 ESTIMATED OVERALL COORDINATE ERROR. REMARK 3 ESU BASED ON R VALUE (A): 0.228 REMARK 3 ESU BASED ON FREE R VALUE (A): 0.185 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.128 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 10.809 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.950 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.922 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4947 ; 0.007 ; 0.022 REMARK 3 BOND LENGTHS OTHERS (A): 3467 ; 0.001 ; 0.020 REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 6680 ; 1.004 ; 1.971 REMARK 3 BOND ANGLES OTHERS (DEGREES): 8347 ; 0.802 ; 3.000 REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 583 ; 5.018 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 219 ;32.679 ;23.333 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 841 ;12.431 ;15.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 28 ;14.940 ;15.000 REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 722 ; 0.061 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5364 ; 0.004 ; 0.021 REMARK 3 GENERAL PLANES OTHERS (A): 1041 ; 0.001 ; 0.020 REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL REMARK 3 REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 2938 ; 1.346 ; 2.000 REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1162 ; 0.333 ; 2.000 REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 4733 ; 2.394 ; 3.000 REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2009 ; 3.490 ; 4.000 REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1947 ; 5.325 ; 6.000 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 : 3 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 100 REMARK 3 ORIGIN FOR THE GROUP (A): -17.210 7.099 26.642 REMARK 3 T TENSOR REMARK 3 T11: 0.1582 T22: 0.2225 REMARK 3 T33: 0.1845 T12: -0.0456 REMARK 3 T13: 0.0378 T23: -0.0311 REMARK 3 L TENSOR REMARK 3 L11: 4.8364 L22: 1.6029 REMARK 3 L33: 0.3951 L12: -2.6601 REMARK 3 L13: 0.4294 L23: -0.4455 REMARK 3 S TENSOR REMARK 3 S11: -0.1947 S12: -0.3444 S13: 0.0227 REMARK 3 S21: 0.2502 S22: 0.1743 S23: 0.0353 REMARK 3 S31: -0.2253 S32: -0.0271 S33: 0.0204 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 : A 101 A 353 REMARK 3 ORIGIN FOR THE GROUP (A): 14.1990 -2.2990 26.7250 REMARK 3 T TENSOR REMARK 3 T11: 0.0403 T22: 0.0338 REMARK 3 T33: 0.0122 T12: -0.0101 REMARK 3 T13: -0.0037 T23: -0.0045 REMARK 3 L TENSOR REMARK 3 L11: 2.8577 L22: 1.7789 REMARK 3 L33: 1.3817 L12: 0.5886 REMARK 3 L13: 0.0779 L23: 0.1009 REMARK 3 S TENSOR REMARK 3 S11: 0.0779 S12: -0.2217 S13: 0.0753 REMARK 3 S21: 0.1610 S22: -0.0182 S23: -0.0905 REMARK 3 S31: -0.0597 S32: 0.0114 S33: -0.0597 REMARK 3 REMARK 3 TLS GROUP : 3 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : B 1 B 264 REMARK 3 ORIGIN FOR THE GROUP (A): -16.3570 12.2750 -2.5060 REMARK 3 T TENSOR REMARK 3 T11: 0.0228 T22: 0.0105 REMARK 3 T33: 0.0430 T12: -0.0071 REMARK 3 T13: -0.0091 T23: 0.0023 REMARK 3 L TENSOR REMARK 3 L11: 1.2113 L22: 1.6065 REMARK 3 L33: 2.6088 L12: -0.2621 REMARK 3 L13: -0.0199 L23: -0.1257 REMARK 3 S TENSOR REMARK 3 S11: 0.0900 S12: -0.0038 S13: -0.0724 REMARK 3 S21: -0.0790 S22: -0.0148 S23: 0.0735 REMARK 3 S31: 0.0987 S32: 0.0550 S33: -0.0752 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : BABINET MODEL WITH 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: REMARK 3 HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS REMARK 3 U VALUES : RESIDUAL ONLY REMARK 4 REMARK 4 3RGF COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-APR-11. REMARK 100 THE RCSB ID CODE IS RCSB064899. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 10-MAY-10 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : NULL REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : SLS REMARK 200 BEAMLINE : X06SA REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.000 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : PSI PILATUS 6M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM REMARK 200 DATA SCALING SOFTWARE : SCALA REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 37725 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200 REMARK 200 RESOLUTION RANGE LOW (A) : 37.567 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0 REMARK 200 DATA REDUNDANCY : 4.600 REMARK 200 R MERGE (I) : 0.08900 REMARK 200 R SYM (I) : 0.08900 REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 10.7000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.32 REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9 REMARK 200 DATA REDUNDANCY IN SHELL : 4.60 REMARK 200 R MERGE FOR SHELL (I) : 0.54200 REMARK 200 R SYM FOR SHELL (I) : 0.54200 REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.600 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: BALBES REMARK 200 STARTING MODEL: PDB ENTRIES 1ZP2, 2I53, 2PK2, 2WH2, 2PK2, 2RK3, REMARK 200 2UZE, 2R3Q, 2R3N, 2VTH REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 42.87 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.15 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG3350, 0.2M LITHIUM CHLORIDE, REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,Y+1/2,-Z REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 35.30500 REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 6950 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 28010 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 3.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 GLY A 28 REMARK 465 ARG A 29 REMARK 465 GLY A 30 REMARK 465 THR A 31 REMARK 465 TYR A 32 REMARK 465 ALA A 116 REMARK 465 ASN A 117 REMARK 465 LYS A 118 REMARK 465 LYS A 119 REMARK 465 PRO A 120 REMARK 465 VAL A 121 REMARK 465 GLN A 122 REMARK 465 LEU A 179 REMARK 465 PHE A 180 REMARK 465 ASN A 181 REMARK 465 SER A 182 REMARK 465 PRO A 183 REMARK 465 LEU A 184 REMARK 465 LYS A 185 REMARK 465 PRO A 186 REMARK 465 LEU A 187 REMARK 465 ALA A 188 REMARK 465 ASP A 189 REMARK 465 LEU A 190 REMARK 465 ASP A 191 REMARK 465 PRO A 192 REMARK 465 VAL A 193 REMARK 465 VAL A 194 REMARK 465 GLU A 239 REMARK 465 ASP A 240 REMARK 465 ILE A 241 REMARK 465 LYS A 242 REMARK 465 THR A 243 REMARK 465 SER A 244 REMARK 465 PRO A 354 REMARK 465 LYS A 355 REMARK 465 ARG A 356 REMARK 465 GLU A 357 REMARK 465 PHE A 358 REMARK 465 LEU A 359 REMARK 465 THR A 360 REMARK 465 GLU A 361 REMARK 465 GLU A 362 REMARK 465 GLU A 363 REMARK 465 PRO A 364 REMARK 465 ASP A 365 REMARK 465 ASP A 366 REMARK 465 LYS A 367 REMARK 465 GLY A 368 REMARK 465 ASP A 369 REMARK 465 LYS A 370 REMARK 465 LYS A 371 REMARK 465 ASN A 372 REMARK 465 GLN A 373 REMARK 465 GLN A 374 REMARK 465 GLN A 375 REMARK 465 GLN A 376 REMARK 465 GLN A 377 REMARK 465 GLY A 378 REMARK 465 ASN A 379 REMARK 465 ASN A 380 REMARK 465 HIS A 381 REMARK 465 THR A 382 REMARK 465 ASN A 383 REMARK 465 GLY A 384 REMARK 465 THR A 385 REMARK 465 GLY A 386 REMARK 465 HIS A 387 REMARK 465 PRO A 388 REMARK 465 GLY A 389 REMARK 465 ASN A 390 REMARK 465 GLN A 391 REMARK 465 ASP A 392 REMARK 465 SER A 393 REMARK 465 SER A 394 REMARK 465 HIS A 395 REMARK 465 THR A 396 REMARK 465 GLN A 397 REMARK 465 GLY A 398 REMARK 465 PRO A 399 REMARK 465 PRO A 400 REMARK 465 LEU A 401 REMARK 465 LYS A 402 REMARK 465 LYS A 403 REMARK 465 ASN B 265 REMARK 465 SER B 266 REMARK 465 GLU B 267 REMARK 465 GLY B 268 REMARK 465 GLU B 269 REMARK 465 GLN B 270 REMARK 465 GLY B 271 REMARK 465 PRO B 272 REMARK 465 ASN B 273 REMARK 465 GLY B 274 REMARK 465 SER B 275 REMARK 465 GLN B 276 REMARK 465 ASN B 277 REMARK 465 SER B 278 REMARK 465 SER B 279 REMARK 465 TYR B 280 REMARK 465 SER B 281 REMARK 465 GLN B 282 REMARK 465 SER B 283 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 ASP A -1 N CB CG OD1 OD2 REMARK 480 LYS A 0 CB CG CD CE NZ REMARK 480 GLU A 21 CG CD OE1 OE2 REMARK 480 GLU A 23 CG CD OE1 OE2 REMARK 480 LYS A 26 CD CE NZ REMARK 480 GLY A 33 N REMARK 480 HIS A 34 CG ND1 CD2 CE1 NE2 REMARK 480 ASP A 42 CG OD1 OD2 REMARK 480 LYS A 44 CG CD CE NZ REMARK 480 LYS A 47 CG CD CE NZ REMARK 480 LYS A 52 NZ REMARK 480 GLU A 55 CG CD OE1 OE2 REMARK 480 LYS A 74 CG CD CE NZ REMARK 480 LYS A 92 CD CE NZ REMARK 480 SER A 114 OG REMARK 480 LYS A 115 CG CD CE NZ REMARK 480 ARG A 178 CB CG CD NE CZ NH1 NH2 REMARK 480 ARG A 237 CG CD NE CZ NH1 NH2 REMARK 480 GLN A 238 CG CD OE1 NE2 REMARK 480 ASN A 245 N CB CG OD1 ND2 REMARK 480 LYS A 265 CE NZ REMARK 480 LYS A 295 NZ REMARK 480 LYS A 301 CG CD CE NZ REMARK 480 LYS A 303 CD CE NZ REMARK 480 GLN A 350 CG CD OE1 NE2 REMARK 480 GLN B 19 CG CD OE1 NE2 REMARK 480 LYS B 27 CG CD CE NZ REMARK 480 LYS B 56 CD CE NZ REMARK 480 ARG B 58 CG CD NE CZ NH1 NH2 REMARK 480 LYS B 79 NZ REMARK 480 ARG B 131 CD NE CZ NH1 NH2 REMARK 480 GLU B 169 CG CD OE1 OE2 REMARK 480 LYS B 211 CG CD CE NZ REMARK 480 GLN B 215 CD OE1 NE2 REMARK 480 VAL B 222 CG1 CG2 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 ASP A 45 114.66 172.94 REMARK 500 ASP A 151 45.02 -159.92 REMARK 500 SER B 221 66.37 -102.27 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 BAX A 465 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 466 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 467 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 468 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 469 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 284 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 285 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 286 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC9 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 287 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 288 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 289 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 290 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 291 DBREF 3RGF A 1 403 UNP P49336 CDK8_HUMAN 1 403 DBREF 3RGF B 1 283 UNP P24863 CCNC_HUMAN 1 283 SEQADV 3RGF ASP A -1 UNP P49336 EXPRESSION TAG SEQADV 3RGF LYS A 0 UNP P49336 EXPRESSION TAG SEQADV 3RGF LYS B -1 UNP P24863 EXPRESSION TAG SEQADV 3RGF ALA B 0 UNP P24863 EXPRESSION TAG SEQRES 1 A 405 ASP LYS MET ASP TYR ASP PHE LYS VAL LYS LEU SER SER SEQRES 2 A 405 GLU ARG GLU ARG VAL GLU ASP LEU PHE GLU TYR GLU GLY SEQRES 3 A 405 CYS LYS VAL GLY ARG GLY THR TYR GLY HIS VAL TYR LYS SEQRES 4 A 405 ALA LYS ARG LYS ASP GLY LYS ASP ASP LYS ASP TYR ALA SEQRES 5 A 405 LEU LYS GLN ILE GLU GLY THR GLY ILE SER MET SER ALA SEQRES 6 A 405 CYS ARG GLU ILE ALA LEU LEU ARG GLU LEU LYS HIS PRO SEQRES 7 A 405 ASN VAL ILE SER LEU GLN LYS VAL PHE LEU SER HIS ALA SEQRES 8 A 405 ASP ARG LYS VAL TRP LEU LEU PHE ASP TYR ALA GLU HIS SEQRES 9 A 405 ASP LEU TRP HIS ILE ILE LYS PHE HIS ARG ALA SER LYS SEQRES 10 A 405 ALA ASN LYS LYS PRO VAL GLN LEU PRO ARG GLY MET VAL SEQRES 11 A 405 LYS SER LEU LEU TYR GLN ILE LEU ASP GLY ILE HIS TYR SEQRES 12 A 405 LEU HIS ALA ASN TRP VAL LEU HIS ARG ASP LEU LYS PRO SEQRES 13 A 405 ALA ASN ILE LEU VAL MET GLY GLU GLY PRO GLU ARG GLY SEQRES 14 A 405 ARG VAL LYS ILE ALA ASP MET GLY PHE ALA ARG LEU PHE SEQRES 15 A 405 ASN SER PRO LEU LYS PRO LEU ALA ASP LEU ASP PRO VAL SEQRES 16 A 405 VAL VAL THR PHE TRP TYR ARG ALA PRO GLU LEU LEU LEU SEQRES 17 A 405 GLY ALA ARG HIS TYR THR LYS ALA ILE ASP ILE TRP ALA SEQRES 18 A 405 ILE GLY CYS ILE PHE ALA GLU LEU LEU THR SER GLU PRO SEQRES 19 A 405 ILE PHE HIS CYS ARG GLN GLU ASP ILE LYS THR SER ASN SEQRES 20 A 405 PRO TYR HIS HIS ASP GLN LEU ASP ARG ILE PHE ASN VAL SEQRES 21 A 405 MET GLY PHE PRO ALA ASP LYS ASP TRP GLU ASP ILE LYS SEQRES 22 A 405 LYS MET PRO GLU HIS SER THR LEU MET LYS ASP PHE ARG SEQRES 23 A 405 ARG ASN THR TYR THR ASN CYS SER LEU ILE LYS TYR MET SEQRES 24 A 405 GLU LYS HIS LYS VAL LYS PRO ASP SER LYS ALA PHE HIS SEQRES 25 A 405 LEU LEU GLN LYS LEU LEU THR MET ASP PRO ILE LYS ARG SEQRES 26 A 405 ILE THR SER GLU GLN ALA MET GLN ASP PRO TYR PHE LEU SEQRES 27 A 405 GLU ASP PRO LEU PRO THR SER ASP VAL PHE ALA GLY CYS SEQRES 28 A 405 GLN ILE PRO TYR PRO LYS ARG GLU PHE LEU THR GLU GLU SEQRES 29 A 405 GLU PRO ASP ASP LYS GLY ASP LYS LYS ASN GLN GLN GLN SEQRES 30 A 405 GLN GLN GLY ASN ASN HIS THR ASN GLY THR GLY HIS PRO SEQRES 31 A 405 GLY ASN GLN ASP SER SER HIS THR GLN GLY PRO PRO LEU SEQRES 32 A 405 LYS LYS SEQRES 1 B 285 LYS ALA MET ALA GLY ASN PHE TRP GLN SER SER HIS TYR SEQRES 2 B 285 LEU GLN TRP ILE LEU ASP LYS GLN ASP LEU LEU LYS GLU SEQRES 3 B 285 ARG GLN LYS ASP LEU LYS PHE LEU SER GLU GLU GLU TYR SEQRES 4 B 285 TRP LYS LEU GLN ILE PHE PHE THR ASN VAL ILE GLN ALA SEQRES 5 B 285 LEU GLY GLU HIS LEU LYS LEU ARG GLN GLN VAL ILE ALA SEQRES 6 B 285 THR ALA THR VAL TYR PHE LYS ARG PHE TYR ALA ARG TYR SEQRES 7 B 285 SER LEU LYS SER ILE ASP PRO VAL LEU MET ALA PRO THR SEQRES 8 B 285 CYS VAL PHE LEU ALA SER LYS VAL GLU GLU PHE GLY VAL SEQRES 9 B 285 VAL SER ASN THR ARG LEU ILE ALA ALA ALA THR SER VAL SEQRES 10 B 285 LEU LYS THR ARG PHE SER TYR ALA PHE PRO LYS GLU PHE SEQRES 11 B 285 PRO TYR ARG MET ASN HIS ILE LEU GLU CYS GLU PHE TYR SEQRES 12 B 285 LEU LEU GLU LEU MET ASP CYS CYS LEU ILE VAL TYR HIS SEQRES 13 B 285 PRO TYR ARG PRO LEU LEU GLN TYR VAL GLN ASP MET GLY SEQRES 14 B 285 GLN GLU ASP MET LEU LEU PRO LEU ALA TRP ARG ILE VAL SEQRES 15 B 285 ASN ASP THR TYR ARG THR ASP LEU CYS LEU LEU TYR PRO SEQRES 16 B 285 PRO PHE MET ILE ALA LEU ALA CYS LEU HIS VAL ALA CYS SEQRES 17 B 285 VAL VAL GLN GLN LYS ASP ALA ARG GLN TRP PHE ALA GLU SEQRES 18 B 285 LEU SER VAL ASP MET GLU LYS ILE LEU GLU ILE ILE ARG SEQRES 19 B 285 VAL ILE LEU LYS LEU TYR GLU GLN TRP LYS ASN PHE ASP SEQRES 20 B 285 GLU ARG LYS GLU MET ALA THR ILE LEU SER LYS MET PRO SEQRES 21 B 285 LYS PRO LYS PRO PRO PRO ASN SER GLU GLY GLU GLN GLY SEQRES 22 B 285 PRO ASN GLY SER GLN ASN SER SER TYR SER GLN SER HET BAX A 465 32 HET EDO A 466 4 HET EDO A 467 4 HET EDO A 468 4 HET EDO A 469 4 HET EDO B 284 4 HET EDO B 285 4 HET GOL B 286 6 HET EDO B 287 4 HET EDO B 288 4 HET EDO B 289 4 HET EDO B 290 4 HET EDO B 291 4 HETNAM BAX 4-{4-[({[4-CHLORO-3-(TRIFLUOROMETHYL) HETNAM 2 BAX PHENYL]AMINO}CARBONYL)AMINO]PHENOXY}-N-METHYLPYRIDINE- HETNAM 3 BAX 2-CARBOXAMIDE HETNAM EDO 1,2-ETHANEDIOL HETNAM GOL GLYCEROL HETSYN BAX SORAFENIB HETSYN EDO ETHYLENE GLYCOL HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL FORMUL 3 BAX C21 H16 CL F3 N4 O3 FORMUL 4 EDO 11(C2 H6 O2) FORMUL 10 GOL C3 H8 O3 FORMUL 16 HOH *175(H2 O) HELIX 1 1 ASP A 2 ARG A 13 1 12 HELIX 2 2 ARG A 15 LEU A 19 1 5 HELIX 3 3 SER A 60 LEU A 73 1 14 HELIX 4 4 LEU A 104 LYS A 115 1 12 HELIX 5 5 PRO A 124 ASN A 145 1 22 HELIX 6 6 LYS A 153 ALA A 155 5 3 HELIX 7 7 ALA A 201 LEU A 206 1 6 HELIX 8 8 THR A 212 SER A 230 1 19 HELIX 9 9 HIS A 248 GLY A 260 1 13 HELIX 10 10 TRP A 267 MET A 273 5 7 HELIX 11 11 GLU A 275 PHE A 283 1 9 HELIX 12 12 ARG A 284 THR A 289 5 6 HELIX 13 13 SER A 292 LYS A 299 1 8 HELIX 14 14 SER A 306 LEU A 316 1 11 HELIX 15 15 ASP A 319 ARG A 323 5 5 HELIX 16 16 THR A 325 GLN A 331 1 7 HELIX 17 17 ASP A 332 LEU A 336 5 5 HELIX 18 18 ASN B 4 GLN B 7 5 4 HELIX 19 19 SER B 8 ILE B 15 1 8 HELIX 20 20 ASP B 17 GLN B 26 1 10 HELIX 21 21 LYS B 27 PHE B 31 5 5 HELIX 22 22 SER B 33 LEU B 55 1 23 HELIX 23 23 ARG B 58 TYR B 76 1 19 HELIX 24 24 ASP B 82 GLU B 98 1 17 HELIX 25 25 SER B 104 PHE B 120 1 17 HELIX 26 26 ARG B 131 MET B 146 1 16 HELIX 27 27 PRO B 155 GLY B 167 1 13 HELIX 28 28 GLN B 168 TYR B 184 1 17 HELIX 29 29 ASP B 187 TYR B 192 1 6 HELIX 30 30 PRO B 193 GLN B 209 1 17 HELIX 31 31 ALA B 213 GLU B 219 1 7 HELIX 32 32 ASP B 223 PHE B 244 1 22 HELIX 33 33 ASP B 245 MET B 257 1 13 SHEET 1 A 5 PHE A 20 GLU A 21 0 SHEET 2 A 5 HIS A 34 ARG A 40 -1 O LYS A 39 N GLU A 21 SHEET 3 A 5 TYR A 49 GLN A 53 -1 O TYR A 49 N ALA A 38 SHEET 4 A 5 LYS A 92 ASP A 98 -1 O PHE A 97 N ALA A 50 SHEET 5 A 5 LYS A 83 SER A 87 -1 N SER A 87 O LYS A 92 SHEET 1 B 3 HIS A 102 ASP A 103 0 SHEET 2 B 3 ILE A 157 VAL A 159 -1 O VAL A 159 N HIS A 102 SHEET 3 B 3 VAL A 169 ILE A 171 -1 O LYS A 170 N LEU A 158 CISPEP 1 ASP A 338 PRO A 339 0 -2.73 SITE 1 AC1 19 ALA A 50 LYS A 52 GLU A 66 LEU A 70 SITE 2 AC1 19 LEU A 73 VAL A 78 ILE A 79 PHE A 97 SITE 3 AC1 19 ASP A 98 TYR A 99 ALA A 100 GLU A 101 SITE 4 AC1 19 LEU A 142 VAL A 147 HIS A 149 ILE A 171 SITE 5 AC1 19 ALA A 172 ASP A 173 PHE A 176 SITE 1 AC2 5 TRP A 267 MET A 273 ASP A 319 PRO A 320 SITE 2 AC2 5 HOH A 489 SITE 1 AC3 3 PRO A 341 THR A 342 SER A 343 SITE 1 AC4 2 ARG A 125 LYS A 303 SITE 1 AC5 3 HIS A 75 PRO A 76 HOH A 508 SITE 1 AC6 6 GLN B 41 THR B 45 THR B 66 PHE B 69 SITE 2 AC6 6 LYS B 70 TYR B 184 SITE 1 AC7 5 ASP A 2 PHE A 5 TYR B 76 SER B 77 SITE 2 AC7 5 LYS B 79 SITE 1 AC8 5 ASN B 46 ARG B 185 TRP B 241 PHE B 244 SITE 2 AC8 5 GLU B 246 SITE 1 AC9 4 GLU B 53 LEU B 57 GLN B 59 ILE B 62 SITE 1 BC1 3 GLN B 13 TRP B 14 ARG B 75 SITE 1 BC2 2 ASN B 133 HIS B 134 SITE 1 BC3 4 ARG B 25 GLU B 34 TYR B 37 TRP B 38 SITE 1 BC4 6 ALA B 0 ALA B 2 GLN B 60 VAL B 152 SITE 2 BC4 6 ARG B 157 HOH B 342 CRYST1 70.690 70.610 79.140 90.00 108.31 90.00 P 1 21 1 2 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 0.014146 0.000000 0.004681 0.00000 SCALE2 0.000000 0.014162 0.000000 0.00000 SCALE3 0.000000 0.000000 0.013310 0.00000 ATOM 1 N ASP A -1 -29.958 28.525 16.777 0.00 69.02 N ATOM 2 CA ASP A -1 -29.261 27.310 16.096 1.00 67.59 C ATOM 3 C ASP A -1 -29.897 27.144 14.713 1.00 66.80 C ATOM 4 O ASP A -1 -31.121 27.209 14.572 1.00 67.76 O ATOM 5 CB ASP A -1 -29.276 26.149 16.942 0.00 69.06 C ATOM 6 CG ASP A -1 -28.302 25.087 16.459 0.00 69.13 C ATOM 7 OD1 ASP A -1 -27.407 24.705 17.241 0.00 69.09 O ATOM 8 OD2 ASP A -1 -28.427 24.635 15.302 0.00 69.08 O ATOM 9 N LYS A 0 -29.056 26.928 13.702 1.00 65.17 N ATOM 10 CA LYS A 0 -29.512 26.771 12.316 1.00 61.78 C ATOM 11 C LYS A 0 -29.854 25.331 11.901 1.00 58.08 C ATOM 12 O LYS A 0 -30.426 25.121 10.827 1.00 62.22 O ATOM 13 CB LYS A 0 -28.470 27.342 11.356 0.00 63.72 C ATOM 14 CG LYS A 0 -28.124 28.810 11.595 0.00 63.86 C ATOM 15 CD LYS A 0 -29.297 29.732 11.295 0.00 63.98 C ATOM 16 CE LYS A 0 -28.891 31.194 11.394 0.00 64.04 C ATOM 17 NZ LYS A 0 -30.024 32.111 11.091 0.00 64.01 N ATOM 18 N MET A 1 -29.505 24.351 12.739 1.00 72.84 N ANISOU 18 N MET A 1 8377 9205 10093 322 1140 847 N ATOM 19 CA MET A 1 -29.775 22.932 12.454 1.00 64.42 C ANISOU 19 CA MET A 1 7362 8368 8748 357 1102 720 C ATOM 20 C MET A 1 -31.265 22.625 12.567 1.00 58.00 C ANISOU 20 C MET A 1 6621 7636 7779 399 1101 587 C ATOM 21 O MET A 1 -31.988 23.334 13.258 1.00 56.35 O ANISOU 21 O MET A 1 6475 7286 7649 363 1107 539 O ATOM 22 CB MET A 1 -29.024 22.034 13.435 1.00 61.98 C ANISOU 22 CB MET A 1 7144 7981 8424 228 994 545 C ATOM 23 CG MET A 1 -27.520 22.141 13.367 1.00 63.50 C ANISOU 23 CG MET A 1 7267 8104 8756 179 977 649 C ATOM 24 SD MET A 1 -26.737 21.017 14.537 1.00 64.46 S ANISOU 24 SD MET A 1 7501 8164 8827 44 852 433 S ATOM 25 CE MET A 1 -25.024 21.518 14.350 1.00 68.33 C ANISOU 25 CE MET A 1 7881 8540 9543 -4 845 594 C ATOM 26 N ASP A 2 -31.712 21.560 11.901 1.00 51.36 N ANISOU 26 N ASP A 2 5759 7015 6739 482 1081 515 N ATOM 27 CA ASP A 2 -33.124 21.173 11.923 1.00 46.82 C ANISOU 27 CA ASP A 2 5221 6514 6054 525 1069 391 C ATOM 28 C ASP A 2 -33.535 20.805 13.345 1.00 42.98 C ANISOU 28 C ASP A 2 4859 5863 5608 392 1012 228 C ATOM 29 O ASP A 2 -32.845 20.049 14.024 1.00 40.05 O ANISOU 29 O ASP A 2 4532 5440 5247 303 948 142 O ATOM 30 CB ASP A 2 -33.387 20.000 10.971 1.00 47.21 C ANISOU 30 CB ASP A 2 5195 6805 5938 642 1019 303 C ATOM 31 CG ASP A 2 -34.867 19.633 10.877 1.00 43.71 C ANISOU 31 CG ASP A 2 4751 6427 5431 697 996 178 C ATOM 32 OD1 ASP A 2 -35.253 18.583 11.421 1.00 44.07 O ANISOU 32 OD1 ASP A 2 4822 6433 5490 632 915 12 O ATOM 33 OD2 ASP A 2 -35.647 20.386 10.262 1.00 46.93 O ANISOU 33 OD2 ASP A 2 5116 6917 5797 809 1062 259 O ATOM 34 N TYR A 3 -34.650 21.367 13.793 1.00 39.86 N ANISOU 34 N TYR A 3 4513 5406 5225 400 1044 205 N ATOM 35 CA TYR A 3 -35.137 21.136 15.146 1.00 39.65 C ANISOU 35 CA TYR A 3 4591 5261 5213 324 1011 86 C ATOM 36 C TYR A 3 -35.459 19.672 15.431 1.00 37.39 C ANISOU 36 C TYR A 3 4300 5043 4863 301 959 -23 C ATOM 37 O TYR A 3 -34.984 19.115 16.420 1.00 37.81 O ANISOU 37 O TYR A 3 4405 5028 4931 230 921 -81 O ATOM 38 CB TYR A 3 -36.370 21.994 15.432 1.00 38.84 C ANISOU 38 CB TYR A 3 4526 5114 5117 369 1065 97 C ATOM 39 CG TYR A 3 -36.888 21.780 16.824 1.00 41.63 C ANISOU 39 CG TYR A 3 4974 5388 5455 335 1043 -2 C ATOM 40 CD1 TYR A 3 -36.218 22.308 17.924 1.00 44.20 C ANISOU 40 CD1 TYR A 3 5376 5583 5835 296 1003 -58 C ATOM 41 CD2 TYR A 3 -38.028 21.024 17.048 1.00 37.94 C ANISOU 41 CD2 TYR A 3 4501 4989 4928 363 1057 -37 C ATOM 42 CE1 TYR A 3 -36.684 22.096 19.214 1.00 45.07 C ANISOU 42 CE1 TYR A 3 5563 5675 5886 317 988 -142 C ATOM 43 CE2 TYR A 3 -38.507 20.816 18.325 1.00 41.20 C ANISOU 43 CE2 TYR A 3 4978 5360 5316 366 1061 -79 C ATOM 44 CZ TYR A 3 -37.836 21.347 19.403 1.00 45.57 C ANISOU 44 CZ TYR A 3 5616 5828 5871 357 1031 -128 C ATOM 45 OH TYR A 3 -38.327 21.121 20.666 1.00 46.44 O ANISOU 45 OH TYR A 3 5780 5951 5913 411 1041 -161 O ATOM 46 N ASP A 4 -36.250 19.048 14.565 1.00 37.52 N ANISOU 46 N ASP A 4 4235 5189 4832 373 952 -50 N ATOM 47 CA ASP A 4 -36.652 17.643 14.760 1.00 37.84 C ANISOU 47 CA ASP A 4 4227 5258 4892 355 890 -155 C ATOM 48 C ASP A 4 -35.458 16.700 14.796 1.00 37.42 C ANISOU 48 C ASP A 4 4155 5210 4854 300 825 -199 C ATOM 49 O ASP A 4 -35.424 15.752 15.583 1.00 39.50 O ANISOU 49 O ASP A 4 4418 5414 5178 237 793 -247 O ATOM 50 CB ASP A 4 -37.630 17.203 13.664 1.00 38.42 C ANISOU 50 CB ASP A 4 4185 5462 4949 462 859 -214 C ATOM 51 CG ASP A 4 -38.947 17.978 13.709 1.00 42.24 C ANISOU 51 CG ASP A 4 4682 5940 5426 513 923 -176 C ATOM 52 OD1 ASP A 4 -39.286 18.523 14.778 1.00 41.75 O ANISOU 52 OD1 ASP A 4 4713 5762 5389 459 980 -127 O ATOM 53 OD2 ASP A 4 -39.636 18.050 12.671 1.00 45.57 O ANISOU 53 OD2 ASP A 4 5018 6491 5805 626 911 -202 O ATOM 54 N PHE A 5 -34.486 16.963 13.927 1.00 37.22 N ANISOU 54 N PHE A 5 4098 5265 4778 337 816 -158 N ATOM 55 CA PHE A 5 -33.216 16.244 13.916 1.00 34.80 C ANISOU 55 CA PHE A 5 3779 4969 4474 290 762 -180 C ATOM 56 C PHE A 5 -32.526 16.356 15.272 1.00 34.80 C ANISOU 56 C PHE A 5 3882 4815 4526 167 768 -168 C ATOM 57 O PHE A 5 -32.202 15.339 15.889 1.00 34.31 O ANISOU 57 O PHE A 5 3823 4722 4493 108 725 -227 O ATOM 58 CB PHE A 5 -32.344 16.808 12.790 1.00 37.11 C ANISOU 58 CB PHE A 5 4017 5383 4702 376 783 -81 C ATOM 59 CG PHE A 5 -30.921 16.322 12.789 1.00 34.21 C ANISOU 59 CG PHE A 5 3642 5020 4335 330 745 -67 C ATOM 60 CD1 PHE A 5 -30.607 15.054 12.331 1.00 32.63 C ANISOU 60 CD1 PHE A 5 3377 4924 4097 367 661 -178 C ATOM 61 CD2 PHE A 5 -29.894 17.160 13.206 1.00 34.32 C ANISOU 61 CD2 PHE A 5 3700 4928 4414 260 784 50 C ATOM 62 CE1 PHE A 5 -29.293 14.619 12.303 1.00 40.36 C ANISOU 62 CE1 PHE A 5 4350 5918 5068 333 631 -158 C ATOM 63 CE2 PHE A 5 -28.579 16.739 13.180 1.00 36.52 C ANISOU 63 CE2 PHE A 5 3963 5213 4702 220 752 74 C ATOM 64 CZ PHE A 5 -28.273 15.463 12.726 1.00 39.15 C ANISOU 64 CZ PHE A 5 4246 5668 4961 257 682 -22 C ATOM 65 N LYS A 6 -32.338 17.584 15.756 1.00 35.29 N ANISOU 65 N LYS A 6 4013 4782 4613 144 813 -101 N ATOM 66 CA LYS A 6 -31.669 17.810 17.050 1.00 38.58 C ANISOU 66 CA LYS A 6 4519 5071 5069 64 793 -128 C ATOM 67 C LYS A 6 -32.357 17.098 18.221 1.00 38.26 C ANISOU 67 C LYS A 6 4524 5010 5004 52 791 -193 C ATOM 68 O LYS A 6 -31.710 16.361 18.974 1.00 37.71 O ANISOU 68 O LYS A 6 4474 4926 4929 9 759 -225 O ATOM 69 CB LYS A 6 -31.564 19.309 17.373 1.00 39.96 C ANISOU 69 CB LYS A 6 4737 5128 5317 67 815 -89 C ATOM 70 CG LYS A 6 -30.497 20.066 16.579 1.00 47.66 C ANISOU 70 CG LYS A 6 5649 6069 6390 60 822 18 C ATOM 71 CD LYS A 6 -30.433 21.553 16.978 1.00 53.16 C ANISOU 71 CD LYS A 6 6358 6595 7245 57 829 47 C ATOM 72 CE LYS A 6 -31.710 22.314 16.583 1.00 54.25 C ANISOU 72 CE LYS A 6 6488 6748 7377 132 899 98 C ATOM 73 NZ LYS A 6 -31.615 23.791 16.804 1.00 57.53 N ANISOU 73 NZ LYS A 6 6884 6980 7994 137 904 139 N ATOM 74 N VAL A 7 -33.659 17.328 18.386 1.00 39.26 N ANISOU 74 N VAL A 7 4655 5143 5118 104 836 -187 N ATOM 75 CA VAL A 7 -34.381 16.757 19.534 1.00 40.09 C ANISOU 75 CA VAL A 7 4782 5242 5207 122 860 -195 C ATOM 76 C VAL A 7 -34.421 15.226 19.478 1.00 37.63 C ANISOU 76 C VAL A 7 4380 4965 4952 97 842 -194 C ATOM 77 O VAL A 7 -34.308 14.571 20.502 1.00 36.43 O ANISOU 77 O VAL A 7 4231 4804 4805 95 857 -169 O ATOM 78 CB VAL A 7 -35.812 17.355 19.721 1.00 40.90 C ANISOU 78 CB VAL A 7 4897 5348 5294 194 921 -166 C ATOM 79 CG1 VAL A 7 -35.721 18.840 20.061 1.00 43.06 C ANISOU 79 CG1 VAL A 7 5260 5559 5540 225 928 -184 C ATOM 80 CG2 VAL A 7 -36.685 17.129 18.490 1.00 41.25 C ANISOU 80 CG2 VAL A 7 4849 5446 5379 218 931 -154 C ATOM 81 N LYS A 8 -34.547 14.655 18.287 1.00 37.57 N ANISOU 81 N LYS A 8 4276 5002 4998 96 804 -225 N ATOM 82 CA LYS A 8 -34.512 13.197 18.148 1.00 38.40 C ANISOU 82 CA LYS A 8 4270 5109 5210 74 757 -258 C ATOM 83 C LYS A 8 -33.163 12.646 18.645 1.00 39.05 C ANISOU 83 C LYS A 8 4381 5175 5281 12 727 -261 C ATOM 84 O LYS A 8 -33.117 11.729 19.480 1.00 35.84 O ANISOU 84 O LYS A 8 3938 4733 4946 -9 739 -225 O ATOM 85 CB LYS A 8 -34.783 12.808 16.692 1.00 39.56 C ANISOU 85 CB LYS A 8 4305 5328 5397 121 687 -345 C ATOM 86 CG LYS A 8 -34.638 11.328 16.344 1.00 44.85 C ANISOU 86 CG LYS A 8 4838 5987 6215 111 597 -432 C ATOM 87 CD LYS A 8 -35.642 10.441 17.076 1.00 49.92 C ANISOU 87 CD LYS A 8 5376 6527 7065 96 614 -398 C ATOM 88 CE LYS A 8 -35.584 9.000 16.545 1.00 52.40 C ANISOU 88 CE LYS A 8 5511 6796 7601 94 500 -511 C ATOM 89 NZ LYS A 8 -35.973 7.999 17.579 1.00 53.27 N ANISOU 89 NZ LYS A 8 5515 6770 7956 47 539 -407 N ATOM 90 N LEU A 9 -32.067 13.225 18.156 1.00 38.15 N ANISOU 90 N LEU A 9 4320 5086 5088 -9 698 -278 N ATOM 91 CA LEU A 9 -30.735 12.767 18.553 1.00 37.55 C ANISOU 91 CA LEU A 9 4271 4998 5000 -68 663 -284 C ATOM 92 C LEU A 9 -30.484 12.926 20.056 1.00 38.07 C ANISOU 92 C LEU A 9 4419 5017 5029 -83 696 -252 C ATOM 93 O LEU A 9 -29.891 12.044 20.679 1.00 36.60 O ANISOU 93 O LEU A 9 4217 4830 4860 -110 686 -242 O ATOM 94 CB LEU A 9 -29.635 13.461 17.735 1.00 36.12 C ANISOU 94 CB LEU A 9 4111 4847 4767 -78 636 -278 C ATOM 95 CG LEU A 9 -29.391 12.848 16.353 1.00 36.20 C ANISOU 95 CG LEU A 9 4020 4962 4772 -31 587 -312 C ATOM 96 CD1 LEU A 9 -28.556 13.783 15.483 1.00 37.90 C ANISOU 96 CD1 LEU A 9 4235 5236 4928 5 600 -240 C ATOM 97 CD2 LEU A 9 -28.721 11.466 16.463 1.00 34.96 C ANISOU 97 CD2 LEU A 9 3809 4810 4663 -68 525 -371 C ATOM 98 N SER A 10 -30.938 14.033 20.634 1.00 40.43 N ANISOU 98 N SER A 10 4797 5293 5271 -43 731 -245 N ATOM 99 CA SER A 10 -30.746 14.272 22.064 1.00 43.63 C ANISOU 99 CA SER A 10 5276 5695 5606 -3 744 -249 C ATOM 100 C SER A 10 -31.579 13.313 22.913 1.00 43.96 C ANISOU 100 C SER A 10 5266 5783 5654 56 810 -168 C ATOM 101 O SER A 10 -31.171 12.944 24.016 1.00 45.93 O ANISOU 101 O SER A 10 5533 6078 5841 104 826 -141 O ATOM 102 CB SER A 10 -31.077 15.719 22.435 1.00 44.51 C ANISOU 102 CB SER A 10 5471 5771 5670 53 744 -292 C ATOM 103 OG SER A 10 -32.462 15.968 22.338 1.00 53.71 O ANISOU 103 OG SER A 10 6623 6953 6832 112 806 -251 O ATOM 104 N SER A 11 -32.740 12.914 22.401 1.00 42.33 N ANISOU 104 N SER A 11 4975 5571 5537 69 852 -117 N ATOM 105 CA SER A 11 -33.603 11.969 23.104 1.00 43.18 C ANISOU 105 CA SER A 11 4986 5695 5724 123 926 2 C ATOM 106 C SER A 11 -32.961 10.581 23.140 1.00 41.89 C ANISOU 106 C SER A 11 4720 5511 5684 72 910 43 C ATOM 107 O SER A 11 -33.040 9.885 24.145 1.00 42.45 O ANISOU 107 O SER A 11 4735 5612 5783 127 978 169 O ATOM 108 CB SER A 11 -34.974 11.895 22.423 1.00 43.36 C ANISOU 108 CB SER A 11 4919 5687 5868 138 953 31 C ATOM 109 OG SER A 11 -35.827 10.973 23.075 1.00 45.32 O ANISOU 109 OG SER A 11 5039 5925 6256 187 1030 177 O ATOM 110 N GLU A 12 -32.315 10.210 22.039 1.00 41.79 N ANISOU 110 N GLU A 12 4674 5463 5741 -14 824 -54 N ATOM 111 CA GLU A 12 -31.726 8.883 21.854 1.00 42.99 C ANISOU 111 CA GLU A 12 4715 5579 6039 -65 785 -49 C ATOM 112 C GLU A 12 -30.269 8.768 22.316 1.00 41.55 C ANISOU 112 C GLU A 12 4608 5428 5750 -101 760 -64 C ATOM 113 O GLU A 12 -29.747 7.658 22.419 1.00 40.87 O ANISOU 113 O GLU A 12 4437 5318 5774 -133 745 -35 O ATOM 114 CB GLU A 12 -31.777 8.512 20.364 1.00 43.70 C ANISOU 114 CB GLU A 12 4720 5644 6238 -101 686 -177 C ATOM 115 CG GLU A 12 -33.183 8.470 19.756 1.00 50.22 C ANISOU 115 CG GLU A 12 5443 6439 7200 -60 680 -199 C ATOM 116 CD GLU A 12 -33.962 7.215 20.118 1.00 56.67 C ANISOU 116 CD GLU A 12 6068 7154 8309 -56 693 -125 C ATOM 117 OE1 GLU A 12 -33.341 6.157 20.381 1.00 57.99 O ANISOU 117 OE1 GLU A 12 6148 7268 8619 -92 672 -100 O ATOM 118 OE2 GLU A 12 -35.212 7.280 20.131 1.00 65.58 O ANISOU 118 OE2 GLU A 12 7116 8244 9559 -17 728 -78 O ATOM 119 N ARG A 13 -29.603 9.897 22.565 1.00 40.13 N ANISOU 119 N ARG A 13 4570 5288 5390 -97 744 -116 N ATOM 120 CA ARG A 13 -28.152 9.891 22.805 1.00 39.91 C ANISOU 120 CA ARG A 13 4603 5277 5284 -140 695 -157 C ATOM 121 C ARG A 13 -27.769 9.262 24.148 1.00 40.02 C ANISOU 121 C ARG A 13 4613 5340 5253 -90 741 -77 C ATOM 122 O ARG A 13 -28.281 9.646 25.195 1.00 40.52 O ANISOU 122 O ARG A 13 4710 5464 5221 16 800 -24 O ATOM 123 CB ARG A 13 -27.563 11.310 22.702 1.00 40.93 C ANISOU 123 CB ARG A 13 4849 5399 5303 -147 651 -237 C ATOM 124 CG ARG A 13 -26.036 11.390 22.945 1.00 42.47 C ANISOU 124 CG ARG A 13 5091 5593 5454 -195 589 -283 C ATOM 125 CD ARG A 13 -25.376 12.590 22.242 1.00 41.43 C ANISOU 125 CD ARG A 13 5001 5406 5332 -236 533 -336 C ATOM 126 NE ARG A 13 -26.220 13.775 22.318 1.00 46.42 N ANISOU 126 NE ARG A 13 5676 6002 5959 -186 551 -357 N ATOM 127 CZ ARG A 13 -26.751 14.434 21.287 1.00 39.95 C ANISOU 127 CZ ARG A 13 4834 5157 5188 -189 569 -332 C ATOM 128 NH1 ARG A 13 -26.523 14.079 20.031 1.00 33.52 N ANISOU 128 NH1 ARG A 13 3953 4375 4409 -218 567 -292 N ATOM 129 NH2 ARG A 13 -27.523 15.482 21.532 1.00 43.44 N ANISOU 129 NH2 ARG A 13 5316 5560 5629 -138 587 -349 N ATOM 130 N GLU A 14 -26.853 8.301 24.101 1.00 40.45 N ANISOU 130 N GLU A 14 4619 5390 5361 -142 715 -64 N ATOM 131 CA GLU A 14 -26.316 7.692 25.311 1.00 43.05 C ANISOU 131 CA GLU A 14 4937 5787 5635 -84 760 23 C ATOM 132 C GLU A 14 -25.407 8.672 26.038 1.00 42.55 C ANISOU 132 C GLU A 14 5004 5789 5372 -42 712 -69 C ATOM 133 O GLU A 14 -24.537 9.302 25.433 1.00 41.30 O ANISOU 133 O GLU A 14 4910 5586 5196 -121 624 -183 O ATOM 134 CB GLU A 14 -25.538 6.413 24.988 1.00 44.45 C ANISOU 134 CB GLU A 14 5021 5927 5940 -158 738 53 C ATOM 135 CG GLU A 14 -26.428 5.221 24.667 1.00 49.69 C ANISOU 135 CG GLU A 14 5509 6511 6859 -166 781 151 C ATOM 136 CD GLU A 14 -25.641 3.931 24.520 1.00 56.86 C ANISOU 136 CD GLU A 14 6312 7372 7920 -220 756 179 C ATOM 137 OE1 GLU A 14 -24.482 3.982 24.054 1.00 60.96 O ANISOU 137 OE1 GLU A 14 6897 7906 8357 -284 676 72 O ATOM 138 OE2 GLU A 14 -26.185 2.866 24.875 1.00 64.73 O ANISOU 138 OE2 GLU A 14 7145 8309 9142 -195 819 321 O ATOM 139 N ARG A 15 -25.638 8.798 27.339 1.00 43.91 N ANISOU 139 N ARG A 15 5197 6075 5411 105 767 -14 N ATOM 140 CA ARG A 15 -24.857 9.668 28.196 1.00 45.49 C ANISOU 140 CA ARG A 15 5500 6356 5430 190 697 -137 C ATOM 141 C ARG A 15 -24.119 8.791 29.189 1.00 44.70 C ANISOU 141 C ARG A 15 5362 6381 5240 276 729 -60 C ATOM 142 O ARG A 15 -24.682 7.828 29.708 1.00 43.88 O ANISOU 142 O ARG A 15 5158 6351 5162 360 849 134 O ATOM 143 CB ARG A 15 -25.762 10.643 28.938 1.00 46.94 C ANISOU 143 CB ARG A 15 5737 6615 5482 351 716 -175 C ATOM 144 CG ARG A 15 -26.536 11.601 28.035 1.00 50.19 C ANISOU 144 CG ARG A 15 6186 6909 5976 282 693 -243 C ATOM 145 CD ARG A 15 -27.537 12.393 28.871 1.00 52.07 C ANISOU 145 CD ARG A 15 6464 7238 6083 462 727 -259 C ATOM 146 NE ARG A 15 -28.367 13.300 28.084 1.00 54.74 N ANISOU 146 NE ARG A 15 6833 7471 6497 411 718 -306 N ATOM 147 CZ ARG A 15 -29.388 14.006 28.577 1.00 57.74 C ANISOU 147 CZ ARG A 15 7241 7904 6792 547 752 -314 C ATOM 148 NH1 ARG A 15 -29.722 13.917 29.865 1.00 57.36 N ANISOU 148 NH1 ARG A 15 7194 8037 6563 766 799 -276 N ATOM 149 NH2 ARG A 15 -30.088 14.805 27.781 1.00 56.83 N ANISOU 149 NH2 ARG A 15 7149 7686 6759 488 747 -349 N ATOM 150 N VAL A 16 -22.857 9.125 29.442 1.00 43.82 N ANISOU 150 N VAL A 16 5312 6288 5049 261 624 -196 N ATOM 151 CA VAL A 16 -22.026 8.344 30.348 1.00 44.48 C ANISOU 151 CA VAL A 16 5365 6505 5031 347 642 -140 C ATOM 152 C VAL A 16 -22.632 8.347 31.751 1.00 45.42 C ANISOU 152 C VAL A 16 5465 6845 4946 615 722 -59 C ATOM 153 O VAL A 16 -22.713 7.302 32.393 1.00 44.34 O ANISOU 153 O VAL A 16 5234 6833 4780 719 841 146 O ATOM 154 CB VAL A 16 -20.547 8.848 30.353 1.00 46.18 C ANISOU 154 CB VAL A 16 5648 6693 5206 286 493 -329 C ATOM 155 CG1 VAL A 16 -20.428 10.230 31.021 1.00 47.31 C ANISOU 155 CG1 VAL A 16 5873 6874 5230 411 370 -550 C ATOM 156 CG2 VAL A 16 -19.638 7.832 31.028 1.00 44.26 C ANISOU 156 CG2 VAL A 16 5359 6570 4889 337 518 -251 C ATOM 157 N GLU A 17 -23.121 9.505 32.191 1.00 47.70 N ANISOU 157 N GLU A 17 5829 7189 5107 745 667 -200 N ATOM 158 CA GLU A 17 -23.677 9.645 33.548 1.00 52.20 C ANISOU 158 CA GLU A 17 6386 8014 5432 1053 727 -153 C ATOM 159 C GLU A 17 -24.958 8.836 33.788 1.00 52.75 C ANISOU 159 C GLU A 17 6342 8167 5535 1154 932 157 C ATOM 160 O GLU A 17 -25.322 8.592 34.932 1.00 54.80 O ANISOU 160 O GLU A 17 6547 8677 5597 1430 1031 296 O ATOM 161 CB GLU A 17 -23.908 11.123 33.913 1.00 53.44 C ANISOU 161 CB GLU A 17 6644 8198 5463 1180 596 -416 C ATOM 162 CG GLU A 17 -24.999 11.856 33.116 1.00 54.58 C ANISOU 162 CG GLU A 17 6818 8183 5736 1083 612 -429 C ATOM 163 CD GLU A 17 -24.492 12.514 31.844 1.00 58.92 C ANISOU 163 CD GLU A 17 7417 8460 6508 813 496 -577 C ATOM 164 OE1 GLU A 17 -25.179 13.428 31.331 1.00 57.78 O ANISOU 164 OE1 GLU A 17 7311 8203 6438 773 470 -649 O ATOM 165 OE2 GLU A 17 -23.416 12.113 31.345 1.00 61.66 O ANISOU 165 OE2 GLU A 17 7756 8718 6956 654 443 -599 O ATOM 166 N ASP A 18 -25.633 8.427 32.714 1.00 52.84 N ANISOU 166 N ASP A 18 6299 7977 5801 952 993 270 N ATOM 167 CA ASP A 18 -26.799 7.542 32.810 1.00 53.89 C ANISOU 167 CA ASP A 18 6284 8127 6065 1008 1174 572 C ATOM 168 C ASP A 18 -26.399 6.070 32.891 1.00 54.26 C ANISOU 168 C ASP A 18 6180 8163 6274 968 1274 806 C ATOM 169 O ASP A 18 -27.013 5.301 33.628 1.00 57.93 O ANISOU 169 O ASP A 18 6496 8746 6768 1133 1441 1099 O ATOM 170 CB ASP A 18 -27.716 7.722 31.596 1.00 53.02 C ANISOU 170 CB ASP A 18 6159 7796 6191 819 1169 559 C ATOM 171 CG ASP A 18 -28.373 9.092 31.539 1.00 53.60 C ANISOU 171 CG ASP A 18 6350 7876 6142 875 1112 395 C ATOM 172 OD1 ASP A 18 -28.529 9.760 32.589 1.00 56.33 O ANISOU 172 OD1 ASP A 18 6750 8414 6241 1108 1114 352 O ATOM 173 OD2 ASP A 18 -28.753 9.492 30.421 1.00 51.48 O ANISOU 173 OD2 ASP A 18 6108 7428 6024 702 1061 307 O ATOM 174 N LEU A 19 -25.381 5.680 32.129 1.00 52.74 N ANISOU 174 N LEU A 19 6009 7827 6203 760 1178 695 N ATOM 175 CA LEU A 19 -24.986 4.270 32.029 1.00 53.96 C ANISOU 175 CA LEU A 19 6015 7924 6562 692 1252 886 C ATOM 176 C LEU A 19 -23.998 3.816 33.085 1.00 54.70 C ANISOU 176 C LEU A 19 6094 8215 6473 841 1286 962 C ATOM 177 O LEU A 19 -23.927 2.622 33.385 1.00 56.64 O ANISOU 177 O LEU A 19 6180 8472 6868 872 1404 1212 O ATOM 178 CB LEU A 19 -24.379 3.971 30.650 1.00 52.39 C ANISOU 178 CB LEU A 19 5833 7495 6580 420 1133 733 C ATOM 179 CG LEU A 19 -25.291 4.200 29.444 1.00 52.62 C ANISOU 179 CG LEU A 19 5844 7336 6813 278 1093 661 C ATOM 180 CD1 LEU A 19 -24.619 3.671 28.188 1.00 52.22 C ANISOU 180 CD1 LEU A 19 5773 7120 6949 76 988 538 C ATOM 181 CD2 LEU A 19 -26.665 3.558 29.639 1.00 53.08 C ANISOU 181 CD2 LEU A 19 5727 7356 7085 349 1229 898 C ATOM 182 N PHE A 20 -23.224 4.745 33.639 1.00 55.85 N ANISOU 182 N PHE A 20 6387 8508 6324 940 1175 746 N ATOM 183 CA PHE A 20 -22.132 4.369 34.532 1.00 56.68 C ANISOU 183 CA PHE A 20 6490 8803 6245 1072 1170 760 C ATOM 184 C PHE A 20 -22.083 5.134 35.849 1.00 60.25 C ANISOU 184 C PHE A 20 7001 9563 6328 1396 1153 682 C ATOM 185 O PHE A 20 -22.285 6.348 35.893 1.00 58.43 O ANISOU 185 O PHE A 20 6890 9347 5963 1446 1034 438 O ATOM 186 CB PHE A 20 -20.798 4.484 33.790 1.00 54.43 C ANISOU 186 CB PHE A 20 6298 8374 6011 851 1006 530 C ATOM 187 CG PHE A 20 -20.603 3.415 32.767 1.00 48.71 C ANISOU 187 CG PHE A 20 5482 7436 5589 617 1034 635 C ATOM 188 CD1 PHE A 20 -20.194 2.148 33.148 1.00 49.48 C ANISOU 188 CD1 PHE A 20 5448 7577 5773 649 1137 852 C ATOM 189 CD2 PHE A 20 -20.869 3.653 31.432 1.00 44.83 C ANISOU 189 CD2 PHE A 20 5021 6713 5299 393 959 518 C ATOM 190 CE1 PHE A 20 -20.027 1.142 32.208 1.00 49.31 C ANISOU 190 CE1 PHE A 20 5330 7349 6058 450 1142 918 C ATOM 191 CE2 PHE A 20 -20.703 2.649 30.487 1.00 45.38 C ANISOU 191 CE2 PHE A 20 4996 6611 5634 218 962 577 C ATOM 192 CZ PHE A 20 -20.281 1.393 30.878 1.00 45.10 C ANISOU 192 CZ PHE A 20 4832 6597 5705 242 1044 762 C ATOM 193 N GLU A 21 -21.805 4.390 36.918 1.00 65.15 N ANISOU 193 N GLU A 21 7521 10438 6794 1635 1270 891 N ATOM 194 CA GLU A 21 -21.587 4.953 38.239 1.00 69.82 C ANISOU 194 CA GLU A 21 8149 11386 6995 1998 1244 809 C ATOM 195 C GLU A 21 -20.084 5.054 38.467 1.00 71.87 C ANISOU 195 C GLU A 21 8483 11703 7123 1983 1083 573 C ATOM 196 O GLU A 21 -19.395 4.037 38.548 1.00 72.53 O ANISOU 196 O GLU A 21 8484 11807 7267 1943 1154 741 O ATOM 197 CB GLU A 21 -22.229 4.070 39.315 1.00 72.42 C ANISOU 197 CB GLU A 21 8296 12012 7207 2324 1492 1223 C ATOM 198 CG GLU A 21 -22.296 4.703 40.688 0.00 77.08 C ANISOU 198 CG GLU A 21 8906 13032 7349 2777 1485 1159 C ATOM 199 CD GLU A 21 -23.126 3.896 41.674 0.00 79.77 C ANISOU 199 CD GLU A 21 9044 13683 7582 3129 1766 1633 C ATOM 200 OE1 GLU A 21 -23.260 2.668 41.487 0.00 79.65 O ANISOU 200 OE1 GLU A 21 8852 13569 7842 3034 1959 2019 O ATOM 201 OE2 GLU A 21 -23.642 4.494 42.641 0.00 82.23 O ANISOU 201 OE2 GLU A 21 9357 14339 7547 3518 1793 1626 O ATOM 202 N TYR A 22 -19.584 6.284 38.548 1.00 74.43 N ANISOU 202 N TYR A 22 8947 12030 7303 2008 859 182 N ATOM 203 CA TYR A 22 -18.168 6.541 38.803 1.00 77.06 C ANISOU 203 CA TYR A 22 9340 12406 7532 2007 674 -83 C ATOM 204 C TYR A 22 -18.036 7.603 39.901 1.00 82.82 C ANISOU 204 C TYR A 22 10126 13408 7934 2353 512 -386 C ATOM 205 O TYR A 22 -17.203 8.504 39.820 1.00 83.80 O ANISOU 205 O TYR A 22 10333 13440 8069 2299 269 -758 O ATOM 206 CB TYR A 22 -17.444 6.950 37.501 1.00 73.91 C ANISOU 206 CB TYR A 22 9026 11634 7421 1612 516 -292 C ATOM 207 CG TYR A 22 -18.045 8.148 36.796 1.00 72.01 C ANISOU 207 CG TYR A 22 8873 11180 7307 1484 406 -497 C ATOM 208 CD1 TYR A 22 -19.182 8.016 36.006 1.00 70.97 C ANISOU 208 CD1 TYR A 22 8724 10891 7352 1344 531 -323 C ATOM 209 CD2 TYR A 22 -17.478 9.414 36.921 1.00 74.22 C ANISOU 209 CD2 TYR A 22 9234 11407 7560 1509 172 -866 C ATOM 210 CE1 TYR A 22 -19.744 9.114 35.366 1.00 71.59 C ANISOU 210 CE1 TYR A 22 8876 10791 7535 1242 442 -492 C ATOM 211 CE2 TYR A 22 -18.033 10.518 36.285 1.00 73.49 C ANISOU 211 CE2 TYR A 22 9201 11109 7613 1400 84 -1027 C ATOM 212 CZ TYR A 22 -19.165 10.362 35.511 1.00 72.03 C ANISOU 212 CZ TYR A 22 9010 10796 7562 1270 228 -831 C ATOM 213 OH TYR A 22 -19.717 11.452 34.878 1.00 73.27 O ANISOU 213 OH TYR A 22 9221 10763 7855 1172 150 -974 O ATOM 214 N GLU A 23 -18.867 7.474 40.936 1.00 89.11 N ANISOU 214 N GLU A 23 10856 14544 8456 2730 646 -221 N ATOM 215 CA GLU A 23 -18.863 8.405 42.065 1.00 94.04 C ANISOU 215 CA GLU A 23 11515 15491 8724 3136 498 -507 C ATOM 216 C GLU A 23 -17.600 8.194 42.892 1.00 98.03 C ANISOU 216 C GLU A 23 12000 16245 9002 3341 378 -667 C ATOM 217 O GLU A 23 -17.502 7.237 43.664 1.00100.40 O ANISOU 217 O GLU A 23 12193 16859 9094 3589 552 -379 O ATOM 218 CB GLU A 23 -20.109 8.207 42.934 1.00 96.47 C ANISOU 218 CB GLU A 23 11738 16141 8775 3520 705 -230 C ATOM 219 CG GLU A 23 -21.416 8.514 42.248 0.00 97.60 C ANISOU 219 CG GLU A 23 11897 16076 9112 3369 807 -99 C ATOM 220 CD GLU A 23 -22.628 8.332 43.149 0.00100.08 C ANISOU 220 CD GLU A 23 12110 16742 9175 3769 1018 197 C ATOM 221 OE1 GLU A 23 -22.460 7.940 44.324 0.00102.85 O ANISOU 221 OE1 GLU A 23 12370 17528 9181 4191 1100 327 O ATOM 222 OE2 GLU A 23 -23.757 8.581 42.677 0.00 99.30 O ANISOU 222 OE2 GLU A 23 12011 16500 9217 3678 1108 316 O ATOM 223 N GLY A 24 -16.637 9.096 42.727 1.00100.12 N ANISOU 223 N GLY A 24 12349 16361 9329 3242 83 -1115 N ATOM 224 CA GLY A 24 -15.299 8.902 43.272 1.00102.67 C ANISOU 224 CA GLY A 24 12654 16829 9526 3344 -63 -1299 C ATOM 225 C GLY A 24 -14.547 7.945 42.368 1.00101.28 C ANISOU 225 C GLY A 24 12463 16389 9631 2952 31 -1079 C ATOM 226 O GLY A 24 -14.657 8.034 41.142 1.00 99.26 O ANISOU 226 O GLY A 24 12253 15740 9722 2550 38 -1042 O ATOM 227 N CYS A 25 -13.788 7.030 42.967 1.00103.31 N ANISOU 227 N CYS A 25 12648 16879 9724 3091 101 -935 N ATOM 228 CA CYS A 25 -13.046 6.011 42.215 1.00101.93 C ANISOU 228 CA CYS A 25 12447 16494 9789 2762 198 -714 C ATOM 229 C CYS A 25 -12.179 6.611 41.100 1.00 99.80 C ANISOU 229 C CYS A 25 12263 15810 9847 2354 -12 -988 C ATOM 230 O CYS A 25 -12.083 6.045 40.011 1.00 97.66 O ANISOU 230 O CYS A 25 11994 15248 9863 2001 80 -804 O ATOM 231 CB CYS A 25 -14.016 4.981 41.621 1.00100.32 C ANISOU 231 CB CYS A 25 12171 16171 9775 2601 496 -245 C ATOM 232 SG CYS A 25 -15.210 4.301 42.792 1.00105.28 S ANISOU 232 SG CYS A 25 12657 17229 10117 3054 785 171 S ATOM 233 N LYS A 26 -11.544 7.748 41.383 1.00101.16 N ANISOU 233 N LYS A 26 12485 15963 9990 2427 -296 -1423 N ATOM 234 CA LYS A 26 -10.747 8.474 40.389 1.00 99.17 C ANISOU 234 CA LYS A 26 12283 15319 10080 2076 -499 -1670 C ATOM 235 C LYS A 26 -9.310 7.942 40.356 1.00 98.88 C ANISOU 235 C LYS A 26 12217 15263 10091 1969 -575 -1706 C ATOM 236 O LYS A 26 -8.370 8.617 40.781 1.00100.72 O ANISOU 236 O LYS A 26 12440 15508 10320 2052 -826 -2051 O ATOM 237 CB LYS A 26 -10.775 9.980 40.696 1.00100.84 C ANISOU 237 CB LYS A 26 12525 15468 10322 2199 -777 -2114 C ATOM 238 CG LYS A 26 -10.182 10.872 39.608 1.00 98.29 C ANISOU 238 CG LYS A 26 12222 14703 10420 1842 -959 -2314 C ATOM 239 CD LYS A 26 -10.262 12.349 40.057 0.00103.38 C ANISOU 239 CD LYS A 26 12863 15287 11130 2005 -1242 -2758 C ATOM 240 CE LYS A 26 -9.555 13.261 39.069 0.00102.57 C ANISOU 240 CE LYS A 26 12737 14741 11494 1677 -1427 -2935 C ATOM 241 NZ LYS A 26 -9.583 14.685 39.504 0.00105.21 N ANISOU 241 NZ LYS A 26 13035 14969 11970 1827 -1719 -3374 N ATOM 242 N VAL A 27 -9.152 6.721 39.849 1.00 97.00 N ANISOU 242 N VAL A 27 11952 14984 9920 1791 -367 -1357 N ATOM 243 CA VAL A 27 -7.838 6.073 39.776 1.00 96.73 C ANISOU 243 CA VAL A 27 11888 14940 9924 1684 -405 -1340 C ATOM 244 C VAL A 27 -7.006 6.626 38.619 1.00 94.57 C ANISOU 244 C VAL A 27 11647 14282 10004 1317 -558 -1490 C ATOM 245 O VAL A 27 -5.787 6.460 38.583 1.00 93.90 O ANISOU 245 O VAL A 27 11539 14161 9977 1237 -662 -1575 O ATOM 246 CB VAL A 27 -7.959 4.536 39.625 1.00 95.63 C ANISOU 246 CB VAL A 27 11692 14877 9765 1628 -131 -913 C ATOM 247 CG1 VAL A 27 -8.707 3.941 40.813 1.00 98.37 C ANISOU 247 CG1 VAL A 27 11968 15618 9790 2014 47 -698 C ATOM 248 CG2 VAL A 27 -8.640 4.166 38.312 1.00 91.78 C ANISOU 248 CG2 VAL A 27 11218 14077 9576 1300 10 -690 C ATOM 249 N GLY A 33 -6.046 13.579 30.986 0.00 74.00 N ANISOU 249 N GLY A 33 8869 9299 9948 -315 -1154 -1836 N ATOM 250 CA GLY A 33 -7.275 13.873 31.703 1.00 74.00 C ANISOU 250 CA GLY A 33 8944 9419 9752 -134 -1150 -1966 C ATOM 251 C GLY A 33 -7.389 13.127 33.020 1.00 74.19 C ANISOU 251 C GLY A 33 9032 9762 9397 103 -1158 -2082 C ATOM 252 O GLY A 33 -6.441 13.098 33.808 1.00 76.01 O ANISOU 252 O GLY A 33 9221 10066 9592 200 -1311 -2270 O ATOM 253 N HIS A 34 -8.552 12.525 33.264 1.00 71.88 N ANISOU 253 N HIS A 34 8821 9664 8827 211 -990 -1954 N ATOM 254 CA HIS A 34 -8.778 11.754 34.485 1.00 71.28 C ANISOU 254 CA HIS A 34 8782 9919 8382 466 -949 -1983 C ATOM 255 C HIS A 34 -9.431 10.418 34.155 1.00 67.23 C ANISOU 255 C HIS A 34 8306 9542 7695 424 -685 -1644 C ATOM 256 O HIS A 34 -10.328 10.350 33.312 1.00 64.65 O ANISOU 256 O HIS A 34 8002 9113 7449 305 -552 -1474 O ATOM 257 CB HIS A 34 -9.653 12.545 35.461 1.00 74.40 C ANISOU 257 CB HIS A 34 9200 10446 8623 738 -1040 -2212 C ATOM 258 CG HIS A 34 -9.017 13.816 35.905 0.00 77.31 C ANISOU 258 CG HIS A 34 9510 10681 9185 815 -1333 -2596 C ATOM 259 ND1 HIS A 34 -7.885 13.871 36.689 0.00 79.21 N ANISOU 259 ND1 HIS A 34 9693 11002 9401 936 -1532 -2840 N ATOM 260 CD2 HIS A 34 -9.367 15.100 35.657 0.00 78.45 C ANISOU 260 CD2 HIS A 34 9625 10593 9591 789 -1474 -2790 C ATOM 261 CE1 HIS A 34 -7.565 15.134 36.907 0.00 81.38 C ANISOU 261 CE1 HIS A 34 9896 11086 9937 981 -1799 -3187 C ATOM 262 NE2 HIS A 34 -8.449 15.900 36.293 0.00 80.97 N ANISOU 262 NE2 HIS A 34 9857 10835 10072 891 -1765 -3156 N ATOM 263 N VAL A 35 -8.973 9.360 34.823 1.00 65.12 N ANISOU 263 N VAL A 35 8028 9499 7215 531 -619 -1554 N ATOM 264 CA VAL A 35 -9.486 8.012 34.588 1.00 61.97 C ANISOU 264 CA VAL A 35 7628 9205 6712 499 -383 -1233 C ATOM 265 C VAL A 35 -10.241 7.511 35.818 1.00 61.85 C ANISOU 265 C VAL A 35 7604 9506 6391 805 -279 -1159 C ATOM 266 O VAL A 35 -9.745 7.619 36.936 1.00 63.36 O ANISOU 266 O VAL A 35 7780 9922 6372 1046 -373 -1310 O ATOM 267 CB VAL A 35 -8.346 7.034 34.238 1.00 60.93 C ANISOU 267 CB VAL A 35 7464 9059 6628 361 -351 -1110 C ATOM 268 CG1 VAL A 35 -8.872 5.611 34.107 1.00 59.69 C ANISOU 268 CG1 VAL A 35 7277 8998 6403 352 -126 -801 C ATOM 269 CG2 VAL A 35 -7.656 7.471 32.953 1.00 55.69 C ANISOU 269 CG2 VAL A 35 6793 8114 6253 84 -423 -1127 C ATOM 270 N TYR A 36 -11.438 6.968 35.600 1.00 59.44 N ANISOU 270 N TYR A 36 7289 9227 6067 813 -86 -921 N ATOM 271 CA TYR A 36 -12.295 6.495 36.687 1.00 59.80 C ANISOU 271 CA TYR A 36 7299 9566 5857 1111 51 -779 C ATOM 272 C TYR A 36 -12.546 4.999 36.571 1.00 57.70 C ANISOU 272 C TYR A 36 6950 9354 5618 1076 280 -414 C ATOM 273 O TYR A 36 -12.663 4.470 35.466 1.00 54.48 O ANISOU 273 O TYR A 36 6527 8721 5451 816 348 -279 O ATOM 274 CB TYR A 36 -13.647 7.217 36.664 1.00 59.65 C ANISOU 274 CB TYR A 36 7309 9530 5827 1189 86 -794 C ATOM 275 CG TYR A 36 -13.560 8.728 36.663 1.00 62.91 C ANISOU 275 CG TYR A 36 7786 9836 6280 1207 -135 -1144 C ATOM 276 CD1 TYR A 36 -13.719 9.457 37.839 1.00 68.89 C ANISOU 276 CD1 TYR A 36 8552 10825 6797 1535 -252 -1372 C ATOM 277 CD2 TYR A 36 -13.330 9.429 35.482 1.00 61.65 C ANISOU 277 CD2 TYR A 36 7660 9350 6413 919 -229 -1244 C ATOM 278 CE1 TYR A 36 -13.645 10.852 37.840 1.00 71.26 C ANISOU 278 CE1 TYR A 36 8891 10994 7190 1554 -477 -1720 C ATOM 279 CE2 TYR A 36 -13.254 10.815 35.470 1.00 65.89 C ANISOU 279 CE2 TYR A 36 8225 9755 7054 931 -426 -1539 C ATOM 280 CZ TYR A 36 -13.412 11.522 36.651 1.00 71.52 C ANISOU 280 CZ TYR A 36 8945 10662 7569 1237 -559 -1790 C ATOM 281 OH TYR A 36 -13.339 12.895 36.635 1.00 73.85 O ANISOU 281 OH TYR A 36 9247 10792 8020 1249 -773 -2105 O ATOM 282 N LYS A 37 -12.634 4.324 37.714 1.00 58.34 N ANISOU 282 N LYS A 37 6960 9741 5465 1359 393 -255 N ATOM 283 CA LYS A 37 -13.141 2.956 37.764 1.00 57.95 C ANISOU 283 CA LYS A 37 6792 9746 5480 1377 636 136 C ATOM 284 C LYS A 37 -14.656 3.062 37.798 1.00 57.18 C ANISOU 284 C LYS A 37 6655 9659 5410 1466 774 302 C ATOM 285 O LYS A 37 -15.207 3.817 38.598 1.00 60.71 O ANISOU 285 O LYS A 37 7129 10310 5628 1726 749 210 O ATOM 286 CB LYS A 37 -12.618 2.211 38.996 1.00 60.54 C ANISOU 286 CB LYS A 37 7032 10413 5556 1670 725 288 C ATOM 287 CG LYS A 37 -12.950 0.727 39.014 1.00 62.65 C ANISOU 287 CG LYS A 37 7142 10695 5966 1667 975 718 C ATOM 288 CD LYS A 37 -12.260 0.017 40.171 1.00 68.72 C ANISOU 288 CD LYS A 37 7819 11799 6492 1952 1061 877 C ATOM 289 CE LYS A 37 -12.637 -1.459 40.237 1.00 69.95 C ANISOU 289 CE LYS A 37 7783 11950 6843 1964 1325 1345 C ATOM 290 NZ LYS A 37 -11.774 -2.212 41.192 1.00 73.16 N ANISOU 290 NZ LYS A 37 8096 12648 7052 2195 1407 1510 N ATOM 291 N ALA A 38 -15.325 2.317 36.925 1.00 54.75 N ANISOU 291 N ALA A 38 6278 9136 5391 1263 904 526 N ATOM 292 CA ALA A 38 -16.760 2.455 36.735 1.00 54.84 C ANISOU 292 CA ALA A 38 6248 9092 5496 1289 1014 663 C ATOM 293 C ALA A 38 -17.485 1.116 36.758 1.00 56.75 C ANISOU 293 C ALA A 38 6301 9310 5950 1305 1244 1067 C ATOM 294 O ALA A 38 -16.926 0.079 36.387 1.00 53.83 O ANISOU 294 O ALA A 38 5846 8829 5776 1168 1290 1200 O ATOM 295 CB ALA A 38 -17.043 3.174 35.430 1.00 52.30 C ANISOU 295 CB ALA A 38 6022 8466 5383 1005 896 465 C ATOM 296 N LYS A 39 -18.737 1.166 37.209 1.00 60.17 N ANISOU 296 N LYS A 39 6655 9840 6367 1481 1384 1264 N ATOM 297 CA LYS A 39 -19.655 0.035 37.177 1.00 63.51 C ANISOU 297 CA LYS A 39 6867 10191 7073 1492 1601 1660 C ATOM 298 C LYS A 39 -20.883 0.438 36.370 1.00 64.26 C ANISOU 298 C LYS A 39 6963 10072 7381 1356 1601 1639 C ATOM 299 O LYS A 39 -21.309 1.595 36.416 1.00 62.53 O ANISOU 299 O LYS A 39 6876 9908 6973 1414 1516 1435 O ATOM 300 CB LYS A 39 -20.103 -0.334 38.595 1.00 67.06 C ANISOU 300 CB LYS A 39 7172 10997 7310 1887 1806 1995 C ATOM 301 CG LYS A 39 -19.001 -0.837 39.516 1.00 69.84 C ANISOU 301 CG LYS A 39 7488 11618 7431 2084 1840 2075 C ATOM 302 CD LYS A 39 -18.776 -2.336 39.379 1.00 71.80 C ANISOU 302 CD LYS A 39 7525 11744 8012 1996 2003 2430 C ATOM 303 CE LYS A 39 -17.998 -2.885 40.565 1.00 73.79 C ANISOU 303 CE LYS A 39 7689 12348 8001 2299 2113 2631 C ATOM 304 NZ LYS A 39 -17.673 -4.325 40.390 1.00 73.29 N ANISOU 304 NZ LYS A 39 7419 12136 8294 2194 2259 2963 N ATOM 305 N ARG A 40 -21.454 -0.516 35.644 1.00 67.59 N ANISOU 305 N ARG A 40 7225 10245 8210 1185 1686 1835 N ATOM 306 CA ARG A 40 -22.729 -0.298 34.958 1.00 71.04 C ANISOU 306 CA ARG A 40 7618 10495 8878 1089 1706 1858 C ATOM 307 C ARG A 40 -23.860 -0.038 35.962 1.00 75.38 C ANISOU 307 C ARG A 40 8082 11265 9295 1381 1875 2111 C ATOM 308 O ARG A 40 -23.960 -0.723 36.982 1.00 76.82 O ANISOU 308 O ARG A 40 8100 11652 9436 1625 2060 2451 O ATOM 309 CB ARG A 40 -23.090 -1.507 34.087 1.00 72.12 C ANISOU 309 CB ARG A 40 7555 10330 9517 887 1749 2015 C ATOM 310 CG ARG A 40 -22.723 -1.366 32.618 1.00 73.23 C ANISOU 310 CG ARG A 40 7794 10199 9831 586 1554 1698 C ATOM 311 CD ARG A 40 -23.547 -2.319 31.745 1.00 79.15 C ANISOU 311 CD ARG A 40 8333 10661 11079 442 1573 1801 C ATOM 312 NE ARG A 40 -24.090 -1.658 30.558 1.00 82.23 N ANISOU 312 NE ARG A 40 8815 10888 11543 283 1431 1537 N ATOM 313 CZ ARG A 40 -25.072 -0.754 30.569 1.00 84.14 C ANISOU 313 CZ ARG A 40 9119 11168 11682 338 1446 1504 C ATOM 314 NH1 ARG A 40 -25.631 -0.363 31.712 1.00 84.01 N ANISOU 314 NH1 ARG A 40 9095 11357 11470 557 1587 1703 N ATOM 315 NH2 ARG A 40 -25.488 -0.217 29.425 1.00 84.49 N ANISOU 315 NH2 ARG A 40 9234 11069 11798 196 1318 1271 N ATOM 316 N LYS A 41 -24.704 0.951 35.666 1.00 77.65 N ANISOU 316 N LYS A 41 8470 11523 9510 1374 1821 1963 N ATOM 317 CA LYS A 41 -25.866 1.258 36.513 1.00 81.66 C ANISOU 317 CA LYS A 41 8901 12231 9896 1649 1976 2190 C ATOM 318 C LYS A 41 -27.021 0.286 36.275 1.00 84.56 C ANISOU 318 C LYS A 41 9006 12425 10699 1614 2154 2560 C ATOM 319 O LYS A 41 -27.828 0.056 37.170 1.00 87.96 O ANISOU 319 O LYS A 41 9278 13044 11100 1879 2353 2909 O ATOM 320 CB LYS A 41 -26.347 2.700 36.300 1.00 80.46 C ANISOU 320 CB LYS A 41 8949 12105 9517 1659 1849 1890 C ATOM 321 CG LYS A 41 -25.582 3.733 37.116 1.00 81.07 C ANISOU 321 CG LYS A 41 9210 12458 9134 1866 1730 1625 C ATOM 322 CD LYS A 41 -26.220 5.109 37.023 1.00 79.23 C ANISOU 322 CD LYS A 41 9131 12244 8729 1914 1625 1373 C ATOM 323 CE LYS A 41 -25.424 6.142 37.801 1.00 79.73 C ANISOU 323 CE LYS A 41 9353 12541 8398 2118 1466 1058 C ATOM 324 NZ LYS A 41 -25.906 7.525 37.542 1.00 79.44 N ANISOU 324 NZ LYS A 41 9465 12449 8268 2113 1326 762 N ATOM 325 N ASP A 42 -27.095 -0.275 35.068 1.00 85.66 N ANISOU 325 N ASP A 42 9082 12212 11252 1307 2073 2481 N ATOM 326 CA ASP A 42 -28.131 -1.251 34.716 1.00 88.20 C ANISOU 326 CA ASP A 42 9127 12305 12079 1242 2195 2777 C ATOM 327 C ASP A 42 -28.102 -2.471 35.629 1.00 91.61 C ANISOU 327 C ASP A 42 9279 12818 12709 1419 2416 3241 C ATOM 328 O ASP A 42 -29.150 -2.996 35.995 1.00 95.15 O ANISOU 328 O ASP A 42 9477 13235 13441 1537 2599 3617 O ATOM 329 CB ASP A 42 -27.970 -1.709 33.263 1.00 87.07 C ANISOU 329 CB ASP A 42 8963 11795 12323 910 2025 2541 C ATOM 330 CG ASP A 42 -28.990 -2.729 32.820 0.00 90.19 C ANISOU 330 CG ASP A 42 9054 11913 13300 833 2099 2776 C ATOM 331 OD1 ASP A 42 -30.149 -2.643 33.275 0.00 91.92 O ANISOU 331 OD1 ASP A 42 9138 12169 13617 971 2242 3031 O ATOM 332 OD2 ASP A 42 -28.645 -3.616 32.012 0.00 89.93 O ANISOU 332 OD2 ASP A 42 8903 11620 13646 643 2005 2696 O ATOM 333 N GLY A 43 -26.902 -2.925 35.982 1.00 92.52 N ANISOU 333 N GLY A 43 9421 13032 12702 1440 2406 3237 N ATOM 334 CA GLY A 43 -26.738 -4.052 36.901 1.00 96.07 C ANISOU 334 CA GLY A 43 9609 13591 13303 1631 2626 3691 C ATOM 335 C GLY A 43 -26.550 -5.388 36.206 1.00 96.84 C ANISOU 335 C GLY A 43 9471 13333 13993 1409 2623 3811 C ATOM 336 O GLY A 43 -25.999 -6.320 36.794 1.00 97.96 O ANISOU 336 O GLY A 43 9440 13530 14250 1506 2753 4097 O ATOM 337 N LYS A 44 -26.997 -5.487 34.955 1.00 96.57 N ANISOU 337 N LYS A 44 9420 12940 14334 1129 2467 3580 N ATOM 338 CA LYS A 44 -26.837 -6.710 34.163 1.00 97.11 C ANISOU 338 CA LYS A 44 9265 12644 14987 917 2409 3601 C ATOM 339 C LYS A 44 -25.407 -6.809 33.630 1.00 94.22 C ANISOU 339 C LYS A 44 9084 12253 14463 756 2230 3273 C ATOM 340 O LYS A 44 -25.192 -6.971 32.425 1.00 92.94 O ANISOU 340 O LYS A 44 8962 11833 14520 517 2029 2953 O ATOM 341 CB LYS A 44 -27.847 -6.731 33.009 1.00 97.26 C ANISOU 341 CB LYS A 44 9197 12327 15431 719 2279 3425 C ATOM 342 CG LYS A 44 -28.043 -8.128 32.392 0.00100.83 C ANISOU 342 CG LYS A 44 9311 12388 16612 573 2247 3528 C ATOM 343 CD LYS A 44 -28.992 -8.070 31.207 0.00100.56 C ANISOU 343 CD LYS A 44 9205 12048 16955 400 2074 3275 C ATOM 344 CE LYS A 44 -29.077 -9.413 30.500 0.00102.01 C ANISOU 344 CE LYS A 44 9062 11830 17866 258 1978 3271 C ATOM 345 NZ LYS A 44 -30.008 -9.376 29.339 0.00101.91 N ANISOU 345 NZ LYS A 44 8961 11537 18222 119 1782 2986 N ATOM 346 N ASP A 45 -24.445 -6.734 34.552 1.00 93.19 N ANISOU 346 N ASP A 45 9049 12413 13948 914 2308 3365 N ATOM 347 CA ASP A 45 -23.014 -6.614 34.248 1.00 89.17 C ANISOU 347 CA ASP A 45 8749 11954 13179 802 2153 3066 C ATOM 348 C ASP A 45 -22.270 -6.379 35.568 1.00 88.85 C ANISOU 348 C ASP A 45 8784 12304 12672 1066 2277 3229 C ATOM 349 O ASP A 45 -22.473 -5.351 36.217 1.00 89.91 O ANISOU 349 O ASP A 45 9075 12717 12370 1250 2296 3175 O ATOM 350 CB ASP A 45 -22.750 -5.438 33.290 1.00 86.02 C ANISOU 350 CB ASP A 45 8658 11523 12504 628 1916 2577 C ATOM 351 CG ASP A 45 -21.387 -5.513 32.621 1.00 81.88 C ANISOU 351 CG ASP A 45 8284 10943 11882 456 1741 2279 C ATOM 352 OD1 ASP A 45 -20.397 -5.874 33.292 1.00 78.11 O ANISOU 352 OD1 ASP A 45 7817 10619 11242 537 1790 2371 O ATOM 353 OD2 ASP A 45 -21.310 -5.196 31.414 1.00 76.26 O ANISOU 353 OD2 ASP A 45 7677 10054 11244 256 1557 1961 O ATOM 354 N ASP A 46 -21.430 -7.328 35.974 1.00 87.69 N ANISOU 354 N ASP A 46 8514 12186 12617 1105 2354 3415 N ATOM 355 CA ASP A 46 -20.644 -7.186 37.207 1.00 87.41 C ANISOU 355 CA ASP A 46 8536 12543 12134 1375 2460 3558 C ATOM 356 C ASP A 46 -19.164 -6.889 36.921 1.00 83.18 C ANISOU 356 C ASP A 46 8235 12061 11308 1253 2271 3200 C ATOM 357 O ASP A 46 -18.366 -6.748 37.850 1.00 83.71 O ANISOU 357 O ASP A 46 8364 12441 10999 1457 2314 3245 O ATOM 358 CB ASP A 46 -20.774 -8.448 38.067 1.00 90.93 C ANISOU 358 CB ASP A 46 8647 13046 12856 1570 2725 4102 C ATOM 359 CG ASP A 46 -20.277 -8.244 39.495 1.00 94.17 C ANISOU 359 CG ASP A 46 9075 13941 12763 1948 2880 4320 C ATOM 360 OD1 ASP A 46 -19.437 -9.049 39.951 1.00 95.61 O ANISOU 360 OD1 ASP A 46 9151 14211 12965 2024 2966 4512 O ATOM 361 OD2 ASP A 46 -20.716 -7.276 40.155 1.00 95.26 O ANISOU 361 OD2 ASP A 46 9331 14386 12479 2186 2905 4284 O ATOM 362 N LYS A 47 -18.808 -6.778 35.641 1.00 78.21 N ANISOU 362 N LYS A 47 7725 11146 10846 943 2061 2850 N ATOM 363 CA LYS A 47 -17.429 -6.499 35.237 1.00 73.58 C ANISOU 363 CA LYS A 47 7344 10580 10035 809 1882 2528 C ATOM 364 C LYS A 47 -17.064 -5.034 35.486 1.00 69.71 C ANISOU 364 C LYS A 47 7131 10310 9046 874 1751 2218 C ATOM 365 O LYS A 47 -17.908 -4.142 35.362 1.00 69.38 O ANISOU 365 O LYS A 47 7170 10275 8915 897 1720 2114 O ATOM 366 CB LYS A 47 -17.226 -6.844 33.757 1.00 71.40 C ANISOU 366 CB LYS A 47 7082 9956 10092 497 1710 2278 C ATOM 367 CG LYS A 47 -17.395 -8.324 33.448 0.00 75.09 C ANISOU 367 CG LYS A 47 7269 10172 11089 423 1785 2507 C ATOM 368 CD LYS A 47 -17.109 -8.626 31.986 0.00 73.44 C ANISOU 368 CD LYS A 47 7084 9666 11152 161 1583 2201 C ATOM 369 CE LYS A 47 -17.228 -10.113 31.693 0.00 74.87 C ANISOU 369 CE LYS A 47 6972 9581 11896 100 1624 2381 C ATOM 370 NZ LYS A 47 -16.953 -10.426 30.264 0.00 73.51 N ANISOU 370 NZ LYS A 47 6814 9152 11965 -109 1404 2044 N ATOM 371 N ASP A 48 -15.806 -4.797 35.847 1.00 66.41 N ANISOU 371 N ASP A 48 6841 10058 8334 909 1669 2069 N ATOM 372 CA ASP A 48 -15.305 -3.445 36.069 1.00 62.77 C ANISOU 372 CA ASP A 48 6615 9766 7469 960 1512 1745 C ATOM 373 C ASP A 48 -14.894 -2.811 34.747 1.00 57.40 C ANISOU 373 C ASP A 48 6097 8839 6875 666 1302 1395 C ATOM 374 O ASP A 48 -14.344 -3.481 33.868 1.00 55.91 O ANISOU 374 O ASP A 48 5878 8451 6916 460 1249 1356 O ATOM 375 CB ASP A 48 -14.110 -3.452 37.029 1.00 64.42 C ANISOU 375 CB ASP A 48 6869 10253 7356 1135 1495 1721 C ATOM 376 CG ASP A 48 -14.493 -3.840 38.448 1.00 71.15 C ANISOU 376 CG ASP A 48 7578 11443 8012 1506 1699 2050 C ATOM 377 OD1 ASP A 48 -13.603 -4.299 39.196 1.00 76.73 O ANISOU 377 OD1 ASP A 48 8245 12366 8545 1660 1740 2140 O ATOM 378 OD2 ASP A 48 -15.673 -3.683 38.824 1.00 73.43 O ANISOU 378 OD2 ASP A 48 7786 11806 8308 1664 1823 2231 O ATOM 379 N TYR A 49 -15.161 -1.515 34.625 1.00 54.05 N ANISOU 379 N TYR A 49 5829 8442 6267 670 1187 1153 N ATOM 380 CA TYR A 49 -14.788 -0.732 33.452 1.00 50.86 C ANISOU 380 CA TYR A 49 5568 7841 5916 433 1004 851 C ATOM 381 C TYR A 49 -13.938 0.453 33.876 1.00 48.61 C ANISOU 381 C TYR A 49 5442 7685 5342 493 852 586 C ATOM 382 O TYR A 49 -13.995 0.886 35.035 1.00 49.12 O ANISOU 382 O TYR A 49 5523 7992 5148 739 869 580 O ATOM 383 CB TYR A 49 -16.039 -0.230 32.730 1.00 50.13 C ANISOU 383 CB TYR A 49 5483 7599 5967 359 1004 816 C ATOM 384 CG TYR A 49 -16.855 -1.341 32.115 1.00 52.05 C ANISOU 384 CG TYR A 49 5555 7659 6563 270 1105 1014 C ATOM 385 CD1 TYR A 49 -17.787 -2.042 32.867 1.00 55.62 C ANISOU 385 CD1 TYR A 49 5835 8172 7128 427 1285 1318 C ATOM 386 CD2 TYR A 49 -16.678 -1.704 30.782 1.00 54.05 C ANISOU 386 CD2 TYR A 49 5796 7683 7059 50 1011 896 C ATOM 387 CE1 TYR A 49 -18.532 -3.075 32.309 1.00 56.55 C ANISOU 387 CE1 TYR A 49 5759 8080 7647 341 1359 1491 C ATOM 388 CE2 TYR A 49 -17.422 -2.730 30.213 1.00 58.31 C ANISOU 388 CE2 TYR A 49 6157 8040 7957 -16 1066 1026 C ATOM 389 CZ TYR A 49 -18.346 -3.413 30.985 1.00 58.78 C ANISOU 389 CZ TYR A 49 6036 8120 8180 117 1234 1318 C ATOM 390 OH TYR A 49 -19.081 -4.432 30.427 1.00 63.28 O ANISOU 390 OH TYR A 49 6396 8469 9177 48 1270 1437 O ATOM 391 N ALA A 50 -13.141 0.963 32.939 1.00 43.20 N ANISOU 391 N ALA A 50 4853 6844 4716 290 698 367 N ATOM 392 CA ALA A 50 -12.424 2.216 33.142 1.00 42.89 C ANISOU 392 CA ALA A 50 4938 6847 4511 308 531 99 C ATOM 393 C ALA A 50 -12.980 3.258 32.191 1.00 40.52 C ANISOU 393 C ALA A 50 4711 6366 4319 174 448 -51 C ATOM 394 O ALA A 50 -13.208 2.970 31.018 1.00 41.21 O ANISOU 394 O ALA A 50 4780 6276 4603 -6 460 -15 O ATOM 395 CB ALA A 50 -10.926 2.033 32.918 1.00 40.63 C ANISOU 395 CB ALA A 50 4677 6534 4227 200 428 4 C ATOM 396 N LEU A 51 -13.203 4.462 32.705 1.00 42.19 N ANISOU 396 N LEU A 51 4994 6634 4402 285 358 -226 N ATOM 397 CA LEU A 51 -13.646 5.594 31.899 1.00 43.72 C ANISOU 397 CA LEU A 51 5250 6659 4700 176 273 -371 C ATOM 398 C LEU A 51 -12.569 6.658 31.890 1.00 44.29 C ANISOU 398 C LEU A 51 5378 6668 4781 133 87 -612 C ATOM 399 O LEU A 51 -12.077 7.025 32.948 1.00 48.99 O ANISOU 399 O LEU A 51 5986 7405 5221 299 -1 -750 O ATOM 400 CB LEU A 51 -14.927 6.203 32.483 1.00 45.19 C ANISOU 400 CB LEU A 51 5453 6928 4788 344 319 -377 C ATOM 401 CG LEU A 51 -16.258 5.537 32.131 1.00 45.31 C ANISOU 401 CG LEU A 51 5406 6915 4896 335 483 -159 C ATOM 402 CD1 LEU A 51 -17.401 6.149 32.940 1.00 44.29 C ANISOU 402 CD1 LEU A 51 5289 6917 4624 546 531 -154 C ATOM 403 CD2 LEU A 51 -16.522 5.669 30.650 1.00 42.04 C ANISOU 403 CD2 LEU A 51 4998 6271 4704 106 462 -175 C ATOM 404 N LYS A 52 -12.207 7.152 30.709 1.00 44.73 N ANISOU 404 N LYS A 52 5447 6520 5030 -67 23 -658 N ATOM 405 CA LYS A 52 -11.290 8.293 30.589 1.00 46.58 C ANISOU 405 CA LYS A 52 5697 6640 5360 -121 -149 -856 C ATOM 406 C LYS A 52 -11.983 9.488 29.946 1.00 47.10 C ANISOU 406 C LYS A 52 5781 6545 5569 -174 -190 -927 C ATOM 407 O LYS A 52 -12.490 9.392 28.836 1.00 46.86 O ANISOU 407 O LYS A 52 5742 6415 5649 -295 -112 -806 O ATOM 408 CB LYS A 52 -10.053 7.939 29.758 1.00 45.29 C ANISOU 408 CB LYS A 52 5500 6375 5332 -295 -183 -808 C ATOM 409 CG LYS A 52 -9.222 9.178 29.386 1.00 49.43 C ANISOU 409 CG LYS A 52 6004 6727 6051 -378 -339 -951 C ATOM 410 CD LYS A 52 -7.815 8.843 28.965 1.00 53.75 C ANISOU 410 CD LYS A 52 6504 7223 6696 -493 -388 -914 C ATOM 411 CE LYS A 52 -6.890 10.055 29.062 1.00 57.13 C ANISOU 411 CE LYS A 52 6877 7495 7334 -526 -567 -1078 C ATOM 412 NZ LYS A 52 -5.498 9.725 28.668 0.00 58.01 N ANISOU 412 NZ LYS A 52 6929 7559 7554 -634 -608 -1019 N ATOM 413 N GLN A 53 -11.992 10.615 30.641 1.00 51.62 N ANISOU 413 N GLN A 53 6369 7099 6145 -67 -323 -1137 N ATOM 414 CA GLN A 53 -12.460 11.861 30.059 1.00 54.34 C ANISOU 414 CA GLN A 53 6712 7260 6676 -122 -383 -1217 C ATOM 415 C GLN A 53 -11.253 12.522 29.398 1.00 56.70 C ANISOU 415 C GLN A 53 6946 7357 7241 -271 -502 -1266 C ATOM 416 O GLN A 53 -10.225 12.702 30.041 1.00 58.85 O ANISOU 416 O GLN A 53 7186 7628 7545 -235 -640 -1415 O ATOM 417 CB GLN A 53 -13.059 12.774 31.133 1.00 56.14 C ANISOU 417 CB GLN A 53 6967 7548 6815 80 -485 -1436 C ATOM 418 CG GLN A 53 -13.880 13.921 30.566 1.00 57.88 C ANISOU 418 CG GLN A 53 7189 7596 7206 42 -505 -1481 C ATOM 419 CD GLN A 53 -14.414 14.860 31.632 1.00 60.78 C ANISOU 419 CD GLN A 53 7578 8017 7498 257 -630 -1733 C ATOM 420 OE1 GLN A 53 -13.714 15.211 32.584 1.00 61.42 O ANISOU 420 OE1 GLN A 53 7639 8154 7544 396 -801 -1973 O ATOM 421 NE2 GLN A 53 -15.662 15.288 31.465 1.00 62.27 N ANISOU 421 NE2 GLN A 53 7802 8197 7661 302 -557 -1697 N ATOM 422 N ILE A 54 -11.374 12.856 28.116 1.00 59.05 N ANISOU 422 N ILE A 54 7208 7498 7731 -420 -444 -1125 N ATOM 423 CA ILE A 54 -10.279 13.466 27.366 1.00 61.13 C ANISOU 423 CA ILE A 54 7379 7574 8274 -551 -520 -1094 C ATOM 424 C ILE A 54 -10.042 14.873 27.887 1.00 65.57 C ANISOU 424 C ILE A 54 7883 7959 9071 -509 -700 -1310 C ATOM 425 O ILE A 54 -10.994 15.617 28.135 1.00 66.87 O ANISOU 425 O ILE A 54 8073 8085 9250 -432 -720 -1407 O ATOM 426 CB ILE A 54 -10.572 13.528 25.842 1.00 60.84 C ANISOU 426 CB ILE A 54 7300 7456 8360 -669 -395 -861 C ATOM 427 CG1 ILE A 54 -10.277 12.184 25.173 1.00 60.09 C ANISOU 427 CG1 ILE A 54 7215 7492 8124 -723 -279 -686 C ATOM 428 CG2 ILE A 54 -9.729 14.605 25.163 1.00 62.71 C ANISOU 428 CG2 ILE A 54 7412 7475 8942 -756 -466 -811 C ATOM 429 CD1 ILE A 54 -11.189 11.082 25.598 1.00 60.12 C ANISOU 429 CD1 ILE A 54 7298 7667 7878 -654 -185 -673 C ATOM 430 N GLU A 55 -8.771 15.226 28.063 1.00 69.02 N ANISOU 430 N GLU A 55 8230 8278 9716 -555 -840 -1396 N ATOM 431 CA GLU A 55 -8.400 16.556 28.532 1.00 72.85 C ANISOU 431 CA GLU A 55 8618 8549 10514 -522 -1047 -1627 C ATOM 432 C GLU A 55 -8.681 17.583 27.441 1.00 74.20 C ANISOU 432 C GLU A 55 8688 8471 11033 -629 -1007 -1477 C ATOM 433 O GLU A 55 -8.435 17.331 26.259 1.00 73.54 O ANISOU 433 O GLU A 55 8554 8354 11035 -750 -867 -1189 O ATOM 434 CB GLU A 55 -6.921 16.596 28.932 1.00 74.49 C ANISOU 434 CB GLU A 55 8727 8677 10901 -554 -1212 -1743 C ATOM 435 CG GLU A 55 -6.509 17.897 29.635 0.00 79.27 C ANISOU 435 CG GLU A 55 9212 9058 11849 -488 -1477 -2060 C ATOM 436 CD GLU A 55 -5.068 17.876 30.122 0.00 80.80 C ANISOU 436 CD GLU A 55 9298 9183 12219 -503 -1661 -2208 C ATOM 437 OE1 GLU A 55 -4.317 16.946 29.758 0.00 79.36 O ANISOU 437 OE1 GLU A 55 9125 9098 11930 -592 -1564 -2017 O ATOM 438 OE2 GLU A 55 -4.686 18.799 30.871 0.00 83.50 O ANISOU 438 OE2 GLU A 55 9536 9369 12822 -417 -1917 -2533 O ATOM 439 N GLY A 56 -9.212 18.733 27.845 1.00 76.72 N ANISOU 439 N GLY A 56 8969 8637 11543 -559 -1127 -1668 N ATOM 440 CA GLY A 56 -9.507 19.820 26.917 1.00 77.65 C ANISOU 440 CA GLY A 56 8970 8502 12030 -641 -1095 -1529 C ATOM 441 C GLY A 56 -10.895 19.700 26.328 1.00 76.20 C ANISOU 441 C GLY A 56 8886 8427 11639 -621 -909 -1372 C ATOM 442 O GLY A 56 -11.544 18.658 26.444 1.00 74.04 O ANISOU 442 O GLY A 56 8755 8407 10971 -575 -785 -1321 O ATOM 443 N THR A 57 -11.348 20.777 25.695 1.00 77.07 N ANISOU 443 N THR A 57 8902 8332 12048 -652 -891 -1288 N ATOM 444 CA THR A 57 -12.667 20.809 25.076 1.00 75.97 C ANISOU 444 CA THR A 57 8839 8276 11751 -629 -724 -1142 C ATOM 445 C THR A 57 -12.603 20.306 23.634 1.00 73.37 C ANISOU 445 C THR A 57 8468 8016 11393 -719 -518 -774 C ATOM 446 O THR A 57 -11.640 20.572 22.912 1.00 73.75 O ANISOU 446 O THR A 57 8368 7940 11715 -798 -503 -587 O ATOM 447 CB THR A 57 -13.255 22.234 25.086 1.00 77.99 C ANISOU 447 CB THR A 57 9009 8293 12332 -596 -798 -1227 C ATOM 448 OG1 THR A 57 -13.126 22.798 26.396 1.00 82.74 O ANISOU 448 OG1 THR A 57 9613 8812 13012 -489 -1033 -1609 O ATOM 449 CG2 THR A 57 -14.727 22.212 24.690 1.00 77.76 C ANISOU 449 CG2 THR A 57 9085 8386 12076 -545 -644 -1132 C ATOM 450 N GLY A 58 -13.637 19.577 23.225 1.00 70.31 N ANISOU 450 N GLY A 58 8198 7837 10679 -685 -365 -676 N ATOM 451 CA GLY A 58 -13.761 19.122 21.849 1.00 68.61 C ANISOU 451 CA GLY A 58 7946 7724 10399 -720 -189 -377 C ATOM 452 C GLY A 58 -12.845 17.956 21.551 1.00 66.72 C ANISOU 452 C GLY A 58 7712 7629 10010 -762 -152 -283 C ATOM 453 O GLY A 58 -12.772 17.002 22.330 1.00 66.67 O ANISOU 453 O GLY A 58 7813 7754 9766 -748 -188 -422 O ATOM 454 N ILE A 59 -12.140 18.029 20.425 1.00 64.55 N ANISOU 454 N ILE A 59 7311 7342 9874 -796 -74 -28 N ATOM 455 CA ILE A 59 -11.292 16.926 20.006 1.00 61.97 C ANISOU 455 CA ILE A 59 6982 7168 9397 -818 -32 74 C ATOM 456 C ILE A 59 -9.994 17.434 19.385 1.00 60.91 C ANISOU 456 C ILE A 59 6667 6914 9561 -861 -32 282 C ATOM 457 O ILE A 59 -9.963 17.928 18.257 1.00 61.09 O ANISOU 457 O ILE A 59 6560 6937 9716 -825 79 551 O ATOM 458 CB ILE A 59 -12.056 15.949 19.076 1.00 60.72 C ANISOU 458 CB ILE A 59 6883 7252 8938 -756 103 184 C ATOM 459 CG1 ILE A 59 -11.310 14.619 18.980 1.00 62.35 C ANISOU 459 CG1 ILE A 59 7121 7616 8952 -769 108 192 C ATOM 460 CG2 ILE A 59 -12.304 16.554 17.704 1.00 61.98 C ANISOU 460 CG2 ILE A 59 6920 7441 9187 -692 223 444 C ATOM 461 CD1 ILE A 59 -11.983 13.612 18.077 1.00 67.52 C ANISOU 461 CD1 ILE A 59 7809 8490 9357 -694 202 252 C ATOM 462 N SER A 60 -8.924 17.316 20.165 1.00 58.97 N ANISOU 462 N SER A 60 6400 6579 9426 -922 -155 166 N ATOM 463 CA SER A 60 -7.596 17.729 19.747 1.00 58.67 C ANISOU 463 CA SER A 60 6180 6410 9703 -973 -173 348 C ATOM 464 C SER A 60 -7.000 16.716 18.790 1.00 57.13 C ANISOU 464 C SER A 60 5967 6434 9306 -950 -52 574 C ATOM 465 O SER A 60 -7.507 15.606 18.644 1.00 56.82 O ANISOU 465 O SER A 60 6064 6624 8900 -908 5 522 O ATOM 466 CB SER A 60 -6.680 17.847 20.963 1.00 58.85 C ANISOU 466 CB SER A 60 6192 6281 9887 -1034 -366 106 C ATOM 467 OG SER A 60 -6.427 16.569 21.521 1.00 52.07 O ANISOU 467 OG SER A 60 5479 5625 8681 -1032 -385 -26 O ATOM 468 N MET A 61 -5.902 17.110 18.161 1.00 57.88 N ANISOU 468 N MET A 61 5874 6447 9671 -967 -21 823 N ATOM 469 CA MET A 61 -5.157 16.238 17.265 1.00 57.73 C ANISOU 469 CA MET A 61 5812 6638 9485 -922 82 1047 C ATOM 470 C MET A 61 -4.932 14.856 17.879 1.00 54.74 C ANISOU 470 C MET A 61 5605 6427 8765 -947 27 836 C ATOM 471 O MET A 61 -5.300 13.836 17.292 1.00 54.03 O ANISOU 471 O MET A 61 5598 6580 8351 -875 108 864 O ATOM 472 CB MET A 61 -3.804 16.868 16.943 1.00 59.87 C ANISOU 472 CB MET A 61 5853 6748 10147 -959 80 1294 C ATOM 473 CG MET A 61 -3.136 16.291 15.727 1.00 63.01 C ANISOU 473 CG MET A 61 6151 7374 10416 -860 229 1624 C ATOM 474 SD MET A 61 -3.813 17.017 14.234 1.00 67.86 S ANISOU 474 SD MET A 61 6607 8108 11067 -687 436 2009 S ATOM 475 CE MET A 61 -2.401 16.836 13.155 1.00 60.81 C ANISOU 475 CE MET A 61 5485 7357 10262 -583 565 2446 C ATOM 476 N SER A 62 -4.327 14.832 19.063 1.00 52.35 N ANISOU 476 N SER A 62 5340 5994 8556 -1034 -121 618 N ATOM 477 CA SER A 62 -4.020 13.575 19.746 1.00 49.05 C ANISOU 477 CA SER A 62 5062 5724 7851 -1052 -169 443 C ATOM 478 C SER A 62 -5.290 12.785 20.056 1.00 44.41 C ANISOU 478 C SER A 62 4655 5294 6925 -1004 -135 279 C ATOM 479 O SER A 62 -5.303 11.555 19.969 1.00 41.72 O ANISOU 479 O SER A 62 4397 5134 6322 -982 -95 258 O ATOM 480 CB SER A 62 -3.257 13.846 21.042 1.00 50.62 C ANISOU 480 CB SER A 62 5258 5767 8210 -1120 -343 221 C ATOM 481 OG SER A 62 -3.987 14.735 21.874 1.00 55.00 O ANISOU 481 OG SER A 62 5841 6171 8885 -1111 -445 5 O ATOM 482 N ALA A 63 -6.349 13.501 20.421 1.00 41.25 N ANISOU 482 N ALA A 63 4297 4811 6564 -984 -153 169 N ATOM 483 CA ALA A 63 -7.625 12.876 20.740 1.00 40.19 C ANISOU 483 CA ALA A 63 4309 4803 6158 -934 -115 37 C ATOM 484 C ALA A 63 -8.208 12.213 19.499 1.00 40.55 C ANISOU 484 C ALA A 63 4354 5023 6030 -873 15 192 C ATOM 485 O ALA A 63 -8.623 11.053 19.552 1.00 38.58 O ANISOU 485 O ALA A 63 4187 4919 5552 -847 42 126 O ATOM 486 CB ALA A 63 -8.594 13.905 21.302 1.00 38.72 C ANISOU 486 CB ALA A 63 4150 4490 6070 -913 -159 -91 C ATOM 487 N CYS A 64 -8.235 12.953 18.386 1.00 42.40 N ANISOU 487 N CYS A 64 4474 5243 6392 -832 89 397 N ATOM 488 CA CYS A 64 -8.681 12.397 17.099 1.00 43.56 C ANISOU 488 CA CYS A 64 4594 5593 6363 -726 197 538 C ATOM 489 C CYS A 64 -7.916 11.134 16.761 1.00 41.45 C ANISOU 489 C CYS A 64 4333 5491 5926 -703 201 556 C ATOM 490 O CYS A 64 -8.502 10.136 16.348 1.00 41.03 O ANISOU 490 O CYS A 64 4329 5599 5660 -635 223 490 O ATOM 491 CB CYS A 64 -8.488 13.397 15.956 1.00 43.10 C ANISOU 491 CB CYS A 64 4376 5529 6471 -652 287 812 C ATOM 492 SG CYS A 64 -9.679 14.714 15.957 1.00 52.86 S ANISOU 492 SG CYS A 64 5595 6626 7864 -635 317 823 S ATOM 493 N ARG A 65 -6.604 11.192 16.941 1.00 40.24 N ANISOU 493 N ARG A 65 4114 5281 5893 -758 168 635 N ATOM 494 CA ARG A 65 -5.736 10.088 16.575 1.00 41.32 C ANISOU 494 CA ARG A 65 4242 5570 5889 -732 174 677 C ATOM 495 C ARG A 65 -5.968 8.873 17.475 1.00 39.12 C ANISOU 495 C ARG A 65 4096 5330 5436 -779 116 452 C ATOM 496 O ARG A 65 -6.102 7.739 16.991 1.00 37.94 O ANISOU 496 O ARG A 65 3969 5338 5110 -716 133 420 O ATOM 497 CB ARG A 65 -4.275 10.542 16.631 1.00 44.40 C ANISOU 497 CB ARG A 65 4518 5867 6484 -788 154 828 C ATOM 498 CG ARG A 65 -3.313 9.642 15.889 1.00 53.90 C ANISOU 498 CG ARG A 65 5668 7251 7560 -722 191 957 C ATOM 499 CD ARG A 65 -3.652 9.580 14.390 1.00 60.50 C ANISOU 499 CD ARG A 65 6416 8311 8260 -534 301 1148 C ATOM 500 NE ARG A 65 -2.566 8.996 13.606 1.00 66.69 N ANISOU 500 NE ARG A 65 7110 9272 8958 -436 341 1318 N ATOM 501 CZ ARG A 65 -2.684 8.538 12.361 1.00 71.38 C ANISOU 501 CZ ARG A 65 7641 10139 9342 -227 410 1428 C ATOM 502 NH1 ARG A 65 -1.617 8.032 11.750 1.00 74.59 N ANISOU 502 NH1 ARG A 65 7964 10711 9668 -127 440 1579 N ATOM 503 NH2 ARG A 65 -3.853 8.577 11.723 1.00 71.62 N ANISOU 503 NH2 ARG A 65 7686 10294 9232 -95 441 1377 N ATOM 504 N GLU A 66 -6.025 9.109 18.781 1.00 36.24 N ANISOU 504 N GLU A 66 3805 4831 5135 -868 44 298 N ATOM 505 CA GLU A 66 -6.337 8.046 19.736 1.00 36.10 C ANISOU 505 CA GLU A 66 3894 4859 4964 -888 12 128 C ATOM 506 C GLU A 66 -7.648 7.332 19.379 1.00 34.67 C ANISOU 506 C GLU A 66 3759 4770 4643 -824 63 72 C ATOM 507 O GLU A 66 -7.713 6.100 19.353 1.00 33.46 O ANISOU 507 O GLU A 66 3623 4706 4384 -805 69 27 O ATOM 508 CB GLU A 66 -6.420 8.628 21.149 1.00 37.19 C ANISOU 508 CB GLU A 66 4089 4876 5165 -933 -66 -22 C ATOM 509 CG GLU A 66 -6.877 7.641 22.225 1.00 37.16 C ANISOU 509 CG GLU A 66 4179 4945 4996 -915 -72 -155 C ATOM 510 CD GLU A 66 -6.598 8.156 23.625 1.00 37.76 C ANISOU 510 CD GLU A 66 4291 4962 5093 -912 -163 -300 C ATOM 511 OE1 GLU A 66 -6.788 9.367 23.849 1.00 36.29 O ANISOU 511 OE1 GLU A 66 4089 4660 5041 -909 -222 -363 O ATOM 512 OE2 GLU A 66 -6.187 7.353 24.492 1.00 33.17 O ANISOU 512 OE2 GLU A 66 3744 4462 4399 -893 -181 -357 O ATOM 513 N ILE A 67 -8.687 8.112 19.095 1.00 35.27 N ANISOU 513 N ILE A 67 3838 4810 4752 -790 92 72 N ATOM 514 CA ILE A 67 -9.984 7.551 18.720 1.00 35.08 C ANISOU 514 CA ILE A 67 3840 4858 4631 -727 130 15 C ATOM 515 C ILE A 67 -9.910 6.824 17.375 1.00 34.76 C ANISOU 515 C ILE A 67 3729 4968 4509 -634 152 70 C ATOM 516 O ILE A 67 -10.441 5.717 17.238 1.00 33.10 O ANISOU 516 O ILE A 67 3521 4822 4233 -596 140 -23 O ATOM 517 CB ILE A 67 -11.088 8.633 18.662 1.00 36.41 C ANISOU 517 CB ILE A 67 4022 4961 4852 -704 156 11 C ATOM 518 CG1 ILE A 67 -11.376 9.187 20.067 1.00 37.89 C ANISOU 518 CG1 ILE A 67 4284 5030 5082 -753 117 -97 C ATOM 519 CG2 ILE A 67 -12.372 8.050 18.081 1.00 38.72 C ANISOU 519 CG2 ILE A 67 4315 5336 5059 -629 190 -37 C ATOM 520 CD1 ILE A 67 -12.098 10.540 20.071 1.00 36.51 C ANISOU 520 CD1 ILE A 67 4109 4754 5008 -740 122 -97 C ATOM 521 N ALA A 68 -9.256 7.444 16.391 1.00 33.14 N ANISOU 521 N ALA A 68 3442 4823 4326 -577 181 222 N ATOM 522 CA ALA A 68 -9.176 6.874 15.044 1.00 33.89 C ANISOU 522 CA ALA A 68 3458 5115 4304 -431 200 275 C ATOM 523 C ALA A 68 -8.483 5.514 15.058 1.00 33.65 C ANISOU 523 C ALA A 68 3428 5164 4196 -424 152 199 C ATOM 524 O ALA A 68 -8.952 4.554 14.436 1.00 32.69 O ANISOU 524 O ALA A 68 3278 5158 3986 -321 119 90 O ATOM 525 CB ALA A 68 -8.443 7.828 14.089 1.00 33.71 C ANISOU 525 CB ALA A 68 3325 5163 4319 -346 263 511 C ATOM 526 N LEU A 69 -7.376 5.439 15.787 1.00 34.84 N ANISOU 526 N LEU A 69 3598 5240 4399 -528 136 239 N ATOM 527 CA LEU A 69 -6.569 4.222 15.855 1.00 34.61 C ANISOU 527 CA LEU A 69 3564 5276 4309 -530 98 192 C ATOM 528 C LEU A 69 -7.242 3.133 16.687 1.00 34.29 C ANISOU 528 C LEU A 69 3581 5175 4272 -582 62 21 C ATOM 529 O LEU A 69 -7.373 2.001 16.237 1.00 33.31 O ANISOU 529 O LEU A 69 3420 5124 4112 -515 26 -68 O ATOM 530 CB LEU A 69 -5.176 4.543 16.410 1.00 35.50 C ANISOU 530 CB LEU A 69 3672 5326 4489 -624 92 297 C ATOM 531 CG LEU A 69 -4.272 5.364 15.484 1.00 36.40 C ANISOU 531 CG LEU A 69 3681 5507 4643 -559 137 516 C ATOM 532 CD1 LEU A 69 -2.921 5.647 16.146 1.00 36.31 C ANISOU 532 CD1 LEU A 69 3649 5397 4751 -669 114 602 C ATOM 533 CD2 LEU A 69 -4.063 4.668 14.159 1.00 37.15 C ANISOU 533 CD2 LEU A 69 3698 5835 4581 -377 156 570 C ATOM 534 N LEU A 70 -7.676 3.473 17.896 1.00 36.73 N ANISOU 534 N LEU A 70 3962 5353 4640 -680 69 -20 N ATOM 535 CA LEU A 70 -8.299 2.484 18.783 1.00 36.41 C ANISOU 535 CA LEU A 70 3950 5263 4620 -712 64 -119 C ATOM 536 C LEU A 70 -9.556 1.894 18.168 1.00 37.87 C ANISOU 536 C LEU A 70 4091 5466 4832 -637 58 -206 C ATOM 537 O LEU A 70 -9.877 0.725 18.394 1.00 36.73 O ANISOU 537 O LEU A 70 3906 5297 4752 -631 40 -273 O ATOM 538 CB LEU A 70 -8.647 3.102 20.137 1.00 37.38 C ANISOU 538 CB LEU A 70 4146 5290 4765 -776 82 -132 C ATOM 539 CG LEU A 70 -7.484 3.392 21.076 1.00 41.57 C ANISOU 539 CG LEU A 70 4711 5796 5286 -838 57 -109 C ATOM 540 CD1 LEU A 70 -7.998 4.096 22.335 1.00 43.06 C ANISOU 540 CD1 LEU A 70 4963 5927 5472 -844 54 -164 C ATOM 541 CD2 LEU A 70 -6.732 2.106 21.409 1.00 39.09 C ANISOU 541 CD2 LEU A 70 4379 5529 4945 -850 53 -104 C ATOM 542 N ARG A 71 -10.266 2.710 17.390 1.00 37.56 N ANISOU 542 N ARG A 71 4040 5460 4772 -574 68 -201 N ATOM 543 CA ARG A 71 -11.464 2.256 16.690 1.00 37.31 C ANISOU 543 CA ARG A 71 3952 5457 4766 -485 45 -304 C ATOM 544 C ARG A 71 -11.140 1.121 15.719 1.00 35.50 C ANISOU 544 C ARG A 71 3631 5332 4524 -380 -28 -397 C ATOM 545 O ARG A 71 -11.946 0.214 15.536 1.00 39.70 O ANISOU 545 O ARG A 71 4095 5833 5156 -335 -83 -532 O ATOM 546 CB ARG A 71 -12.122 3.433 15.944 1.00 37.01 C ANISOU 546 CB ARG A 71 3913 5469 4679 -416 73 -264 C ATOM 547 CG ARG A 71 -13.460 3.130 15.330 1.00 39.24 C ANISOU 547 CG ARG A 71 4143 5778 4988 -322 44 -380 C ATOM 548 CD ARG A 71 -14.497 2.912 16.436 1.00 46.02 C ANISOU 548 CD ARG A 71 5034 6486 5964 -410 67 -422 C ATOM 549 NE ARG A 71 -15.840 2.707 15.927 1.00 47.31 N ANISOU 549 NE ARG A 71 5136 6647 6192 -335 40 -524 N ATOM 550 CZ ARG A 71 -16.255 1.603 15.309 1.00 57.54 C ANISOU 550 CZ ARG A 71 6322 7959 7580 -256 -47 -669 C ATOM 551 NH1 ARG A 71 -17.513 1.524 14.897 1.00 60.49 N ANISOU 551 NH1 ARG A 71 6630 8315 8037 -190 -83 -770 N ATOM 552 NH2 ARG A 71 -15.426 0.581 15.091 1.00 52.85 N ANISOU 552 NH2 ARG A 71 5672 7391 7018 -236 -111 -728 N ATOM 553 N GLU A 72 -9.964 1.173 15.106 1.00 35.98 N ANISOU 553 N GLU A 72 3674 5510 4486 -330 -38 -331 N ATOM 554 CA GLU A 72 -9.558 0.186 14.102 1.00 36.99 C ANISOU 554 CA GLU A 72 3714 5777 4565 -190 -117 -430 C ATOM 555 C GLU A 72 -8.754 -0.978 14.678 1.00 36.73 C ANISOU 555 C GLU A 72 3670 5685 4599 -258 -152 -468 C ATOM 556 O GLU A 72 -8.798 -2.082 14.142 1.00 35.96 O ANISOU 556 O GLU A 72 3489 5626 4548 -164 -242 -617 O ATOM 557 CB GLU A 72 -8.701 0.852 13.021 1.00 37.42 C ANISOU 557 CB GLU A 72 3733 6034 4452 -54 -93 -305 C ATOM 558 CG GLU A 72 -9.349 2.013 12.290 1.00 38.87 C ANISOU 558 CG GLU A 72 3897 6310 4562 49 -42 -222 C ATOM 559 CD GLU A 72 -10.679 1.666 11.666 1.00 38.14 C ANISOU 559 CD GLU A 72 3754 6272 4468 178 -108 -409 C ATOM 560 OE1 GLU A 72 -10.740 0.714 10.858 1.00 35.43 O ANISOU 560 OE1 GLU A 72 3325 6062 4076 345 -211 -581 O ATOM 561 OE2 GLU A 72 -11.664 2.361 11.978 1.00 37.68 O ANISOU 561 OE2 GLU A 72 3732 6122 4464 124 -68 -398 O ATOM 562 N LEU A 73 -7.996 -0.719 15.741 1.00 35.76 N ANISOU 562 N LEU A 73 3622 5475 4490 -403 -93 -347 N ATOM 563 CA LEU A 73 -7.063 -1.708 16.280 1.00 36.47 C ANISOU 563 CA LEU A 73 3706 5536 4617 -460 -111 -346 C ATOM 564 C LEU A 73 -7.804 -2.828 17.007 1.00 36.18 C ANISOU 564 C LEU A 73 3626 5361 4759 -505 -129 -438 C ATOM 565 O LEU A 73 -8.714 -2.573 17.785 1.00 35.70 O ANISOU 565 O LEU A 73 3590 5196 4779 -565 -82 -419 O ATOM 566 CB LEU A 73 -6.039 -1.033 17.201 1.00 37.35 C ANISOU 566 CB LEU A 73 3896 5610 4684 -580 -53 -200 C ATOM 567 CG LEU A 73 -5.011 -0.154 16.473 1.00 38.07 C ANISOU 567 CG LEU A 73 3981 5810 4673 -541 -39 -73 C ATOM 568 CD1 LEU A 73 -4.305 0.762 17.457 1.00 41.22 C ANISOU 568 CD1 LEU A 73 4440 6119 5102 -668 -4 36 C ATOM 569 CD2 LEU A 73 -4.010 -0.999 15.705 1.00 39.86 C ANISOU 569 CD2 LEU A 73 4147 6169 4830 -451 -77 -72 C ATOM 570 N LYS A 74 -7.422 -4.069 16.720 1.00 37.55 N ANISOU 570 N LYS A 74 3717 5535 5014 -461 -194 -525 N ATOM 571 CA LYS A 74 -8.084 -5.246 17.286 1.00 36.92 C ANISOU 571 CA LYS A 74 3547 5302 5179 -490 -214 -593 C ATOM 572 C LYS A 74 -7.087 -6.397 17.444 1.00 36.30 C ANISOU 572 C LYS A 74 3414 5208 5170 -498 -246 -599 C ATOM 573 O LYS A 74 -6.716 -7.062 16.468 1.00 35.26 O ANISOU 573 O LYS A 74 3206 5144 5047 -389 -350 -737 O ATOM 574 CB LYS A 74 -9.258 -5.683 16.403 1.00 39.04 C ANISOU 574 CB LYS A 74 3700 5537 5598 -381 -313 -782 C ATOM 575 CG LYS A 74 -10.084 -6.823 16.951 0.00 41.20 C ANISOU 575 CG LYS A 74 3838 5607 6208 -414 -336 -834 C ATOM 576 CD LYS A 74 -11.302 -7.095 16.083 0.00 42.45 C ANISOU 576 CD LYS A 74 3870 5717 6540 -308 -452 -1040 C ATOM 577 CE LYS A 74 -12.120 -8.258 16.621 0.00 43.54 C ANISOU 577 CE LYS A 74 3832 5612 7100 -346 -479 -1073 C ATOM 578 NZ LYS A 74 -13.308 -8.548 15.771 0.00 44.86 N ANISOU 578 NZ LYS A 74 3851 5708 7484 -241 -619 -1303 N ATOM 579 N HIS A 75 -6.661 -6.617 18.686 1.00 33.15 N ANISOU 579 N HIS A 75 3051 4739 4807 -606 -158 -455 N ATOM 580 CA HIS A 75 -5.666 -7.621 19.007 1.00 33.19 C ANISOU 580 CA HIS A 75 3014 4730 4868 -626 -163 -422 C ATOM 581 C HIS A 75 -5.748 -7.916 20.508 1.00 34.00 C ANISOU 581 C HIS A 75 3118 4741 5060 -711 -49 -256 C ATOM 582 O HIS A 75 -5.998 -7.017 21.296 1.00 30.59 O ANISOU 582 O HIS A 75 2776 4333 4513 -752 30 -158 O ATOM 583 CB HIS A 75 -4.271 -7.119 18.626 1.00 32.31 C ANISOU 583 CB HIS A 75 2989 4773 4514 -621 -172 -377 C ATOM 584 CG HIS A 75 -3.202 -8.161 18.723 1.00 30.24 C ANISOU 584 CG HIS A 75 2682 4520 4289 -622 -194 -366 C ATOM 585 ND1 HIS A 75 -2.490 -8.390 19.881 1.00 32.59 N ANISOU 585 ND1 HIS A 75 3014 4792 4575 -710 -115 -224 N ATOM 586 CD2 HIS A 75 -2.718 -9.034 17.806 1.00 31.27 C ANISOU 586 CD2 HIS A 75 2730 4695 4455 -526 -291 -489 C ATOM 587 CE1 HIS A 75 -1.615 -9.359 19.674 1.00 33.60 C ANISOU 587 CE1 HIS A 75 3088 4935 4744 -688 -152 -242 C ATOM 588 NE2 HIS A 75 -1.735 -9.769 18.424 1.00 32.58 N ANISOU 588 NE2 HIS A 75 2887 4843 4649 -578 -262 -407 N ATOM 589 N PRO A 76 -5.559 -9.185 20.907 1.00 36.37 N ANISOU 589 N PRO A 76 3302 4946 5570 -714 -40 -222 N ATOM 590 CA PRO A 76 -5.747 -9.495 22.333 1.00 36.81 C ANISOU 590 CA PRO A 76 3330 4946 5710 -753 90 -25 C ATOM 591 C PRO A 76 -4.828 -8.734 23.297 1.00 34.54 C ANISOU 591 C PRO A 76 3184 4796 5143 -788 168 103 C ATOM 592 O PRO A 76 -5.217 -8.502 24.436 1.00 36.35 O ANISOU 592 O PRO A 76 3425 5042 5342 -778 271 239 O ATOM 593 CB PRO A 76 -5.487 -11.005 22.410 1.00 36.36 C ANISOU 593 CB PRO A 76 3106 4769 5939 -741 80 -1 C ATOM 594 CG PRO A 76 -5.731 -11.513 21.039 1.00 38.49 C ANISOU 594 CG PRO A 76 3285 4974 6367 -687 -78 -238 C ATOM 595 CD PRO A 76 -5.380 -10.400 20.091 1.00 37.47 C ANISOU 595 CD PRO A 76 3301 5015 5921 -657 -149 -363 C ATOM 596 N ASN A 77 -3.646 -8.327 22.842 1.00 32.47 N ANISOU 596 N ASN A 77 3011 4640 4684 -809 113 56 N ATOM 597 CA ASN A 77 -2.684 -7.638 23.703 1.00 32.16 C ANISOU 597 CA ASN A 77 3082 4712 4426 -841 154 144 C ATOM 598 C ASN A 77 -2.638 -6.120 23.534 1.00 32.06 C ANISOU 598 C ASN A 77 3189 4761 4231 -862 124 98 C ATOM 599 O ASN A 77 -1.736 -5.465 24.051 1.00 27.72 O ANISOU 599 O ASN A 77 2712 4283 3537 -889 118 127 O ATOM 600 CB ASN A 77 -1.298 -8.253 23.521 1.00 31.58 C ANISOU 600 CB ASN A 77 3001 4693 4304 -857 124 158 C ATOM 601 CG ASN A 77 -1.283 -9.727 23.858 1.00 33.20 C ANISOU 601 CG ASN A 77 3079 4823 4714 -836 162 223 C ATOM 602 OD1 ASN A 77 -0.982 -10.565 23.012 1.00 41.17 O ANISOU 602 OD1 ASN A 77 4012 5787 5842 -820 95 143 O ATOM 603 ND2 ASN A 77 -1.650 -10.055 25.093 1.00 34.90 N ANISOU 603 ND2 ASN A 77 3251 5028 4983 -815 272 373 N ATOM 604 N VAL A 78 -3.630 -5.569 22.837 1.00 31.72 N ANISOU 604 N VAL A 78 3149 4678 4226 -846 100 25 N ATOM 605 CA VAL A 78 -3.818 -4.124 22.758 1.00 32.48 C ANISOU 605 CA VAL A 78 3336 4802 4203 -861 87 2 C ATOM 606 C VAL A 78 -5.173 -3.797 23.375 1.00 32.55 C ANISOU 606 C VAL A 78 3349 4760 4260 -837 139 9 C ATOM 607 O VAL A 78 -6.177 -4.405 23.011 1.00 30.86 O ANISOU 607 O VAL A 78 3058 4477 4192 -809 150 -14 O ATOM 608 CB VAL A 78 -3.781 -3.630 21.297 1.00 33.85 C ANISOU 608 CB VAL A 78 3505 5004 4353 -838 25 -64 C ATOM 609 CG1 VAL A 78 -3.958 -2.106 21.243 1.00 31.07 C ANISOU 609 CG1 VAL A 78 3222 4657 3925 -856 24 -53 C ATOM 610 CG2 VAL A 78 -2.480 -4.064 20.620 1.00 29.41 C ANISOU 610 CG2 VAL A 78 2919 4516 3738 -829 -17 -50 C ATOM 611 N ILE A 79 -5.196 -2.863 24.322 1.00 34.13 N ANISOU 611 N ILE A 79 3624 4993 4351 -835 162 29 N ATOM 612 CA ILE A 79 -6.434 -2.509 25.021 1.00 35.79 C ANISOU 612 CA ILE A 79 3842 5184 4573 -788 218 47 C ATOM 613 C ILE A 79 -7.538 -2.156 24.022 1.00 36.67 C ANISOU 613 C ILE A 79 3936 5226 4769 -788 201 -15 C ATOM 614 O ILE A 79 -7.299 -1.432 23.046 1.00 35.10 O ANISOU 614 O ILE A 79 3770 5030 4535 -812 144 -76 O ATOM 615 CB ILE A 79 -6.226 -1.351 26.041 1.00 36.82 C ANISOU 615 CB ILE A 79 4061 5378 4551 -758 207 22 C ATOM 616 CG1 ILE A 79 -7.398 -1.282 27.024 1.00 37.84 C ANISOU 616 CG1 ILE A 79 4182 5537 4659 -663 285 69 C ATOM 617 CG2 ILE A 79 -6.047 -0.011 25.335 1.00 38.05 C ANISOU 617 CG2 ILE A 79 4278 5494 4685 -806 129 -67 C ATOM 618 CD1 ILE A 79 -7.181 -0.328 28.155 1.00 40.49 C ANISOU 618 CD1 ILE A 79 4588 5969 4827 -583 258 16 C ATOM 619 N SER A 80 -8.731 -2.700 24.262 1.00 38.03 N ANISOU 619 N SER A 80 4039 5344 5067 -749 258 22 N ATOM 620 CA SER A 80 -9.890 -2.486 23.393 1.00 38.22 C ANISOU 620 CA SER A 80 4030 5302 5191 -738 239 -44 C ATOM 621 C SER A 80 -10.689 -1.263 23.817 1.00 38.59 C ANISOU 621 C SER A 80 4155 5360 5145 -717 267 -49 C ATOM 622 O SER A 80 -11.033 -1.112 24.991 1.00 40.13 O ANISOU 622 O SER A 80 4369 5589 5291 -670 334 25 O ATOM 623 CB SER A 80 -10.822 -3.702 23.429 1.00 39.20 C ANISOU 623 CB SER A 80 4008 5327 5558 -710 275 -4 C ATOM 624 OG SER A 80 -10.250 -4.819 22.776 1.00 42.93 O ANISOU 624 OG SER A 80 4387 5757 6167 -720 217 -49 O ATOM 625 N LEU A 81 -10.988 -0.395 22.860 1.00 37.98 N ANISOU 625 N LEU A 81 4117 5275 5040 -727 218 -128 N ATOM 626 CA LEU A 81 -11.929 0.691 23.084 1.00 40.01 C ANISOU 626 CA LEU A 81 4428 5519 5253 -705 241 -142 C ATOM 627 C LEU A 81 -13.338 0.106 22.976 1.00 41.27 C ANISOU 627 C LEU A 81 4504 5618 5559 -667 282 -129 C ATOM 628 O LEU A 81 -13.756 -0.301 21.902 1.00 42.21 O ANISOU 628 O LEU A 81 4553 5701 5785 -660 236 -198 O ATOM 629 CB LEU A 81 -11.720 1.798 22.049 1.00 39.22 C ANISOU 629 CB LEU A 81 4375 5428 5099 -722 188 -199 C ATOM 630 CG LEU A 81 -12.662 2.999 22.067 1.00 38.73 C ANISOU 630 CG LEU A 81 4363 5340 5015 -701 204 -219 C ATOM 631 CD1 LEU A 81 -12.412 3.879 23.285 1.00 34.91 C ANISOU 631 CD1 LEU A 81 3956 4855 4451 -697 206 -222 C ATOM 632 CD2 LEU A 81 -12.490 3.798 20.780 1.00 33.66 C ANISOU 632 CD2 LEU A 81 3715 4712 4362 -698 169 -232 C ATOM 633 N GLN A 82 -14.058 0.041 24.092 1.00 41.91 N ANISOU 633 N GLN A 82 4573 5698 5651 -621 364 -42 N ATOM 634 CA GLN A 82 -15.415 -0.515 24.094 1.00 42.22 C ANISOU 634 CA GLN A 82 4507 5665 5872 -584 416 8 C ATOM 635 C GLN A 82 -16.450 0.479 23.570 1.00 41.45 C ANISOU 635 C GLN A 82 4452 5548 5749 -570 403 -58 C ATOM 636 O GLN A 82 -17.422 0.071 22.925 1.00 40.61 O ANISOU 636 O GLN A 82 4251 5368 5812 -560 391 -88 O ATOM 637 CB GLN A 82 -15.819 -0.976 25.500 1.00 43.39 C ANISOU 637 CB GLN A 82 4602 5844 6041 -509 534 182 C ATOM 638 CG GLN A 82 -14.902 -2.037 26.118 1.00 47.41 C ANISOU 638 CG GLN A 82 5045 6380 6589 -501 572 287 C ATOM 639 CD GLN A 82 -14.950 -3.379 25.404 1.00 52.23 C ANISOU 639 CD GLN A 82 5494 6857 7494 -546 545 294 C ATOM 640 OE1 GLN A 82 -15.927 -3.704 24.729 1.00 55.83 O ANISOU 640 OE1 GLN A 82 5846 7194 8171 -553 519 253 O ATOM 641 NE2 GLN A 82 -13.888 -4.171 25.558 1.00 51.45 N ANISOU 641 NE2 GLN A 82 5362 6771 7415 -567 538 328 N ATOM 642 N LYS A 83 -16.255 1.771 23.853 1.00 39.97 N ANISOU 642 N LYS A 83 4392 5418 5378 -564 396 -92 N ATOM 643 CA LYS A 83 -17.253 2.790 23.513 1.00 41.57 C ANISOU 643 CA LYS A 83 4637 5603 5555 -543 398 -135 C ATOM 644 C LYS A 83 -16.702 4.210 23.648 1.00 40.42 C ANISOU 644 C LYS A 83 4613 5488 5257 -552 361 -192 C ATOM 645 O LYS A 83 -15.863 4.471 24.504 1.00 40.63 O ANISOU 645 O LYS A 83 4693 5557 5189 -543 347 -194 O ATOM 646 CB LYS A 83 -18.474 2.638 24.433 1.00 43.35 C ANISOU 646 CB LYS A 83 4821 5824 5826 -469 491 -39 C ATOM 647 CG LYS A 83 -19.811 2.548 23.718 1.00 51.04 C ANISOU 647 CG LYS A 83 5719 6725 6948 -459 500 -52 C ATOM 648 CD LYS A 83 -20.966 2.436 24.718 1.00 58.85 C ANISOU 648 CD LYS A 83 6657 7718 7986 -376 607 82 C ATOM 649 CE LYS A 83 -22.046 1.458 24.251 1.00 61.48 C ANISOU 649 CE LYS A 83 6815 7937 8607 -377 626 131 C ATOM 650 NZ LYS A 83 -21.617 0.036 24.409 1.00 60.50 N ANISOU 650 NZ LYS A 83 6544 7748 8696 -395 637 212 N ATOM 651 N VAL A 84 -17.181 5.118 22.795 1.00 39.53 N ANISOU 651 N VAL A 84 4525 5348 5147 -559 337 -241 N ATOM 652 CA VAL A 84 -16.908 6.553 22.923 1.00 38.70 C ANISOU 652 CA VAL A 84 4502 5229 4973 -562 307 -282 C ATOM 653 C VAL A 84 -18.218 7.288 23.240 1.00 40.04 C ANISOU 653 C VAL A 84 4701 5380 5133 -505 346 -291 C ATOM 654 O VAL A 84 -19.189 7.141 22.508 1.00 42.52 O ANISOU 654 O VAL A 84 4972 5679 5504 -494 373 -280 O ATOM 655 CB VAL A 84 -16.324 7.146 21.626 1.00 38.36 C ANISOU 655 CB VAL A 84 4444 5170 4959 -601 264 -286 C ATOM 656 CG1 VAL A 84 -16.068 8.635 21.789 1.00 35.81 C ANISOU 656 CG1 VAL A 84 4170 4790 4648 -609 236 -303 C ATOM 657 CG2 VAL A 84 -15.029 6.413 21.208 1.00 35.21 C ANISOU 657 CG2 VAL A 84 4010 4808 4561 -641 229 -266 C ATOM 658 N PHE A 85 -18.244 8.064 24.327 1.00 38.20 N ANISOU 658 N PHE A 85 4533 5157 4824 -453 339 -329 N ATOM 659 CA PHE A 85 -19.403 8.894 24.662 1.00 37.28 C ANISOU 659 CA PHE A 85 4452 5031 4683 -385 367 -350 C ATOM 660 C PHE A 85 -19.087 10.347 24.354 1.00 37.05 C ANISOU 660 C PHE A 85 4468 4925 4686 -407 300 -430 C ATOM 661 O PHE A 85 -18.033 10.847 24.724 1.00 39.42 O ANISOU 661 O PHE A 85 4788 5195 4997 -424 223 -495 O ATOM 662 CB PHE A 85 -19.776 8.757 26.137 1.00 37.98 C ANISOU 662 CB PHE A 85 4563 5209 4657 -262 404 -343 C ATOM 663 CG PHE A 85 -20.228 7.384 26.526 1.00 40.05 C ANISOU 663 CG PHE A 85 4747 5534 4936 -222 498 -209 C ATOM 664 CD1 PHE A 85 -21.545 6.992 26.333 1.00 43.43 C ANISOU 664 CD1 PHE A 85 5112 5946 5444 -192 581 -118 C ATOM 665 CD2 PHE A 85 -19.346 6.487 27.101 1.00 41.16 C ANISOU 665 CD2 PHE A 85 4857 5737 5045 -212 506 -160 C ATOM 666 CE1 PHE A 85 -21.972 5.727 26.699 1.00 45.46 C ANISOU 666 CE1 PHE A 85 5256 6224 5792 -156 669 31 C ATOM 667 CE2 PHE A 85 -19.764 5.216 27.470 1.00 46.31 C ANISOU 667 CE2 PHE A 85 5406 6424 5765 -171 604 -4 C ATOM 668 CZ PHE A 85 -21.083 4.836 27.271 1.00 48.84 C ANISOU 668 CZ PHE A 85 5644 6705 6208 -145 685 98 C ATOM 669 N LEU A 86 -19.994 11.012 23.652 1.00 37.27 N ANISOU 669 N LEU A 86 4492 4907 4760 -403 326 -418 N ATOM 670 CA LEU A 86 -19.809 12.399 23.274 1.00 38.03 C ANISOU 670 CA LEU A 86 4603 4908 4938 -420 279 -457 C ATOM 671 C LEU A 86 -20.788 13.228 24.097 1.00 39.93 C ANISOU 671 C LEU A 86 4896 5136 5140 -331 280 -530 C ATOM 672 O LEU A 86 -22.003 13.123 23.935 1.00 38.91 O ANISOU 672 O LEU A 86 4769 5038 4979 -290 350 -489 O ATOM 673 CB LEU A 86 -20.042 12.598 21.771 1.00 37.82 C ANISOU 673 CB LEU A 86 4520 4864 4985 -457 316 -370 C ATOM 674 CG LEU A 86 -19.155 11.794 20.805 1.00 43.57 C ANISOU 674 CG LEU A 86 5187 5644 5725 -503 314 -301 C ATOM 675 CD1 LEU A 86 -19.659 11.912 19.367 1.00 42.31 C ANISOU 675 CD1 LEU A 86 4963 5533 5580 -470 355 -227 C ATOM 676 CD2 LEU A 86 -17.693 12.230 20.886 1.00 40.71 C ANISOU 676 CD2 LEU A 86 4808 5224 5436 -556 254 -289 C ATOM 677 N SER A 87 -20.244 14.041 24.990 1.00 42.25 N ANISOU 677 N SER A 87 5222 5386 5446 -289 190 -653 N ATOM 678 CA SER A 87 -21.039 14.858 25.882 1.00 43.99 C ANISOU 678 CA SER A 87 5490 5610 5614 -170 164 -762 C ATOM 679 C SER A 87 -21.235 16.228 25.226 1.00 45.12 C ANISOU 679 C SER A 87 5614 5594 5935 -205 125 -792 C ATOM 680 O SER A 87 -20.328 17.057 25.215 1.00 46.93 O ANISOU 680 O SER A 87 5807 5690 6332 -242 22 -870 O ATOM 681 CB SER A 87 -20.325 14.955 27.229 1.00 44.73 C ANISOU 681 CB SER A 87 5613 5764 5620 -66 60 -919 C ATOM 682 OG SER A 87 -21.130 15.585 28.198 1.00 50.79 O ANISOU 682 OG SER A 87 6424 6592 6283 100 32 -1038 O ATOM 683 N HIS A 88 -22.428 16.457 24.680 1.00 46.03 N ANISOU 683 N HIS A 88 5735 5712 6042 -188 210 -720 N ATOM 684 CA HIS A 88 -22.675 17.617 23.816 1.00 48.18 C ANISOU 684 CA HIS A 88 5969 5847 6490 -225 209 -687 C ATOM 685 C HIS A 88 -22.794 18.946 24.552 1.00 49.65 C ANISOU 685 C HIS A 88 6170 5912 6785 -154 109 -847 C ATOM 686 O HIS A 88 -22.388 19.975 24.015 1.00 49.75 O ANISOU 686 O HIS A 88 6114 5751 7037 -204 65 -836 O ATOM 687 CB HIS A 88 -23.917 17.397 22.941 1.00 48.13 C ANISOU 687 CB HIS A 88 5956 5899 6431 -219 328 -563 C ATOM 688 CG HIS A 88 -23.660 16.535 21.743 1.00 49.19 C ANISOU 688 CG HIS A 88 6032 6098 6560 -286 388 -428 C ATOM 689 ND1 HIS A 88 -23.819 16.989 20.450 1.00 53.27 N ANISOU 689 ND1 HIS A 88 6483 6599 7157 -300 437 -313 N ATOM 690 CD2 HIS A 88 -23.241 15.251 21.641 1.00 43.94 C ANISOU 690 CD2 HIS A 88 5353 5527 5817 -316 401 -397 C ATOM 691 CE1 HIS A 88 -23.518 16.019 19.606 1.00 47.07 C ANISOU 691 CE1 HIS A 88 5651 5916 6318 -319 465 -241 C ATOM 692 NE2 HIS A 88 -23.167 14.954 20.303 1.00 42.13 N ANISOU 692 NE2 HIS A 88 5056 5340 5613 -340 439 -298 N ATOM 693 N ALA A 89 -23.336 18.928 25.767 1.00 50.15 N ANISOU 693 N ALA A 89 6301 6065 6689 -20 74 -987 N ATOM 694 CA ALA A 89 -23.525 20.165 26.541 1.00 53.05 C ANISOU 694 CA ALA A 89 6681 6339 7138 88 -46 -1189 C ATOM 695 C ALA A 89 -22.199 20.820 26.959 1.00 55.34 C ANISOU 695 C ALA A 89 6915 6479 7634 71 -226 -1366 C ATOM 696 O ALA A 89 -22.058 22.040 26.879 1.00 57.87 O ANISOU 696 O ALA A 89 7176 6596 8217 69 -329 -1472 O ATOM 697 CB ALA A 89 -24.399 19.900 27.763 1.00 51.99 C ANISOU 697 CB ALA A 89 6624 6394 6738 283 -38 -1291 C ATOM 698 N ASP A 90 -21.234 20.009 27.390 1.00 57.56 N ANISOU 698 N ASP A 90 7197 6845 7827 59 -268 -1396 N ATOM 699 CA ASP A 90 -19.898 20.504 27.781 1.00 60.38 C ANISOU 699 CA ASP A 90 7488 7066 8388 39 -448 -1565 C ATOM 700 C ASP A 90 -18.799 20.173 26.763 1.00 60.90 C ANISOU 700 C ASP A 90 7470 7027 8639 -146 -415 -1387 C ATOM 701 O ASP A 90 -17.629 20.477 26.993 1.00 63.18 O ANISOU 701 O ASP A 90 7687 7197 9122 -183 -550 -1489 O ATOM 702 CB ASP A 90 -19.505 19.963 29.164 1.00 61.67 C ANISOU 702 CB ASP A 90 7702 7419 8313 202 -548 -1765 C ATOM 703 CG ASP A 90 -19.447 18.435 29.216 1.00 59.10 C ANISOU 703 CG ASP A 90 7424 7319 7712 188 -407 -1588 C ATOM 704 OD1 ASP A 90 -19.819 17.772 28.226 1.00 52.24 O ANISOU 704 OD1 ASP A 90 6555 6460 6832 61 -249 -1348 O ATOM 705 OD2 ASP A 90 -19.037 17.898 30.263 1.00 59.74 O ANISOU 705 OD2 ASP A 90 7530 7572 7598 321 -462 -1697 O ATOM 706 N ARG A 91 -19.179 19.545 25.651 1.00 60.87 N ANISOU 706 N ARG A 91 7469 7083 8578 -242 -244 -1131 N ATOM 707 CA ARG A 91 -18.242 19.173 24.583 1.00 60.58 C ANISOU 707 CA ARG A 91 7352 6998 8668 -380 -193 -938 C ATOM 708 C ARG A 91 -17.051 18.345 25.080 1.00 59.16 C ANISOU 708 C ARG A 91 7172 6883 8422 -407 -257 -988 C ATOM 709 O ARG A 91 -15.912 18.528 24.636 1.00 60.91 O ANISOU 709 O ARG A 91 7301 6992 8849 -495 -303 -929 O ATOM 710 CB ARG A 91 -17.786 20.415 23.807 1.00 63.32 C ANISOU 710 CB ARG A 91 7566 7103 9391 -448 -227 -858 C ATOM 711 CG ARG A 91 -18.940 21.123 23.089 1.00 67.71 C ANISOU 711 CG ARG A 91 8108 7615 10002 -425 -127 -747 C ATOM 712 CD ARG A 91 -18.513 21.770 21.772 1.00 71.62 C ANISOU 712 CD ARG A 91 8453 7980 10780 -496 -51 -492 C ATOM 713 NE ARG A 91 -17.487 22.799 21.967 1.00 75.36 N ANISOU 713 NE ARG A 91 8782 8186 11665 -540 -179 -532 N ATOM 714 CZ ARG A 91 -16.199 22.690 21.627 1.00 76.34 C ANISOU 714 CZ ARG A 91 8791 8236 11979 -614 -204 -422 C ATOM 715 NH1 ARG A 91 -15.721 21.590 21.044 1.00 71.44 N ANISOU 715 NH1 ARG A 91 8194 7804 11147 -647 -110 -267 N ATOM 716 NH2 ARG A 91 -15.374 23.705 21.868 1.00 78.09 N ANISOU 716 NH2 ARG A 91 8857 8177 12638 -651 -334 -471 N ATOM 717 N LYS A 92 -17.333 17.419 25.994 1.00 55.28 N ANISOU 717 N LYS A 92 6772 6583 7650 -321 -247 -1070 N ATOM 718 CA LYS A 92 -16.319 16.517 26.519 1.00 51.74 C ANISOU 718 CA LYS A 92 6330 6230 7100 -328 -288 -1102 C ATOM 719 C LYS A 92 -16.425 15.152 25.846 1.00 47.61 C ANISOU 719 C LYS A 92 5823 5844 6421 -391 -143 -903 C ATOM 720 O LYS A 92 -17.507 14.737 25.429 1.00 46.35 O ANISOU 720 O LYS A 92 5691 5758 6161 -376 -27 -803 O ATOM 721 CB LYS A 92 -16.469 16.373 28.032 1.00 51.63 C ANISOU 721 CB LYS A 92 6378 6357 6883 -156 -371 -1309 C ATOM 722 CG LYS A 92 -16.129 17.632 28.804 1.00 56.17 C ANISOU 722 CG LYS A 92 6920 6805 7615 -65 -570 -1579 C ATOM 723 CD LYS A 92 -14.752 18.211 28.629 0.00 58.41 C ANISOU 723 CD LYS A 92 7100 6890 8203 -160 -722 -1663 C ATOM 724 CE LYS A 92 -13.696 17.321 29.262 0.00 58.44 C ANISOU 724 CE LYS A 92 7109 7026 8069 -138 -775 -1717 C ATOM 725 NZ LYS A 92 -12.330 17.897 29.124 0.00 59.60 N ANISOU 725 NZ LYS A 92 7139 6969 8539 -230 -934 -1803 N ATOM 726 N VAL A 93 -15.292 14.464 25.740 1.00 44.94 N ANISOU 726 N VAL A 93 5456 5532 6088 -456 -163 -861 N ATOM 727 CA VAL A 93 -15.228 13.144 25.130 1.00 42.21 C ANISOU 727 CA VAL A 93 5110 5301 5628 -509 -55 -706 C ATOM 728 C VAL A 93 -14.829 12.110 26.174 1.00 40.69 C ANISOU 728 C VAL A 93 4950 5248 5261 -450 -63 -752 C ATOM 729 O VAL A 93 -13.879 12.331 26.927 1.00 40.18 O ANISOU 729 O VAL A 93 4881 5178 5208 -426 -170 -869 O ATOM 730 CB VAL A 93 -14.186 13.108 23.993 1.00 42.17 C ANISOU 730 CB VAL A 93 5027 5227 5767 -620 -53 -582 C ATOM 731 CG1 VAL A 93 -14.155 11.722 23.346 1.00 37.16 C ANISOU 731 CG1 VAL A 93 4387 4719 5012 -648 37 -462 C ATOM 732 CG2 VAL A 93 -14.482 14.190 22.963 1.00 43.29 C ANISOU 732 CG2 VAL A 93 5107 5249 6094 -650 -29 -492 C ATOM 733 N TRP A 94 -15.532 10.979 26.197 1.00 37.47 N ANISOU 733 N TRP A 94 4557 4960 4721 -422 46 -654 N ATOM 734 CA TRP A 94 -15.233 9.895 27.139 1.00 39.22 C ANISOU 734 CA TRP A 94 4784 5320 4797 -355 72 -639 C ATOM 735 C TRP A 94 -14.918 8.601 26.417 1.00 38.51 C ANISOU 735 C TRP A 94 4648 5256 4727 -439 143 -502 C ATOM 736 O TRP A 94 -15.654 8.206 25.518 1.00 40.75 O ANISOU 736 O TRP A 94 4902 5516 5066 -479 210 -420 O ATOM 737 CB TRP A 94 -16.414 9.622 28.050 1.00 39.31 C ANISOU 737 CB TRP A 94 4816 5452 4668 -208 149 -617 C ATOM 738 CG TRP A 94 -16.780 10.743 28.929 1.00 40.23 C ANISOU 738 CG TRP A 94 4978 5590 4717 -74 75 -770 C ATOM 739 CD1 TRP A 94 -17.447 11.882 28.579 1.00 37.94 C ANISOU 739 CD1 TRP A 94 4710 5196 4511 -77 42 -844 C ATOM 740 CD2 TRP A 94 -16.542 10.830 30.334 1.00 44.19 C ANISOU 740 CD2 TRP A 94 5499 6247 5044 114 20 -883 C ATOM 741 NE1 TRP A 94 -17.623 12.682 29.683 1.00 40.49 N ANISOU 741 NE1 TRP A 94 5066 5579 4738 91 -45 -1016 N ATOM 742 CE2 TRP A 94 -17.076 12.060 30.773 1.00 40.25 C ANISOU 742 CE2 TRP A 94 5035 5724 4533 224 -65 -1053 C ATOM 743 CE3 TRP A 94 -15.920 9.992 31.264 1.00 41.77 C ANISOU 743 CE3 TRP A 94 5175 6113 4581 223 31 -861 C ATOM 744 CZ2 TRP A 94 -17.009 12.470 32.103 1.00 46.69 C ANISOU 744 CZ2 TRP A 94 5871 6699 5172 457 -156 -1229 C ATOM 745 CZ3 TRP A 94 -15.856 10.403 32.588 1.00 44.66 C ANISOU 745 CZ3 TRP A 94 5560 6655 4755 460 -44 -1011 C ATOM 746 CH2 TRP A 94 -16.399 11.629 32.993 1.00 45.81 C ANISOU 746 CH2 TRP A 94 5742 6788 4878 583 -145 -1207 C ATOM 747 N LEU A 95 -13.833 7.942 26.831 1.00 39.47 N ANISOU 747 N LEU A 95 4756 5431 4809 -451 115 -499 N ATOM 748 CA LEU A 95 -13.457 6.624 26.318 1.00 36.99 C ANISOU 748 CA LEU A 95 4392 5146 4515 -511 171 -387 C ATOM 749 C LEU A 95 -13.760 5.559 27.359 1.00 36.71 C ANISOU 749 C LEU A 95 4332 5229 4386 -414 249 -311 C ATOM 750 O LEU A 95 -13.461 5.738 28.536 1.00 38.02 O ANISOU 750 O LEU A 95 4523 5497 4426 -304 228 -356 O ATOM 751 CB LEU A 95 -11.964 6.577 25.989 1.00 38.12 C ANISOU 751 CB LEU A 95 4523 5265 4696 -593 98 -405 C ATOM 752 CG LEU A 95 -11.383 7.692 25.121 1.00 39.77 C ANISOU 752 CG LEU A 95 4722 5361 5026 -671 26 -436 C ATOM 753 CD1 LEU A 95 -9.886 7.447 24.858 1.00 39.13 C ANISOU 753 CD1 LEU A 95 4607 5270 4990 -740 -28 -413 C ATOM 754 CD2 LEU A 95 -12.151 7.822 23.818 1.00 39.70 C ANISOU 754 CD2 LEU A 95 4687 5314 5085 -701 81 -363 C ATOM 755 N LEU A 96 -14.343 4.448 26.915 1.00 36.59 N ANISOU 755 N LEU A 96 4248 5204 4451 -436 334 -194 N ATOM 756 CA LEU A 96 -14.682 3.332 27.787 1.00 36.61 C ANISOU 756 CA LEU A 96 4181 5289 4438 -347 432 -61 C ATOM 757 C LEU A 96 -13.810 2.128 27.435 1.00 36.69 C ANISOU 757 C LEU A 96 4125 5283 4533 -418 437 2 C ATOM 758 O LEU A 96 -13.658 1.786 26.261 1.00 36.31 O ANISOU 758 O LEU A 96 4045 5145 4606 -519 401 -25 O ATOM 759 CB LEU A 96 -16.160 2.980 27.629 1.00 36.79 C ANISOU 759 CB LEU A 96 4136 5274 4568 -311 524 36 C ATOM 760 CG LEU A 96 -16.712 1.886 28.545 1.00 41.04 C ANISOU 760 CG LEU A 96 4561 5879 5151 -202 653 232 C ATOM 761 CD1 LEU A 96 -16.723 2.348 29.997 1.00 45.52 C ANISOU 761 CD1 LEU A 96 5169 6632 5493 -15 699 270 C ATOM 762 CD2 LEU A 96 -18.103 1.486 28.090 1.00 45.32 C ANISOU 762 CD2 LEU A 96 5004 6326 5891 -205 723 323 C ATOM 763 N PHE A 97 -13.226 1.511 28.460 1.00 38.24 N ANISOU 763 N PHE A 97 4295 5586 4647 -341 478 80 N ATOM 764 CA PHE A 97 -12.396 0.311 28.319 1.00 37.14 C ANISOU 764 CA PHE A 97 4085 5440 4588 -389 495 158 C ATOM 765 C PHE A 97 -12.774 -0.665 29.412 1.00 39.75 C ANISOU 765 C PHE A 97 4312 5862 4928 -261 627 356 C ATOM 766 O PHE A 97 -13.309 -0.261 30.446 1.00 41.70 O ANISOU 766 O PHE A 97 4570 6238 5036 -107 688 413 O ATOM 767 CB PHE A 97 -10.909 0.620 28.531 1.00 36.01 C ANISOU 767 CB PHE A 97 4009 5356 4318 -419 408 70 C ATOM 768 CG PHE A 97 -10.391 1.769 27.730 1.00 35.67 C ANISOU 768 CG PHE A 97 4048 5240 4264 -513 290 -84 C ATOM 769 CD1 PHE A 97 -9.865 1.566 26.465 1.00 34.80 C ANISOU 769 CD1 PHE A 97 3921 5045 4256 -631 245 -103 C ATOM 770 CD2 PHE A 97 -10.389 3.051 28.255 1.00 36.16 C ANISOU 770 CD2 PHE A 97 4184 5326 4229 -462 223 -201 C ATOM 771 CE1 PHE A 97 -9.366 2.624 25.730 1.00 36.36 C ANISOU 771 CE1 PHE A 97 4164 5189 4464 -696 162 -186 C ATOM 772 CE2 PHE A 97 -9.893 4.112 27.524 1.00 37.53 C ANISOU 772 CE2 PHE A 97 4397 5404 4459 -550 123 -308 C ATOM 773 CZ PHE A 97 -9.382 3.899 26.256 1.00 33.63 C ANISOU 773 CZ PHE A 97 3876 4832 4072 -667 107 -275 C ATOM 774 N ASP A 98 -12.451 -1.936 29.203 1.00 39.96 N ANISOU 774 N ASP A 98 4228 5835 5120 -302 671 469 N ATOM 775 CA ASP A 98 -12.479 -2.916 30.279 1.00 42.44 C ANISOU 775 CA ASP A 98 4424 6245 5457 -176 804 695 C ATOM 776 C ASP A 98 -11.365 -2.577 31.267 1.00 42.07 C ANISOU 776 C ASP A 98 4456 6396 5132 -78 783 667 C ATOM 777 O ASP A 98 -10.252 -2.233 30.867 1.00 41.00 O ANISOU 777 O ASP A 98 4409 6250 4919 -172 666 511 O ATOM 778 CB ASP A 98 -12.277 -4.338 29.744 1.00 44.06 C ANISOU 778 CB ASP A 98 4477 6311 5951 -257 835 802 C ATOM 779 CG ASP A 98 -13.457 -4.840 28.920 1.00 49.73 C ANISOU 779 CG ASP A 98 5069 6833 6994 -316 847 826 C ATOM 780 OD1 ASP A 98 -14.597 -4.340 29.090 1.00 49.60 O ANISOU 780 OD1 ASP A 98 5042 6812 6992 -260 894 864 O ATOM 781 OD2 ASP A 98 -13.236 -5.759 28.101 1.00 55.12 O ANISOU 781 OD2 ASP A 98 5652 7365 7927 -407 796 792 O ATOM 782 N TYR A 99 -11.672 -2.683 32.553 1.00 42.76 N ANISOU 782 N TYR A 99 4496 6678 5074 132 895 824 N ATOM 783 CA TYR A 99 -10.720 -2.368 33.607 1.00 42.96 C ANISOU 783 CA TYR A 99 4579 6933 4810 282 867 781 C ATOM 784 C TYR A 99 -9.649 -3.451 33.720 1.00 42.09 C ANISOU 784 C TYR A 99 4398 6845 4748 252 899 889 C ATOM 785 O TYR A 99 -9.960 -4.632 33.835 1.00 43.88 O ANISOU 785 O TYR A 99 4469 7035 5167 277 1038 1139 O ATOM 786 CB TYR A 99 -11.443 -2.221 34.953 1.00 45.31 C ANISOU 786 CB TYR A 99 4826 7484 4905 573 989 933 C ATOM 787 CG TYR A 99 -10.547 -1.692 36.046 1.00 48.91 C ANISOU 787 CG TYR A 99 5350 8215 5021 775 920 815 C ATOM 788 CD1 TYR A 99 -10.038 -0.402 35.983 1.00 50.23 C ANISOU 788 CD1 TYR A 99 5664 8388 5034 752 721 484 C ATOM 789 CD2 TYR A 99 -10.192 -2.485 37.134 1.00 52.25 C ANISOU 789 CD2 TYR A 99 5668 8887 5299 1002 1045 1032 C ATOM 790 CE1 TYR A 99 -9.202 0.089 36.973 1.00 56.45 C ANISOU 790 CE1 TYR A 99 6494 9410 5543 947 621 328 C ATOM 791 CE2 TYR A 99 -9.359 -2.000 38.132 1.00 56.48 C ANISOU 791 CE2 TYR A 99 6258 9701 5503 1217 960 890 C ATOM 792 CZ TYR A 99 -8.868 -0.711 38.045 1.00 57.27 C ANISOU 792 CZ TYR A 99 6505 9789 5466 1186 735 516 C ATOM 793 OH TYR A 99 -8.038 -0.219 39.026 1.00 67.27 O ANISOU 793 OH TYR A 99 7807 11316 6438 1409 616 329 O ATOM 794 N ALA A 100 -8.388 -3.037 33.695 1.00 41.21 N ANISOU 794 N ALA A 100 4386 6780 4493 202 768 707 N ATOM 795 CA ALA A 100 -7.277 -3.950 33.908 1.00 41.59 C ANISOU 795 CA ALA A 100 4381 6880 4539 193 789 792 C ATOM 796 C ALA A 100 -6.862 -3.809 35.361 1.00 45.24 C ANISOU 796 C ALA A 100 4838 7650 4701 456 823 835 C ATOM 797 O ALA A 100 -6.400 -2.749 35.780 1.00 44.23 O ANISOU 797 O ALA A 100 4817 7637 4352 530 685 604 O ATOM 798 CB ALA A 100 -6.125 -3.621 32.980 1.00 39.14 C ANISOU 798 CB ALA A 100 4166 6445 4261 -9 628 585 C ATOM 799 N GLU A 101 -7.066 -4.876 36.131 1.00 43.38 N ANISOU 799 N GLU A 101 4631 6977 4874 -489 1410 -175 N ATOM 800 CA GLU A 101 -6.762 -4.879 37.558 1.00 45.39 C ANISOU 800 CA GLU A 101 4957 7386 4904 -574 1518 -208 C ATOM 801 C GLU A 101 -5.335 -4.396 37.796 1.00 44.83 C ANISOU 801 C GLU A 101 5047 7258 4727 -544 1433 -248 C ATOM 802 O GLU A 101 -5.109 -3.469 38.572 1.00 45.61 O ANISOU 802 O GLU A 101 5170 7425 4733 -517 1516 -401 O ATOM 803 CB GLU A 101 -6.953 -6.289 38.136 1.00 48.28 C ANISOU 803 CB GLU A 101 5349 7851 5145 -738 1534 -28 C ATOM 804 CG GLU A 101 -7.048 -6.353 39.654 1.00 52.00 C ANISOU 804 CG GLU A 101 5851 8535 5372 -848 1680 -45 C ATOM 805 CD GLU A 101 -8.455 -6.101 40.169 1.00 62.81 C ANISOU 805 CD GLU A 101 7050 10062 6752 -876 1882 -135 C ATOM 806 OE1 GLU A 101 -8.688 -5.016 40.745 1.00 63.24 O ANISOU 806 OE1 GLU A 101 7062 10204 6764 -815 2011 -335 O ATOM 807 OE2 GLU A 101 -9.325 -6.991 40.001 1.00 67.32 O ANISOU 807 OE2 GLU A 101 7525 10668 7386 -961 1915 -16 O ATOM 808 N HIS A 102 -4.384 -5.000 37.081 1.00 42.46 N ANISOU 808 N HIS A 102 4847 6830 4457 -546 1267 -124 N ATOM 809 CA HIS A 102 -2.967 -4.797 37.348 1.00 40.85 C ANISOU 809 CA HIS A 102 4789 6584 4147 -541 1174 -127 C ATOM 810 C HIS A 102 -2.259 -4.018 36.255 1.00 39.65 C ANISOU 810 C HIS A 102 4663 6258 4145 -421 1066 -186 C ATOM 811 O HIS A 102 -2.739 -3.927 35.117 1.00 39.23 O ANISOU 811 O HIS A 102 4537 6100 4268 -352 1025 -174 O ATOM 812 CB HIS A 102 -2.273 -6.151 37.502 1.00 39.71 C ANISOU 812 CB HIS A 102 4739 6433 3914 -643 1071 70 C ATOM 813 CG HIS A 102 -2.975 -7.079 38.437 1.00 42.31 C ANISOU 813 CG HIS A 102 5046 6914 4116 -776 1159 179 C ATOM 814 ND1 HIS A 102 -2.952 -6.914 39.803 1.00 46.41 N ANISOU 814 ND1 HIS A 102 5602 7619 4411 -856 1258 151 N ATOM 815 CD2 HIS A 102 -3.739 -8.169 38.200 1.00 46.50 C ANISOU 815 CD2 HIS A 102 5517 7442 4708 -854 1168 318 C ATOM 816 CE1 HIS A 102 -3.673 -7.863 40.368 1.00 53.68 C ANISOU 816 CE1 HIS A 102 6490 8650 5254 -978 1328 283 C ATOM 817 NE2 HIS A 102 -4.162 -8.638 39.418 1.00 50.24 N ANISOU 817 NE2 HIS A 102 5993 8093 5001 -980 1275 386 N ATOM 818 N ASP A 103 -1.097 -3.478 36.613 1.00 39.23 N ANISOU 818 N ASP A 103 4713 6183 4009 -406 1016 -243 N ATOM 819 CA ASP A 103 -0.154 -2.916 35.646 1.00 37.43 C ANISOU 819 CA ASP A 103 4533 5794 3896 -321 902 -264 C ATOM 820 C ASP A 103 1.270 -3.321 36.028 1.00 37.17 C ANISOU 820 C ASP A 103 4623 5757 3744 -371 798 -202 C ATOM 821 O ASP A 103 1.525 -3.731 37.166 1.00 37.24 O ANISOU 821 O ASP A 103 4683 5895 3572 -458 819 -174 O ATOM 822 CB ASP A 103 -0.297 -1.401 35.593 1.00 39.52 C ANISOU 822 CB ASP A 103 4761 6009 4246 -225 963 -446 C ATOM 823 CG ASP A 103 0.107 -0.738 36.885 1.00 40.27 C ANISOU 823 CG ASP A 103 4907 6208 4185 -261 1037 -585 C ATOM 824 OD1 ASP A 103 -0.778 -0.463 37.711 1.00 46.11 O ANISOU 824 OD1 ASP A 103 5586 7070 4862 -280 1177 -685 O ATOM 825 OD2 ASP A 103 1.317 -0.508 37.078 1.00 44.32 O ANISOU 825 OD2 ASP A 103 5516 6691 4633 -277 957 -601 O ATOM 826 N LEU A 104 2.200 -3.209 35.086 1.00 35.55 N ANISOU 826 N LEU A 104 4458 5413 3634 -319 684 -175 N ATOM 827 CA LEU A 104 3.540 -3.758 35.293 1.00 35.82 C ANISOU 827 CA LEU A 104 4586 5433 3593 -360 573 -97 C ATOM 828 C LEU A 104 4.391 -2.931 36.279 1.00 36.30 C ANISOU 828 C LEU A 104 4706 5558 3528 -379 576 -206 C ATOM 829 O LEU A 104 5.291 -3.469 36.926 1.00 36.54 O ANISOU 829 O LEU A 104 4802 5645 3438 -439 502 -137 O ATOM 830 CB LEU A 104 4.247 -3.953 33.951 1.00 36.02 C ANISOU 830 CB LEU A 104 4621 5305 3761 -304 466 -42 C ATOM 831 CG LEU A 104 5.180 -5.155 33.802 1.00 39.80 C ANISOU 831 CG LEU A 104 5151 5747 4224 -343 356 94 C ATOM 832 CD1 LEU A 104 4.537 -6.434 34.327 1.00 39.02 C ANISOU 832 CD1 LEU A 104 5046 5713 4067 -422 369 221 C ATOM 833 CD2 LEU A 104 5.589 -5.332 32.341 1.00 36.96 C ANISOU 833 CD2 LEU A 104 4780 5249 4014 -286 285 119 C ATOM 834 N TRP A 105 4.075 -1.646 36.430 1.00 36.98 N ANISOU 834 N TRP A 105 4765 5638 3647 -330 656 -376 N ATOM 835 CA TRP A 105 4.771 -0.781 37.394 1.00 37.89 C ANISOU 835 CA TRP A 105 4931 5816 3648 -356 669 -515 C ATOM 836 C TRP A 105 4.522 -1.209 38.853 1.00 39.55 C ANISOU 836 C TRP A 105 5171 6236 3621 -459 730 -520 C ATOM 837 O TRP A 105 5.455 -1.250 39.661 1.00 41.16 O ANISOU 837 O TRP A 105 5444 6523 3670 -523 668 -526 O ATOM 838 CB TRP A 105 4.349 0.677 37.184 1.00 37.31 C ANISOU 838 CB TRP A 105 4814 5665 3698 -278 753 -706 C ATOM 839 CG TRP A 105 5.083 1.686 38.013 1.00 39.74 C ANISOU 839 CG TRP A 105 5170 6000 3928 -301 764 -879 C ATOM 840 CD1 TRP A 105 6.178 2.411 37.640 1.00 43.41 C ANISOU 840 CD1 TRP A 105 5673 6349 4472 -280 683 -933 C ATOM 841 CD2 TRP A 105 4.754 2.114 39.343 1.00 47.94 C ANISOU 841 CD2 TRP A 105 6219 7197 4798 -357 868 -1036 C ATOM 842 NE1 TRP A 105 6.560 3.249 38.655 1.00 47.87 N ANISOU 842 NE1 TRP A 105 6272 6978 4937 -323 719 -1116 N ATOM 843 CE2 TRP A 105 5.703 3.090 39.713 1.00 48.01 C ANISOU 843 CE2 TRP A 105 6277 7170 4794 -369 833 -1190 C ATOM 844 CE3 TRP A 105 3.755 1.760 40.259 1.00 49.64 C ANISOU 844 CE3 TRP A 105 6405 7590 4865 -408 992 -1067 C ATOM 845 CZ2 TRP A 105 5.686 3.717 40.959 1.00 51.56 C ANISOU 845 CZ2 TRP A 105 6754 7757 5082 -429 912 -1388 C ATOM 846 CZ3 TRP A 105 3.736 2.386 41.499 1.00 55.34 C ANISOU 846 CZ3 TRP A 105 7152 8460 5414 -466 1082 -1257 C ATOM 847 CH2 TRP A 105 4.698 3.355 41.838 1.00 54.56 C ANISOU 847 CH2 TRP A 105 7109 8322 5301 -475 1038 -1423 C ATOM 848 N HIS A 106 3.269 -1.509 39.184 1.00 38.30 N ANISOU 848 N HIS A 106 4954 6171 3428 -480 849 -516 N ATOM 849 CA HIS A 106 2.918 -2.038 40.514 1.00 40.10 C ANISOU 849 CA HIS A 106 5205 6615 3416 -591 921 -492 C ATOM 850 C HIS A 106 3.403 -3.475 40.704 1.00 38.87 C ANISOU 850 C HIS A 106 5104 6502 3163 -675 813 -252 C ATOM 851 O HIS A 106 3.821 -3.844 41.797 1.00 38.06 O ANISOU 851 O HIS A 106 5063 6555 2841 -772 794 -202 O ATOM 852 CB HIS A 106 1.403 -1.982 40.757 1.00 41.51 C ANISOU 852 CB HIS A 106 5287 6883 3603 -595 1092 -548 C ATOM 853 CG HIS A 106 0.881 -0.600 40.992 1.00 43.68 C ANISOU 853 CG HIS A 106 5507 7161 3930 -528 1222 -800 C ATOM 854 ND1 HIS A 106 0.271 0.143 40.005 1.00 47.80 N ANISOU 854 ND1 HIS A 106 5939 7525 4700 -406 1256 -882 N ATOM 855 CD2 HIS A 106 0.891 0.180 42.097 1.00 48.59 C ANISOU 855 CD2 HIS A 106 6149 7919 4396 -565 1323 -994 C ATOM 856 CE1 HIS A 106 -0.083 1.318 40.495 1.00 49.47 C ANISOU 856 CE1 HIS A 106 6113 7755 4929 -362 1374 -1111 C ATOM 857 NE2 HIS A 106 0.282 1.366 41.763 1.00 51.59 N ANISOU 857 NE2 HIS A 106 6447 8201 4953 -458 1423 -1197 N ATOM 858 N ILE A 107 3.346 -4.283 39.647 1.00 38.73 N ANISOU 858 N ILE A 107 5062 6345 3310 -641 740 -106 N ATOM 859 CA ILE A 107 3.834 -5.663 39.722 1.00 40.17 C ANISOU 859 CA ILE A 107 5290 6523 3449 -706 632 117 C ATOM 860 C ILE A 107 5.330 -5.668 40.068 1.00 42.08 C ANISOU 860 C ILE A 107 5615 6761 3613 -718 492 149 C ATOM 861 O ILE A 107 5.756 -6.349 40.994 1.00 44.10 O ANISOU 861 O ILE A 107 5924 7131 3701 -805 437 271 O ATOM 862 CB ILE A 107 3.557 -6.448 38.419 1.00 38.15 C ANISOU 862 CB ILE A 107 4991 6098 3406 -660 579 227 C ATOM 863 CG1 ILE A 107 2.067 -6.786 38.313 1.00 41.66 C ANISOU 863 CG1 ILE A 107 5351 6585 3895 -686 698 246 C ATOM 864 CG2 ILE A 107 4.382 -7.736 38.360 1.00 35.65 C ANISOU 864 CG2 ILE A 107 4728 5722 3095 -701 443 425 C ATOM 865 CD1 ILE A 107 1.652 -7.320 36.951 1.00 42.88 C ANISOU 865 CD1 ILE A 107 5449 6582 4262 -637 654 302 C ATOM 866 N ILE A 108 6.111 -4.872 39.350 1.00 41.81 N ANISOU 866 N ILE A 108 5583 6603 3699 -637 433 45 N ATOM 867 CA ILE A 108 7.554 -4.801 39.586 1.00 41.04 C ANISOU 867 CA ILE A 108 5541 6495 3556 -644 300 61 C ATOM 868 C ILE A 108 7.886 -4.210 40.953 1.00 44.42 C ANISOU 868 C ILE A 108 6017 7109 3753 -719 315 -33 C ATOM 869 O ILE A 108 8.761 -4.732 41.656 1.00 43.23 O ANISOU 869 O ILE A 108 5914 7041 3469 -780 203 70 O ATOM 870 CB ILE A 108 8.256 -4.022 38.470 1.00 39.38 C ANISOU 870 CB ILE A 108 5313 6116 3534 -550 252 -34 C ATOM 871 CG1 ILE A 108 8.254 -4.868 37.191 1.00 34.76 C ANISOU 871 CG1 ILE A 108 4697 5375 3134 -496 199 88 C ATOM 872 CG2 ILE A 108 9.685 -3.649 38.880 1.00 39.54 C ANISOU 872 CG2 ILE A 108 5373 6153 3496 -567 139 -68 C ATOM 873 CD1 ILE A 108 8.475 -4.075 35.916 1.00 31.11 C ANISOU 873 CD1 ILE A 108 4204 4763 2855 -407 199 -3 C ATOM 874 N LYS A 109 7.184 -3.142 41.333 1.00 45.66 N ANISOU 874 N LYS A 109 6154 7332 3861 -714 448 -231 N ATOM 875 CA LYS A 109 7.364 -2.534 42.651 1.00 49.59 C ANISOU 875 CA LYS A 109 6695 8022 4124 -793 485 -360 C ATOM 876 C LYS A 109 7.096 -3.537 43.782 1.00 51.01 C ANISOU 876 C LYS A 109 6915 8413 4054 -912 488 -204 C ATOM 877 O LYS A 109 7.820 -3.560 44.774 1.00 51.94 O ANISOU 877 O LYS A 109 7092 8683 3959 -994 416 -194 O ATOM 878 CB LYS A 109 6.464 -1.303 42.820 1.00 51.23 C ANISOU 878 CB LYS A 109 6862 8251 4350 -760 655 -609 C ATOM 879 CG LYS A 109 6.719 -0.528 44.114 1.00 57.12 C ANISOU 879 CG LYS A 109 7654 9184 4865 -838 700 -797 C ATOM 880 CD LYS A 109 5.764 0.649 44.293 1.00 62.69 C ANISOU 880 CD LYS A 109 8308 9897 5613 -796 883 -1061 C ATOM 881 CE LYS A 109 6.082 1.428 45.576 1.00 65.97 C ANISOU 881 CE LYS A 109 8774 10498 5794 -881 929 -1279 C ATOM 882 NZ LYS A 109 5.016 2.413 45.930 1.00 68.00 N ANISOU 882 NZ LYS A 109 8974 10792 6070 -849 1134 -1541 N ATOM 883 N PHE A 110 6.065 -4.360 43.622 1.00 51.87 N ANISOU 883 N PHE A 110 6988 8532 4189 -929 565 -75 N ATOM 884 CA PHE A 110 5.740 -5.403 44.595 1.00 55.84 C ANISOU 884 CA PHE A 110 7525 9214 4478 -1050 573 110 C ATOM 885 C PHE A 110 6.899 -6.383 44.766 1.00 58.43 C ANISOU 885 C PHE A 110 7912 9524 4763 -1087 375 337 C ATOM 886 O PHE A 110 7.258 -6.733 45.882 1.00 60.28 O ANISOU 886 O PHE A 110 8206 9946 4754 -1190 326 431 O ATOM 887 CB PHE A 110 4.476 -6.150 44.164 1.00 55.31 C ANISOU 887 CB PHE A 110 7394 9111 4510 -1056 678 218 C ATOM 888 CG PHE A 110 4.063 -7.258 45.096 1.00 58.32 C ANISOU 888 CG PHE A 110 7804 9659 4696 -1190 697 431 C ATOM 889 CD1 PHE A 110 3.268 -6.992 46.206 1.00 60.12 C ANISOU 889 CD1 PHE A 110 8029 10131 4682 -1289 854 362 C ATOM 890 CD2 PHE A 110 4.442 -8.573 44.845 1.00 57.61 C ANISOU 890 CD2 PHE A 110 7741 9477 4673 -1219 567 701 C ATOM 891 CE1 PHE A 110 2.876 -8.012 47.058 1.00 62.32 C ANISOU 891 CE1 PHE A 110 8336 10572 4772 -1425 878 578 C ATOM 892 CE2 PHE A 110 4.053 -9.598 45.689 1.00 60.39 C ANISOU 892 CE2 PHE A 110 8120 9963 4861 -1348 581 920 C ATOM 893 CZ PHE A 110 3.269 -9.319 46.801 1.00 62.22 C ANISOU 893 CZ PHE A 110 8354 10452 4834 -1457 736 869 C ATOM 894 N HIS A 111 7.488 -6.813 43.655 1.00 60.00 N ANISOU 894 N HIS A 111 8092 9503 5201 -1001 263 423 N ATOM 895 CA HIS A 111 8.603 -7.765 43.698 1.00 61.69 C ANISOU 895 CA HIS A 111 8343 9667 5428 -1014 75 631 C ATOM 896 C HIS A 111 9.932 -7.132 44.120 1.00 63.52 C ANISOU 896 C HIS A 111 8608 9949 5578 -1011 -52 555 C ATOM 897 O HIS A 111 10.798 -7.816 44.667 1.00 64.87 O ANISOU 897 O HIS A 111 8813 10173 5664 -1055 -202 723 O ATOM 898 CB HIS A 111 8.744 -8.477 42.352 1.00 59.23 C ANISOU 898 CB HIS A 111 7990 9109 5405 -923 15 727 C ATOM 899 CG HIS A 111 7.654 -9.468 42.091 1.00 60.50 C ANISOU 899 CG HIS A 111 8127 9228 5634 -955 85 867 C ATOM 900 ND1 HIS A 111 7.608 -10.700 42.708 1.00 63.14 N ANISOU 900 ND1 HIS A 111 8491 9603 5895 -1040 28 1110 N ATOM 901 CD2 HIS A 111 6.562 -9.406 41.295 1.00 61.53 C ANISOU 901 CD2 HIS A 111 8198 9277 5903 -920 203 803 C ATOM 902 CE1 HIS A 111 6.540 -11.357 42.294 1.00 67.59 C ANISOU 902 CE1 HIS A 111 9018 10106 6558 -1062 114 1181 C ATOM 903 NE2 HIS A 111 5.888 -10.594 41.434 1.00 64.87 N ANISOU 903 NE2 HIS A 111 8615 9694 6338 -990 217 994 N ATOM 904 N ARG A 112 10.092 -5.834 43.871 1.00 64.20 N ANISOU 904 N ARG A 112 8679 10013 5702 -964 1 308 N ATOM 905 CA ARG A 112 11.264 -5.106 44.349 1.00 66.05 C ANISOU 905 CA ARG A 112 8938 10309 5849 -980 -104 203 C ATOM 906 C ARG A 112 11.171 -4.903 45.865 1.00 68.48 C ANISOU 906 C ARG A 112 9302 10893 5823 -1106 -88 167 C ATOM 907 O ARG A 112 12.191 -4.810 46.550 1.00 69.51 O ANISOU 907 O ARG A 112 9464 11131 5815 -1158 -224 180 O ATOM 908 CB ARG A 112 11.403 -3.758 43.630 1.00 65.17 C ANISOU 908 CB ARG A 112 8795 10075 5892 -903 -44 -50 C ATOM 909 CG ARG A 112 12.762 -3.092 43.830 1.00 68.22 C ANISOU 909 CG ARG A 112 9189 10466 6265 -912 -173 -143 C ATOM 910 CD ARG A 112 12.910 -1.808 43.016 1.00 70.44 C ANISOU 910 CD ARG A 112 9438 10593 6734 -840 -115 -365 C ATOM 911 NE ARG A 112 11.928 -0.791 43.403 1.00 75.17 N ANISOU 911 NE ARG A 112 10043 11248 7271 -851 52 -583 N ATOM 912 CZ ARG A 112 10.861 -0.421 42.690 1.00 76.15 C ANISOU 912 CZ ARG A 112 10129 11260 7543 -778 193 -652 C ATOM 913 NH1 ARG A 112 10.590 -0.964 41.504 1.00 75.46 N ANISOU 913 NH1 ARG A 112 10003 11009 7660 -698 190 -525 N ATOM 914 NH2 ARG A 112 10.052 0.518 43.172 1.00 77.79 N ANISOU 914 NH2 ARG A 112 10333 11527 7697 -786 339 -861 N ATOM 915 N ALA A 113 9.938 -4.850 46.370 1.00 70.33 N ANISOU 915 N ALA A 113 9542 11253 5926 -1157 80 122 N ATOM 916 CA ALA A 113 9.658 -4.657 47.792 1.00 72.50 C ANISOU 916 CA ALA A 113 9870 11816 5862 -1285 136 72 C ATOM 917 C ALA A 113 9.713 -5.964 48.590 1.00 75.14 C ANISOU 917 C ALA A 113 10250 12301 6000 -1390 49 374 C ATOM 918 O ALA A 113 10.242 -5.986 49.705 1.00 76.34 O ANISOU 918 O ALA A 113 10459 12675 5872 -1495 -32 410 O ATOM 919 CB ALA A 113 8.296 -3.989 47.969 1.00 72.70 C ANISOU 919 CB ALA A 113 9865 11914 5843 -1291 374 -124 C ATOM 920 N SER A 114 9.154 -7.041 48.032 1.00 75.21 N ANISOU 920 N SER A 114 10234 12191 6153 -1369 61 592 N ATOM 921 CA SER A 114 9.193 -8.364 48.681 1.00 76.98 C ANISOU 921 CA SER A 114 10500 12509 6242 -1463 -28 911 C ATOM 922 C SER A 114 10.626 -8.909 48.732 1.00 77.35 C ANISOU 922 C SER A 114 10569 12501 6320 -1447 -278 1087 C ATOM 923 O SER A 114 11.027 -9.527 49.719 1.00 79.19 O ANISOU 923 O SER A 114 10853 12903 6331 -1546 -390 1286 O ATOM 924 CB SER A 114 8.269 -9.358 47.970 1.00 75.74 C ANISOU 924 CB SER A 114 10302 12197 6278 -1442 43 1083 C ATOM 925 OG SER A 114 8.236 -10.613 48.631 0.00 80.07 O ANISOU 925 OG SER A 114 10892 12824 6710 -1543 -32 1396 O ATOM 926 N LYS A 115 11.391 -8.673 47.667 1.00 75.53 N ANISOU 926 N LYS A 115 10293 12040 6365 -1322 -363 1017 N ATOM 927 CA LYS A 115 12.826 -8.962 47.662 1.00 75.89 C ANISOU 927 CA LYS A 115 10335 12034 6465 -1292 -588 1124 C ATOM 928 C LYS A 115 13.574 -7.897 48.456 1.00 77.02 C ANISOU 928 C LYS A 115 10503 12364 6399 -1343 -645 938 C ATOM 929 O LYS A 115 14.456 -8.211 49.253 1.00 79.50 O ANISOU 929 O LYS A 115 10841 12812 6552 -1404 -818 1067 O ATOM 930 CB LYS A 115 13.368 -9.011 46.232 1.00 73.33 C ANISOU 930 CB LYS A 115 9944 11418 6499 -1149 -635 1088 C ATOM 931 CG LYS A 115 14.863 -9.242 46.119 0.00 76.18 C ANISOU 931 CG LYS A 115 10277 11714 6955 -1103 -849 1170 C ATOM 932 CD LYS A 115 15.341 -9.083 44.685 0.00 73.77 C ANISOU 932 CD LYS A 115 9901 11148 6980 -970 -855 1080 C ATOM 933 CE LYS A 115 16.844 -9.277 44.577 0.00 74.04 C ANISOU 933 CE LYS A 115 9887 11127 7119 -923 -1054 1146 C ATOM 934 NZ LYS A 115 17.328 -9.127 43.177 0.00 71.81 N ANISOU 934 NZ LYS A 115 9532 10609 7144 -803 -1043 1055 N ATOM 935 N LEU A 123 10.370 -12.088 40.764 1.00 62.45 N ANISOU 935 N LEU A 123 8377 9043 6307 -838 -349 1294 N ATOM 936 CA LEU A 123 9.492 -12.327 39.620 1.00 62.03 C ANISOU 936 CA LEU A 123 8281 8843 6445 -795 -258 1242 C ATOM 937 C LEU A 123 9.741 -13.711 39.006 1.00 60.60 C ANISOU 937 C LEU A 123 8086 8470 6469 -773 -346 1408 C ATOM 938 O LEU A 123 10.807 -13.937 38.433 1.00 59.14 O ANISOU 938 O LEU A 123 7884 8157 6428 -696 -451 1410 O ATOM 939 CB LEU A 123 9.706 -11.240 38.562 1.00 61.08 C ANISOU 939 CB LEU A 123 8124 8645 6439 -697 -217 1020 C ATOM 940 CG LEU A 123 8.993 -9.906 38.815 1.00 62.23 C ANISOU 940 CG LEU A 123 8265 8915 6466 -705 -86 830 C ATOM 941 CD1 LEU A 123 9.628 -8.765 38.027 1.00 60.24 C ANISOU 941 CD1 LEU A 123 7992 8592 6305 -617 -90 647 C ATOM 942 CD2 LEU A 123 7.513 -10.034 38.479 1.00 61.41 C ANISOU 942 CD2 LEU A 123 8123 8810 6399 -725 48 810 C ATOM 943 N PRO A 124 8.769 -14.642 39.135 1.00 60.44 N ANISOU 943 N PRO A 124 8066 8423 6474 -844 -298 1541 N ATOM 944 CA PRO A 124 8.908 -15.974 38.530 1.00 60.32 C ANISOU 944 CA PRO A 124 8037 8203 6680 -829 -373 1682 C ATOM 945 C PRO A 124 9.263 -15.923 37.037 1.00 57.54 C ANISOU 945 C PRO A 124 7639 7663 6561 -719 -384 1536 C ATOM 946 O PRO A 124 8.769 -15.059 36.301 1.00 51.57 O ANISOU 946 O PRO A 124 6854 6923 5815 -681 -293 1353 O ATOM 947 CB PRO A 124 7.522 -16.601 38.729 1.00 61.93 C ANISOU 947 CB PRO A 124 8234 8425 6871 -931 -271 1772 C ATOM 948 CG PRO A 124 6.962 -15.922 39.915 1.00 63.54 C ANISOU 948 CG PRO A 124 8465 8878 6801 -1019 -184 1774 C ATOM 949 CD PRO A 124 7.509 -14.520 39.895 1.00 61.85 C ANISOU 949 CD PRO A 124 8251 8763 6484 -949 -168 1565 C ATOM 950 N ARG A 125 10.112 -16.853 36.607 1.00 57.75 N ANISOU 950 N ARG A 125 7656 7515 6773 -668 -495 1619 N ATOM 951 CA ARG A 125 10.668 -16.824 35.258 1.00 55.45 C ANISOU 951 CA ARG A 125 7321 7065 6682 -564 -511 1477 C ATOM 952 C ARG A 125 9.627 -17.092 34.168 1.00 52.13 C ANISOU 952 C ARG A 125 6873 6550 6385 -570 -422 1383 C ATOM 953 O ARG A 125 9.666 -16.450 33.112 1.00 48.55 O ANISOU 953 O ARG A 125 6390 6071 5985 -507 -379 1208 O ATOM 954 CB ARG A 125 11.870 -17.780 35.140 1.00 57.10 C ANISOU 954 CB ARG A 125 7515 7115 7067 -503 -646 1579 C ATOM 955 CG ARG A 125 13.140 -17.303 35.874 1.00 62.94 C ANISOU 955 CG ARG A 125 8254 7941 7717 -467 -750 1617 C ATOM 956 CD ARG A 125 13.277 -15.767 35.872 1.00 67.59 C ANISOU 956 CD ARG A 125 8845 8692 8145 -453 -690 1435 C ATOM 957 NE ARG A 125 14.633 -15.281 36.134 1.00 71.08 N ANISOU 957 NE ARG A 125 9264 9173 8572 -401 -789 1412 N ATOM 958 CZ ARG A 125 14.934 -14.035 36.513 1.00 71.34 C ANISOU 958 CZ ARG A 125 9305 9355 8447 -411 -770 1298 C ATOM 959 NH1 ARG A 125 13.976 -13.126 36.713 1.00 70.04 N ANISOU 959 NH1 ARG A 125 9174 9311 8128 -461 -653 1195 N ATOM 960 NH2 ARG A 125 16.204 -13.694 36.711 1.00 69.50 N ANISOU 960 NH2 ARG A 125 9037 9145 8224 -371 -871 1283 N ATOM 961 N GLY A 126 8.705 -18.022 34.423 1.00 50.24 N ANISOU 961 N GLY A 126 6638 6266 6184 -654 -398 1504 N ATOM 962 CA GLY A 126 7.582 -18.275 33.507 1.00 48.05 C ANISOU 962 CA GLY A 126 6326 5924 6007 -682 -317 1420 C ATOM 963 C GLY A 126 6.755 -17.023 33.229 1.00 45.14 C ANISOU 963 C GLY A 126 5933 5704 5514 -679 -207 1262 C ATOM 964 O GLY A 126 6.368 -16.756 32.092 1.00 43.88 O ANISOU 964 O GLY A 126 5736 5497 5439 -641 -171 1122 O ATOM 965 N MET A 127 6.500 -16.248 34.277 1.00 42.93 N ANISOU 965 N MET A 127 5672 5605 5034 -717 -158 1285 N ATOM 966 CA MET A 127 5.747 -15.002 34.170 1.00 40.14 C ANISOU 966 CA MET A 127 5291 5387 4574 -706 -52 1137 C ATOM 967 C MET A 127 6.508 -13.921 33.378 1.00 38.28 C ANISOU 967 C MET A 127 5050 5137 4358 -600 -67 971 C ATOM 968 O MET A 127 5.918 -13.206 32.571 1.00 38.48 O ANISOU 968 O MET A 127 5036 5171 4414 -563 -7 842 O ATOM 969 CB MET A 127 5.420 -14.497 35.574 1.00 40.90 C ANISOU 969 CB MET A 127 5412 5677 4451 -775 6 1190 C ATOM 970 CG MET A 127 4.632 -13.220 35.615 1.00 40.62 C ANISOU 970 CG MET A 127 5342 5775 4318 -760 124 1033 C ATOM 971 SD MET A 127 4.105 -12.827 37.285 1.00 50.59 S ANISOU 971 SD MET A 127 6626 7272 5322 -859 216 1080 S ATOM 972 CE MET A 127 3.516 -11.157 37.002 1.00 51.51 C ANISOU 972 CE MET A 127 6693 7478 5402 -788 334 836 C ATOM 973 N VAL A 128 7.808 -13.794 33.623 1.00 36.49 N ANISOU 973 N VAL A 128 4855 4892 4117 -555 -150 985 N ATOM 974 CA VAL A 128 8.640 -12.856 32.869 1.00 35.59 C ANISOU 974 CA VAL A 128 4732 4754 4037 -466 -167 844 C ATOM 975 C VAL A 128 8.558 -13.139 31.370 1.00 33.27 C ANISOU 975 C VAL A 128 4404 4330 3908 -415 -165 764 C ATOM 976 O VAL A 128 8.303 -12.239 30.572 1.00 30.96 O ANISOU 976 O VAL A 128 4089 4053 3620 -374 -118 640 O ATOM 977 CB VAL A 128 10.114 -12.927 33.300 1.00 35.61 C ANISOU 977 CB VAL A 128 4756 4739 4034 -433 -270 888 C ATOM 978 CG1 VAL A 128 11.000 -12.143 32.314 1.00 28.05 C ANISOU 978 CG1 VAL A 128 3775 3730 3151 -350 -283 750 C ATOM 979 CG2 VAL A 128 10.270 -12.410 34.724 1.00 33.28 C ANISOU 979 CG2 VAL A 128 4498 4605 3543 -486 -278 935 C ATOM 980 N LYS A 129 8.763 -14.399 31.003 1.00 33.69 N ANISOU 980 N LYS A 129 4453 4254 4095 -422 -219 835 N ATOM 981 CA LYS A 129 8.737 -14.800 29.605 1.00 33.20 C ANISOU 981 CA LYS A 129 4361 4073 4180 -384 -220 746 C ATOM 982 C LYS A 129 7.381 -14.493 28.970 1.00 32.50 C ANISOU 982 C LYS A 129 4242 4025 4081 -414 -145 676 C ATOM 983 O LYS A 129 7.322 -13.965 27.859 1.00 29.86 O ANISOU 983 O LYS A 129 3887 3684 3776 -371 -126 560 O ATOM 984 CB LYS A 129 9.084 -16.288 29.459 1.00 33.64 C ANISOU 984 CB LYS A 129 4417 3972 4395 -394 -285 828 C ATOM 985 CG LYS A 129 9.140 -16.774 28.007 1.00 35.96 C ANISOU 985 CG LYS A 129 4681 4145 4837 -359 -284 708 C ATOM 986 CD LYS A 129 9.452 -18.260 27.897 1.00 36.49 C ANISOU 986 CD LYS A 129 4745 4033 5087 -368 -342 769 C ATOM 987 CE LYS A 129 10.861 -18.590 28.364 1.00 36.50 C ANISOU 987 CE LYS A 129 4747 3965 5157 -304 -421 833 C ATOM 988 NZ LYS A 129 11.187 -20.035 28.197 1.00 35.22 N ANISOU 988 NZ LYS A 129 4572 3600 5211 -296 -478 886 N ATOM 989 N SER A 130 6.298 -14.829 29.669 1.00 33.37 N ANISOU 989 N SER A 130 4343 4186 4148 -492 -105 756 N ATOM 990 CA SER A 130 4.951 -14.637 29.130 1.00 31.34 C ANISOU 990 CA SER A 130 4038 3971 3901 -526 -41 701 C ATOM 991 C SER A 130 4.601 -13.159 28.993 1.00 30.30 C ANISOU 991 C SER A 130 3883 3955 3675 -479 18 600 C ATOM 992 O SER A 130 3.961 -12.762 28.024 1.00 30.68 O ANISOU 992 O SER A 130 3887 4008 3761 -457 38 518 O ATOM 993 CB SER A 130 3.915 -15.344 29.999 1.00 34.03 C ANISOU 993 CB SER A 130 4361 4346 4222 -628 -2 816 C ATOM 994 OG SER A 130 4.163 -16.732 30.033 1.00 30.77 O ANISOU 994 OG SER A 130 3966 3799 3927 -675 -60 916 O ATOM 995 N LEU A 131 5.026 -12.344 29.951 1.00 29.85 N ANISOU 995 N LEU A 131 3855 3986 3501 -464 40 606 N ATOM 996 CA LEU A 131 4.887 -10.896 29.826 1.00 29.58 C ANISOU 996 CA LEU A 131 3806 4028 3406 -409 89 500 C ATOM 997 C LEU A 131 5.600 -10.410 28.561 1.00 29.97 C ANISOU 997 C LEU A 131 3856 4005 3525 -335 50 416 C ATOM 998 O LEU A 131 5.000 -9.743 27.715 1.00 29.48 O ANISOU 998 O LEU A 131 3756 3953 3490 -302 76 348 O ATOM 999 CB LEU A 131 5.439 -10.182 31.066 1.00 30.59 C ANISOU 999 CB LEU A 131 3973 4246 3403 -412 107 502 C ATOM 1000 CG LEU A 131 4.568 -10.311 32.322 1.00 31.87 C ANISOU 1000 CG LEU A 131 4129 4529 3452 -487 177 558 C ATOM 1001 CD1 LEU A 131 5.379 -10.027 33.602 1.00 29.06 C ANISOU 1001 CD1 LEU A 131 3831 4262 2949 -513 161 587 C ATOM 1002 CD2 LEU A 131 3.349 -9.400 32.225 1.00 28.90 C ANISOU 1002 CD2 LEU A 131 3687 4227 3066 -473 280 465 C ATOM 1003 N LEU A 132 6.869 -10.782 28.417 1.00 29.34 N ANISOU 1003 N LEU A 132 3814 3859 3477 -311 -13 428 N ATOM 1004 CA LEU A 132 7.646 -10.376 27.255 1.00 28.54 C ANISOU 1004 CA LEU A 132 3711 3702 3431 -252 -39 352 C ATOM 1005 C LEU A 132 7.005 -10.815 25.950 1.00 29.15 C ANISOU 1005 C LEU A 132 3757 3737 3583 -253 -39 312 C ATOM 1006 O LEU A 132 6.868 -10.012 25.026 1.00 30.34 O ANISOU 1006 O LEU A 132 3891 3906 3731 -218 -25 248 O ATOM 1007 CB LEU A 132 9.082 -10.910 27.331 1.00 27.31 C ANISOU 1007 CB LEU A 132 3579 3480 3318 -230 -102 373 C ATOM 1008 CG LEU A 132 9.988 -10.490 26.170 1.00 24.83 C ANISOU 1008 CG LEU A 132 3256 3125 3054 -176 -112 290 C ATOM 1009 CD1 LEU A 132 10.009 -8.973 25.990 1.00 23.21 C ANISOU 1009 CD1 LEU A 132 3051 2979 2788 -149 -73 231 C ATOM 1010 CD2 LEU A 132 11.374 -11.021 26.387 1.00 25.50 C ANISOU 1010 CD2 LEU A 132 3343 3153 3193 -152 -167 310 C ATOM 1011 N TYR A 133 6.605 -12.081 25.865 1.00 30.20 N ANISOU 1011 N TYR A 133 3881 3812 3782 -299 -60 352 N ATOM 1012 CA TYR A 133 6.003 -12.581 24.630 1.00 29.43 C ANISOU 1012 CA TYR A 133 3752 3678 3751 -313 -69 296 C ATOM 1013 C TYR A 133 4.754 -11.787 24.210 1.00 30.73 C ANISOU 1013 C TYR A 133 3869 3929 3877 -318 -35 266 C ATOM 1014 O TYR A 133 4.571 -11.489 23.025 1.00 30.10 O ANISOU 1014 O TYR A 133 3771 3861 3805 -299 -49 203 O ATOM 1015 CB TYR A 133 5.652 -14.059 24.721 1.00 29.64 C ANISOU 1015 CB TYR A 133 3773 3618 3870 -375 -95 339 C ATOM 1016 CG TYR A 133 5.262 -14.631 23.381 1.00 31.72 C ANISOU 1016 CG TYR A 133 4011 3837 4204 -393 -115 251 C ATOM 1017 CD1 TYR A 133 6.235 -15.067 22.480 1.00 31.53 C ANISOU 1017 CD1 TYR A 133 4004 3737 4238 -359 -141 170 C ATOM 1018 CD2 TYR A 133 3.929 -14.698 22.989 1.00 35.96 C ANISOU 1018 CD2 TYR A 133 4498 4421 4743 -446 -105 236 C ATOM 1019 CE1 TYR A 133 5.885 -15.576 21.229 1.00 37.76 C ANISOU 1019 CE1 TYR A 133 4774 4504 5069 -384 -155 67 C ATOM 1020 CE2 TYR A 133 3.567 -15.208 21.738 1.00 36.59 C ANISOU 1020 CE2 TYR A 133 4554 4477 4870 -472 -134 144 C ATOM 1021 CZ TYR A 133 4.549 -15.644 20.866 1.00 40.25 C ANISOU 1021 CZ TYR A 133 5048 4871 5373 -444 -158 55 C ATOM 1022 OH TYR A 133 4.201 -16.156 19.633 1.00 46.12 O ANISOU 1022 OH TYR A 133 5773 5608 6144 -479 -183 -55 O ATOM 1023 N GLN A 134 3.903 -11.461 25.178 1.00 29.24 N ANISOU 1023 N GLN A 134 3657 3807 3646 -343 10 313 N ATOM 1024 CA GLN A 134 2.638 -10.792 24.889 1.00 28.88 C ANISOU 1024 CA GLN A 134 3544 3838 3592 -343 44 290 C ATOM 1025 C GLN A 134 2.828 -9.313 24.545 1.00 27.39 C ANISOU 1025 C GLN A 134 3352 3688 3365 -266 59 242 C ATOM 1026 O GLN A 134 2.137 -8.779 23.675 1.00 28.73 O ANISOU 1026 O GLN A 134 3473 3888 3555 -242 50 215 O ATOM 1027 CB GLN A 134 1.666 -10.970 26.060 1.00 29.31 C ANISOU 1027 CB GLN A 134 3560 3954 3623 -397 103 346 C ATOM 1028 CG GLN A 134 1.239 -12.437 26.265 1.00 31.76 C ANISOU 1028 CG GLN A 134 3859 4216 3991 -489 88 411 C ATOM 1029 CD GLN A 134 0.055 -12.580 27.191 1.00 36.43 C ANISOU 1029 CD GLN A 134 4390 4887 4563 -557 158 466 C ATOM 1030 OE1 GLN A 134 -0.776 -11.678 27.292 1.00 33.86 O ANISOU 1030 OE1 GLN A 134 3999 4654 4213 -532 213 428 O ATOM 1031 NE2 GLN A 134 -0.028 -13.717 27.879 1.00 34.74 N ANISOU 1031 NE2 GLN A 134 4193 4638 4370 -644 159 560 N ATOM 1032 N ILE A 135 3.768 -8.660 25.218 1.00 26.37 N ANISOU 1032 N ILE A 135 3273 3557 3190 -232 75 237 N ATOM 1033 CA ILE A 135 4.156 -7.301 24.866 1.00 25.88 C ANISOU 1033 CA ILE A 135 3218 3502 3113 -166 84 193 C ATOM 1034 C ILE A 135 4.650 -7.284 23.415 1.00 27.55 C ANISOU 1034 C ILE A 135 3440 3677 3352 -143 36 171 C ATOM 1035 O ILE A 135 4.266 -6.410 22.631 1.00 27.51 O ANISOU 1035 O ILE A 135 3408 3689 3354 -107 32 159 O ATOM 1036 CB ILE A 135 5.274 -6.772 25.778 1.00 25.53 C ANISOU 1036 CB ILE A 135 3228 3450 3021 -150 96 182 C ATOM 1037 CG1 ILE A 135 4.778 -6.584 27.215 1.00 25.70 C ANISOU 1037 CG1 ILE A 135 3245 3537 2982 -176 151 188 C ATOM 1038 CG2 ILE A 135 5.812 -5.444 25.260 1.00 22.53 C ANISOU 1038 CG2 ILE A 135 2859 3050 2651 -94 99 137 C ATOM 1039 CD1 ILE A 135 5.918 -6.458 28.215 1.00 25.95 C ANISOU 1039 CD1 ILE A 135 3336 3578 2947 -187 139 189 C ATOM 1040 N LEU A 136 5.494 -8.252 23.068 1.00 27.77 N ANISOU 1040 N LEU A 136 3501 3657 3393 -165 2 167 N ATOM 1041 CA LEU A 136 6.037 -8.351 21.713 1.00 29.72 C ANISOU 1041 CA LEU A 136 3759 3886 3650 -154 -29 129 C ATOM 1042 C LEU A 136 4.927 -8.626 20.711 1.00 31.49 C ANISOU 1042 C LEU A 136 3938 4146 3881 -178 -54 116 C ATOM 1043 O LEU A 136 4.880 -8.014 19.648 1.00 29.88 O ANISOU 1043 O LEU A 136 3728 3977 3649 -159 -72 103 O ATOM 1044 CB LEU A 136 7.112 -9.439 21.622 1.00 28.77 C ANISOU 1044 CB LEU A 136 3668 3700 3563 -168 -51 108 C ATOM 1045 CG LEU A 136 8.464 -9.110 22.266 1.00 25.95 C ANISOU 1045 CG LEU A 136 3343 3315 3203 -139 -47 113 C ATOM 1046 CD1 LEU A 136 9.295 -10.371 22.417 1.00 27.77 C ANISOU 1046 CD1 LEU A 136 3583 3472 3498 -148 -75 110 C ATOM 1047 CD2 LEU A 136 9.235 -8.052 21.466 1.00 25.10 C ANISOU 1047 CD2 LEU A 136 3243 3225 3069 -105 -34 79 C ATOM 1048 N ASP A 137 4.025 -9.536 21.065 1.00 33.37 N ANISOU 1048 N ASP A 137 4143 4383 4153 -227 -59 129 N ATOM 1049 CA ASP A 137 2.858 -9.837 20.231 1.00 31.98 C ANISOU 1049 CA ASP A 137 3909 4251 3991 -261 -90 115 C ATOM 1050 C ASP A 137 2.060 -8.567 19.916 1.00 31.64 C ANISOU 1050 C ASP A 137 3816 4280 3927 -217 -91 138 C ATOM 1051 O ASP A 137 1.785 -8.266 18.754 1.00 32.67 O ANISOU 1051 O ASP A 137 3927 4454 4033 -211 -137 128 O ATOM 1052 CB ASP A 137 1.961 -10.867 20.932 1.00 34.04 C ANISOU 1052 CB ASP A 137 4131 4498 4306 -328 -83 139 C ATOM 1053 CG ASP A 137 1.111 -11.670 19.965 1.00 33.04 C ANISOU 1053 CG ASP A 137 3955 4385 4213 -389 -131 99 C ATOM 1054 OD1 ASP A 137 1.018 -11.292 18.782 1.00 29.66 O ANISOU 1054 OD1 ASP A 137 3516 4006 3747 -376 -174 58 O ATOM 1055 OD2 ASP A 137 0.532 -12.691 20.395 1.00 34.77 O ANISOU 1055 OD2 ASP A 137 4147 4570 4495 -460 -130 112 O ATOM 1056 N GLY A 138 1.687 -7.823 20.950 1.00 31.92 N ANISOU 1056 N GLY A 138 3828 4328 3973 -185 -42 169 N ATOM 1057 CA GLY A 138 0.914 -6.588 20.770 1.00 32.21 C ANISOU 1057 CA GLY A 138 3806 4407 4024 -128 -37 188 C ATOM 1058 C GLY A 138 1.639 -5.547 19.926 1.00 32.89 C ANISOU 1058 C GLY A 138 3930 4480 4086 -74 -62 197 C ATOM 1059 O GLY A 138 1.063 -4.980 18.998 1.00 32.88 O ANISOU 1059 O GLY A 138 3888 4515 4091 -49 -109 227 O ATOM 1060 N ILE A 139 2.913 -5.316 20.234 1.00 31.83 N ANISOU 1060 N ILE A 139 3871 4296 3925 -61 -38 183 N ATOM 1061 CA ILE A 139 3.721 -4.350 19.496 1.00 32.20 C ANISOU 1061 CA ILE A 139 3957 4325 3953 -25 -50 197 C ATOM 1062 C ILE A 139 3.971 -4.790 18.058 1.00 30.66 C ANISOU 1062 C ILE A 139 3776 4167 3705 -55 -102 198 C ATOM 1063 O ILE A 139 3.979 -3.953 17.154 1.00 29.84 O ANISOU 1063 O ILE A 139 3672 4087 3579 -33 -130 242 O ATOM 1064 CB ILE A 139 5.047 -4.048 20.222 1.00 32.83 C ANISOU 1064 CB ILE A 139 4099 4350 4023 -16 -12 174 C ATOM 1065 CG1 ILE A 139 4.753 -3.292 21.521 1.00 39.65 C ANISOU 1065 CG1 ILE A 139 4950 5195 4919 14 38 162 C ATOM 1066 CG2 ILE A 139 5.984 -3.211 19.347 1.00 34.20 C ANISOU 1066 CG2 ILE A 139 4309 4505 4181 0 -20 192 C ATOM 1067 CD1 ILE A 139 4.062 -1.940 21.307 1.00 39.10 C ANISOU 1067 CD1 ILE A 139 4840 5110 4906 73 45 183 C ATOM 1068 N HIS A 140 4.139 -6.093 17.844 1.00 29.46 N ANISOU 1068 N HIS A 140 3636 4021 3535 -107 -115 150 N ATOM 1069 CA HIS A 140 4.278 -6.642 16.492 1.00 30.34 C ANISOU 1069 CA HIS A 140 3757 4181 3588 -146 -157 119 C ATOM 1070 C HIS A 140 3.055 -6.325 15.632 1.00 30.88 C ANISOU 1070 C HIS A 140 3768 4332 3632 -153 -220 157 C ATOM 1071 O HIS A 140 3.188 -5.983 14.458 1.00 30.63 O ANISOU 1071 O HIS A 140 3749 4365 3525 -163 -258 174 O ATOM 1072 CB HIS A 140 4.506 -8.152 16.530 1.00 31.62 C ANISOU 1072 CB HIS A 140 3931 4313 3768 -199 -158 42 C ATOM 1073 CG HIS A 140 4.031 -8.864 15.303 1.00 34.56 C ANISOU 1073 CG HIS A 140 4288 4747 4095 -253 -208 -13 C ATOM 1074 ND1 HIS A 140 4.716 -8.823 14.107 1.00 47.85 N ANISOU 1074 ND1 HIS A 140 6005 6484 5693 -268 -214 -59 N ATOM 1075 CD2 HIS A 140 2.926 -9.614 15.079 1.00 41.87 C ANISOU 1075 CD2 HIS A 140 5165 5702 5043 -304 -252 -39 C ATOM 1076 CE1 HIS A 140 4.055 -9.521 13.200 1.00 48.14 C ANISOU 1076 CE1 HIS A 140 6019 6584 5687 -326 -264 -119 C ATOM 1077 NE2 HIS A 140 2.965 -10.009 13.764 1.00 45.11 N ANISOU 1077 NE2 HIS A 140 5583 6181 5375 -350 -293 -108 N ATOM 1078 N TYR A 141 1.871 -6.451 16.232 1.00 30.84 N ANISOU 1078 N TYR A 141 3694 4334 3688 -152 -230 175 N ATOM 1079 CA TYR A 141 0.617 -6.123 15.567 1.00 29.63 C ANISOU 1079 CA TYR A 141 3461 4260 3538 -151 -298 218 C ATOM 1080 C TYR A 141 0.554 -4.630 15.252 1.00 30.87 C ANISOU 1080 C TYR A 141 3606 4424 3698 -78 -314 307 C ATOM 1081 O TYR A 141 0.198 -4.248 14.145 1.00 31.44 O ANISOU 1081 O TYR A 141 3657 4567 3719 -80 -389 360 O ATOM 1082 CB TYR A 141 -0.585 -6.546 16.429 1.00 28.51 C ANISOU 1082 CB TYR A 141 3231 4120 3480 -164 -287 216 C ATOM 1083 CG TYR A 141 -1.918 -6.047 15.910 1.00 27.50 C ANISOU 1083 CG TYR A 141 2993 4069 3385 -146 -354 268 C ATOM 1084 CD1 TYR A 141 -2.568 -6.692 14.858 1.00 28.52 C ANISOU 1084 CD1 TYR A 141 3077 4284 3474 -209 -445 251 C ATOM 1085 CD2 TYR A 141 -2.532 -4.924 16.476 1.00 29.39 C ANISOU 1085 CD2 TYR A 141 3166 4297 3705 -65 -331 325 C ATOM 1086 CE1 TYR A 141 -3.798 -6.227 14.378 1.00 30.32 C ANISOU 1086 CE1 TYR A 141 3190 4593 3737 -191 -524 308 C ATOM 1087 CE2 TYR A 141 -3.752 -4.448 15.999 1.00 28.45 C ANISOU 1087 CE2 TYR A 141 2927 4242 3639 -35 -400 378 C ATOM 1088 CZ TYR A 141 -4.380 -5.103 14.955 1.00 26.68 C ANISOU 1088 CZ TYR A 141 2654 4112 3370 -98 -502 378 C ATOM 1089 OH TYR A 141 -5.590 -4.626 14.495 1.00 31.43 O ANISOU 1089 OH TYR A 141 3125 4786 4031 -67 -585 441 O ATOM 1090 N LEU A 142 0.898 -3.791 16.223 1.00 32.03 N ANISOU 1090 N LEU A 142 3767 4495 3907 -19 -251 326 N ATOM 1091 CA LEU A 142 0.916 -2.343 15.994 1.00 32.68 C ANISOU 1091 CA LEU A 142 3842 4548 4025 51 -261 406 C ATOM 1092 C LEU A 142 1.882 -1.977 14.858 1.00 30.89 C ANISOU 1092 C LEU A 142 3688 4341 3708 33 -290 450 C ATOM 1093 O LEU A 142 1.530 -1.224 13.953 1.00 29.81 O ANISOU 1093 O LEU A 142 3531 4240 3555 53 -353 544 O ATOM 1094 CB LEU A 142 1.306 -1.588 17.274 1.00 31.28 C ANISOU 1094 CB LEU A 142 3683 4276 3927 104 -178 383 C ATOM 1095 CG LEU A 142 0.299 -1.569 18.432 1.00 29.99 C ANISOU 1095 CG LEU A 142 3440 4104 3850 134 -131 348 C ATOM 1096 CD1 LEU A 142 0.914 -0.838 19.625 1.00 27.80 C ANISOU 1096 CD1 LEU A 142 3202 3748 3614 170 -47 303 C ATOM 1097 CD2 LEU A 142 -1.023 -0.912 18.048 1.00 24.56 C ANISOU 1097 CD2 LEU A 142 2640 3442 3248 191 -177 405 C ATOM 1098 N HIS A 143 3.090 -2.526 14.915 1.00 30.02 N ANISOU 1098 N HIS A 143 3654 4212 3541 -8 -243 388 N ATOM 1099 CA HIS A 143 4.135 -2.225 13.934 1.00 32.57 C ANISOU 1099 CA HIS A 143 4039 4560 3775 -34 -244 415 C ATOM 1100 C HIS A 143 3.766 -2.681 12.516 1.00 34.05 C ANISOU 1100 C HIS A 143 4221 4872 3843 -86 -315 432 C ATOM 1101 O HIS A 143 4.034 -1.973 11.540 1.00 33.95 O ANISOU 1101 O HIS A 143 4233 4911 3756 -96 -344 517 O ATOM 1102 CB HIS A 143 5.474 -2.821 14.385 1.00 30.67 C ANISOU 1102 CB HIS A 143 3858 4277 3519 -61 -174 329 C ATOM 1103 CG HIS A 143 6.119 -2.057 15.498 1.00 27.62 C ANISOU 1103 CG HIS A 143 3490 3791 3214 -21 -118 331 C ATOM 1104 ND1 HIS A 143 7.378 -2.351 15.974 1.00 23.35 N ANISOU 1104 ND1 HIS A 143 2990 3208 2673 -37 -67 274 N ATOM 1105 CD2 HIS A 143 5.690 -0.984 16.208 1.00 26.74 C ANISOU 1105 CD2 HIS A 143 3357 3615 3189 33 -108 374 C ATOM 1106 CE1 HIS A 143 7.686 -1.510 16.946 1.00 25.50 C ANISOU 1106 CE1 HIS A 143 3268 3405 3014 -4 -36 281 C ATOM 1107 NE2 HIS A 143 6.680 -0.667 17.106 1.00 26.02 N ANISOU 1107 NE2 HIS A 143 3301 3452 3135 38 -53 333 N ATOM 1108 N ALA A 144 3.108 -3.830 12.418 1.00 33.87 N ANISOU 1108 N ALA A 144 4167 4901 3802 -128 -346 357 N ATOM 1109 CA ALA A 144 2.652 -4.353 11.129 1.00 35.14 C ANISOU 1109 CA ALA A 144 4317 5191 3845 -189 -422 346 C ATOM 1110 C ALA A 144 1.594 -3.443 10.502 1.00 36.09 C ANISOU 1110 C ALA A 144 4377 5380 3954 -162 -519 478 C ATOM 1111 O ALA A 144 1.434 -3.425 9.288 1.00 34.13 O ANISOU 1111 O ALA A 144 4136 5256 3577 -207 -591 516 O ATOM 1112 CB ALA A 144 2.101 -5.770 11.287 1.00 34.19 C ANISOU 1112 CB ALA A 144 4165 5086 3739 -244 -437 228 C ATOM 1113 N ASN A 145 0.876 -2.701 11.342 1.00 35.46 N ANISOU 1113 N ASN A 145 4235 5226 4011 -87 -521 544 N ATOM 1114 CA ASN A 145 -0.085 -1.703 10.884 1.00 35.90 C ANISOU 1114 CA ASN A 145 4221 5315 4104 -36 -611 681 C ATOM 1115 C ASN A 145 0.499 -0.289 10.884 1.00 34.35 C ANISOU 1115 C ASN A 145 4062 5036 3954 27 -590 801 C ATOM 1116 O ASN A 145 -0.238 0.692 10.793 1.00 35.46 O ANISOU 1116 O ASN A 145 4139 5148 4184 95 -649 921 O ATOM 1117 CB ASN A 145 -1.340 -1.774 11.761 1.00 36.85 C ANISOU 1117 CB ASN A 145 4227 5404 4370 12 -622 668 C ATOM 1118 CG ASN A 145 -2.192 -2.975 11.436 1.00 36.76 C ANISOU 1118 CG ASN A 145 4155 5495 4319 -60 -681 595 C ATOM 1119 OD1 ASN A 145 -2.865 -2.992 10.418 1.00 39.45 O ANISOU 1119 OD1 ASN A 145 4447 5951 4593 -88 -795 648 O ATOM 1120 ND2 ASN A 145 -2.165 -3.986 12.296 1.00 35.64 N ANISOU 1120 ND2 ASN A 145 4013 5310 4218 -97 -612 479 N ATOM 1121 N TRP A 146 1.824 -0.201 10.977 1.00 34.69 N ANISOU 1121 N TRP A 146 4198 5031 3952 3 -508 769 N ATOM 1122 CA TRP A 146 2.557 1.066 10.946 1.00 36.03 C ANISOU 1122 CA TRP A 146 4413 5114 4164 39 -479 871 C ATOM 1123 C TRP A 146 2.098 2.022 12.033 1.00 34.29 C ANISOU 1123 C TRP A 146 4144 4749 4137 134 -453 897 C ATOM 1124 O TRP A 146 2.006 3.226 11.805 1.00 33.57 O ANISOU 1124 O TRP A 146 4044 4587 4125 185 -481 1022 O ATOM 1125 CB TRP A 146 2.440 1.730 9.565 1.00 37.77 C ANISOU 1125 CB TRP A 146 4644 5423 4282 17 -568 1034 C ATOM 1126 CG TRP A 146 3.012 0.897 8.486 1.00 46.66 C ANISOU 1126 CG TRP A 146 5826 6704 5199 -83 -575 993 C ATOM 1127 CD1 TRP A 146 2.330 0.085 7.617 1.00 52.60 C ANISOU 1127 CD1 TRP A 146 6553 7615 5818 -140 -659 968 C ATOM 1128 CD2 TRP A 146 4.397 0.771 8.153 1.00 46.50 C ANISOU 1128 CD2 TRP A 146 5890 6701 5077 -144 -488 952 C ATOM 1129 NE1 TRP A 146 3.211 -0.533 6.763 1.00 55.65 N ANISOU 1129 NE1 TRP A 146 7009 8115 6020 -230 -623 902 N ATOM 1130 CE2 TRP A 146 4.486 -0.128 7.070 1.00 53.72 C ANISOU 1130 CE2 TRP A 146 6828 7788 5796 -231 -514 894 C ATOM 1131 CE3 TRP A 146 5.571 1.340 8.660 1.00 51.19 C ANISOU 1131 CE3 TRP A 146 6532 7186 5732 -137 -391 950 C ATOM 1132 CZ2 TRP A 146 5.709 -0.477 6.483 1.00 57.06 C ANISOU 1132 CZ2 TRP A 146 7317 8279 6084 -304 -431 830 C ATOM 1133 CZ3 TRP A 146 6.789 0.996 8.075 1.00 53.31 C ANISOU 1133 CZ3 TRP A 146 6859 7522 5873 -212 -318 901 C ATOM 1134 CH2 TRP A 146 6.845 0.092 7.000 1.00 55.12 C ANISOU 1134 CH2 TRP A 146 7107 7926 5911 -290 -332 839 C ATOM 1135 N VAL A 147 1.782 1.472 13.201 1.00 34.06 N ANISOU 1135 N VAL A 147 4080 4676 4183 155 -397 778 N ATOM 1136 CA VAL A 147 1.449 2.277 14.367 1.00 34.06 C ANISOU 1136 CA VAL A 147 4041 4553 4349 235 -346 758 C ATOM 1137 C VAL A 147 2.585 2.140 15.360 1.00 32.40 C ANISOU 1137 C VAL A 147 3902 4269 4141 215 -245 653 C ATOM 1138 O VAL A 147 2.997 1.026 15.696 1.00 29.82 O ANISOU 1138 O VAL A 147 3604 3988 3739 161 -212 560 O ATOM 1139 CB VAL A 147 0.118 1.851 15.010 1.00 35.77 C ANISOU 1139 CB VAL A 147 4151 4796 4645 272 -354 709 C ATOM 1140 CG1 VAL A 147 -0.097 2.584 16.329 1.00 32.95 C ANISOU 1140 CG1 VAL A 147 3758 4324 4435 345 -271 649 C ATOM 1141 CG2 VAL A 147 -1.039 2.136 14.052 1.00 37.49 C ANISOU 1141 CG2 VAL A 147 4277 5082 4885 303 -469 823 C ATOM 1142 N LEU A 148 3.109 3.284 15.791 1.00 30.00 N ANISOU 1142 N LEU A 148 3623 3846 3931 255 -206 673 N ATOM 1143 CA LEU A 148 4.187 3.328 16.758 1.00 30.29 C ANISOU 1143 CA LEU A 148 3717 3813 3977 234 -123 578 C ATOM 1144 C LEU A 148 3.621 3.746 18.113 1.00 30.43 C ANISOU 1144 C LEU A 148 3693 3759 4112 292 -68 492 C ATOM 1145 O LEU A 148 2.759 4.626 18.196 1.00 31.80 O ANISOU 1145 O LEU A 148 3805 3871 4409 365 -79 526 O ATOM 1146 CB LEU A 148 5.258 4.328 16.311 1.00 31.03 C ANISOU 1146 CB LEU A 148 3870 3828 4092 220 -113 643 C ATOM 1147 CG LEU A 148 5.892 4.126 14.932 1.00 33.07 C ANISOU 1147 CG LEU A 148 4171 4167 4228 157 -150 737 C ATOM 1148 CD1 LEU A 148 6.912 5.228 14.654 1.00 30.42 C ANISOU 1148 CD1 LEU A 148 3883 3739 3937 136 -125 808 C ATOM 1149 CD2 LEU A 148 6.552 2.740 14.818 1.00 28.26 C ANISOU 1149 CD2 LEU A 148 3593 3662 3482 89 -126 644 C ATOM 1150 N HIS A 149 4.099 3.104 19.173 1.00 31.11 N ANISOU 1150 N HIS A 149 3806 3857 4156 260 -9 380 N ATOM 1151 CA HIS A 149 3.628 3.410 20.515 1.00 30.13 C ANISOU 1151 CA HIS A 149 3649 3695 4103 297 55 284 C ATOM 1152 C HIS A 149 4.237 4.717 21.013 1.00 30.35 C ANISOU 1152 C HIS A 149 3706 3596 4229 327 94 248 C ATOM 1153 O HIS A 149 3.513 5.618 21.417 1.00 29.47 O ANISOU 1153 O HIS A 149 3543 3411 4242 395 119 222 O ATOM 1154 CB HIS A 149 3.959 2.268 21.478 1.00 29.45 C ANISOU 1154 CB HIS A 149 3590 3678 3922 242 95 197 C ATOM 1155 CG HIS A 149 3.307 2.417 22.814 1.00 28.75 C ANISOU 1155 CG HIS A 149 3462 3594 3866 265 165 105 C ATOM 1156 ND1 HIS A 149 3.725 3.343 23.744 1.00 31.40 N ANISOU 1156 ND1 HIS A 149 3821 3862 4249 284 220 20 N ATOM 1157 CD2 HIS A 149 2.253 1.776 23.368 1.00 29.34 C ANISOU 1157 CD2 HIS A 149 3474 3743 3931 264 194 77 C ATOM 1158 CE1 HIS A 149 2.959 3.261 24.816 1.00 35.37 C ANISOU 1158 CE1 HIS A 149 4279 4406 4753 297 286 -63 C ATOM 1159 NE2 HIS A 149 2.058 2.317 24.613 1.00 30.31 N ANISOU 1159 NE2 HIS A 149 3584 3854 4080 284 275 -22 N ATOM 1160 N ARG A 150 5.569 4.788 20.995 1.00 32.02 N ANISOU 1160 N ARG A 150 3990 3780 4395 274 100 237 N ATOM 1161 CA ARG A 150 6.338 6.009 21.312 1.00 35.29 C ANISOU 1161 CA ARG A 150 4438 4069 4903 279 127 208 C ATOM 1162 C ARG A 150 6.498 6.342 22.807 1.00 35.32 C ANISOU 1162 C ARG A 150 4448 4036 4934 280 192 56 C ATOM 1163 O ARG A 150 7.101 7.354 23.151 1.00 37.09 O ANISOU 1163 O ARG A 150 4697 4152 5244 278 214 7 O ATOM 1164 CB ARG A 150 5.792 7.227 20.549 1.00 36.97 C ANISOU 1164 CB ARG A 150 4619 4168 5259 341 98 307 C ATOM 1165 CG ARG A 150 5.531 6.956 19.065 1.00 41.92 C ANISOU 1165 CG ARG A 150 5239 4854 5835 334 24 468 C ATOM 1166 CD ARG A 150 5.246 8.209 18.278 1.00 48.21 C ANISOU 1166 CD ARG A 150 6019 5534 6766 382 -18 599 C ATOM 1167 NE ARG A 150 4.099 8.963 18.780 1.00 57.56 N ANISOU 1167 NE ARG A 150 7127 6625 8120 483 -12 575 N ATOM 1168 CZ ARG A 150 2.835 8.800 18.387 1.00 66.38 C ANISOU 1168 CZ ARG A 150 8160 7789 9273 547 -61 637 C ATOM 1169 NH1 ARG A 150 2.508 7.881 17.480 1.00 72.39 N ANISOU 1169 NH1 ARG A 150 8910 8698 9899 513 -128 724 N ATOM 1170 NH2 ARG A 150 1.881 9.563 18.913 1.00 63.47 N ANISOU 1170 NH2 ARG A 150 7709 7322 9085 647 -43 600 N ATOM 1171 N ASP A 151 5.989 5.486 23.690 1.00 36.26 N ANISOU 1171 N ASP A 151 4548 4253 4975 273 223 -19 N ATOM 1172 CA ASP A 151 6.088 5.722 25.135 1.00 34.92 C ANISOU 1172 CA ASP A 151 4388 4087 4793 263 286 -164 C ATOM 1173 C ASP A 151 5.898 4.441 25.958 1.00 32.98 C ANISOU 1173 C ASP A 151 4145 3982 4405 219 304 -200 C ATOM 1174 O ASP A 151 5.188 4.430 26.964 1.00 34.44 O ANISOU 1174 O ASP A 151 4300 4214 4571 229 364 -287 O ATOM 1175 CB ASP A 151 5.087 6.797 25.581 1.00 36.52 C ANISOU 1175 CB ASP A 151 4532 4208 5135 341 341 -238 C ATOM 1176 CG ASP A 151 5.412 7.369 26.971 1.00 38.90 C ANISOU 1176 CG ASP A 151 4857 4492 5433 323 411 -414 C ATOM 1177 OD1 ASP A 151 6.599 7.357 27.368 1.00 40.27 O ANISOU 1177 OD1 ASP A 151 5094 4666 5538 255 397 -457 O ATOM 1178 OD2 ASP A 151 4.486 7.839 27.661 1.00 40.27 O ANISOU 1178 OD2 ASP A 151 4976 4656 5670 376 482 -517 O ATOM 1179 N LEU A 152 6.549 3.365 25.531 1.00 32.38 N ANISOU 1179 N LEU A 152 4101 3967 4233 167 256 -133 N ATOM 1180 CA LEU A 152 6.487 2.099 26.252 1.00 31.02 C ANISOU 1180 CA LEU A 152 3939 3905 3944 120 259 -141 C ATOM 1181 C LEU A 152 7.255 2.180 27.564 1.00 31.55 C ANISOU 1181 C LEU A 152 4048 4002 3938 76 282 -231 C ATOM 1182 O LEU A 152 8.377 2.691 27.614 1.00 32.97 O ANISOU 1182 O LEU A 152 4265 4134 4128 54 259 -260 O ATOM 1183 CB LEU A 152 7.034 0.956 25.403 1.00 29.62 C ANISOU 1183 CB LEU A 152 3782 3759 3715 85 200 -55 C ATOM 1184 CG LEU A 152 6.112 0.395 24.328 1.00 33.53 C ANISOU 1184 CG LEU A 152 4234 4277 4228 103 173 20 C ATOM 1185 CD1 LEU A 152 6.900 -0.507 23.381 1.00 29.34 C ANISOU 1185 CD1 LEU A 152 3733 3760 3656 68 121 72 C ATOM 1186 CD2 LEU A 152 4.923 -0.351 24.960 1.00 29.92 C ANISOU 1186 CD2 LEU A 152 3729 3893 3745 95 202 12 C ATOM 1187 N LYS A 153 6.625 1.670 28.619 1.00 30.97 N ANISOU 1187 N LYS A 153 3962 4020 3783 55 324 -271 N ATOM 1188 CA LYS A 153 7.192 1.635 29.959 1.00 30.17 C ANISOU 1188 CA LYS A 153 3901 3986 3576 2 342 -349 C ATOM 1189 C LYS A 153 6.240 0.813 30.818 1.00 30.41 C ANISOU 1189 C LYS A 153 3909 4136 3508 -27 391 -343 C ATOM 1190 O LYS A 153 5.093 0.610 30.423 1.00 32.07 O ANISOU 1190 O LYS A 153 4062 4357 3768 4 427 -313 O ATOM 1191 CB LYS A 153 7.380 3.045 30.532 1.00 30.35 C ANISOU 1191 CB LYS A 153 3931 3953 3647 19 387 -486 C ATOM 1192 CG LYS A 153 6.097 3.878 30.632 1.00 34.92 C ANISOU 1192 CG LYS A 153 4450 4499 4317 84 473 -562 C ATOM 1193 CD LYS A 153 6.423 5.344 30.828 1.00 37.25 C ANISOU 1193 CD LYS A 153 4753 4680 4721 113 502 -688 C ATOM 1194 CE LYS A 153 5.187 6.206 30.749 1.00 43.22 C ANISOU 1194 CE LYS A 153 5437 5370 5616 198 579 -755 C ATOM 1195 NZ LYS A 153 5.540 7.643 30.701 1.00 46.61 N ANISOU 1195 NZ LYS A 153 5872 5638 6198 234 595 -855 N ATOM 1196 N PRO A 154 6.701 0.331 31.988 1.00 30.05 N ANISOU 1196 N PRO A 154 3906 4190 3322 -93 389 -362 N ATOM 1197 CA PRO A 154 5.845 -0.545 32.808 1.00 30.50 C ANISOU 1197 CA PRO A 154 3947 4371 3271 -138 438 -328 C ATOM 1198 C PRO A 154 4.435 -0.020 33.114 1.00 32.04 C ANISOU 1198 C PRO A 154 4073 4606 3495 -107 552 -406 C ATOM 1199 O PRO A 154 3.484 -0.802 33.095 1.00 31.50 O ANISOU 1199 O PRO A 154 3958 4596 3415 -124 586 -340 O ATOM 1200 CB PRO A 154 6.660 -0.722 34.088 1.00 31.06 C ANISOU 1200 CB PRO A 154 4077 4543 3179 -211 418 -356 C ATOM 1201 CG PRO A 154 8.085 -0.635 33.613 1.00 30.54 C ANISOU 1201 CG PRO A 154 4051 4399 3152 -210 316 -332 C ATOM 1202 CD PRO A 154 8.081 0.379 32.504 1.00 29.12 C ANISOU 1202 CD PRO A 154 3846 4084 3136 -139 325 -381 C ATOM 1203 N ALA A 155 4.296 1.278 33.376 1.00 34.17 N ANISOU 1203 N ALA A 155 4327 4836 3821 -62 612 -550 N ATOM 1204 CA ALA A 155 2.985 1.864 33.697 1.00 36.22 C ANISOU 1204 CA ALA A 155 4504 5124 4132 -18 730 -646 C ATOM 1205 C ALA A 155 1.987 1.716 32.538 1.00 37.00 C ANISOU 1205 C ALA A 155 4516 5158 4383 49 723 -563 C ATOM 1206 O ALA A 155 0.777 1.652 32.756 1.00 39.05 O ANISOU 1206 O ALA A 155 4688 5477 4671 68 806 -587 O ATOM 1207 CB ALA A 155 3.135 3.330 34.076 1.00 37.46 C ANISOU 1207 CB ALA A 155 4661 5211 4361 29 786 -825 C ATOM 1208 N ASN A 156 2.502 1.664 31.313 1.00 35.55 N ANISOU 1208 N ASN A 156 4351 4866 4290 80 625 -468 N ATOM 1209 CA ASN A 156 1.668 1.464 30.133 1.00 35.33 C ANISOU 1209 CA ASN A 156 4250 4793 4382 131 593 -379 C ATOM 1210 C ASN A 156 1.416 -0.003 29.783 1.00 35.27 C ANISOU 1210 C ASN A 156 4236 4853 4311 72 548 -256 C ATOM 1211 O ASN A 156 0.700 -0.284 28.824 1.00 36.14 O ANISOU 1211 O ASN A 156 4284 4945 4502 98 514 -189 O ATOM 1212 CB ASN A 156 2.275 2.188 28.925 1.00 36.14 C ANISOU 1212 CB ASN A 156 4373 4758 4599 187 515 -337 C ATOM 1213 CG ASN A 156 1.825 3.623 28.825 1.00 33.73 C ANISOU 1213 CG ASN A 156 4018 4352 4445 275 557 -418 C ATOM 1214 OD1 ASN A 156 0.721 3.974 29.257 1.00 35.29 O ANISOU 1214 OD1 ASN A 156 4129 4576 4705 321 636 -485 O ATOM 1215 ND2 ASN A 156 2.677 4.470 28.254 1.00 32.93 N ANISOU 1215 ND2 ASN A 156 3964 4129 4420 300 509 -411 N ATOM 1216 N ILE A 157 2.000 -0.938 30.536 1.00 33.48 N ANISOU 1216 N ILE A 157 4072 4700 3949 -11 539 -224 N ATOM 1217 CA ILE A 157 1.696 -2.354 30.327 1.00 32.54 C ANISOU 1217 CA ILE A 157 3946 4627 3792 -72 505 -113 C ATOM 1218 C ILE A 157 0.679 -2.792 31.372 1.00 32.21 C ANISOU 1218 C ILE A 157 3852 4707 3680 -125 601 -123 C ATOM 1219 O ILE A 157 1.028 -2.990 32.528 1.00 31.40 O ANISOU 1219 O ILE A 157 3798 4687 3446 -184 639 -139 O ATOM 1220 CB ILE A 157 2.957 -3.250 30.402 1.00 31.07 C ANISOU 1220 CB ILE A 157 3851 4425 3528 -127 423 -42 C ATOM 1221 CG1 ILE A 157 4.054 -2.741 29.460 1.00 31.19 C ANISOU 1221 CG1 ILE A 157 3909 4337 3603 -82 349 -47 C ATOM 1222 CG2 ILE A 157 2.595 -4.701 30.092 1.00 29.81 C ANISOU 1222 CG2 ILE A 157 3679 4279 3368 -184 387 67 C ATOM 1223 CD1 ILE A 157 3.616 -2.530 28.016 1.00 32.61 C ANISOU 1223 CD1 ILE A 157 4045 4450 3896 -30 314 -19 C ATOM 1224 N LEU A 158 -0.580 -2.915 30.965 1.00 32.82 N ANISOU 1224 N LEU A 158 3826 4806 3840 -108 639 -111 N ATOM 1225 CA LEU A 158 -1.644 -3.376 31.864 1.00 33.31 C ANISOU 1225 CA LEU A 158 3817 4991 3848 -166 742 -113 C ATOM 1226 C LEU A 158 -1.739 -4.891 31.820 1.00 33.11 C ANISOU 1226 C LEU A 158 3806 4993 3781 -265 700 18 C ATOM 1227 O LEU A 158 -1.310 -5.518 30.851 1.00 33.83 O ANISOU 1227 O LEU A 158 3928 4999 3927 -267 597 90 O ATOM 1228 CB LEU A 158 -2.997 -2.764 31.475 1.00 34.29 C ANISOU 1228 CB LEU A 158 3798 5127 4105 -101 806 -167 C ATOM 1229 CG LEU A 158 -3.048 -1.242 31.311 1.00 36.14 C ANISOU 1229 CG LEU A 158 3998 5293 4441 15 837 -287 C ATOM 1230 CD1 LEU A 158 -4.455 -0.765 30.929 1.00 31.89 C ANISOU 1230 CD1 LEU A 158 3297 4765 4055 85 890 -321 C ATOM 1231 CD2 LEU A 158 -2.583 -0.563 32.591 1.00 36.48 C ANISOU 1231 CD2 LEU A 158 4095 5387 4378 4 930 -413 C ATOM 1232 N VAL A 159 -2.302 -5.480 32.870 1.00 35.81 N ANISOU 1232 N VAL A 159 4127 5453 4027 -351 786 48 N ATOM 1233 CA VAL A 159 -2.538 -6.923 32.919 1.00 35.54 C ANISOU 1233 CA VAL A 159 4096 5435 3973 -455 758 183 C ATOM 1234 C VAL A 159 -3.886 -7.204 33.587 1.00 38.34 C ANISOU 1234 C VAL A 159 4340 5916 4311 -523 883 190 C ATOM 1235 O VAL A 159 -4.176 -6.708 34.683 1.00 39.65 O ANISOU 1235 O VAL A 159 4492 6206 4370 -543 1002 126 O ATOM 1236 CB VAL A 159 -1.402 -7.674 33.666 1.00 37.20 C ANISOU 1236 CB VAL A 159 4432 5650 4052 -526 706 274 C ATOM 1237 CG1 VAL A 159 -1.597 -9.191 33.569 1.00 35.83 C ANISOU 1237 CG1 VAL A 159 4264 5448 3903 -625 661 426 C ATOM 1238 CG2 VAL A 159 -0.041 -7.291 33.107 1.00 30.42 C ANISOU 1238 CG2 VAL A 159 3664 4684 3212 -458 598 250 C ATOM 1239 N MET A 160 -4.709 -7.999 32.913 1.00 38.99 N ANISOU 1239 N MET A 160 4340 5974 4500 -564 860 258 N ATOM 1240 CA MET A 160 -6.055 -8.290 33.379 1.00 39.47 C ANISOU 1240 CA MET A 160 4271 6148 4577 -631 975 268 C ATOM 1241 C MET A 160 -6.014 -9.249 34.568 1.00 41.37 C ANISOU 1241 C MET A 160 4562 6484 4673 -772 1037 379 C ATOM 1242 O MET A 160 -5.133 -10.111 34.662 1.00 38.88 O ANISOU 1242 O MET A 160 4361 6104 4308 -828 950 492 O ATOM 1243 CB MET A 160 -6.885 -8.898 32.248 1.00 40.45 C ANISOU 1243 CB MET A 160 4290 6213 4863 -646 912 309 C ATOM 1244 CG MET A 160 -7.061 -7.996 31.017 1.00 38.57 C ANISOU 1244 CG MET A 160 3991 5902 4761 -518 840 226 C ATOM 1245 SD MET A 160 -7.981 -6.483 31.348 1.00 39.07 S ANISOU 1245 SD MET A 160 3915 6048 4884 -405 963 86 S ATOM 1246 CE MET A 160 -9.630 -7.096 31.674 1.00 37.69 C ANISOU 1246 CE MET A 160 3543 6000 4777 -494 1070 110 C ATOM 1247 N GLY A 161 -6.970 -9.083 35.476 1.00 44.24 N ANISOU 1247 N GLY A 161 4833 7003 4972 -827 1191 351 N ATOM 1248 CA GLY A 161 -7.049 -9.902 36.684 1.00 46.94 C ANISOU 1248 CA GLY A 161 5215 7468 5153 -973 1271 465 C ATOM 1249 C GLY A 161 -8.040 -11.027 36.486 1.00 49.46 C ANISOU 1249 C GLY A 161 5437 7793 5563 -1091 1293 586 C ATOM 1250 O GLY A 161 -8.260 -11.457 35.353 1.00 46.25 O ANISOU 1250 O GLY A 161 4985 7259 5328 -1072 1194 607 O ATOM 1251 N GLU A 162 -8.650 -11.486 37.584 1.00 51.76 N ANISOU 1251 N GLU A 162 5692 8240 5732 -1222 1427 660 N ATOM 1252 CA GLU A 162 -9.620 -12.583 37.536 1.00 54.72 C ANISOU 1252 CA GLU A 162 5969 8630 6190 -1360 1465 787 C ATOM 1253 C GLU A 162 -10.766 -12.258 36.586 1.00 54.14 C ANISOU 1253 C GLU A 162 5708 8539 6322 -1307 1484 686 C ATOM 1254 O GLU A 162 -11.264 -11.134 36.553 1.00 56.03 O ANISOU 1254 O GLU A 162 5847 8853 6590 -1201 1566 527 O ATOM 1255 CB GLU A 162 -10.188 -12.895 38.929 1.00 58.12 C ANISOU 1255 CB GLU A 162 6374 9269 6441 -1508 1638 866 C ATOM 1256 CG GLU A 162 -9.174 -13.473 39.928 1.00 64.39 C ANISOU 1256 CG GLU A 162 7345 10099 7020 -1599 1605 1022 C ATOM 1257 CD GLU A 162 -8.631 -14.846 39.529 1.00 69.64 C ANISOU 1257 CD GLU A 162 8100 10583 7775 -1681 1451 1233 C ATOM 1258 OE1 GLU A 162 -9.324 -15.593 38.799 1.00 70.89 O ANISOU 1258 OE1 GLU A 162 8169 10640 8125 -1735 1423 1287 O ATOM 1259 OE2 GLU A 162 -7.499 -15.177 39.951 1.00 71.21 O ANISOU 1259 OE2 GLU A 162 8455 10738 7865 -1690 1354 1340 O ATOM 1260 N GLY A 163 -11.183 -13.262 35.824 1.00 52.44 N ANISOU 1260 N GLY A 163 5443 8221 6260 -1382 1403 780 N ATOM 1261 CA GLY A 163 -12.161 -13.081 34.767 1.00 51.03 C ANISOU 1261 CA GLY A 163 5095 8012 6283 -1338 1375 700 C ATOM 1262 C GLY A 163 -11.745 -13.880 33.547 1.00 49.46 C ANISOU 1262 C GLY A 163 4950 7621 6223 -1344 1188 750 C ATOM 1263 O GLY A 163 -10.797 -14.668 33.607 1.00 47.06 O ANISOU 1263 O GLY A 163 4798 7204 5876 -1391 1102 852 O ATOM 1264 N PRO A 164 -12.444 -13.672 32.423 1.00 50.35 N ANISOU 1264 N PRO A 164 4932 7697 6500 -1293 1122 673 N ATOM 1265 CA PRO A 164 -12.171 -14.437 31.209 1.00 50.31 C ANISOU 1265 CA PRO A 164 4964 7534 6619 -1310 952 695 C ATOM 1266 C PRO A 164 -10.825 -14.133 30.538 1.00 47.29 C ANISOU 1266 C PRO A 164 4748 7019 6200 -1194 820 658 C ATOM 1267 O PRO A 164 -10.396 -14.896 29.680 1.00 48.20 O ANISOU 1267 O PRO A 164 4924 7001 6389 -1221 694 677 O ATOM 1268 CB PRO A 164 -13.335 -14.063 30.288 1.00 51.59 C ANISOU 1268 CB PRO A 164 4927 7740 6933 -1277 925 610 C ATOM 1269 CG PRO A 164 -13.817 -12.753 30.790 1.00 54.07 C ANISOU 1269 CG PRO A 164 5140 8189 7214 -1165 1044 517 C ATOM 1270 CD PRO A 164 -13.571 -12.739 32.256 1.00 52.21 C ANISOU 1270 CD PRO A 164 4970 8050 6819 -1220 1202 561 C ATOM 1271 N GLU A 165 -10.168 -13.042 30.925 1.00 45.80 N ANISOU 1271 N GLU A 165 4629 6868 5905 -1072 854 595 N ATOM 1272 CA GLU A 165 -8.871 -12.672 30.352 1.00 44.99 C ANISOU 1272 CA GLU A 165 4674 6654 5767 -967 743 561 C ATOM 1273 C GLU A 165 -7.737 -12.673 31.385 1.00 43.72 C ANISOU 1273 C GLU A 165 4669 6490 5452 -970 773 612 C ATOM 1274 O GLU A 165 -6.775 -11.915 31.253 1.00 42.40 O ANISOU 1274 O GLU A 165 4594 6286 5230 -865 731 555 O ATOM 1275 CB GLU A 165 -8.983 -11.297 29.682 1.00 45.68 C ANISOU 1275 CB GLU A 165 4706 6761 5890 -813 725 439 C ATOM 1276 CG GLU A 165 -9.879 -11.285 28.449 1.00 46.40 C ANISOU 1276 CG GLU A 165 4663 6842 6126 -794 646 402 C ATOM 1277 CD GLU A 165 -9.676 -10.049 27.595 1.00 48.63 C ANISOU 1277 CD GLU A 165 4932 7103 6441 -640 582 321 C ATOM 1278 OE1 GLU A 165 -9.053 -10.165 26.512 1.00 47.86 O ANISOU 1278 OE1 GLU A 165 4906 6918 6360 -608 453 316 O ATOM 1279 OE2 GLU A 165 -10.127 -8.961 28.015 1.00 43.97 O ANISOU 1279 OE2 GLU A 165 4263 6582 5863 -554 665 261 O ATOM 1280 N ARG A 166 -7.850 -13.539 32.395 1.00 44.44 N ANISOU 1280 N ARG A 166 4785 6623 5476 -1099 837 729 N ATOM 1281 CA ARG A 166 -6.880 -13.627 33.498 1.00 44.79 C ANISOU 1281 CA ARG A 166 4966 6695 5358 -1122 859 803 C ATOM 1282 C ARG A 166 -5.433 -13.682 33.011 1.00 41.78 C ANISOU 1282 C ARG A 166 4728 6173 4971 -1046 725 805 C ATOM 1283 O ARG A 166 -5.058 -14.583 32.266 1.00 40.89 O ANISOU 1283 O ARG A 166 4654 5918 4966 -1069 619 854 O ATOM 1284 CB ARG A 166 -7.172 -14.863 34.368 1.00 47.87 C ANISOU 1284 CB ARG A 166 5370 7108 5710 -1290 903 976 C ATOM 1285 CG ARG A 166 -6.305 -14.984 35.625 1.00 52.39 C ANISOU 1285 CG ARG A 166 6071 7744 6092 -1332 926 1079 C ATOM 1286 CD ARG A 166 -6.664 -16.228 36.454 1.00 59.30 C ANISOU 1286 CD ARG A 166 6956 8640 6934 -1507 965 1282 C ATOM 1287 NE ARG A 166 -5.949 -16.262 37.735 1.00 60.10 N ANISOU 1287 NE ARG A 166 7170 8843 6822 -1555 990 1393 N ATOM 1288 CZ ARG A 166 -4.765 -16.841 37.953 1.00 64.58 C ANISOU 1288 CZ ARG A 166 7872 9308 7357 -1554 869 1516 C ATOM 1289 NH1 ARG A 166 -4.107 -17.475 36.981 1.00 61.08 N ANISOU 1289 NH1 ARG A 166 7472 8644 7091 -1505 724 1535 N ATOM 1290 NH2 ARG A 166 -4.230 -16.790 39.170 1.00 69.12 N ANISOU 1290 NH2 ARG A 166 8534 10011 7717 -1604 892 1617 N ATOM 1291 N GLY A 167 -4.628 -12.711 33.435 1.00 40.91 N ANISOU 1291 N GLY A 167 4690 6107 4747 -959 734 739 N ATOM 1292 CA GLY A 167 -3.203 -12.683 33.101 1.00 38.27 C ANISOU 1292 CA GLY A 167 4481 5661 4400 -890 619 740 C ATOM 1293 C GLY A 167 -2.867 -12.282 31.672 1.00 36.70 C ANISOU 1293 C GLY A 167 4275 5348 4323 -786 527 643 C ATOM 1294 O GLY A 167 -1.737 -12.490 31.229 1.00 35.82 O ANISOU 1294 O GLY A 167 4250 5130 4228 -744 431 651 O ATOM 1295 N ARG A 168 -3.824 -11.700 30.948 1.00 36.36 N ANISOU 1295 N ARG A 168 4121 5332 4360 -744 554 557 N ATOM 1296 CA ARG A 168 -3.552 -11.222 29.591 1.00 36.43 C ANISOU 1296 CA ARG A 168 4125 5259 4459 -650 466 477 C ATOM 1297 C ARG A 168 -3.014 -9.797 29.610 1.00 34.24 C ANISOU 1297 C ARG A 168 3874 5002 4132 -534 482 385 C ATOM 1298 O ARG A 168 -3.625 -8.901 30.194 1.00 33.69 O ANISOU 1298 O ARG A 168 3744 5024 4034 -502 575 327 O ATOM 1299 CB ARG A 168 -4.806 -11.270 28.725 1.00 38.68 C ANISOU 1299 CB ARG A 168 4277 5563 4857 -660 462 445 C ATOM 1300 CG ARG A 168 -4.548 -10.863 27.281 1.00 37.40 C ANISOU 1300 CG ARG A 168 4113 5333 4764 -579 360 382 C ATOM 1301 CD ARG A 168 -5.686 -11.288 26.394 1.00 41.22 C ANISOU 1301 CD ARG A 168 4477 5833 5352 -621 321 372 C ATOM 1302 NE ARG A 168 -5.611 -12.702 26.042 1.00 44.60 N ANISOU 1302 NE ARG A 168 4932 6182 5831 -726 262 415 N ATOM 1303 CZ ARG A 168 -6.648 -13.451 25.663 1.00 47.86 C ANISOU 1303 CZ ARG A 168 5243 6608 6332 -816 246 424 C ATOM 1304 NH1 ARG A 168 -7.876 -12.943 25.595 1.00 46.32 N ANISOU 1304 NH1 ARG A 168 4900 6515 6183 -812 282 402 N ATOM 1305 NH2 ARG A 168 -6.455 -14.730 25.360 1.00 51.58 N ANISOU 1305 NH2 ARG A 168 5754 6982 6864 -910 191 451 N ATOM 1306 N VAL A 169 -1.870 -9.594 28.967 1.00 31.98 N ANISOU 1306 N VAL A 169 3674 4628 3850 -475 398 364 N ATOM 1307 CA VAL A 169 -1.299 -8.260 28.831 1.00 31.96 C ANISOU 1307 CA VAL A 169 3698 4620 3824 -374 401 283 C ATOM 1308 C VAL A 169 -2.179 -7.405 27.919 1.00 30.32 C ANISOU 1308 C VAL A 169 3393 4420 3708 -303 401 225 C ATOM 1309 O VAL A 169 -2.690 -7.898 26.918 1.00 30.30 O ANISOU 1309 O VAL A 169 3339 4394 3779 -317 342 244 O ATOM 1310 CB VAL A 169 0.152 -8.324 28.274 1.00 30.65 C ANISOU 1310 CB VAL A 169 3635 4359 3650 -339 312 285 C ATOM 1311 CG1 VAL A 169 0.609 -6.970 27.736 1.00 30.17 C ANISOU 1311 CG1 VAL A 169 3585 4273 3605 -242 302 209 C ATOM 1312 CG2 VAL A 169 1.110 -8.826 29.352 1.00 35.34 C ANISOU 1312 CG2 VAL A 169 4316 4957 4153 -383 309 337 C ATOM 1313 N LYS A 170 -2.374 -6.143 28.299 1.00 30.20 N ANISOU 1313 N LYS A 170 3347 4436 3691 -230 463 154 N ATOM 1314 CA LYS A 170 -3.027 -5.143 27.449 1.00 29.54 C ANISOU 1314 CA LYS A 170 3177 4336 3710 -140 449 110 C ATOM 1315 C LYS A 170 -2.123 -3.930 27.362 1.00 30.08 C ANISOU 1315 C LYS A 170 3312 4341 3777 -56 439 57 C ATOM 1316 O LYS A 170 -1.921 -3.226 28.359 1.00 29.91 O ANISOU 1316 O LYS A 170 3309 4340 3714 -36 517 -10 O ATOM 1317 CB LYS A 170 -4.375 -4.705 28.021 1.00 32.94 C ANISOU 1317 CB LYS A 170 3473 4851 4193 -125 549 68 C ATOM 1318 CG LYS A 170 -5.400 -5.815 28.191 1.00 35.43 C ANISOU 1318 CG LYS A 170 3700 5240 4522 -219 576 119 C ATOM 1319 CD LYS A 170 -5.938 -6.311 26.868 1.00 35.69 C ANISOU 1319 CD LYS A 170 3667 5245 4648 -228 471 163 C ATOM 1320 CE LYS A 170 -7.050 -7.334 27.095 1.00 34.21 C ANISOU 1320 CE LYS A 170 3373 5130 4497 -330 504 202 C ATOM 1321 NZ LYS A 170 -7.493 -7.971 25.839 1.00 30.51 N ANISOU 1321 NZ LYS A 170 2851 4637 4105 -362 390 233 N ATOM 1322 N ILE A 171 -1.559 -3.702 26.178 1.00 31.57 N ANISOU 1322 N ILE A 171 3535 4456 4003 -17 347 82 N ATOM 1323 CA ILE A 171 -0.755 -2.520 25.931 1.00 31.05 C ANISOU 1323 CA ILE A 171 3521 4318 3958 56 332 48 C ATOM 1324 C ILE A 171 -1.672 -1.317 25.872 1.00 30.74 C ANISOU 1324 C ILE A 171 3386 4267 4027 144 371 7 C ATOM 1325 O ILE A 171 -2.686 -1.341 25.178 1.00 32.10 O ANISOU 1325 O ILE A 171 3458 4460 4279 169 341 43 O ATOM 1326 CB ILE A 171 0.029 -2.610 24.606 1.00 30.28 C ANISOU 1326 CB ILE A 171 3478 4160 3866 65 232 99 C ATOM 1327 CG1 ILE A 171 1.073 -3.717 24.673 1.00 31.92 C ANISOU 1327 CG1 ILE A 171 3776 4360 3992 -5 200 120 C ATOM 1328 CG2 ILE A 171 0.719 -1.276 24.307 1.00 27.58 C ANISOU 1328 CG2 ILE A 171 3173 3741 3564 134 224 79 C ATOM 1329 CD1 ILE A 171 1.657 -4.061 23.328 1.00 31.46 C ANISOU 1329 CD1 ILE A 171 3752 4268 3934 -10 118 154 C ATOM 1330 N ALA A 172 -1.323 -0.276 26.620 1.00 31.86 N ANISOU 1330 N ALA A 172 3551 4372 4183 190 435 -72 N ATOM 1331 CA ALA A 172 -2.067 0.979 26.603 1.00 32.39 C ANISOU 1331 CA ALA A 172 3531 4394 4383 288 475 -126 C ATOM 1332 C ALA A 172 -1.090 2.114 26.375 1.00 32.98 C ANISOU 1332 C ALA A 172 3678 4348 4503 339 452 -151 C ATOM 1333 O ALA A 172 0.122 1.915 26.446 1.00 33.18 O ANISOU 1333 O ALA A 172 3814 4352 4442 291 423 -146 O ATOM 1334 CB ALA A 172 -2.817 1.175 27.919 1.00 32.92 C ANISOU 1334 CB ALA A 172 3532 4533 4445 289 607 -234 C ATOM 1335 N ASP A 173 -1.630 3.294 26.085 1.00 36.45 N ANISOU 1335 N ASP A 173 4049 4705 5097 437 462 -173 N ATOM 1336 CA ASP A 173 -0.848 4.522 25.954 1.00 41.61 C ANISOU 1336 CA ASP A 173 4758 5222 5831 487 452 -203 C ATOM 1337 C ASP A 173 -1.609 5.609 26.690 1.00 44.65 C ANISOU 1337 C ASP A 173 5058 5549 6357 574 546 -325 C ATOM 1338 O ASP A 173 -2.375 6.370 26.098 1.00 47.09 O ANISOU 1338 O ASP A 173 5274 5778 6839 670 524 -291 O ATOM 1339 CB ASP A 173 -0.638 4.890 24.478 1.00 42.88 C ANISOU 1339 CB ASP A 173 4927 5301 6064 522 339 -65 C ATOM 1340 CG ASP A 173 0.427 5.971 24.280 1.00 52.86 C ANISOU 1340 CG ASP A 173 6271 6425 7387 540 323 -68 C ATOM 1341 OD1 ASP A 173 0.659 6.785 25.207 1.00 53.93 O ANISOU 1341 OD1 ASP A 173 6420 6490 7582 563 398 -193 O ATOM 1342 OD2 ASP A 173 1.039 5.997 23.187 1.00 61.74 O ANISOU 1342 OD2 ASP A 173 7445 7516 8497 522 239 49 O ATOM 1343 N MET A 174 -1.395 5.672 27.996 1.00 47.30 N ANISOU 1343 N MET A 174 5423 5930 6619 540 650 -472 N ATOM 1344 CA MET A 174 -2.212 6.511 28.865 1.00 49.83 C ANISOU 1344 CA MET A 174 5654 6232 7047 609 768 -626 C ATOM 1345 C MET A 174 -1.779 7.982 28.921 1.00 52.22 C ANISOU 1345 C MET A 174 5978 6354 7511 684 784 -719 C ATOM 1346 O MET A 174 -2.481 8.809 29.501 1.00 53.19 O ANISOU 1346 O MET A 174 6016 6427 7768 762 880 -858 O ATOM 1347 CB MET A 174 -2.274 5.872 30.250 1.00 51.23 C ANISOU 1347 CB MET A 174 5849 6567 7048 527 881 -745 C ATOM 1348 CG MET A 174 -2.784 4.435 30.150 1.00 51.84 C ANISOU 1348 CG MET A 174 5898 6797 7002 452 863 -635 C ATOM 1349 SD MET A 174 -3.406 3.728 31.659 1.00 56.12 S ANISOU 1349 SD MET A 174 6404 7536 7383 370 1012 -737 S ATOM 1350 CE MET A 174 -1.888 3.168 32.426 1.00 53.48 C ANISOU 1350 CE MET A 174 6249 7257 6815 250 980 -738 C ATOM 1351 N GLY A 175 -0.642 8.308 28.308 1.00 53.82 N ANISOU 1351 N GLY A 175 6284 6452 7714 660 697 -649 N ATOM 1352 CA GLY A 175 -0.220 9.704 28.124 1.00 57.62 C ANISOU 1352 CA GLY A 175 6783 6732 8379 723 692 -697 C ATOM 1353 C GLY A 175 -0.035 10.053 26.653 1.00 59.61 C ANISOU 1353 C GLY A 175 7039 6864 8745 763 569 -500 C ATOM 1354 O GLY A 175 0.948 10.694 26.278 1.00 62.33 O ANISOU 1354 O GLY A 175 7463 7085 9134 742 524 -466 O ATOM 1355 N PHE A 176 -0.983 9.628 25.819 1.00 61.48 N ANISOU 1355 N PHE A 176 7187 7151 9020 810 513 -366 N ATOM 1356 CA PHE A 176 -0.918 9.843 24.362 1.00 62.11 C ANISOU 1356 CA PHE A 176 7267 7160 9170 837 386 -161 C ATOM 1357 C PHE A 176 -0.928 11.332 23.983 1.00 65.01 C ANISOU 1357 C PHE A 176 7612 7305 9784 932 365 -133 C ATOM 1358 O PHE A 176 -0.264 11.741 23.023 1.00 64.11 O ANISOU 1358 O PHE A 176 7560 7101 9699 917 278 15 O ATOM 1359 CB PHE A 176 -2.085 9.119 23.669 1.00 62.05 C ANISOU 1359 CB PHE A 176 7150 7267 9157 869 328 -48 C ATOM 1360 CG PHE A 176 -1.945 9.026 22.170 1.00 59.00 C ANISOU 1360 CG PHE A 176 6781 6875 8760 862 189 165 C ATOM 1361 CD1 PHE A 176 -1.000 8.191 21.599 1.00 56.58 C ANISOU 1361 CD1 PHE A 176 6584 6653 8262 756 135 239 C ATOM 1362 CD2 PHE A 176 -2.760 9.773 21.332 1.00 59.11 C ANISOU 1362 CD2 PHE A 176 6700 6807 8953 963 111 289 C ATOM 1363 CE1 PHE A 176 -0.868 8.103 20.215 1.00 56.05 C ANISOU 1363 CE1 PHE A 176 6536 6603 8159 741 18 420 C ATOM 1364 CE2 PHE A 176 -2.632 9.688 19.958 1.00 52.70 C ANISOU 1364 CE2 PHE A 176 5910 6015 8100 946 -22 491 C ATOM 1365 CZ PHE A 176 -1.686 8.852 19.399 1.00 56.66 C ANISOU 1365 CZ PHE A 176 6525 6615 8386 830 -62 549 C ATOM 1366 N ALA A 177 -1.679 12.129 24.743 1.00 68.39 N ANISOU 1366 N ALA A 177 7950 7641 10393 1028 451 -275 N ATOM 1367 CA ALA A 177 -1.793 13.573 24.511 1.00 71.60 C ANISOU 1367 CA ALA A 177 8321 7805 11078 1132 442 -270 C ATOM 1368 C ALA A 177 -0.447 14.304 24.621 1.00 73.09 C ANISOU 1368 C ALA A 177 8640 7844 11285 1069 442 -304 C ATOM 1369 O ALA A 177 -0.117 15.140 23.774 1.00 74.38 O ANISOU 1369 O ALA A 177 8826 7834 11600 1098 366 -162 O ATOM 1370 CB ALA A 177 -2.804 14.181 25.480 1.00 72.66 C ANISOU 1370 CB ALA A 177 8331 7881 11396 1241 560 -468 C ATOM 1371 N ARG A 178 0.317 13.989 25.666 1.00 73.50 N ANISOU 1371 N ARG A 178 8773 7968 11185 978 524 -484 N ATOM 1372 CA ARG A 178 1.624 14.609 25.894 1.00 73.76 C ANISOU 1372 CA ARG A 178 8919 7882 11224 903 526 -542 C ATOM 1373 C ARG A 178 2.726 13.923 25.090 1.00 71.64 C ANISOU 1373 C ARG A 178 8752 7695 10774 790 438 -375 C ATOM 1374 O ARG A 178 3.343 14.534 24.219 1.00 71.65 O ANISOU 1374 O ARG A 178 8795 7564 10863 776 371 -235 O ATOM 1375 CB ARG A 178 1.994 14.592 27.372 0.00 76.17 C ANISOU 1375 CB ARG A 178 9261 8244 11436 848 638 -809 C ATOM 1376 CG ARG A 178 1.046 15.384 28.257 0.00 78.52 C ANISOU 1376 CG ARG A 178 9466 8455 11913 949 751 -1021 C ATOM 1377 CD ARG A 178 1.541 15.438 29.693 0.00 79.15 C ANISOU 1377 CD ARG A 178 9598 8602 11872 875 857 -1294 C ATOM 1378 NE ARG A 178 0.659 16.226 30.549 0.00 81.62 N ANISOU 1378 NE ARG A 178 9822 8838 12352 968 982 -1526 N ATOM 1379 CZ ARG A 178 0.887 16.466 31.836 0.00 82.80 C ANISOU 1379 CZ ARG A 178 10001 9037 12423 920 1093 -1799 C ATOM 1380 NH1 ARG A 178 1.973 15.979 32.422 0.00 81.77 N ANISOU 1380 NH1 ARG A 178 9984 9034 12050 779 1077 -1856 N ATOM 1381 NH2 ARG A 178 0.030 17.194 32.538 0.00 85.16 N ANISOU 1381 NH2 ARG A 178 10207 9265 12883 1013 1217 -2021 N ATOM 1382 N VAL A 195 8.736 13.748 34.343 1.00 77.44 N ANISOU 1382 N VAL A 195 9936 9001 10489 76 743 -1883 N ATOM 1383 CA VAL A 195 9.076 12.998 33.134 1.00 74.98 C ANISOU 1383 CA VAL A 195 9626 8691 10172 83 652 -1610 C ATOM 1384 C VAL A 195 10.253 12.046 33.364 1.00 72.11 C ANISOU 1384 C VAL A 195 9314 8487 9599 -27 565 -1540 C ATOM 1385 O VAL A 195 11.273 12.435 33.941 1.00 72.03 O ANISOU 1385 O VAL A 195 9340 8475 9555 -115 530 -1652 O ATOM 1386 CB VAL A 195 9.419 13.951 31.964 1.00 75.70 C ANISOU 1386 CB VAL A 195 9710 8535 10518 118 612 -1507 C ATOM 1387 CG1 VAL A 195 8.156 14.604 31.430 1.00 76.79 C ANISOU 1387 CG1 VAL A 195 9783 8525 10870 249 667 -1483 C ATOM 1388 CG2 VAL A 195 10.428 15.015 32.412 1.00 77.08 C ANISOU 1388 CG2 VAL A 195 9921 8573 10793 41 602 -1665 C ATOM 1389 N THR A 196 10.099 10.804 32.909 1.00 69.21 N ANISOU 1389 N THR A 196 8940 8250 9105 -20 526 -1360 N ATOM 1390 CA THR A 196 11.145 9.781 33.020 1.00 66.98 C ANISOU 1390 CA THR A 196 8693 8106 8652 -104 439 -1268 C ATOM 1391 C THR A 196 11.709 9.416 31.637 1.00 61.44 C ANISOU 1391 C THR A 196 7984 7336 8025 -92 370 -1064 C ATOM 1392 O THR A 196 10.950 9.167 30.702 1.00 62.23 O ANISOU 1392 O THR A 196 8057 7399 8190 -23 381 -937 O ATOM 1393 CB THR A 196 10.604 8.504 33.715 1.00 67.70 C ANISOU 1393 CB THR A 196 8786 8409 8526 -117 450 -1232 C ATOM 1394 OG1 THR A 196 11.672 7.572 33.922 1.00 67.85 O ANISOU 1394 OG1 THR A 196 8835 8543 8401 -193 357 -1150 O ATOM 1395 CG2 THR A 196 9.503 7.834 32.876 1.00 69.39 C ANISOU 1395 CG2 THR A 196 8959 8629 8777 -38 475 -1084 C ATOM 1396 N PHE A 197 13.037 9.381 31.517 1.00 56.41 N ANISOU 1396 N PHE A 197 7365 6695 7374 -166 300 -1040 N ATOM 1397 CA PHE A 197 13.710 9.034 30.255 1.00 51.17 C ANISOU 1397 CA PHE A 197 6690 5985 6765 -169 247 -866 C ATOM 1398 C PHE A 197 14.390 7.661 30.324 1.00 45.40 C ANISOU 1398 C PHE A 197 5960 5408 5881 -207 183 -777 C ATOM 1399 O PHE A 197 15.252 7.340 29.499 1.00 39.54 O ANISOU 1399 O PHE A 197 5204 4652 5168 -228 139 -675 O ATOM 1400 CB PHE A 197 14.757 10.095 29.896 1.00 52.29 C ANISOU 1400 CB PHE A 197 6832 5986 7048 -223 227 -895 C ATOM 1401 CG PHE A 197 14.215 11.494 29.836 1.00 57.84 C ANISOU 1401 CG PHE A 197 7536 6504 7938 -190 282 -981 C ATOM 1402 CD1 PHE A 197 13.605 11.966 28.683 1.00 59.71 C ANISOU 1402 CD1 PHE A 197 7757 6606 8322 -122 302 -853 C ATOM 1403 CD2 PHE A 197 14.329 12.345 30.931 1.00 65.09 C ANISOU 1403 CD2 PHE A 197 8467 7377 8886 -228 307 -1190 C ATOM 1404 CE1 PHE A 197 13.106 13.260 28.618 1.00 64.39 C ANISOU 1404 CE1 PHE A 197 8345 7005 9116 -82 344 -916 C ATOM 1405 CE2 PHE A 197 13.832 13.647 30.877 1.00 69.43 C ANISOU 1405 CE2 PHE A 197 9013 7728 9640 -191 361 -1282 C ATOM 1406 CZ PHE A 197 13.220 14.104 29.716 1.00 69.21 C ANISOU 1406 CZ PHE A 197 8966 7548 9783 -113 378 -1136 C ATOM 1407 N TRP A 198 13.984 6.844 31.293 1.00 40.82 N ANISOU 1407 N TRP A 198 5392 4972 5146 -214 181 -810 N ATOM 1408 CA TRP A 198 14.646 5.567 31.545 1.00 37.15 C ANISOU 1408 CA TRP A 198 4927 4638 4549 -250 111 -729 C ATOM 1409 C TRP A 198 14.457 4.551 30.416 1.00 34.13 C ANISOU 1409 C TRP A 198 4526 4257 4183 -206 97 -566 C ATOM 1410 O TRP A 198 15.233 3.596 30.320 1.00 29.19 O ANISOU 1410 O TRP A 198 3891 3693 3509 -227 35 -492 O ATOM 1411 CB TRP A 198 14.156 4.930 32.853 1.00 37.72 C ANISOU 1411 CB TRP A 198 5022 4864 4447 -274 114 -779 C ATOM 1412 CG TRP A 198 14.277 5.771 34.085 1.00 40.09 C ANISOU 1412 CG TRP A 198 5345 5205 4683 -328 131 -958 C ATOM 1413 CD1 TRP A 198 15.017 6.906 34.247 1.00 45.44 C ANISOU 1413 CD1 TRP A 198 6024 5799 5443 -370 120 -1084 C ATOM 1414 CD2 TRP A 198 13.649 5.519 35.347 1.00 42.80 C ANISOU 1414 CD2 TRP A 198 5712 5694 4855 -357 165 -1041 C ATOM 1415 NE1 TRP A 198 14.876 7.385 35.530 1.00 46.10 N ANISOU 1415 NE1 TRP A 198 6134 5965 5418 -421 143 -1258 N ATOM 1416 CE2 TRP A 198 14.045 6.547 36.226 1.00 47.07 C ANISOU 1416 CE2 TRP A 198 6272 6240 5372 -414 174 -1233 C ATOM 1417 CE3 TRP A 198 12.784 4.524 35.818 1.00 44.57 C ANISOU 1417 CE3 TRP A 198 5944 6050 4942 -350 195 -972 C ATOM 1418 CZ2 TRP A 198 13.604 6.610 37.554 1.00 51.83 C ANISOU 1418 CZ2 TRP A 198 6904 6993 5798 -462 215 -1368 C ATOM 1419 CZ3 TRP A 198 12.347 4.586 37.137 1.00 45.88 C ANISOU 1419 CZ3 TRP A 198 6135 6362 4934 -401 238 -1085 C ATOM 1420 CH2 TRP A 198 12.754 5.622 37.986 1.00 48.30 C ANISOU 1420 CH2 TRP A 198 6463 6687 5201 -455 250 -1286 C ATOM 1421 N TYR A 199 13.431 4.757 29.583 1.00 31.81 N ANISOU 1421 N TYR A 199 4223 3899 3963 -144 149 -518 N ATOM 1422 CA TYR A 199 13.059 3.821 28.522 1.00 29.92 C ANISOU 1422 CA TYR A 199 3969 3673 3726 -107 139 -386 C ATOM 1423 C TYR A 199 13.333 4.392 27.124 1.00 28.46 C ANISOU 1423 C TYR A 199 3772 3386 3657 -88 141 -315 C ATOM 1424 O TYR A 199 13.083 3.730 26.131 1.00 27.33 O ANISOU 1424 O TYR A 199 3617 3257 3510 -65 133 -219 O ATOM 1425 CB TYR A 199 11.579 3.390 28.705 1.00 29.44 C ANISOU 1425 CB TYR A 199 3899 3659 3629 -63 183 -372 C ATOM 1426 CG TYR A 199 11.339 2.900 30.116 1.00 30.83 C ANISOU 1426 CG TYR A 199 4090 3948 3677 -96 193 -434 C ATOM 1427 CD1 TYR A 199 10.980 3.783 31.128 1.00 32.62 C ANISOU 1427 CD1 TYR A 199 4325 4185 3884 -105 245 -568 C ATOM 1428 CD2 TYR A 199 11.567 1.574 30.461 1.00 31.90 C ANISOU 1428 CD2 TYR A 199 4234 4180 3708 -127 148 -360 C ATOM 1429 CE1 TYR A 199 10.813 3.346 32.442 1.00 37.24 C ANISOU 1429 CE1 TYR A 199 4929 4902 4319 -150 258 -625 C ATOM 1430 CE2 TYR A 199 11.405 1.129 31.769 1.00 34.20 C ANISOU 1430 CE2 TYR A 199 4544 4585 3864 -170 151 -391 C ATOM 1431 CZ TYR A 199 11.028 2.017 32.754 1.00 33.28 C ANISOU 1431 CZ TYR A 199 4439 4504 3700 -186 207 -523 C ATOM 1432 OH TYR A 199 10.876 1.581 34.051 1.00 31.91 O ANISOU 1432 OH TYR A 199 4288 4470 3364 -241 214 -552 O ATOM 1433 N ARG A 200 13.882 5.599 27.060 1.00 29.69 N ANISOU 1433 N ARG A 200 3931 3444 3908 -109 151 -364 N ATOM 1434 CA ARG A 200 14.151 6.288 25.787 1.00 32.13 C ANISOU 1434 CA ARG A 200 4231 3651 4324 -105 158 -282 C ATOM 1435 C ARG A 200 15.429 5.792 25.108 1.00 30.26 C ANISOU 1435 C ARG A 200 3980 3447 4071 -154 129 -221 C ATOM 1436 O ARG A 200 16.492 5.788 25.725 1.00 32.31 O ANISOU 1436 O ARG A 200 4229 3727 4320 -208 102 -280 O ATOM 1437 CB ARG A 200 14.308 7.796 26.017 1.00 34.86 C ANISOU 1437 CB ARG A 200 4584 3859 4801 -119 183 -352 C ATOM 1438 CG ARG A 200 13.099 8.646 25.706 1.00 44.97 C ANISOU 1438 CG ARG A 200 5860 5035 6190 -49 220 -338 C ATOM 1439 CD ARG A 200 13.552 10.047 25.277 1.00 54.24 C ANISOU 1439 CD ARG A 200 7040 6037 7534 -70 230 -331 C ATOM 1440 NE ARG A 200 12.440 10.987 25.136 1.00 64.18 N ANISOU 1440 NE ARG A 200 8287 7165 8933 6 260 -330 N ATOM 1441 CZ ARG A 200 12.565 12.261 24.762 1.00 72.84 C ANISOU 1441 CZ ARG A 200 9386 8078 10210 6 269 -310 C ATOM 1442 NH1 ARG A 200 13.762 12.778 24.483 1.00 77.84 N ANISOU 1442 NH1 ARG A 200 10035 8643 10900 -79 257 -288 N ATOM 1443 NH2 ARG A 200 11.484 13.029 24.669 1.00 77.55 N ANISOU 1443 NH2 ARG A 200 9962 8554 10950 92 290 -306 N ATOM 1444 N ALA A 201 15.325 5.414 23.834 1.00 28.94 N ANISOU 1444 N ALA A 201 3805 3289 3901 -139 134 -111 N ATOM 1445 CA ALA A 201 16.481 4.952 23.044 1.00 27.58 C ANISOU 1445 CA ALA A 201 3609 3154 3715 -182 127 -61 C ATOM 1446 C ALA A 201 17.554 6.041 22.875 1.00 28.84 C ANISOU 1446 C ALA A 201 3755 3235 3968 -245 140 -69 C ATOM 1447 O ALA A 201 17.233 7.220 22.775 1.00 28.07 O ANISOU 1447 O ALA A 201 3675 3028 3963 -249 159 -61 O ATOM 1448 CB ALA A 201 16.010 4.466 21.673 1.00 27.10 C ANISOU 1448 CB ALA A 201 3549 3129 3619 -158 141 43 C ATOM 1449 N PRO A 202 18.840 5.647 22.818 1.00 31.63 N ANISOU 1449 N PRO A 202 4068 3634 4316 -296 130 -82 N ATOM 1450 CA PRO A 202 19.913 6.642 22.768 1.00 30.51 C ANISOU 1450 CA PRO A 202 3899 3425 4270 -372 141 -98 C ATOM 1451 C PRO A 202 19.853 7.611 21.589 1.00 32.25 C ANISOU 1451 C PRO A 202 4130 3560 4564 -399 189 5 C ATOM 1452 O PRO A 202 20.222 8.791 21.751 1.00 30.47 O ANISOU 1452 O PRO A 202 3905 3221 4450 -451 199 -8 O ATOM 1453 CB PRO A 202 21.183 5.790 22.705 1.00 31.17 C ANISOU 1453 CB PRO A 202 3916 3599 4328 -407 126 -112 C ATOM 1454 CG PRO A 202 20.733 4.453 22.236 1.00 31.66 C ANISOU 1454 CG PRO A 202 3980 3752 4298 -346 125 -73 C ATOM 1455 CD PRO A 202 19.378 4.276 22.824 1.00 30.76 C ANISOU 1455 CD PRO A 202 3923 3631 4133 -287 106 -86 C ATOM 1456 N GLU A 203 19.395 7.136 20.428 1.00 31.04 N ANISOU 1456 N GLU A 203 3987 3458 4349 -371 214 110 N ATOM 1457 CA GLU A 203 19.222 8.008 19.259 1.00 32.91 C ANISOU 1457 CA GLU A 203 4242 3634 4629 -398 249 238 C ATOM 1458 C GLU A 203 18.278 9.195 19.524 1.00 34.90 C ANISOU 1458 C GLU A 203 4535 3739 4988 -366 238 262 C ATOM 1459 O GLU A 203 18.499 10.293 19.012 1.00 36.46 O ANISOU 1459 O GLU A 203 4740 3825 5288 -411 257 344 O ATOM 1460 CB GLU A 203 18.781 7.219 18.012 1.00 33.08 C ANISOU 1460 CB GLU A 203 4272 3764 4534 -374 266 335 C ATOM 1461 CG GLU A 203 17.422 6.545 18.076 1.00 32.53 C ANISOU 1461 CG GLU A 203 4231 3735 4393 -289 231 336 C ATOM 1462 CD GLU A 203 17.475 5.095 18.540 1.00 34.47 C ANISOU 1462 CD GLU A 203 4459 4087 4551 -259 215 247 C ATOM 1463 OE1 GLU A 203 18.400 4.710 19.289 1.00 31.49 O ANISOU 1463 OE1 GLU A 203 4049 3726 4189 -280 210 163 O ATOM 1464 OE2 GLU A 203 16.569 4.334 18.158 1.00 32.17 O ANISOU 1464 OE2 GLU A 203 4181 3857 4184 -214 199 267 O ATOM 1465 N LEU A 204 17.245 8.989 20.336 1.00 34.97 N ANISOU 1465 N LEU A 204 4563 3738 4986 -290 212 191 N ATOM 1466 CA LEU A 204 16.391 10.107 20.758 1.00 36.16 C ANISOU 1466 CA LEU A 204 4736 3742 5263 -250 209 176 C ATOM 1467 C LEU A 204 17.146 11.065 21.684 1.00 36.19 C ANISOU 1467 C LEU A 204 4736 3628 5388 -307 216 62 C ATOM 1468 O LEU A 204 16.967 12.269 21.595 1.00 36.37 O ANISOU 1468 O LEU A 204 4770 3487 5561 -313 227 84 O ATOM 1469 CB LEU A 204 15.121 9.612 21.461 1.00 34.96 C ANISOU 1469 CB LEU A 204 4590 3627 5067 -160 196 109 C ATOM 1470 CG LEU A 204 14.065 8.930 20.599 1.00 36.10 C ANISOU 1470 CG LEU A 204 4733 3851 5133 -98 181 215 C ATOM 1471 CD1 LEU A 204 12.979 8.348 21.492 1.00 33.85 C ANISOU 1471 CD1 LEU A 204 4439 3615 4806 -29 176 127 C ATOM 1472 CD2 LEU A 204 13.479 9.885 19.581 1.00 36.26 C ANISOU 1472 CD2 LEU A 204 4759 3772 5248 -73 173 361 C ATOM 1473 N LEU A 205 17.991 10.531 22.561 1.00 35.85 N ANISOU 1473 N LEU A 205 4673 3664 5286 -351 202 -58 N ATOM 1474 CA LEU A 205 18.798 11.370 23.452 1.00 35.99 C ANISOU 1474 CA LEU A 205 4680 3594 5401 -422 196 -181 C ATOM 1475 C LEU A 205 19.881 12.139 22.685 1.00 38.20 C ANISOU 1475 C LEU A 205 4936 3791 5788 -518 215 -103 C ATOM 1476 O LEU A 205 20.369 13.176 23.151 1.00 41.47 O ANISOU 1476 O LEU A 205 5345 4075 6336 -582 216 -176 O ATOM 1477 CB LEU A 205 19.443 10.532 24.563 1.00 35.50 C ANISOU 1477 CB LEU A 205 4595 3661 5231 -448 157 -310 C ATOM 1478 CG LEU A 205 18.519 9.647 25.401 1.00 36.76 C ANISOU 1478 CG LEU A 205 4777 3926 5264 -375 140 -375 C ATOM 1479 CD1 LEU A 205 19.317 8.860 26.436 1.00 34.36 C ANISOU 1479 CD1 LEU A 205 4450 3749 4856 -415 87 -467 C ATOM 1480 CD2 LEU A 205 17.426 10.482 26.059 1.00 39.49 C ANISOU 1480 CD2 LEU A 205 5157 4175 5674 -327 166 -465 C ATOM 1481 N LEU A 206 20.259 11.642 21.510 1.00 37.04 N ANISOU 1481 N LEU A 206 4771 3722 5582 -537 236 38 N ATOM 1482 CA LEU A 206 21.211 12.356 20.659 1.00 38.82 C ANISOU 1482 CA LEU A 206 4969 3885 5894 -635 271 136 C ATOM 1483 C LEU A 206 20.514 13.177 19.559 1.00 39.44 C ANISOU 1483 C LEU A 206 5088 3853 6044 -622 296 313 C ATOM 1484 O LEU A 206 21.138 13.554 18.573 1.00 39.52 O ANISOU 1484 O LEU A 206 5084 3852 6079 -700 333 446 O ATOM 1485 CB LEU A 206 22.217 11.377 20.056 1.00 36.66 C ANISOU 1485 CB LEU A 206 4640 3776 5515 -681 293 172 C ATOM 1486 CG LEU A 206 23.089 10.633 21.071 1.00 37.01 C ANISOU 1486 CG LEU A 206 4627 3918 5519 -700 256 26 C ATOM 1487 CD1 LEU A 206 23.842 9.479 20.393 1.00 34.11 C ANISOU 1487 CD1 LEU A 206 4197 3710 5052 -706 280 63 C ATOM 1488 CD2 LEU A 206 24.054 11.591 21.755 1.00 36.39 C ANISOU 1488 CD2 LEU A 206 4508 3744 5575 -801 242 -60 C ATOM 1489 N GLY A 207 19.218 13.437 19.727 1.00 41.06 N ANISOU 1489 N GLY A 207 5335 3985 6280 -526 275 321 N ATOM 1490 CA GLY A 207 18.494 14.389 18.877 1.00 41.91 C ANISOU 1490 CA GLY A 207 5474 3952 6496 -502 277 485 C ATOM 1491 C GLY A 207 17.778 13.856 17.640 1.00 41.88 C ANISOU 1491 C GLY A 207 5487 4056 6370 -456 269 665 C ATOM 1492 O GLY A 207 17.381 14.648 16.780 1.00 42.59 O ANISOU 1492 O GLY A 207 5598 4049 6536 -457 262 840 O ATOM 1493 N ALA A 208 17.589 12.539 17.537 1.00 39.46 N ANISOU 1493 N ALA A 208 5171 3942 5879 -418 263 629 N ATOM 1494 CA ALA A 208 16.870 11.970 16.390 1.00 40.17 C ANISOU 1494 CA ALA A 208 5276 4148 5840 -381 249 774 C ATOM 1495 C ALA A 208 15.485 12.605 16.240 1.00 43.83 C ANISOU 1495 C ALA A 208 5758 4506 6389 -289 203 860 C ATOM 1496 O ALA A 208 14.784 12.849 17.223 1.00 43.37 O ANISOU 1496 O ALA A 208 5695 4358 6427 -214 187 748 O ATOM 1497 CB ALA A 208 16.751 10.474 16.518 1.00 38.65 C ANISOU 1497 CB ALA A 208 5069 4144 5473 -346 244 684 C ATOM 1498 N ARG A 209 15.098 12.864 14.996 1.00 48.59 N ANISOU 1498 N ARG A 209 6377 5131 6954 -295 181 1061 N ATOM 1499 CA ARG A 209 13.944 13.712 14.704 1.00 52.58 C ANISOU 1499 CA ARG A 209 6888 5507 7582 -217 127 1189 C ATOM 1500 C ARG A 209 12.624 12.958 14.524 1.00 50.95 C ANISOU 1500 C ARG A 209 6665 5410 7282 -116 72 1198 C ATOM 1501 O ARG A 209 11.566 13.583 14.501 1.00 51.29 O ANISOU 1501 O ARG A 209 6692 5347 7447 -30 23 1269 O ATOM 1502 CB ARG A 209 14.225 14.537 13.443 1.00 56.19 C ANISOU 1502 CB ARG A 209 7370 5919 8061 -285 117 1437 C ATOM 1503 CG ARG A 209 15.408 15.499 13.563 1.00 65.22 C ANISOU 1503 CG ARG A 209 8523 6916 9343 -391 169 1459 C ATOM 1504 CD ARG A 209 15.189 16.563 14.640 1.00 71.19 C ANISOU 1504 CD ARG A 209 9272 7411 10365 -346 163 1357 C ATOM 1505 NE ARG A 209 13.895 17.234 14.506 1.00 75.60 N ANISOU 1505 NE ARG A 209 9828 7829 11066 -232 100 1458 N ATOM 1506 CZ ARG A 209 13.628 18.226 13.656 1.00 79.36 C ANISOU 1506 CZ ARG A 209 10319 8165 11668 -237 60 1696 C ATOM 1507 NH1 ARG A 209 14.562 18.695 12.830 1.00 82.82 N ANISOU 1507 NH1 ARG A 209 10785 8589 12094 -364 85 1868 N ATOM 1508 NH2 ARG A 209 12.409 18.754 13.630 1.00 79.96 N ANISOU 1508 NH2 ARG A 209 10377 8116 11890 -113 -6 1771 N ATOM 1509 N HIS A 210 12.686 11.633 14.386 1.00 48.64 N ANISOU 1509 N HIS A 210 6368 5320 6792 -127 79 1127 N ATOM 1510 CA HIS A 210 11.497 10.824 14.106 1.00 47.38 C ANISOU 1510 CA HIS A 210 6190 5281 6533 -54 26 1138 C ATOM 1511 C HIS A 210 11.437 9.596 15.005 1.00 42.33 C ANISOU 1511 C HIS A 210 5533 4744 5806 -32 49 944 C ATOM 1512 O HIS A 210 12.451 8.942 15.238 1.00 41.69 O ANISOU 1512 O HIS A 210 5461 4733 5645 -92 93 852 O ATOM 1513 CB HIS A 210 11.490 10.360 12.640 1.00 49.01 C ANISOU 1513 CB HIS A 210 6413 5652 6558 -105 -3 1294 C ATOM 1514 CG HIS A 210 11.627 11.472 11.649 1.00 58.24 C ANISOU 1514 CG HIS A 210 7604 6750 7774 -146 -28 1519 C ATOM 1515 ND1 HIS A 210 10.595 12.335 11.349 1.00 63.86 N ANISOU 1515 ND1 HIS A 210 8302 7354 8607 -74 -106 1672 N ATOM 1516 CD2 HIS A 210 12.676 11.860 10.885 1.00 64.15 C ANISOU 1516 CD2 HIS A 210 8384 7520 8469 -254 16 1630 C ATOM 1517 CE1 HIS A 210 11.003 13.210 10.447 1.00 67.68 C ANISOU 1517 CE1 HIS A 210 8817 7789 9111 -137 -118 1882 C ATOM 1518 NE2 HIS A 210 12.263 12.943 10.149 1.00 65.99 N ANISOU 1518 NE2 HIS A 210 8632 7657 8784 -253 -39 1860 N ATOM 1519 N TYR A 211 10.241 9.287 15.501 1.00 38.52 N ANISOU 1519 N TYR A 211 5018 4268 5349 54 16 892 N ATOM 1520 CA TYR A 211 10.009 8.027 16.189 1.00 37.18 C ANISOU 1520 CA TYR A 211 4833 4211 5081 68 28 748 C ATOM 1521 C TYR A 211 10.049 6.875 15.194 1.00 35.59 C ANISOU 1521 C TYR A 211 4638 4185 4699 27 8 788 C ATOM 1522 O TYR A 211 9.708 7.030 14.021 1.00 37.73 O ANISOU 1522 O TYR A 211 4913 4512 4911 15 -35 925 O ATOM 1523 CB TYR A 211 8.685 8.040 16.950 1.00 36.69 C ANISOU 1523 CB TYR A 211 4725 4116 5098 160 11 691 C ATOM 1524 CG TYR A 211 8.776 8.789 18.251 1.00 37.69 C ANISOU 1524 CG TYR A 211 4847 4109 5365 190 56 567 C ATOM 1525 CD1 TYR A 211 9.268 8.170 19.389 1.00 37.60 C ANISOU 1525 CD1 TYR A 211 4847 4138 5302 165 99 409 C ATOM 1526 CD2 TYR A 211 8.391 10.130 18.341 1.00 45.00 C ANISOU 1526 CD2 TYR A 211 5758 4865 6476 242 54 607 C ATOM 1527 CE1 TYR A 211 9.361 8.848 20.593 1.00 42.52 C ANISOU 1527 CE1 TYR A 211 5468 4661 6025 181 140 281 C ATOM 1528 CE2 TYR A 211 8.484 10.822 19.543 1.00 48.79 C ANISOU 1528 CE2 TYR A 211 6234 5222 7082 265 103 463 C ATOM 1529 CZ TYR A 211 8.971 10.168 20.667 1.00 47.66 C ANISOU 1529 CZ TYR A 211 6105 5148 6856 229 147 294 C ATOM 1530 OH TYR A 211 9.070 10.831 21.867 1.00 53.78 O ANISOU 1530 OH TYR A 211 6880 5827 7727 240 194 137 O ATOM 1531 N THR A 212 10.497 5.725 15.667 1.00 33.55 N ANISOU 1531 N THR A 212 4382 4012 4354 3 35 665 N ATOM 1532 CA THR A 212 10.671 4.559 14.808 1.00 33.24 C ANISOU 1532 CA THR A 212 4348 4121 4160 -39 28 663 C ATOM 1533 C THR A 212 10.243 3.291 15.535 1.00 29.15 C ANISOU 1533 C THR A 212 3812 3660 3605 -17 25 542 C ATOM 1534 O THR A 212 10.095 3.289 16.753 1.00 25.43 O ANISOU 1534 O THR A 212 3330 3130 3203 14 40 461 O ATOM 1535 CB THR A 212 12.148 4.388 14.450 1.00 34.48 C ANISOU 1535 CB THR A 212 4525 4311 4264 -113 83 641 C ATOM 1536 OG1 THR A 212 12.895 4.189 15.662 1.00 32.26 O ANISOU 1536 OG1 THR A 212 4237 3975 4046 -113 117 520 O ATOM 1537 CG2 THR A 212 12.677 5.615 13.693 1.00 31.21 C ANISOU 1537 CG2 THR A 212 4130 3846 3883 -156 97 774 C ATOM 1538 N LYS A 213 10.082 2.213 14.778 1.00 27.74 N ANISOU 1538 N LYS A 213 3631 3597 3311 -43 8 529 N ATOM 1539 CA LYS A 213 9.834 0.889 15.355 1.00 28.62 C ANISOU 1539 CA LYS A 213 3728 3751 3393 -39 7 422 C ATOM 1540 C LYS A 213 10.963 0.467 16.290 1.00 27.88 C ANISOU 1540 C LYS A 213 3644 3620 3329 -53 52 329 C ATOM 1541 O LYS A 213 10.712 -0.085 17.360 1.00 30.29 O ANISOU 1541 O LYS A 213 3940 3903 3666 -33 50 265 O ATOM 1542 CB LYS A 213 9.631 -0.157 14.249 1.00 28.40 C ANISOU 1542 CB LYS A 213 3701 3842 3249 -76 -15 409 C ATOM 1543 CG LYS A 213 8.400 0.115 13.374 1.00 30.25 C ANISOU 1543 CG LYS A 213 3916 4138 3440 -67 -82 499 C ATOM 1544 CD LYS A 213 8.235 -0.938 12.300 1.00 34.74 C ANISOU 1544 CD LYS A 213 4488 4834 3878 -118 -107 461 C ATOM 1545 CE LYS A 213 7.081 -0.592 11.357 1.00 40.23 C ANISOU 1545 CE LYS A 213 5160 5611 4514 -119 -191 563 C ATOM 1546 NZ LYS A 213 6.753 -1.711 10.421 1.00 39.22 N ANISOU 1546 NZ LYS A 213 5030 5616 4256 -176 -226 498 N ATOM 1547 N ALA A 214 12.202 0.775 15.918 1.00 28.70 N ANISOU 1547 N ALA A 214 3760 3720 3424 -91 89 331 N ATOM 1548 CA ALA A 214 13.361 0.423 16.746 1.00 26.82 C ANISOU 1548 CA ALA A 214 3515 3453 3224 -104 119 251 C ATOM 1549 C ALA A 214 13.354 1.090 18.123 1.00 27.21 C ANISOU 1549 C ALA A 214 3564 3416 3358 -81 114 222 C ATOM 1550 O ALA A 214 13.824 0.504 19.100 1.00 25.76 O ANISOU 1550 O ALA A 214 3373 3227 3188 -80 111 154 O ATOM 1551 CB ALA A 214 14.668 0.742 16.000 1.00 26.72 C ANISOU 1551 CB ALA A 214 3496 3461 3195 -155 165 264 C ATOM 1552 N ILE A 215 12.824 2.312 18.201 1.00 27.79 N ANISOU 1552 N ILE A 215 3647 3424 3490 -63 112 273 N ATOM 1553 CA ILE A 215 12.740 3.029 19.467 1.00 27.09 C ANISOU 1553 CA ILE A 215 3559 3254 3479 -44 116 221 C ATOM 1554 C ILE A 215 11.825 2.275 20.436 1.00 28.59 C ANISOU 1554 C ILE A 215 3740 3475 3646 -9 104 164 C ATOM 1555 O ILE A 215 12.174 2.112 21.606 1.00 30.12 O ANISOU 1555 O ILE A 215 3938 3664 3843 -16 108 91 O ATOM 1556 CB ILE A 215 12.290 4.500 19.267 1.00 28.16 C ANISOU 1556 CB ILE A 215 3700 3290 3709 -24 120 280 C ATOM 1557 CG1 ILE A 215 13.455 5.325 18.716 1.00 29.29 C ANISOU 1557 CG1 ILE A 215 3853 3382 3893 -79 142 325 C ATOM 1558 CG2 ILE A 215 11.794 5.105 20.568 1.00 25.74 C ANISOU 1558 CG2 ILE A 215 3390 2910 3480 12 131 198 C ATOM 1559 CD1 ILE A 215 13.046 6.637 18.043 1.00 25.57 C ANISOU 1559 CD1 ILE A 215 3391 2813 3510 -70 138 435 C ATOM 1560 N ASP A 216 10.685 1.797 19.936 1.00 29.59 N ANISOU 1560 N ASP A 216 3852 3645 3743 19 85 202 N ATOM 1561 CA ASP A 216 9.807 0.895 20.692 1.00 28.91 C ANISOU 1561 CA ASP A 216 3750 3603 3630 36 79 162 C ATOM 1562 C ASP A 216 10.519 -0.382 21.143 1.00 30.18 C ANISOU 1562 C ASP A 216 3921 3807 3739 4 73 118 C ATOM 1563 O ASP A 216 10.340 -0.822 22.271 1.00 32.86 O ANISOU 1563 O ASP A 216 4261 4158 4067 2 75 80 O ATOM 1564 CB ASP A 216 8.586 0.491 19.854 1.00 28.75 C ANISOU 1564 CB ASP A 216 3701 3632 3590 55 52 214 C ATOM 1565 CG ASP A 216 7.539 1.582 19.744 1.00 28.91 C ANISOU 1565 CG ASP A 216 3689 3610 3683 106 47 258 C ATOM 1566 OD1 ASP A 216 7.639 2.624 20.441 1.00 29.68 O ANISOU 1566 OD1 ASP A 216 3789 3629 3858 132 76 231 O ATOM 1567 OD2 ASP A 216 6.593 1.379 18.937 1.00 28.90 O ANISOU 1567 OD2 ASP A 216 3655 3654 3671 121 10 315 O ATOM 1568 N ILE A 217 11.314 -0.988 20.262 1.00 29.60 N ANISOU 1568 N ILE A 217 3852 3759 3637 -22 65 127 N ATOM 1569 CA ILE A 217 12.033 -2.220 20.612 1.00 29.32 C ANISOU 1569 CA ILE A 217 3814 3742 3583 -39 55 88 C ATOM 1570 C ILE A 217 13.032 -1.998 21.763 1.00 29.08 C ANISOU 1570 C ILE A 217 3787 3686 3577 -49 53 53 C ATOM 1571 O ILE A 217 13.180 -2.845 22.648 1.00 27.86 O ANISOU 1571 O ILE A 217 3632 3541 3413 -52 30 38 O ATOM 1572 CB ILE A 217 12.761 -2.832 19.382 1.00 29.18 C ANISOU 1572 CB ILE A 217 3790 3753 3545 -59 62 80 C ATOM 1573 CG1 ILE A 217 11.760 -3.216 18.283 1.00 29.95 C ANISOU 1573 CG1 ILE A 217 3886 3899 3596 -62 51 101 C ATOM 1574 CG2 ILE A 217 13.556 -4.060 19.780 1.00 30.50 C ANISOU 1574 CG2 ILE A 217 3942 3914 3732 -62 51 34 C ATOM 1575 CD1 ILE A 217 10.660 -4.142 18.726 1.00 29.62 C ANISOU 1575 CD1 ILE A 217 3835 3866 3555 -57 24 91 C ATOM 1576 N TRP A 218 13.700 -0.848 21.762 1.00 31.28 N ANISOU 1576 N TRP A 218 4069 3931 3887 -59 69 48 N ATOM 1577 CA TRP A 218 14.634 -0.518 22.840 1.00 30.13 C ANISOU 1577 CA TRP A 218 3921 3768 3760 -77 56 4 C ATOM 1578 C TRP A 218 13.903 -0.428 24.172 1.00 27.45 C ANISOU 1578 C TRP A 218 3598 3439 3393 -70 48 -26 C ATOM 1579 O TRP A 218 14.360 -0.975 25.162 1.00 30.29 O ANISOU 1579 O TRP A 218 3958 3829 3722 -86 17 -46 O ATOM 1580 CB TRP A 218 15.388 0.779 22.542 1.00 30.03 C ANISOU 1580 CB TRP A 218 3904 3706 3800 -102 78 -1 C ATOM 1581 CG TRP A 218 16.249 1.263 23.681 1.00 29.12 C ANISOU 1581 CG TRP A 218 3783 3575 3706 -131 58 -61 C ATOM 1582 CD1 TRP A 218 15.846 2.015 24.750 1.00 27.69 C ANISOU 1582 CD1 TRP A 218 3623 3372 3527 -135 57 -116 C ATOM 1583 CD2 TRP A 218 17.650 1.031 23.858 1.00 26.58 C ANISOU 1583 CD2 TRP A 218 3424 3269 3407 -165 34 -84 C ATOM 1584 NE1 TRP A 218 16.907 2.260 25.584 1.00 29.04 N ANISOU 1584 NE1 TRP A 218 3780 3550 3705 -177 26 -173 N ATOM 1585 CE2 TRP A 218 18.029 1.669 25.061 1.00 26.79 C ANISOU 1585 CE2 TRP A 218 3454 3287 3439 -194 6 -146 C ATOM 1586 CE3 TRP A 218 18.622 0.340 23.123 1.00 30.41 C ANISOU 1586 CE3 TRP A 218 3864 3780 3912 -173 36 -68 C ATOM 1587 CZ2 TRP A 218 19.342 1.644 25.544 1.00 25.69 C ANISOU 1587 CZ2 TRP A 218 3271 3167 3323 -235 -36 -180 C ATOM 1588 CZ3 TRP A 218 19.934 0.312 23.608 1.00 28.46 C ANISOU 1588 CZ3 TRP A 218 3564 3544 3704 -203 4 -102 C ATOM 1589 CH2 TRP A 218 20.277 0.962 24.807 1.00 24.83 C ANISOU 1589 CH2 TRP A 218 3107 3079 3249 -235 -38 -150 C ATOM 1590 N ALA A 219 12.766 0.255 24.196 1.00 28.11 N ANISOU 1590 N ALA A 219 3690 3505 3486 -46 76 -26 N ATOM 1591 CA ALA A 219 11.939 0.322 25.410 1.00 27.84 C ANISOU 1591 CA ALA A 219 3663 3498 3419 -40 90 -67 C ATOM 1592 C ALA A 219 11.542 -1.085 25.907 1.00 25.87 C ANISOU 1592 C ALA A 219 3412 3315 3104 -50 70 -39 C ATOM 1593 O ALA A 219 11.582 -1.363 27.104 1.00 25.63 O ANISOU 1593 O ALA A 219 3394 3330 3015 -73 63 -62 O ATOM 1594 CB ALA A 219 10.696 1.175 25.169 1.00 27.67 C ANISOU 1594 CB ALA A 219 3628 3443 3442 1 129 -70 C ATOM 1595 N ILE A 220 11.170 -1.966 24.985 1.00 24.90 N ANISOU 1595 N ILE A 220 3277 3198 2988 -42 59 12 N ATOM 1596 CA ILE A 220 10.795 -3.332 25.355 1.00 27.08 C ANISOU 1596 CA ILE A 220 3549 3509 3229 -58 39 44 C ATOM 1597 C ILE A 220 11.983 -4.038 26.012 1.00 25.90 C ANISOU 1597 C ILE A 220 3410 3364 3066 -80 -6 52 C ATOM 1598 O ILE A 220 11.836 -4.708 27.033 1.00 26.18 O ANISOU 1598 O ILE A 220 3457 3435 3057 -102 -25 79 O ATOM 1599 CB ILE A 220 10.284 -4.132 24.133 1.00 27.35 C ANISOU 1599 CB ILE A 220 3567 3537 3289 -52 30 76 C ATOM 1600 CG1 ILE A 220 8.922 -3.595 23.690 1.00 26.26 C ANISOU 1600 CG1 ILE A 220 3405 3413 3158 -33 55 84 C ATOM 1601 CG2 ILE A 220 10.198 -5.625 24.457 1.00 25.58 C ANISOU 1601 CG2 ILE A 220 3342 3317 3061 -76 2 105 C ATOM 1602 CD1 ILE A 220 8.470 -4.137 22.332 1.00 24.82 C ANISOU 1602 CD1 ILE A 220 3205 3240 2987 -34 35 106 C ATOM 1603 N GLY A 221 13.164 -3.859 25.433 1.00 25.79 N ANISOU 1603 N GLY A 221 3387 3321 3092 -75 -24 38 N ATOM 1604 CA GLY A 221 14.396 -4.359 26.038 1.00 26.71 C ANISOU 1604 CA GLY A 221 3493 3439 3217 -87 -74 43 C ATOM 1605 C GLY A 221 14.625 -3.838 27.446 1.00 26.34 C ANISOU 1605 C GLY A 221 3463 3436 3109 -114 -97 25 C ATOM 1606 O GLY A 221 14.994 -4.600 28.340 1.00 28.03 O ANISOU 1606 O GLY A 221 3679 3682 3289 -130 -151 64 O ATOM 1607 N CYS A 222 14.402 -2.543 27.653 1.00 27.48 N ANISOU 1607 N CYS A 222 3620 3580 3240 -121 -60 -34 N ATOM 1608 CA CYS A 222 14.483 -1.964 29.003 1.00 27.35 C ANISOU 1608 CA CYS A 222 3625 3616 3152 -153 -70 -83 C ATOM 1609 C CYS A 222 13.495 -2.638 29.963 1.00 26.89 C ANISOU 1609 C CYS A 222 3588 3630 2998 -169 -61 -51 C ATOM 1610 O CYS A 222 13.825 -2.907 31.122 1.00 26.71 O ANISOU 1610 O CYS A 222 3582 3681 2886 -207 -102 -43 O ATOM 1611 CB CYS A 222 14.206 -0.462 28.971 1.00 29.36 C ANISOU 1611 CB CYS A 222 3888 3834 3434 -152 -17 -169 C ATOM 1612 SG CYS A 222 15.355 0.490 27.978 1.00 30.26 S ANISOU 1612 SG CYS A 222 3979 3863 3656 -156 -20 -192 S ATOM 1613 N ILE A 223 12.284 -2.901 29.482 1.00 26.61 N ANISOU 1613 N ILE A 223 3549 3585 2976 -148 -11 -27 N ATOM 1614 CA ILE A 223 11.260 -3.544 30.312 1.00 28.22 C ANISOU 1614 CA ILE A 223 3763 3860 3101 -172 14 8 C ATOM 1615 C ILE A 223 11.678 -4.974 30.650 1.00 26.79 C ANISOU 1615 C ILE A 223 3588 3695 2896 -198 -53 111 C ATOM 1616 O ILE A 223 11.566 -5.401 31.794 1.00 28.49 O ANISOU 1616 O ILE A 223 3824 3988 3012 -242 -69 153 O ATOM 1617 CB ILE A 223 9.858 -3.518 29.634 1.00 28.74 C ANISOU 1617 CB ILE A 223 3803 3910 3208 -145 78 12 C ATOM 1618 CG1 ILE A 223 9.385 -2.068 29.442 1.00 30.14 C ANISOU 1618 CG1 ILE A 223 3967 4060 3424 -110 137 -78 C ATOM 1619 CG2 ILE A 223 8.836 -4.289 30.469 1.00 26.35 C ANISOU 1619 CG2 ILE A 223 3497 3684 2832 -183 109 57 C ATOM 1620 CD1 ILE A 223 8.129 -1.930 28.574 1.00 25.98 C ANISOU 1620 CD1 ILE A 223 3398 3509 2965 -70 179 -64 C ATOM 1621 N PHE A 224 12.191 -5.699 29.661 1.00 28.88 N ANISOU 1621 N PHE A 224 3835 3885 3255 -172 -91 152 N ATOM 1622 CA PHE A 224 12.613 -7.096 29.859 1.00 30.92 C ANISOU 1622 CA PHE A 224 4091 4122 3536 -183 -156 247 C ATOM 1623 C PHE A 224 13.715 -7.191 30.920 1.00 32.14 C ANISOU 1623 C PHE A 224 4252 4320 3638 -204 -233 281 C ATOM 1624 O PHE A 224 13.677 -8.045 31.805 1.00 34.07 O ANISOU 1624 O PHE A 224 4513 4601 3831 -237 -281 377 O ATOM 1625 CB PHE A 224 13.074 -7.680 28.516 1.00 30.99 C ANISOU 1625 CB PHE A 224 4070 4037 3667 -144 -170 242 C ATOM 1626 CG PHE A 224 13.486 -9.137 28.557 1.00 32.64 C ANISOU 1626 CG PHE A 224 4268 4188 3945 -141 -230 321 C ATOM 1627 CD1 PHE A 224 12.909 -10.045 29.444 1.00 29.95 C ANISOU 1627 CD1 PHE A 224 3947 3861 3571 -180 -255 420 C ATOM 1628 CD2 PHE A 224 14.429 -9.610 27.647 1.00 29.30 C ANISOU 1628 CD2 PHE A 224 3810 3689 3634 -101 -255 296 C ATOM 1629 CE1 PHE A 224 13.302 -11.383 29.439 1.00 31.62 C ANISOU 1629 CE1 PHE A 224 4148 3989 3878 -174 -316 502 C ATOM 1630 CE2 PHE A 224 14.820 -10.937 27.641 1.00 29.58 C ANISOU 1630 CE2 PHE A 224 3828 3647 3766 -87 -308 354 C ATOM 1631 CZ PHE A 224 14.254 -11.828 28.540 1.00 28.74 C ANISOU 1631 CZ PHE A 224 3744 3531 3644 -122 -345 463 C ATOM 1632 N ALA A 225 14.688 -6.298 30.833 1.00 31.46 N ANISOU 1632 N ALA A 225 4153 4235 3565 -193 -252 211 N ATOM 1633 CA ALA A 225 15.786 -6.264 31.795 1.00 31.01 C ANISOU 1633 CA ALA A 225 4091 4232 3460 -217 -338 230 C ATOM 1634 C ALA A 225 15.235 -6.006 33.197 1.00 29.78 C ANISOU 1634 C ALA A 225 3979 4196 3138 -276 -337 238 C ATOM 1635 O ALA A 225 15.639 -6.640 34.165 1.00 30.88 O ANISOU 1635 O ALA A 225 4129 4401 3202 -310 -417 326 O ATOM 1636 CB ALA A 225 16.783 -5.189 31.407 1.00 27.82 C ANISOU 1636 CB ALA A 225 3657 3810 3104 -209 -342 135 C ATOM 1637 N GLU A 226 14.279 -5.093 33.278 1.00 27.58 N ANISOU 1637 N GLU A 226 3724 3951 2806 -287 -243 149 N ATOM 1638 CA GLU A 226 13.674 -4.733 34.540 1.00 30.17 C ANISOU 1638 CA GLU A 226 4089 4402 2971 -343 -213 121 C ATOM 1639 C GLU A 226 12.858 -5.893 35.113 1.00 31.29 C ANISOU 1639 C GLU A 226 4250 4601 3038 -378 -209 249 C ATOM 1640 O GLU A 226 12.879 -6.125 36.321 1.00 30.38 O ANISOU 1640 O GLU A 226 4166 4608 2770 -440 -238 297 O ATOM 1641 CB GLU A 226 12.822 -3.483 34.362 1.00 30.56 C ANISOU 1641 CB GLU A 226 4142 4448 3022 -330 -102 -17 C ATOM 1642 CG GLU A 226 12.296 -2.878 35.641 1.00 31.00 C ANISOU 1642 CG GLU A 226 4228 4633 2917 -384 -51 -100 C ATOM 1643 CD GLU A 226 11.719 -1.487 35.446 1.00 32.78 C ANISOU 1643 CD GLU A 226 4445 4823 3188 -357 48 -263 C ATOM 1644 OE1 GLU A 226 11.779 -0.953 34.307 1.00 34.80 O ANISOU 1644 OE1 GLU A 226 4674 4951 3596 -299 64 -291 O ATOM 1645 OE2 GLU A 226 11.210 -0.926 36.446 1.00 37.06 O ANISOU 1645 OE2 GLU A 226 5006 5465 3611 -394 110 -364 O ATOM 1646 N LEU A 227 12.165 -6.634 34.251 1.00 30.80 N ANISOU 1646 N LEU A 227 4170 4455 3078 -349 -176 309 N ATOM 1647 CA LEU A 227 11.482 -7.854 34.684 1.00 33.03 C ANISOU 1647 CA LEU A 227 4463 4761 3324 -390 -180 445 C ATOM 1648 C LEU A 227 12.466 -8.913 35.217 1.00 36.20 C ANISOU 1648 C LEU A 227 4875 5156 3724 -408 -305 589 C ATOM 1649 O LEU A 227 12.148 -9.640 36.159 1.00 36.28 O ANISOU 1649 O LEU A 227 4912 5239 3633 -469 -328 713 O ATOM 1650 CB LEU A 227 10.647 -8.445 33.550 1.00 32.72 C ANISOU 1650 CB LEU A 227 4395 4619 3417 -360 -134 465 C ATOM 1651 CG LEU A 227 9.396 -7.664 33.111 1.00 33.02 C ANISOU 1651 CG LEU A 227 4411 4675 3461 -347 -22 369 C ATOM 1652 CD1 LEU A 227 8.785 -8.305 31.884 1.00 28.80 C ANISOU 1652 CD1 LEU A 227 3843 4041 3060 -320 -9 390 C ATOM 1653 CD2 LEU A 227 8.374 -7.557 34.222 1.00 30.57 C ANISOU 1653 CD2 LEU A 227 4108 4493 3014 -409 55 377 C ATOM 1654 N LEU A 228 13.648 -8.994 34.604 1.00 35.64 N ANISOU 1654 N LEU A 228 4775 4997 3769 -356 -383 579 N ATOM 1655 CA LEU A 228 14.659 -9.981 34.985 1.00 36.25 C ANISOU 1655 CA LEU A 228 4840 5045 3889 -351 -510 711 C ATOM 1656 C LEU A 228 15.369 -9.655 36.291 1.00 36.94 C ANISOU 1656 C LEU A 228 4947 5270 3819 -401 -596 748 C ATOM 1657 O LEU A 228 15.789 -10.561 36.993 1.00 36.65 O ANISOU 1657 O LEU A 228 4915 5254 3758 -423 -699 905 O ATOM 1658 CB LEU A 228 15.702 -10.139 33.866 1.00 35.66 C ANISOU 1658 CB LEU A 228 4707 4839 4001 -273 -553 669 C ATOM 1659 CG LEU A 228 15.176 -10.891 32.642 1.00 34.61 C ANISOU 1659 CG LEU A 228 4556 4571 4024 -232 -503 666 C ATOM 1660 CD1 LEU A 228 16.083 -10.672 31.437 1.00 32.25 C ANISOU 1660 CD1 LEU A 228 4203 4182 3869 -164 -501 571 C ATOM 1661 CD2 LEU A 228 15.021 -12.372 32.967 1.00 33.36 C ANISOU 1661 CD2 LEU A 228 4401 4341 3931 -243 -564 824 C ATOM 1662 N THR A 229 15.501 -8.367 36.610 1.00 36.16 N ANISOU 1662 N THR A 229 4859 5263 3619 -421 -560 606 N ATOM 1663 CA THR A 229 16.239 -7.937 37.798 1.00 37.33 C ANISOU 1663 CA THR A 229 5022 5552 3608 -477 -646 605 C ATOM 1664 C THR A 229 15.408 -7.195 38.851 1.00 36.79 C ANISOU 1664 C THR A 229 5011 5652 3315 -556 -570 530 C ATOM 1665 O THR A 229 15.890 -6.983 39.958 1.00 37.10 O ANISOU 1665 O THR A 229 5074 5838 3185 -620 -642 539 O ATOM 1666 CB THR A 229 17.376 -6.978 37.406 1.00 37.65 C ANISOU 1666 CB THR A 229 5018 5566 3721 -448 -687 474 C ATOM 1667 OG1 THR A 229 16.813 -5.712 37.046 1.00 34.87 O ANISOU 1667 OG1 THR A 229 4682 5210 3359 -449 -566 296 O ATOM 1668 CG2 THR A 229 18.188 -7.540 36.232 1.00 35.70 C ANISOU 1668 CG2 THR A 229 4703 5161 3701 -367 -729 508 C ATOM 1669 N SER A 230 14.193 -6.777 38.491 1.00 36.59 N ANISOU 1669 N SER A 230 4999 5612 3291 -551 -425 445 N ATOM 1670 CA SER A 230 13.319 -5.953 39.341 1.00 40.02 C ANISOU 1670 CA SER A 230 5471 6190 3547 -610 -320 331 C ATOM 1671 C SER A 230 13.757 -4.491 39.495 1.00 40.91 C ANISOU 1671 C SER A 230 5583 6332 3628 -612 -295 121 C ATOM 1672 O SER A 230 13.123 -3.751 40.238 1.00 41.47 O ANISOU 1672 O SER A 230 5681 6517 3559 -657 -207 -1 O ATOM 1673 CB SER A 230 13.117 -6.582 40.735 1.00 43.99 C ANISOU 1673 CB SER A 230 6020 6877 3817 -707 -355 453 C ATOM 1674 OG SER A 230 12.511 -7.863 40.626 1.00 51.40 O ANISOU 1674 OG SER A 230 6960 7777 4792 -718 -355 645 O ATOM 1675 N GLU A 231 14.821 -4.068 38.810 1.00 42.07 N ANISOU 1675 N GLU A 231 5696 6375 3913 -567 -364 72 N ATOM 1676 CA GLU A 231 15.237 -2.658 38.847 1.00 43.76 C ANISOU 1676 CA GLU A 231 5906 6585 4136 -574 -338 -126 C ATOM 1677 C GLU A 231 15.339 -2.076 37.432 1.00 39.65 C ANISOU 1677 C GLU A 231 5345 5882 3839 -496 -290 -189 C ATOM 1678 O GLU A 231 15.727 -2.792 36.504 1.00 37.21 O ANISOU 1678 O GLU A 231 5002 5471 3664 -446 -332 -85 O ATOM 1679 CB GLU A 231 16.557 -2.483 39.618 1.00 48.28 C ANISOU 1679 CB GLU A 231 6474 7247 4624 -630 -476 -139 C ATOM 1680 CG GLU A 231 17.845 -2.822 38.858 1.00 52.63 C ANISOU 1680 CG GLU A 231 6963 7692 5343 -586 -591 -68 C ATOM 1681 CD GLU A 231 19.080 -2.149 39.459 1.00 59.92 C ANISOU 1681 CD GLU A 231 7861 8684 6221 -641 -701 -154 C ATOM 1682 OE1 GLU A 231 19.130 -1.987 40.699 1.00 65.39 O ANISOU 1682 OE1 GLU A 231 8592 9548 6707 -723 -750 -186 O ATOM 1683 OE2 GLU A 231 20.003 -1.788 38.689 1.00 55.45 O ANISOU 1683 OE2 GLU A 231 7234 8015 5821 -610 -737 -190 O ATOM 1684 N PRO A 232 14.982 -0.783 37.260 1.00 36.80 N ANISOU 1684 N PRO A 232 4987 5477 3517 -487 -201 -360 N ATOM 1685 CA PRO A 232 15.084 -0.183 35.933 1.00 35.45 C ANISOU 1685 CA PRO A 232 4782 5140 3546 -423 -162 -397 C ATOM 1686 C PRO A 232 16.547 -0.108 35.511 1.00 34.46 C ANISOU 1686 C PRO A 232 4620 4961 3511 -427 -262 -381 C ATOM 1687 O PRO A 232 17.360 0.471 36.225 1.00 33.43 O ANISOU 1687 O PRO A 232 4489 4886 3326 -483 -320 -464 O ATOM 1688 CB PRO A 232 14.492 1.226 36.119 1.00 35.07 C ANISOU 1688 CB PRO A 232 4748 5064 3515 -423 -63 -578 C ATOM 1689 CG PRO A 232 13.881 1.233 37.494 1.00 38.88 C ANISOU 1689 CG PRO A 232 5268 5708 3799 -481 -26 -646 C ATOM 1690 CD PRO A 232 14.653 0.230 38.276 1.00 39.46 C ANISOU 1690 CD PRO A 232 5356 5911 3727 -541 -144 -530 C ATOM 1691 N ILE A 233 16.872 -0.707 34.371 1.00 32.58 N ANISOU 1691 N ILE A 233 4346 4627 3406 -375 -278 -285 N ATOM 1692 CA ILE A 233 18.269 -0.869 33.953 1.00 33.33 C ANISOU 1692 CA ILE A 233 4388 4685 3591 -375 -366 -253 C ATOM 1693 C ILE A 233 18.983 0.474 33.717 1.00 32.74 C ANISOU 1693 C ILE A 233 4291 4554 3595 -403 -355 -379 C ATOM 1694 O ILE A 233 20.159 0.609 34.026 1.00 33.93 O ANISOU 1694 O ILE A 233 4401 4733 3759 -442 -440 -398 O ATOM 1695 CB ILE A 233 18.366 -1.749 32.700 1.00 31.84 C ANISOU 1695 CB ILE A 233 4162 4406 3529 -312 -359 -151 C ATOM 1696 CG1 ILE A 233 19.835 -1.989 32.309 1.00 32.66 C ANISOU 1696 CG1 ILE A 233 4195 4483 3731 -308 -438 -127 C ATOM 1697 CG2 ILE A 233 17.573 -1.134 31.546 1.00 33.02 C ANISOU 1697 CG2 ILE A 233 4321 4459 3766 -272 -252 -188 C ATOM 1698 CD1 ILE A 233 20.019 -3.076 31.257 1.00 29.00 C ANISOU 1698 CD1 ILE A 233 3691 3951 3376 -248 -437 -38 C ATOM 1699 N PHE A 234 18.263 1.458 33.190 1.00 33.45 N ANISOU 1699 N PHE A 234 4402 4559 3746 -386 -256 -458 N ATOM 1700 CA PHE A 234 18.827 2.786 32.964 1.00 34.27 C ANISOU 1700 CA PHE A 234 4492 4584 3944 -417 -237 -570 C ATOM 1701 C PHE A 234 18.250 3.826 33.915 1.00 36.74 C ANISOU 1701 C PHE A 234 4849 4916 4194 -455 -193 -724 C ATOM 1702 O PHE A 234 18.037 4.985 33.535 1.00 35.70 O ANISOU 1702 O PHE A 234 4723 4672 4170 -452 -129 -815 O ATOM 1703 CB PHE A 234 18.632 3.192 31.505 1.00 32.24 C ANISOU 1703 CB PHE A 234 4219 4192 3839 -370 -168 -531 C ATOM 1704 CG PHE A 234 19.204 2.205 30.542 1.00 32.43 C ANISOU 1704 CG PHE A 234 4199 4207 3917 -338 -195 -411 C ATOM 1705 CD1 PHE A 234 20.549 1.863 30.605 1.00 31.20 C ANISOU 1705 CD1 PHE A 234 3983 4081 3791 -368 -272 -393 C ATOM 1706 CD2 PHE A 234 18.404 1.597 29.591 1.00 31.36 C ANISOU 1706 CD2 PHE A 234 4071 4039 3804 -279 -146 -328 C ATOM 1707 CE1 PHE A 234 21.078 0.939 29.729 1.00 31.93 C ANISOU 1707 CE1 PHE A 234 4026 4162 3945 -332 -285 -304 C ATOM 1708 CE2 PHE A 234 18.929 0.686 28.718 1.00 29.43 C ANISOU 1708 CE2 PHE A 234 3787 3787 3606 -253 -163 -247 C ATOM 1709 CZ PHE A 234 20.274 0.354 28.788 1.00 31.36 C ANISOU 1709 CZ PHE A 234 3972 4054 3889 -276 -226 -239 C ATOM 1710 N HIS A 235 18.030 3.396 35.159 1.00 40.58 N ANISOU 1710 N HIS A 235 5365 5546 4506 -493 -226 -751 N ATOM 1711 CA HIS A 235 17.584 4.265 36.244 1.00 44.32 C ANISOU 1711 CA HIS A 235 5879 6078 4883 -541 -186 -921 C ATOM 1712 C HIS A 235 18.526 5.454 36.378 1.00 45.80 C ANISOU 1712 C HIS A 235 6050 6201 5152 -602 -216 -1065 C ATOM 1713 O HIS A 235 19.748 5.300 36.377 1.00 43.52 O ANISOU 1713 O HIS A 235 5720 5933 4882 -647 -318 -1036 O ATOM 1714 CB HIS A 235 17.533 3.487 37.571 1.00 46.74 C ANISOU 1714 CB HIS A 235 6216 6585 4958 -596 -244 -904 C ATOM 1715 CG HIS A 235 17.241 4.341 38.766 1.00 54.79 C ANISOU 1715 CG HIS A 235 7276 7699 5843 -664 -208 -1098 C ATOM 1716 ND1 HIS A 235 16.015 4.344 39.397 1.00 65.65 N ANISOU 1716 ND1 HIS A 235 8690 9157 7098 -658 -105 -1159 N ATOM 1717 CD2 HIS A 235 18.017 5.217 39.449 1.00 63.33 C ANISOU 1717 CD2 HIS A 235 8360 8812 6890 -743 -257 -1262 C ATOM 1718 CE1 HIS A 235 16.048 5.187 40.415 1.00 68.29 C ANISOU 1718 CE1 HIS A 235 9052 9571 7322 -728 -84 -1360 C ATOM 1719 NE2 HIS A 235 17.250 5.732 40.467 1.00 67.86 N ANISOU 1719 NE2 HIS A 235 8981 9485 7318 -783 -180 -1429 N ATOM 1720 N CYS A 236 17.938 6.633 36.527 1.00 48.66 N ANISOU 1720 N CYS A 236 6436 6480 5572 -604 -128 -1227 N ATOM 1721 CA CYS A 236 18.676 7.881 36.468 1.00 51.88 C ANISOU 1721 CA CYS A 236 6830 6775 6109 -657 -137 -1368 C ATOM 1722 C CYS A 236 17.938 8.966 37.257 1.00 54.01 C ANISOU 1722 C CYS A 236 7139 7018 6366 -676 -51 -1591 C ATOM 1723 O CYS A 236 16.706 9.002 37.269 1.00 52.09 O ANISOU 1723 O CYS A 236 6916 6761 6114 -610 51 -1612 O ATOM 1724 CB CYS A 236 18.815 8.298 35.000 1.00 50.72 C ANISOU 1724 CB CYS A 236 6650 6433 6189 -606 -99 -1275 C ATOM 1725 SG CYS A 236 19.725 9.815 34.720 1.00 60.26 S ANISOU 1725 SG CYS A 236 7834 7465 7597 -678 -103 -1404 S ATOM 1726 N ARG A 237 18.694 9.852 37.902 1.00 58.50 N ANISOU 1726 N ARG A 237 7707 7575 6944 -767 -90 -1768 N ATOM 1727 CA ARG A 237 18.108 10.987 38.621 1.00 62.92 C ANISOU 1727 CA ARG A 237 8301 8086 7522 -789 -6 -2017 C ATOM 1728 C ARG A 237 17.425 11.941 37.642 1.00 64.90 C ANISOU 1728 C ARG A 237 8542 8082 8034 -706 101 -2033 C ATOM 1729 O ARG A 237 17.845 12.066 36.488 1.00 63.96 O ANISOU 1729 O ARG A 237 8392 7817 8092 -680 82 -1892 O ATOM 1730 CB ARG A 237 19.180 11.734 39.419 1.00 65.29 C ANISOU 1730 CB ARG A 237 8598 8412 7797 -916 -84 -2207 C ATOM 1731 CG ARG A 237 19.884 10.987 40.478 0.00 68.49 C ANISOU 1731 CG ARG A 237 9009 9069 7947 -1008 -205 -2212 C ATOM 1732 CD ARG A 237 20.843 11.886 41.242 0.00 71.01 C ANISOU 1732 CD ARG A 237 9320 9404 8256 -1139 -280 -2432 C ATOM 1733 NE ARG A 237 21.641 11.150 42.217 0.00 72.13 N ANISOU 1733 NE ARG A 237 9457 9801 8150 -1233 -427 -2412 N ATOM 1734 CZ ARG A 237 22.531 11.713 43.028 0.00 74.43 C ANISOU 1734 CZ ARG A 237 9736 10170 8373 -1362 -525 -2589 C ATOM 1735 NH1 ARG A 237 22.737 13.023 42.983 0.00 75.88 N ANISOU 1735 NH1 ARG A 237 9917 10183 8732 -1417 -482 -2813 N ATOM 1736 NH2 ARG A 237 23.215 10.968 43.885 0.00 75.39 N ANISOU 1736 NH2 ARG A 237 9846 10538 8260 -1440 -674 -2539 N ATOM 1737 N GLN A 238 16.371 12.606 38.111 1.00 68.88 N ANISOU 1737 N GLN A 238 9067 8542 8560 -666 212 -2202 N ATOM 1738 CA GLN A 238 15.569 13.501 37.272 1.00 70.40 C ANISOU 1738 CA GLN A 238 9245 8496 9009 -571 310 -2213 C ATOM 1739 C GLN A 238 16.338 14.769 36.917 1.00 72.10 C ANISOU 1739 C GLN A 238 9451 8484 9460 -621 293 -2311 C ATOM 1740 O GLN A 238 17.199 15.212 37.677 1.00 75.15 O ANISOU 1740 O GLN A 238 9848 8903 9803 -732 240 -2477 O ATOM 1741 CB GLN A 238 14.263 13.870 37.985 1.00 72.70 C ANISOU 1741 CB GLN A 238 9544 8806 9271 -512 437 -2390 C ATOM 1742 CG GLN A 238 13.330 12.668 38.215 0.00 73.48 C ANISOU 1742 CG GLN A 238 9642 9107 9171 -460 475 -2275 C ATOM 1743 CD GLN A 238 12.025 13.047 38.894 0.00 75.01 C ANISOU 1743 CD GLN A 238 9826 9330 9346 -403 617 -2453 C ATOM 1744 OE1 GLN A 238 11.935 14.070 39.575 0.00 77.00 O ANISOU 1744 OE1 GLN A 238 10085 9519 9652 -426 681 -2712 O ATOM 1745 NE2 GLN A 238 11.005 12.216 38.715 0.00 73.96 N ANISOU 1745 NE2 GLN A 238 9668 9293 9142 -332 672 -2327 N ATOM 1746 N ASN A 245 17.374 20.333 24.128 0.00 69.30 N ANISOU 1746 N ASN A 245 8988 6283 11059 -468 304 -386 N ATOM 1747 CA ASN A 245 16.244 19.775 24.690 1.00 66.22 C ANISOU 1747 CA ASN A 245 8598 5990 10573 -343 314 -482 C ATOM 1748 C ASN A 245 16.177 18.248 24.682 1.00 63.32 C ANISOU 1748 C ASN A 245 8225 5922 9912 -319 298 -448 C ATOM 1749 O ASN A 245 15.883 17.636 25.712 1.00 63.22 O ANISOU 1749 O ASN A 245 8211 6044 9767 -291 305 -623 O ATOM 1750 CB ASN A 245 14.913 20.351 24.124 0.00 69.38 C ANISOU 1750 CB ASN A 245 8993 6231 11137 -206 322 -367 C ATOM 1751 CG ASN A 245 13.693 20.239 25.033 0.00 69.57 C ANISOU 1751 CG ASN A 245 9000 6273 11162 -80 354 -548 C ATOM 1752 OD1 ASN A 245 13.724 19.577 26.072 0.00 68.72 O ANISOU 1752 OD1 ASN A 245 8893 6332 10886 -90 374 -744 O ATOM 1753 ND2 ASN A 245 12.607 20.893 24.637 0.00 70.78 N ANISOU 1753 ND2 ASN A 245 9129 6257 11506 40 360 -473 N ATOM 1754 N PRO A 246 16.439 17.628 23.514 1.00 60.88 N ANISOU 1754 N PRO A 246 7912 5718 9503 -335 279 -224 N ATOM 1755 CA PRO A 246 16.489 16.164 23.444 1.00 58.42 C ANISOU 1755 CA PRO A 246 7592 5668 8937 -322 264 -198 C ATOM 1756 C PRO A 246 17.727 15.579 24.133 1.00 55.88 C ANISOU 1756 C PRO A 246 7256 5479 8497 -423 250 -317 C ATOM 1757 O PRO A 246 17.687 14.431 24.593 1.00 54.50 O ANISOU 1757 O PRO A 246 7074 5496 8137 -401 234 -370 O ATOM 1758 CB PRO A 246 16.521 15.879 21.937 1.00 58.48 C ANISOU 1758 CB PRO A 246 7599 5719 8900 -325 255 57 C ATOM 1759 CG PRO A 246 17.121 17.111 21.333 1.00 60.74 C ANISOU 1759 CG PRO A 246 7892 5806 9382 -402 264 160 C ATOM 1760 CD PRO A 246 16.683 18.257 22.202 1.00 61.39 C ANISOU 1760 CD PRO A 246 7981 5662 9681 -370 274 13 C ATOM 1761 N TYR A 247 18.807 16.363 24.205 1.00 52.72 N ANISOU 1761 N TYR A 247 6844 4973 8216 -533 250 -352 N ATOM 1762 CA TYR A 247 20.050 15.911 24.828 1.00 50.35 C ANISOU 1762 CA TYR A 247 6511 4791 7829 -634 224 -459 C ATOM 1763 C TYR A 247 19.930 15.831 26.346 1.00 49.74 C ANISOU 1763 C TYR A 247 6441 4763 7694 -632 202 -700 C ATOM 1764 O TYR A 247 19.644 16.826 27.006 1.00 50.52 O ANISOU 1764 O TYR A 247 6559 4708 7928 -639 217 -844 O ATOM 1765 CB TYR A 247 21.208 16.831 24.449 1.00 51.38 C ANISOU 1765 CB TYR A 247 6614 4792 8118 -764 230 -427 C ATOM 1766 CG TYR A 247 22.559 16.331 24.905 1.00 51.28 C ANISOU 1766 CG TYR A 247 6544 4913 8028 -870 197 -507 C ATOM 1767 CD1 TYR A 247 23.150 15.214 24.306 1.00 49.96 C ANISOU 1767 CD1 TYR A 247 6334 4935 7715 -877 193 -401 C ATOM 1768 CD2 TYR A 247 23.250 16.971 25.932 1.00 51.62 C ANISOU 1768 CD2 TYR A 247 6567 4895 8152 -963 167 -697 C ATOM 1769 CE1 TYR A 247 24.395 14.751 24.716 1.00 48.17 C ANISOU 1769 CE1 TYR A 247 6036 4827 7442 -962 157 -469 C ATOM 1770 CE2 TYR A 247 24.496 16.515 26.351 1.00 52.85 C ANISOU 1770 CE2 TYR A 247 6655 5183 8244 -1059 121 -763 C ATOM 1771 CZ TYR A 247 25.061 15.405 25.739 1.00 53.03 C ANISOU 1771 CZ TYR A 247 6625 5386 8137 -1053 116 -641 C ATOM 1772 OH TYR A 247 26.291 14.959 26.143 1.00 52.57 O ANISOU 1772 OH TYR A 247 6483 5451 8041 -1136 66 -701 O ATOM 1773 N HIS A 248 20.144 14.633 26.885 1.00 49.46 N ANISOU 1773 N HIS A 248 6393 4942 7458 -623 168 -742 N ATOM 1774 CA HIS A 248 20.102 14.396 28.325 1.00 50.46 C ANISOU 1774 CA HIS A 248 6528 5163 7480 -634 139 -945 C ATOM 1775 C HIS A 248 21.367 13.652 28.756 1.00 47.96 C ANISOU 1775 C HIS A 248 6166 5009 7048 -719 72 -973 C ATOM 1776 O HIS A 248 21.520 12.450 28.509 1.00 44.88 O ANISOU 1776 O HIS A 248 5755 4777 6520 -688 47 -876 O ATOM 1777 CB HIS A 248 18.841 13.619 28.706 1.00 51.27 C ANISOU 1777 CB HIS A 248 6661 5374 7446 -523 158 -955 C ATOM 1778 CG HIS A 248 17.570 14.306 28.306 1.00 59.55 C ANISOU 1778 CG HIS A 248 7733 6275 8618 -429 218 -929 C ATOM 1779 ND1 HIS A 248 17.177 15.516 28.842 1.00 66.34 N ANISOU 1779 ND1 HIS A 248 8608 6962 9637 -425 254 -1078 N ATOM 1780 CD2 HIS A 248 16.608 13.957 27.420 1.00 62.01 C ANISOU 1780 CD2 HIS A 248 8047 6584 8929 -334 241 -776 C ATOM 1781 CE1 HIS A 248 16.027 15.881 28.304 1.00 67.78 C ANISOU 1781 CE1 HIS A 248 8794 7035 9924 -321 296 -1008 C ATOM 1782 NE2 HIS A 248 15.660 14.953 27.438 1.00 69.07 N ANISOU 1782 NE2 HIS A 248 8949 7308 9986 -268 284 -820 N ATOM 1783 N HIS A 249 22.254 14.395 29.410 1.00 47.90 N ANISOU 1783 N HIS A 249 6135 4950 7115 -826 39 -1112 N ATOM 1784 CA HIS A 249 23.618 13.966 29.691 1.00 48.19 C ANISOU 1784 CA HIS A 249 6104 5103 7101 -923 -33 -1130 C ATOM 1785 C HIS A 249 23.675 12.822 30.687 1.00 46.68 C ANISOU 1785 C HIS A 249 5908 5133 6693 -903 -104 -1187 C ATOM 1786 O HIS A 249 24.351 11.817 30.439 1.00 44.42 O ANISOU 1786 O HIS A 249 5568 4980 6328 -902 -150 -1088 O ATOM 1787 CB HIS A 249 24.458 15.145 30.220 1.00 48.44 C ANISOU 1787 CB HIS A 249 6111 5018 7276 -1052 -58 -1285 C ATOM 1788 CG HIS A 249 25.839 14.753 30.649 1.00 51.31 C ANISOU 1788 CG HIS A 249 6390 5513 7592 -1156 -147 -1324 C ATOM 1789 ND1 HIS A 249 26.133 14.342 31.933 1.00 51.84 N ANISOU 1789 ND1 HIS A 249 6448 5739 7509 -1192 -236 -1472 N ATOM 1790 CD2 HIS A 249 27.002 14.683 29.958 1.00 49.94 C ANISOU 1790 CD2 HIS A 249 6127 5349 7499 -1232 -162 -1228 C ATOM 1791 CE1 HIS A 249 27.417 14.043 32.015 1.00 51.90 C ANISOU 1791 CE1 HIS A 249 6361 5841 7519 -1278 -315 -1460 C ATOM 1792 NE2 HIS A 249 27.967 14.243 30.831 1.00 52.81 N ANISOU 1792 NE2 HIS A 249 6420 5866 7780 -1303 -266 -1321 N ATOM 1793 N ASP A 250 22.981 12.984 31.814 1.00 45.27 N ANISOU 1793 N ASP A 250 5783 4993 6425 -889 -109 -1344 N ATOM 1794 CA ASP A 250 23.014 11.984 32.883 1.00 43.77 C ANISOU 1794 CA ASP A 250 5597 5018 6016 -886 -180 -1393 C ATOM 1795 C ASP A 250 22.406 10.664 32.417 1.00 40.43 C ANISOU 1795 C ASP A 250 5183 4704 5475 -783 -169 -1223 C ATOM 1796 O ASP A 250 22.865 9.600 32.803 1.00 41.29 O ANISOU 1796 O ASP A 250 5264 4973 5452 -785 -243 -1170 O ATOM 1797 CB ASP A 250 22.285 12.482 34.142 1.00 44.56 C ANISOU 1797 CB ASP A 250 5757 5146 6027 -897 -165 -1600 C ATOM 1798 CG ASP A 250 23.010 13.643 34.846 1.00 51.00 C ANISOU 1798 CG ASP A 250 6562 5888 6926 -1019 -198 -1810 C ATOM 1799 OD1 ASP A 250 24.238 13.808 34.680 1.00 53.14 O ANISOU 1799 OD1 ASP A 250 6768 6155 7269 -1111 -268 -1799 O ATOM 1800 OD2 ASP A 250 22.338 14.390 35.594 1.00 53.70 O ANISOU 1800 OD2 ASP A 250 6955 6182 7268 -1024 -150 -2002 O ATOM 1801 N GLN A 251 21.365 10.733 31.597 1.00 40.11 N ANISOU 1801 N GLN A 251 5177 4572 5492 -694 -84 -1137 N ATOM 1802 CA GLN A 251 20.726 9.521 31.082 1.00 38.21 C ANISOU 1802 CA GLN A 251 4944 4420 5154 -605 -71 -987 C ATOM 1803 C GLN A 251 21.675 8.721 30.174 1.00 36.87 C ANISOU 1803 C GLN A 251 4713 4293 5001 -611 -107 -841 C ATOM 1804 O GLN A 251 21.786 7.500 30.313 1.00 36.02 O ANISOU 1804 O GLN A 251 4590 4313 4783 -580 -151 -771 O ATOM 1805 CB GLN A 251 19.435 9.869 30.342 1.00 36.42 C ANISOU 1805 CB GLN A 251 4755 4085 4999 -517 17 -931 C ATOM 1806 CG GLN A 251 18.633 8.659 29.892 1.00 37.79 C ANISOU 1806 CG GLN A 251 4937 4351 5071 -433 29 -802 C ATOM 1807 CD GLN A 251 18.128 7.816 31.049 1.00 40.42 C ANISOU 1807 CD GLN A 251 5293 4836 5229 -421 7 -855 C ATOM 1808 OE1 GLN A 251 17.249 8.237 31.791 1.00 37.71 O ANISOU 1808 OE1 GLN A 251 4981 4495 4851 -404 51 -961 O ATOM 1809 NE2 GLN A 251 18.667 6.608 31.189 1.00 40.57 N ANISOU 1809 NE2 GLN A 251 5292 4982 5142 -429 -58 -775 N ATOM 1810 N LEU A 252 22.358 9.414 29.259 1.00 36.67 N ANISOU 1810 N LEU A 252 4652 4159 5123 -653 -82 -797 N ATOM 1811 CA LEU A 252 23.356 8.786 28.383 1.00 36.16 C ANISOU 1811 CA LEU A 252 4516 4137 5085 -671 -96 -684 C ATOM 1812 C LEU A 252 24.487 8.176 29.200 1.00 35.98 C ANISOU 1812 C LEU A 252 4425 4240 5004 -722 -193 -732 C ATOM 1813 O LEU A 252 24.926 7.054 28.929 1.00 36.11 O ANISOU 1813 O LEU A 252 4393 4353 4976 -688 -225 -650 O ATOM 1814 CB LEU A 252 23.939 9.801 27.380 1.00 37.15 C ANISOU 1814 CB LEU A 252 4611 4130 5374 -732 -44 -639 C ATOM 1815 CG LEU A 252 23.021 10.280 26.249 1.00 36.61 C ANISOU 1815 CG LEU A 252 4592 3948 5370 -681 39 -530 C ATOM 1816 CD1 LEU A 252 23.587 11.538 25.584 1.00 39.16 C ANISOU 1816 CD1 LEU A 252 4897 4119 5863 -765 79 -499 C ATOM 1817 CD2 LEU A 252 22.803 9.179 25.216 1.00 34.94 C ANISOU 1817 CD2 LEU A 252 4371 3826 5080 -617 65 -391 C ATOM 1818 N ASP A 253 24.953 8.922 30.196 1.00 37.72 N ANISOU 1818 N ASP A 253 4639 4457 5237 -804 -245 -870 N ATOM 1819 CA ASP A 253 25.973 8.438 31.128 1.00 39.44 C ANISOU 1819 CA ASP A 253 4790 4806 5387 -860 -359 -923 C ATOM 1820 C ASP A 253 25.549 7.125 31.795 1.00 38.22 C ANISOU 1820 C ASP A 253 4658 4802 5061 -791 -419 -873 C ATOM 1821 O ASP A 253 26.337 6.184 31.901 1.00 39.35 O ANISOU 1821 O ASP A 253 4729 5045 5176 -784 -498 -808 O ATOM 1822 CB ASP A 253 26.263 9.499 32.192 1.00 39.73 C ANISOU 1822 CB ASP A 253 4839 4823 5433 -960 -405 -1103 C ATOM 1823 CG ASP A 253 27.193 9.001 33.278 1.00 43.76 C ANISOU 1823 CG ASP A 253 5289 5496 5842 -1021 -543 -1160 C ATOM 1824 OD1 ASP A 253 28.371 8.722 32.983 1.00 45.49 O ANISOU 1824 OD1 ASP A 253 5398 5753 6133 -1061 -602 -1111 O ATOM 1825 OD2 ASP A 253 26.746 8.902 34.437 1.00 52.52 O ANISOU 1825 OD2 ASP A 253 6454 6704 6796 -1032 -594 -1252 O ATOM 1826 N ARG A 254 24.306 7.068 32.249 1.00 36.59 N ANISOU 1826 N ARG A 254 4545 4606 4753 -742 -380 -900 N ATOM 1827 CA ARG A 254 23.781 5.837 32.823 1.00 38.52 C ANISOU 1827 CA ARG A 254 4817 4981 4839 -685 -422 -834 C ATOM 1828 C ARG A 254 23.743 4.715 31.782 1.00 35.44 C ANISOU 1828 C ARG A 254 4396 4586 4482 -605 -401 -674 C ATOM 1829 O ARG A 254 24.087 3.581 32.090 1.00 36.84 O ANISOU 1829 O ARG A 254 4541 4859 4597 -579 -475 -598 O ATOM 1830 CB ARG A 254 22.390 6.062 33.424 1.00 39.10 C ANISOU 1830 CB ARG A 254 4985 5062 4810 -655 -360 -897 C ATOM 1831 CG ARG A 254 21.692 4.781 33.857 1.00 43.32 C ANISOU 1831 CG ARG A 254 5551 5715 5193 -600 -380 -803 C ATOM 1832 CD ARG A 254 22.391 4.111 35.039 1.00 48.04 C ANISOU 1832 CD ARG A 254 6130 6475 5647 -651 -507 -800 C ATOM 1833 NE ARG A 254 21.851 2.776 35.299 1.00 52.29 N ANISOU 1833 NE ARG A 254 6690 7104 6072 -600 -533 -667 N ATOM 1834 CZ ARG A 254 22.081 2.058 36.396 1.00 53.97 C ANISOU 1834 CZ ARG A 254 6910 7467 6130 -634 -634 -627 C ATOM 1835 NH1 ARG A 254 22.838 2.536 37.377 1.00 57.48 N ANISOU 1835 NH1 ARG A 254 7340 8009 6490 -719 -726 -719 N ATOM 1836 NH2 ARG A 254 21.542 0.849 36.516 1.00 50.61 N ANISOU 1836 NH2 ARG A 254 6506 7094 5630 -589 -648 -487 N ATOM 1837 N ILE A 255 23.337 5.027 30.552 1.00 34.01 N ANISOU 1837 N ILE A 255 4224 4295 4402 -567 -305 -624 N ATOM 1838 CA ILE A 255 23.325 4.016 29.492 1.00 31.38 C ANISOU 1838 CA ILE A 255 3862 3965 4096 -501 -278 -498 C ATOM 1839 C ILE A 255 24.740 3.483 29.227 1.00 32.04 C ANISOU 1839 C ILE A 255 3839 4090 4245 -522 -335 -464 C ATOM 1840 O ILE A 255 24.935 2.277 29.093 1.00 30.44 O ANISOU 1840 O ILE A 255 3601 3941 4023 -469 -369 -391 O ATOM 1841 CB ILE A 255 22.668 4.525 28.195 1.00 30.16 C ANISOU 1841 CB ILE A 255 3737 3706 4018 -469 -172 -451 C ATOM 1842 CG1 ILE A 255 21.172 4.756 28.413 1.00 33.79 C ANISOU 1842 CG1 ILE A 255 4281 4136 4420 -423 -124 -464 C ATOM 1843 CG2 ILE A 255 22.854 3.511 27.048 1.00 29.48 C ANISOU 1843 CG2 ILE A 255 3612 3638 3950 -420 -145 -347 C ATOM 1844 CD1 ILE A 255 20.479 5.433 27.257 1.00 28.14 C ANISOU 1844 CD1 ILE A 255 3592 3315 3784 -395 -41 -415 C ATOM 1845 N PHE A 256 25.730 4.372 29.201 1.00 34.34 N ANISOU 1845 N PHE A 256 4070 4351 4627 -599 -347 -522 N ATOM 1846 CA PHE A 256 27.117 3.954 28.967 1.00 35.04 C ANISOU 1846 CA PHE A 256 4034 4484 4795 -623 -396 -500 C ATOM 1847 C PHE A 256 27.728 3.175 30.143 1.00 35.84 C ANISOU 1847 C PHE A 256 4084 4701 4832 -625 -536 -506 C ATOM 1848 O PHE A 256 28.505 2.250 29.922 1.00 34.58 O ANISOU 1848 O PHE A 256 3829 4587 4722 -588 -582 -447 O ATOM 1849 CB PHE A 256 28.006 5.160 28.623 1.00 38.05 C ANISOU 1849 CB PHE A 256 4354 4802 5301 -721 -369 -557 C ATOM 1850 CG PHE A 256 27.570 5.924 27.399 1.00 35.14 C ANISOU 1850 CG PHE A 256 4024 4321 5007 -729 -242 -518 C ATOM 1851 CD1 PHE A 256 27.003 5.273 26.299 1.00 36.15 C ANISOU 1851 CD1 PHE A 256 4177 4443 5115 -654 -163 -422 C ATOM 1852 CD2 PHE A 256 27.750 7.297 27.338 1.00 35.03 C ANISOU 1852 CD2 PHE A 256 4020 4206 5084 -817 -208 -572 C ATOM 1853 CE1 PHE A 256 26.613 5.990 25.179 1.00 33.28 C ANISOU 1853 CE1 PHE A 256 3850 3995 4802 -668 -61 -369 C ATOM 1854 CE2 PHE A 256 27.368 8.015 26.221 1.00 36.61 C ANISOU 1854 CE2 PHE A 256 4255 4297 5356 -827 -103 -508 C ATOM 1855 CZ PHE A 256 26.802 7.362 25.138 1.00 34.02 C ANISOU 1855 CZ PHE A 256 3953 3985 4987 -753 -32 -399 C ATOM 1856 N ASN A 257 27.400 3.559 31.378 1.00 36.01 N ANISOU 1856 N ASN A 257 4164 4773 4745 -668 -604 -579 N ATOM 1857 CA ASN A 257 27.818 2.799 32.571 1.00 37.66 C ANISOU 1857 CA ASN A 257 4344 5112 4853 -674 -748 -563 C ATOM 1858 C ASN A 257 27.356 1.345 32.541 1.00 36.07 C ANISOU 1858 C ASN A 257 4158 4951 4595 -578 -771 -435 C ATOM 1859 O ASN A 257 28.020 0.467 33.087 1.00 35.92 O ANISOU 1859 O ASN A 257 4073 5012 4564 -560 -890 -369 O ATOM 1860 CB ASN A 257 27.280 3.439 33.863 1.00 40.37 C ANISOU 1860 CB ASN A 257 4773 5520 5045 -738 -792 -668 C ATOM 1861 CG ASN A 257 28.226 4.456 34.455 1.00 47.80 C ANISOU 1861 CG ASN A 257 5659 6484 6018 -851 -862 -796 C ATOM 1862 OD1 ASN A 257 29.437 4.233 34.514 1.00 55.26 O ANISOU 1862 OD1 ASN A 257 6485 7479 7033 -884 -958 -777 O ATOM 1863 ND2 ASN A 257 27.677 5.582 34.910 1.00 54.45 N ANISOU 1863 ND2 ASN A 257 6581 7287 6822 -913 -815 -938 N ATOM 1864 N VAL A 258 26.203 1.106 31.927 1.00 34.11 N ANISOU 1864 N VAL A 258 3994 4642 4323 -518 -667 -397 N ATOM 1865 CA VAL A 258 25.669 -0.244 31.787 1.00 32.70 C ANISOU 1865 CA VAL A 258 3835 4477 4112 -435 -675 -283 C ATOM 1866 C VAL A 258 26.175 -0.933 30.526 1.00 32.63 C ANISOU 1866 C VAL A 258 3747 4405 4244 -373 -629 -226 C ATOM 1867 O VAL A 258 26.670 -2.059 30.591 1.00 31.77 O ANISOU 1867 O VAL A 258 3576 4316 4178 -322 -697 -152 O ATOM 1868 CB VAL A 258 24.131 -0.228 31.785 1.00 32.33 C ANISOU 1868 CB VAL A 258 3908 4408 3969 -409 -590 -278 C ATOM 1869 CG1 VAL A 258 23.558 -1.595 31.355 1.00 27.20 C ANISOU 1869 CG1 VAL A 258 3271 3743 3322 -331 -579 -165 C ATOM 1870 CG2 VAL A 258 23.625 0.194 33.163 1.00 29.11 C ANISOU 1870 CG2 VAL A 258 3569 4089 3402 -464 -633 -335 C ATOM 1871 N MET A 259 26.055 -0.253 29.388 1.00 31.97 N ANISOU 1871 N MET A 259 3667 4247 4235 -378 -513 -261 N ATOM 1872 CA MET A 259 26.321 -0.867 28.083 1.00 31.33 C ANISOU 1872 CA MET A 259 3531 4120 4252 -325 -441 -222 C ATOM 1873 C MET A 259 27.781 -0.795 27.628 1.00 32.67 C ANISOU 1873 C MET A 259 3561 4300 4553 -345 -450 -243 C ATOM 1874 O MET A 259 28.197 -1.564 26.756 1.00 31.46 O ANISOU 1874 O MET A 259 3338 4134 4483 -293 -407 -220 O ATOM 1875 CB MET A 259 25.457 -0.193 27.016 1.00 31.67 C ANISOU 1875 CB MET A 259 3644 4098 4290 -327 -313 -232 C ATOM 1876 CG MET A 259 23.945 -0.261 27.284 1.00 33.48 C ANISOU 1876 CG MET A 259 3992 4314 4414 -299 -288 -214 C ATOM 1877 SD MET A 259 23.333 -1.947 27.253 1.00 32.87 S ANISOU 1877 SD MET A 259 3931 4253 4304 -219 -313 -137 S ATOM 1878 CE MET A 259 23.658 -2.383 25.551 1.00 29.58 C ANISOU 1878 CE MET A 259 3463 3797 3980 -183 -221 -131 C ATOM 1879 N GLY A 260 28.550 0.119 28.212 1.00 33.01 N ANISOU 1879 N GLY A 260 3555 4368 4620 -424 -501 -298 N ATOM 1880 CA GLY A 260 29.825 0.536 27.638 1.00 35.70 C ANISOU 1880 CA GLY A 260 3763 4710 5092 -469 -478 -329 C ATOM 1881 C GLY A 260 29.581 1.633 26.608 1.00 36.42 C ANISOU 1881 C GLY A 260 3891 4732 5213 -523 -344 -352 C ATOM 1882 O GLY A 260 28.437 1.926 26.267 1.00 34.94 O ANISOU 1882 O GLY A 260 3823 4495 4956 -507 -277 -336 O ATOM 1883 N PHE A 261 30.653 2.251 26.128 1.00 38.10 N ANISOU 1883 N PHE A 261 3996 4943 5536 -592 -309 -380 N ATOM 1884 CA PHE A 261 30.563 3.318 25.128 1.00 38.68 C ANISOU 1884 CA PHE A 261 4094 4951 5650 -659 -185 -377 C ATOM 1885 C PHE A 261 30.697 2.651 23.762 1.00 39.25 C ANISOU 1885 C PHE A 261 4124 5042 5748 -612 -72 -329 C ATOM 1886 O PHE A 261 31.580 1.819 23.578 1.00 40.29 O ANISOU 1886 O PHE A 261 4131 5230 5948 -578 -80 -338 O ATOM 1887 CB PHE A 261 31.689 4.339 25.348 1.00 39.50 C ANISOU 1887 CB PHE A 261 4099 5048 5863 -776 -203 -428 C ATOM 1888 CG PHE A 261 31.458 5.658 24.670 1.00 40.61 C ANISOU 1888 CG PHE A 261 4293 5092 6044 -864 -103 -419 C ATOM 1889 CD1 PHE A 261 30.672 6.634 25.271 1.00 43.35 C ANISOU 1889 CD1 PHE A 261 4756 5354 6363 -901 -124 -457 C ATOM 1890 CD2 PHE A 261 32.022 5.928 23.431 1.00 44.33 C ANISOU 1890 CD2 PHE A 261 4697 5559 6589 -910 16 -369 C ATOM 1891 CE1 PHE A 261 30.449 7.854 24.650 1.00 44.18 C ANISOU 1891 CE1 PHE A 261 4908 5345 6534 -974 -40 -435 C ATOM 1892 CE2 PHE A 261 31.807 7.152 22.801 1.00 47.57 C ANISOU 1892 CE2 PHE A 261 5160 5872 7042 -997 101 -331 C ATOM 1893 CZ PHE A 261 31.018 8.117 23.412 1.00 46.37 C ANISOU 1893 CZ PHE A 261 5124 5612 6885 -1025 67 -359 C ATOM 1894 N PRO A 262 29.815 2.991 22.804 1.00 39.29 N ANISOU 1894 N PRO A 262 4226 5003 5698 -609 32 -284 N ATOM 1895 CA PRO A 262 29.807 2.250 21.546 1.00 39.39 C ANISOU 1895 CA PRO A 262 4215 5055 5696 -564 134 -252 C ATOM 1896 C PRO A 262 31.034 2.547 20.691 1.00 41.09 C ANISOU 1896 C PRO A 262 4298 5312 6002 -633 225 -258 C ATOM 1897 O PRO A 262 31.389 3.709 20.499 1.00 39.84 O ANISOU 1897 O PRO A 262 4129 5119 5888 -735 264 -240 O ATOM 1898 CB PRO A 262 28.551 2.768 20.852 1.00 39.61 C ANISOU 1898 CB PRO A 262 4383 5036 5633 -564 199 -193 C ATOM 1899 CG PRO A 262 28.408 4.151 21.361 1.00 39.53 C ANISOU 1899 CG PRO A 262 4421 4946 5655 -642 178 -190 C ATOM 1900 CD PRO A 262 28.851 4.105 22.784 1.00 38.52 C ANISOU 1900 CD PRO A 262 4255 4823 5560 -648 60 -262 C ATOM 1901 N ALA A 263 31.685 1.495 20.210 1.00 41.78 N ANISOU 1901 N ALA A 263 4278 5468 6130 -579 261 -288 N ATOM 1902 CA ALA A 263 32.750 1.636 19.228 1.00 45.12 C ANISOU 1902 CA ALA A 263 4570 5951 6623 -635 380 -302 C ATOM 1903 C ALA A 263 32.144 2.102 17.910 1.00 44.45 C ANISOU 1903 C ALA A 263 4574 5879 6438 -680 517 -243 C ATOM 1904 O ALA A 263 30.952 1.919 17.664 1.00 44.92 O ANISOU 1904 O ALA A 263 4770 5914 6385 -634 514 -207 O ATOM 1905 CB ALA A 263 33.478 0.311 19.045 1.00 46.12 C ANISOU 1905 CB ALA A 263 4561 6140 6822 -547 391 -366 C ATOM 1906 N ASP A 264 32.958 2.716 17.065 1.00 47.53 N ANISOU 1906 N ASP A 264 4879 6315 6863 -776 633 -225 N ATOM 1907 CA ASP A 264 32.474 3.203 15.775 1.00 48.78 C ANISOU 1907 CA ASP A 264 5116 6505 6912 -834 761 -147 C ATOM 1908 C ASP A 264 31.885 2.089 14.918 1.00 46.24 C ANISOU 1908 C ASP A 264 4837 6259 6473 -750 822 -176 C ATOM 1909 O ASP A 264 30.907 2.306 14.207 1.00 47.26 O ANISOU 1909 O ASP A 264 5092 6394 6470 -758 856 -108 O ATOM 1910 CB ASP A 264 33.583 3.946 15.025 1.00 52.13 C ANISOU 1910 CB ASP A 264 5425 6986 7394 -962 885 -118 C ATOM 1911 CG ASP A 264 33.748 5.375 15.514 1.00 58.95 C ANISOU 1911 CG ASP A 264 6311 7749 8339 -1078 847 -50 C ATOM 1912 OD1 ASP A 264 32.733 6.113 15.552 1.00 66.58 O ANISOU 1912 OD1 ASP A 264 7428 8620 9248 -1091 812 33 O ATOM 1913 OD2 ASP A 264 34.884 5.757 15.865 1.00 65.98 O ANISOU 1913 OD2 ASP A 264 7060 8645 9363 -1154 849 -85 O ATOM 1914 N LYS A 265 32.452 0.891 15.019 1.00 45.40 N ANISOU 1914 N LYS A 265 4623 6202 6426 -668 824 -281 N ATOM 1915 CA LYS A 265 31.930 -0.268 14.294 1.00 45.79 C ANISOU 1915 CA LYS A 265 4705 6305 6389 -585 875 -339 C ATOM 1916 C LYS A 265 30.553 -0.728 14.821 1.00 43.08 C ANISOU 1916 C LYS A 265 4513 5887 5970 -503 764 -317 C ATOM 1917 O LYS A 265 29.798 -1.359 14.083 1.00 38.87 O ANISOU 1917 O LYS A 265 4051 5389 5329 -466 804 -337 O ATOM 1918 CB LYS A 265 32.934 -1.432 14.345 1.00 47.84 C ANISOU 1918 CB LYS A 265 4798 6606 6774 -509 901 -465 C ATOM 1919 CG LYS A 265 33.009 -2.141 15.709 1.00 52.83 C ANISOU 1919 CG LYS A 265 5394 7150 7530 -408 739 -494 C ATOM 1920 CD LYS A 265 34.317 -2.907 15.887 1.00 56.76 C ANISOU 1920 CD LYS A 265 5685 7676 8207 -353 749 -588 C ATOM 1921 CE LYS A 265 34.392 -3.595 17.225 0.00 57.79 C ANISOU 1921 CE LYS A 265 5782 7725 8450 -258 573 -586 C ATOM 1922 NZ LYS A 265 35.655 -4.364 17.393 0.00 59.62 N ANISOU 1922 NZ LYS A 265 5800 7976 8877 -192 568 -664 N ATOM 1923 N ASP A 266 30.250 -0.430 16.089 1.00 41.91 N ANISOU 1923 N ASP A 266 4405 5647 5873 -481 629 -286 N ATOM 1924 CA ASP A 266 28.958 -0.789 16.696 1.00 42.95 C ANISOU 1924 CA ASP A 266 4669 5714 5936 -414 530 -261 C ATOM 1925 C ASP A 266 27.815 0.125 16.248 1.00 41.96 C ANISOU 1925 C ASP A 266 4684 5567 5692 -459 546 -171 C ATOM 1926 O ASP A 266 26.659 -0.308 16.225 1.00 41.85 O ANISOU 1926 O ASP A 266 4770 5536 5597 -407 510 -156 O ATOM 1927 CB ASP A 266 29.015 -0.724 18.232 1.00 44.44 C ANISOU 1927 CB ASP A 266 4853 5833 6198 -387 389 -260 C ATOM 1928 CG ASP A 266 30.056 -1.651 18.837 1.00 49.19 C ANISOU 1928 CG ASP A 266 5317 6449 6925 -331 335 -323 C ATOM 1929 OD1 ASP A 266 30.390 -2.690 18.222 1.00 51.44 O ANISOU 1929 OD1 ASP A 266 5533 6765 7248 -272 389 -381 O ATOM 1930 OD2 ASP A 266 30.533 -1.329 19.950 1.00 54.15 O ANISOU 1930 OD2 ASP A 266 5902 7054 7618 -345 232 -319 O ATOM 1931 N TRP A 267 28.129 1.387 15.939 1.00 40.20 N ANISOU 1931 N TRP A 267 4464 5335 5477 -554 592 -105 N ATOM 1932 CA TRP A 267 27.115 2.363 15.533 1.00 39.97 C ANISOU 1932 CA TRP A 267 4557 5265 5367 -593 598 -1 C ATOM 1933 C TRP A 267 27.718 3.378 14.562 1.00 43.70 C ANISOU 1933 C TRP A 267 5002 5767 5833 -706 701 78 C ATOM 1934 O TRP A 267 28.040 4.515 14.935 1.00 42.89 O ANISOU 1934 O TRP A 267 4897 5588 5813 -778 688 129 O ATOM 1935 CB TRP A 267 26.534 3.063 16.767 1.00 38.27 C ANISOU 1935 CB TRP A 267 4404 4933 5202 -581 492 15 C ATOM 1936 CG TRP A 267 25.307 3.895 16.510 1.00 36.55 C ANISOU 1936 CG TRP A 267 4307 4653 4929 -586 480 108 C ATOM 1937 CD1 TRP A 267 24.738 4.179 15.297 1.00 38.47 C ANISOU 1937 CD1 TRP A 267 4604 4932 5080 -609 540 202 C ATOM 1938 CD2 TRP A 267 24.520 4.590 17.491 1.00 34.24 C ANISOU 1938 CD2 TRP A 267 4084 4252 4674 -565 403 115 C ATOM 1939 NE1 TRP A 267 23.640 4.985 15.469 1.00 36.75 N ANISOU 1939 NE1 TRP A 267 4478 4626 4860 -595 494 278 N ATOM 1940 CE2 TRP A 267 23.484 5.256 16.802 1.00 32.53 C ANISOU 1940 CE2 TRP A 267 3952 3997 4410 -566 419 216 C ATOM 1941 CE3 TRP A 267 24.588 4.711 18.883 1.00 34.16 C ANISOU 1941 CE3 TRP A 267 4069 4184 4727 -548 323 41 C ATOM 1942 CZ2 TRP A 267 22.524 6.035 17.457 1.00 33.03 C ANISOU 1942 CZ2 TRP A 267 4086 3951 4514 -538 366 236 C ATOM 1943 CZ3 TRP A 267 23.630 5.487 19.537 1.00 32.22 C ANISOU 1943 CZ3 TRP A 267 3902 3844 4496 -531 279 48 C ATOM 1944 CH2 TRP A 267 22.616 6.138 18.822 1.00 30.07 C ANISOU 1944 CH2 TRP A 267 3703 3519 4202 -521 306 141 C ATOM 1945 N GLU A 268 27.860 2.961 13.309 1.00 46.40 N ANISOU 1945 N GLU A 268 5329 6226 6076 -728 806 87 N ATOM 1946 CA GLU A 268 28.637 3.732 12.331 1.00 50.90 C ANISOU 1946 CA GLU A 268 5852 6861 6628 -846 924 159 C ATOM 1947 C GLU A 268 28.023 5.083 11.969 1.00 50.90 C ANISOU 1947 C GLU A 268 5951 6792 6598 -922 920 324 C ATOM 1948 O GLU A 268 28.752 6.024 11.668 1.00 56.06 O ANISOU 1948 O GLU A 268 6562 7431 7306 -1031 982 400 O ATOM 1949 CB GLU A 268 28.884 2.903 11.068 1.00 52.41 C ANISOU 1949 CB GLU A 268 6008 7216 6691 -854 1046 115 C ATOM 1950 CG GLU A 268 29.965 1.848 11.264 1.00 59.00 C ANISOU 1950 CG GLU A 268 6694 8110 7612 -809 1092 -43 C ATOM 1951 CD GLU A 268 30.158 0.941 10.060 1.00 64.81 C ANISOU 1951 CD GLU A 268 7393 9001 8229 -806 1220 -127 C ATOM 1952 OE1 GLU A 268 29.199 0.737 9.285 1.00 68.16 O ANISOU 1952 OE1 GLU A 268 7926 9484 8486 -802 1231 -95 O ATOM 1953 OE2 GLU A 268 31.277 0.416 9.903 1.00 67.25 O ANISOU 1953 OE2 GLU A 268 7557 9379 8616 -805 1308 -236 O ATOM 1954 N ASP A 269 26.698 5.176 12.007 1.00 48.99 N ANISOU 1954 N ASP A 269 5830 6498 6287 -865 845 384 N ATOM 1955 CA ASP A 269 26.001 6.419 11.670 1.00 50.90 C ANISOU 1955 CA ASP A 269 6162 6655 6521 -915 826 549 C ATOM 1956 C ASP A 269 25.618 7.245 12.903 1.00 48.90 C ANISOU 1956 C ASP A 269 5945 6218 6417 -890 727 549 C ATOM 1957 O ASP A 269 24.788 8.150 12.807 1.00 50.59 O ANISOU 1957 O ASP A 269 6240 6331 6650 -893 689 663 O ATOM 1958 CB ASP A 269 24.751 6.118 10.832 1.00 51.72 C ANISOU 1958 CB ASP A 269 6365 6824 6463 -873 805 626 C ATOM 1959 CG ASP A 269 25.081 5.666 9.421 1.00 57.75 C ANISOU 1959 CG ASP A 269 7113 7776 7055 -934 913 655 C ATOM 1960 OD1 ASP A 269 26.273 5.685 9.028 1.00 58.25 O ANISOU 1960 OD1 ASP A 269 7088 7916 7128 -1014 1021 629 O ATOM 1961 OD2 ASP A 269 24.133 5.283 8.703 1.00 64.62 O ANISOU 1961 OD2 ASP A 269 8053 8726 7773 -906 892 696 O ATOM 1962 N ILE A 270 26.228 6.949 14.051 1.00 46.33 N ANISOU 1962 N ILE A 270 5554 5850 6198 -864 683 418 N ATOM 1963 CA ILE A 270 26.095 7.800 15.236 1.00 44.18 C ANISOU 1963 CA ILE A 270 5304 5423 6062 -866 604 392 C ATOM 1964 C ILE A 270 26.540 9.238 14.911 1.00 45.89 C ANISOU 1964 C ILE A 270 5519 5534 6382 -982 644 499 C ATOM 1965 O ILE A 270 25.987 10.195 15.439 1.00 44.14 O ANISOU 1965 O ILE A 270 5356 5159 6255 -983 593 528 O ATOM 1966 CB ILE A 270 26.903 7.248 16.450 1.00 41.56 C ANISOU 1966 CB ILE A 270 4887 5097 5809 -845 551 240 C ATOM 1967 CG1 ILE A 270 26.456 7.934 17.747 1.00 42.09 C ANISOU 1967 CG1 ILE A 270 5000 5029 5963 -828 457 187 C ATOM 1968 CG2 ILE A 270 28.404 7.415 16.233 1.00 36.95 C ANISOU 1968 CG2 ILE A 270 4175 4561 5304 -942 614 217 C ATOM 1969 CD1 ILE A 270 27.080 7.360 19.020 1.00 36.69 C ANISOU 1969 CD1 ILE A 270 4250 4371 5321 -805 381 50 C ATOM 1970 N LYS A 271 27.520 9.366 14.017 1.00 47.66 N ANISOU 1970 N LYS A 271 5673 5840 6596 -1082 743 556 N ATOM 1971 CA LYS A 271 28.045 10.670 13.603 1.00 51.61 C ANISOU 1971 CA LYS A 271 6164 6249 7197 -1213 794 677 C ATOM 1972 C LYS A 271 27.047 11.528 12.817 1.00 52.60 C ANISOU 1972 C LYS A 271 6402 6295 7290 -1226 793 868 C ATOM 1973 O LYS A 271 27.257 12.726 12.652 1.00 54.85 O ANISOU 1973 O LYS A 271 6700 6448 7692 -1320 809 982 O ATOM 1974 CB LYS A 271 29.365 10.519 12.822 1.00 53.78 C ANISOU 1974 CB LYS A 271 6322 6655 7458 -1325 915 693 C ATOM 1975 CG LYS A 271 29.392 9.420 11.762 1.00 59.04 C ANISOU 1975 CG LYS A 271 6968 7528 7936 -1295 1000 691 C ATOM 1976 CD LYS A 271 30.634 9.532 10.876 1.00 67.23 C ANISOU 1976 CD LYS A 271 7894 8690 8962 -1425 1144 728 C ATOM 1977 CE LYS A 271 30.961 8.208 10.191 1.00 71.01 C ANISOU 1977 CE LYS A 271 8307 9378 9297 -1379 1230 628 C ATOM 1978 NZ LYS A 271 29.822 7.699 9.373 1.00 72.94 N ANISOU 1978 NZ LYS A 271 8668 9705 9340 -1316 1227 682 N ATOM 1979 N LYS A 272 25.967 10.919 12.342 1.00 53.53 N ANISOU 1979 N LYS A 272 6594 6483 7260 -1133 766 906 N ATOM 1980 CA LYS A 272 24.883 11.655 11.694 1.00 52.82 C ANISOU 1980 CA LYS A 272 6605 6321 7144 -1121 736 1086 C ATOM 1981 C LYS A 272 23.879 12.245 12.690 1.00 50.01 C ANISOU 1981 C LYS A 272 6310 5771 6919 -1033 632 1057 C ATOM 1982 O LYS A 272 23.059 13.075 12.302 1.00 52.43 O ANISOU 1982 O LYS A 272 6684 5968 7268 -1022 598 1208 O ATOM 1983 CB LYS A 272 24.142 10.753 10.698 1.00 53.73 C ANISOU 1983 CB LYS A 272 6764 6614 7039 -1069 745 1137 C ATOM 1984 CG LYS A 272 24.933 10.414 9.439 1.00 57.48 C ANISOU 1984 CG LYS A 272 7198 7281 7359 -1169 861 1203 C ATOM 1985 CD LYS A 272 24.036 9.719 8.417 1.00 63.36 C ANISOU 1985 CD LYS A 272 8005 8188 7882 -1128 855 1263 C ATOM 1986 CE LYS A 272 24.679 9.635 7.037 1.00 69.35 C ANISOU 1986 CE LYS A 272 8745 9143 8463 -1246 974 1361 C ATOM 1987 NZ LYS A 272 23.682 9.281 5.979 1.00 68.51 N ANISOU 1987 NZ LYS A 272 8716 9179 8135 -1228 946 1461 N ATOM 1988 N MET A 273 23.927 11.816 13.955 1.00 46.08 N ANISOU 1988 N MET A 273 5787 5237 6484 -969 582 869 N ATOM 1989 CA MET A 273 23.013 12.338 14.982 1.00 44.43 C ANISOU 1989 CA MET A 273 5629 4864 6389 -889 500 809 C ATOM 1990 C MET A 273 23.296 13.826 15.256 1.00 43.75 C ANISOU 1990 C MET A 273 5551 4563 6510 -966 499 861 C ATOM 1991 O MET A 273 24.453 14.229 15.345 1.00 45.79 O ANISOU 1991 O MET A 273 5750 4796 6851 -1077 540 840 O ATOM 1992 CB MET A 273 23.129 11.542 16.291 1.00 42.98 C ANISOU 1992 CB MET A 273 5414 4714 6203 -826 454 600 C ATOM 1993 CG MET A 273 22.718 10.064 16.197 1.00 43.75 C ANISOU 1993 CG MET A 273 5508 4982 6132 -740 442 541 C ATOM 1994 SD MET A 273 20.996 9.776 15.702 1.00 46.27 S ANISOU 1994 SD MET A 273 5909 5317 6354 -630 400 626 S ATOM 1995 CE MET A 273 21.191 9.589 13.936 1.00 51.35 C ANISOU 1995 CE MET A 273 6557 6096 6858 -691 464 793 C ATOM 1996 N PRO A 274 22.241 14.648 15.384 1.00 43.50 N ANISOU 1996 N PRO A 274 5584 4365 6579 -908 453 925 N ATOM 1997 CA PRO A 274 22.434 16.081 15.625 1.00 44.66 C ANISOU 1997 CA PRO A 274 5742 4275 6951 -973 451 970 C ATOM 1998 C PRO A 274 23.318 16.448 16.834 1.00 42.63 C ANISOU 1998 C PRO A 274 5439 3928 6833 -1036 445 774 C ATOM 1999 O PRO A 274 24.046 17.432 16.766 1.00 41.97 O ANISOU 1999 O PRO A 274 5334 3704 6907 -1150 470 815 O ATOM 2000 CB PRO A 274 21.006 16.589 15.829 1.00 45.29 C ANISOU 2000 CB PRO A 274 5884 4211 7113 -854 392 1006 C ATOM 2001 CG PRO A 274 20.173 15.672 15.020 1.00 43.84 C ANISOU 2001 CG PRO A 274 5725 4203 6732 -773 376 1103 C ATOM 2002 CD PRO A 274 20.820 14.329 15.144 1.00 44.40 C ANISOU 2002 CD PRO A 274 5753 4498 6618 -783 404 980 C ATOM 2003 N GLU A 275 23.257 15.666 17.912 1.00 41.02 N ANISOU 2003 N GLU A 275 5216 3806 6563 -971 407 571 N ATOM 2004 CA GLU A 275 24.023 15.958 19.130 1.00 40.94 C ANISOU 2004 CA GLU A 275 5164 3737 6656 -1028 383 376 C ATOM 2005 C GLU A 275 25.345 15.195 19.213 1.00 41.30 C ANISOU 2005 C GLU A 275 5118 3950 6625 -1106 400 311 C ATOM 2006 O GLU A 275 25.996 15.198 20.266 1.00 42.66 O ANISOU 2006 O GLU A 275 5244 4122 6844 -1146 361 143 O ATOM 2007 CB GLU A 275 23.189 15.640 20.381 1.00 39.23 C ANISOU 2007 CB GLU A 275 4980 3514 6410 -921 326 194 C ATOM 2008 CG GLU A 275 21.860 16.391 20.473 1.00 39.63 C ANISOU 2008 CG GLU A 275 5100 3397 6561 -830 313 218 C ATOM 2009 CD GLU A 275 22.033 17.891 20.598 1.00 47.34 C ANISOU 2009 CD GLU A 275 6089 4115 7784 -899 321 220 C ATOM 2010 OE1 GLU A 275 23.142 18.343 20.957 1.00 53.25 O ANISOU 2010 OE1 GLU A 275 6795 4814 8622 -1021 326 143 O ATOM 2011 OE2 GLU A 275 21.054 18.622 20.333 1.00 52.44 O ANISOU 2011 OE2 GLU A 275 6780 4596 8548 -830 318 298 O ATOM 2012 N HIS A 276 25.750 14.549 18.121 1.00 40.12 N ANISOU 2012 N HIS A 276 4936 3948 6361 -1129 456 434 N ATOM 2013 CA HIS A 276 26.988 13.766 18.133 1.00 41.44 C ANISOU 2013 CA HIS A 276 4997 4276 6471 -1187 481 369 C ATOM 2014 C HIS A 276 28.167 14.594 18.634 1.00 40.42 C ANISOU 2014 C HIS A 276 4790 4059 6508 -1324 482 302 C ATOM 2015 O HIS A 276 28.923 14.134 19.476 1.00 38.88 O ANISOU 2015 O HIS A 276 4518 3938 6318 -1341 440 156 O ATOM 2016 CB HIS A 276 27.309 13.183 16.751 1.00 42.09 C ANISOU 2016 CB HIS A 276 5051 4510 6432 -1212 567 510 C ATOM 2017 CG HIS A 276 28.609 12.443 16.706 1.00 42.16 C ANISOU 2017 CG HIS A 276 4934 4671 6413 -1267 608 438 C ATOM 2018 ND1 HIS A 276 28.813 11.254 17.375 1.00 44.18 N ANISOU 2018 ND1 HIS A 276 5140 5050 6597 -1187 562 300 N ATOM 2019 CD2 HIS A 276 29.779 12.734 16.092 1.00 45.97 C ANISOU 2019 CD2 HIS A 276 5321 5199 6948 -1394 690 488 C ATOM 2020 CE1 HIS A 276 30.049 10.842 17.167 1.00 45.16 C ANISOU 2020 CE1 HIS A 276 5137 5281 6740 -1250 609 264 C ATOM 2021 NE2 HIS A 276 30.655 11.721 16.389 1.00 45.49 N ANISOU 2021 NE2 HIS A 276 5144 5286 6852 -1378 693 370 N ATOM 2022 N SER A 277 28.315 15.811 18.121 1.00 42.81 N ANISOU 2022 N SER A 277 5110 4202 6954 -1424 523 416 N ATOM 2023 CA SER A 277 29.397 16.702 18.545 1.00 46.82 C ANISOU 2023 CA SER A 277 5544 4603 7644 -1572 526 357 C ATOM 2024 C SER A 277 29.378 16.955 20.053 1.00 46.40 C ANISOU 2024 C SER A 277 5491 4466 7673 -1559 431 135 C ATOM 2025 O SER A 277 30.425 16.952 20.707 1.00 46.94 O ANISOU 2025 O SER A 277 5462 4573 7798 -1646 400 10 O ATOM 2026 CB SER A 277 29.304 18.043 17.811 1.00 50.23 C ANISOU 2026 CB SER A 277 6019 4831 8236 -1671 575 528 C ATOM 2027 OG SER A 277 29.618 17.888 16.440 1.00 57.08 O ANISOU 2027 OG SER A 277 6867 5802 9020 -1729 669 734 O ATOM 2028 N THR A 278 28.182 17.192 20.584 1.00 45.50 N ANISOU 2028 N THR A 278 5481 4247 7561 -1453 386 85 N ATOM 2029 CA THR A 278 27.976 17.392 22.016 1.00 45.90 C ANISOU 2029 CA THR A 278 5548 4239 7652 -1430 306 -136 C ATOM 2030 C THR A 278 28.444 16.166 22.803 1.00 42.77 C ANISOU 2030 C THR A 278 5090 4063 7098 -1391 247 -269 C ATOM 2031 O THR A 278 29.112 16.296 23.829 1.00 42.28 O ANISOU 2031 O THR A 278 4976 4014 7073 -1454 183 -434 O ATOM 2032 CB THR A 278 26.484 17.639 22.330 1.00 46.72 C ANISOU 2032 CB THR A 278 5764 4234 7751 -1299 288 -158 C ATOM 2033 OG1 THR A 278 25.887 18.400 21.272 1.00 52.28 O ANISOU 2033 OG1 THR A 278 6523 4785 8555 -1292 340 37 O ATOM 2034 CG2 THR A 278 26.322 18.382 23.652 1.00 48.58 C ANISOU 2034 CG2 THR A 278 6024 4337 8098 -1317 237 -380 C ATOM 2035 N LEU A 279 28.085 14.982 22.311 1.00 39.90 N ANISOU 2035 N LEU A 279 4732 3867 6562 -1289 262 -192 N ATOM 2036 CA LEU A 279 28.493 13.725 22.928 1.00 38.66 C ANISOU 2036 CA LEU A 279 4516 3906 6268 -1240 206 -283 C ATOM 2037 C LEU A 279 30.010 13.624 23.007 1.00 40.78 C ANISOU 2037 C LEU A 279 4645 4252 6596 -1353 195 -322 C ATOM 2038 O LEU A 279 30.560 13.306 24.063 1.00 39.94 O ANISOU 2038 O LEU A 279 4483 4219 6475 -1370 108 -458 O ATOM 2039 CB LEU A 279 27.939 12.536 22.143 1.00 37.17 C ANISOU 2039 CB LEU A 279 4348 3854 5921 -1129 241 -177 C ATOM 2040 CG LEU A 279 28.206 11.145 22.723 1.00 35.97 C ANISOU 2040 CG LEU A 279 4145 3880 5641 -1059 184 -250 C ATOM 2041 CD1 LEU A 279 27.387 10.936 23.976 1.00 38.84 C ANISOU 2041 CD1 LEU A 279 4579 4244 5937 -988 103 -365 C ATOM 2042 CD2 LEU A 279 27.886 10.082 21.689 1.00 31.35 C ANISOU 2042 CD2 LEU A 279 3564 3407 4941 -980 238 -143 C ATOM 2043 N MET A 280 30.684 13.907 21.894 1.00 42.22 N ANISOU 2043 N MET A 280 4767 4430 6844 -1435 282 -197 N ATOM 2044 CA MET A 280 32.147 13.858 21.849 1.00 43.94 C ANISOU 2044 CA MET A 280 4832 4724 7138 -1548 290 -225 C ATOM 2045 C MET A 280 32.755 14.823 22.866 1.00 46.25 C ANISOU 2045 C MET A 280 5085 4910 7580 -1667 217 -363 C ATOM 2046 O MET A 280 33.743 14.497 23.532 1.00 46.36 O ANISOU 2046 O MET A 280 4979 5022 7615 -1718 149 -467 O ATOM 2047 CB MET A 280 32.674 14.200 20.447 1.00 45.07 C ANISOU 2047 CB MET A 280 4926 4867 7331 -1636 417 -62 C ATOM 2048 CG MET A 280 32.277 13.236 19.338 1.00 46.41 C ANISOU 2048 CG MET A 280 5116 5172 7344 -1546 498 58 C ATOM 2049 SD MET A 280 32.798 11.529 19.588 1.00 53.52 S ANISOU 2049 SD MET A 280 5911 6299 8125 -1442 467 -33 S ATOM 2050 CE MET A 280 31.441 10.886 20.562 1.00 52.50 C ANISOU 2050 CE MET A 280 5916 6157 7876 -1282 357 -107 C ATOM 2051 N LYS A 281 32.163 16.011 22.976 1.00 46.67 N ANISOU 2051 N LYS A 281 5232 4758 7743 -1710 226 -367 N ATOM 2052 CA LYS A 281 32.650 17.032 23.897 1.00 48.76 C ANISOU 2052 CA LYS A 281 5472 4893 8163 -1830 165 -515 C ATOM 2053 C LYS A 281 32.490 16.623 25.366 1.00 48.41 C ANISOU 2053 C LYS A 281 5440 4926 8029 -1782 41 -721 C ATOM 2054 O LYS A 281 33.375 16.877 26.179 1.00 49.83 O ANISOU 2054 O LYS A 281 5533 5131 8269 -1885 -37 -860 O ATOM 2055 CB LYS A 281 31.925 18.355 23.639 1.00 50.86 C ANISOU 2055 CB LYS A 281 5844 4897 8583 -1866 209 -473 C ATOM 2056 CG LYS A 281 32.248 19.463 24.640 1.00 53.86 C ANISOU 2056 CG LYS A 281 6220 5109 9136 -1982 148 -658 C ATOM 2057 CD LYS A 281 31.511 20.758 24.314 1.00 59.62 C ANISOU 2057 CD LYS A 281 7051 5549 10052 -2005 197 -607 C ATOM 2058 CE LYS A 281 29.986 20.625 24.425 1.00 61.94 C ANISOU 2058 CE LYS A 281 7481 5789 10264 -1830 201 -601 C ATOM 2059 NZ LYS A 281 29.514 20.258 25.792 1.00 60.71 N ANISOU 2059 NZ LYS A 281 7362 5708 9999 -1756 120 -837 N ATOM 2060 N ASP A 282 31.363 15.993 25.691 1.00 46.35 N ANISOU 2060 N ASP A 282 5283 4712 7615 -1634 21 -735 N ATOM 2061 CA ASP A 282 31.016 15.655 27.072 1.00 45.79 C ANISOU 2061 CA ASP A 282 5248 4716 7435 -1587 -82 -913 C ATOM 2062 C ASP A 282 31.584 14.318 27.542 1.00 45.67 C ANISOU 2062 C ASP A 282 5149 4936 7266 -1540 -163 -930 C ATOM 2063 O ASP A 282 31.843 14.150 28.730 1.00 48.69 O ANISOU 2063 O ASP A 282 5513 5404 7584 -1562 -272 -1074 O ATOM 2064 CB ASP A 282 29.484 15.614 27.245 1.00 45.40 C ANISOU 2064 CB ASP A 282 5342 4609 7299 -1454 -57 -917 C ATOM 2065 CG ASP A 282 28.835 16.990 27.168 1.00 46.40 C ANISOU 2065 CG ASP A 282 5550 4487 7593 -1485 -8 -953 C ATOM 2066 OD1 ASP A 282 27.590 17.041 27.122 1.00 54.08 O ANISOU 2066 OD1 ASP A 282 6621 5396 8531 -1374 26 -935 O ATOM 2067 OD2 ASP A 282 29.552 18.009 27.156 1.00 42.71 O ANISOU 2067 OD2 ASP A 282 5041 3880 7306 -1618 -4 -999 O ATOM 2068 N PHE A 283 31.755 13.362 26.631 1.00 42.28 N ANISOU 2068 N PHE A 283 4673 4612 6779 -1473 -115 -785 N ATOM 2069 CA PHE A 283 32.117 11.997 27.018 1.00 42.91 C ANISOU 2069 CA PHE A 283 4685 4888 6729 -1398 -187 -785 C ATOM 2070 C PHE A 283 33.463 11.543 26.468 1.00 44.08 C ANISOU 2070 C PHE A 283 4664 5135 6951 -1451 -179 -734 C ATOM 2071 O PHE A 283 33.893 11.991 25.408 1.00 44.72 O ANISOU 2071 O PHE A 283 4696 5161 7135 -1514 -76 -647 O ATOM 2072 CB PHE A 283 31.034 11.012 26.565 1.00 39.71 C ANISOU 2072 CB PHE A 283 4368 4534 6184 -1246 -145 -688 C ATOM 2073 CG PHE A 283 29.721 11.197 27.265 1.00 39.94 C ANISOU 2073 CG PHE A 283 4539 4513 6124 -1178 -163 -748 C ATOM 2074 CD1 PHE A 283 29.461 10.539 28.457 1.00 38.81 C ANISOU 2074 CD1 PHE A 283 4419 4479 5846 -1132 -262 -834 C ATOM 2075 CD2 PHE A 283 28.745 12.036 26.736 1.00 41.62 C ANISOU 2075 CD2 PHE A 283 4854 4571 6388 -1160 -81 -710 C ATOM 2076 CE1 PHE A 283 28.247 10.700 29.112 1.00 43.96 C ANISOU 2076 CE1 PHE A 283 5193 5102 6410 -1076 -262 -896 C ATOM 2077 CE2 PHE A 283 27.526 12.202 27.383 1.00 44.68 C ANISOU 2077 CE2 PHE A 283 5352 4915 6708 -1090 -89 -775 C ATOM 2078 CZ PHE A 283 27.277 11.535 28.574 1.00 44.26 C ANISOU 2078 CZ PHE A 283 5319 4985 6514 -1051 -171 -876 C ATOM 2079 N ARG A 284 34.107 10.642 27.211 1.00 46.30 N ANISOU 2079 N ARG A 284 4850 5566 7176 -1424 -290 -783 N ATOM 2080 CA ARG A 284 35.313 9.941 26.779 1.00 46.80 C ANISOU 2080 CA ARG A 284 4735 5743 7304 -1435 -293 -740 C ATOM 2081 C ARG A 284 35.098 8.432 26.926 1.00 46.20 C ANISOU 2081 C ARG A 284 4646 5796 7110 -1287 -342 -695 C ATOM 2082 O ARG A 284 34.679 7.961 27.981 1.00 44.25 O ANISOU 2082 O ARG A 284 4454 5605 6754 -1233 -457 -740 O ATOM 2083 CB ARG A 284 36.522 10.381 27.607 1.00 49.40 C ANISOU 2083 CB ARG A 284 4921 6117 7732 -1559 -406 -845 C ATOM 2084 CG ARG A 284 37.055 11.765 27.239 1.00 53.56 C ANISOU 2084 CG ARG A 284 5408 6516 8424 -1725 -343 -876 C ATOM 2085 CD ARG A 284 38.150 12.250 28.182 1.00 57.74 C ANISOU 2085 CD ARG A 284 5805 7088 9047 -1860 -472 -1005 C ATOM 2086 NE ARG A 284 39.160 11.228 28.472 1.00 64.36 N ANISOU 2086 NE ARG A 284 6462 8105 9888 -1826 -569 -1000 N ATOM 2087 CZ ARG A 284 40.127 10.835 27.638 1.00 68.95 C ANISOU 2087 CZ ARG A 284 6866 8750 10581 -1838 -502 -929 C ATOM 2088 NH1 ARG A 284 40.249 11.363 26.420 1.00 71.42 N ANISOU 2088 NH1 ARG A 284 7164 8981 10991 -1897 -330 -849 N ATOM 2089 NH2 ARG A 284 40.982 9.895 28.024 1.00 69.66 N ANISOU 2089 NH2 ARG A 284 6787 8993 10688 -1790 -607 -935 N ATOM 2090 N ARG A 285 35.380 7.694 25.853 1.00 47.04 N ANISOU 2090 N ARG A 285 4683 5947 7242 -1228 -247 -607 N ATOM 2091 CA ARG A 285 35.345 6.227 25.836 1.00 47.80 C ANISOU 2091 CA ARG A 285 4741 6145 7275 -1092 -281 -567 C ATOM 2092 C ARG A 285 35.968 5.589 27.081 1.00 48.81 C ANISOU 2092 C ARG A 285 4778 6372 7397 -1071 -459 -616 C ATOM 2093 O ARG A 285 35.396 4.668 27.663 1.00 46.71 O ANISOU 2093 O ARG A 285 4573 6149 7025 -968 -537 -593 O ATOM 2094 CB ARG A 285 36.074 5.713 24.583 1.00 49.11 C ANISOU 2094 CB ARG A 285 4778 6356 7525 -1074 -158 -514 C ATOM 2095 CG ARG A 285 36.343 4.201 24.555 1.00 53.45 C ANISOU 2095 CG ARG A 285 5241 6996 8070 -942 -194 -496 C ATOM 2096 CD ARG A 285 36.894 3.723 23.209 1.00 57.28 C ANISOU 2096 CD ARG A 285 5618 7522 8624 -919 -41 -469 C ATOM 2097 NE ARG A 285 36.181 4.327 22.084 1.00 59.66 N ANISOU 2097 NE ARG A 285 6037 7769 8861 -957 115 -417 N ATOM 2098 CZ ARG A 285 34.953 3.995 21.687 1.00 61.37 C ANISOU 2098 CZ ARG A 285 6416 7953 8950 -881 157 -373 C ATOM 2099 NH1 ARG A 285 34.261 3.037 22.311 1.00 57.67 N ANISOU 2099 NH1 ARG A 285 6017 7490 8407 -766 66 -379 N ATOM 2100 NH2 ARG A 285 34.407 4.631 20.654 1.00 62.90 N ANISOU 2100 NH2 ARG A 285 6699 8109 9092 -928 284 -314 N ATOM 2101 N ASN A 286 37.141 6.084 27.474 1.00 49.21 N ANISOU 2101 N ASN A 286 4678 6460 7560 -1174 -526 -674 N ATOM 2102 CA ASN A 286 37.908 5.508 28.580 1.00 51.82 C ANISOU 2102 CA ASN A 286 4889 6902 7898 -1164 -710 -708 C ATOM 2103 C ASN A 286 37.145 5.426 29.906 1.00 50.02 C ANISOU 2103 C ASN A 286 4795 6704 7504 -1146 -853 -743 C ATOM 2104 O ASN A 286 37.406 4.548 30.725 1.00 50.11 O ANISOU 2104 O ASN A 286 4756 6818 7466 -1087 -999 -719 O ATOM 2105 CB ASN A 286 39.190 6.306 28.793 1.00 54.61 C ANISOU 2105 CB ASN A 286 5069 7283 8398 -1307 -760 -778 C ATOM 2106 CG ASN A 286 39.993 5.804 29.965 1.00 61.41 C ANISOU 2106 CG ASN A 286 5800 8271 9263 -1308 -970 -810 C ATOM 2107 OD1 ASN A 286 39.981 6.403 31.044 1.00 64.07 O ANISOU 2107 OD1 ASN A 286 6177 8633 9532 -1395 -1101 -893 O ATOM 2108 ND2 ASN A 286 40.676 4.680 29.773 1.00 69.10 N ANISOU 2108 ND2 ASN A 286 6617 9325 10313 -1207 -1010 -748 N ATOM 2109 N THR A 287 36.208 6.345 30.105 1.00 47.91 N ANISOU 2109 N THR A 287 4695 6352 7158 -1197 -806 -796 N ATOM 2110 CA THR A 287 35.364 6.358 31.295 1.00 46.43 C ANISOU 2110 CA THR A 287 4646 6197 6799 -1186 -906 -847 C ATOM 2111 C THR A 287 34.549 5.075 31.487 1.00 45.62 C ANISOU 2111 C THR A 287 4623 6149 6563 -1043 -931 -752 C ATOM 2112 O THR A 287 34.181 4.743 32.611 1.00 47.16 O ANISOU 2112 O THR A 287 4880 6426 6613 -1031 -1049 -767 O ATOM 2113 CB THR A 287 34.394 7.548 31.228 1.00 45.72 C ANISOU 2113 CB THR A 287 4715 5977 6678 -1243 -809 -921 C ATOM 2114 OG1 THR A 287 35.149 8.759 31.071 1.00 45.57 O ANISOU 2114 OG1 THR A 287 4626 5885 6804 -1385 -789 -1005 O ATOM 2115 CG2 THR A 287 33.526 7.632 32.483 1.00 40.53 C ANISOU 2115 CG2 THR A 287 4192 5365 5843 -1239 -893 -1001 C ATOM 2116 N TYR A 288 34.270 4.363 30.396 1.00 44.01 N ANISOU 2116 N TYR A 288 4418 5902 6401 -945 -819 -658 N ATOM 2117 CA TYR A 288 33.355 3.227 30.420 1.00 42.90 C ANISOU 2117 CA TYR A 288 4367 5779 6154 -818 -818 -573 C ATOM 2118 C TYR A 288 34.013 1.929 29.963 1.00 43.43 C ANISOU 2118 C TYR A 288 4306 5888 6306 -720 -840 -488 C ATOM 2119 O TYR A 288 33.333 0.995 29.533 1.00 40.56 O ANISOU 2119 O TYR A 288 4000 5501 5908 -616 -793 -418 O ATOM 2120 CB TYR A 288 32.142 3.541 29.543 1.00 40.84 C ANISOU 2120 CB TYR A 288 4249 5415 5852 -784 -661 -553 C ATOM 2121 CG TYR A 288 31.483 4.859 29.888 1.00 41.29 C ANISOU 2121 CG TYR A 288 4419 5401 5866 -866 -625 -638 C ATOM 2122 CD1 TYR A 288 30.615 4.961 30.966 1.00 46.75 C ANISOU 2122 CD1 TYR A 288 5228 6122 6413 -864 -684 -687 C ATOM 2123 CD2 TYR A 288 31.737 6.005 29.144 1.00 42.00 C ANISOU 2123 CD2 TYR A 288 4496 5392 6068 -948 -529 -672 C ATOM 2124 CE1 TYR A 288 30.007 6.165 31.291 1.00 47.11 C ANISOU 2124 CE1 TYR A 288 5368 6092 6438 -929 -643 -787 C ATOM 2125 CE2 TYR A 288 31.133 7.217 29.457 1.00 43.29 C ANISOU 2125 CE2 TYR A 288 4760 5464 6226 -1015 -498 -753 C ATOM 2126 CZ TYR A 288 30.269 7.290 30.532 1.00 47.04 C ANISOU 2126 CZ TYR A 288 5343 5962 6567 -1000 -554 -822 C ATOM 2127 OH TYR A 288 29.671 8.485 30.854 1.00 46.67 O ANISOU 2127 OH TYR A 288 5386 5814 6533 -1057 -516 -924 O ATOM 2128 N THR A 289 35.335 1.872 30.084 1.00 46.91 N ANISOU 2128 N THR A 289 4566 6386 6872 -753 -916 -503 N ATOM 2129 CA THR A 289 36.121 0.745 29.576 1.00 49.19 C ANISOU 2129 CA THR A 289 4699 6702 7290 -658 -925 -443 C ATOM 2130 C THR A 289 35.791 -0.611 30.212 1.00 50.20 C ANISOU 2130 C THR A 289 4847 6863 7363 -539 -1040 -352 C ATOM 2131 O THR A 289 35.784 -1.635 29.520 1.00 48.62 O ANISOU 2131 O THR A 289 4605 6627 7242 -430 -986 -300 O ATOM 2132 CB THR A 289 37.639 0.991 29.727 1.00 51.19 C ANISOU 2132 CB THR A 289 4730 7020 7700 -720 -1002 -480 C ATOM 2133 OG1 THR A 289 38.338 -0.203 29.365 1.00 55.35 O ANISOU 2133 OG1 THR A 289 5100 7571 8361 -607 -1023 -425 O ATOM 2134 CG2 THR A 289 38.007 1.375 31.163 1.00 51.46 C ANISOU 2134 CG2 THR A 289 4745 7144 7665 -799 -1203 -512 C ATOM 2135 N ASN A 290 35.530 -0.621 31.517 1.00 51.00 N ANISOU 2135 N ASN A 290 5013 7033 7331 -566 -1196 -334 N ATOM 2136 CA ASN A 290 35.157 -1.856 32.209 1.00 52.40 C ANISOU 2136 CA ASN A 290 5226 7243 7442 -470 -1313 -222 C ATOM 2137 C ASN A 290 33.627 -2.063 32.319 1.00 49.27 C ANISOU 2137 C ASN A 290 5040 6805 6875 -440 -1246 -188 C ATOM 2138 O ASN A 290 33.163 -2.781 33.206 1.00 49.84 O ANISOU 2138 O ASN A 290 5177 6924 6836 -407 -1354 -102 O ATOM 2139 CB ASN A 290 35.812 -1.894 33.600 1.00 56.35 C ANISOU 2139 CB ASN A 290 5662 7870 7881 -518 -1536 -195 C ATOM 2140 CG ASN A 290 37.341 -1.966 33.538 1.00 65.29 C ANISOU 2140 CG ASN A 290 6554 9049 9203 -525 -1630 -203 C ATOM 2141 OD1 ASN A 290 37.918 -2.492 32.582 1.00 73.56 O ANISOU 2141 OD1 ASN A 290 7469 10038 10441 -447 -1552 -190 O ATOM 2142 ND2 ASN A 290 38.002 -1.441 34.570 1.00 71.19 N ANISOU 2142 ND2 ASN A 290 7238 9914 9899 -620 -1798 -235 N ATOM 2143 N CYS A 291 32.856 -1.447 31.416 1.00 45.36 N ANISOU 2143 N CYS A 291 4644 6228 6364 -455 -1073 -244 N ATOM 2144 CA CYS A 291 31.393 -1.550 31.413 1.00 41.44 C ANISOU 2144 CA CYS A 291 4327 5690 5726 -429 -998 -222 C ATOM 2145 C CYS A 291 30.883 -2.367 30.228 1.00 40.52 C ANISOU 2145 C CYS A 291 4229 5488 5678 -334 -876 -176 C ATOM 2146 O CYS A 291 31.392 -2.239 29.118 1.00 41.70 O ANISOU 2146 O CYS A 291 4300 5594 5949 -323 -774 -209 O ATOM 2147 CB CYS A 291 30.753 -0.163 31.353 1.00 39.98 C ANISOU 2147 CB CYS A 291 4249 5475 5465 -518 -907 -321 C ATOM 2148 SG CYS A 291 31.268 0.965 32.662 1.00 40.08 S ANISOU 2148 SG CYS A 291 4254 5574 5399 -648 -1027 -425 S ATOM 2149 N SER A 292 29.870 -3.193 30.481 1.00 37.70 N ANISOU 2149 N SER A 292 3975 5115 5234 -275 -883 -105 N ATOM 2150 CA SER A 292 29.183 -3.974 29.446 1.00 37.54 C ANISOU 2150 CA SER A 292 3994 5014 5255 -197 -774 -75 C ATOM 2151 C SER A 292 27.892 -4.555 30.006 1.00 34.15 C ANISOU 2151 C SER A 292 3700 4581 4695 -172 -791 -8 C ATOM 2152 O SER A 292 27.748 -4.700 31.214 1.00 32.89 O ANISOU 2152 O SER A 292 3576 4487 4433 -197 -902 42 O ATOM 2153 CB SER A 292 30.054 -5.125 28.934 1.00 38.22 C ANISOU 2153 CB SER A 292 3945 5067 5508 -109 -797 -38 C ATOM 2154 OG SER A 292 30.259 -6.098 29.949 1.00 43.36 O ANISOU 2154 OG SER A 292 4570 5741 6166 -65 -951 61 O ATOM 2155 N LEU A 293 26.955 -4.879 29.119 1.00 33.91 N ANISOU 2155 N LEU A 293 3740 4485 4661 -134 -679 -6 N ATOM 2156 CA LEU A 293 25.701 -5.495 29.525 1.00 34.30 C ANISOU 2156 CA LEU A 293 3900 4523 4608 -114 -681 57 C ATOM 2157 C LEU A 293 25.948 -6.837 30.218 1.00 36.89 C ANISOU 2157 C LEU A 293 4195 4848 4973 -62 -799 168 C ATOM 2158 O LEU A 293 25.237 -7.178 31.164 1.00 36.26 O ANISOU 2158 O LEU A 293 4193 4806 4778 -80 -856 244 O ATOM 2159 CB LEU A 293 24.764 -5.669 28.333 1.00 31.67 C ANISOU 2159 CB LEU A 293 3624 4122 4288 -83 -551 35 C ATOM 2160 CG LEU A 293 23.350 -6.177 28.637 1.00 32.17 C ANISOU 2160 CG LEU A 293 3796 4175 4253 -75 -535 88 C ATOM 2161 CD1 LEU A 293 22.563 -5.189 29.501 1.00 24.16 C ANISOU 2161 CD1 LEU A 293 2868 3221 3089 -137 -530 66 C ATOM 2162 CD2 LEU A 293 22.590 -6.490 27.350 1.00 24.22 C ANISOU 2162 CD2 LEU A 293 2818 3104 3280 -43 -427 63 C ATOM 2163 N ILE A 294 26.962 -7.573 29.761 1.00 36.99 N ANISOU 2163 N ILE A 294 4087 4815 5152 0 -832 182 N ATOM 2164 CA ILE A 294 27.360 -8.829 30.402 1.00 38.88 C ANISOU 2164 CA ILE A 294 4273 5029 5470 59 -959 298 C ATOM 2165 C ILE A 294 27.693 -8.598 31.873 1.00 40.77 C ANISOU 2165 C ILE A 294 4516 5377 5598 8 -1114 376 C ATOM 2166 O ILE A 294 27.159 -9.284 32.738 1.00 41.95 O ANISOU 2166 O ILE A 294 4728 5543 5666 6 -1197 497 O ATOM 2167 CB ILE A 294 28.560 -9.498 29.677 1.00 40.22 C ANISOU 2167 CB ILE A 294 4284 5132 5866 141 -967 276 C ATOM 2168 CG1 ILE A 294 28.130 -9.995 28.295 1.00 39.68 C ANISOU 2168 CG1 ILE A 294 4224 4964 5888 193 -821 203 C ATOM 2169 CG2 ILE A 294 29.127 -10.667 30.493 1.00 38.51 C ANISOU 2169 CG2 ILE A 294 3994 4884 5754 206 -1129 411 C ATOM 2170 CD1 ILE A 294 29.264 -10.592 27.491 1.00 44.25 C ANISOU 2170 CD1 ILE A 294 4644 5484 6684 272 -796 146 C ATOM 2171 N LYS A 295 28.546 -7.612 32.153 1.00 42.98 N ANISOU 2171 N LYS A 295 4732 5738 5862 -47 -1153 307 N ATOM 2172 CA LYS A 295 28.948 -7.310 33.530 1.00 44.14 C ANISOU 2172 CA LYS A 295 4875 6008 5888 -109 -1309 357 C ATOM 2173 C LYS A 295 27.783 -6.785 34.375 1.00 41.19 C ANISOU 2173 C LYS A 295 4659 5715 5277 -187 -1291 356 C ATOM 2174 O LYS A 295 27.636 -7.161 35.533 1.00 41.91 O ANISOU 2174 O LYS A 295 4790 5897 5238 -218 -1410 456 O ATOM 2175 CB LYS A 295 30.130 -6.329 33.565 1.00 46.00 C ANISOU 2175 CB LYS A 295 4996 6306 6174 -161 -1349 260 C ATOM 2176 CG LYS A 295 31.478 -6.974 33.204 1.00 54.61 C ANISOU 2176 CG LYS A 295 5898 7365 7487 -89 -1424 291 C ATOM 2177 CD LYS A 295 32.645 -6.039 33.490 1.00 59.34 C ANISOU 2177 CD LYS A 295 6375 8051 8121 -159 -1494 212 C ATOM 2178 CE LYS A 295 33.986 -6.704 33.231 1.00 65.13 C ANISOU 2178 CE LYS A 295 6899 8766 9082 -85 -1578 248 C ATOM 2179 NZ LYS A 295 35.110 -5.800 33.585 0.00 68.02 N ANISOU 2179 NZ LYS A 295 7134 9229 9481 -166 -1658 175 N ATOM 2180 N TYR A 296 26.954 -5.926 33.803 1.00 39.25 N ANISOU 2180 N TYR A 296 4498 5442 4975 -220 -1143 246 N ATOM 2181 CA TYR A 296 25.781 -5.446 34.523 1.00 38.76 C ANISOU 2181 CA TYR A 296 4571 5446 4712 -281 -1104 228 C ATOM 2182 C TYR A 296 24.859 -6.602 34.898 1.00 39.02 C ANISOU 2182 C TYR A 296 4675 5470 4681 -250 -1118 366 C ATOM 2183 O TYR A 296 24.496 -6.750 36.055 1.00 40.47 O ANISOU 2183 O TYR A 296 4918 5760 4698 -300 -1190 432 O ATOM 2184 CB TYR A 296 24.998 -4.416 33.720 1.00 35.65 C ANISOU 2184 CB TYR A 296 4241 4996 4309 -299 -941 102 C ATOM 2185 CG TYR A 296 23.725 -3.991 34.416 1.00 38.43 C ANISOU 2185 CG TYR A 296 4716 5406 4481 -346 -888 75 C ATOM 2186 CD1 TYR A 296 23.750 -3.018 35.413 1.00 40.65 C ANISOU 2186 CD1 TYR A 296 5033 5789 4623 -428 -919 -15 C ATOM 2187 CD2 TYR A 296 22.497 -4.581 34.100 1.00 34.33 C ANISOU 2187 CD2 TYR A 296 4267 4844 3934 -310 -806 129 C ATOM 2188 CE1 TYR A 296 22.590 -2.632 36.074 1.00 38.79 C ANISOU 2188 CE1 TYR A 296 4899 5614 4226 -467 -856 -58 C ATOM 2189 CE2 TYR A 296 21.325 -4.203 34.758 1.00 34.32 C ANISOU 2189 CE2 TYR A 296 4359 4904 3775 -352 -748 101 C ATOM 2190 CZ TYR A 296 21.382 -3.224 35.742 1.00 39.17 C ANISOU 2190 CZ TYR A 296 5006 5623 4255 -426 -767 4 C ATOM 2191 OH TYR A 296 20.239 -2.828 36.397 1.00 42.37 O ANISOU 2191 OH TYR A 296 5493 6095 4510 -463 -695 -46 O ATOM 2192 N MET A 297 24.470 -7.412 33.921 1.00 39.52 N ANISOU 2192 N MET A 297 4733 5412 4871 -177 -1047 404 N ATOM 2193 CA MET A 297 23.509 -8.484 34.179 1.00 41.16 C ANISOU 2193 CA MET A 297 5008 5590 5040 -158 -1046 527 C ATOM 2194 C MET A 297 24.084 -9.573 35.095 1.00 43.98 C ANISOU 2194 C MET A 297 5328 5971 5410 -143 -1210 698 C ATOM 2195 O MET A 297 23.335 -10.215 35.821 1.00 44.65 O ANISOU 2195 O MET A 297 5485 6087 5391 -169 -1240 821 O ATOM 2196 CB MET A 297 22.988 -9.093 32.870 1.00 38.03 C ANISOU 2196 CB MET A 297 4610 5053 4787 -93 -937 508 C ATOM 2197 CG MET A 297 22.164 -8.143 32.015 1.00 40.24 C ANISOU 2197 CG MET A 297 4942 5316 5030 -111 -786 380 C ATOM 2198 SD MET A 297 20.634 -7.526 32.756 1.00 43.86 S ANISOU 2198 SD MET A 297 5524 5860 5283 -179 -718 367 S ATOM 2199 CE MET A 297 19.755 -9.053 33.028 1.00 52.68 C ANISOU 2199 CE MET A 297 6680 6934 6401 -165 -739 521 C ATOM 2200 N GLU A 298 25.406 -9.749 35.070 1.00 46.96 N ANISOU 2200 N GLU A 298 5587 6338 5917 -103 -1316 715 N ATOM 2201 CA GLU A 298 26.103 -10.702 35.940 1.00 51.44 C ANISOU 2201 CA GLU A 298 6099 6928 6519 -79 -1496 888 C ATOM 2202 C GLU A 298 25.949 -10.395 37.427 1.00 53.74 C ANISOU 2202 C GLU A 298 6456 7400 6564 -174 -1608 969 C ATOM 2203 O GLU A 298 25.796 -11.313 38.234 1.00 53.64 O ANISOU 2203 O GLU A 298 6469 7412 6499 -179 -1718 1157 O ATOM 2204 CB GLU A 298 27.603 -10.748 35.613 1.00 53.62 C ANISOU 2204 CB GLU A 298 6211 7174 6988 -20 -1585 865 C ATOM 2205 CG GLU A 298 27.979 -11.745 34.528 1.00 57.56 C ANISOU 2205 CG GLU A 298 6619 7496 7758 97 -1546 875 C ATOM 2206 CD GLU A 298 29.481 -11.834 34.306 1.00 60.43 C ANISOU 2206 CD GLU A 298 6800 7842 8318 160 -1635 856 C ATOM 2207 OE1 GLU A 298 30.195 -10.850 34.601 1.00 63.13 O ANISOU 2207 OE1 GLU A 298 7085 8298 8602 104 -1675 779 O ATOM 2208 OE2 GLU A 298 29.946 -12.892 33.831 1.00 63.72 O ANISOU 2208 OE2 GLU A 298 7122 8127 8961 264 -1661 910 O ATOM 2209 N LYS A 299 26.008 -9.115 37.792 1.00 53.52 N ANISOU 2209 N LYS A 299 6454 7496 6383 -255 -1583 829 N ATOM 2210 CA LYS A 299 25.859 -8.728 39.198 1.00 56.90 C ANISOU 2210 CA LYS A 299 6949 8118 6552 -357 -1677 866 C ATOM 2211 C LYS A 299 24.396 -8.682 39.649 1.00 56.15 C ANISOU 2211 C LYS A 299 6998 8080 6255 -417 -1569 877 C ATOM 2212 O LYS A 299 24.123 -8.397 40.810 1.00 56.93 O ANISOU 2212 O LYS A 299 7163 8352 6114 -508 -1620 899 O ATOM 2213 CB LYS A 299 26.572 -7.398 39.498 1.00 58.92 C ANISOU 2213 CB LYS A 299 7169 8484 6735 -429 -1704 695 C ATOM 2214 CG LYS A 299 25.903 -6.135 38.971 1.00 60.50 C ANISOU 2214 CG LYS A 299 7433 8662 6894 -468 -1526 483 C ATOM 2215 CD LYS A 299 26.543 -4.889 39.583 1.00 65.41 C ANISOU 2215 CD LYS A 299 8035 9404 7415 -562 -1576 329 C ATOM 2216 CE LYS A 299 25.760 -3.623 39.245 1.00 67.63 C ANISOU 2216 CE LYS A 299 8393 9656 7647 -606 -1407 129 C ATOM 2217 NZ LYS A 299 26.167 -2.473 40.105 1.00 69.55 N ANISOU 2217 NZ LYS A 299 8644 10026 7754 -714 -1457 -26 N ATOM 2218 N HIS A 300 23.470 -8.952 38.728 1.00 53.95 N ANISOU 2218 N HIS A 300 6760 7670 6070 -370 -1419 853 N ATOM 2219 CA HIS A 300 22.052 -9.096 39.051 1.00 53.07 C ANISOU 2219 CA HIS A 300 6761 7595 5810 -415 -1314 882 C ATOM 2220 C HIS A 300 21.584 -10.539 38.872 1.00 52.74 C ANISOU 2220 C HIS A 300 6729 7445 5864 -371 -1331 1074 C ATOM 2221 O HIS A 300 20.391 -10.794 38.742 1.00 55.25 O ANISOU 2221 O HIS A 300 7116 7739 6137 -390 -1220 1091 O ATOM 2222 CB HIS A 300 21.217 -8.145 38.186 1.00 50.78 C ANISOU 2222 CB HIS A 300 6507 7248 5539 -409 -1128 694 C ATOM 2223 CG HIS A 300 21.315 -6.719 38.615 1.00 53.78 C ANISOU 2223 CG HIS A 300 6908 7736 5789 -474 -1094 516 C ATOM 2224 ND1 HIS A 300 20.556 -6.203 39.641 1.00 59.02 N ANISOU 2224 ND1 HIS A 300 7654 8551 6220 -558 -1056 470 N ATOM 2225 CD2 HIS A 300 22.102 -5.706 38.181 1.00 52.68 C ANISOU 2225 CD2 HIS A 300 6716 7572 5727 -473 -1089 368 C ATOM 2226 CE1 HIS A 300 20.863 -4.929 39.813 1.00 60.82 C ANISOU 2226 CE1 HIS A 300 7881 8830 6398 -600 -1032 287 C ATOM 2227 NE2 HIS A 300 21.800 -4.604 38.941 1.00 56.18 N ANISOU 2227 NE2 HIS A 300 7213 8133 6000 -553 -1055 230 N ATOM 2228 N LYS A 301 22.537 -11.468 38.839 1.00 53.04 N ANISOU 2228 N LYS A 301 6689 7407 6058 -310 -1469 1211 N ATOM 2229 CA LYS A 301 22.264 -12.910 38.836 1.00 54.09 C ANISOU 2229 CA LYS A 301 6824 7423 6303 -271 -1519 1414 C ATOM 2230 C LYS A 301 21.687 -13.465 37.530 1.00 51.05 C ANISOU 2230 C LYS A 301 6432 6838 6129 -200 -1392 1361 C ATOM 2231 O LYS A 301 21.240 -14.612 37.486 1.00 53.68 O ANISOU 2231 O LYS A 301 6781 7059 6554 -182 -1407 1505 O ATOM 2232 CB LYS A 301 21.364 -13.293 40.023 1.00 56.82 C ANISOU 2232 CB LYS A 301 7273 7899 6419 -368 -1540 1575 C ATOM 2233 CG LYS A 301 21.988 -13.156 41.385 0.00 60.26 C ANISOU 2233 CG LYS A 301 7716 8530 6650 -439 -1703 1690 C ATOM 2234 CD LYS A 301 22.970 -14.283 41.676 0.00 62.30 C ANISOU 2234 CD LYS A 301 7898 8714 7059 -380 -1902 1917 C ATOM 2235 CE LYS A 301 23.465 -14.234 43.112 0.00 64.79 C ANISOU 2235 CE LYS A 301 8231 9249 7136 -465 -2081 2068 C ATOM 2236 NZ LYS A 301 24.399 -15.353 43.420 0.00 66.85 N ANISOU 2236 NZ LYS A 301 8411 9432 7558 -401 -2292 2318 N ATOM 2237 N VAL A 302 21.707 -12.676 36.460 1.00 47.79 N ANISOU 2237 N VAL A 302 5992 6375 5790 -166 -1274 1161 N ATOM 2238 CA VAL A 302 21.238 -13.159 35.162 1.00 42.24 C ANISOU 2238 CA VAL A 302 5277 5505 5268 -104 -1162 1096 C ATOM 2239 C VAL A 302 22.440 -13.704 34.393 1.00 41.60 C ANISOU 2239 C VAL A 302 5079 5292 5435 -5 -1219 1080 C ATOM 2240 O VAL A 302 23.451 -13.020 34.258 1.00 43.58 O ANISOU 2240 O VAL A 302 5255 5587 5716 15 -1250 994 O ATOM 2241 CB VAL A 302 20.525 -12.047 34.388 1.00 40.89 C ANISOU 2241 CB VAL A 302 5145 5360 5033 -125 -1004 908 C ATOM 2242 CG1 VAL A 302 20.187 -12.499 32.975 1.00 33.27 C ANISOU 2242 CG1 VAL A 302 4157 4243 4241 -65 -905 833 C ATOM 2243 CG2 VAL A 302 19.274 -11.622 35.139 1.00 36.56 C ANISOU 2243 CG2 VAL A 302 4695 4927 4271 -210 -940 921 C ATOM 2244 N LYS A 303 22.334 -14.941 33.918 1.00 39.93 N ANISOU 2244 N LYS A 303 4844 4917 5409 55 -1228 1155 N ATOM 2245 CA LYS A 303 23.462 -15.642 33.303 1.00 41.26 C ANISOU 2245 CA LYS A 303 4892 4950 5834 159 -1285 1148 C ATOM 2246 C LYS A 303 23.695 -15.204 31.857 1.00 41.44 C ANISOU 2246 C LYS A 303 4863 4913 5969 207 -1151 938 C ATOM 2247 O LYS A 303 22.769 -15.233 31.043 1.00 40.88 O ANISOU 2247 O LYS A 303 4850 4792 5891 194 -1027 853 O ATOM 2248 CB LYS A 303 23.240 -17.156 33.337 1.00 43.87 C ANISOU 2248 CB LYS A 303 5219 5107 6342 205 -1342 1295 C ATOM 2249 CG LYS A 303 23.250 -17.770 34.740 1.00 47.80 C ANISOU 2249 CG LYS A 303 5748 5647 6768 168 -1501 1546 C ATOM 2250 CD LYS A 303 23.020 -19.254 34.736 0.00 50.21 C ANISOU 2250 CD LYS A 303 6050 5752 7275 210 -1555 1704 C ATOM 2251 CE LYS A 303 23.066 -19.835 36.141 0.00 52.41 C ANISOU 2251 CE LYS A 303 6362 6081 7472 165 -1722 1984 C ATOM 2252 NZ LYS A 303 22.810 -21.302 36.148 0.00 54.08 N ANISOU 2252 NZ LYS A 303 6574 6072 7904 201 -1777 2159 N ATOM 2253 N PRO A 304 24.931 -14.789 31.530 1.00 42.91 N ANISOU 2253 N PRO A 304 4936 5116 6252 255 -1175 857 N ATOM 2254 CA PRO A 304 25.254 -14.363 30.168 1.00 41.13 C ANISOU 2254 CA PRO A 304 4654 4852 6121 291 -1044 670 C ATOM 2255 C PRO A 304 25.050 -15.424 29.078 1.00 40.77 C ANISOU 2255 C PRO A 304 4583 4640 6268 362 -968 611 C ATOM 2256 O PRO A 304 24.776 -15.064 27.937 1.00 40.38 O ANISOU 2256 O PRO A 304 4543 4584 6216 359 -833 460 O ATOM 2257 CB PRO A 304 26.732 -13.977 30.263 1.00 43.28 C ANISOU 2257 CB PRO A 304 4787 5170 6488 329 -1113 638 C ATOM 2258 CG PRO A 304 26.933 -13.608 31.681 1.00 47.63 C ANISOU 2258 CG PRO A 304 5359 5844 6895 273 -1258 765 C ATOM 2259 CD PRO A 304 26.046 -14.526 32.460 1.00 45.59 C ANISOU 2259 CD PRO A 304 5195 5546 6583 258 -1324 934 C ATOM 2260 N ASP A 305 25.182 -16.707 29.414 1.00 41.93 N ANISOU 2260 N ASP A 305 4699 4652 6579 420 -1057 726 N ATOM 2261 CA ASP A 305 24.948 -17.783 28.436 1.00 42.57 C ANISOU 2261 CA ASP A 305 4760 4556 6859 483 -989 655 C ATOM 2262 C ASP A 305 23.478 -18.216 28.331 1.00 40.91 C ANISOU 2262 C ASP A 305 4678 4295 6571 422 -933 683 C ATOM 2263 O ASP A 305 23.159 -19.119 27.559 1.00 43.61 O ANISOU 2263 O ASP A 305 5016 4489 7066 456 -881 618 O ATOM 2264 CB ASP A 305 25.871 -18.997 28.694 1.00 47.67 C ANISOU 2264 CB ASP A 305 5291 5042 7779 590 -1102 743 C ATOM 2265 CG ASP A 305 25.731 -19.570 30.097 1.00 52.76 C ANISOU 2265 CG ASP A 305 5973 5670 8403 572 -1272 997 C ATOM 2266 OD1 ASP A 305 24.987 -19.001 30.927 1.00 58.92 O ANISOU 2266 OD1 ASP A 305 6863 6584 8939 473 -1297 1094 O ATOM 2267 OD2 ASP A 305 26.379 -20.598 30.372 1.00 66.04 O ANISOU 2267 OD2 ASP A 305 7570 7206 10317 659 -1381 1102 O ATOM 2268 N SER A 306 22.580 -17.574 29.078 1.00 38.50 N ANISOU 2268 N SER A 306 4479 4114 6036 328 -938 763 N ATOM 2269 CA SER A 306 21.151 -17.902 28.989 1.00 37.74 C ANISOU 2269 CA SER A 306 4489 3988 5862 263 -878 787 C ATOM 2270 C SER A 306 20.523 -17.393 27.687 1.00 37.09 C ANISOU 2270 C SER A 306 4432 3925 5736 245 -730 596 C ATOM 2271 O SER A 306 20.960 -16.392 27.118 1.00 37.63 O ANISOU 2271 O SER A 306 4473 4087 5737 250 -668 475 O ATOM 2272 CB SER A 306 20.376 -17.351 30.195 1.00 36.51 C ANISOU 2272 CB SER A 306 4424 3973 5474 170 -915 919 C ATOM 2273 OG SER A 306 20.374 -15.930 30.234 1.00 31.82 O ANISOU 2273 OG SER A 306 3851 3546 4693 130 -862 828 O ATOM 2274 N LYS A 307 19.496 -18.085 27.213 1.00 36.80 N ANISOU 2274 N LYS A 307 4445 3802 5736 217 -681 577 N ATOM 2275 CA LYS A 307 18.739 -17.596 26.067 1.00 35.54 C ANISOU 2275 CA LYS A 307 4317 3683 5501 185 -560 420 C ATOM 2276 C LYS A 307 18.076 -16.250 26.379 1.00 34.24 C ANISOU 2276 C LYS A 307 4214 3693 5103 120 -518 422 C ATOM 2277 O LYS A 307 17.940 -15.406 25.494 1.00 35.17 O ANISOU 2277 O LYS A 307 4335 3882 5147 112 -435 300 O ATOM 2278 CB LYS A 307 17.720 -18.634 25.607 1.00 34.81 C ANISOU 2278 CB LYS A 307 4262 3471 5494 156 -533 406 C ATOM 2279 CG LYS A 307 18.363 -19.914 25.054 1.00 38.14 C ANISOU 2279 CG LYS A 307 4620 3698 6175 227 -552 350 C ATOM 2280 CD LYS A 307 17.420 -20.655 24.115 1.00 43.46 C ANISOU 2280 CD LYS A 307 5322 4275 6916 190 -489 240 C ATOM 2281 CE LYS A 307 17.481 -22.165 24.269 1.00 45.07 C ANISOU 2281 CE LYS A 307 5504 4249 7371 218 -546 288 C ATOM 2282 NZ LYS A 307 18.701 -22.776 23.717 1.00 40.46 N ANISOU 2282 NZ LYS A 307 4827 3534 7011 325 -547 179 N ATOM 2283 N ALA A 308 17.698 -16.036 27.640 1.00 32.63 N ANISOU 2283 N ALA A 308 4055 3557 4784 73 -575 562 N ATOM 2284 CA ALA A 308 17.153 -14.747 28.072 1.00 30.63 C ANISOU 2284 CA ALA A 308 3850 3460 4326 18 -535 552 C ATOM 2285 C ALA A 308 18.131 -13.604 27.810 1.00 29.63 C ANISOU 2285 C ALA A 308 3684 3412 4160 45 -521 462 C ATOM 2286 O ALA A 308 17.754 -12.557 27.269 1.00 27.91 O ANISOU 2286 O ALA A 308 3487 3266 3851 25 -444 371 O ATOM 2287 CB ALA A 308 16.772 -14.779 29.559 1.00 29.16 C ANISOU 2287 CB ALA A 308 3711 3347 4021 -37 -599 706 C ATOM 2288 N PHE A 309 19.385 -13.795 28.193 1.00 32.46 N ANISOU 2288 N PHE A 309 3979 3753 4600 88 -599 494 N ATOM 2289 CA PHE A 309 20.354 -12.729 28.043 1.00 32.85 C ANISOU 2289 CA PHE A 309 3982 3879 4623 99 -591 417 C ATOM 2290 C PHE A 309 20.602 -12.421 26.566 1.00 32.25 C ANISOU 2290 C PHE A 309 3867 3775 4610 127 -489 271 C ATOM 2291 O PHE A 309 20.683 -11.256 26.173 1.00 29.08 O ANISOU 2291 O PHE A 309 3471 3449 4128 102 -429 199 O ATOM 2292 CB PHE A 309 21.673 -13.057 28.733 1.00 34.77 C ANISOU 2292 CB PHE A 309 4144 4113 4955 139 -705 482 C ATOM 2293 CG PHE A 309 22.704 -11.982 28.564 1.00 36.73 C ANISOU 2293 CG PHE A 309 4328 4437 5191 139 -697 398 C ATOM 2294 CD1 PHE A 309 22.719 -10.883 29.408 1.00 35.18 C ANISOU 2294 CD1 PHE A 309 4164 4360 4841 78 -726 405 C ATOM 2295 CD2 PHE A 309 23.633 -12.047 27.533 1.00 38.61 C ANISOU 2295 CD2 PHE A 309 4470 4628 5571 192 -651 299 C ATOM 2296 CE1 PHE A 309 23.651 -9.886 29.249 1.00 35.10 C ANISOU 2296 CE1 PHE A 309 4094 4407 4834 66 -719 324 C ATOM 2297 CE2 PHE A 309 24.568 -11.042 27.360 1.00 37.52 C ANISOU 2297 CE2 PHE A 309 4267 4562 5428 178 -635 228 C ATOM 2298 CZ PHE A 309 24.580 -9.963 28.217 1.00 37.01 C ANISOU 2298 CZ PHE A 309 4236 4600 5224 113 -675 245 C ATOM 2299 N HIS A 310 20.725 -13.464 25.754 1.00 31.51 N ANISOU 2299 N HIS A 310 3737 3574 4662 174 -467 229 N ATOM 2300 CA HIS A 310 21.029 -13.266 24.347 1.00 32.02 C ANISOU 2300 CA HIS A 310 3762 3632 4770 195 -367 86 C ATOM 2301 C HIS A 310 19.898 -12.532 23.628 1.00 30.74 C ANISOU 2301 C HIS A 310 3677 3534 4469 141 -279 32 C ATOM 2302 O HIS A 310 20.154 -11.694 22.770 1.00 33.00 O ANISOU 2302 O HIS A 310 3949 3880 4707 130 -206 -49 O ATOM 2303 CB HIS A 310 21.424 -14.584 23.674 1.00 31.39 C ANISOU 2303 CB HIS A 310 3623 3424 4879 258 -359 28 C ATOM 2304 CG HIS A 310 22.822 -15.012 24.001 1.00 33.28 C ANISOU 2304 CG HIS A 310 3750 3614 5281 328 -420 41 C ATOM 2305 ND1 HIS A 310 23.900 -14.703 23.201 1.00 34.92 N ANISOU 2305 ND1 HIS A 310 3860 3847 5561 365 -357 -75 N ATOM 2306 CD2 HIS A 310 23.328 -15.671 25.072 1.00 38.76 C ANISOU 2306 CD2 HIS A 310 4405 4245 6076 367 -542 167 C ATOM 2307 CE1 HIS A 310 25.003 -15.185 23.745 1.00 35.90 C ANISOU 2307 CE1 HIS A 310 3878 3919 5842 430 -437 -34 C ATOM 2308 NE2 HIS A 310 24.684 -15.768 24.887 1.00 32.62 N ANISOU 2308 NE2 HIS A 310 3499 3449 5445 435 -559 120 N ATOM 2309 N LEU A 311 18.654 -12.818 23.998 1.00 30.78 N ANISOU 2309 N LEU A 311 3754 3530 4411 105 -290 90 N ATOM 2310 CA LEU A 311 17.525 -12.071 23.458 1.00 28.21 C ANISOU 2310 CA LEU A 311 3487 3271 3960 60 -225 57 C ATOM 2311 C LEU A 311 17.621 -10.622 23.902 1.00 28.08 C ANISOU 2311 C LEU A 311 3489 3351 3829 35 -214 70 C ATOM 2312 O LEU A 311 17.496 -9.718 23.083 1.00 26.44 O ANISOU 2312 O LEU A 311 3288 3190 3566 21 -152 13 O ATOM 2313 CB LEU A 311 16.191 -12.668 23.907 1.00 27.43 C ANISOU 2313 CB LEU A 311 3442 3149 3831 23 -242 122 C ATOM 2314 CG LEU A 311 14.912 -11.987 23.410 1.00 27.84 C ANISOU 2314 CG LEU A 311 3537 3268 3773 -18 -186 96 C ATOM 2315 CD1 LEU A 311 14.933 -11.731 21.898 1.00 28.34 C ANISOU 2315 CD1 LEU A 311 3587 3350 3830 -13 -125 -13 C ATOM 2316 CD2 LEU A 311 13.683 -12.814 23.808 1.00 22.61 C ANISOU 2316 CD2 LEU A 311 2904 2573 3116 -57 -202 154 C ATOM 2317 N LEU A 312 17.852 -10.413 25.199 1.00 28.59 N ANISOU 2317 N LEU A 312 3562 3443 3860 24 -278 147 N ATOM 2318 CA LEU A 312 17.908 -9.075 25.769 1.00 28.09 C ANISOU 2318 CA LEU A 312 3519 3460 3694 -6 -272 143 C ATOM 2319 C LEU A 312 18.947 -8.229 25.045 1.00 30.55 C ANISOU 2319 C LEU A 312 3782 3787 4037 2 -237 70 C ATOM 2320 O LEU A 312 18.728 -7.043 24.789 1.00 27.54 O ANISOU 2320 O LEU A 312 3423 3445 3595 -24 -191 37 O ATOM 2321 CB LEU A 312 18.252 -9.131 27.253 1.00 28.85 C ANISOU 2321 CB LEU A 312 3621 3594 3748 -24 -356 220 C ATOM 2322 CG LEU A 312 18.464 -7.774 27.945 1.00 27.60 C ANISOU 2322 CG LEU A 312 3478 3516 3491 -60 -357 189 C ATOM 2323 CD1 LEU A 312 17.181 -6.977 27.959 1.00 27.25 C ANISOU 2323 CD1 LEU A 312 3496 3508 3351 -89 -288 162 C ATOM 2324 CD2 LEU A 312 18.992 -7.978 29.351 1.00 29.02 C ANISOU 2324 CD2 LEU A 312 3655 3749 3620 -82 -456 257 C ATOM 2325 N GLN A 313 20.075 -8.859 24.728 1.00 31.78 N ANISOU 2325 N GLN A 313 3865 3905 4303 38 -258 51 N ATOM 2326 CA GLN A 313 21.180 -8.189 24.079 1.00 33.70 C ANISOU 2326 CA GLN A 313 4043 4170 4591 40 -221 -14 C ATOM 2327 C GLN A 313 20.825 -7.775 22.653 1.00 32.64 C ANISOU 2327 C GLN A 313 3923 4048 4429 28 -117 -79 C ATOM 2328 O GLN A 313 21.258 -6.728 22.192 1.00 33.78 O ANISOU 2328 O GLN A 313 4054 4232 4550 -1 -70 -107 O ATOM 2329 CB GLN A 313 22.411 -9.086 24.083 1.00 35.72 C ANISOU 2329 CB GLN A 313 4200 4385 4988 90 -262 -23 C ATOM 2330 CG GLN A 313 23.690 -8.333 23.830 1.00 41.26 C ANISOU 2330 CG GLN A 313 4814 5125 5738 81 -244 -72 C ATOM 2331 CD GLN A 313 24.910 -9.203 23.991 1.00 44.35 C ANISOU 2331 CD GLN A 313 5087 5480 6285 139 -297 -76 C ATOM 2332 OE1 GLN A 313 24.932 -10.344 23.533 1.00 44.23 O ANISOU 2332 OE1 GLN A 313 5040 5393 6372 197 -287 -98 O ATOM 2333 NE2 GLN A 313 25.944 -8.664 24.643 1.00 45.92 N ANISOU 2333 NE2 GLN A 313 5209 5721 6517 126 -358 -63 N ATOM 2334 N LYS A 314 20.028 -8.587 21.963 1.00 31.59 N ANISOU 2334 N LYS A 314 3819 3887 4296 42 -88 -98 N ATOM 2335 CA LYS A 314 19.578 -8.239 20.620 1.00 31.46 C ANISOU 2335 CA LYS A 314 3823 3905 4225 22 -4 -152 C ATOM 2336 C LYS A 314 18.536 -7.103 20.646 1.00 31.62 C ANISOU 2336 C LYS A 314 3912 3967 4134 -15 10 -110 C ATOM 2337 O LYS A 314 18.401 -6.374 19.671 1.00 34.04 O ANISOU 2337 O LYS A 314 4230 4314 4388 -39 67 -125 O ATOM 2338 CB LYS A 314 19.034 -9.469 19.906 1.00 31.08 C ANISOU 2338 CB LYS A 314 3781 3818 4209 40 11 -200 C ATOM 2339 CG LYS A 314 20.100 -10.485 19.571 1.00 32.21 C ANISOU 2339 CG LYS A 314 3846 3909 4482 85 22 -271 C ATOM 2340 CD LYS A 314 19.519 -11.852 19.217 1.00 33.57 C ANISOU 2340 CD LYS A 314 4028 4005 4721 105 16 -319 C ATOM 2341 CE LYS A 314 20.653 -12.854 19.007 1.00 31.66 C ANISOU 2341 CE LYS A 314 3696 3686 4646 165 24 -396 C ATOM 2342 NZ LYS A 314 20.203 -14.248 18.741 1.00 30.41 N ANISOU 2342 NZ LYS A 314 3541 3419 4593 189 13 -452 N ATOM 2343 N LEU A 315 17.829 -6.942 21.763 1.00 30.57 N ANISOU 2343 N LEU A 315 3820 3827 3969 -21 -38 -54 N ATOM 2344 CA LEU A 315 16.885 -5.835 21.947 1.00 29.03 C ANISOU 2344 CA LEU A 315 3675 3660 3697 -44 -23 -26 C ATOM 2345 C LEU A 315 17.583 -4.534 22.363 1.00 29.85 C ANISOU 2345 C LEU A 315 3772 3774 3797 -64 -18 -29 C ATOM 2346 O LEU A 315 17.275 -3.449 21.839 1.00 32.06 O ANISOU 2346 O LEU A 315 4071 4059 4052 -81 22 -25 O ATOM 2347 CB LEU A 315 15.833 -6.207 22.997 1.00 29.85 C ANISOU 2347 CB LEU A 315 3816 3761 3766 -45 -59 16 C ATOM 2348 CG LEU A 315 14.919 -7.399 22.700 1.00 28.89 C ANISOU 2348 CG LEU A 315 3704 3620 3653 -41 -66 28 C ATOM 2349 CD1 LEU A 315 14.149 -7.782 23.966 1.00 32.26 C ANISOU 2349 CD1 LEU A 315 4155 4050 4051 -55 -99 86 C ATOM 2350 CD2 LEU A 315 13.944 -7.109 21.554 1.00 28.14 C ANISOU 2350 CD2 LEU A 315 3622 3549 3519 -50 -26 10 C ATOM 2351 N LEU A 316 18.508 -4.632 23.311 1.00 29.48 N ANISOU 2351 N LEU A 316 3694 3725 3783 -66 -65 -32 N ATOM 2352 CA LEU A 316 19.294 -3.469 23.749 1.00 31.48 C ANISOU 2352 CA LEU A 316 3930 3985 4045 -98 -70 -52 C ATOM 2353 C LEU A 316 20.572 -3.326 22.929 1.00 31.27 C ANISOU 2353 C LEU A 316 3834 3960 4087 -108 -40 -80 C ATOM 2354 O LEU A 316 21.685 -3.427 23.445 1.00 34.39 O ANISOU 2354 O LEU A 316 4166 4362 4537 -113 -81 -95 O ATOM 2355 CB LEU A 316 19.619 -3.561 25.244 1.00 31.11 C ANISOU 2355 CB LEU A 316 3881 3959 3981 -108 -147 -44 C ATOM 2356 CG LEU A 316 18.410 -3.568 26.181 1.00 31.95 C ANISOU 2356 CG LEU A 316 4052 4086 4002 -113 -161 -23 C ATOM 2357 CD1 LEU A 316 18.877 -3.756 27.623 1.00 29.69 C ANISOU 2357 CD1 LEU A 316 3763 3846 3671 -135 -240 -11 C ATOM 2358 CD2 LEU A 316 17.595 -2.284 26.029 1.00 28.88 C ANISOU 2358 CD2 LEU A 316 3704 3686 3582 -128 -103 -56 C ATOM 2359 N THR A 317 20.392 -3.098 21.638 1.00 31.28 N ANISOU 2359 N THR A 317 3839 3966 4079 -114 32 -84 N ATOM 2360 CA THR A 317 21.485 -2.762 20.746 1.00 31.15 C ANISOU 2360 CA THR A 317 3761 3967 4105 -139 87 -108 C ATOM 2361 C THR A 317 21.444 -1.255 20.552 1.00 29.76 C ANISOU 2361 C THR A 317 3611 3778 3917 -192 120 -82 C ATOM 2362 O THR A 317 20.381 -0.674 20.321 1.00 29.48 O ANISOU 2362 O THR A 317 3643 3727 3833 -193 133 -45 O ATOM 2363 CB THR A 317 21.347 -3.500 19.400 1.00 32.19 C ANISOU 2363 CB THR A 317 3885 4131 4217 -125 151 -129 C ATOM 2364 OG1 THR A 317 21.548 -4.906 19.614 1.00 32.94 O ANISOU 2364 OG1 THR A 317 3944 4210 4362 -76 121 -167 O ATOM 2365 CG2 THR A 317 22.366 -3.006 18.398 1.00 33.29 C ANISOU 2365 CG2 THR A 317 3966 4311 4373 -166 231 -149 C ATOM 2366 N MET A 318 22.607 -0.628 20.660 1.00 30.94 N ANISOU 2366 N MET A 318 3701 3928 4129 -235 130 -100 N ATOM 2367 CA MET A 318 22.719 0.830 20.613 1.00 30.47 C ANISOU 2367 CA MET A 318 3659 3830 4089 -294 155 -78 C ATOM 2368 C MET A 318 22.347 1.379 19.243 1.00 28.59 C ANISOU 2368 C MET A 318 3451 3598 3814 -321 233 -18 C ATOM 2369 O MET A 318 21.600 2.346 19.135 1.00 31.04 O ANISOU 2369 O MET A 318 3820 3858 4115 -335 239 32 O ATOM 2370 CB MET A 318 24.142 1.248 20.951 1.00 33.48 C ANISOU 2370 CB MET A 318 3951 4214 4554 -347 148 -112 C ATOM 2371 CG MET A 318 24.609 0.795 22.325 1.00 41.90 C ANISOU 2371 CG MET A 318 4981 5290 5649 -331 51 -159 C ATOM 2372 SD MET A 318 24.086 1.932 23.606 1.00 48.66 S ANISOU 2372 SD MET A 318 5904 6096 6487 -367 -7 -187 S ATOM 2373 CE MET A 318 25.399 3.119 23.505 1.00 43.53 C ANISOU 2373 CE MET A 318 5179 5419 5943 -465 11 -218 C ATOM 2374 N ASP A 319 22.871 0.767 18.192 1.00 29.00 N ANISOU 2374 N ASP A 319 3458 3715 3845 -327 293 -23 N ATOM 2375 CA ASP A 319 22.527 1.183 16.846 1.00 28.71 C ANISOU 2375 CA ASP A 319 3453 3716 3740 -361 365 40 C ATOM 2376 C ASP A 319 21.132 0.681 16.520 1.00 28.53 C ANISOU 2376 C ASP A 319 3505 3708 3629 -312 340 65 C ATOM 2377 O ASP A 319 20.899 -0.525 16.539 1.00 28.38 O ANISOU 2377 O ASP A 319 3477 3721 3585 -266 324 9 O ATOM 2378 CB ASP A 319 23.518 0.627 15.834 1.00 29.37 C ANISOU 2378 CB ASP A 319 3463 3888 3807 -389 448 6 C ATOM 2379 CG ASP A 319 23.358 1.247 14.471 1.00 31.43 C ANISOU 2379 CG ASP A 319 3754 4209 3978 -450 528 85 C ATOM 2380 OD1 ASP A 319 22.308 1.882 14.228 1.00 27.71 O ANISOU 2380 OD1 ASP A 319 3365 3710 3454 -452 501 173 O ATOM 2381 OD2 ASP A 319 24.289 1.120 13.650 1.00 30.33 O ANISOU 2381 OD2 ASP A 319 3550 4150 3822 -498 617 64 O ATOM 2382 N PRO A 320 20.201 1.595 16.200 1.00 29.53 N ANISOU 2382 N PRO A 320 3695 3803 3724 -322 332 150 N ATOM 2383 CA PRO A 320 18.840 1.123 15.954 1.00 29.91 C ANISOU 2383 CA PRO A 320 3795 3870 3699 -276 298 172 C ATOM 2384 C PRO A 320 18.657 0.221 14.728 1.00 29.44 C ANISOU 2384 C PRO A 320 3736 3916 3534 -281 331 160 C ATOM 2385 O PRO A 320 17.724 -0.575 14.718 1.00 29.06 O ANISOU 2385 O PRO A 320 3712 3888 3444 -243 294 136 O ATOM 2386 CB PRO A 320 18.033 2.420 15.814 1.00 28.11 C ANISOU 2386 CB PRO A 320 3615 3580 3485 -283 282 274 C ATOM 2387 CG PRO A 320 19.036 3.483 15.552 1.00 31.70 C ANISOU 2387 CG PRO A 320 4050 3998 3996 -350 326 321 C ATOM 2388 CD PRO A 320 20.256 3.063 16.280 1.00 30.70 C ANISOU 2388 CD PRO A 320 3862 3873 3928 -366 338 225 C ATOM 2389 N ILE A 321 19.513 0.332 13.712 1.00 31.42 N ANISOU 2389 N ILE A 321 3959 4240 3740 -336 404 168 N ATOM 2390 CA ILE A 321 19.389 -0.557 12.544 1.00 32.55 C ANISOU 2390 CA ILE A 321 4102 4499 3767 -349 446 127 C ATOM 2391 C ILE A 321 19.926 -1.955 12.867 1.00 32.45 C ANISOU 2391 C ILE A 321 4037 4494 3798 -308 457 -15 C ATOM 2392 O ILE A 321 19.693 -2.902 12.123 1.00 33.49 O ANISOU 2392 O ILE A 321 4170 4696 3860 -304 480 -87 O ATOM 2393 CB ILE A 321 20.065 0.007 11.260 1.00 35.39 C ANISOU 2393 CB ILE A 321 4452 4961 4035 -431 535 180 C ATOM 2394 CG1 ILE A 321 21.585 0.079 11.399 1.00 37.40 C ANISOU 2394 CG1 ILE A 321 4624 5220 4366 -465 613 126 C ATOM 2395 CG2 ILE A 321 19.493 1.385 10.904 1.00 37.52 C ANISOU 2395 CG2 ILE A 321 4776 5204 4275 -470 511 349 C ATOM 2396 CD1 ILE A 321 22.276 0.520 10.121 1.00 35.62 C ANISOU 2396 CD1 ILE A 321 4379 5114 4040 -556 720 171 C ATOM 2397 N LYS A 322 20.634 -2.086 13.986 1.00 30.59 N ANISOU 2397 N LYS A 322 3754 4182 3685 -279 434 -55 N ATOM 2398 CA LYS A 322 21.110 -3.389 14.419 1.00 30.31 C ANISOU 2398 CA LYS A 322 3666 4130 3721 -228 425 -164 C ATOM 2399 C LYS A 322 20.215 -4.021 15.482 1.00 27.53 C ANISOU 2399 C LYS A 322 3350 3703 3408 -172 333 -164 C ATOM 2400 O LYS A 322 20.482 -5.127 15.920 1.00 27.35 O ANISOU 2400 O LYS A 322 3292 3646 3454 -129 310 -230 O ATOM 2401 CB LYS A 322 22.572 -3.306 14.881 1.00 29.55 C ANISOU 2401 CB LYS A 322 3476 4018 3735 -232 452 -203 C ATOM 2402 CG LYS A 322 23.521 -3.023 13.731 1.00 33.32 C ANISOU 2402 CG LYS A 322 3896 4587 4177 -289 566 -228 C ATOM 2403 CD LYS A 322 24.958 -2.834 14.189 1.00 32.63 C ANISOU 2403 CD LYS A 322 3697 4488 4213 -300 593 -262 C ATOM 2404 CE LYS A 322 25.890 -2.752 13.000 1.00 35.86 C ANISOU 2404 CE LYS A 322 4033 5004 4587 -356 725 -304 C ATOM 2405 NZ LYS A 322 27.270 -2.395 13.408 1.00 35.22 N ANISOU 2405 NZ LYS A 322 3830 4919 4634 -381 755 -324 N ATOM 2406 N ARG A 323 19.142 -3.342 15.876 1.00 28.80 N ANISOU 2406 N ARG A 323 3575 3835 3531 -173 285 -88 N ATOM 2407 CA ARG A 323 18.159 -3.940 16.788 1.00 28.54 C ANISOU 2407 CA ARG A 323 3575 3754 3516 -131 215 -85 C ATOM 2408 C ARG A 323 17.287 -4.955 16.066 1.00 28.73 C ANISOU 2408 C ARG A 323 3619 3809 3487 -123 211 -121 C ATOM 2409 O ARG A 323 16.846 -4.732 14.944 1.00 29.65 O ANISOU 2409 O ARG A 323 3758 3994 3515 -152 239 -111 O ATOM 2410 CB ARG A 323 17.244 -2.880 17.419 1.00 28.35 C ANISOU 2410 CB ARG A 323 3598 3696 3477 -132 179 -10 C ATOM 2411 CG ARG A 323 17.836 -2.210 18.604 1.00 28.13 C ANISOU 2411 CG ARG A 323 3557 3616 3513 -133 156 -5 C ATOM 2412 CD ARG A 323 17.009 -1.031 19.123 1.00 26.29 C ANISOU 2412 CD ARG A 323 3366 3343 3279 -134 139 43 C ATOM 2413 NE ARG A 323 17.942 0.029 19.486 1.00 27.93 N ANISOU 2413 NE ARG A 323 3557 3513 3541 -167 152 42 N ATOM 2414 CZ ARG A 323 17.700 1.332 19.430 1.00 28.54 C ANISOU 2414 CZ ARG A 323 3658 3541 3646 -187 164 82 C ATOM 2415 NH1 ARG A 323 16.510 1.797 19.067 1.00 30.97 N ANISOU 2415 NH1 ARG A 323 4003 3830 3934 -164 162 136 N ATOM 2416 NH2 ARG A 323 18.676 2.174 19.753 1.00 31.47 N ANISOU 2416 NH2 ARG A 323 4006 3870 4080 -229 175 68 N ATOM 2417 N ILE A 324 17.042 -6.065 16.744 1.00 30.19 N ANISOU 2417 N ILE A 324 3798 3946 3728 -90 170 -158 N ATOM 2418 CA ILE A 324 16.049 -7.056 16.345 1.00 33.57 C ANISOU 2418 CA ILE A 324 4246 4377 4131 -88 151 -192 C ATOM 2419 C ILE A 324 14.656 -6.404 16.164 1.00 31.97 C ANISOU 2419 C ILE A 324 4089 4209 3851 -105 123 -124 C ATOM 2420 O ILE A 324 14.322 -5.419 16.846 1.00 32.34 O ANISOU 2420 O ILE A 324 4151 4238 3899 -98 106 -52 O ATOM 2421 CB ILE A 324 15.993 -8.157 17.458 1.00 34.87 C ANISOU 2421 CB ILE A 324 4400 4457 4393 -56 100 -202 C ATOM 2422 CG1 ILE A 324 15.378 -9.445 16.976 1.00 39.72 C ANISOU 2422 CG1 ILE A 324 5016 5046 5028 -59 90 -265 C ATOM 2423 CG2 ILE A 324 15.233 -7.658 18.681 1.00 35.04 C ANISOU 2423 CG2 ILE A 324 4451 4455 4408 -52 52 -118 C ATOM 2424 CD1 ILE A 324 15.347 -10.511 18.067 1.00 41.10 C ANISOU 2424 CD1 ILE A 324 5182 5122 5312 -33 38 -248 C ATOM 2425 N THR A 325 13.847 -6.937 15.253 1.00 31.20 N ANISOU 2425 N THR A 325 4003 4160 3693 -126 117 -154 N ATOM 2426 CA THR A 325 12.445 -6.510 15.150 1.00 32.21 C ANISOU 2426 CA THR A 325 4151 4317 3768 -135 75 -91 C ATOM 2427 C THR A 325 11.571 -7.302 16.128 1.00 31.72 C ANISOU 2427 C THR A 325 4085 4198 3768 -123 32 -90 C ATOM 2428 O THR A 325 11.990 -8.321 16.684 1.00 28.27 O ANISOU 2428 O THR A 325 3639 3700 3403 -114 28 -135 O ATOM 2429 CB THR A 325 11.871 -6.691 13.726 1.00 35.31 C ANISOU 2429 CB THR A 325 4552 4808 4055 -174 71 -115 C ATOM 2430 OG1 THR A 325 11.755 -8.090 13.426 1.00 32.10 O ANISOU 2430 OG1 THR A 325 4136 4394 3666 -191 67 -225 O ATOM 2431 CG2 THR A 325 12.761 -5.997 12.670 1.00 32.68 C ANISOU 2431 CG2 THR A 325 4226 4554 3636 -202 125 -108 C ATOM 2432 N SER A 326 10.347 -6.829 16.328 1.00 31.52 N ANISOU 2432 N SER A 326 4061 4192 3722 -122 0 -30 N ATOM 2433 CA SER A 326 9.420 -7.496 17.233 1.00 31.29 C ANISOU 2433 CA SER A 326 4020 4127 3742 -123 -28 -20 C ATOM 2434 C SER A 326 9.126 -8.920 16.767 1.00 31.99 C ANISOU 2434 C SER A 326 4099 4203 3851 -157 -46 -91 C ATOM 2435 O SER A 326 9.052 -9.833 17.582 1.00 34.40 O ANISOU 2435 O SER A 326 4400 4442 4229 -162 -57 -96 O ATOM 2436 CB SER A 326 8.118 -6.702 17.368 1.00 30.15 C ANISOU 2436 CB SER A 326 3857 4018 3579 -115 -49 45 C ATOM 2437 OG SER A 326 7.443 -6.613 16.124 1.00 38.08 O ANISOU 2437 OG SER A 326 4849 5096 4523 -137 -79 47 O ATOM 2438 N GLU A 327 8.969 -9.107 15.461 1.00 32.78 N ANISOU 2438 N GLU A 327 4199 4369 3887 -186 -52 -144 N ATOM 2439 CA GLU A 327 8.682 -10.427 14.912 1.00 34.20 C ANISOU 2439 CA GLU A 327 4370 4535 4089 -226 -68 -239 C ATOM 2440 C GLU A 327 9.876 -11.376 15.040 1.00 34.16 C ANISOU 2440 C GLU A 327 4368 4446 4164 -212 -34 -324 C ATOM 2441 O GLU A 327 9.702 -12.544 15.369 1.00 31.69 O ANISOU 2441 O GLU A 327 4048 4048 3946 -226 -51 -369 O ATOM 2442 CB GLU A 327 8.192 -10.343 13.459 1.00 36.45 C ANISOU 2442 CB GLU A 327 4655 4935 4261 -270 -87 -287 C ATOM 2443 CG GLU A 327 9.106 -9.619 12.462 1.00 47.09 C ANISOU 2443 CG GLU A 327 6023 6366 5503 -270 -46 -301 C ATOM 2444 CD GLU A 327 8.806 -8.121 12.290 1.00 53.54 C ANISOU 2444 CD GLU A 327 6847 7252 6246 -254 -61 -170 C ATOM 2445 OE1 GLU A 327 9.145 -7.582 11.208 1.00 54.94 O ANISOU 2445 OE1 GLU A 327 7040 7527 6308 -279 -47 -160 O ATOM 2446 OE2 GLU A 327 8.249 -7.488 13.224 1.00 48.78 O ANISOU 2446 OE2 GLU A 327 6231 6601 5701 -219 -82 -79 O ATOM 2447 N GLN A 328 11.082 -10.876 14.782 1.00 32.16 N ANISOU 2447 N GLN A 328 4119 4209 3892 -185 11 -341 N ATOM 2448 CA GLN A 328 12.301 -11.664 14.969 1.00 33.57 C ANISOU 2448 CA GLN A 328 4279 4307 4168 -156 44 -416 C ATOM 2449 C GLN A 328 12.419 -12.103 16.432 1.00 31.97 C ANISOU 2449 C GLN A 328 4070 3991 4084 -125 10 -346 C ATOM 2450 O GLN A 328 12.774 -13.242 16.720 1.00 32.15 O ANISOU 2450 O GLN A 328 4079 3915 4224 -112 -1 -390 O ATOM 2451 CB GLN A 328 13.534 -10.845 14.553 1.00 34.22 C ANISOU 2451 CB GLN A 328 4351 4442 4209 -136 101 -426 C ATOM 2452 CG GLN A 328 13.626 -10.625 13.038 1.00 37.61 C ANISOU 2452 CG GLN A 328 4787 4991 4514 -177 148 -502 C ATOM 2453 CD GLN A 328 14.696 -9.612 12.594 1.00 39.25 C ANISOU 2453 CD GLN A 328 4983 5269 4660 -176 212 -479 C ATOM 2454 OE1 GLN A 328 15.284 -8.864 13.383 1.00 30.09 O ANISOU 2454 OE1 GLN A 328 3813 4072 3547 -149 214 -400 O ATOM 2455 NE2 GLN A 328 14.927 -9.585 11.307 1.00 43.64 N ANISOU 2455 NE2 GLN A 328 5542 5936 5104 -217 265 -551 N ATOM 2456 N ALA A 329 12.103 -11.190 17.347 1.00 31.07 N ANISOU 2456 N ALA A 329 3970 3896 3939 -115 -8 -236 N ATOM 2457 CA ALA A 329 12.173 -11.472 18.776 1.00 30.27 C ANISOU 2457 CA ALA A 329 3869 3724 3908 -99 -40 -160 C ATOM 2458 C ALA A 329 11.186 -12.581 19.183 1.00 30.41 C ANISOU 2458 C ALA A 329 3890 3681 3985 -131 -75 -142 C ATOM 2459 O ALA A 329 11.546 -13.466 19.961 1.00 28.63 O ANISOU 2459 O ALA A 329 3660 3364 3856 -122 -101 -112 O ATOM 2460 CB ALA A 329 11.941 -10.198 19.584 1.00 27.51 C ANISOU 2460 CB ALA A 329 3534 3424 3494 -91 -41 -75 C ATOM 2461 N MET A 330 9.974 -12.570 18.625 1.00 29.87 N ANISOU 2461 N MET A 330 3822 3661 3868 -172 -80 -155 N ATOM 2462 CA MET A 330 8.983 -13.626 18.934 1.00 31.51 C ANISOU 2462 CA MET A 330 4022 3812 4140 -218 -109 -142 C ATOM 2463 C MET A 330 9.445 -15.003 18.481 1.00 32.46 C ANISOU 2463 C MET A 330 4135 3822 4375 -228 -117 -231 C ATOM 2464 O MET A 330 9.057 -16.018 19.072 1.00 31.57 O ANISOU 2464 O MET A 330 4019 3611 4364 -258 -144 -197 O ATOM 2465 CB MET A 330 7.626 -13.319 18.301 1.00 31.77 C ANISOU 2465 CB MET A 330 4038 3929 4106 -263 -119 -151 C ATOM 2466 CG MET A 330 6.929 -12.113 18.914 1.00 33.34 C ANISOU 2466 CG MET A 330 4228 4207 4233 -250 -111 -61 C ATOM 2467 SD MET A 330 5.448 -11.626 18.011 1.00 39.54 S ANISOU 2467 SD MET A 330 4972 5098 4955 -283 -135 -67 S ATOM 2468 CE MET A 330 4.358 -12.993 18.392 1.00 38.14 C ANISOU 2468 CE MET A 330 4759 4868 4867 -359 -160 -70 C ATOM 2469 N GLN A 331 10.271 -15.032 17.437 1.00 31.45 N ANISOU 2469 N GLN A 331 4002 3708 4238 -206 -89 -345 N ATOM 2470 CA GLN A 331 10.814 -16.289 16.907 1.00 33.02 C ANISOU 2470 CA GLN A 331 4188 3799 4560 -203 -83 -465 C ATOM 2471 C GLN A 331 12.056 -16.781 17.667 1.00 29.78 C ANISOU 2471 C GLN A 331 3759 3270 4284 -139 -87 -437 C ATOM 2472 O GLN A 331 12.566 -17.861 17.378 1.00 29.19 O ANISOU 2472 O GLN A 331 3665 3077 4351 -122 -84 -528 O ATOM 2473 CB GLN A 331 11.164 -16.129 15.419 1.00 35.43 C ANISOU 2473 CB GLN A 331 4488 4190 4784 -211 -38 -618 C ATOM 2474 CG GLN A 331 9.975 -15.849 14.497 1.00 40.28 C ANISOU 2474 CG GLN A 331 5113 4922 5271 -280 -54 -657 C ATOM 2475 CD GLN A 331 8.949 -16.971 14.495 1.00 46.66 C ANISOU 2475 CD GLN A 331 5913 5651 6164 -343 -97 -701 C ATOM 2476 OE1 GLN A 331 9.267 -18.122 14.182 1.00 53.27 O ANISOU 2476 OE1 GLN A 331 6743 6377 7122 -353 -90 -824 O ATOM 2477 NE2 GLN A 331 7.708 -16.641 14.852 1.00 54.26 N ANISOU 2477 NE2 GLN A 331 6869 6665 7082 -387 -139 -608 N ATOM 2478 N ASP A 332 12.537 -16.002 18.633 1.00 28.32 N ANISOU 2478 N ASP A 332 3578 3115 4066 -104 -98 -319 N ATOM 2479 CA ASP A 332 13.753 -16.345 19.386 1.00 28.82 C ANISOU 2479 CA ASP A 332 3615 3092 4244 -44 -119 -278 C ATOM 2480 C ASP A 332 13.593 -17.683 20.126 1.00 30.33 C ANISOU 2480 C ASP A 332 3803 3122 4599 -46 -173 -219 C ATOM 2481 O ASP A 332 12.510 -17.975 20.641 1.00 29.98 O ANISOU 2481 O ASP A 332 3787 3063 4543 -103 -200 -139 O ATOM 2482 CB ASP A 332 14.094 -15.233 20.385 1.00 27.97 C ANISOU 2482 CB ASP A 332 3517 3062 4049 -27 -135 -159 C ATOM 2483 CG ASP A 332 15.493 -15.370 20.962 1.00 33.99 C ANISOU 2483 CG ASP A 332 4237 3772 4905 35 -162 -133 C ATOM 2484 OD1 ASP A 332 16.420 -14.702 20.445 1.00 30.72 O ANISOU 2484 OD1 ASP A 332 3790 3414 4467 64 -123 -196 O ATOM 2485 OD2 ASP A 332 15.672 -16.158 21.920 1.00 34.55 O ANISOU 2485 OD2 ASP A 332 4302 3748 5077 49 -225 -41 O ATOM 2486 N PRO A 333 14.663 -18.504 20.163 1.00 31.07 N ANISOU 2486 N PRO A 333 3855 3091 4860 14 -188 -254 N ATOM 2487 CA PRO A 333 14.588 -19.812 20.831 1.00 32.89 C ANISOU 2487 CA PRO A 333 4080 3142 5277 18 -248 -183 C ATOM 2488 C PRO A 333 14.334 -19.731 22.345 1.00 34.22 C ANISOU 2488 C PRO A 333 4276 3310 5418 -2 -318 33 C ATOM 2489 O PRO A 333 13.932 -20.728 22.958 1.00 35.24 O ANISOU 2489 O PRO A 333 4416 3310 5663 -28 -368 132 O ATOM 2490 CB PRO A 333 15.947 -20.454 20.522 1.00 32.33 C ANISOU 2490 CB PRO A 333 3942 2954 5389 108 -247 -268 C ATOM 2491 CG PRO A 333 16.835 -19.339 20.115 1.00 33.80 C ANISOU 2491 CG PRO A 333 4097 3282 5465 148 -197 -329 C ATOM 2492 CD PRO A 333 15.952 -18.326 19.467 1.00 30.76 C ANISOU 2492 CD PRO A 333 3760 3062 4864 81 -144 -372 C ATOM 2493 N TYR A 334 14.540 -18.551 22.926 1.00 32.57 N ANISOU 2493 N TYR A 334 4079 3245 5052 2 -319 104 N ATOM 2494 CA TYR A 334 14.115 -18.268 24.290 1.00 31.35 C ANISOU 2494 CA TYR A 334 3960 3142 4810 -35 -367 281 C ATOM 2495 C TYR A 334 12.660 -18.693 24.549 1.00 31.99 C ANISOU 2495 C TYR A 334 4079 3215 4860 -122 -359 343 C ATOM 2496 O TYR A 334 12.356 -19.226 25.612 1.00 35.61 O ANISOU 2496 O TYR A 334 4558 3634 5338 -159 -405 497 O ATOM 2497 CB TYR A 334 14.289 -16.781 24.580 1.00 31.39 C ANISOU 2497 CB TYR A 334 3977 3317 4633 -33 -342 285 C ATOM 2498 CG TYR A 334 13.791 -16.326 25.933 1.00 32.09 C ANISOU 2498 CG TYR A 334 4104 3491 4597 -79 -372 430 C ATOM 2499 CD1 TYR A 334 14.269 -16.904 27.109 1.00 35.53 C ANISOU 2499 CD1 TYR A 334 4542 3886 5071 -77 -452 576 C ATOM 2500 CD2 TYR A 334 12.857 -15.303 26.036 1.00 31.40 C ANISOU 2500 CD2 TYR A 334 4047 3532 4352 -122 -320 418 C ATOM 2501 CE1 TYR A 334 13.822 -16.480 28.352 1.00 34.46 C ANISOU 2501 CE1 TYR A 334 4445 3855 4791 -130 -472 699 C ATOM 2502 CE2 TYR A 334 12.407 -14.871 27.269 1.00 35.32 C ANISOU 2502 CE2 TYR A 334 4574 4118 4729 -164 -330 523 C ATOM 2503 CZ TYR A 334 12.894 -15.458 28.424 1.00 32.58 C ANISOU 2503 CZ TYR A 334 4236 3748 4394 -174 -403 659 C ATOM 2504 OH TYR A 334 12.439 -15.015 29.642 1.00 37.78 O ANISOU 2504 OH TYR A 334 4929 4521 4905 -227 -405 753 O ATOM 2505 N PHE A 335 11.784 -18.487 23.569 1.00 28.86 N ANISOU 2505 N PHE A 335 3687 2862 4416 -159 -303 230 N ATOM 2506 CA PHE A 335 10.361 -18.800 23.714 1.00 27.64 C ANISOU 2506 CA PHE A 335 3550 2717 4235 -246 -292 273 C ATOM 2507 C PHE A 335 10.035 -20.265 23.429 1.00 29.84 C ANISOU 2507 C PHE A 335 3819 2819 4698 -283 -317 259 C ATOM 2508 O PHE A 335 8.908 -20.689 23.626 1.00 29.41 O ANISOU 2508 O PHE A 335 3771 2752 4652 -366 -313 307 O ATOM 2509 CB PHE A 335 9.515 -17.863 22.842 1.00 25.14 C ANISOU 2509 CB PHE A 335 3230 2536 3786 -271 -238 173 C ATOM 2510 CG PHE A 335 9.624 -16.410 23.243 1.00 27.98 C ANISOU 2510 CG PHE A 335 3600 3046 3985 -245 -213 203 C ATOM 2511 CD1 PHE A 335 9.173 -15.987 24.490 1.00 27.58 C ANISOU 2511 CD1 PHE A 335 3565 3062 3851 -273 -214 326 C ATOM 2512 CD2 PHE A 335 10.202 -15.469 22.393 1.00 30.47 C ANISOU 2512 CD2 PHE A 335 3909 3433 4234 -198 -184 106 C ATOM 2513 CE1 PHE A 335 9.279 -14.656 24.877 1.00 31.14 C ANISOU 2513 CE1 PHE A 335 4025 3635 4170 -249 -187 331 C ATOM 2514 CE2 PHE A 335 10.314 -14.127 22.777 1.00 28.32 C ANISOU 2514 CE2 PHE A 335 3647 3273 3841 -177 -163 134 C ATOM 2515 CZ PHE A 335 9.860 -13.723 24.018 1.00 31.47 C ANISOU 2515 CZ PHE A 335 4061 3723 4173 -199 -166 235 C ATOM 2516 N LEU A 336 11.024 -21.033 22.975 1.00 33.54 N ANISOU 2516 N LEU A 336 4267 3146 5330 -224 -337 187 N ATOM 2517 CA LEU A 336 10.869 -22.476 22.771 1.00 34.64 C ANISOU 2517 CA LEU A 336 4397 3080 5687 -248 -365 167 C ATOM 2518 C LEU A 336 11.469 -23.284 23.922 1.00 34.76 C ANISOU 2518 C LEU A 336 4413 2948 5847 -223 -438 350 C ATOM 2519 O LEU A 336 11.220 -24.478 24.039 1.00 37.01 O ANISOU 2519 O LEU A 336 4696 3045 6321 -256 -472 392 O ATOM 2520 CB LEU A 336 11.532 -22.897 21.460 1.00 35.00 C ANISOU 2520 CB LEU A 336 4411 3045 5844 -196 -334 -54 C ATOM 2521 CG LEU A 336 10.951 -22.321 20.160 1.00 37.37 C ANISOU 2521 CG LEU A 336 4710 3477 6010 -231 -273 -240 C ATOM 2522 CD1 LEU A 336 11.595 -23.017 18.969 1.00 37.45 C ANISOU 2522 CD1 LEU A 336 4692 3390 6148 -194 -241 -461 C ATOM 2523 CD2 LEU A 336 9.442 -22.473 20.103 1.00 34.70 C ANISOU 2523 CD2 LEU A 336 4388 3174 5621 -342 -277 -220 C ATOM 2524 N GLU A 337 12.266 -22.618 24.747 1.00 34.70 N ANISOU 2524 N GLU A 337 4405 3025 5753 -170 -470 460 N ATOM 2525 CA GLU A 337 12.939 -23.221 25.885 1.00 36.99 C ANISOU 2525 CA GLU A 337 4693 3216 6145 -141 -556 653 C ATOM 2526 C GLU A 337 11.934 -23.348 27.013 1.00 37.25 C ANISOU 2526 C GLU A 337 4774 3295 6085 -243 -577 857 C ATOM 2527 O GLU A 337 11.099 -22.463 27.207 1.00 36.66 O ANISOU 2527 O GLU A 337 4724 3398 5806 -304 -524 859 O ATOM 2528 CB GLU A 337 14.091 -22.311 26.328 1.00 37.14 C ANISOU 2528 CB GLU A 337 4692 3352 6068 -62 -584 680 C ATOM 2529 CG GLU A 337 15.022 -22.871 27.397 1.00 37.07 C ANISOU 2529 CG GLU A 337 4664 3257 6165 -13 -694 867 C ATOM 2530 CD GLU A 337 16.084 -21.858 27.839 1.00 38.36 C ANISOU 2530 CD GLU A 337 4800 3565 6211 47 -726 880 C ATOM 2531 OE1 GLU A 337 15.719 -20.711 28.178 1.00 34.30 O ANISOU 2531 OE1 GLU A 337 4320 3245 5465 3 -690 880 O ATOM 2532 OE2 GLU A 337 17.285 -22.208 27.851 1.00 38.76 O ANISOU 2532 OE2 GLU A 337 4785 3529 6414 139 -787 885 O ATOM 2533 N ASP A 338 12.010 -24.445 27.752 1.00 40.30 N ANISOU 2533 N ASP A 338 5167 3520 6626 -264 -649 1032 N ATOM 2534 CA ASP A 338 11.181 -24.621 28.941 1.00 43.68 C ANISOU 2534 CA ASP A 338 5639 4001 6957 -369 -669 1257 C ATOM 2535 C ASP A 338 11.475 -23.484 29.937 1.00 42.91 C ANISOU 2535 C ASP A 338 5565 4134 6605 -365 -679 1354 C ATOM 2536 O ASP A 338 12.638 -23.173 30.176 1.00 43.99 O ANISOU 2536 O ASP A 338 5683 4290 6741 -279 -738 1366 O ATOM 2537 CB ASP A 338 11.469 -25.977 29.588 1.00 46.02 C ANISOU 2537 CB ASP A 338 5938 4074 7474 -379 -763 1456 C ATOM 2538 CG ASP A 338 10.595 -26.241 30.795 1.00 51.45 C ANISOU 2538 CG ASP A 338 6673 4820 8057 -505 -776 1706 C ATOM 2539 OD1 ASP A 338 11.136 -26.250 31.920 1.00 61.76 O ANISOU 2539 OD1 ASP A 338 7999 6173 9292 -501 -855 1918 O ATOM 2540 OD2 ASP A 338 9.370 -26.428 30.623 1.00 54.87 O ANISOU 2540 OD2 ASP A 338 7117 5264 8468 -614 -707 1691 O ATOM 2541 N PRO A 339 10.431 -22.845 30.502 1.00 42.23 N ANISOU 2541 N PRO A 339 5511 4225 6308 -459 -619 1405 N ATOM 2542 CA PRO A 339 8.998 -23.026 30.278 1.00 42.11 C ANISOU 2542 CA PRO A 339 5501 4230 6270 -565 -541 1387 C ATOM 2543 C PRO A 339 8.476 -22.168 29.134 1.00 40.51 C ANISOU 2543 C PRO A 339 5273 4119 6000 -547 -457 1156 C ATOM 2544 O PRO A 339 8.949 -21.056 28.937 1.00 38.35 O ANISOU 2544 O PRO A 339 4996 3976 5598 -483 -435 1058 O ATOM 2545 CB PRO A 339 8.385 -22.558 31.597 1.00 42.55 C ANISOU 2545 CB PRO A 339 5590 4470 6107 -653 -518 1556 C ATOM 2546 CG PRO A 339 9.295 -21.475 32.044 1.00 42.26 C ANISOU 2546 CG PRO A 339 5565 4586 5906 -580 -540 1532 C ATOM 2547 CD PRO A 339 10.685 -21.865 31.575 1.00 41.63 C ANISOU 2547 CD PRO A 339 5463 4359 5997 -467 -628 1495 C ATOM 2548 N LEU A 340 7.500 -22.692 28.400 1.00 41.33 N ANISOU 2548 N LEU A 340 5356 4153 6194 -611 -418 1080 N ATOM 2549 CA LEU A 340 6.856 -21.961 27.326 1.00 41.48 C ANISOU 2549 CA LEU A 340 5346 4267 6145 -609 -353 887 C ATOM 2550 C LEU A 340 6.029 -20.803 27.870 1.00 39.86 C ANISOU 2550 C LEU A 340 5139 4283 5722 -645 -288 912 C ATOM 2551 O LEU A 340 5.508 -20.886 28.979 1.00 42.03 O ANISOU 2551 O LEU A 340 5426 4623 5922 -717 -272 1066 O ATOM 2552 CB LEU A 340 5.931 -22.886 26.539 1.00 43.13 C ANISOU 2552 CB LEU A 340 5528 4358 6501 -687 -342 817 C ATOM 2553 CG LEU A 340 6.552 -23.983 25.677 1.00 47.06 C ANISOU 2553 CG LEU A 340 6019 4630 7230 -653 -385 715 C ATOM 2554 CD1 LEU A 340 5.446 -24.704 24.922 1.00 43.56 C ANISOU 2554 CD1 LEU A 340 5547 4111 6894 -752 -368 623 C ATOM 2555 CD2 LEU A 340 7.564 -23.388 24.704 1.00 47.55 C ANISOU 2555 CD2 LEU A 340 6073 4722 7271 -539 -379 532 C ATOM 2556 N PRO A 341 5.890 -19.725 27.084 1.00 37.81 N ANISOU 2556 N PRO A 341 4860 4140 5366 -599 -246 761 N ATOM 2557 CA PRO A 341 5.022 -18.630 27.497 1.00 36.92 C ANISOU 2557 CA PRO A 341 4731 4213 5084 -624 -181 764 C ATOM 2558 C PRO A 341 3.569 -19.073 27.495 1.00 38.43 C ANISOU 2558 C PRO A 341 4878 4422 5302 -728 -140 790 C ATOM 2559 O PRO A 341 3.194 -19.926 26.689 1.00 38.02 O ANISOU 2559 O PRO A 341 4801 4258 5385 -768 -161 735 O ATOM 2560 CB PRO A 341 5.249 -17.581 26.407 1.00 35.93 C ANISOU 2560 CB PRO A 341 4591 4155 4907 -547 -163 600 C ATOM 2561 CG PRO A 341 5.603 -18.381 25.213 1.00 35.11 C ANISOU 2561 CG PRO A 341 4478 3918 4942 -531 -199 495 C ATOM 2562 CD PRO A 341 6.439 -19.496 25.734 1.00 37.59 C ANISOU 2562 CD PRO A 341 4819 4076 5387 -527 -252 582 C ATOM 2563 N THR A 342 2.769 -18.491 28.387 1.00 39.21 N ANISOU 2563 N THR A 342 4958 4665 5275 -774 -77 860 N ATOM 2564 CA THR A 342 1.361 -18.850 28.543 1.00 40.00 C ANISOU 2564 CA THR A 342 4998 4807 5394 -880 -25 898 C ATOM 2565 C THR A 342 0.459 -17.638 28.291 1.00 40.11 C ANISOU 2565 C THR A 342 4947 4985 5306 -858 43 804 C ATOM 2566 O THR A 342 0.868 -16.493 28.484 1.00 40.17 O ANISOU 2566 O THR A 342 4972 5089 5200 -779 66 757 O ATOM 2567 CB THR A 342 1.096 -19.411 29.956 1.00 42.13 C ANISOU 2567 CB THR A 342 5287 5102 5618 -974 3 1089 C ATOM 2568 OG1 THR A 342 1.554 -18.473 30.939 1.00 41.47 O ANISOU 2568 OG1 THR A 342 5240 5162 5354 -934 35 1128 O ATOM 2569 CG2 THR A 342 1.834 -20.737 30.152 1.00 41.12 C ANISOU 2569 CG2 THR A 342 5210 4782 5631 -1002 -77 1208 C ATOM 2570 N SER A 343 -0.770 -17.900 27.861 1.00 41.03 N ANISOU 2570 N SER A 343 4984 5125 5482 -928 70 776 N ATOM 2571 CA SER A 343 -1.725 -16.839 27.571 1.00 40.92 C ANISOU 2571 CA SER A 343 4886 5254 5407 -904 124 696 C ATOM 2572 C SER A 343 -2.137 -16.109 28.850 1.00 40.37 C ANISOU 2572 C SER A 343 4800 5333 5208 -915 221 758 C ATOM 2573 O SER A 343 -2.453 -14.924 28.815 1.00 39.19 O ANISOU 2573 O SER A 343 4609 5293 4990 -848 267 683 O ATOM 2574 CB SER A 343 -2.946 -17.387 26.822 1.00 41.75 C ANISOU 2574 CB SER A 343 4893 5352 5619 -984 117 657 C ATOM 2575 OG SER A 343 -3.464 -18.545 27.446 1.00 48.76 O ANISOU 2575 OG SER A 343 5764 6182 6582 -1113 136 768 O ATOM 2576 N ASP A 344 -2.112 -16.823 29.972 1.00 40.27 N ANISOU 2576 N ASP A 344 4818 5319 5163 -1001 251 896 N ATOM 2577 CA ASP A 344 -2.278 -16.230 31.298 1.00 40.74 C ANISOU 2577 CA ASP A 344 4884 5528 5066 -1021 342 958 C ATOM 2578 C ASP A 344 -0.875 -16.091 31.907 1.00 38.83 C ANISOU 2578 C ASP A 344 4757 5263 4733 -968 292 1005 C ATOM 2579 O ASP A 344 -0.292 -17.085 32.327 1.00 37.73 O ANISOU 2579 O ASP A 344 4678 5033 4624 -1018 236 1134 O ATOM 2580 CB ASP A 344 -3.192 -17.148 32.142 1.00 42.24 C ANISOU 2580 CB ASP A 344 5033 5756 5261 -1169 407 1098 C ATOM 2581 CG ASP A 344 -3.409 -16.658 33.580 1.00 45.59 C ANISOU 2581 CG ASP A 344 5465 6360 5498 -1213 515 1167 C ATOM 2582 OD1 ASP A 344 -2.671 -15.777 34.070 1.00 41.34 O ANISOU 2582 OD1 ASP A 344 4986 5896 4825 -1138 522 1122 O ATOM 2583 OD2 ASP A 344 -4.339 -17.186 34.239 1.00 53.83 O ANISOU 2583 OD2 ASP A 344 6453 7477 6525 -1337 598 1264 O ATOM 2584 N VAL A 345 -0.327 -14.872 31.950 1.00 38.55 N ANISOU 2584 N VAL A 345 4745 5299 4602 -870 303 906 N ATOM 2585 CA VAL A 345 1.030 -14.663 32.502 1.00 38.87 C ANISOU 2585 CA VAL A 345 4881 5328 4559 -822 247 937 C ATOM 2586 C VAL A 345 1.184 -15.159 33.948 1.00 42.45 C ANISOU 2586 C VAL A 345 5384 5861 4886 -911 265 1093 C ATOM 2587 O VAL A 345 2.298 -15.439 34.389 1.00 43.12 O ANISOU 2587 O VAL A 345 5542 5907 4935 -895 186 1169 O ATOM 2588 CB VAL A 345 1.507 -13.174 32.455 1.00 38.07 C ANISOU 2588 CB VAL A 345 4790 5304 4370 -721 269 801 C ATOM 2589 CG1 VAL A 345 1.581 -12.656 31.017 1.00 29.63 C ANISOU 2589 CG1 VAL A 345 3691 4157 3412 -632 234 676 C ATOM 2590 CG2 VAL A 345 0.634 -12.286 33.327 1.00 32.89 C ANISOU 2590 CG2 VAL A 345 4092 4817 3589 -743 389 755 C ATOM 2591 N PHE A 346 0.074 -15.258 34.680 1.00 44.40 N ANISOU 2591 N PHE A 346 5583 6228 5060 -1005 367 1146 N ATOM 2592 CA PHE A 346 0.089 -15.798 36.044 1.00 48.00 C ANISOU 2592 CA PHE A 346 6083 6779 5375 -1112 394 1314 C ATOM 2593 C PHE A 346 -0.094 -17.321 36.079 1.00 50.82 C ANISOU 2593 C PHE A 346 6450 7011 5849 -1215 345 1502 C ATOM 2594 O PHE A 346 -0.207 -17.900 37.157 1.00 52.26 O ANISOU 2594 O PHE A 346 6664 7263 5928 -1321 366 1676 O ATOM 2595 CB PHE A 346 -1.009 -15.152 36.895 1.00 49.05 C ANISOU 2595 CB PHE A 346 6156 7122 5356 -1175 549 1278 C ATOM 2596 CG PHE A 346 -0.991 -13.641 36.890 1.00 47.11 C ANISOU 2596 CG PHE A 346 5890 6984 5024 -1076 613 1080 C ATOM 2597 CD1 PHE A 346 0.110 -12.943 37.360 1.00 48.50 C ANISOU 2597 CD1 PHE A 346 6147 7202 5079 -1019 567 1034 C ATOM 2598 CD2 PHE A 346 -2.097 -12.921 36.450 1.00 43.76 C ANISOU 2598 CD2 PHE A 346 5357 6617 4655 -1045 716 944 C ATOM 2599 CE1 PHE A 346 0.118 -11.547 37.372 1.00 50.58 C ANISOU 2599 CE1 PHE A 346 6391 7543 5283 -936 628 847 C ATOM 2600 CE2 PHE A 346 -2.102 -11.536 36.467 1.00 46.93 C ANISOU 2600 CE2 PHE A 346 5734 7092 5003 -951 775 769 C ATOM 2601 CZ PHE A 346 -0.988 -10.844 36.930 1.00 48.73 C ANISOU 2601 CZ PHE A 346 6054 7345 5117 -899 733 716 C ATOM 2602 N ALA A 347 -0.112 -17.965 34.912 1.00 50.96 N ANISOU 2602 N ALA A 347 6442 6843 6079 -1189 279 1468 N ATOM 2603 CA ALA A 347 -0.329 -19.408 34.819 1.00 54.45 C ANISOU 2603 CA ALA A 347 6885 7129 6673 -1285 232 1618 C ATOM 2604 C ALA A 347 0.592 -20.190 35.750 1.00 58.36 C ANISOU 2604 C ALA A 347 7471 7572 7133 -1322 152 1827 C ATOM 2605 O ALA A 347 1.768 -19.859 35.897 1.00 57.28 O ANISOU 2605 O ALA A 347 7395 7422 6945 -1234 72 1819 O ATOM 2606 CB ALA A 347 -0.138 -19.876 33.392 1.00 52.75 C ANISOU 2606 CB ALA A 347 6649 6715 6679 -1227 154 1510 C ATOM 2607 N GLY A 348 0.043 -21.228 36.380 1.00 63.19 N ANISOU 2607 N GLY A 348 8082 8151 7775 -1459 168 2025 N ATOM 2608 CA GLY A 348 0.797 -22.050 37.331 1.00 66.25 C ANISOU 2608 CA GLY A 348 8552 8489 8132 -1510 85 2267 C ATOM 2609 C GLY A 348 1.109 -21.347 38.642 1.00 68.43 C ANISOU 2609 C GLY A 348 8880 9004 8117 -1533 117 2346 C ATOM 2610 O GLY A 348 2.025 -21.744 39.360 1.00 69.72 O ANISOU 2610 O GLY A 348 9117 9153 8222 -1536 18 2516 O ATOM 2611 N CYS A 349 0.347 -20.304 38.960 1.00 70.32 N ANISOU 2611 N CYS A 349 9075 9467 8176 -1549 253 2219 N ATOM 2612 CA CYS A 349 0.551 -19.556 40.194 1.00 73.57 C ANISOU 2612 CA CYS A 349 9533 10126 8296 -1579 304 2250 C ATOM 2613 C CYS A 349 -0.701 -18.775 40.593 1.00 73.89 C ANISOU 2613 C CYS A 349 9498 10389 8186 -1642 491 2140 C ATOM 2614 O CYS A 349 -1.694 -18.745 39.859 1.00 72.19 O ANISOU 2614 O CYS A 349 9187 10135 8105 -1648 571 2038 O ATOM 2615 CB CYS A 349 1.738 -18.598 40.051 1.00 73.20 C ANISOU 2615 CB CYS A 349 9532 10101 8180 -1439 225 2108 C ATOM 2616 SG CYS A 349 2.346 -17.946 41.633 1.00 83.76 S ANISOU 2616 SG CYS A 349 10949 11708 9169 -1486 226 2178 S ATOM 2617 N GLN A 350 -0.636 -18.157 41.771 1.00 75.15 N ANISOU 2617 N GLN A 350 9695 10788 8068 -1689 559 2157 N ATOM 2618 CA GLN A 350 -1.716 -17.321 42.289 1.00 75.81 C ANISOU 2618 CA GLN A 350 9708 11106 7990 -1739 750 2030 C ATOM 2619 C GLN A 350 -1.262 -15.865 42.311 1.00 73.86 C ANISOU 2619 C GLN A 350 9471 10969 7625 -1617 776 1785 C ATOM 2620 O GLN A 350 -0.062 -15.582 42.327 1.00 73.84 O ANISOU 2620 O GLN A 350 9547 10922 7585 -1539 652 1768 O ATOM 2621 CB GLN A 350 -2.130 -17.781 43.691 1.00 78.91 C ANISOU 2621 CB GLN A 350 10132 11710 8140 -1913 836 2230 C ATOM 2622 CG GLN A 350 -2.665 -19.243 43.682 0.00 82.12 C ANISOU 2622 CG GLN A 350 10523 11993 8684 -2051 819 2492 C ATOM 2623 CD GLN A 350 -3.868 -19.484 42.779 0.00 81.60 C ANISOU 2623 CD GLN A 350 10328 11832 8845 -2072 910 2408 C ATOM 2624 OE1 GLN A 350 -4.019 -20.564 42.208 0.00 81.69 O ANISOU 2624 OE1 GLN A 350 10325 11634 9079 -2119 840 2537 O ATOM 2625 NE2 GLN A 350 -4.728 -18.480 42.648 0.00 81.10 N ANISOU 2625 NE2 GLN A 350 10162 11917 8735 -2036 1061 2187 N ATOM 2626 N ILE A 351 -2.234 -14.953 42.304 1.00 72.82 N ANISOU 2626 N ILE A 351 9247 10968 7453 -1602 938 1596 N ATOM 2627 CA ILE A 351 -1.986 -13.510 42.205 1.00 69.89 C ANISOU 2627 CA ILE A 351 8867 10669 7021 -1482 980 1340 C ATOM 2628 C ILE A 351 -1.951 -12.870 43.602 1.00 71.54 C ANISOU 2628 C ILE A 351 9117 11146 6919 -1551 1083 1297 C ATOM 2629 O ILE A 351 -2.991 -12.786 44.264 1.00 71.50 O ANISOU 2629 O ILE A 351 9046 11322 6797 -1642 1254 1280 O ATOM 2630 CB ILE A 351 -3.089 -12.825 41.365 1.00 68.03 C ANISOU 2630 CB ILE A 351 8494 10408 6944 -1411 1093 1147 C ATOM 2631 CG1 ILE A 351 -3.070 -13.346 39.925 1.00 66.58 C ANISOU 2631 CG1 ILE A 351 8275 9981 7042 -1341 982 1162 C ATOM 2632 CG2 ILE A 351 -2.925 -11.311 41.380 1.00 65.33 C ANISOU 2632 CG2 ILE A 351 8139 10137 6549 -1294 1151 895 C ATOM 2633 CD1 ILE A 351 -4.397 -13.176 39.197 1.00 65.98 C ANISOU 2633 CD1 ILE A 351 8050 9894 7124 -1329 1079 1067 C ATOM 2634 N PRO A 352 -0.761 -12.412 44.052 1.00 71.76 N ANISOU 2634 N PRO A 352 9247 11211 6809 -1512 983 1268 N ATOM 2635 CA PRO A 352 -0.626 -11.808 45.381 1.00 74.46 C ANISOU 2635 CA PRO A 352 9640 11817 6836 -1586 1062 1212 C ATOM 2636 C PRO A 352 -0.751 -10.278 45.422 1.00 74.14 C ANISOU 2636 C PRO A 352 9562 11860 6748 -1494 1168 896 C ATOM 2637 O PRO A 352 -0.728 -9.696 46.507 1.00 74.96 O ANISOU 2637 O PRO A 352 9700 12189 6591 -1555 1254 804 O ATOM 2638 CB PRO A 352 0.787 -12.227 45.794 1.00 74.51 C ANISOU 2638 CB PRO A 352 9769 11801 6741 -1598 868 1364 C ATOM 2639 CG PRO A 352 1.549 -12.320 44.497 1.00 72.93 C ANISOU 2639 CG PRO A 352 9567 11320 6825 -1459 715 1342 C ATOM 2640 CD PRO A 352 0.546 -12.487 43.372 1.00 70.80 C ANISOU 2640 CD PRO A 352 9193 10897 6810 -1411 788 1287 C ATOM 2641 N TYR A 353 -0.898 -9.641 44.260 1.00 73.62 N ANISOU 2641 N TYR A 353 9429 11615 6929 -1353 1162 733 N ATOM 2642 CA TYR A 353 -0.877 -8.172 44.159 1.00 72.70 C ANISOU 2642 CA TYR A 353 9282 11518 6822 -1248 1233 447 C ATOM 2643 C TYR A 353 -2.188 -7.552 44.641 1.00 75.25 C ANISOU 2643 C TYR A 353 9499 12006 7088 -1271 1460 285 C ATOM 2644 O TYR A 353 -2.204 -6.763 45.589 1.00 77.77 O ANISOU 2644 O TYR A 353 9835 12508 7206 -1300 1566 124 O ATOM 2645 CB TYR A 353 -0.598 -7.735 42.717 1.00 69.87 C ANISOU 2645 CB TYR A 353 8887 10909 6751 -1095 1143 360 C ATOM 2646 CG TYR A 353 0.492 -8.539 42.046 1.00 66.24 C ANISOU 2646 CG TYR A 353 8500 10272 6396 -1071 944 526 C ATOM 2647 CD1 TYR A 353 0.190 -9.464 41.047 1.00 61.70 C ANISOU 2647 CD1 TYR A 353 7885 9530 6027 -1058 884 656 C ATOM 2648 CD2 TYR A 353 1.823 -8.397 42.429 1.00 64.23 C ANISOU 2648 CD2 TYR A 353 8345 10020 6038 -1066 816 543 C ATOM 2649 CE1 TYR A 353 1.190 -10.213 40.437 1.00 58.76 C ANISOU 2649 CE1 TYR A 353 7573 8994 5761 -1031 714 786 C ATOM 2650 CE2 TYR A 353 2.830 -9.143 41.824 1.00 61.89 C ANISOU 2650 CE2 TYR A 353 8098 9561 5855 -1036 641 687 C ATOM 2651 CZ TYR A 353 2.504 -10.050 40.831 1.00 58.03 C ANISOU 2651 CZ TYR A 353 7570 8903 5574 -1016 598 803 C ATOM 2652 OH TYR A 353 3.495 -10.792 40.236 1.00 61.46 O ANISOU 2652 OH TYR A 353 8047 9176 6131 -981 439 923 O TER 2653 TYR A 353 ATOM 2654 N LYS B -1 1.949 4.111 6.204 1.00 49.59 N ATOM 2655 CA LYS B -1 0.857 4.884 6.871 1.00 49.81 C ATOM 2656 C LYS B -1 -0.092 3.998 7.709 1.00 47.00 C ATOM 2657 O LYS B -1 -0.320 2.828 7.395 1.00 46.17 O ATOM 2658 CB LYS B -1 0.070 5.673 5.829 1.00 51.57 C ATOM 2659 CG LYS B -1 -0.835 6.754 6.417 1.00 53.75 C ATOM 2660 CD LYS B -1 -1.181 7.831 5.397 1.00 60.27 C ATOM 2661 CE LYS B -1 -0.137 8.957 5.358 1.00 63.06 C ATOM 2662 NZ LYS B -1 1.184 8.517 4.824 1.00 59.66 N ATOM 2663 N ALA B 0 -0.648 4.585 8.767 1.00 44.65 N ATOM 2664 CA ALA B 0 -1.375 3.843 9.798 1.00 42.47 C ATOM 2665 C ALA B 0 -2.538 3.009 9.253 1.00 39.38 C ATOM 2666 O ALA B 0 -3.389 3.519 8.537 1.00 42.27 O ATOM 2667 CB ALA B 0 -1.870 4.800 10.889 1.00 41.42 C ATOM 2668 N MET B 1 -2.543 1.721 9.599 1.00 48.95 N ANISOU 2668 N MET B 1 6064 6762 5772 1249 -700 460 N ATOM 2669 CA MET B 1 -3.604 0.775 9.232 1.00 44.71 C ANISOU 2669 CA MET B 1 5731 5990 5268 1254 -654 497 C ATOM 2670 C MET B 1 -3.637 0.397 7.746 1.00 43.76 C ANISOU 2670 C MET B 1 5627 5780 5221 1300 -598 446 C ATOM 2671 O MET B 1 -4.613 -0.200 7.270 1.00 41.31 O ANISOU 2671 O MET B 1 5473 5276 4948 1259 -559 454 O ATOM 2672 CB MET B 1 -4.983 1.274 9.690 1.00 43.48 C ANISOU 2672 CB MET B 1 5664 5737 5118 1059 -608 509 C ATOM 2673 CG MET B 1 -5.049 1.745 11.141 1.00 40.36 C ANISOU 2673 CG MET B 1 5268 5430 4637 1003 -649 549 C ATOM 2674 SD MET B 1 -4.287 0.633 12.336 1.00 40.21 S ANISOU 2674 SD MET B 1 5333 5436 4510 1195 -744 653 S ATOM 2675 CE MET B 1 -5.104 -0.929 11.958 1.00 39.47 C ANISOU 2675 CE MET B 1 5479 5068 4449 1265 -705 731 C ATOM 2676 N ALA B 2 -2.566 0.715 7.023 1.00 43.97 N ANISOU 2676 N ALA B 2 5494 5951 5262 1382 -595 393 N ATOM 2677 CA ALA B 2 -2.411 0.248 5.651 1.00 44.89 C ANISOU 2677 CA ALA B 2 5631 6000 5424 1467 -543 346 C ATOM 2678 C ALA B 2 -2.357 -1.273 5.664 1.00 45.86 C ANISOU 2678 C ALA B 2 5935 5964 5527 1657 -568 394 C ATOM 2679 O ALA B 2 -1.660 -1.862 6.490 1.00 50.97 O ANISOU 2679 O ALA B 2 6586 6659 6121 1809 -631 453 O ATOM 2680 CB ALA B 2 -1.142 0.812 5.038 1.00 45.04 C ANISOU 2680 CB ALA B 2 5435 6231 5448 1539 -530 295 C ATOM 2681 N GLY B 3 -3.095 -1.907 4.761 1.00 46.05 N ANISOU 2681 N GLY B 3 6116 5792 5588 1650 -526 369 N ATOM 2682 CA GLY B 3 -3.149 -3.372 4.704 1.00 45.49 C ANISOU 2682 CA GLY B 3 6254 5527 5502 1812 -547 408 C ATOM 2683 C GLY B 3 -4.192 -4.007 5.621 1.00 45.09 C ANISOU 2683 C GLY B 3 6404 5288 5441 1726 -572 489 C ATOM 2684 O GLY B 3 -4.314 -5.234 5.659 1.00 46.92 O ANISOU 2684 O GLY B 3 6837 5332 5661 1838 -590 531 O ATOM 2685 N ASN B 4 -4.946 -3.189 6.358 1.00 41.64 N ANISOU 2685 N ASN B 4 5920 4894 5006 1530 -566 513 N ATOM 2686 CA ASN B 4 -5.973 -3.709 7.264 1.00 40.09 C ANISOU 2686 CA ASN B 4 5895 4543 4796 1432 -573 597 C ATOM 2687 C ASN B 4 -7.410 -3.535 6.759 1.00 38.02 C ANISOU 2687 C ASN B 4 5705 4142 4597 1218 -521 573 C ATOM 2688 O ASN B 4 -8.356 -3.707 7.522 1.00 38.40 O ANISOU 2688 O ASN B 4 5847 4103 4641 1095 -510 638 O ATOM 2689 CB ASN B 4 -5.840 -3.059 8.649 1.00 38.41 C ANISOU 2689 CB ASN B 4 5600 4476 4520 1383 -604 656 C ATOM 2690 CG ASN B 4 -6.599 -3.815 9.716 1.00 36.22 C ANISOU 2690 CG ASN B 4 5509 4054 4199 1344 -612 765 C ATOM 2691 OD1 ASN B 4 -6.454 -5.025 9.838 1.00 39.03 O ANISOU 2691 OD1 ASN B 4 6037 4258 4533 1472 -636 827 O ATOM 2692 ND2 ASN B 4 -7.426 -3.110 10.484 1.00 32.28 N ANISOU 2692 ND2 ASN B 4 4987 3594 3683 1170 -583 790 N ATOM 2693 N PHE B 5 -7.588 -3.223 5.479 1.00 39.06 N ANISOU 2693 N PHE B 5 5794 4262 4784 1178 -489 483 N ATOM 2694 CA PHE B 5 -8.921 -2.891 4.967 1.00 38.31 C ANISOU 2694 CA PHE B 5 5730 4077 4748 976 -451 454 C ATOM 2695 C PHE B 5 -9.999 -3.934 5.289 1.00 40.11 C ANISOU 2695 C PHE B 5 6160 4086 4995 891 -454 516 C ATOM 2696 O PHE B 5 -11.120 -3.570 5.636 1.00 36.54 O ANISOU 2696 O PHE B 5 5702 3612 4571 709 -427 542 O ATOM 2697 CB PHE B 5 -8.891 -2.657 3.458 1.00 39.64 C ANISOU 2697 CB PHE B 5 5863 4240 4957 978 -430 354 C ATOM 2698 CG PHE B 5 -10.243 -2.372 2.878 1.00 38.00 C ANISOU 2698 CG PHE B 5 5684 3948 4804 787 -408 324 C ATOM 2699 CD1 PHE B 5 -10.861 -1.157 3.112 1.00 38.14 C ANISOU 2699 CD1 PHE B 5 5570 4079 4844 638 -379 318 C ATOM 2700 CD2 PHE B 5 -10.910 -3.325 2.130 1.00 38.91 C ANISOU 2700 CD2 PHE B 5 5963 3872 4949 758 -422 301 C ATOM 2701 CE1 PHE B 5 -12.108 -0.886 2.593 1.00 32.63 C ANISOU 2701 CE1 PHE B 5 4882 3320 4196 479 -364 295 C ATOM 2702 CE2 PHE B 5 -12.167 -3.064 1.611 1.00 36.67 C ANISOU 2702 CE2 PHE B 5 5687 3531 4716 578 -415 274 C ATOM 2703 CZ PHE B 5 -12.764 -1.840 1.846 1.00 37.13 C ANISOU 2703 CZ PHE B 5 5592 3719 4796 446 -386 274 C ATOM 2704 N TRP B 6 -9.661 -5.220 5.179 1.00 42.83 N ANISOU 2704 N TRP B 6 6683 4267 5323 1021 -483 543 N ATOM 2705 CA TRP B 6 -10.660 -6.290 5.309 1.00 45.01 C ANISOU 2705 CA TRP B 6 7173 4304 5624 927 -485 595 C ATOM 2706 C TRP B 6 -11.199 -6.488 6.728 1.00 46.37 C ANISOU 2706 C TRP B 6 7405 4447 5765 842 -476 718 C ATOM 2707 O TRP B 6 -12.208 -7.160 6.910 1.00 50.05 O ANISOU 2707 O TRP B 6 8014 4743 6260 706 -462 769 O ATOM 2708 CB TRP B 6 -10.115 -7.615 4.761 1.00 46.64 C ANISOU 2708 CB TRP B 6 7583 4320 5819 1098 -517 585 C ATOM 2709 CG TRP B 6 -9.802 -7.534 3.296 1.00 50.63 C ANISOU 2709 CG TRP B 6 8065 4825 6348 1160 -515 461 C ATOM 2710 CD1 TRP B 6 -8.578 -7.666 2.714 1.00 53.93 C ANISOU 2710 CD1 TRP B 6 8450 5310 6731 1387 -521 407 C ATOM 2711 CD2 TRP B 6 -10.727 -7.268 2.231 1.00 50.09 C ANISOU 2711 CD2 TRP B 6 7995 4704 6334 998 -505 378 C ATOM 2712 NE1 TRP B 6 -8.682 -7.514 1.355 1.00 55.78 N ANISOU 2712 NE1 TRP B 6 8678 5529 6987 1376 -506 297 N ATOM 2713 CE2 TRP B 6 -9.990 -7.271 1.031 1.00 53.03 C ANISOU 2713 CE2 TRP B 6 8353 5104 6690 1139 -503 276 C ATOM 2714 CE3 TRP B 6 -12.106 -7.034 2.177 1.00 45.87 C ANISOU 2714 CE3 TRP B 6 7462 4113 5854 753 -498 383 C ATOM 2715 CZ2 TRP B 6 -10.586 -7.049 -0.216 1.00 53.89 C ANISOU 2715 CZ2 TRP B 6 8468 5179 6827 1043 -500 179 C ATOM 2716 CZ3 TRP B 6 -12.699 -6.818 0.940 1.00 48.01 C ANISOU 2716 CZ3 TRP B 6 7724 4356 6162 659 -504 285 C ATOM 2717 CH2 TRP B 6 -11.939 -6.823 -0.238 1.00 51.31 C ANISOU 2717 CH2 TRP B 6 8145 4796 6553 804 -509 185 C ATOM 2718 N GLN B 7 -10.545 -5.912 7.731 1.00 45.65 N ANISOU 2718 N GLN B 7 7208 4526 5610 912 -483 765 N ATOM 2719 CA GLN B 7 -11.116 -5.895 9.086 1.00 45.67 C ANISOU 2719 CA GLN B 7 7251 4535 5567 818 -464 874 C ATOM 2720 C GLN B 7 -11.226 -4.464 9.609 1.00 40.66 C ANISOU 2720 C GLN B 7 6411 4125 4913 728 -437 850 C ATOM 2721 O GLN B 7 -11.266 -4.227 10.807 1.00 38.38 O ANISOU 2721 O GLN B 7 6117 3910 4555 711 -431 923 O ATOM 2722 CB GLN B 7 -10.343 -6.815 10.044 1.00 50.43 C ANISOU 2722 CB GLN B 7 7994 5083 6083 993 -507 978 C ATOM 2723 CG GLN B 7 -8.839 -6.787 9.891 1.00 55.71 C ANISOU 2723 CG GLN B 7 8586 5874 6707 1238 -566 944 C ATOM 2724 CD GLN B 7 -8.325 -7.676 8.761 1.00 61.50 C ANISOU 2724 CD GLN B 7 9422 6468 7477 1390 -586 888 C ATOM 2725 OE1 GLN B 7 -8.824 -8.780 8.547 1.00 69.02 O ANISOU 2725 OE1 GLN B 7 10597 7178 8450 1382 -584 924 O ATOM 2726 NE2 GLN B 7 -7.321 -7.188 8.032 1.00 57.38 N ANISOU 2726 NE2 GLN B 7 8743 6098 6961 1524 -602 799 N ATOM 2727 N SER B 8 -11.340 -3.518 8.684 1.00 36.44 N ANISOU 2727 N SER B 8 5725 3684 4435 664 -419 746 N ATOM 2728 CA SER B 8 -11.431 -2.097 9.022 1.00 34.62 C ANISOU 2728 CA SER B 8 5314 3645 4194 581 -393 709 C ATOM 2729 C SER B 8 -12.877 -1.680 9.257 1.00 34.04 C ANISOU 2729 C SER B 8 5232 3545 4158 381 -331 728 C ATOM 2730 O SER B 8 -13.803 -2.353 8.799 1.00 35.12 O ANISOU 2730 O SER B 8 5460 3533 4352 287 -312 743 O ATOM 2731 CB SER B 8 -10.851 -1.274 7.879 1.00 33.45 C ANISOU 2731 CB SER B 8 5021 3601 4087 613 -397 598 C ATOM 2732 OG SER B 8 -11.721 -1.271 6.755 1.00 28.93 O ANISOU 2732 OG SER B 8 4462 2937 3592 511 -371 544 O ATOM 2733 N SER B 9 -13.080 -0.566 9.956 1.00 34.18 N ANISOU 2733 N SER B 9 5137 3707 4143 316 -299 722 N ATOM 2734 CA SER B 9 -14.433 -0.028 10.123 1.00 34.20 C ANISOU 2734 CA SER B 9 5103 3711 4181 148 -231 730 C ATOM 2735 C SER B 9 -15.002 0.448 8.781 1.00 34.41 C ANISOU 2735 C SER B 9 5050 3722 4303 74 -219 644 C ATOM 2736 O SER B 9 -16.205 0.320 8.533 1.00 35.04 O ANISOU 2736 O SER B 9 5136 3738 4438 -54 -183 657 O ATOM 2737 CB SER B 9 -14.481 1.078 11.188 1.00 33.08 C ANISOU 2737 CB SER B 9 4876 3723 3971 117 -197 734 C ATOM 2738 OG SER B 9 -14.023 2.328 10.706 1.00 34.89 O ANISOU 2738 OG SER B 9 4967 4076 4213 126 -204 639 O ATOM 2739 N HIS B 10 -14.142 0.987 7.917 1.00 34.46 N ANISOU 2739 N HIS B 10 4977 3794 4322 151 -251 561 N ATOM 2740 CA HIS B 10 -14.548 1.352 6.558 1.00 34.41 C ANISOU 2740 CA HIS B 10 4917 3768 4389 104 -248 483 C ATOM 2741 C HIS B 10 -15.260 0.158 5.907 1.00 35.35 C ANISOU 2741 C HIS B 10 5157 3714 4559 58 -264 499 C ATOM 2742 O HIS B 10 -16.423 0.261 5.518 1.00 34.62 O ANISOU 2742 O HIS B 10 5047 3586 4523 -69 -245 492 O ATOM 2743 CB HIS B 10 -13.329 1.779 5.733 1.00 33.98 C ANISOU 2743 CB HIS B 10 4796 3789 4326 217 -278 410 C ATOM 2744 CG HIS B 10 -13.645 2.257 4.345 1.00 34.78 C ANISOU 2744 CG HIS B 10 4847 3885 4481 180 -271 333 C ATOM 2745 ND1 HIS B 10 -12.821 3.126 3.663 1.00 33.73 N ANISOU 2745 ND1 HIS B 10 4618 3857 4341 230 -268 270 N ATOM 2746 CD2 HIS B 10 -14.671 1.980 3.503 1.00 36.76 C ANISOU 2746 CD2 HIS B 10 5136 4046 4787 97 -272 313 C ATOM 2747 CE1 HIS B 10 -13.321 3.358 2.462 1.00 35.16 C ANISOU 2747 CE1 HIS B 10 4790 4006 4562 191 -263 219 C ATOM 2748 NE2 HIS B 10 -14.446 2.678 2.342 1.00 38.59 N ANISOU 2748 NE2 HIS B 10 5302 4328 5034 112 -272 240 N ATOM 2749 N TYR B 11 -14.570 -0.974 5.817 1.00 37.72 N ANISOU 2749 N TYR B 11 5583 3908 4839 162 -304 519 N ATOM 2750 CA TYR B 11 -15.133 -2.173 5.179 1.00 39.56 C ANISOU 2750 CA TYR B 11 5963 3952 5115 122 -327 523 C ATOM 2751 C TYR B 11 -16.357 -2.715 5.902 1.00 39.12 C ANISOU 2751 C TYR B 11 5977 3803 5083 -34 -298 607 C ATOM 2752 O TYR B 11 -17.377 -2.978 5.283 1.00 39.67 O ANISOU 2752 O TYR B 11 6063 3793 5215 -167 -300 589 O ATOM 2753 CB TYR B 11 -14.092 -3.286 5.081 1.00 41.04 C ANISOU 2753 CB TYR B 11 6293 4033 5266 288 -370 534 C ATOM 2754 CG TYR B 11 -14.640 -4.560 4.468 1.00 46.77 C ANISOU 2754 CG TYR B 11 7204 4536 6029 247 -397 533 C ATOM 2755 CD1 TYR B 11 -15.154 -4.559 3.172 1.00 51.64 C ANISOU 2755 CD1 TYR B 11 7824 5100 6697 180 -416 445 C ATOM 2756 CD2 TYR B 11 -14.667 -5.755 5.184 1.00 53.40 C ANISOU 2756 CD2 TYR B 11 8229 5212 6848 266 -408 621 C ATOM 2757 CE1 TYR B 11 -15.667 -5.715 2.595 1.00 53.10 C ANISOU 2757 CE1 TYR B 11 8189 5075 6912 127 -452 432 C ATOM 2758 CE2 TYR B 11 -15.184 -6.928 4.614 1.00 58.73 C ANISOU 2758 CE2 TYR B 11 9095 5660 7560 211 -435 616 C ATOM 2759 CZ TYR B 11 -15.680 -6.894 3.316 1.00 58.79 C ANISOU 2759 CZ TYR B 11 9098 5621 7620 137 -460 514 C ATOM 2760 OH TYR B 11 -16.191 -8.030 2.734 1.00 63.67 O ANISOU 2760 OH TYR B 11 9911 6012 8270 69 -497 496 O ATOM 2761 N LEU B 12 -16.243 -2.875 7.214 1.00 40.76 N ANISOU 2761 N LEU B 12 6221 4031 5236 -21 -272 700 N ATOM 2762 CA LEU B 12 -17.234 -3.612 7.996 1.00 42.61 C ANISOU 2762 CA LEU B 12 6553 4160 5477 -152 -235 801 C ATOM 2763 C LEU B 12 -18.493 -2.811 8.338 1.00 42.95 C ANISOU 2763 C LEU B 12 6466 4300 5554 -322 -168 817 C ATOM 2764 O LEU B 12 -19.534 -3.402 8.596 1.00 45.24 O ANISOU 2764 O LEU B 12 6804 4505 5879 -469 -134 881 O ATOM 2765 CB LEU B 12 -16.600 -4.157 9.280 1.00 42.44 C ANISOU 2765 CB LEU B 12 6641 4120 5365 -58 -231 905 C ATOM 2766 CG LEU B 12 -15.478 -5.190 9.095 1.00 47.34 C ANISOU 2766 CG LEU B 12 7419 4619 5951 120 -295 915 C ATOM 2767 CD1 LEU B 12 -14.696 -5.365 10.395 1.00 41.79 C ANISOU 2767 CD1 LEU B 12 6770 3966 5141 245 -302 1008 C ATOM 2768 CD2 LEU B 12 -16.008 -6.541 8.594 1.00 45.75 C ANISOU 2768 CD2 LEU B 12 7417 4169 5799 57 -312 943 C ATOM 2769 N GLN B 13 -18.407 -1.483 8.343 1.00 42.38 N ANISOU 2769 N GLN B 13 6230 4402 5471 -302 -145 762 N ATOM 2770 CA GLN B 13 -19.566 -0.645 8.674 1.00 43.45 C ANISOU 2770 CA GLN B 13 6238 4639 5633 -431 -76 772 C ATOM 2771 C GLN B 13 -19.955 0.384 7.623 1.00 41.01 C ANISOU 2771 C GLN B 13 5783 4414 5383 -458 -84 675 C ATOM 2772 O GLN B 13 -21.099 0.835 7.613 1.00 42.81 O ANISOU 2772 O GLN B 13 5915 4694 5656 -569 -39 682 O ATOM 2773 CB GLN B 13 -19.323 0.087 9.991 1.00 44.74 C ANISOU 2773 CB GLN B 13 6359 4931 5707 -390 -22 816 C ATOM 2774 CG GLN B 13 -19.275 -0.823 11.190 1.00 52.13 C ANISOU 2774 CG GLN B 13 7431 5804 6573 -391 4 933 C ATOM 2775 CD GLN B 13 -19.000 -0.071 12.477 1.00 58.06 C ANISOU 2775 CD GLN B 13 8151 6692 7217 -343 50 966 C ATOM 2776 OE1 GLN B 13 -18.064 -0.403 13.212 1.00 62.87 O ANISOU 2776 OE1 GLN B 13 8849 7305 7736 -236 16 1007 O ATOM 2777 NE2 GLN B 13 -19.806 0.953 12.755 1.00 53.90 N ANISOU 2777 NE2 GLN B 13 7502 6282 6693 -412 122 944 N ATOM 2778 N TRP B 14 -19.019 0.785 6.765 1.00 38.76 N ANISOU 2778 N TRP B 14 5477 4153 5096 -352 -135 592 N ATOM 2779 CA TRP B 14 -19.252 1.917 5.869 1.00 35.45 C ANISOU 2779 CA TRP B 14 4930 3826 4713 -360 -136 510 C ATOM 2780 C TRP B 14 -19.114 1.592 4.374 1.00 34.18 C ANISOU 2780 C TRP B 14 4794 3595 4597 -343 -199 436 C ATOM 2781 O TRP B 14 -18.878 2.485 3.569 1.00 32.73 O ANISOU 2781 O TRP B 14 4532 3484 4420 -306 -209 368 O ATOM 2782 CB TRP B 14 -18.378 3.105 6.295 1.00 33.19 C ANISOU 2782 CB TRP B 14 4567 3671 4370 -270 -118 477 C ATOM 2783 CG TRP B 14 -18.895 3.724 7.560 1.00 34.44 C ANISOU 2783 CG TRP B 14 4682 3915 4490 -311 -51 525 C ATOM 2784 CD1 TRP B 14 -18.398 3.563 8.822 1.00 37.48 C ANISOU 2784 CD1 TRP B 14 5118 4328 4794 -271 -32 579 C ATOM 2785 CD2 TRP B 14 -20.053 4.551 7.689 1.00 29.75 C ANISOU 2785 CD2 TRP B 14 3992 3388 3925 -389 9 523 C ATOM 2786 NE1 TRP B 14 -19.163 4.263 9.723 1.00 36.33 N ANISOU 2786 NE1 TRP B 14 4922 4263 4620 -324 40 606 N ATOM 2787 CE2 TRP B 14 -20.185 4.878 9.051 1.00 33.88 C ANISOU 2787 CE2 TRP B 14 4517 3977 4380 -391 71 572 C ATOM 2788 CE3 TRP B 14 -20.989 5.055 6.780 1.00 34.32 C ANISOU 2788 CE3 TRP B 14 4481 3984 4574 -445 13 485 C ATOM 2789 CZ2 TRP B 14 -21.219 5.692 9.533 1.00 37.73 C ANISOU 2789 CZ2 TRP B 14 4921 4545 4869 -441 149 580 C ATOM 2790 CZ3 TRP B 14 -22.021 5.868 7.262 1.00 34.87 C ANISOU 2790 CZ3 TRP B 14 4457 4139 4652 -490 84 498 C ATOM 2791 CH2 TRP B 14 -22.118 6.179 8.623 1.00 33.35 C ANISOU 2791 CH2 TRP B 14 4270 4008 4393 -484 156 543 C ATOM 2792 N ILE B 15 -19.264 0.315 4.016 1.00 35.17 N ANISOU 2792 N ILE B 15 5044 3575 4746 -373 -239 451 N ATOM 2793 CA ILE B 15 -19.557 -0.081 2.636 1.00 35.40 C ANISOU 2793 CA ILE B 15 5107 3525 4818 -402 -297 382 C ATOM 2794 C ILE B 15 -21.042 -0.434 2.612 1.00 38.25 C ANISOU 2794 C ILE B 15 5445 3845 5244 -579 -297 412 C ATOM 2795 O ILE B 15 -21.452 -1.503 3.076 1.00 39.43 O ANISOU 2795 O ILE B 15 5697 3874 5410 -663 -299 471 O ATOM 2796 CB ILE B 15 -18.714 -1.286 2.141 1.00 37.03 C ANISOU 2796 CB ILE B 15 5483 3582 5003 -312 -349 360 C ATOM 2797 CG1 ILE B 15 -17.225 -0.927 2.091 1.00 38.91 C ANISOU 2797 CG1 ILE B 15 5714 3890 5182 -129 -348 328 C ATOM 2798 CG2 ILE B 15 -19.149 -1.708 0.738 1.00 35.71 C ANISOU 2798 CG2 ILE B 15 5368 3329 4870 -357 -411 281 C ATOM 2799 CD1 ILE B 15 -16.886 0.210 1.147 1.00 34.80 C ANISOU 2799 CD1 ILE B 15 5074 3491 4656 -85 -345 249 C ATOM 2800 N LEU B 16 -21.844 0.483 2.081 1.00 36.62 N ANISOU 2800 N LEU B 16 5100 3741 5074 -638 -295 377 N ATOM 2801 CA LEU B 16 -23.284 0.419 2.243 1.00 38.04 C ANISOU 2801 CA LEU B 16 5196 3942 5314 -799 -282 414 C ATOM 2802 C LEU B 16 -23.937 -0.339 1.097 1.00 41.06 C ANISOU 2802 C LEU B 16 5624 4229 5747 -900 -367 365 C ATOM 2803 O LEU B 16 -23.330 -0.551 0.045 1.00 41.23 O ANISOU 2803 O LEU B 16 5725 4191 5748 -828 -433 288 O ATOM 2804 CB LEU B 16 -23.857 1.834 2.358 1.00 36.96 C ANISOU 2804 CB LEU B 16 4879 3976 5187 -792 -235 406 C ATOM 2805 CG LEU B 16 -23.252 2.720 3.460 1.00 33.21 C ANISOU 2805 CG LEU B 16 4365 3597 4655 -700 -155 438 C ATOM 2806 CD1 LEU B 16 -23.753 4.141 3.354 1.00 30.73 C ANISOU 2806 CD1 LEU B 16 3904 3423 4349 -676 -118 411 C ATOM 2807 CD2 LEU B 16 -23.551 2.169 4.846 1.00 35.41 C ANISOU 2807 CD2 LEU B 16 4677 3862 4917 -759 -88 533 C ATOM 2808 N ASP B 17 -25.166 -0.782 1.338 1.00 43.68 N ANISOU 2808 N ASP B 17 5907 4550 6140 -1071 -365 411 N ATOM 2809 CA ASP B 17 -25.997 -1.399 0.318 1.00 44.36 C ANISOU 2809 CA ASP B 17 6003 4571 6280 -1203 -454 364 C ATOM 2810 C ASP B 17 -26.661 -0.282 -0.476 1.00 43.32 C ANISOU 2810 C ASP B 17 5693 4597 6170 -1198 -484 312 C ATOM 2811 O ASP B 17 -27.174 0.675 0.103 1.00 41.62 O ANISOU 2811 O ASP B 17 5316 4530 5967 -1190 -416 352 O ATOM 2812 CB ASP B 17 -27.053 -2.286 0.973 1.00 48.92 C ANISOU 2812 CB ASP B 17 6579 5090 6919 -1407 -435 443 C ATOM 2813 CG ASP B 17 -27.844 -3.108 -0.033 1.00 55.14 C ANISOU 2813 CG ASP B 17 7404 5784 7763 -1570 -543 391 C ATOM 2814 OD1 ASP B 17 -27.533 -4.308 -0.180 1.00 60.11 O ANISOU 2814 OD1 ASP B 17 8234 6215 8390 -1620 -587 383 O ATOM 2815 OD2 ASP B 17 -28.770 -2.558 -0.677 1.00 60.34 O ANISOU 2815 OD2 ASP B 17 7897 6564 8463 -1643 -588 355 O ATOM 2816 N LYS B 18 -26.637 -0.411 -1.799 1.00 43.57 N ANISOU 2816 N LYS B 18 5766 4592 6195 -1189 -584 223 N ATOM 2817 CA LYS B 18 -27.207 0.585 -2.697 1.00 45.19 C ANISOU 2817 CA LYS B 18 5830 4934 6408 -1168 -630 173 C ATOM 2818 C LYS B 18 -28.697 0.825 -2.422 1.00 45.60 C ANISOU 2818 C LYS B 18 5690 5103 6535 -1315 -628 218 C ATOM 2819 O LYS B 18 -29.142 1.970 -2.355 1.00 43.54 O ANISOU 2819 O LYS B 18 5265 4998 6280 -1258 -593 231 O ATOM 2820 CB LYS B 18 -27.012 0.148 -4.153 1.00 46.62 C ANISOU 2820 CB LYS B 18 6117 5037 6558 -1158 -748 73 C ATOM 2821 CG LYS B 18 -27.294 1.241 -5.174 1.00 49.19 C ANISOU 2821 CG LYS B 18 6334 5496 6860 -1088 -797 21 C ATOM 2822 CD LYS B 18 -26.944 0.788 -6.577 1.00 53.57 C ANISOU 2822 CD LYS B 18 7023 5971 7358 -1058 -905 -78 C ATOM 2823 CE LYS B 18 -27.403 1.796 -7.617 1.00 56.91 C ANISOU 2823 CE LYS B 18 7344 6528 7753 -1008 -965 -119 C ATOM 2824 NZ LYS B 18 -27.188 1.289 -9.001 1.00 61.03 N ANISOU 2824 NZ LYS B 18 8003 6978 8207 -993 -1077 -217 N ATOM 2825 N GLN B 19 -29.453 -0.255 -2.246 1.00 47.20 N ANISOU 2825 N GLN B 19 5913 5227 6793 -1501 -661 246 N ATOM 2826 CA GLN B 19 -30.894 -0.162 -1.986 1.00 49.19 C ANISOU 2826 CA GLN B 19 5966 5600 7125 -1662 -659 293 C ATOM 2827 C GLN B 19 -31.210 0.550 -0.671 1.00 48.35 C ANISOU 2827 C GLN B 19 5716 5623 7030 -1635 -516 388 C ATOM 2828 O GLN B 19 -32.156 1.324 -0.601 1.00 49.21 O ANISOU 2828 O GLN B 19 5617 5903 7177 -1649 -493 410 O ATOM 2829 CB GLN B 19 -31.542 -1.556 -1.996 1.00 51.93 C ANISOU 2829 CB GLN B 19 6382 5818 7530 -1892 -715 309 C ATOM 2830 CG GLN B 19 -33.060 -1.545 -2.041 0.00 55.16 C ANISOU 2830 CG GLN B 19 6569 6362 8026 -2083 -745 339 C ATOM 2831 CD GLN B 19 -33.658 -2.926 -2.261 0.00 57.46 C ANISOU 2831 CD GLN B 19 6944 6513 8376 -2333 -825 337 C ATOM 2832 OE1 GLN B 19 -34.685 -3.068 -2.926 0.00 58.88 O ANISOU 2832 OE1 GLN B 19 6992 6767 8613 -2487 -925 305 O ATOM 2833 NE2 GLN B 19 -33.019 -3.949 -1.704 0.00 57.74 N ANISOU 2833 NE2 GLN B 19 7201 6340 8396 -2376 -788 371 N ATOM 2834 N ASP B 20 -30.427 0.278 0.369 1.00 49.87 N ANISOU 2834 N ASP B 20 6026 5739 7185 -1585 -422 443 N ATOM 2835 CA ASP B 20 -30.545 1.009 1.632 1.00 49.83 C ANISOU 2835 CA ASP B 20 5919 5850 7163 -1531 -285 521 C ATOM 2836 C ASP B 20 -30.294 2.499 1.400 1.00 47.79 C ANISOU 2836 C ASP B 20 5560 5730 6869 -1353 -262 479 C ATOM 2837 O ASP B 20 -31.036 3.353 1.886 1.00 48.72 O ANISOU 2837 O ASP B 20 5509 5999 7003 -1334 -190 512 O ATOM 2838 CB ASP B 20 -29.528 0.505 2.663 1.00 51.21 C ANISOU 2838 CB ASP B 20 6265 5913 7278 -1478 -212 573 C ATOM 2839 CG ASP B 20 -29.917 -0.814 3.298 1.00 57.67 C ANISOU 2839 CG ASP B 20 7174 6612 8127 -1651 -190 653 C ATOM 2840 OD1 ASP B 20 -31.008 -1.355 3.009 1.00 65.10 O ANISOU 2840 OD1 ASP B 20 8035 7557 9143 -1838 -223 671 O ATOM 2841 OD2 ASP B 20 -29.104 -1.315 4.105 1.00 67.16 O ANISOU 2841 OD2 ASP B 20 8531 7712 9274 -1602 -142 703 O ATOM 2842 N LEU B 21 -29.227 2.794 0.665 1.00 45.65 N ANISOU 2842 N LEU B 21 5401 5400 6546 -1221 -316 407 N ATOM 2843 CA LEU B 21 -28.834 4.166 0.377 1.00 43.11 C ANISOU 2843 CA LEU B 21 5020 5176 6184 -1060 -297 367 C ATOM 2844 C LEU B 21 -29.968 4.934 -0.312 1.00 42.65 C ANISOU 2844 C LEU B 21 4783 5252 6169 -1070 -336 350 C ATOM 2845 O LEU B 21 -30.337 6.033 0.107 1.00 40.99 O ANISOU 2845 O LEU B 21 4455 5164 5955 -990 -267 369 O ATOM 2846 CB LEU B 21 -27.586 4.158 -0.499 1.00 42.12 C ANISOU 2846 CB LEU B 21 5040 4960 6002 -952 -359 296 C ATOM 2847 CG LEU B 21 -26.885 5.473 -0.792 1.00 43.20 C ANISOU 2847 CG LEU B 21 5161 5164 6088 -795 -335 258 C ATOM 2848 CD1 LEU B 21 -26.317 6.063 0.491 1.00 43.12 C ANISOU 2848 CD1 LEU B 21 5153 5189 6043 -727 -227 299 C ATOM 2849 CD2 LEU B 21 -25.793 5.214 -1.806 1.00 37.69 C ANISOU 2849 CD2 LEU B 21 4598 4381 5343 -722 -399 192 C ATOM 2850 N LEU B 22 -30.537 4.341 -1.354 1.00 43.29 N ANISOU 2850 N LEU B 22 4849 5311 6286 -1164 -450 312 N ATOM 2851 CA LEU B 22 -31.572 5.014 -2.126 1.00 45.60 C ANISOU 2851 CA LEU B 22 4974 5738 6612 -1163 -511 292 C ATOM 2852 C LEU B 22 -32.878 5.131 -1.348 1.00 47.40 C ANISOU 2852 C LEU B 22 4995 6104 6910 -1254 -449 362 C ATOM 2853 O LEU B 22 -33.615 6.097 -1.528 1.00 46.47 O ANISOU 2853 O LEU B 22 4712 6135 6809 -1184 -443 367 O ATOM 2854 CB LEU B 22 -31.774 4.323 -3.480 1.00 47.37 C ANISOU 2854 CB LEU B 22 5250 5906 6843 -1239 -666 224 C ATOM 2855 CG LEU B 22 -30.528 4.364 -4.383 1.00 47.91 C ANISOU 2855 CG LEU B 22 5507 5867 6830 -1121 -717 151 C ATOM 2856 CD1 LEU B 22 -30.866 3.946 -5.814 1.00 52.76 C ANISOU 2856 CD1 LEU B 22 6155 6460 7430 -1169 -870 76 C ATOM 2857 CD2 LEU B 22 -29.868 5.745 -4.383 1.00 48.04 C ANISOU 2857 CD2 LEU B 22 5513 5949 6791 -933 -652 148 C ATOM 2858 N LYS B 23 -33.141 4.169 -0.465 1.00 48.83 N ANISOU 2858 N LYS B 23 5188 6238 7126 -1401 -395 422 N ATOM 2859 CA LYS B 23 -34.321 4.221 0.398 1.00 50.76 C ANISOU 2859 CA LYS B 23 5236 6621 7431 -1495 -309 500 C ATOM 2860 C LYS B 23 -34.249 5.411 1.349 1.00 49.00 C ANISOU 2860 C LYS B 23 4940 6508 7170 -1337 -169 535 C ATOM 2861 O LYS B 23 -35.219 6.148 1.496 1.00 47.78 O ANISOU 2861 O LYS B 23 4586 6520 7048 -1303 -127 559 O ATOM 2862 CB LYS B 23 -34.488 2.914 1.190 1.00 53.19 C ANISOU 2862 CB LYS B 23 5606 6833 7771 -1688 -265 566 C ATOM 2863 CG LYS B 23 -35.647 2.943 2.189 1.00 56.87 C ANISOU 2863 CG LYS B 23 5871 7448 8291 -1793 -149 660 C ATOM 2864 CD LYS B 23 -36.167 1.553 2.532 1.00 65.44 C ANISOU 2864 CD LYS B 23 6979 8451 9433 -2045 -149 721 C ATOM 2865 CE LYS B 23 -37.383 1.637 3.457 1.00 69.62 C ANISOU 2865 CE LYS B 23 7279 9158 10016 -2155 -23 819 C ATOM 2866 NZ LYS B 23 -38.166 0.374 3.511 1.00 70.37 N ANISOU 2866 NZ LYS B 23 7340 9208 10191 -2439 -47 875 N ATOM 2867 N GLU B 24 -33.097 5.604 1.987 1.00 48.94 N ANISOU 2867 N GLU B 24 5095 6410 7090 -1236 -102 534 N ATOM 2868 CA GLU B 24 -32.899 6.763 2.866 1.00 48.97 C ANISOU 2868 CA GLU B 24 5066 6497 7042 -1084 19 551 C ATOM 2869 C GLU B 24 -32.930 8.100 2.112 1.00 47.46 C ANISOU 2869 C GLU B 24 4813 6382 6836 -921 -14 495 C ATOM 2870 O GLU B 24 -33.284 9.136 2.684 1.00 47.66 O ANISOU 2870 O GLU B 24 4753 6511 6845 -811 78 508 O ATOM 2871 CB GLU B 24 -31.594 6.630 3.664 1.00 48.97 C ANISOU 2871 CB GLU B 24 5258 6384 6964 -1025 75 555 C ATOM 2872 CG GLU B 24 -31.679 5.665 4.853 1.00 54.55 C ANISOU 2872 CG GLU B 24 6012 7053 7662 -1139 159 638 C ATOM 2873 CD GLU B 24 -32.786 6.025 5.851 1.00 63.06 C ANISOU 2873 CD GLU B 24 6924 8282 8753 -1169 289 708 C ATOM 2874 OE1 GLU B 24 -33.187 7.212 5.926 1.00 58.78 O ANISOU 2874 OE1 GLU B 24 6268 7865 8202 -1048 339 687 O ATOM 2875 OE2 GLU B 24 -33.261 5.110 6.562 1.00 71.63 O ANISOU 2875 OE2 GLU B 24 8000 9359 9856 -1311 347 787 O ATOM 2876 N ARG B 25 -32.576 8.059 0.832 1.00 45.37 N ANISOU 2876 N ARG B 25 4607 6060 6571 -901 -140 433 N ATOM 2877 CA ARG B 25 -32.547 9.238 -0.023 1.00 45.30 C ANISOU 2877 CA ARG B 25 4570 6103 6541 -753 -183 387 C ATOM 2878 C ARG B 25 -33.946 9.699 -0.457 1.00 46.26 C ANISOU 2878 C ARG B 25 4475 6382 6719 -747 -215 403 C ATOM 2879 O ARG B 25 -34.143 10.866 -0.797 1.00 44.42 O ANISOU 2879 O ARG B 25 4192 6217 6468 -598 -211 388 O ATOM 2880 CB ARG B 25 -31.680 8.941 -1.246 1.00 44.94 C ANISOU 2880 CB ARG B 25 4668 5946 6462 -740 -301 323 C ATOM 2881 CG ARG B 25 -31.305 10.148 -2.079 1.00 46.41 C ANISOU 2881 CG ARG B 25 4883 6148 6602 -583 -330 282 C ATOM 2882 CD ARG B 25 -30.153 9.814 -3.022 1.00 43.30 C ANISOU 2882 CD ARG B 25 4663 5635 6155 -565 -405 227 C ATOM 2883 NE ARG B 25 -28.874 9.733 -2.314 1.00 46.64 N ANISOU 2883 NE ARG B 25 5222 5967 6533 -535 -331 224 N ATOM 2884 CZ ARG B 25 -27.759 9.189 -2.806 1.00 50.36 C ANISOU 2884 CZ ARG B 25 5838 6335 6963 -530 -369 186 C ATOM 2885 NH1 ARG B 25 -27.739 8.657 -4.024 1.00 50.02 N ANISOU 2885 NH1 ARG B 25 5845 6252 6909 -554 -473 142 N ATOM 2886 NH2 ARG B 25 -26.651 9.169 -2.070 1.00 53.09 N ANISOU 2886 NH2 ARG B 25 6277 6624 7271 -496 -303 189 N ATOM 2887 N GLN B 26 -34.918 8.790 -0.431 1.00 48.32 N ANISOU 2887 N GLN B 26 4608 6702 7050 -908 -248 435 N ATOM 2888 CA GLN B 26 -36.286 9.109 -0.850 1.00 50.28 C ANISOU 2888 CA GLN B 26 4621 7124 7359 -918 -291 453 C ATOM 2889 C GLN B 26 -36.871 10.297 -0.088 1.00 49.84 C ANISOU 2889 C GLN B 26 4425 7210 7300 -766 -166 490 C ATOM 2890 O GLN B 26 -37.685 11.037 -0.629 1.00 50.60 O ANISOU 2890 O GLN B 26 4368 7439 7420 -670 -206 488 O ATOM 2891 CB GLN B 26 -37.204 7.885 -0.706 1.00 53.43 C ANISOU 2891 CB GLN B 26 4896 7567 7839 -1148 -323 491 C ATOM 2892 CG GLN B 26 -37.061 6.873 -1.835 1.00 56.12 C ANISOU 2892 CG GLN B 26 5323 7807 8193 -1288 -491 438 C ATOM 2893 CD GLN B 26 -37.647 7.379 -3.142 1.00 62.20 C ANISOU 2893 CD GLN B 26 5989 8676 8968 -1230 -639 390 C ATOM 2894 OE1 GLN B 26 -36.922 7.845 -4.023 1.00 62.36 O ANISOU 2894 OE1 GLN B 26 6144 8627 8922 -1107 -711 333 O ATOM 2895 NE2 GLN B 26 -38.969 7.310 -3.264 1.00 68.33 N ANISOU 2895 NE2 GLN B 26 6517 9628 9819 -1315 -682 419 N ATOM 2896 N LYS B 27 -36.456 10.467 1.164 1.00 50.25 N ANISOU 2896 N LYS B 27 4539 7235 7318 -734 -18 521 N ATOM 2897 CA LYS B 27 -36.833 11.633 1.964 1.00 49.62 C ANISOU 2897 CA LYS B 27 4378 7261 7214 -570 113 542 C ATOM 2898 C LYS B 27 -36.543 12.934 1.214 1.00 47.43 C ANISOU 2898 C LYS B 27 4150 6973 6896 -365 71 493 C ATOM 2899 O LYS B 27 -37.403 13.801 1.101 1.00 48.66 O ANISOU 2899 O LYS B 27 4160 7258 7070 -237 91 504 O ATOM 2900 CB LYS B 27 -36.076 11.633 3.299 1.00 49.43 C ANISOU 2900 CB LYS B 27 4490 7165 7127 -558 254 561 C ATOM 2901 CG LYS B 27 -36.641 10.588 4.290 0.00 52.42 C ANISOU 2901 CG LYS B 27 4787 7592 7536 -728 341 634 C ATOM 2902 CD LYS B 27 -35.570 10.019 5.214 0.00 51.55 C ANISOU 2902 CD LYS B 27 4880 7347 7359 -778 404 649 C ATOM 2903 CE LYS B 27 -34.927 11.089 6.082 0.00 50.72 C ANISOU 2903 CE LYS B 27 4877 7231 7162 -609 512 626 C ATOM 2904 NZ LYS B 27 -33.986 10.503 7.076 0.00 50.13 N ANISOU 2904 NZ LYS B 27 4976 7054 7016 -660 569 648 N ATOM 2905 N ASP B 28 -35.327 13.059 0.701 1.00 43.40 N ANISOU 2905 N ASP B 28 3848 6310 6331 -332 15 444 N ATOM 2906 CA ASP B 28 -34.919 14.266 -0.004 1.00 41.75 C ANISOU 2906 CA ASP B 28 3719 6067 6077 -157 -17 405 C ATOM 2907 C ASP B 28 -35.434 14.325 -1.436 1.00 40.59 C ANISOU 2907 C ASP B 28 3504 5966 5953 -137 -165 389 C ATOM 2908 O ASP B 28 -35.564 15.409 -1.990 1.00 40.31 O ANISOU 2908 O ASP B 28 3473 5952 5892 23 -185 379 O ATOM 2909 CB ASP B 28 -33.392 14.416 0.016 1.00 40.45 C ANISOU 2909 CB ASP B 28 3790 5736 5842 -138 -9 363 C ATOM 2910 CG ASP B 28 -32.880 15.013 1.317 1.00 41.96 C ANISOU 2910 CG ASP B 28 4060 5897 5985 -75 130 366 C ATOM 2911 OD1 ASP B 28 -33.702 15.525 2.106 1.00 45.76 O ANISOU 2911 OD1 ASP B 28 4433 6478 6475 -8 227 392 O ATOM 2912 OD2 ASP B 28 -31.654 14.977 1.555 1.00 41.99 O ANISOU 2912 OD2 ASP B 28 4231 5787 5937 -87 142 338 O ATOM 2913 N LEU B 29 -35.745 13.175 -2.026 1.00 41.34 N ANISOU 2913 N LEU B 29 3546 6071 6090 -297 -272 386 N ATOM 2914 CA LEU B 29 -36.205 13.130 -3.415 1.00 43.14 C ANISOU 2914 CA LEU B 29 3721 6343 6325 -293 -430 363 C ATOM 2915 C LEU B 29 -37.651 13.605 -3.601 1.00 46.85 C ANISOU 2915 C LEU B 29 3941 7012 6849 -231 -460 398 C ATOM 2916 O LEU B 29 -38.146 13.649 -4.725 1.00 46.46 O ANISOU 2916 O LEU B 29 3827 7025 6801 -213 -600 383 O ATOM 2917 CB LEU B 29 -36.034 11.723 -3.999 1.00 43.93 C ANISOU 2917 CB LEU B 29 3869 6377 6445 -490 -543 336 C ATOM 2918 CG LEU B 29 -34.595 11.259 -4.219 1.00 43.54 C ANISOU 2918 CG LEU B 29 4068 6141 6335 -518 -552 292 C ATOM 2919 CD1 LEU B 29 -34.577 9.811 -4.658 1.00 47.25 C ANISOU 2919 CD1 LEU B 29 4582 6543 6829 -707 -651 266 C ATOM 2920 CD2 LEU B 29 -33.883 12.138 -5.245 1.00 44.00 C ANISOU 2920 CD2 LEU B 29 4256 6146 6316 -370 -605 254 C ATOM 2921 N LYS B 30 -38.326 13.942 -2.505 1.00 49.55 N ANISOU 2921 N LYS B 30 4138 7461 7227 -192 -329 443 N ATOM 2922 CA LYS B 30 -39.636 14.587 -2.569 1.00 55.22 C ANISOU 2922 CA LYS B 30 4612 8380 7990 -83 -330 479 C ATOM 2923 C LYS B 30 -39.497 16.067 -2.921 1.00 55.27 C ANISOU 2923 C LYS B 30 4685 8376 7940 178 -315 470 C ATOM 2924 O LYS B 30 -40.447 16.691 -3.390 1.00 58.10 O ANISOU 2924 O LYS B 30 4879 8878 8318 308 -364 492 O ATOM 2925 CB LYS B 30 -40.384 14.418 -1.239 1.00 56.88 C ANISOU 2925 CB LYS B 30 4648 8714 8251 -124 -175 532 C ATOM 2926 CG LYS B 30 -40.893 12.995 -1.021 1.00 63.38 C ANISOU 2926 CG LYS B 30 5347 9589 9146 -389 -203 559 C ATOM 2927 CD LYS B 30 -41.434 12.764 0.396 1.00 70.61 C ANISOU 2927 CD LYS B 30 6133 10601 10094 -446 -23 621 C ATOM 2928 CE LYS B 30 -40.307 12.621 1.420 1.00 70.56 C ANISOU 2928 CE LYS B 30 6361 10426 10022 -462 104 618 C ATOM 2929 NZ LYS B 30 -40.727 11.841 2.627 1.00 70.17 N ANISOU 2929 NZ LYS B 30 6225 10436 10001 -613 239 682 N ATOM 2930 N PHE B 31 -38.305 16.615 -2.688 1.00 54.30 N ANISOU 2930 N PHE B 31 4805 8081 7747 251 -249 442 N ATOM 2931 CA PHE B 31 -38.000 18.015 -2.981 1.00 53.27 C ANISOU 2931 CA PHE B 31 4789 7895 7557 476 -226 433 C ATOM 2932 C PHE B 31 -37.192 18.152 -4.267 1.00 49.92 C ANISOU 2932 C PHE B 31 4542 7351 7075 491 -351 402 C ATOM 2933 O PHE B 31 -37.410 19.067 -5.056 1.00 50.62 O ANISOU 2933 O PHE B 31 4653 7451 7129 652 -407 410 O ATOM 2934 CB PHE B 31 -37.214 18.620 -1.813 1.00 53.01 C ANISOU 2934 CB PHE B 31 4909 7752 7480 536 -64 420 C ATOM 2935 CG PHE B 31 -37.950 18.569 -0.497 1.00 56.86 C ANISOU 2935 CG PHE B 31 5250 8354 8002 541 78 449 C ATOM 2936 CD1 PHE B 31 -38.803 19.602 -0.122 1.00 60.66 C ANISOU 2936 CD1 PHE B 31 5625 8939 8485 742 158 469 C ATOM 2937 CD2 PHE B 31 -37.800 17.482 0.359 1.00 59.00 C ANISOU 2937 CD2 PHE B 31 5494 8628 8294 356 136 461 C ATOM 2938 CE1 PHE B 31 -39.488 19.556 1.090 1.00 63.16 C ANISOU 2938 CE1 PHE B 31 5803 9372 8822 756 303 495 C ATOM 2939 CE2 PHE B 31 -38.483 17.429 1.576 1.00 60.57 C ANISOU 2939 CE2 PHE B 31 5562 8939 8511 359 278 496 C ATOM 2940 CZ PHE B 31 -39.327 18.467 1.940 1.00 61.83 C ANISOU 2940 CZ PHE B 31 5609 9214 8670 558 365 511 C ATOM 2941 N LEU B 32 -36.252 17.238 -4.468 1.00 47.72 N ANISOU 2941 N LEU B 32 4396 6959 6779 331 -389 370 N ATOM 2942 CA LEU B 32 -35.345 17.298 -5.604 1.00 45.10 C ANISOU 2942 CA LEU B 32 4246 6510 6381 337 -482 338 C ATOM 2943 C LEU B 32 -35.578 16.096 -6.491 1.00 44.05 C ANISOU 2943 C LEU B 32 4065 6408 6264 185 -628 316 C ATOM 2944 O LEU B 32 -35.868 15.011 -6.001 1.00 43.66 O ANISOU 2944 O LEU B 32 3929 6388 6270 22 -628 315 O ATOM 2945 CB LEU B 32 -33.903 17.283 -5.110 1.00 41.70 C ANISOU 2945 CB LEU B 32 4026 5914 5904 296 -397 309 C ATOM 2946 CG LEU B 32 -33.481 18.423 -4.177 1.00 43.44 C ANISOU 2946 CG LEU B 32 4330 6077 6098 417 -258 315 C ATOM 2947 CD1 LEU B 32 -32.317 17.973 -3.312 1.00 38.72 C ANISOU 2947 CD1 LEU B 32 3859 5370 5481 315 -177 290 C ATOM 2948 CD2 LEU B 32 -33.127 19.712 -4.963 1.00 38.52 C ANISOU 2948 CD2 LEU B 32 3839 5383 5414 578 -272 316 C ATOM 2949 N SER B 33 -35.447 16.284 -7.798 1.00 43.30 N ANISOU 2949 N SER B 33 4042 6298 6113 234 -751 299 N ATOM 2950 CA SER B 33 -35.429 15.153 -8.715 1.00 43.87 C ANISOU 2950 CA SER B 33 4131 6364 6175 92 -892 260 C ATOM 2951 C SER B 33 -34.106 14.414 -8.522 1.00 41.19 C ANISOU 2951 C SER B 33 3983 5862 5805 -14 -846 221 C ATOM 2952 O SER B 33 -33.176 14.944 -7.915 1.00 39.68 O ANISOU 2952 O SER B 33 3912 5576 5587 42 -729 225 O ATOM 2953 CB SER B 33 -35.568 15.622 -10.163 1.00 45.36 C ANISOU 2953 CB SER B 33 4369 6578 6288 192 -1029 252 C ATOM 2954 OG SER B 33 -34.424 16.361 -10.560 1.00 44.92 O ANISOU 2954 OG SER B 33 4532 6393 6145 293 -979 246 O ATOM 2955 N GLU B 34 -34.025 13.194 -9.038 1.00 41.43 N ANISOU 2955 N GLU B 34 4043 5861 5836 -163 -943 179 N ATOM 2956 CA GLU B 34 -32.790 12.413 -8.986 1.00 41.80 C ANISOU 2956 CA GLU B 34 4274 5758 5849 -243 -914 139 C ATOM 2957 C GLU B 34 -31.645 13.145 -9.672 1.00 40.06 C ANISOU 2957 C GLU B 34 4239 5450 5533 -124 -892 122 C ATOM 2958 O GLU B 34 -30.519 13.139 -9.190 1.00 38.39 O ANISOU 2958 O GLU B 34 4150 5138 5299 -121 -798 113 O ATOM 2959 CB GLU B 34 -32.987 11.050 -9.646 1.00 43.85 C ANISOU 2959 CB GLU B 34 4554 5992 6114 -399 -1040 89 C ATOM 2960 CG GLU B 34 -33.867 10.104 -8.845 1.00 52.26 C ANISOU 2960 CG GLU B 34 5472 7105 7278 -566 -1042 107 C ATOM 2961 CD GLU B 34 -33.965 8.715 -9.461 1.00 62.71 C ANISOU 2961 CD GLU B 34 6854 8366 8606 -738 -1165 52 C ATOM 2962 OE1 GLU B 34 -34.909 7.976 -9.094 1.00 67.62 O ANISOU 2962 OE1 GLU B 34 7338 9046 9309 -893 -1203 66 O ATOM 2963 OE2 GLU B 34 -33.106 8.365 -10.307 1.00 63.65 O ANISOU 2963 OE2 GLU B 34 7159 8377 8646 -720 -1220 -7 O ATOM 2964 N GLU B 35 -31.946 13.767 -10.808 1.00 41.36 N ANISOU 2964 N GLU B 35 4418 5660 5636 -28 -981 121 N ATOM 2965 CA GLU B 35 -30.959 14.528 -11.552 1.00 39.85 C ANISOU 2965 CA GLU B 35 4399 5395 5347 82 -958 117 C ATOM 2966 C GLU B 35 -30.403 15.661 -10.684 1.00 37.08 C ANISOU 2966 C GLU B 35 4085 5000 5003 176 -810 157 C ATOM 2967 O GLU B 35 -29.190 15.837 -10.566 1.00 34.63 O ANISOU 2967 O GLU B 35 3911 4593 4652 181 -731 146 O ATOM 2968 CB GLU B 35 -31.584 15.067 -12.838 1.00 41.27 C ANISOU 2968 CB GLU B 35 4575 5647 5458 177 -1080 126 C ATOM 2969 CG GLU B 35 -30.625 15.822 -13.742 1.00 47.49 C ANISOU 2969 CG GLU B 35 5550 6363 6131 282 -1059 132 C ATOM 2970 CD GLU B 35 -31.206 16.073 -15.122 1.00 54.68 C ANISOU 2970 CD GLU B 35 6481 7342 6952 357 -1201 135 C ATOM 2971 OE1 GLU B 35 -31.511 17.241 -15.435 1.00 57.47 O ANISOU 2971 OE1 GLU B 35 6843 7724 7268 500 -1197 192 O ATOM 2972 OE2 GLU B 35 -31.376 15.099 -15.886 1.00 62.92 O ANISOU 2972 OE2 GLU B 35 7544 8406 7958 276 -1322 81 O ATOM 2973 N GLU B 36 -31.298 16.405 -10.050 1.00 35.27 N ANISOU 2973 N GLU B 36 3728 4846 4826 247 -774 199 N ATOM 2974 CA GLU B 36 -30.898 17.509 -9.180 1.00 35.39 C ANISOU 2974 CA GLU B 36 3786 4815 4846 339 -640 228 C ATOM 2975 C GLU B 36 -30.071 17.028 -7.994 1.00 34.61 C ANISOU 2975 C GLU B 36 3723 4647 4778 245 -532 210 C ATOM 2976 O GLU B 36 -29.135 17.709 -7.560 1.00 32.52 O ANISOU 2976 O GLU B 36 3570 4301 4485 281 -438 210 O ATOM 2977 CB GLU B 36 -32.135 18.269 -8.695 1.00 34.59 C ANISOU 2977 CB GLU B 36 3531 4816 4794 443 -622 270 C ATOM 2978 CG GLU B 36 -32.776 19.080 -9.794 1.00 35.86 C ANISOU 2978 CG GLU B 36 3685 5030 4908 584 -712 300 C ATOM 2979 CD GLU B 36 -34.131 19.631 -9.418 1.00 40.01 C ANISOU 2979 CD GLU B 36 4025 5688 5488 695 -717 339 C ATOM 2980 OE1 GLU B 36 -34.750 19.113 -8.471 1.00 43.46 O ANISOU 2980 OE1 GLU B 36 4303 6205 6004 627 -675 340 O ATOM 2981 OE2 GLU B 36 -34.587 20.576 -10.089 1.00 45.31 O ANISOU 2981 OE2 GLU B 36 4708 6387 6119 856 -762 375 O ATOM 2982 N TYR B 37 -30.418 15.856 -7.470 1.00 35.09 N ANISOU 2982 N TYR B 37 3696 4741 4896 120 -550 198 N ATOM 2983 CA TYR B 37 -29.650 15.274 -6.374 1.00 35.25 C ANISOU 2983 CA TYR B 37 3758 4698 4936 35 -461 187 C ATOM 2984 C TYR B 37 -28.200 14.966 -6.790 1.00 33.71 C ANISOU 2984 C TYR B 37 3730 4395 4682 10 -455 152 C ATOM 2985 O TYR B 37 -27.275 15.329 -6.065 1.00 35.32 O ANISOU 2985 O TYR B 37 4006 4543 4870 20 -364 151 O ATOM 2986 CB TYR B 37 -30.334 14.026 -5.798 1.00 34.50 C ANISOU 2986 CB TYR B 37 3551 4647 4909 -100 -484 191 C ATOM 2987 CG TYR B 37 -29.833 13.691 -4.413 1.00 31.99 C ANISOU 2987 CG TYR B 37 3253 4289 4611 -154 -374 203 C ATOM 2988 CD1 TYR B 37 -30.479 14.176 -3.284 1.00 33.80 C ANISOU 2988 CD1 TYR B 37 3382 4586 4875 -126 -280 238 C ATOM 2989 CD2 TYR B 37 -28.698 12.919 -4.233 1.00 32.80 C ANISOU 2989 CD2 TYR B 37 3479 4295 4689 -218 -362 180 C ATOM 2990 CE1 TYR B 37 -30.016 13.890 -2.010 1.00 34.35 C ANISOU 2990 CE1 TYR B 37 3482 4624 4944 -170 -182 250 C ATOM 2991 CE2 TYR B 37 -28.222 12.623 -2.963 1.00 35.66 C ANISOU 2991 CE2 TYR B 37 3865 4627 5058 -257 -272 195 C ATOM 2992 CZ TYR B 37 -28.885 13.114 -1.851 1.00 38.26 C ANISOU 2992 CZ TYR B 37 4102 5022 5413 -237 -185 231 C ATOM 2993 OH TYR B 37 -28.421 12.822 -0.581 1.00 34.69 O ANISOU 2993 OH TYR B 37 3683 4546 4951 -272 -99 248 O ATOM 2994 N TRP B 38 -27.994 14.338 -7.951 1.00 34.62 N ANISOU 2994 N TRP B 38 3904 4491 4759 -18 -551 123 N ATOM 2995 CA TRP B 38 -26.619 14.079 -8.417 1.00 36.53 C ANISOU 2995 CA TRP B 38 4295 4647 4939 -22 -534 91 C ATOM 2996 C TRP B 38 -25.872 15.346 -8.853 1.00 35.01 C ANISOU 2996 C TRP B 38 4194 4425 4683 77 -480 104 C ATOM 2997 O TRP B 38 -24.646 15.366 -8.850 1.00 35.04 O ANISOU 2997 O TRP B 38 4292 4373 4649 72 -426 89 O ATOM 2998 CB TRP B 38 -26.501 12.940 -9.462 1.00 37.46 C ANISOU 2998 CB TRP B 38 4472 4741 5022 -76 -637 45 C ATOM 2999 CG TRP B 38 -27.110 13.080 -10.863 1.00 41.74 C ANISOU 2999 CG TRP B 38 5026 5325 5509 -37 -751 31 C ATOM 3000 CD1 TRP B 38 -28.168 12.358 -11.358 1.00 43.97 C ANISOU 3000 CD1 TRP B 38 5236 5658 5812 -100 -873 11 C ATOM 3001 CD2 TRP B 38 -26.637 13.886 -11.965 1.00 41.76 C ANISOU 3001 CD2 TRP B 38 5129 5322 5418 59 -762 34 C ATOM 3002 NE1 TRP B 38 -28.405 12.695 -12.668 1.00 42.91 N ANISOU 3002 NE1 TRP B 38 5148 5557 5598 -38 -966 -2 N ATOM 3003 CE2 TRP B 38 -27.487 13.628 -13.066 1.00 41.25 C ANISOU 3003 CE2 TRP B 38 5049 5311 5313 65 -896 16 C ATOM 3004 CE3 TRP B 38 -25.605 14.820 -12.119 1.00 43.73 C ANISOU 3004 CE3 TRP B 38 5477 5530 5610 132 -672 54 C ATOM 3005 CZ2 TRP B 38 -27.330 14.263 -14.305 1.00 44.58 C ANISOU 3005 CZ2 TRP B 38 5564 5746 5630 156 -940 22 C ATOM 3006 CZ3 TRP B 38 -25.454 15.457 -13.355 1.00 44.01 C ANISOU 3006 CZ3 TRP B 38 5601 5571 5549 212 -705 65 C ATOM 3007 CH2 TRP B 38 -26.316 15.175 -14.428 1.00 43.76 C ANISOU 3007 CH2 TRP B 38 5564 5593 5470 230 -837 51 C ATOM 3008 N LYS B 39 -26.603 16.398 -9.202 1.00 35.58 N ANISOU 3008 N LYS B 39 4237 4537 4747 165 -493 136 N ATOM 3009 CA LYS B 39 -25.985 17.702 -9.460 1.00 33.34 C ANISOU 3009 CA LYS B 39 4050 4207 4410 252 -429 160 C ATOM 3010 C LYS B 39 -25.510 18.332 -8.149 1.00 32.77 C ANISOU 3010 C LYS B 39 3983 4095 4372 248 -314 167 C ATOM 3011 O LYS B 39 -24.370 18.783 -8.048 1.00 31.18 O ANISOU 3011 O LYS B 39 3878 3831 4136 237 -248 161 O ATOM 3012 CB LYS B 39 -26.946 18.607 -10.227 1.00 32.02 C ANISOU 3012 CB LYS B 39 3867 4081 4219 362 -484 198 C ATOM 3013 CG LYS B 39 -27.090 18.173 -11.671 1.00 30.95 C ANISOU 3013 CG LYS B 39 3774 3971 4013 374 -595 188 C ATOM 3014 CD LYS B 39 -28.185 18.917 -12.417 1.00 35.25 C ANISOU 3014 CD LYS B 39 4282 4579 4532 488 -675 229 C ATOM 3015 CE LYS B 39 -28.213 18.488 -13.877 1.00 34.32 C ANISOU 3015 CE LYS B 39 4230 4487 4323 497 -791 214 C ATOM 3016 NZ LYS B 39 -29.329 19.095 -14.669 1.00 31.87 N ANISOU 3016 NZ LYS B 39 3876 4256 3977 611 -896 254 N ATOM 3017 N LEU B 40 -26.367 18.311 -7.135 1.00 34.86 N ANISOU 3017 N LEU B 40 4141 4405 4699 247 -291 177 N ATOM 3018 CA LEU B 40 -26.006 18.787 -5.788 1.00 34.07 C ANISOU 3018 CA LEU B 40 4048 4277 4622 240 -187 175 C ATOM 3019 C LEU B 40 -24.749 18.107 -5.234 1.00 34.20 C ANISOU 3019 C LEU B 40 4118 4248 4627 148 -149 146 C ATOM 3020 O LEU B 40 -23.902 18.766 -4.616 1.00 33.85 O ANISOU 3020 O LEU B 40 4140 4157 4563 146 -78 137 O ATOM 3021 CB LEU B 40 -27.169 18.549 -4.828 1.00 35.35 C ANISOU 3021 CB LEU B 40 4075 4514 4845 242 -169 189 C ATOM 3022 CG LEU B 40 -27.352 19.493 -3.649 1.00 40.62 C ANISOU 3022 CG LEU B 40 4741 5173 5520 301 -68 194 C ATOM 3023 CD1 LEU B 40 -27.490 20.937 -4.111 1.00 44.00 C ANISOU 3023 CD1 LEU B 40 5246 5556 5916 429 -47 208 C ATOM 3024 CD2 LEU B 40 -28.590 19.083 -2.879 1.00 44.24 C ANISOU 3024 CD2 LEU B 40 5046 5732 6033 303 -51 214 C ATOM 3025 N GLN B 41 -24.642 16.795 -5.454 1.00 32.43 N ANISOU 3025 N GLN B 41 3868 4039 4416 76 -203 131 N ATOM 3026 CA GLN B 41 -23.479 16.012 -5.028 1.00 33.29 C ANISOU 3026 CA GLN B 41 4025 4112 4513 10 -180 108 C ATOM 3027 C GLN B 41 -22.203 16.446 -5.740 1.00 31.30 C ANISOU 3027 C GLN B 41 3873 3818 4203 26 -161 93 C ATOM 3028 O GLN B 41 -21.142 16.538 -5.127 1.00 32.01 O ANISOU 3028 O GLN B 41 3995 3887 4280 0 -108 82 O ATOM 3029 CB GLN B 41 -23.693 14.518 -5.312 1.00 34.32 C ANISOU 3029 CB GLN B 41 4131 4246 4662 -55 -250 95 C ATOM 3030 CG GLN B 41 -24.630 13.800 -4.361 1.00 40.28 C ANISOU 3030 CG GLN B 41 4794 5034 5478 -114 -250 114 C ATOM 3031 CD GLN B 41 -24.881 12.361 -4.802 1.00 48.66 C ANISOU 3031 CD GLN B 41 5856 6076 6558 -191 -328 100 C ATOM 3032 OE1 GLN B 41 -25.456 12.115 -5.865 1.00 55.51 O ANISOU 3032 OE1 GLN B 41 6713 6956 7422 -196 -412 85 O ATOM 3033 NE2 GLN B 41 -24.446 11.407 -3.989 1.00 46.05 N ANISOU 3033 NE2 GLN B 41 5549 5706 6242 -251 -306 103 N ATOM 3034 N ILE B 42 -22.300 16.659 -7.048 1.00 31.89 N ANISOU 3034 N ILE B 42 3989 3890 4238 65 -207 95 N ATOM 3035 CA ILE B 42 -21.165 17.150 -7.814 1.00 32.19 C ANISOU 3035 CA ILE B 42 4118 3898 4215 80 -176 92 C ATOM 3036 C ILE B 42 -20.718 18.485 -7.213 1.00 31.11 C ANISOU 3036 C ILE B 42 4017 3728 4074 90 -94 109 C ATOM 3037 O ILE B 42 -19.530 18.729 -7.018 1.00 29.66 O ANISOU 3037 O ILE B 42 3874 3527 3870 53 -40 99 O ATOM 3038 CB ILE B 42 -21.514 17.378 -9.291 1.00 32.23 C ANISOU 3038 CB ILE B 42 4174 3908 4163 133 -231 103 C ATOM 3039 CG1 ILE B 42 -21.681 16.043 -10.023 1.00 35.53 C ANISOU 3039 CG1 ILE B 42 4591 4346 4564 113 -314 69 C ATOM 3040 CG2 ILE B 42 -20.424 18.211 -9.974 1.00 31.68 C ANISOU 3040 CG2 ILE B 42 4201 3808 4026 149 -171 118 C ATOM 3041 CD1 ILE B 42 -22.195 16.186 -11.454 1.00 32.61 C ANISOU 3041 CD1 ILE B 42 4270 3994 4127 165 -389 74 C ATOM 3042 N PHE B 43 -21.699 19.326 -6.918 1.00 30.68 N ANISOU 3042 N PHE B 43 3946 3668 4041 141 -88 131 N ATOM 3043 CA PHE B 43 -21.455 20.676 -6.452 1.00 30.80 C ANISOU 3043 CA PHE B 43 4023 3630 4048 163 -18 143 C ATOM 3044 C PHE B 43 -20.664 20.684 -5.145 1.00 30.37 C ANISOU 3044 C PHE B 43 3963 3563 4011 96 42 115 C ATOM 3045 O PHE B 43 -19.638 21.366 -5.044 1.00 30.25 O ANISOU 3045 O PHE B 43 4016 3506 3971 55 91 107 O ATOM 3046 CB PHE B 43 -22.781 21.432 -6.296 1.00 29.23 C ANISOU 3046 CB PHE B 43 3802 3433 3872 254 -25 168 C ATOM 3047 CG PHE B 43 -22.617 22.807 -5.725 1.00 32.69 C ANISOU 3047 CG PHE B 43 4326 3795 4302 288 49 172 C ATOM 3048 CD1 PHE B 43 -22.111 23.831 -6.507 1.00 29.49 C ANISOU 3048 CD1 PHE B 43 4044 3311 3850 310 72 197 C ATOM 3049 CD2 PHE B 43 -22.922 23.066 -4.393 1.00 26.28 C ANISOU 3049 CD2 PHE B 43 3485 2980 3519 292 98 150 C ATOM 3050 CE1 PHE B 43 -21.941 25.098 -5.986 1.00 34.24 C ANISOU 3050 CE1 PHE B 43 4748 3819 4444 330 138 198 C ATOM 3051 CE2 PHE B 43 -22.749 24.332 -3.866 1.00 31.39 C ANISOU 3051 CE2 PHE B 43 4234 3542 4151 322 163 142 C ATOM 3052 CZ PHE B 43 -22.253 25.351 -4.673 1.00 32.10 C ANISOU 3052 CZ PHE B 43 4455 3539 4203 338 180 165 C ATOM 3053 N PHE B 44 -21.128 19.918 -4.159 1.00 29.51 N ANISOU 3053 N PHE B 44 3775 3497 3941 76 34 102 N ATOM 3054 CA PHE B 44 -20.467 19.887 -2.841 1.00 29.55 C ANISOU 3054 CA PHE B 44 3778 3501 3950 22 81 77 C ATOM 3055 C PHE B 44 -19.132 19.144 -2.851 1.00 28.79 C ANISOU 3055 C PHE B 44 3684 3420 3835 -44 75 58 C ATOM 3056 O PHE B 44 -18.226 19.491 -2.090 1.00 26.63 O ANISOU 3056 O PHE B 44 3431 3141 3546 -90 109 38 O ATOM 3057 CB PHE B 44 -21.413 19.369 -1.744 1.00 27.77 C ANISOU 3057 CB PHE B 44 3476 3318 3757 29 88 79 C ATOM 3058 CG PHE B 44 -22.434 20.384 -1.344 1.00 32.51 C ANISOU 3058 CG PHE B 44 4078 3909 4367 103 127 87 C ATOM 3059 CD1 PHE B 44 -22.049 21.526 -0.659 1.00 38.06 C ANISOU 3059 CD1 PHE B 44 4862 4558 5042 115 187 64 C ATOM 3060 CD2 PHE B 44 -23.760 20.245 -1.705 1.00 37.00 C ANISOU 3060 CD2 PHE B 44 4568 4522 4967 164 100 115 C ATOM 3061 CE1 PHE B 44 -22.971 22.490 -0.318 1.00 38.36 C ANISOU 3061 CE1 PHE B 44 4918 4574 5082 205 229 67 C ATOM 3062 CE2 PHE B 44 -24.688 21.210 -1.358 1.00 41.55 C ANISOU 3062 CE2 PHE B 44 5137 5099 5550 257 141 123 C ATOM 3063 CZ PHE B 44 -24.289 22.333 -0.669 1.00 35.05 C ANISOU 3063 CZ PHE B 44 4412 4209 4696 286 209 99 C ATOM 3064 N THR B 45 -19.000 18.142 -3.715 1.00 29.05 N ANISOU 3064 N THR B 45 3697 3474 3865 -44 27 62 N ATOM 3065 CA THR B 45 -17.679 17.593 -4.019 1.00 28.61 C ANISOU 3065 CA THR B 45 3653 3434 3784 -77 29 47 C ATOM 3066 C THR B 45 -16.722 18.721 -4.408 1.00 27.07 C ANISOU 3066 C THR B 45 3510 3221 3556 -99 78 47 C ATOM 3067 O THR B 45 -15.610 18.805 -3.890 1.00 23.65 O ANISOU 3067 O THR B 45 3065 2809 3113 -149 106 31 O ATOM 3068 CB THR B 45 -17.721 16.566 -5.188 1.00 30.05 C ANISOU 3068 CB THR B 45 3839 3627 3953 -52 -23 44 C ATOM 3069 OG1 THR B 45 -18.596 15.486 -4.858 1.00 32.10 O ANISOU 3069 OG1 THR B 45 4059 3890 4247 -54 -73 44 O ATOM 3070 CG2 THR B 45 -16.319 16.005 -5.485 1.00 26.25 C ANISOU 3070 CG2 THR B 45 3365 3169 3440 -62 -8 27 C ATOM 3071 N ASN B 46 -17.152 19.573 -5.338 1.00 28.33 N ANISOU 3071 N ASN B 46 3725 3342 3696 -67 86 69 N ATOM 3072 CA ASN B 46 -16.310 20.683 -5.820 1.00 29.50 C ANISOU 3072 CA ASN B 46 3941 3457 3811 -100 140 81 C ATOM 3073 C ASN B 46 -16.017 21.734 -4.734 1.00 30.68 C ANISOU 3073 C ASN B 46 4122 3564 3973 -152 186 66 C ATOM 3074 O ASN B 46 -14.922 22.298 -4.688 1.00 29.85 O ANISOU 3074 O ASN B 46 4038 3451 3850 -228 226 60 O ATOM 3075 CB ASN B 46 -16.926 21.345 -7.067 1.00 27.96 C ANISOU 3075 CB ASN B 46 3820 3220 3584 -42 135 120 C ATOM 3076 CG ASN B 46 -16.892 20.431 -8.305 1.00 30.82 C ANISOU 3076 CG ASN B 46 4178 3625 3907 -6 94 126 C ATOM 3077 OD1 ASN B 46 -16.059 19.535 -8.411 1.00 33.26 O ANISOU 3077 OD1 ASN B 46 4449 3981 4205 -31 95 103 O ATOM 3078 ND2 ASN B 46 -17.793 20.670 -9.244 1.00 26.08 N ANISOU 3078 ND2 ASN B 46 3621 3008 3279 62 55 153 N ATOM 3079 N VAL B 47 -16.990 21.987 -3.863 1.00 31.86 N ANISOU 3079 N VAL B 47 4270 3689 4148 -117 180 58 N ATOM 3080 CA VAL B 47 -16.819 22.941 -2.769 1.00 32.11 C ANISOU 3080 CA VAL B 47 4348 3673 4180 -154 220 31 C ATOM 3081 C VAL B 47 -15.741 22.446 -1.818 1.00 33.55 C ANISOU 3081 C VAL B 47 4479 3911 4358 -238 219 -5 C ATOM 3082 O VAL B 47 -14.865 23.212 -1.413 1.00 35.42 O ANISOU 3082 O VAL B 47 4756 4124 4579 -318 246 -29 O ATOM 3083 CB VAL B 47 -18.136 23.139 -1.986 1.00 34.01 C ANISOU 3083 CB VAL B 47 4585 3897 4440 -79 222 27 C ATOM 3084 CG1 VAL B 47 -17.878 23.801 -0.635 1.00 32.72 C ANISOU 3084 CG1 VAL B 47 4466 3703 4265 -117 259 -17 C ATOM 3085 CG2 VAL B 47 -19.128 23.956 -2.812 1.00 33.93 C ANISOU 3085 CG2 VAL B 47 4635 3829 4430 15 226 61 C ATOM 3086 N ILE B 48 -15.814 21.165 -1.467 1.00 30.78 N ANISOU 3086 N ILE B 48 4044 3631 4019 -221 182 -7 N ATOM 3087 CA ILE B 48 -14.839 20.545 -0.580 1.00 30.38 C ANISOU 3087 CA ILE B 48 3941 3643 3959 -276 169 -32 C ATOM 3088 C ILE B 48 -13.447 20.531 -1.226 1.00 28.91 C ANISOU 3088 C ILE B 48 3730 3498 3758 -332 175 -34 C ATOM 3089 O ILE B 48 -12.462 20.851 -0.573 1.00 28.21 O ANISOU 3089 O ILE B 48 3622 3442 3656 -405 180 -59 O ATOM 3090 CB ILE B 48 -15.287 19.119 -0.156 1.00 31.13 C ANISOU 3090 CB ILE B 48 3971 3788 4069 -234 129 -21 C ATOM 3091 CG1 ILE B 48 -16.538 19.193 0.733 1.00 32.27 C ANISOU 3091 CG1 ILE B 48 4122 3915 4224 -200 139 -18 C ATOM 3092 CG2 ILE B 48 -14.185 18.387 0.600 1.00 27.36 C ANISOU 3092 CG2 ILE B 48 3445 3377 3573 -268 107 -36 C ATOM 3093 CD1 ILE B 48 -17.209 17.811 0.979 1.00 25.66 C ANISOU 3093 CD1 ILE B 48 3230 3112 3409 -173 107 7 C ATOM 3094 N GLN B 49 -13.365 20.204 -2.509 1.00 27.93 N ANISOU 3094 N GLN B 49 3602 3378 3630 -301 177 -9 N ATOM 3095 CA GLN B 49 -12.080 20.260 -3.217 1.00 28.95 C ANISOU 3095 CA GLN B 49 3703 3556 3740 -347 202 -5 C ATOM 3096 C GLN B 49 -11.476 21.674 -3.216 1.00 30.61 C ANISOU 3096 C GLN B 49 3964 3727 3941 -444 252 -7 C ATOM 3097 O GLN B 49 -10.265 21.830 -3.048 1.00 30.60 O ANISOU 3097 O GLN B 49 3908 3786 3932 -526 268 -19 O ATOM 3098 CB GLN B 49 -12.239 19.765 -4.653 1.00 29.03 C ANISOU 3098 CB GLN B 49 3727 3571 3732 -287 205 22 C ATOM 3099 CG GLN B 49 -10.970 19.874 -5.529 1.00 30.67 C ANISOU 3099 CG GLN B 49 3907 3836 3908 -323 253 33 C ATOM 3100 CD GLN B 49 -9.969 18.763 -5.276 1.00 32.22 C ANISOU 3100 CD GLN B 49 4003 4136 4104 -305 239 13 C ATOM 3101 OE1 GLN B 49 -10.330 17.667 -4.848 1.00 39.79 O ANISOU 3101 OE1 GLN B 49 4938 5105 5075 -241 189 -1 O ATOM 3102 NE2 GLN B 49 -8.703 19.036 -5.564 1.00 35.34 N ANISOU 3102 NE2 GLN B 49 4338 4608 4483 -359 288 17 N ATOM 3103 N ALA B 50 -12.318 22.692 -3.405 1.00 31.24 N ANISOU 3103 N ALA B 50 4146 3704 4020 -434 272 7 N ATOM 3104 CA ALA B 50 -11.867 24.087 -3.400 1.00 32.96 C ANISOU 3104 CA ALA B 50 4447 3847 4228 -526 320 6 C ATOM 3105 C ALA B 50 -11.380 24.491 -2.018 1.00 33.59 C ANISOU 3105 C ALA B 50 4519 3930 4313 -613 309 -46 C ATOM 3106 O ALA B 50 -10.331 25.111 -1.884 1.00 37.10 O ANISOU 3106 O ALA B 50 4960 4384 4751 -735 329 -61 O ATOM 3107 CB ALA B 50 -12.984 25.031 -3.874 1.00 32.37 C ANISOU 3107 CB ALA B 50 4502 3649 4149 -465 339 35 C ATOM 3108 N LEU B 51 -12.137 24.125 -0.988 1.00 34.69 N ANISOU 3108 N LEU B 51 4653 4070 4458 -556 275 -75 N ATOM 3109 CA LEU B 51 -11.717 24.361 0.392 1.00 35.38 C ANISOU 3109 CA LEU B 51 4736 4175 4531 -624 256 -129 C ATOM 3110 C LEU B 51 -10.357 23.722 0.656 1.00 35.87 C ANISOU 3110 C LEU B 51 4679 4362 4587 -700 226 -144 C ATOM 3111 O LEU B 51 -9.457 24.360 1.204 1.00 37.14 O ANISOU 3111 O LEU B 51 4838 4539 4736 -817 219 -180 O ATOM 3112 CB LEU B 51 -12.743 23.814 1.378 1.00 33.41 C ANISOU 3112 CB LEU B 51 4484 3933 4278 -535 232 -145 C ATOM 3113 CG LEU B 51 -14.077 24.560 1.449 1.00 39.84 C ANISOU 3113 CG LEU B 51 5400 4643 5096 -456 264 -142 C ATOM 3114 CD1 LEU B 51 -15.142 23.715 2.181 1.00 39.53 C ANISOU 3114 CD1 LEU B 51 5315 4647 5060 -361 251 -138 C ATOM 3115 CD2 LEU B 51 -13.895 25.897 2.126 1.00 33.38 C ANISOU 3115 CD2 LEU B 51 4702 3728 4251 -519 291 -192 C ATOM 3116 N GLY B 52 -10.211 22.466 0.247 1.00 34.51 N ANISOU 3116 N GLY B 52 4410 4279 4424 -630 203 -117 N ATOM 3117 CA GLY B 52 -8.962 21.748 0.422 1.00 33.72 C ANISOU 3117 CA GLY B 52 4187 4307 4317 -665 175 -124 C ATOM 3118 C GLY B 52 -7.788 22.401 -0.288 1.00 34.53 C ANISOU 3118 C GLY B 52 4249 4449 4422 -773 213 -118 C ATOM 3119 O GLY B 52 -6.710 22.506 0.277 1.00 34.89 O ANISOU 3119 O GLY B 52 4211 4584 4461 -861 190 -144 O ATOM 3120 N GLU B 53 -7.997 22.831 -1.531 1.00 34.20 N ANISOU 3120 N GLU B 53 4260 4349 4384 -768 269 -80 N ATOM 3121 CA GLU B 53 -6.935 23.448 -2.314 1.00 35.53 C ANISOU 3121 CA GLU B 53 4396 4554 4549 -874 324 -60 C ATOM 3122 C GLU B 53 -6.492 24.766 -1.699 1.00 37.03 C ANISOU 3122 C GLU B 53 4642 4686 4742 -1035 334 -89 C ATOM 3123 O GLU B 53 -5.292 25.022 -1.561 1.00 36.88 O ANISOU 3123 O GLU B 53 4530 4757 4727 -1162 340 -101 O ATOM 3124 CB GLU B 53 -7.367 23.645 -3.772 1.00 36.51 C ANISOU 3124 CB GLU B 53 4592 4617 4661 -825 384 -5 C ATOM 3125 CG GLU B 53 -7.442 22.335 -4.535 1.00 40.61 C ANISOU 3125 CG GLU B 53 5046 5216 5169 -695 376 15 C ATOM 3126 CD GLU B 53 -8.118 22.449 -5.895 1.00 44.34 C ANISOU 3126 CD GLU B 53 5611 5622 5613 -626 414 60 C ATOM 3127 OE1 GLU B 53 -8.536 23.556 -6.286 1.00 48.38 O ANISOU 3127 OE1 GLU B 53 6238 6029 6116 -668 450 88 O ATOM 3128 OE2 GLU B 53 -8.226 21.411 -6.577 1.00 45.53 O ANISOU 3128 OE2 GLU B 53 5729 5824 5745 -523 404 68 O ATOM 3129 N HIS B 54 -7.465 25.583 -1.305 1.00 35.08 N ANISOU 3129 N HIS B 54 4545 4292 4493 -1029 335 -105 N ATOM 3130 CA HIS B 54 -7.182 26.841 -0.642 1.00 36.25 C ANISOU 3130 CA HIS B 54 4785 4352 4638 -1171 339 -146 C ATOM 3131 C HIS B 54 -6.342 26.626 0.613 1.00 37.76 C ANISOU 3131 C HIS B 54 4879 4649 4820 -1260 273 -210 C ATOM 3132 O HIS B 54 -5.397 27.368 0.852 1.00 39.79 O ANISOU 3132 O HIS B 54 5121 4920 5078 -1428 272 -237 O ATOM 3133 CB HIS B 54 -8.481 27.558 -0.283 1.00 35.67 C ANISOU 3133 CB HIS B 54 4886 4110 4556 -1101 345 -162 C ATOM 3134 CG HIS B 54 -8.275 28.913 0.313 1.00 36.20 C ANISOU 3134 CG HIS B 54 5090 4051 4613 -1234 356 -209 C ATOM 3135 ND1 HIS B 54 -8.336 30.069 -0.433 1.00 45.57 N ANISOU 3135 ND1 HIS B 54 6423 5088 5802 -1298 416 -177 N ATOM 3136 CD2 HIS B 54 -7.996 29.297 1.580 1.00 36.41 C ANISOU 3136 CD2 HIS B 54 5145 4069 4619 -1317 311 -287 C ATOM 3137 CE1 HIS B 54 -8.118 31.108 0.352 1.00 43.38 C ANISOU 3137 CE1 HIS B 54 6265 4702 5513 -1418 410 -238 C ATOM 3138 NE2 HIS B 54 -7.908 30.667 1.578 1.00 38.88 N ANISOU 3138 NE2 HIS B 54 5626 4220 4928 -1433 344 -310 N ATOM 3139 N LEU B 55 -6.678 25.606 1.402 1.00 38.31 N ANISOU 3139 N LEU B 55 4883 4795 4877 -1152 215 -229 N ATOM 3140 CA LEU B 55 -5.920 25.297 2.615 1.00 39.47 C ANISOU 3140 CA LEU B 55 4940 5054 5001 -1211 141 -283 C ATOM 3141 C LEU B 55 -4.626 24.501 2.341 1.00 42.19 C ANISOU 3141 C LEU B 55 5087 5587 5356 -1238 117 -264 C ATOM 3142 O LEU B 55 -3.880 24.198 3.272 1.00 41.72 O ANISOU 3142 O LEU B 55 4930 5645 5275 -1281 46 -301 O ATOM 3143 CB LEU B 55 -6.804 24.542 3.608 1.00 39.66 C ANISOU 3143 CB LEU B 55 4990 5082 4998 -1082 95 -301 C ATOM 3144 CG LEU B 55 -7.978 25.311 4.235 1.00 38.89 C ANISOU 3144 CG LEU B 55 5063 4835 4877 -1051 112 -335 C ATOM 3145 CD1 LEU B 55 -8.924 24.329 4.922 1.00 34.69 C ANISOU 3145 CD1 LEU B 55 4526 4329 4325 -906 90 -325 C ATOM 3146 CD2 LEU B 55 -7.494 26.383 5.224 1.00 34.07 C ANISOU 3146 CD2 LEU B 55 4533 4183 4228 -1191 82 -413 C ATOM 3147 N LYS B 56 -4.370 24.170 1.074 1.00 43.64 N ANISOU 3147 N LYS B 56 5212 5805 5564 -1203 177 -208 N ATOM 3148 CA LYS B 56 -3.156 23.444 0.654 1.00 45.49 C ANISOU 3148 CA LYS B 56 5256 6220 5807 -1208 176 -186 C ATOM 3149 C LYS B 56 -3.065 22.061 1.305 1.00 43.72 C ANISOU 3149 C LYS B 56 4931 6111 5568 -1066 105 -190 C ATOM 3150 O LYS B 56 -2.005 21.635 1.762 1.00 45.32 O ANISOU 3150 O LYS B 56 4981 6473 5765 -1088 57 -203 O ATOM 3151 CB LYS B 56 -1.887 24.266 0.936 1.00 47.06 C ANISOU 3151 CB LYS B 56 5361 6508 6013 -1408 167 -213 C ATOM 3152 CG LYS B 56 -1.836 25.604 0.217 1.00 51.68 C ANISOU 3152 CG LYS B 56 6049 6973 6613 -1565 246 -198 C ATOM 3153 CD LYS B 56 -0.460 26.232 0.263 0.00 54.69 C ANISOU 3153 CD LYS B 56 6301 7469 7011 -1775 250 -210 C ATOM 3154 CE LYS B 56 0.497 25.600 -0.740 0.00 55.47 C ANISOU 3154 CE LYS B 56 6208 7745 7124 -1753 312 -153 C ATOM 3155 NZ LYS B 56 1.828 26.268 -0.737 0.00 57.56 N ANISOU 3155 NZ LYS B 56 6324 8135 7410 -1975 327 -158 N ATOM 3156 N LEU B 57 -4.191 21.365 1.347 1.00 41.77 N ANISOU 3156 N LEU B 57 4771 5784 5316 -923 97 -176 N ATOM 3157 CA LEU B 57 -4.227 20.024 1.906 1.00 39.41 C ANISOU 3157 CA LEU B 57 4410 5561 5003 -788 38 -169 C ATOM 3158 C LEU B 57 -3.922 19.043 0.780 1.00 38.95 C ANISOU 3158 C LEU B 57 4280 5561 4958 -676 74 -128 C ATOM 3159 O LEU B 57 -4.259 19.299 -0.374 1.00 37.48 O ANISOU 3159 O LEU B 57 4145 5313 4784 -668 141 -104 O ATOM 3160 CB LEU B 57 -5.593 19.741 2.530 1.00 37.40 C ANISOU 3160 CB LEU B 57 4282 5191 4737 -708 18 -171 C ATOM 3161 CG LEU B 57 -6.074 20.777 3.559 1.00 37.65 C ANISOU 3161 CG LEU B 57 4416 5146 4746 -796 2 -216 C ATOM 3162 CD1 LEU B 57 -7.500 20.489 4.031 1.00 35.76 C ANISOU 3162 CD1 LEU B 57 4286 4804 4496 -704 5 -209 C ATOM 3163 CD2 LEU B 57 -5.122 20.845 4.739 1.00 33.64 C ANISOU 3163 CD2 LEU B 57 3835 4749 4198 -868 -73 -258 C ATOM 3164 N ARG B 58 -3.265 17.937 1.117 1.00 38.25 N ANISOU 3164 N ARG B 58 4084 5591 4859 -581 28 -122 N ATOM 3165 CA ARG B 58 -3.029 16.854 0.160 1.00 37.25 C ANISOU 3165 CA ARG B 58 3911 5508 4736 -445 57 -93 C ATOM 3166 C ARG B 58 -4.344 16.202 -0.228 1.00 37.67 C ANISOU 3166 C ARG B 58 4100 5421 4792 -342 62 -77 C ATOM 3167 O ARG B 58 -5.326 16.270 0.514 1.00 36.73 O ANISOU 3167 O ARG B 58 4074 5209 4673 -348 30 -82 O ATOM 3168 CB ARG B 58 -2.087 15.799 0.741 1.00 38.18 C ANISOU 3168 CB ARG B 58 3900 5767 4837 -345 -2 -90 C ATOM 3169 CG ARG B 58 -0.603 16.212 0.617 0.00 41.69 C ANISOU 3169 CG ARG B 58 4159 6396 5285 -416 10 -96 C ATOM 3170 CD ARG B 58 0.324 15.009 0.508 0.00 42.80 C ANISOU 3170 CD ARG B 58 4165 6682 5415 -257 -10 -80 C ATOM 3171 NE ARG B 58 1.714 15.409 0.307 0.00 44.70 N ANISOU 3171 NE ARG B 58 4201 7119 5664 -322 11 -82 N ATOM 3172 CZ ARG B 58 2.705 14.563 0.048 0.00 46.07 C ANISOU 3172 CZ ARG B 58 4220 7453 5830 -188 15 -68 C ATOM 3173 NH1 ARG B 58 3.940 15.017 -0.120 0.00 47.82 N ANISOU 3173 NH1 ARG B 58 4235 7871 6063 -265 39 -68 N ATOM 3174 NH2 ARG B 58 2.463 13.263 -0.044 0.00 45.77 N ANISOU 3174 NH2 ARG B 58 4235 7380 5775 21 -4 -53 N ATOM 3175 N GLN B 59 -4.343 15.561 -1.395 1.00 36.49 N ANISOU 3175 N GLN B 59 3957 5266 4642 -251 104 -60 N ATOM 3176 CA GLN B 59 -5.555 15.043 -1.997 1.00 36.13 C ANISOU 3176 CA GLN B 59 4035 5093 4599 -177 108 -50 C ATOM 3177 C GLN B 59 -6.242 14.014 -1.105 1.00 34.91 C ANISOU 3177 C GLN B 59 3931 4886 4448 -100 42 -46 C ATOM 3178 O GLN B 59 -7.467 13.965 -1.068 1.00 32.00 O ANISOU 3178 O GLN B 59 3659 4407 4091 -100 32 -40 O ATOM 3179 CB GLN B 59 -5.264 14.455 -3.386 1.00 36.30 C ANISOU 3179 CB GLN B 59 4056 5133 4604 -89 157 -43 C ATOM 3180 CG GLN B 59 -6.509 14.130 -4.215 1.00 37.51 C ANISOU 3180 CG GLN B 59 4340 5159 4753 -41 158 -39 C ATOM 3181 CD GLN B 59 -7.395 15.348 -4.465 1.00 38.31 C ANISOU 3181 CD GLN B 59 4517 5174 4862 -136 180 -30 C ATOM 3182 OE1 GLN B 59 -6.918 16.396 -4.885 1.00 39.44 O ANISOU 3182 OE1 GLN B 59 4644 5344 4997 -217 235 -20 O ATOM 3183 NE2 GLN B 59 -8.696 15.199 -4.219 1.00 34.83 N ANISOU 3183 NE2 GLN B 59 4162 4632 4439 -123 140 -28 N ATOM 3184 N GLN B 60 -5.454 13.223 -0.380 1.00 34.84 N ANISOU 3184 N GLN B 60 3850 4961 4426 -36 -2 -44 N ATOM 3185 CA GLN B 60 -5.986 12.189 0.516 1.00 37.94 C ANISOU 3185 CA GLN B 60 4299 5304 4814 39 -61 -28 C ATOM 3186 C GLN B 60 -6.822 12.762 1.672 1.00 35.36 C ANISOU 3186 C GLN B 60 4027 4924 4484 -43 -87 -27 C ATOM 3187 O GLN B 60 -7.811 12.149 2.093 1.00 33.08 O ANISOU 3187 O GLN B 60 3821 4548 4198 -13 -106 -7 O ATOM 3188 CB GLN B 60 -4.845 11.318 1.074 1.00 40.70 C ANISOU 3188 CB GLN B 60 4560 5764 5140 136 -105 -18 C ATOM 3189 CG GLN B 60 -5.298 10.283 2.100 1.00 47.22 C ANISOU 3189 CG GLN B 60 5457 6536 5950 211 -167 10 C ATOM 3190 CD GLN B 60 -4.301 9.154 2.305 1.00 58.82 C ANISOU 3190 CD GLN B 60 6875 8080 7395 358 -207 29 C ATOM 3191 OE1 GLN B 60 -3.093 9.382 2.449 1.00 64.43 O ANISOU 3191 OE1 GLN B 60 7448 8942 8091 378 -220 21 O ATOM 3192 NE2 GLN B 60 -4.810 7.923 2.342 1.00 58.67 N ANISOU 3192 NE2 GLN B 60 6965 7955 7373 462 -229 56 N ATOM 3193 N VAL B 61 -6.410 13.921 2.183 1.00 34.57 N ANISOU 3193 N VAL B 61 3882 4877 4375 -149 -84 -49 N ATOM 3194 CA VAL B 61 -7.162 14.623 3.222 1.00 33.01 C ANISOU 3194 CA VAL B 61 3748 4630 4163 -223 -96 -61 C ATOM 3195 C VAL B 61 -8.483 15.133 2.659 1.00 30.48 C ANISOU 3195 C VAL B 61 3524 4186 3871 -248 -50 -58 C ATOM 3196 O VAL B 61 -9.519 14.979 3.291 1.00 29.86 O ANISOU 3196 O VAL B 61 3512 4044 3790 -239 -54 -47 O ATOM 3197 CB VAL B 61 -6.366 15.792 3.831 1.00 35.33 C ANISOU 3197 CB VAL B 61 3989 4997 4437 -338 -108 -98 C ATOM 3198 CG1 VAL B 61 -7.172 16.467 4.946 1.00 34.46 C ANISOU 3198 CG1 VAL B 61 3967 4826 4298 -396 -118 -119 C ATOM 3199 CG2 VAL B 61 -5.030 15.308 4.360 1.00 35.22 C ANISOU 3199 CG2 VAL B 61 3853 5132 4395 -314 -166 -100 C ATOM 3200 N ILE B 62 -8.443 15.704 1.456 1.00 30.41 N ANISOU 3200 N ILE B 62 3516 4154 3885 -273 -3 -62 N ATOM 3201 CA ILE B 62 -9.652 16.162 0.757 1.00 28.32 C ANISOU 3201 CA ILE B 62 3335 3783 3642 -277 32 -54 C ATOM 3202 C ILE B 62 -10.622 14.992 0.527 1.00 29.92 C ANISOU 3202 C ILE B 62 3578 3931 3861 -194 11 -30 C ATOM 3203 O ILE B 62 -11.847 15.120 0.726 1.00 30.62 O ANISOU 3203 O ILE B 62 3719 3950 3964 -197 15 -21 O ATOM 3204 CB ILE B 62 -9.293 16.840 -0.601 1.00 28.64 C ANISOU 3204 CB ILE B 62 3375 3819 3689 -304 82 -53 C ATOM 3205 CG1 ILE B 62 -8.481 18.111 -0.368 1.00 32.66 C ANISOU 3205 CG1 ILE B 62 3861 4359 4190 -416 109 -72 C ATOM 3206 CG2 ILE B 62 -10.545 17.194 -1.404 1.00 24.86 C ANISOU 3206 CG2 ILE B 62 2982 3240 3224 -284 103 -38 C ATOM 3207 CD1 ILE B 62 -7.896 18.720 -1.637 1.00 31.27 C ANISOU 3207 CD1 ILE B 62 3675 4194 4012 -456 167 -59 C ATOM 3208 N ALA B 63 -10.062 13.853 0.118 1.00 28.67 N ANISOU 3208 N ALA B 63 3392 3803 3697 -123 -10 -22 N ATOM 3209 CA ALA B 63 -10.835 12.641 -0.134 1.00 29.12 C ANISOU 3209 CA ALA B 63 3499 3796 3768 -56 -36 -4 C ATOM 3210 C ALA B 63 -11.530 12.129 1.141 1.00 28.57 C ANISOU 3210 C ALA B 63 3459 3698 3701 -61 -64 18 C ATOM 3211 O ALA B 63 -12.705 11.772 1.127 1.00 26.51 O ANISOU 3211 O ALA B 63 3244 3367 3462 -67 -68 35 O ATOM 3212 CB ALA B 63 -9.921 11.563 -0.716 1.00 29.25 C ANISOU 3212 CB ALA B 63 3498 3846 3772 32 -50 -7 C ATOM 3213 N THR B 64 -10.785 12.090 2.238 1.00 30.17 N ANISOU 3213 N THR B 64 3628 3963 3873 -61 -84 22 N ATOM 3214 CA THR B 64 -11.331 11.708 3.536 1.00 29.89 C ANISOU 3214 CA THR B 64 3626 3912 3818 -66 -102 48 C ATOM 3215 C THR B 64 -12.457 12.647 3.973 1.00 29.28 C ANISOU 3215 C THR B 64 3579 3798 3748 -131 -66 43 C ATOM 3216 O THR B 64 -13.510 12.194 4.428 1.00 28.49 O ANISOU 3216 O THR B 64 3517 3653 3657 -133 -58 73 O ATOM 3217 CB THR B 64 -10.213 11.655 4.587 1.00 29.36 C ANISOU 3217 CB THR B 64 3517 3938 3702 -52 -138 47 C ATOM 3218 OG1 THR B 64 -9.375 10.540 4.288 1.00 30.29 O ANISOU 3218 OG1 THR B 64 3614 4082 3814 40 -172 65 O ATOM 3219 CG2 THR B 64 -10.768 11.493 5.997 1.00 28.25 C ANISOU 3219 CG2 THR B 64 3423 3790 3519 -65 -150 74 C ATOM 3220 N ALA B 65 -12.239 13.946 3.810 1.00 29.36 N ANISOU 3220 N ALA B 65 3574 3827 3755 -182 -40 8 N ATOM 3221 CA ALA B 65 -13.263 14.949 4.108 1.00 29.65 C ANISOU 3221 CA ALA B 65 3649 3821 3797 -221 0 -3 C ATOM 3222 C ALA B 65 -14.525 14.700 3.286 1.00 27.00 C ANISOU 3222 C ALA B 65 3331 3421 3508 -199 17 19 C ATOM 3223 O ALA B 65 -15.638 14.828 3.794 1.00 28.91 O ANISOU 3223 O ALA B 65 3589 3639 3757 -201 41 34 O ATOM 3224 CB ALA B 65 -12.724 16.370 3.838 1.00 27.37 C ANISOU 3224 CB ALA B 65 3363 3537 3500 -277 23 -45 C ATOM 3225 N THR B 66 -14.334 14.348 2.015 1.00 26.98 N ANISOU 3225 N THR B 66 3320 3402 3531 -177 4 20 N ATOM 3226 CA THR B 66 -15.436 14.104 1.083 1.00 24.66 C ANISOU 3226 CA THR B 66 3038 3057 3273 -160 2 34 C ATOM 3227 C THR B 66 -16.214 12.873 1.492 1.00 25.82 C ANISOU 3227 C THR B 66 3191 3180 3440 -153 -22 65 C ATOM 3228 O THR B 66 -17.437 12.852 1.385 1.00 28.80 O ANISOU 3228 O THR B 66 3561 3533 3847 -165 -17 82 O ATOM 3229 CB THR B 66 -14.924 13.941 -0.373 1.00 26.60 C ANISOU 3229 CB THR B 66 3289 3296 3521 -135 -11 22 C ATOM 3230 OG1 THR B 66 -14.120 15.074 -0.728 1.00 27.73 O ANISOU 3230 OG1 THR B 66 3428 3464 3646 -158 21 3 O ATOM 3231 CG2 THR B 66 -16.070 13.833 -1.349 1.00 23.77 C ANISOU 3231 CG2 THR B 66 2949 2894 3189 -122 -27 30 C ATOM 3232 N VAL B 67 -15.517 11.848 1.978 1.00 27.10 N ANISOU 3232 N VAL B 67 3363 3349 3584 -134 -48 78 N ATOM 3233 CA VAL B 67 -16.189 10.633 2.446 1.00 24.65 C ANISOU 3233 CA VAL B 67 3079 2998 3288 -138 -67 117 C ATOM 3234 C VAL B 67 -17.013 10.903 3.721 1.00 25.01 C ANISOU 3234 C VAL B 67 3119 3061 3325 -174 -30 147 C ATOM 3235 O VAL B 67 -18.135 10.432 3.842 1.00 25.60 O ANISOU 3235 O VAL B 67 3191 3107 3430 -206 -21 179 O ATOM 3236 CB VAL B 67 -15.192 9.495 2.674 1.00 24.70 C ANISOU 3236 CB VAL B 67 3118 2997 3271 -90 -102 130 C ATOM 3237 CG1 VAL B 67 -15.857 8.334 3.401 1.00 20.34 C ANISOU 3237 CG1 VAL B 67 2614 2387 2725 -106 -113 182 C ATOM 3238 CG2 VAL B 67 -14.585 9.048 1.329 1.00 22.64 C ANISOU 3238 CG2 VAL B 67 2870 2713 3018 -41 -128 100 C ATOM 3239 N TYR B 68 -16.457 11.658 4.661 1.00 25.51 N ANISOU 3239 N TYR B 68 3178 3174 3341 -174 -8 135 N ATOM 3240 CA TYR B 68 -17.208 12.091 5.850 1.00 26.43 C ANISOU 3240 CA TYR B 68 3298 3313 3430 -197 38 152 C ATOM 3241 C TYR B 68 -18.549 12.754 5.480 1.00 28.37 C ANISOU 3241 C TYR B 68 3514 3548 3719 -211 81 151 C ATOM 3242 O TYR B 68 -19.599 12.421 6.045 1.00 26.79 O ANISOU 3242 O TYR B 68 3299 3353 3529 -229 116 190 O ATOM 3243 CB TYR B 68 -16.373 13.059 6.695 1.00 24.79 C ANISOU 3243 CB TYR B 68 3103 3157 3160 -197 47 115 C ATOM 3244 CG TYR B 68 -15.143 12.475 7.392 1.00 27.88 C ANISOU 3244 CG TYR B 68 3507 3591 3496 -179 1 122 C ATOM 3245 CD1 TYR B 68 -14.922 11.092 7.478 1.00 28.08 C ANISOU 3245 CD1 TYR B 68 3552 3598 3521 -147 -34 171 C ATOM 3246 CD2 TYR B 68 -14.210 13.319 7.997 1.00 27.08 C ANISOU 3246 CD2 TYR B 68 3403 3547 3339 -193 -13 79 C ATOM 3247 CE1 TYR B 68 -13.804 10.585 8.129 1.00 30.37 C ANISOU 3247 CE1 TYR B 68 3851 3933 3755 -107 -82 182 C ATOM 3248 CE2 TYR B 68 -13.085 12.816 8.632 1.00 31.05 C ANISOU 3248 CE2 TYR B 68 3899 4110 3788 -170 -68 85 C ATOM 3249 CZ TYR B 68 -12.890 11.452 8.702 1.00 30.67 C ANISOU 3249 CZ TYR B 68 3864 4050 3738 -117 -102 139 C ATOM 3250 OH TYR B 68 -11.779 10.963 9.344 1.00 27.27 O ANISOU 3250 OH TYR B 68 3424 3686 3250 -74 -161 151 O ATOM 3251 N PHE B 69 -18.493 13.682 4.523 1.00 28.01 N ANISOU 3251 N PHE B 69 3455 3491 3695 -199 80 114 N ATOM 3252 CA PHE B 69 -19.662 14.425 4.046 1.00 27.72 C ANISOU 3252 CA PHE B 69 3390 3449 3695 -188 110 112 C ATOM 3253 C PHE B 69 -20.703 13.467 3.446 1.00 28.40 C ANISOU 3253 C PHE B 69 3431 3522 3835 -205 86 148 C ATOM 3254 O PHE B 69 -21.900 13.560 3.752 1.00 26.51 O ANISOU 3254 O PHE B 69 3143 3309 3622 -210 119 173 O ATOM 3255 CB PHE B 69 -19.196 15.460 3.008 1.00 27.69 C ANISOU 3255 CB PHE B 69 3403 3423 3695 -168 102 75 C ATOM 3256 CG PHE B 69 -20.282 16.357 2.471 1.00 28.33 C ANISOU 3256 CG PHE B 69 3468 3493 3804 -133 126 75 C ATOM 3257 CD1 PHE B 69 -20.435 17.650 2.951 1.00 32.00 C ANISOU 3257 CD1 PHE B 69 3967 3947 4245 -105 176 52 C ATOM 3258 CD2 PHE B 69 -21.110 15.935 1.449 1.00 32.37 C ANISOU 3258 CD2 PHE B 69 3939 4003 4360 -121 91 95 C ATOM 3259 CE1 PHE B 69 -21.412 18.489 2.439 1.00 24.98 C ANISOU 3259 CE1 PHE B 69 3070 3044 3378 -49 197 56 C ATOM 3260 CE2 PHE B 69 -22.092 16.773 0.931 1.00 30.79 C ANISOU 3260 CE2 PHE B 69 3715 3805 4180 -72 102 100 C ATOM 3261 CZ PHE B 69 -22.244 18.046 1.430 1.00 29.81 C ANISOU 3261 CZ PHE B 69 3623 3669 4035 -27 158 84 C ATOM 3262 N LYS B 70 -20.237 12.541 2.610 1.00 27.08 N ANISOU 3262 N LYS B 70 3282 3322 3685 -215 28 148 N ATOM 3263 CA LYS B 70 -21.113 11.551 1.971 1.00 28.54 C ANISOU 3263 CA LYS B 70 3444 3482 3919 -248 -12 171 C ATOM 3264 C LYS B 70 -21.764 10.602 2.966 1.00 28.27 C ANISOU 3264 C LYS B 70 3399 3446 3897 -302 8 221 C ATOM 3265 O LYS B 70 -22.936 10.255 2.820 1.00 29.60 O ANISOU 3265 O LYS B 70 3511 3624 4111 -349 6 247 O ATOM 3266 CB LYS B 70 -20.337 10.708 0.957 1.00 29.24 C ANISOU 3266 CB LYS B 70 3583 3521 4007 -239 -74 149 C ATOM 3267 CG LYS B 70 -19.964 11.427 -0.320 1.00 30.46 C ANISOU 3267 CG LYS B 70 3745 3676 4151 -199 -95 110 C ATOM 3268 CD LYS B 70 -19.175 10.483 -1.206 1.00 30.92 C ANISOU 3268 CD LYS B 70 3859 3692 4196 -180 -144 87 C ATOM 3269 CE LYS B 70 -18.638 11.160 -2.440 1.00 33.23 C ANISOU 3269 CE LYS B 70 4169 3995 4462 -138 -151 54 C ATOM 3270 NZ LYS B 70 -19.695 11.509 -3.396 1.00 31.73 N ANISOU 3270 NZ LYS B 70 3964 3804 4288 -143 -184 50 N ATOM 3271 N ARG B 71 -20.997 10.159 3.953 1.00 27.31 N ANISOU 3271 N ARG B 71 3327 3318 3732 -298 24 240 N ATOM 3272 CA ARG B 71 -21.523 9.273 4.979 1.00 28.84 C ANISOU 3272 CA ARG B 71 3532 3505 3921 -348 52 300 C ATOM 3273 C ARG B 71 -22.655 9.945 5.735 1.00 27.99 C ANISOU 3273 C ARG B 71 3354 3463 3816 -367 128 325 C ATOM 3274 O ARG B 71 -23.670 9.322 6.020 1.00 28.28 O ANISOU 3274 O ARG B 71 3350 3508 3887 -430 153 374 O ATOM 3275 CB ARG B 71 -20.422 8.861 5.958 1.00 30.65 C ANISOU 3275 CB ARG B 71 3834 3727 4084 -319 53 318 C ATOM 3276 CG ARG B 71 -19.401 7.901 5.394 1.00 30.61 C ANISOU 3276 CG ARG B 71 3895 3658 4075 -288 -14 310 C ATOM 3277 CD ARG B 71 -18.349 7.624 6.451 1.00 32.09 C ANISOU 3277 CD ARG B 71 4137 3864 4192 -242 -16 332 C ATOM 3278 NE ARG B 71 -17.388 6.607 6.047 1.00 35.03 N ANISOU 3278 NE ARG B 71 4572 4179 4558 -190 -74 335 N ATOM 3279 CZ ARG B 71 -16.392 6.166 6.812 1.00 32.28 C ANISOU 3279 CZ ARG B 71 4270 3845 4151 -129 -96 358 C ATOM 3280 NH1 ARG B 71 -16.205 6.655 8.034 1.00 36.93 N ANISOU 3280 NH1 ARG B 71 4855 4504 4674 -126 -71 379 N ATOM 3281 NH2 ARG B 71 -15.576 5.233 6.348 1.00 33.43 N ANISOU 3281 NH2 ARG B 71 4470 3937 4295 -62 -146 359 N ATOM 3282 N PHE B 72 -22.480 11.224 6.056 1.00 28.59 N ANISOU 3282 N PHE B 72 3418 3587 3857 -312 168 288 N ATOM 3283 CA PHE B 72 -23.463 11.936 6.864 1.00 30.00 C ANISOU 3283 CA PHE B 72 3544 3830 4023 -302 252 303 C ATOM 3284 C PHE B 72 -24.793 12.052 6.126 1.00 30.31 C ANISOU 3284 C PHE B 72 3478 3900 4137 -317 257 316 C ATOM 3285 O PHE B 72 -25.850 11.762 6.690 1.00 29.58 O ANISOU 3285 O PHE B 72 3315 3860 4063 -353 313 364 O ATOM 3286 CB PHE B 72 -22.969 13.336 7.268 1.00 28.64 C ANISOU 3286 CB PHE B 72 3407 3680 3797 -235 287 249 C ATOM 3287 CG PHE B 72 -23.926 14.059 8.170 1.00 31.99 C ANISOU 3287 CG PHE B 72 3797 4164 4193 -203 382 256 C ATOM 3288 CD1 PHE B 72 -23.899 13.850 9.537 1.00 33.98 C ANISOU 3288 CD1 PHE B 72 4088 4451 4371 -210 442 282 C ATOM 3289 CD2 PHE B 72 -24.885 14.914 7.646 1.00 32.91 C ANISOU 3289 CD2 PHE B 72 3846 4307 4352 -154 412 242 C ATOM 3290 CE1 PHE B 72 -24.791 14.495 10.366 1.00 36.02 C ANISOU 3290 CE1 PHE B 72 4320 4772 4594 -170 541 286 C ATOM 3291 CE2 PHE B 72 -25.779 15.563 8.467 1.00 31.45 C ANISOU 3291 CE2 PHE B 72 3625 4183 4141 -103 507 247 C ATOM 3292 CZ PHE B 72 -25.738 15.349 9.830 1.00 32.48 C ANISOU 3292 CZ PHE B 72 3796 4350 4194 -113 577 267 C ATOM 3293 N TYR B 73 -24.730 12.476 4.867 1.00 28.95 N ANISOU 3293 N TYR B 73 3291 3707 4002 -289 198 278 N ATOM 3294 CA TYR B 73 -25.932 12.640 4.051 1.00 30.23 C ANISOU 3294 CA TYR B 73 3350 3908 4228 -291 181 286 C ATOM 3295 C TYR B 73 -26.447 11.337 3.430 1.00 32.11 C ANISOU 3295 C TYR B 73 3550 4126 4523 -386 116 315 C ATOM 3296 O TYR B 73 -27.583 11.294 2.959 1.00 31.57 O ANISOU 3296 O TYR B 73 3374 4111 4510 -412 99 330 O ATOM 3297 CB TYR B 73 -25.713 13.731 3.003 1.00 33.17 C ANISOU 3297 CB TYR B 73 3735 4268 4602 -213 147 239 C ATOM 3298 CG TYR B 73 -25.539 15.089 3.667 1.00 30.74 C ANISOU 3298 CG TYR B 73 3460 3974 4247 -130 219 214 C ATOM 3299 CD1 TYR B 73 -26.597 15.696 4.323 1.00 30.59 C ANISOU 3299 CD1 TYR B 73 3370 4021 4232 -82 295 230 C ATOM 3300 CD2 TYR B 73 -24.307 15.725 3.690 1.00 26.24 C ANISOU 3300 CD2 TYR B 73 2992 3350 3627 -106 216 172 C ATOM 3301 CE1 TYR B 73 -26.442 16.914 4.958 1.00 33.62 C ANISOU 3301 CE1 TYR B 73 3809 4399 4567 0 362 198 C ATOM 3302 CE2 TYR B 73 -24.142 16.946 4.319 1.00 31.77 C ANISOU 3302 CE2 TYR B 73 3742 4046 4285 -48 277 141 C ATOM 3303 CZ TYR B 73 -25.214 17.538 4.948 1.00 30.26 C ANISOU 3303 CZ TYR B 73 3503 3902 4092 10 348 151 C ATOM 3304 OH TYR B 73 -25.058 18.746 5.581 1.00 35.90 O ANISOU 3304 OH TYR B 73 4290 4595 4756 75 409 111 O ATOM 3305 N ALA B 74 -25.631 10.279 3.459 1.00 30.88 N ANISOU 3305 N ALA B 74 3484 3895 4355 -435 76 320 N ATOM 3306 CA ALA B 74 -26.109 8.925 3.161 1.00 32.39 C ANISOU 3306 CA ALA B 74 3672 4042 4593 -539 27 351 C ATOM 3307 C ALA B 74 -27.166 8.491 4.183 1.00 34.61 C ANISOU 3307 C ALA B 74 3876 4376 4897 -621 99 420 C ATOM 3308 O ALA B 74 -28.103 7.772 3.850 1.00 33.90 O ANISOU 3308 O ALA B 74 3718 4294 4869 -721 71 448 O ATOM 3309 CB ALA B 74 -24.948 7.930 3.155 1.00 31.12 C ANISOU 3309 CB ALA B 74 3645 3778 4402 -549 -15 346 C ATOM 3310 N ARG B 75 -27.012 8.942 5.427 1.00 36.49 N ANISOU 3310 N ARG B 75 4125 4657 5082 -583 192 447 N ATOM 3311 CA ARG B 75 -27.957 8.615 6.492 1.00 38.32 C ANISOU 3311 CA ARG B 75 4290 4952 5318 -649 283 518 C ATOM 3312 C ARG B 75 -29.041 9.687 6.670 1.00 37.78 C ANISOU 3312 C ARG B 75 4077 5011 5267 -598 356 517 C ATOM 3313 O ARG B 75 -30.224 9.367 6.770 1.00 39.58 O ANISOU 3313 O ARG B 75 4176 5314 5549 -670 392 564 O ATOM 3314 CB ARG B 75 -27.204 8.412 7.807 1.00 40.50 C ANISOU 3314 CB ARG B 75 4672 5208 5507 -630 347 552 C ATOM 3315 CG ARG B 75 -28.021 7.751 8.919 1.00 51.45 C ANISOU 3315 CG ARG B 75 6029 6637 6883 -716 441 642 C ATOM 3316 CD ARG B 75 -28.422 6.293 8.605 1.00 62.72 C ANISOU 3316 CD ARG B 75 7472 7987 8373 -862 399 701 C ATOM 3317 NE ARG B 75 -27.312 5.471 8.106 1.00 67.32 N ANISOU 3317 NE ARG B 75 8204 8430 8946 -859 301 680 N ATOM 3318 CZ ARG B 75 -26.307 5.000 8.849 1.00 71.46 C ANISOU 3318 CZ ARG B 75 8868 8889 9395 -822 305 707 C ATOM 3319 NH1 ARG B 75 -25.362 4.260 8.277 1.00 71.36 N ANISOU 3319 NH1 ARG B 75 8974 8758 9383 -802 215 685 N ATOM 3320 NH2 ARG B 75 -26.228 5.260 10.154 1.00 69.89 N ANISOU 3320 NH2 ARG B 75 8696 8747 9113 -792 395 755 N ATOM 3321 N TYR B 76 -28.641 10.953 6.711 1.00 35.79 N ANISOU 3321 N TYR B 76 3846 4783 4972 -473 380 465 N ATOM 3322 CA TYR B 76 -29.564 12.039 7.058 1.00 35.62 C ANISOU 3322 CA TYR B 76 3718 4868 4949 -392 464 462 C ATOM 3323 C TYR B 76 -29.912 12.939 5.884 1.00 34.86 C ANISOU 3323 C TYR B 76 3558 4791 4896 -311 407 415 C ATOM 3324 O TYR B 76 -29.177 13.025 4.908 1.00 33.58 O ANISOU 3324 O TYR B 76 3467 4554 4739 -296 316 373 O ATOM 3325 CB TYR B 76 -28.976 12.896 8.177 1.00 35.09 C ANISOU 3325 CB TYR B 76 3741 4806 4785 -303 550 438 C ATOM 3326 CG TYR B 76 -28.847 12.174 9.488 1.00 35.73 C ANISOU 3326 CG TYR B 76 3873 4899 4804 -360 624 493 C ATOM 3327 CD1 TYR B 76 -29.970 11.703 10.156 1.00 39.87 C ANISOU 3327 CD1 TYR B 76 4292 5512 5343 -417 716 564 C ATOM 3328 CD2 TYR B 76 -27.606 11.973 10.071 1.00 36.28 C ANISOU 3328 CD2 TYR B 76 4089 4900 4794 -356 603 479 C ATOM 3329 CE1 TYR B 76 -29.855 11.042 11.363 1.00 39.08 C ANISOU 3329 CE1 TYR B 76 4254 5422 5174 -469 791 625 C ATOM 3330 CE2 TYR B 76 -27.485 11.313 11.263 1.00 37.59 C ANISOU 3330 CE2 TYR B 76 4313 5078 4890 -397 664 536 C ATOM 3331 CZ TYR B 76 -28.609 10.849 11.907 1.00 36.39 C ANISOU 3331 CZ TYR B 76 4077 5004 4747 -454 761 611 C ATOM 3332 OH TYR B 76 -28.471 10.204 13.107 1.00 42.47 O ANISOU 3332 OH TYR B 76 4921 5783 5434 -493 827 677 O ATOM 3333 N SER B 77 -31.040 13.629 6.015 1.00 36.57 N ANISOU 3333 N SER B 77 3643 5115 5137 -247 468 428 N ATOM 3334 CA SER B 77 -31.525 14.540 4.988 1.00 36.61 C ANISOU 3334 CA SER B 77 3581 5152 5178 -148 420 397 C ATOM 3335 C SER B 77 -30.654 15.787 4.915 1.00 36.80 C ANISOU 3335 C SER B 77 3740 5102 5140 -22 430 338 C ATOM 3336 O SER B 77 -30.043 16.196 5.910 1.00 35.57 O ANISOU 3336 O SER B 77 3685 4916 4916 9 503 319 O ATOM 3337 CB SER B 77 -32.979 14.945 5.268 1.00 39.24 C ANISOU 3337 CB SER B 77 3727 5633 5550 -94 492 433 C ATOM 3338 OG SER B 77 -33.384 16.025 4.439 1.00 35.35 O ANISOU 3338 OG SER B 77 3191 5167 5073 45 457 404 O ATOM 3339 N LEU B 78 -30.615 16.381 3.724 1.00 36.88 N ANISOU 3339 N LEU B 78 3758 5084 5171 41 351 310 N ATOM 3340 CA LEU B 78 -29.890 17.623 3.482 1.00 37.19 C ANISOU 3340 CA LEU B 78 3923 5045 5162 150 357 262 C ATOM 3341 C LEU B 78 -30.329 18.763 4.397 1.00 37.67 C ANISOU 3341 C LEU B 78 3993 5135 5184 275 468 248 C ATOM 3342 O LEU B 78 -29.569 19.704 4.604 1.00 37.65 O ANISOU 3342 O LEU B 78 4131 5048 5127 336 494 203 O ATOM 3343 CB LEU B 78 -30.056 18.051 2.020 1.00 38.27 C ANISOU 3343 CB LEU B 78 4050 5165 5327 205 262 253 C ATOM 3344 CG LEU B 78 -29.315 17.174 1.007 1.00 36.45 C ANISOU 3344 CG LEU B 78 3869 4875 5106 108 154 245 C ATOM 3345 CD1 LEU B 78 -29.912 17.325 -0.386 1.00 36.31 C ANISOU 3345 CD1 LEU B 78 3795 4884 5117 149 58 250 C ATOM 3346 CD2 LEU B 78 -27.823 17.480 1.010 1.00 36.46 C ANISOU 3346 CD2 LEU B 78 4036 4766 5052 98 156 206 C ATOM 3347 N LYS B 79 -31.547 18.679 4.936 1.00 38.75 N ANISOU 3347 N LYS B 79 3983 5392 5347 310 537 284 N ATOM 3348 CA LYS B 79 -32.075 19.705 5.839 1.00 38.72 C ANISOU 3348 CA LYS B 79 3982 5429 5301 447 657 270 C ATOM 3349 C LYS B 79 -31.583 19.565 7.277 1.00 35.82 C ANISOU 3349 C LYS B 79 3703 5051 4857 411 755 256 C ATOM 3350 O LYS B 79 -31.764 20.473 8.060 1.00 34.70 O ANISOU 3350 O LYS B 79 3615 4913 4657 524 851 225 O ATOM 3351 CB LYS B 79 -33.615 19.685 5.842 1.00 40.78 C ANISOU 3351 CB LYS B 79 4027 5848 5618 513 703 317 C ATOM 3352 CG LYS B 79 -34.237 18.580 6.700 1.00 44.98 C ANISOU 3352 CG LYS B 79 4424 6496 6169 397 770 373 C ATOM 3353 CD LYS B 79 -35.743 18.533 6.550 1.00 49.63 C ANISOU 3353 CD LYS B 79 4770 7261 6827 445 804 423 C ATOM 3354 CE LYS B 79 -36.341 17.349 7.309 1.00 53.95 C ANISOU 3354 CE LYS B 79 5179 7918 7401 294 869 489 C ATOM 3355 NZ LYS B 79 -37.793 17.281 7.188 0.00 58.22 N ANISOU 3355 NZ LYS B 79 5458 8649 8013 321 906 540 N ATOM 3356 N SER B 80 -31.004 18.422 7.636 1.00 34.77 N ANISOU 3356 N SER B 80 3591 4903 4715 265 731 281 N ATOM 3357 CA SER B 80 -30.637 18.168 9.032 1.00 32.76 C ANISOU 3357 CA SER B 80 3410 4659 4380 232 819 282 C ATOM 3358 C SER B 80 -29.593 19.185 9.486 1.00 32.50 C ANISOU 3358 C SER B 80 3564 4525 4257 295 831 206 C ATOM 3359 O SER B 80 -29.792 19.891 10.470 1.00 36.21 O ANISOU 3359 O SER B 80 4089 5016 4653 378 930 176 O ATOM 3360 CB SER B 80 -30.120 16.742 9.208 1.00 32.31 C ANISOU 3360 CB SER B 80 3362 4586 4330 74 773 328 C ATOM 3361 OG SER B 80 -28.885 16.552 8.534 1.00 38.44 O ANISOU 3361 OG SER B 80 4250 5252 5105 26 665 294 O ATOM 3362 N ILE B 81 -28.485 19.247 8.754 1.00 31.25 N ANISOU 3362 N ILE B 81 3504 4264 4105 250 731 172 N ATOM 3363 CA ILE B 81 -27.453 20.263 8.947 1.00 31.25 C ANISOU 3363 CA ILE B 81 3670 4165 4040 286 723 99 C ATOM 3364 C ILE B 81 -27.128 20.891 7.591 1.00 30.10 C ANISOU 3364 C ILE B 81 3554 3939 3944 314 644 77 C ATOM 3365 O ILE B 81 -27.014 20.195 6.567 1.00 30.78 O ANISOU 3365 O ILE B 81 3580 4023 4092 255 562 108 O ATOM 3366 CB ILE B 81 -26.173 19.676 9.568 1.00 31.73 C ANISOU 3366 CB ILE B 81 3827 4188 4039 184 685 83 C ATOM 3367 CG1 ILE B 81 -26.477 19.042 10.923 1.00 33.35 C ANISOU 3367 CG1 ILE B 81 4023 4471 4179 161 761 114 C ATOM 3368 CG2 ILE B 81 -25.101 20.769 9.744 1.00 35.66 C ANISOU 3368 CG2 ILE B 81 4480 4594 4473 200 667 3 C ATOM 3369 CD1 ILE B 81 -25.267 18.462 11.609 1.00 33.73 C ANISOU 3369 CD1 ILE B 81 4166 4494 4155 80 718 106 C ATOM 3370 N ASP B 82 -26.999 22.207 7.582 1.00 29.61 N ANISOU 3370 N ASP B 82 3597 3804 3848 404 673 25 N ATOM 3371 CA ASP B 82 -26.686 22.938 6.357 1.00 31.89 C ANISOU 3371 CA ASP B 82 3940 4005 4171 436 612 12 C ATOM 3372 C ASP B 82 -25.384 22.387 5.754 1.00 31.13 C ANISOU 3372 C ASP B 82 3890 3858 4081 311 524 7 C ATOM 3373 O ASP B 82 -24.344 22.421 6.393 1.00 30.85 O ANISOU 3373 O ASP B 82 3942 3785 3992 243 522 -31 O ATOM 3374 CB ASP B 82 -26.564 24.438 6.678 1.00 33.57 C ANISOU 3374 CB ASP B 82 4303 4120 4332 534 666 -48 C ATOM 3375 CG ASP B 82 -26.221 25.293 5.457 1.00 36.37 C ANISOU 3375 CG ASP B 82 4741 4366 4712 566 615 -53 C ATOM 3376 OD1 ASP B 82 -26.058 24.754 4.337 1.00 32.92 O ANISOU 3376 OD1 ASP B 82 4244 3940 4325 519 538 -12 O ATOM 3377 OD2 ASP B 82 -26.110 26.526 5.636 1.00 34.87 O ANISOU 3377 OD2 ASP B 82 4694 4071 4484 638 654 -98 O ATOM 3378 N PRO B 83 -25.442 21.856 4.523 1.00 32.85 N ANISOU 3378 N PRO B 83 4043 4083 4357 286 451 44 N ATOM 3379 CA PRO B 83 -24.216 21.348 3.922 1.00 31.63 C ANISOU 3379 CA PRO B 83 3930 3887 4201 187 381 37 C ATOM 3380 C PRO B 83 -23.095 22.386 3.785 1.00 30.90 C ANISOU 3380 C PRO B 83 3975 3697 4069 169 380 -9 C ATOM 3381 O PRO B 83 -21.921 22.007 3.747 1.00 29.47 O ANISOU 3381 O PRO B 83 3824 3503 3871 79 344 -24 O ATOM 3382 CB PRO B 83 -24.676 20.852 2.546 1.00 32.32 C ANISOU 3382 CB PRO B 83 3942 3994 4345 194 312 76 C ATOM 3383 CG PRO B 83 -25.971 21.545 2.298 1.00 31.93 C ANISOU 3383 CG PRO B 83 3839 3971 4319 311 338 95 C ATOM 3384 CD PRO B 83 -26.600 21.677 3.627 1.00 32.19 C ANISOU 3384 CD PRO B 83 3842 4055 4334 348 424 89 C ATOM 3385 N VAL B 84 -23.452 23.667 3.716 1.00 31.60 N ANISOU 3385 N VAL B 84 4146 3718 4144 252 421 -30 N ATOM 3386 CA VAL B 84 -22.467 24.748 3.692 1.00 31.43 C ANISOU 3386 CA VAL B 84 4271 3587 4083 219 429 -76 C ATOM 3387 C VAL B 84 -21.667 24.780 4.997 1.00 31.06 C ANISOU 3387 C VAL B 84 4283 3540 3979 145 451 -131 C ATOM 3388 O VAL B 84 -20.511 25.179 4.993 1.00 30.39 O ANISOU 3388 O VAL B 84 4277 3401 3868 56 429 -166 O ATOM 3389 CB VAL B 84 -23.147 26.124 3.428 1.00 34.19 C ANISOU 3389 CB VAL B 84 4719 3844 4427 339 473 -84 C ATOM 3390 CG1 VAL B 84 -22.228 27.289 3.781 1.00 33.99 C ANISOU 3390 CG1 VAL B 84 4871 3689 4354 292 497 -143 C ATOM 3391 CG2 VAL B 84 -23.576 26.217 1.993 1.00 34.26 C ANISOU 3391 CG2 VAL B 84 4701 3840 4476 396 431 -30 C ATOM 3392 N LEU B 85 -22.286 24.348 6.098 1.00 29.56 N ANISOU 3392 N LEU B 85 4048 3420 3763 177 492 -135 N ATOM 3393 CA LEU B 85 -21.599 24.213 7.381 1.00 30.45 C ANISOU 3393 CA LEU B 85 4211 3553 3806 114 503 -181 C ATOM 3394 C LEU B 85 -20.865 22.881 7.473 1.00 30.17 C ANISOU 3394 C LEU B 85 4093 3596 3776 20 445 -151 C ATOM 3395 O LEU B 85 -19.772 22.804 8.037 1.00 30.26 O ANISOU 3395 O LEU B 85 4147 3611 3739 -60 412 -186 O ATOM 3396 CB LEU B 85 -22.592 24.326 8.551 1.00 30.05 C ANISOU 3396 CB LEU B 85 4162 3549 3708 199 584 -194 C ATOM 3397 CG LEU B 85 -22.027 24.096 9.957 1.00 32.82 C ANISOU 3397 CG LEU B 85 4567 3936 3966 147 597 -235 C ATOM 3398 CD1 LEU B 85 -20.832 25.002 10.202 1.00 33.41 C ANISOU 3398 CD1 LEU B 85 4784 3924 3988 73 561 -315 C ATOM 3399 CD2 LEU B 85 -23.104 24.318 11.029 1.00 33.86 C ANISOU 3399 CD2 LEU B 85 4710 4113 4040 249 697 -246 C ATOM 3400 N MET B 86 -21.472 21.825 6.940 1.00 32.48 N ANISOU 3400 N MET B 86 4269 3948 4123 31 427 -88 N ATOM 3401 CA MET B 86 -20.888 20.485 7.053 1.00 30.58 C ANISOU 3401 CA MET B 86 3967 3765 3887 -40 377 -56 C ATOM 3402 C MET B 86 -19.598 20.357 6.229 1.00 27.41 C ANISOU 3402 C MET B 86 3578 3336 3499 -106 309 -67 C ATOM 3403 O MET B 86 -18.651 19.712 6.665 1.00 25.34 O ANISOU 3403 O MET B 86 3311 3109 3209 -160 271 -71 O ATOM 3404 CB MET B 86 -21.897 19.413 6.638 1.00 30.60 C ANISOU 3404 CB MET B 86 3859 3819 3948 -23 373 9 C ATOM 3405 CG MET B 86 -21.385 17.961 6.791 1.00 29.41 C ANISOU 3405 CG MET B 86 3669 3705 3802 -89 325 46 C ATOM 3406 SD MET B 86 -21.012 17.459 8.480 1.00 33.27 S ANISOU 3406 SD MET B 86 4196 4240 4204 -115 354 51 S ATOM 3407 CE MET B 86 -22.653 17.348 9.192 1.00 35.17 C ANISOU 3407 CE MET B 86 4379 4536 4446 -72 448 94 C ATOM 3408 N ALA B 87 -19.563 20.972 5.050 1.00 27.16 N ANISOU 3408 N ALA B 87 3562 3252 3506 -93 297 -68 N ATOM 3409 CA ALA B 87 -18.398 20.873 4.163 1.00 27.47 C ANISOU 3409 CA ALA B 87 3606 3277 3556 -151 249 -72 C ATOM 3410 C ALA B 87 -17.076 21.259 4.857 1.00 28.05 C ANISOU 3410 C ALA B 87 3725 3354 3580 -229 236 -118 C ATOM 3411 O ALA B 87 -16.162 20.442 4.941 1.00 28.01 O ANISOU 3411 O ALA B 87 3672 3404 3567 -272 194 -113 O ATOM 3412 CB ALA B 87 -18.615 21.697 2.887 1.00 29.05 C ANISOU 3412 CB ALA B 87 3841 3412 3784 -123 254 -63 C ATOM 3413 N PRO B 88 -16.981 22.489 5.388 1.00 30.41 N ANISOU 3413 N PRO B 88 4117 3596 3844 -244 268 -167 N ATOM 3414 CA PRO B 88 -15.749 22.887 6.084 1.00 30.94 C ANISOU 3414 CA PRO B 88 4223 3672 3862 -337 243 -219 C ATOM 3415 C PRO B 88 -15.487 22.128 7.389 1.00 31.25 C ANISOU 3415 C PRO B 88 4235 3795 3845 -348 218 -231 C ATOM 3416 O PRO B 88 -14.329 21.958 7.773 1.00 31.86 O ANISOU 3416 O PRO B 88 4293 3923 3891 -420 168 -255 O ATOM 3417 CB PRO B 88 -15.954 24.388 6.355 1.00 30.67 C ANISOU 3417 CB PRO B 88 4319 3534 3801 -344 285 -273 C ATOM 3418 CG PRO B 88 -17.420 24.612 6.258 1.00 31.40 C ANISOU 3418 CG PRO B 88 4432 3588 3911 -223 339 -250 C ATOM 3419 CD PRO B 88 -17.944 23.601 5.284 1.00 32.15 C ANISOU 3419 CD PRO B 88 4416 3734 4067 -176 321 -180 C ATOM 3420 N THR B 89 -16.548 21.691 8.066 1.00 29.01 N ANISOU 3420 N THR B 89 3946 3532 3545 -277 253 -210 N ATOM 3421 CA THR B 89 -16.420 20.826 9.240 1.00 26.36 C ANISOU 3421 CA THR B 89 3592 3275 3150 -278 237 -200 C ATOM 3422 C THR B 89 -15.737 19.513 8.875 1.00 26.43 C ANISOU 3422 C THR B 89 3512 3345 3184 -295 177 -151 C ATOM 3423 O THR B 89 -14.896 19.026 9.625 1.00 27.07 O ANISOU 3423 O THR B 89 3586 3488 3213 -323 129 -157 O ATOM 3424 CB THR B 89 -17.800 20.518 9.882 1.00 27.08 C ANISOU 3424 CB THR B 89 3682 3382 3227 -201 303 -169 C ATOM 3425 OG1 THR B 89 -18.479 21.748 10.166 1.00 26.46 O ANISOU 3425 OG1 THR B 89 3685 3245 3124 -157 367 -216 O ATOM 3426 CG2 THR B 89 -17.637 19.708 11.191 1.00 21.98 C ANISOU 3426 CG2 THR B 89 3040 2810 2499 -207 296 -153 C ATOM 3427 N CYS B 90 -16.083 18.950 7.718 1.00 25.39 N ANISOU 3427 N CYS B 90 3323 3196 3127 -271 173 -106 N ATOM 3428 CA CYS B 90 -15.471 17.699 7.273 1.00 27.23 C ANISOU 3428 CA CYS B 90 3491 3470 3384 -272 121 -66 C ATOM 3429 C CYS B 90 -13.987 17.883 6.955 1.00 26.85 C ANISOU 3429 C CYS B 90 3420 3456 3327 -320 73 -95 C ATOM 3430 O CYS B 90 -13.156 17.062 7.340 1.00 26.38 O ANISOU 3430 O CYS B 90 3324 3459 3242 -319 24 -82 O ATOM 3431 CB CYS B 90 -16.218 17.111 6.067 1.00 26.79 C ANISOU 3431 CB CYS B 90 3396 3382 3402 -239 126 -24 C ATOM 3432 SG CYS B 90 -17.883 16.494 6.479 1.00 30.27 S ANISOU 3432 SG CYS B 90 3819 3818 3864 -201 168 25 S ATOM 3433 N VAL B 91 -13.659 18.970 6.269 1.00 29.09 N ANISOU 3433 N VAL B 91 3724 3701 3628 -361 88 -130 N ATOM 3434 CA VAL B 91 -12.256 19.320 5.990 1.00 30.05 C ANISOU 3434 CA VAL B 91 3812 3864 3742 -430 55 -158 C ATOM 3435 C VAL B 91 -11.447 19.451 7.292 1.00 30.92 C ANISOU 3435 C VAL B 91 3924 4041 3784 -478 11 -197 C ATOM 3436 O VAL B 91 -10.353 18.905 7.405 1.00 31.17 O ANISOU 3436 O VAL B 91 3880 4161 3801 -495 -43 -195 O ATOM 3437 CB VAL B 91 -12.175 20.620 5.154 1.00 31.25 C ANISOU 3437 CB VAL B 91 4010 3944 3918 -483 92 -183 C ATOM 3438 CG1 VAL B 91 -10.756 21.155 5.096 1.00 31.93 C ANISOU 3438 CG1 VAL B 91 4063 4077 3991 -586 67 -217 C ATOM 3439 CG2 VAL B 91 -12.737 20.372 3.739 1.00 25.71 C ANISOU 3439 CG2 VAL B 91 3297 3201 3272 -431 117 -140 C ATOM 3440 N PHE B 92 -12.017 20.149 8.273 1.00 29.70 N ANISOU 3440 N PHE B 92 3853 3851 3579 -488 31 -234 N ATOM 3441 CA PHE B 92 -11.389 20.363 9.581 1.00 29.10 C ANISOU 3441 CA PHE B 92 3803 3834 3418 -533 -14 -280 C ATOM 3442 C PHE B 92 -11.096 19.046 10.325 1.00 30.71 C ANISOU 3442 C PHE B 92 3955 4133 3579 -480 -66 -238 C ATOM 3443 O PHE B 92 -9.995 18.854 10.843 1.00 30.32 O ANISOU 3443 O PHE B 92 3860 4175 3485 -514 -138 -255 O ATOM 3444 CB PHE B 92 -12.299 21.281 10.404 1.00 29.38 C ANISOU 3444 CB PHE B 92 3960 3799 3403 -526 35 -326 C ATOM 3445 CG PHE B 92 -11.807 21.586 11.794 1.00 30.45 C ANISOU 3445 CG PHE B 92 4153 3984 3432 -568 -9 -385 C ATOM 3446 CD1 PHE B 92 -10.686 22.380 11.997 1.00 30.94 C ANISOU 3446 CD1 PHE B 92 4226 4066 3465 -681 -67 -455 C ATOM 3447 CD2 PHE B 92 -12.514 21.130 12.909 1.00 29.71 C ANISOU 3447 CD2 PHE B 92 4108 3918 3260 -501 11 -373 C ATOM 3448 CE1 PHE B 92 -10.257 22.691 13.287 1.00 31.88 C ANISOU 3448 CE1 PHE B 92 4407 4233 3475 -725 -121 -519 C ATOM 3449 CE2 PHE B 92 -12.094 21.435 14.194 1.00 33.37 C ANISOU 3449 CE2 PHE B 92 4641 4429 3607 -533 -31 -430 C ATOM 3450 CZ PHE B 92 -10.963 22.220 14.387 1.00 33.79 C ANISOU 3450 CZ PHE B 92 4709 4502 3629 -644 -105 -508 C ATOM 3451 N LEU B 93 -12.066 18.132 10.361 1.00 29.63 N ANISOU 3451 N LEU B 93 3823 3977 3457 -399 -33 -177 N ATOM 3452 CA LEU B 93 -11.878 16.871 11.066 1.00 29.81 C ANISOU 3452 CA LEU B 93 3824 4064 3436 -347 -73 -125 C ATOM 3453 C LEU B 93 -10.876 15.978 10.349 1.00 29.30 C ANISOU 3453 C LEU B 93 3670 4051 3412 -324 -130 -93 C ATOM 3454 O LEU B 93 -10.054 15.326 10.993 1.00 27.69 O ANISOU 3454 O LEU B 93 3437 3928 3156 -298 -196 -78 O ATOM 3455 CB LEU B 93 -13.204 16.129 11.222 1.00 30.53 C ANISOU 3455 CB LEU B 93 3947 4110 3541 -288 -15 -63 C ATOM 3456 CG LEU B 93 -13.138 14.801 11.986 1.00 29.06 C ANISOU 3456 CG LEU B 93 3768 3967 3308 -239 -45 5 C ATOM 3457 CD1 LEU B 93 -12.672 15.017 13.429 1.00 28.50 C ANISOU 3457 CD1 LEU B 93 3750 3966 3113 -246 -79 -17 C ATOM 3458 CD2 LEU B 93 -14.492 14.130 11.953 1.00 27.14 C ANISOU 3458 CD2 LEU B 93 3547 3670 3097 -211 22 69 C ATOM 3459 N ALA B 94 -10.971 15.931 9.023 1.00 29.27 N ANISOU 3459 N ALA B 94 3627 4003 3492 -318 -105 -83 N ATOM 3460 CA ALA B 94 -10.095 15.088 8.209 1.00 29.45 C ANISOU 3460 CA ALA B 94 3571 4068 3552 -279 -142 -57 C ATOM 3461 C ALA B 94 -8.649 15.527 8.359 1.00 31.82 C ANISOU 3461 C ALA B 94 3794 4472 3825 -325 -195 -96 C ATOM 3462 O ALA B 94 -7.747 14.693 8.451 1.00 32.04 O ANISOU 3462 O ALA B 94 3753 4582 3838 -271 -249 -74 O ATOM 3463 CB ALA B 94 -10.510 15.138 6.755 1.00 27.29 C ANISOU 3463 CB ALA B 94 3286 3728 3355 -271 -98 -49 C ATOM 3464 N SER B 95 -8.427 16.837 8.402 1.00 32.52 N ANISOU 3464 N SER B 95 3893 4556 3907 -424 -183 -153 N ATOM 3465 CA SER B 95 -7.080 17.359 8.564 1.00 33.39 C ANISOU 3465 CA SER B 95 3920 4768 3996 -499 -235 -195 C ATOM 3466 C SER B 95 -6.476 16.917 9.888 1.00 34.08 C ANISOU 3466 C SER B 95 3987 4960 4000 -482 -320 -200 C ATOM 3467 O SER B 95 -5.296 16.593 9.948 1.00 35.98 O ANISOU 3467 O SER B 95 4116 5325 4230 -479 -385 -200 O ATOM 3468 CB SER B 95 -7.057 18.884 8.440 1.00 35.98 C ANISOU 3468 CB SER B 95 4294 5044 4330 -628 -205 -257 C ATOM 3469 OG SER B 95 -5.725 19.372 8.590 1.00 42.52 O ANISOU 3469 OG SER B 95 5031 5979 5145 -728 -260 -296 O ATOM 3470 N LYS B 96 -7.283 16.876 10.943 1.00 36.30 N ANISOU 3470 N LYS B 96 4372 5204 4218 -460 -319 -199 N ATOM 3471 CA LYS B 96 -6.804 16.400 12.238 1.00 39.56 C ANISOU 3471 CA LYS B 96 4788 5713 4532 -430 -400 -195 C ATOM 3472 C LYS B 96 -6.503 14.897 12.208 1.00 40.40 C ANISOU 3472 C LYS B 96 4845 5868 4638 -303 -437 -116 C ATOM 3473 O LYS B 96 -5.459 14.464 12.677 1.00 41.98 O ANISOU 3473 O LYS B 96 4969 6190 4793 -270 -525 -109 O ATOM 3474 CB LYS B 96 -7.798 16.747 13.345 1.00 40.50 C ANISOU 3474 CB LYS B 96 5042 5776 4570 -434 -371 -211 C ATOM 3475 CG LYS B 96 -7.895 18.255 13.595 1.00 42.92 C ANISOU 3475 CG LYS B 96 5415 6039 4853 -548 -353 -303 C ATOM 3476 CD LYS B 96 -8.629 18.597 14.876 1.00 40.41 C ANISOU 3476 CD LYS B 96 5231 5699 4426 -539 -337 -333 C ATOM 3477 CE LYS B 96 -10.119 18.324 14.754 1.00 39.03 C ANISOU 3477 CE LYS B 96 5130 5424 4277 -464 -228 -284 C ATOM 3478 NZ LYS B 96 -10.893 18.950 15.864 1.00 33.99 N ANISOU 3478 NZ LYS B 96 4621 4757 3537 -461 -185 -327 N ATOM 3479 N VAL B 97 -7.407 14.125 11.616 1.00 40.12 N ANISOU 3479 N VAL B 97 4852 5735 4655 -233 -375 -59 N ATOM 3480 CA VAL B 97 -7.290 12.663 11.548 1.00 42.15 C ANISOU 3480 CA VAL B 97 5103 5996 4916 -112 -401 17 C ATOM 3481 C VAL B 97 -6.089 12.202 10.712 1.00 43.98 C ANISOU 3481 C VAL B 97 5211 6307 5191 -59 -442 21 C ATOM 3482 O VAL B 97 -5.394 11.246 11.070 1.00 41.92 O ANISOU 3482 O VAL B 97 4919 6114 4895 43 -505 62 O ATOM 3483 CB VAL B 97 -8.576 12.043 10.938 1.00 40.10 C ANISOU 3483 CB VAL B 97 4918 5601 4717 -79 -324 65 C ATOM 3484 CG1 VAL B 97 -8.376 10.559 10.629 1.00 40.41 C ANISOU 3484 CG1 VAL B 97 4964 5617 4774 33 -348 134 C ATOM 3485 CG2 VAL B 97 -9.761 12.253 11.866 1.00 37.52 C ANISOU 3485 CG2 VAL B 97 4694 5219 4342 -108 -277 80 C ATOM 3486 N GLU B 98 -5.856 12.890 9.597 1.00 45.50 N ANISOU 3486 N GLU B 98 5340 6494 5455 -118 -400 -19 N ATOM 3487 CA GLU B 98 -4.763 12.550 8.683 1.00 47.56 C ANISOU 3487 CA GLU B 98 5476 6837 5756 -71 -415 -18 C ATOM 3488 C GLU B 98 -3.400 13.062 9.164 1.00 49.81 C ANISOU 3488 C GLU B 98 5629 7293 6005 -117 -488 -54 C ATOM 3489 O GLU B 98 -2.407 12.935 8.444 1.00 51.04 O ANISOU 3489 O GLU B 98 5653 7546 6194 -91 -493 -58 O ATOM 3490 CB GLU B 98 -5.068 13.091 7.278 1.00 46.96 C ANISOU 3490 CB GLU B 98 5391 6693 5758 -120 -333 -39 C ATOM 3491 CG GLU B 98 -6.319 12.481 6.628 1.00 48.91 C ANISOU 3491 CG GLU B 98 5745 6793 6046 -69 -277 -6 C ATOM 3492 CD GLU B 98 -6.115 11.053 6.134 1.00 51.90 C ANISOU 3492 CD GLU B 98 6126 7155 6438 68 -291 37 C ATOM 3493 OE1 GLU B 98 -4.979 10.536 6.211 1.00 53.15 O ANISOU 3493 OE1 GLU B 98 6197 7419 6577 146 -335 45 O ATOM 3494 OE2 GLU B 98 -7.104 10.446 5.664 1.00 45.70 O ANISOU 3494 OE2 GLU B 98 5431 6250 5683 99 -260 62 O ATOM 3495 N GLU B 99 -3.366 13.634 10.371 1.00 51.80 N ANISOU 3495 N GLU B 99 5910 7587 6184 -186 -544 -83 N ATOM 3496 CA GLU B 99 -2.145 14.145 11.012 1.00 55.43 C ANISOU 3496 CA GLU B 99 6250 8214 6597 -249 -635 -125 C ATOM 3497 C GLU B 99 -1.479 15.294 10.252 1.00 56.74 C ANISOU 3497 C GLU B 99 6312 8429 6818 -396 -608 -183 C ATOM 3498 O GLU B 99 -0.266 15.492 10.362 1.00 57.56 O ANISOU 3498 O GLU B 99 6260 8696 6914 -438 -673 -205 O ATOM 3499 CB GLU B 99 -1.130 13.019 11.259 1.00 57.11 C ANISOU 3499 CB GLU B 99 6350 8568 6780 -104 -718 -78 C ATOM 3500 CG GLU B 99 -1.681 11.865 12.071 1.00 59.86 C ANISOU 3500 CG GLU B 99 6815 8864 7064 38 -750 -10 C ATOM 3501 CD GLU B 99 -0.603 11.136 12.855 1.00 68.58 C ANISOU 3501 CD GLU B 99 7829 10132 8096 152 -870 23 C ATOM 3502 OE1 GLU B 99 0.413 10.728 12.249 1.00 75.26 O ANISOU 3502 OE1 GLU B 99 8523 11094 8980 232 -894 33 O ATOM 3503 OE2 GLU B 99 -0.781 10.964 14.081 1.00 69.77 O ANISOU 3503 OE2 GLU B 99 8063 10302 8145 174 -937 41 O ATOM 3504 N PHE B 100 -2.270 16.052 9.493 1.00 56.78 N ANISOU 3504 N PHE B 100 6399 8297 6877 -477 -513 -202 N ATOM 3505 CA PHE B 100 -1.754 17.230 8.791 1.00 59.67 C ANISOU 3505 CA PHE B 100 6703 8678 7291 -631 -477 -249 C ATOM 3506 C PHE B 100 -1.717 18.451 9.703 1.00 59.56 C ANISOU 3506 C PHE B 100 6748 8654 7228 -791 -518 -322 C ATOM 3507 O PHE B 100 -0.773 19.242 9.644 1.00 60.47 O ANISOU 3507 O PHE B 100 6767 8857 7353 -932 -549 -366 O ATOM 3508 CB PHE B 100 -2.554 17.519 7.515 1.00 59.05 C ANISOU 3508 CB PHE B 100 6695 8457 7283 -635 -362 -232 C ATOM 3509 CG PHE B 100 -2.009 16.823 6.306 1.00 66.34 C ANISOU 3509 CG PHE B 100 7511 9435 8259 -553 -320 -191 C ATOM 3510 CD1 PHE B 100 -1.246 17.515 5.374 1.00 73.28 C ANISOU 3510 CD1 PHE B 100 8292 10370 9180 -650 -271 -202 C ATOM 3511 CD2 PHE B 100 -2.228 15.461 6.116 1.00 72.81 C ANISOU 3511 CD2 PHE B 100 8335 10250 9079 -380 -325 -141 C ATOM 3512 CE1 PHE B 100 -0.726 16.864 4.254 1.00 78.29 C ANISOU 3512 CE1 PHE B 100 8831 11067 9850 -562 -221 -166 C ATOM 3513 CE2 PHE B 100 -1.716 14.799 5.001 1.00 75.69 C ANISOU 3513 CE2 PHE B 100 8618 10661 9481 -289 -284 -113 C ATOM 3514 CZ PHE B 100 -0.961 15.501 4.069 1.00 78.77 C ANISOU 3514 CZ PHE B 100 8904 11120 9906 -374 -229 -126 C ATOM 3515 N GLY B 101 -2.738 18.595 10.545 1.00 57.97 N ANISOU 3515 N GLY B 101 6707 8348 6972 -774 -516 -337 N ATOM 3516 CA GLY B 101 -2.783 19.681 11.525 1.00 57.87 C ANISOU 3516 CA GLY B 101 6782 8312 6893 -903 -557 -415 C ATOM 3517 C GLY B 101 -4.190 20.090 11.906 1.00 55.85 C ANISOU 3517 C GLY B 101 6720 7891 6610 -881 -490 -430 C ATOM 3518 O GLY B 101 -5.171 19.706 11.255 1.00 52.83 O ANISOU 3518 O GLY B 101 6392 7403 6277 -793 -406 -380 O ATOM 3519 N VAL B 102 -4.284 20.870 12.975 1.00 56.60 N ANISOU 3519 N VAL B 102 6916 7970 6621 -959 -531 -502 N ATOM 3520 CA VAL B 102 -5.540 21.526 13.331 1.00 55.27 C ANISOU 3520 CA VAL B 102 6932 7647 6423 -950 -457 -532 C ATOM 3521 C VAL B 102 -5.503 22.888 12.653 1.00 53.54 C ANISOU 3521 C VAL B 102 6768 7316 6257 -1085 -408 -590 C ATOM 3522 O VAL B 102 -4.698 23.748 13.019 1.00 56.77 O ANISOU 3522 O VAL B 102 7180 7753 6636 -1232 -468 -666 O ATOM 3523 CB VAL B 102 -5.795 21.593 14.886 1.00 57.05 C ANISOU 3523 CB VAL B 102 7267 7899 6510 -935 -511 -579 C ATOM 3524 CG1 VAL B 102 -4.515 21.373 15.674 1.00 61.73 C ANISOU 3524 CG1 VAL B 102 7765 8664 7027 -989 -651 -610 C ATOM 3525 CG2 VAL B 102 -6.484 22.900 15.301 1.00 56.04 C ANISOU 3525 CG2 VAL B 102 7318 7635 6339 -1006 -461 -667 C ATOM 3526 N VAL B 103 -6.328 23.052 11.617 1.00 49.73 N ANISOU 3526 N VAL B 103 6328 6712 5856 -1041 -306 -551 N ATOM 3527 CA VAL B 103 -6.452 24.335 10.947 1.00 46.28 C ANISOU 3527 CA VAL B 103 5976 6143 5465 -1145 -249 -591 C ATOM 3528 C VAL B 103 -6.922 25.320 12.005 1.00 46.94 C ANISOU 3528 C VAL B 103 6236 6134 5465 -1191 -253 -680 C ATOM 3529 O VAL B 103 -7.829 25.016 12.782 1.00 47.29 O ANISOU 3529 O VAL B 103 6364 6156 5448 -1082 -232 -680 O ATOM 3530 CB VAL B 103 -7.454 24.304 9.772 1.00 45.51 C ANISOU 3530 CB VAL B 103 5916 5929 5447 -1057 -146 -529 C ATOM 3531 CG1 VAL B 103 -7.525 25.675 9.096 1.00 41.54 C ANISOU 3531 CG1 VAL B 103 5517 5283 4981 -1159 -91 -562 C ATOM 3532 CG2 VAL B 103 -7.075 23.225 8.754 1.00 40.22 C ANISOU 3532 CG2 VAL B 103 5093 5346 4844 -994 -141 -448 C ATOM 3533 N SER B 104 -6.282 26.482 12.078 1.00 46.24 N ANISOU 3533 N SER B 104 6209 5994 5368 -1355 -279 -757 N ATOM 3534 CA SER B 104 -6.633 27.439 13.114 1.00 45.97 C ANISOU 3534 CA SER B 104 6360 5863 5244 -1402 -291 -857 C ATOM 3535 C SER B 104 -8.069 27.906 12.899 1.00 43.83 C ANISOU 3535 C SER B 104 6251 5418 4983 -1281 -177 -849 C ATOM 3536 O SER B 104 -8.637 27.736 11.812 1.00 42.62 O ANISOU 3536 O SER B 104 6068 5209 4918 -1207 -101 -774 O ATOM 3537 CB SER B 104 -5.663 28.628 13.137 1.00 47.78 C ANISOU 3537 CB SER B 104 6637 6046 5470 -1621 -342 -944 C ATOM 3538 OG SER B 104 -5.776 29.404 11.964 1.00 46.53 O ANISOU 3538 OG SER B 104 6527 5748 5405 -1682 -261 -918 O ATOM 3539 N ASN B 105 -8.655 28.464 13.948 1.00 44.46 N ANISOU 3539 N ASN B 105 6498 5428 4967 -1252 -168 -926 N ATOM 3540 CA ASN B 105 -10.016 28.965 13.884 1.00 45.03 C ANISOU 3540 CA ASN B 105 6720 5351 5037 -1122 -59 -928 C ATOM 3541 C ASN B 105 -10.134 29.965 12.749 1.00 44.50 C ANISOU 3541 C ASN B 105 6729 5119 5059 -1172 1 -922 C ATOM 3542 O ASN B 105 -10.941 29.796 11.850 1.00 43.98 O ANISOU 3542 O ASN B 105 6643 5002 5067 -1061 77 -846 O ATOM 3543 CB ASN B 105 -10.424 29.638 15.202 1.00 47.08 C ANISOU 3543 CB ASN B 105 7169 5552 5167 -1104 -59 -1035 C ATOM 3544 CG ASN B 105 -10.464 28.670 16.385 1.00 49.24 C ANISOU 3544 CG ASN B 105 7396 5982 5332 -1035 -104 -1032 C ATOM 3545 OD1 ASN B 105 -10.354 27.448 16.226 1.00 46.71 O ANISOU 3545 OD1 ASN B 105 6911 5796 5039 -978 -125 -941 O ATOM 3546 ND2 ASN B 105 -10.623 29.222 17.583 1.00 50.17 N ANISOU 3546 ND2 ASN B 105 7675 6071 5315 -1035 -118 -1133 N ATOM 3547 N THR B 106 -9.299 30.994 12.782 1.00 46.54 N ANISOU 3547 N THR B 106 7076 5297 5308 -1348 -40 -998 N ATOM 3548 CA THR B 106 -9.433 32.112 11.855 1.00 47.29 C ANISOU 3548 CA THR B 106 7297 5203 5468 -1405 21 -999 C ATOM 3549 C THR B 106 -9.099 31.703 10.429 1.00 45.58 C ANISOU 3549 C THR B 106 6931 5025 5363 -1425 47 -890 C ATOM 3550 O THR B 106 -9.671 32.234 9.480 1.00 46.72 O ANISOU 3550 O THR B 106 7153 5034 5564 -1375 124 -843 O ATOM 3551 CB THR B 106 -8.539 33.299 12.264 1.00 50.24 C ANISOU 3551 CB THR B 106 7811 5474 5804 -1621 -33 -1108 C ATOM 3552 OG1 THR B 106 -7.169 32.890 12.246 1.00 55.35 O ANISOU 3552 OG1 THR B 106 8280 6283 6468 -1800 -130 -1107 O ATOM 3553 CG2 THR B 106 -8.904 33.794 13.653 1.00 49.61 C ANISOU 3553 CG2 THR B 106 7914 5336 5598 -1596 -57 -1230 C ATOM 3554 N ARG B 107 -8.183 30.753 10.282 1.00 44.09 N ANISOU 3554 N ARG B 107 6532 5023 5197 -1483 -15 -849 N ATOM 3555 CA ARG B 107 -7.805 30.254 8.964 1.00 43.17 C ANISOU 3555 CA ARG B 107 6265 4964 5172 -1491 12 -751 C ATOM 3556 C ARG B 107 -8.890 29.381 8.344 1.00 41.44 C ANISOU 3556 C ARG B 107 5995 4759 4991 -1286 72 -662 C ATOM 3557 O ARG B 107 -9.118 29.439 7.135 1.00 38.39 O ANISOU 3557 O ARG B 107 5594 4323 4669 -1255 127 -593 O ATOM 3558 CB ARG B 107 -6.500 29.475 9.052 1.00 44.69 C ANISOU 3558 CB ARG B 107 6247 5360 5371 -1592 -71 -740 C ATOM 3559 CG ARG B 107 -5.991 29.010 7.730 1.00 44.94 C ANISOU 3559 CG ARG B 107 6130 5460 5486 -1604 -36 -651 C ATOM 3560 CD ARG B 107 -4.477 28.974 7.670 1.00 47.39 C ANISOU 3560 CD ARG B 107 6279 5917 5810 -1781 -98 -663 C ATOM 3561 NE ARG B 107 -4.061 28.191 6.508 1.00 50.49 N ANISOU 3561 NE ARG B 107 6502 6416 6266 -1736 -60 -572 N ATOM 3562 CZ ARG B 107 -3.843 26.877 6.508 1.00 50.01 C ANISOU 3562 CZ ARG B 107 6275 6519 6208 -1616 -92 -528 C ATOM 3563 NH1 ARG B 107 -3.962 26.158 7.624 1.00 52.23 N ANISOU 3563 NH1 ARG B 107 6528 6885 6432 -1536 -167 -556 N ATOM 3564 NH2 ARG B 107 -3.492 26.277 5.378 1.00 51.80 N ANISOU 3564 NH2 ARG B 107 6377 6820 6486 -1573 -47 -455 N ATOM 3565 N LEU B 108 -9.560 28.572 9.166 1.00 39.62 N ANISOU 3565 N LEU B 108 5739 4599 4715 -1155 59 -663 N ATOM 3566 CA LEU B 108 -10.667 27.755 8.673 1.00 36.89 C ANISOU 3566 CA LEU B 108 5346 4264 4404 -979 112 -585 C ATOM 3567 C LEU B 108 -11.816 28.646 8.201 1.00 35.79 C ANISOU 3567 C LEU B 108 5355 3958 4286 -892 194 -579 C ATOM 3568 O LEU B 108 -12.314 28.464 7.100 1.00 32.28 O ANISOU 3568 O LEU B 108 4876 3486 3903 -821 235 -508 O ATOM 3569 CB LEU B 108 -11.164 26.787 9.747 1.00 36.80 C ANISOU 3569 CB LEU B 108 5293 4353 4335 -877 90 -584 C ATOM 3570 CG LEU B 108 -12.271 25.808 9.336 1.00 36.16 C ANISOU 3570 CG LEU B 108 5147 4300 4293 -720 136 -503 C ATOM 3571 CD1 LEU B 108 -11.843 24.969 8.141 1.00 37.71 C ANISOU 3571 CD1 LEU B 108 5205 4558 4565 -719 122 -428 C ATOM 3572 CD2 LEU B 108 -12.625 24.921 10.508 1.00 35.01 C ANISOU 3572 CD2 LEU B 108 4974 4248 4080 -652 118 -501 C ATOM 3573 N ILE B 109 -12.217 29.612 9.029 1.00 36.01 N ANISOU 3573 N ILE B 109 5551 3876 4256 -889 215 -657 N ATOM 3574 CA ILE B 109 -13.332 30.496 8.686 1.00 37.00 C ANISOU 3574 CA ILE B 109 5826 3841 4393 -780 294 -656 C ATOM 3575 C ILE B 109 -12.962 31.405 7.518 1.00 38.02 C ANISOU 3575 C ILE B 109 6030 3839 4578 -858 317 -630 C ATOM 3576 O ILE B 109 -13.771 31.611 6.615 1.00 37.75 O ANISOU 3576 O ILE B 109 6026 3730 4587 -747 370 -569 O ATOM 3577 CB ILE B 109 -13.813 31.355 9.876 1.00 40.19 C ANISOU 3577 CB ILE B 109 6412 4147 4710 -744 317 -754 C ATOM 3578 CG1 ILE B 109 -14.222 30.471 11.067 1.00 41.54 C ANISOU 3578 CG1 ILE B 109 6521 4453 4811 -663 307 -772 C ATOM 3579 CG2 ILE B 109 -15.001 32.233 9.457 1.00 38.02 C ANISOU 3579 CG2 ILE B 109 6282 3712 4452 -597 404 -745 C ATOM 3580 CD1 ILE B 109 -15.330 29.456 10.753 1.00 34.11 C ANISOU 3580 CD1 ILE B 109 5452 3600 3910 -497 355 -680 C ATOM 3581 N ALA B 110 -11.738 31.928 7.526 1.00 40.10 N ANISOU 3581 N ALA B 110 6318 4082 4837 -1052 276 -670 N ATOM 3582 CA ALA B 110 -11.259 32.756 6.423 1.00 41.01 C ANISOU 3582 CA ALA B 110 6501 4080 5001 -1155 304 -636 C ATOM 3583 C ALA B 110 -11.238 31.967 5.120 1.00 38.64 C ANISOU 3583 C ALA B 110 6048 3867 4766 -1108 323 -526 C ATOM 3584 O ALA B 110 -11.593 32.497 4.078 1.00 40.09 O ANISOU 3584 O ALA B 110 6309 3942 4982 -1072 374 -467 O ATOM 3585 CB ALA B 110 -9.874 33.331 6.730 1.00 43.77 C ANISOU 3585 CB ALA B 110 6867 4425 5337 -1399 254 -697 C ATOM 3586 N ALA B 111 -10.852 30.694 5.179 1.00 37.47 N ANISOU 3586 N ALA B 111 5700 3908 4628 -1094 280 -497 N ATOM 3587 CA ALA B 111 -10.813 29.859 3.979 1.00 36.04 C ANISOU 3587 CA ALA B 111 5384 3812 4497 -1042 293 -405 C ATOM 3588 C ALA B 111 -12.224 29.611 3.414 1.00 36.78 C ANISOU 3588 C ALA B 111 5506 3858 4610 -849 334 -350 C ATOM 3589 O ALA B 111 -12.450 29.770 2.217 1.00 36.44 O ANISOU 3589 O ALA B 111 5480 3770 4598 -813 367 -285 O ATOM 3590 CB ALA B 111 -10.097 28.535 4.267 1.00 35.81 C ANISOU 3590 CB ALA B 111 5156 3983 4470 -1056 236 -396 C ATOM 3591 N ALA B 112 -13.175 29.244 4.271 1.00 36.30 N ANISOU 3591 N ALA B 112 5449 3817 4526 -728 332 -374 N ATOM 3592 CA ALA B 112 -14.558 29.031 3.819 1.00 36.26 C ANISOU 3592 CA ALA B 112 5449 3785 4542 -552 367 -325 C ATOM 3593 C ALA B 112 -15.175 30.318 3.247 1.00 36.55 C ANISOU 3593 C ALA B 112 5656 3647 4583 -499 418 -315 C ATOM 3594 O ALA B 112 -15.823 30.301 2.197 1.00 35.75 O ANISOU 3594 O ALA B 112 5551 3521 4511 -403 436 -247 O ATOM 3595 CB ALA B 112 -15.417 28.479 4.954 1.00 34.39 C ANISOU 3595 CB ALA B 112 5182 3610 4277 -451 367 -352 C ATOM 3596 N THR B 113 -14.952 31.433 3.932 1.00 37.18 N ANISOU 3596 N THR B 113 5898 3602 4627 -558 436 -383 N ATOM 3597 CA THR B 113 -15.465 32.733 3.495 1.00 37.27 C ANISOU 3597 CA THR B 113 6106 3420 4636 -505 486 -379 C ATOM 3598 C THR B 113 -14.930 33.102 2.116 1.00 38.01 C ANISOU 3598 C THR B 113 6229 3452 4762 -576 498 -306 C ATOM 3599 O THR B 113 -15.700 33.410 1.203 1.00 38.76 O ANISOU 3599 O THR B 113 6377 3477 4871 -453 526 -240 O ATOM 3600 CB THR B 113 -15.077 33.825 4.502 1.00 39.92 C ANISOU 3600 CB THR B 113 6626 3619 4923 -594 494 -478 C ATOM 3601 OG1 THR B 113 -15.562 33.458 5.799 1.00 37.78 O ANISOU 3601 OG1 THR B 113 6334 3416 4603 -522 489 -546 O ATOM 3602 CG2 THR B 113 -15.650 35.190 4.093 1.00 41.84 C ANISOU 3602 CG2 THR B 113 7103 3635 5160 -522 550 -475 C ATOM 3603 N SER B 114 -13.610 33.032 1.969 1.00 37.79 N ANISOU 3603 N SER B 114 6152 3467 4739 -770 476 -313 N ATOM 3604 CA SER B 114 -12.931 33.343 0.711 1.00 40.23 C ANISOU 3604 CA SER B 114 6476 3739 5070 -864 500 -242 C ATOM 3605 C SER B 114 -13.338 32.429 -0.449 1.00 38.33 C ANISOU 3605 C SER B 114 6108 3603 4851 -752 499 -151 C ATOM 3606 O SER B 114 -13.667 32.900 -1.538 1.00 39.73 O ANISOU 3606 O SER B 114 6370 3696 5029 -700 532 -80 O ATOM 3607 CB SER B 114 -11.410 33.283 0.916 1.00 41.87 C ANISOU 3607 CB SER B 114 6607 4020 5281 -1095 477 -272 C ATOM 3608 OG SER B 114 -10.711 33.603 -0.274 1.00 47.01 O ANISOU 3608 OG SER B 114 7266 4646 5949 -1197 516 -200 O ATOM 3609 N VAL B 115 -13.321 31.122 -0.219 1.00 39.02 N ANISOU 3609 N VAL B 115 6008 3868 4950 -715 458 -154 N ATOM 3610 CA VAL B 115 -13.649 30.166 -1.273 1.00 37.90 C ANISOU 3610 CA VAL B 115 5750 3825 4824 -622 448 -83 C ATOM 3611 C VAL B 115 -15.087 30.350 -1.768 1.00 39.20 C ANISOU 3611 C VAL B 115 5977 3926 4990 -437 456 -40 C ATOM 3612 O VAL B 115 -15.313 30.424 -2.975 1.00 39.51 O ANISOU 3612 O VAL B 115 6041 3945 5025 -386 466 28 O ATOM 3613 CB VAL B 115 -13.400 28.704 -0.827 1.00 37.63 C ANISOU 3613 CB VAL B 115 5525 3972 4802 -613 400 -100 C ATOM 3614 CG1 VAL B 115 -14.125 27.727 -1.739 1.00 32.46 C ANISOU 3614 CG1 VAL B 115 4784 3389 4160 -487 382 -43 C ATOM 3615 CG2 VAL B 115 -11.910 28.415 -0.810 1.00 35.94 C ANISOU 3615 CG2 VAL B 115 5219 3848 4586 -770 390 -114 C ATOM 3616 N LEU B 116 -16.054 30.451 -0.858 1.00 39.51 N ANISOU 3616 N LEU B 116 6040 3944 5030 -331 453 -79 N ATOM 3617 CA LEU B 116 -17.440 30.672 -1.292 1.00 41.38 C ANISOU 3617 CA LEU B 116 6313 4137 5271 -147 460 -39 C ATOM 3618 C LEU B 116 -17.576 31.964 -2.101 1.00 43.53 C ANISOU 3618 C LEU B 116 6774 4240 5527 -115 497 4 C ATOM 3619 O LEU B 116 -18.279 32.000 -3.109 1.00 43.49 O ANISOU 3619 O LEU B 116 6780 4226 5521 2 489 73 O ATOM 3620 CB LEU B 116 -18.418 30.673 -0.121 1.00 39.53 C ANISOU 3620 CB LEU B 116 6071 3912 5036 -39 469 -88 C ATOM 3621 CG LEU B 116 -18.646 29.347 0.613 1.00 43.95 C ANISOU 3621 CG LEU B 116 6454 4635 5609 -31 438 -108 C ATOM 3622 CD1 LEU B 116 -19.846 29.475 1.529 1.00 47.13 C ANISOU 3622 CD1 LEU B 116 6857 5045 6006 104 466 -134 C ATOM 3623 CD2 LEU B 116 -18.831 28.162 -0.332 1.00 41.59 C ANISOU 3623 CD2 LEU B 116 6009 4456 5340 -7 393 -49 C ATOM 3624 N LYS B 117 -16.881 33.011 -1.669 1.00 46.84 N ANISOU 3624 N LYS B 117 7347 4521 5929 -226 532 -34 N ATOM 3625 CA LYS B 117 -16.957 34.315 -2.321 1.00 48.68 C ANISOU 3625 CA LYS B 117 7793 4560 6144 -209 574 6 C ATOM 3626 C LYS B 117 -16.264 34.334 -3.690 1.00 49.71 C ANISOU 3626 C LYS B 117 7934 4688 6265 -290 585 92 C ATOM 3627 O LYS B 117 -16.754 34.962 -4.625 1.00 51.85 O ANISOU 3627 O LYS B 117 8327 4857 6516 -196 603 166 O ATOM 3628 CB LYS B 117 -16.344 35.383 -1.411 1.00 51.67 C ANISOU 3628 CB LYS B 117 8343 4782 6506 -333 605 -69 C ATOM 3629 CG LYS B 117 -16.349 36.787 -2.001 1.00 57.60 C ANISOU 3629 CG LYS B 117 9349 5298 7238 -335 652 -29 C ATOM 3630 CD LYS B 117 -15.897 37.831 -0.995 1.00 61.44 C ANISOU 3630 CD LYS B 117 10025 5613 7708 -448 676 -120 C ATOM 3631 CE LYS B 117 -16.094 39.244 -1.541 1.00 67.26 C ANISOU 3631 CE LYS B 117 11048 6084 8425 -418 725 -79 C ATOM 3632 NZ LYS B 117 -15.316 39.472 -2.793 1.00 68.64 N ANISOU 3632 NZ LYS B 117 11259 6219 8600 -551 749 22 N ATOM 3633 N THR B 118 -15.129 33.647 -3.799 1.00 49.48 N ANISOU 3633 N THR B 118 7778 4777 6244 -454 576 85 N ATOM 3634 CA THR B 118 -14.283 33.705 -4.993 1.00 50.45 C ANISOU 3634 CA THR B 118 7910 4908 6351 -556 606 159 C ATOM 3635 C THR B 118 -14.693 32.710 -6.082 1.00 48.84 C ANISOU 3635 C THR B 118 7586 4836 6134 -444 578 223 C ATOM 3636 O THR B 118 -14.764 33.068 -7.258 1.00 49.06 O ANISOU 3636 O THR B 118 7699 4816 6127 -410 602 305 O ATOM 3637 CB THR B 118 -12.800 33.446 -4.623 1.00 51.80 C ANISOU 3637 CB THR B 118 7985 5163 6535 -781 616 120 C ATOM 3638 OG1 THR B 118 -12.282 34.578 -3.917 1.00 54.47 O ANISOU 3638 OG1 THR B 118 8471 5352 6874 -923 642 72 O ATOM 3639 CG2 THR B 118 -11.951 33.202 -5.870 1.00 54.95 C ANISOU 3639 CG2 THR B 118 8334 5629 6915 -865 653 197 C ATOM 3640 N ARG B 119 -14.947 31.465 -5.690 1.00 45.39 N ANISOU 3640 N ARG B 119 6966 4560 5719 -391 527 187 N ATOM 3641 CA ARG B 119 -15.223 30.391 -6.650 1.00 43.76 C ANISOU 3641 CA ARG B 119 6644 4483 5501 -310 492 230 C ATOM 3642 C ARG B 119 -16.722 30.082 -6.807 1.00 41.01 C ANISOU 3642 C ARG B 119 6276 4150 5157 -116 441 246 C ATOM 3643 O ARG B 119 -17.135 29.569 -7.849 1.00 41.15 O ANISOU 3643 O ARG B 119 6260 4226 5150 -36 408 294 O ATOM 3644 CB ARG B 119 -14.410 29.144 -6.262 1.00 43.83 C ANISOU 3644 CB ARG B 119 6470 4654 5529 -391 468 186 C ATOM 3645 CG ARG B 119 -14.897 27.792 -6.803 1.00 50.28 C ANISOU 3645 CG ARG B 119 7158 5602 6345 -292 415 197 C ATOM 3646 CD ARG B 119 -14.571 27.534 -8.282 1.00 54.10 C ANISOU 3646 CD ARG B 119 7654 6123 6780 -279 427 257 C ATOM 3647 NE ARG B 119 -14.887 26.143 -8.632 1.00 57.62 N ANISOU 3647 NE ARG B 119 7979 6690 7223 -207 370 244 N ATOM 3648 CZ ARG B 119 -16.105 25.675 -8.930 1.00 62.87 C ANISOU 3648 CZ ARG B 119 8627 7372 7890 -83 306 252 C ATOM 3649 NH1 ARG B 119 -17.166 26.482 -8.966 1.00 66.37 N ANISOU 3649 NH1 ARG B 119 9150 7734 8333 8 292 279 N ATOM 3650 NH2 ARG B 119 -16.265 24.384 -9.224 1.00 61.56 N ANISOU 3650 NH2 ARG B 119 8362 7304 7723 -47 253 233 N ATOM 3651 N PHE B 120 -17.539 30.422 -5.810 1.00 39.03 N ANISOU 3651 N PHE B 120 6044 3853 4932 -41 434 205 N ATOM 3652 CA PHE B 120 -18.951 30.005 -5.798 1.00 38.64 C ANISOU 3652 CA PHE B 120 5928 3856 4898 132 387 214 C ATOM 3653 C PHE B 120 -19.976 31.132 -5.611 1.00 38.75 C ANISOU 3653 C PHE B 120 6069 3747 4907 274 406 229 C ATOM 3654 O PHE B 120 -21.096 30.881 -5.143 1.00 38.24 O ANISOU 3654 O PHE B 120 5928 3734 4865 404 382 216 O ATOM 3655 CB PHE B 120 -19.163 28.938 -4.719 1.00 37.05 C ANISOU 3655 CB PHE B 120 5566 3776 4735 119 359 154 C ATOM 3656 CG PHE B 120 -18.308 27.722 -4.899 1.00 35.88 C ANISOU 3656 CG PHE B 120 5293 3749 4592 18 333 142 C ATOM 3657 CD1 PHE B 120 -18.628 26.773 -5.858 1.00 37.35 C ANISOU 3657 CD1 PHE B 120 5395 4023 4772 65 283 175 C ATOM 3658 CD2 PHE B 120 -17.178 27.527 -4.120 1.00 38.30 C ANISOU 3658 CD2 PHE B 120 5569 4079 4903 -117 352 95 C ATOM 3659 CE1 PHE B 120 -17.845 25.650 -6.034 1.00 35.04 C ANISOU 3659 CE1 PHE B 120 5005 3828 4480 -9 263 160 C ATOM 3660 CE2 PHE B 120 -16.389 26.400 -4.291 1.00 37.12 C ANISOU 3660 CE2 PHE B 120 5304 4043 4757 -184 328 88 C ATOM 3661 CZ PHE B 120 -16.721 25.464 -5.254 1.00 36.41 C ANISOU 3661 CZ PHE B 120 5146 4026 4662 -125 289 120 C ATOM 3662 N SER B 121 -19.624 32.355 -5.993 1.00 38.00 N ANISOU 3662 N SER B 121 6166 3490 4781 257 451 261 N ATOM 3663 CA SER B 121 -20.536 33.492 -5.800 1.00 42.31 C ANISOU 3663 CA SER B 121 6862 3895 5319 409 474 274 C ATOM 3664 C SER B 121 -21.814 33.378 -6.636 1.00 43.30 C ANISOU 3664 C SER B 121 6947 4071 5435 616 423 340 C ATOM 3665 O SER B 121 -22.820 34.004 -6.316 1.00 46.82 O ANISOU 3665 O SER B 121 7444 4461 5885 785 429 342 O ATOM 3666 CB SER B 121 -19.847 34.838 -6.078 1.00 42.79 C ANISOU 3666 CB SER B 121 7164 3745 5347 336 533 300 C ATOM 3667 OG SER B 121 -19.578 35.014 -7.456 1.00 48.17 O ANISOU 3667 OG SER B 121 7915 4400 5987 331 531 394 O ATOM 3668 N TYR B 122 -21.776 32.587 -7.701 1.00 42.78 N ANISOU 3668 N TYR B 122 6789 4116 5351 610 370 389 N ATOM 3669 CA TYR B 122 -22.993 32.274 -8.453 1.00 45.11 C ANISOU 3669 CA TYR B 122 7007 4496 5635 789 298 440 C ATOM 3670 C TYR B 122 -24.066 31.572 -7.614 1.00 46.03 C ANISOU 3670 C TYR B 122 6938 4743 5806 881 262 394 C ATOM 3671 O TYR B 122 -25.253 31.795 -7.826 1.00 50.74 O ANISOU 3671 O TYR B 122 7499 5374 6407 1059 225 426 O ATOM 3672 CB TYR B 122 -22.672 31.443 -9.696 1.00 42.19 C ANISOU 3672 CB TYR B 122 6577 4229 5225 745 242 484 C ATOM 3673 CG TYR B 122 -22.024 30.110 -9.435 1.00 39.42 C ANISOU 3673 CG TYR B 122 6063 4012 4901 604 224 430 C ATOM 3674 CD1 TYR B 122 -22.791 28.989 -9.134 1.00 42.97 C ANISOU 3674 CD1 TYR B 122 6327 4608 5392 642 158 396 C ATOM 3675 CD2 TYR B 122 -20.649 29.951 -9.525 1.00 35.00 C ANISOU 3675 CD2 TYR B 122 5536 3437 4326 435 272 416 C ATOM 3676 CE1 TYR B 122 -22.210 27.768 -8.910 1.00 33.88 C ANISOU 3676 CE1 TYR B 122 5052 3558 4262 524 141 351 C ATOM 3677 CE2 TYR B 122 -20.058 28.721 -9.295 1.00 32.13 C ANISOU 3677 CE2 TYR B 122 5028 3195 3984 332 254 369 C ATOM 3678 CZ TYR B 122 -20.848 27.630 -8.991 1.00 34.19 C ANISOU 3678 CZ TYR B 122 5131 3577 4282 382 187 337 C ATOM 3679 OH TYR B 122 -20.277 26.386 -8.766 1.00 33.22 O ANISOU 3679 OH TYR B 122 4888 3555 4178 290 168 295 O ATOM 3680 N ALA B 123 -23.640 30.735 -6.668 1.00 45.73 N ANISOU 3680 N ALA B 123 6781 4786 5809 760 276 326 N ATOM 3681 CA ALA B 123 -24.549 29.992 -5.795 1.00 45.57 C ANISOU 3681 CA ALA B 123 6586 4892 5838 816 257 287 C ATOM 3682 C ALA B 123 -24.786 30.698 -4.461 1.00 47.03 C ANISOU 3682 C ALA B 123 6824 5007 6038 858 330 234 C ATOM 3683 O ALA B 123 -25.863 30.577 -3.881 1.00 48.43 O ANISOU 3683 O ALA B 123 6901 5258 6242 978 334 224 O ATOM 3684 CB ALA B 123 -23.999 28.579 -5.546 1.00 44.13 C ANISOU 3684 CB ALA B 123 6252 4835 5680 671 228 252 C ATOM 3685 N PHE B 124 -23.776 31.414 -3.966 1.00 48.32 N ANISOU 3685 N PHE B 124 7142 5037 6180 754 389 197 N ATOM 3686 CA PHE B 124 -23.853 32.058 -2.652 1.00 48.64 C ANISOU 3686 CA PHE B 124 7257 5004 6220 773 455 131 C ATOM 3687 C PHE B 124 -23.587 33.555 -2.743 1.00 50.25 C ANISOU 3687 C PHE B 124 7710 4993 6389 809 505 132 C ATOM 3688 O PHE B 124 -22.438 33.989 -2.707 1.00 51.09 O ANISOU 3688 O PHE B 124 7942 4992 6476 651 529 111 O ATOM 3689 CB PHE B 124 -22.873 31.404 -1.677 1.00 48.28 C ANISOU 3689 CB PHE B 124 7159 5007 6179 593 468 62 C ATOM 3690 CG PHE B 124 -23.052 29.923 -1.559 1.00 48.36 C ANISOU 3690 CG PHE B 124 6953 5201 6219 551 423 65 C ATOM 3691 CD1 PHE B 124 -24.204 29.398 -0.998 1.00 50.60 C ANISOU 3691 CD1 PHE B 124 7102 5594 6528 657 424 62 C ATOM 3692 CD2 PHE B 124 -22.082 29.051 -2.032 1.00 51.41 C ANISOU 3692 CD2 PHE B 124 7275 5648 6609 407 384 73 C ATOM 3693 CE1 PHE B 124 -24.385 28.020 -0.898 1.00 52.66 C ANISOU 3693 CE1 PHE B 124 7180 6007 6820 603 382 70 C ATOM 3694 CE2 PHE B 124 -22.256 27.678 -1.937 1.00 51.26 C ANISOU 3694 CE2 PHE B 124 7083 5775 6617 375 341 74 C ATOM 3695 CZ PHE B 124 -23.410 27.163 -1.366 1.00 49.19 C ANISOU 3695 CZ PHE B 124 6703 5606 6383 464 338 74 C ATOM 3696 N PRO B 125 -24.657 34.354 -2.861 1.00 52.50 N ANISOU 3696 N PRO B 125 8068 5213 6667 1019 521 159 N ATOM 3697 CA PRO B 125 -24.496 35.805 -2.875 1.00 55.44 C ANISOU 3697 CA PRO B 125 8703 5355 7004 1074 573 158 C ATOM 3698 C PRO B 125 -24.184 36.381 -1.483 1.00 56.70 C ANISOU 3698 C PRO B 125 8981 5413 7151 1028 639 56 C ATOM 3699 O PRO B 125 -23.514 37.408 -1.377 1.00 58.83 O ANISOU 3699 O PRO B 125 9481 5480 7392 958 677 32 O ATOM 3700 CB PRO B 125 -25.853 36.301 -3.383 1.00 57.98 C ANISOU 3700 CB PRO B 125 9033 5674 7324 1345 561 219 C ATOM 3701 CG PRO B 125 -26.824 35.249 -2.958 1.00 55.67 C ANISOU 3701 CG PRO B 125 8473 5609 7071 1429 534 207 C ATOM 3702 CD PRO B 125 -26.072 33.946 -2.971 1.00 52.69 C ANISOU 3702 CD PRO B 125 7928 5375 6715 1217 492 191 C ATOM 3703 N LYS B 126 -24.675 35.729 -0.431 1.00 55.53 N ANISOU 3703 N LYS B 126 8683 5400 7015 1062 654 -3 N ATOM 3704 CA LYS B 126 -24.368 36.142 0.939 1.00 55.94 C ANISOU 3704 CA LYS B 126 8835 5381 7037 1016 711 -107 C ATOM 3705 C LYS B 126 -23.063 35.492 1.388 1.00 52.90 C ANISOU 3705 C LYS B 126 8404 5046 6649 756 687 -155 C ATOM 3706 O LYS B 126 -22.700 34.417 0.904 1.00 49.87 O ANISOU 3706 O LYS B 126 7845 4808 6294 656 636 -116 O ATOM 3707 CB LYS B 126 -25.512 35.767 1.882 1.00 56.65 C ANISOU 3707 CB LYS B 126 8794 5602 7129 1181 750 -141 C ATOM 3708 CG LYS B 126 -26.792 36.547 1.621 1.00 63.21 C ANISOU 3708 CG LYS B 126 9674 6385 7958 1460 785 -106 C ATOM 3709 CD LYS B 126 -27.878 36.188 2.626 1.00 69.82 C ANISOU 3709 CD LYS B 126 10366 7369 8794 1615 840 -141 C ATOM 3710 CE LYS B 126 -29.191 36.884 2.296 1.00 75.05 C ANISOU 3710 CE LYS B 126 11034 8019 9461 1911 871 -99 C ATOM 3711 NZ LYS B 126 -30.311 36.408 3.159 1.00 77.37 N ANISOU 3711 NZ LYS B 126 11134 8501 9763 2059 930 -118 N ATOM 3712 N GLU B 127 -22.353 36.149 2.301 1.00 52.23 N ANISOU 3712 N GLU B 127 8481 4839 6526 651 718 -244 N ATOM 3713 CA GLU B 127 -21.072 35.633 2.779 1.00 51.72 C ANISOU 3713 CA GLU B 127 8373 4824 6452 409 687 -293 C ATOM 3714 C GLU B 127 -21.281 34.489 3.770 1.00 48.66 C ANISOU 3714 C GLU B 127 7795 4635 6061 403 677 -331 C ATOM 3715 O GLU B 127 -22.297 34.440 4.463 1.00 46.85 O ANISOU 3715 O GLU B 127 7533 4453 5815 560 718 -353 O ATOM 3716 CB GLU B 127 -20.221 36.743 3.406 1.00 54.59 C ANISOU 3716 CB GLU B 127 8975 4995 6772 281 709 -378 C ATOM 3717 CG GLU B 127 -20.642 37.171 4.808 1.00 61.78 C ANISOU 3717 CG GLU B 127 9986 5861 7625 356 751 -486 C ATOM 3718 CD GLU B 127 -19.901 38.410 5.297 1.00 71.19 C ANISOU 3718 CD GLU B 127 11453 6825 8770 239 767 -575 C ATOM 3719 OE1 GLU B 127 -20.378 39.043 6.264 1.00 72.00 O ANISOU 3719 OE1 GLU B 127 11706 6837 8816 341 811 -663 O ATOM 3720 OE2 GLU B 127 -18.845 38.754 4.716 1.00 76.61 O ANISOU 3720 OE2 GLU B 127 12210 7424 9474 43 737 -559 O ATOM 3721 N PHE B 128 -20.314 33.570 3.805 1.00 44.55 N ANISOU 3721 N PHE B 128 7148 4229 5551 226 627 -331 N ATOM 3722 CA PHE B 128 -20.286 32.470 4.768 1.00 41.12 C ANISOU 3722 CA PHE B 128 6557 3964 5104 192 611 -362 C ATOM 3723 C PHE B 128 -20.699 32.987 6.140 1.00 41.82 C ANISOU 3723 C PHE B 128 6749 4013 5127 257 662 -451 C ATOM 3724 O PHE B 128 -19.977 33.780 6.740 1.00 39.07 O ANISOU 3724 O PHE B 128 6565 3548 4730 161 664 -530 O ATOM 3725 CB PHE B 128 -18.877 31.872 4.833 1.00 40.02 C ANISOU 3725 CB PHE B 128 6354 3888 4963 -21 555 -378 C ATOM 3726 CG PHE B 128 -18.774 30.625 5.671 1.00 37.27 C ANISOU 3726 CG PHE B 128 5845 3715 4602 -52 527 -390 C ATOM 3727 CD1 PHE B 128 -19.315 29.422 5.219 1.00 29.98 C ANISOU 3727 CD1 PHE B 128 4740 2929 3722 6 508 -320 C ATOM 3728 CD2 PHE B 128 -18.108 30.645 6.888 1.00 37.51 C ANISOU 3728 CD2 PHE B 128 5916 3764 4571 -145 514 -469 C ATOM 3729 CE1 PHE B 128 -19.213 28.267 5.971 1.00 38.43 C ANISOU 3729 CE1 PHE B 128 5683 4138 4779 -25 486 -322 C ATOM 3730 CE2 PHE B 128 -17.988 29.479 7.652 1.00 42.80 C ANISOU 3730 CE2 PHE B 128 6452 4590 5220 -167 486 -468 C ATOM 3731 CZ PHE B 128 -18.544 28.286 7.190 1.00 39.62 C ANISOU 3731 CZ PHE B 128 5879 4309 4865 -105 477 -391 C ATOM 3732 N PRO B 129 -21.872 32.551 6.634 1.00 42.85 N ANISOU 3732 N PRO B 129 6785 4243 5253 418 705 -439 N ATOM 3733 CA PRO B 129 -22.429 33.115 7.861 1.00 44.33 C ANISOU 3733 CA PRO B 129 7080 4394 5370 519 773 -518 C ATOM 3734 C PRO B 129 -21.989 32.421 9.147 1.00 44.37 C ANISOU 3734 C PRO B 129 7038 4511 5310 429 767 -575 C ATOM 3735 O PRO B 129 -22.375 32.860 10.235 1.00 47.72 O ANISOU 3735 O PRO B 129 7562 4913 5656 504 825 -648 O ATOM 3736 CB PRO B 129 -23.932 32.921 7.664 1.00 45.76 C ANISOU 3736 CB PRO B 129 7149 4657 5582 739 829 -461 C ATOM 3737 CG PRO B 129 -24.031 31.649 6.877 1.00 44.14 C ANISOU 3737 CG PRO B 129 6713 4610 5449 690 772 -369 C ATOM 3738 CD PRO B 129 -22.777 31.554 6.034 1.00 41.27 C ANISOU 3738 CD PRO B 129 6377 4192 5112 512 696 -351 C ATOM 3739 N TYR B 130 -21.190 31.363 9.040 1.00 39.71 N ANISOU 3739 N TYR B 130 6310 4038 4742 281 699 -544 N ATOM 3740 CA TYR B 130 -20.888 30.534 10.203 1.00 40.07 C ANISOU 3740 CA TYR B 130 6290 4209 4724 220 688 -575 C ATOM 3741 C TYR B 130 -19.542 30.856 10.848 1.00 40.02 C ANISOU 3741 C TYR B 130 6392 4158 4654 48 629 -658 C ATOM 3742 O TYR B 130 -18.600 31.292 10.185 1.00 38.26 O ANISOU 3742 O TYR B 130 6218 3855 4463 -78 577 -666 O ATOM 3743 CB TYR B 130 -20.962 29.047 9.838 1.00 36.79 C ANISOU 3743 CB TYR B 130 5654 3959 4365 190 650 -486 C ATOM 3744 CG TYR B 130 -22.318 28.621 9.322 1.00 34.92 C ANISOU 3744 CG TYR B 130 5291 3790 4187 337 697 -410 C ATOM 3745 CD1 TYR B 130 -23.431 28.614 10.158 1.00 38.95 C ANISOU 3745 CD1 TYR B 130 5779 4361 4660 469 782 -416 C ATOM 3746 CD2 TYR B 130 -22.491 28.211 8.000 1.00 33.69 C ANISOU 3746 CD2 TYR B 130 5030 3651 4121 340 656 -333 C ATOM 3747 CE1 TYR B 130 -24.685 28.214 9.694 1.00 38.87 C ANISOU 3747 CE1 TYR B 130 5626 4434 4710 592 822 -344 C ATOM 3748 CE2 TYR B 130 -23.743 27.814 7.529 1.00 36.26 C ANISOU 3748 CE2 TYR B 130 5228 4051 4499 463 684 -268 C ATOM 3749 CZ TYR B 130 -24.834 27.816 8.384 1.00 36.88 C ANISOU 3749 CZ TYR B 130 5267 4197 4550 584 765 -272 C ATOM 3750 OH TYR B 130 -26.078 27.432 7.926 1.00 40.14 O ANISOU 3750 OH TYR B 130 5529 4702 5020 694 789 -207 O ATOM 3751 N ARG B 131 -19.481 30.609 12.152 1.00 39.53 N ANISOU 3751 N ARG B 131 6358 4165 4498 41 638 -716 N ATOM 3752 CA ARG B 131 -18.309 30.869 12.970 1.00 41.89 C ANISOU 3752 CA ARG B 131 6752 4448 4716 -110 573 -804 C ATOM 3753 C ARG B 131 -17.805 29.559 13.568 1.00 40.03 C ANISOU 3753 C ARG B 131 6369 4392 4449 -177 517 -771 C ATOM 3754 O ARG B 131 -18.412 28.499 13.380 1.00 38.05 O ANISOU 3754 O ARG B 131 5965 4255 4238 -107 538 -683 O ATOM 3755 CB ARG B 131 -18.648 31.876 14.071 1.00 44.08 C ANISOU 3755 CB ARG B 131 7240 4629 4880 -49 625 -917 C ATOM 3756 CG ARG B 131 -18.701 33.323 13.585 1.00 48.69 C ANISOU 3756 CG ARG B 131 8026 4994 5479 -33 653 -974 C ATOM 3757 CD ARG B 131 -18.821 34.281 14.768 0.00 51.46 C ANISOU 3757 CD ARG B 131 8611 5240 5702 4 689 -1107 C ATOM 3758 NE ARG B 131 -18.555 35.665 14.389 0.00 53.14 N ANISOU 3758 NE ARG B 131 9052 5218 5921 -34 692 -1176 N ATOM 3759 CZ ARG B 131 -18.471 36.671 15.253 0.00 55.16 C ANISOU 3759 CZ ARG B 131 9554 5332 6073 -35 708 -1307 C ATOM 3760 NH1 ARG B 131 -18.632 36.448 16.550 0.00 55.89 N ANISOU 3760 NH1 ARG B 131 9691 5508 6037 7 723 -1385 N ATOM 3761 NH2 ARG B 131 -18.225 37.901 14.822 0.00 56.57 N ANISOU 3761 NH2 ARG B 131 9951 5277 6267 -79 710 -1360 N ATOM 3762 N MET B 132 -16.683 29.628 14.270 1.00 40.77 N ANISOU 3762 N MET B 132 6511 4508 4470 -314 438 -839 N ATOM 3763 CA MET B 132 -16.023 28.414 14.743 1.00 41.91 C ANISOU 3763 CA MET B 132 6520 4816 4586 -378 367 -802 C ATOM 3764 C MET B 132 -16.875 27.615 15.736 1.00 41.97 C ANISOU 3764 C MET B 132 6497 4933 4517 -263 422 -772 C ATOM 3765 O MET B 132 -16.833 26.386 15.731 1.00 40.88 O ANISOU 3765 O MET B 132 6217 4916 4399 -259 398 -690 O ATOM 3766 CB MET B 132 -14.653 28.735 15.344 1.00 41.36 C ANISOU 3766 CB MET B 132 6506 4761 4446 -542 262 -886 C ATOM 3767 CG MET B 132 -13.724 27.539 15.384 1.00 42.23 C ANISOU 3767 CG MET B 132 6448 5031 4564 -616 168 -830 C ATOM 3768 SD MET B 132 -13.274 26.910 13.744 1.00 39.27 S ANISOU 3768 SD MET B 132 5893 4680 4347 -655 146 -727 S ATOM 3769 CE MET B 132 -12.574 25.337 14.254 1.00 39.63 C ANISOU 3769 CE MET B 132 5777 4919 4362 -661 62 -666 C ATOM 3770 N ASN B 133 -17.651 28.299 16.574 1.00 43.61 N ANISOU 3770 N ASN B 133 6843 5093 4635 -168 501 -836 N ATOM 3771 CA ASN B 133 -18.560 27.601 17.489 1.00 43.96 C ANISOU 3771 CA ASN B 133 6856 5244 4602 -54 578 -800 C ATOM 3772 C ASN B 133 -19.539 26.688 16.737 1.00 41.17 C ANISOU 3772 C ASN B 133 6327 4957 4358 33 639 -674 C ATOM 3773 O ASN B 133 -19.891 25.611 17.216 1.00 39.88 O ANISOU 3773 O ASN B 133 6069 4913 4169 57 661 -603 O ATOM 3774 CB ASN B 133 -19.304 28.584 18.414 1.00 47.01 C ANISOU 3774 CB ASN B 133 7422 5566 4874 55 674 -893 C ATOM 3775 CG ASN B 133 -20.157 29.601 17.652 1.00 49.73 C ANISOU 3775 CG ASN B 133 7830 5774 5293 166 757 -908 C ATOM 3776 OD1 ASN B 133 -19.764 30.100 16.599 1.00 54.19 O ANISOU 3776 OD1 ASN B 133 8399 6233 5956 110 713 -905 O ATOM 3777 ND2 ASN B 133 -21.320 29.923 18.203 1.00 52.40 N ANISOU 3777 ND2 ASN B 133 8219 6117 5575 333 882 -923 N ATOM 3778 N HIS B 134 -19.946 27.102 15.544 1.00 38.56 N ANISOU 3778 N HIS B 134 5958 4546 4146 68 659 -645 N ATOM 3779 CA HIS B 134 -20.799 26.264 14.704 1.00 37.54 C ANISOU 3779 CA HIS B 134 5659 4479 4126 130 693 -535 C ATOM 3780 C HIS B 134 -20.028 25.074 14.119 1.00 34.49 C ANISOU 3780 C HIS B 134 5137 4164 3804 25 601 -462 C ATOM 3781 O HIS B 134 -20.571 23.977 14.004 1.00 33.56 O ANISOU 3781 O HIS B 134 4893 4135 3726 49 617 -376 O ATOM 3782 CB HIS B 134 -21.442 27.091 13.585 1.00 38.74 C ANISOU 3782 CB HIS B 134 5820 4529 4371 209 728 -527 C ATOM 3783 CG HIS B 134 -22.216 28.274 14.080 1.00 42.17 C ANISOU 3783 CG HIS B 134 6395 4880 4748 339 821 -596 C ATOM 3784 ND1 HIS B 134 -21.977 29.557 13.639 1.00 42.16 N ANISOU 3784 ND1 HIS B 134 6549 4716 4755 351 817 -661 N ATOM 3785 CD2 HIS B 134 -23.223 28.369 14.981 1.00 46.05 C ANISOU 3785 CD2 HIS B 134 6904 5424 5169 470 927 -609 C ATOM 3786 CE1 HIS B 134 -22.801 30.392 14.246 1.00 46.59 C ANISOU 3786 CE1 HIS B 134 7226 5223 5252 494 911 -717 C ATOM 3787 NE2 HIS B 134 -23.569 29.696 15.065 1.00 45.29 N ANISOU 3787 NE2 HIS B 134 6972 5197 5038 573 983 -688 N ATOM 3788 N ILE B 135 -18.764 25.287 13.763 1.00 33.77 N ANISOU 3788 N ILE B 135 5073 4035 3722 -90 508 -497 N ATOM 3789 CA ILE B 135 -17.920 24.205 13.259 1.00 32.35 C ANISOU 3789 CA ILE B 135 4773 3927 3593 -174 423 -438 C ATOM 3790 C ILE B 135 -17.779 23.130 14.335 1.00 33.61 C ANISOU 3790 C ILE B 135 4897 4200 3672 -178 406 -407 C ATOM 3791 O ILE B 135 -17.897 21.931 14.060 1.00 31.24 O ANISOU 3791 O ILE B 135 4488 3966 3417 -174 390 -323 O ATOM 3792 CB ILE B 135 -16.502 24.701 12.860 1.00 31.81 C ANISOU 3792 CB ILE B 135 4734 3820 3533 -299 334 -489 C ATOM 3793 CG1 ILE B 135 -16.558 25.763 11.739 1.00 34.24 C ANISOU 3793 CG1 ILE B 135 5093 4003 3915 -309 354 -507 C ATOM 3794 CG2 ILE B 135 -15.626 23.540 12.440 1.00 26.78 C ANISOU 3794 CG2 ILE B 135 3965 3273 2935 -359 255 -430 C ATOM 3795 CD1 ILE B 135 -17.077 25.279 10.406 1.00 32.70 C ANISOU 3795 CD1 ILE B 135 4792 3804 3828 -261 368 -423 C ATOM 3796 N LEU B 136 -17.543 23.572 15.565 1.00 34.82 N ANISOU 3796 N LEU B 136 5161 4369 3700 -185 408 -475 N ATOM 3797 CA LEU B 136 -17.258 22.660 16.660 1.00 37.45 C ANISOU 3797 CA LEU B 136 5487 4808 3933 -192 381 -449 C ATOM 3798 C LEU B 136 -18.493 21.860 17.043 1.00 37.61 C ANISOU 3798 C LEU B 136 5459 4885 3945 -103 478 -366 C ATOM 3799 O LEU B 136 -18.386 20.678 17.359 1.00 39.85 O ANISOU 3799 O LEU B 136 5683 5246 4213 -112 456 -288 O ATOM 3800 CB LEU B 136 -16.675 23.417 17.866 1.00 38.60 C ANISOU 3800 CB LEU B 136 5777 4958 3930 -226 350 -553 C ATOM 3801 CG LEU B 136 -15.303 24.072 17.622 1.00 40.53 C ANISOU 3801 CG LEU B 136 6052 5171 4176 -350 235 -632 C ATOM 3802 CD1 LEU B 136 -14.777 24.751 18.877 1.00 39.13 C ANISOU 3802 CD1 LEU B 136 6020 5005 3842 -393 192 -740 C ATOM 3803 CD2 LEU B 136 -14.275 23.060 17.106 1.00 40.26 C ANISOU 3803 CD2 LEU B 136 5877 5220 4200 -415 133 -568 C ATOM 3804 N GLU B 137 -19.661 22.494 16.991 1.00 38.44 N ANISOU 3804 N GLU B 137 5587 4953 4065 -16 587 -377 N ATOM 3805 CA GLU B 137 -20.926 21.805 17.261 1.00 39.82 C ANISOU 3805 CA GLU B 137 5689 5193 4247 60 691 -295 C ATOM 3806 C GLU B 137 -21.207 20.780 16.165 1.00 36.66 C ANISOU 3806 C GLU B 137 5135 4809 3985 36 666 -195 C ATOM 3807 O GLU B 137 -21.561 19.638 16.448 1.00 36.14 O ANISOU 3807 O GLU B 137 5002 4811 3920 25 685 -108 O ATOM 3808 CB GLU B 137 -22.082 22.815 17.373 1.00 41.81 C ANISOU 3808 CB GLU B 137 5983 5412 4490 174 812 -335 C ATOM 3809 CG GLU B 137 -23.432 22.237 17.848 1.00 50.74 C ANISOU 3809 CG GLU B 137 7030 6637 5610 255 939 -259 C ATOM 3810 CD GLU B 137 -23.440 21.773 19.313 1.00 59.68 C ANISOU 3810 CD GLU B 137 8231 7858 6586 260 990 -248 C ATOM 3811 OE1 GLU B 137 -22.402 21.887 20.005 1.00 64.28 O ANISOU 3811 OE1 GLU B 137 8929 8433 7060 208 916 -304 O ATOM 3812 OE2 GLU B 137 -24.503 21.291 19.776 1.00 63.20 O ANISOU 3812 OE2 GLU B 137 8610 8390 7013 314 1106 -179 O ATOM 3813 N CYS B 138 -21.020 21.189 14.915 1.00 35.66 N ANISOU 3813 N CYS B 138 4970 4612 3968 21 623 -208 N ATOM 3814 CA CYS B 138 -21.203 20.301 13.769 1.00 33.64 C ANISOU 3814 CA CYS B 138 4587 4361 3835 -4 586 -130 C ATOM 3815 C CYS B 138 -20.250 19.097 13.841 1.00 35.28 C ANISOU 3815 C CYS B 138 4764 4606 4036 -78 500 -84 C ATOM 3816 O CYS B 138 -20.635 17.962 13.527 1.00 35.08 O ANISOU 3816 O CYS B 138 4656 4608 4064 -91 497 -3 O ATOM 3817 CB CYS B 138 -20.989 21.077 12.480 1.00 31.05 C ANISOU 3817 CB CYS B 138 4252 3949 3594 -5 549 -162 C ATOM 3818 SG CYS B 138 -21.450 20.209 10.981 1.00 31.65 S ANISOU 3818 SG CYS B 138 4191 4027 3807 -13 514 -83 S ATOM 3819 N GLU B 139 -19.011 19.347 14.264 1.00 35.01 N ANISOU 3819 N GLU B 139 4796 4571 3934 -126 428 -137 N ATOM 3820 CA GLU B 139 -18.006 18.290 14.377 1.00 33.31 C ANISOU 3820 CA GLU B 139 4552 4400 3705 -173 340 -98 C ATOM 3821 C GLU B 139 -18.511 17.165 15.271 1.00 34.46 C ANISOU 3821 C GLU B 139 4694 4604 3794 -153 375 -18 C ATOM 3822 O GLU B 139 -18.359 15.984 14.944 1.00 34.91 O ANISOU 3822 O GLU B 139 4700 4670 3895 -166 338 56 O ATOM 3823 CB GLU B 139 -16.692 18.853 14.925 1.00 32.70 C ANISOU 3823 CB GLU B 139 4539 4340 3546 -221 261 -173 C ATOM 3824 CG GLU B 139 -15.540 17.854 14.974 1.00 32.68 C ANISOU 3824 CG GLU B 139 4491 4396 3531 -252 161 -137 C ATOM 3825 CD GLU B 139 -14.252 18.494 15.468 1.00 40.98 C ANISOU 3825 CD GLU B 139 5579 5485 4508 -308 74 -215 C ATOM 3826 OE1 GLU B 139 -14.317 19.310 16.408 1.00 40.25 O ANISOU 3826 OE1 GLU B 139 5582 5397 4315 -318 88 -282 O ATOM 3827 OE2 GLU B 139 -13.176 18.188 14.919 1.00 41.55 O ANISOU 3827 OE2 GLU B 139 5581 5588 4619 -344 -9 -213 O ATOM 3828 N PHE B 140 -19.117 17.532 16.398 1.00 36.89 N ANISOU 3828 N PHE B 140 5069 4946 4000 -118 451 -31 N ATOM 3829 CA PHE B 140 -19.665 16.534 17.322 1.00 36.04 C ANISOU 3829 CA PHE B 140 4970 4897 3825 -104 504 54 C ATOM 3830 C PHE B 140 -20.781 15.695 16.702 1.00 34.28 C ANISOU 3830 C PHE B 140 4648 4668 3708 -106 566 147 C ATOM 3831 O PHE B 140 -20.832 14.483 16.912 1.00 33.07 O ANISOU 3831 O PHE B 140 4481 4530 3554 -132 558 236 O ATOM 3832 CB PHE B 140 -20.141 17.187 18.626 1.00 38.63 C ANISOU 3832 CB PHE B 140 5395 5271 4011 -59 590 17 C ATOM 3833 CG PHE B 140 -19.192 16.996 19.780 1.00 40.73 C ANISOU 3833 CG PHE B 140 5762 5589 4124 -70 527 1 C ATOM 3834 CD1 PHE B 140 -19.659 16.577 21.016 1.00 45.24 C ANISOU 3834 CD1 PHE B 140 6402 6227 4560 -39 598 49 C ATOM 3835 CD2 PHE B 140 -17.825 17.224 19.623 1.00 40.86 C ANISOU 3835 CD2 PHE B 140 5800 5601 4126 -112 394 -59 C ATOM 3836 CE1 PHE B 140 -18.778 16.396 22.080 1.00 48.83 C ANISOU 3836 CE1 PHE B 140 6958 6737 4859 -41 528 36 C ATOM 3837 CE2 PHE B 140 -16.947 17.043 20.672 1.00 40.06 C ANISOU 3837 CE2 PHE B 140 5777 5563 3881 -119 320 -75 C ATOM 3838 CZ PHE B 140 -17.420 16.627 21.903 1.00 47.81 C ANISOU 3838 CZ PHE B 140 6840 6606 4720 -80 381 -28 C ATOM 3839 N TYR B 141 -21.667 16.331 15.946 1.00 32.99 N ANISOU 3839 N TYR B 141 4421 4480 3632 -81 621 127 N ATOM 3840 CA TYR B 141 -22.717 15.603 15.225 1.00 32.04 C ANISOU 3840 CA TYR B 141 4189 4364 3623 -96 661 204 C ATOM 3841 C TYR B 141 -22.149 14.682 14.155 1.00 31.52 C ANISOU 3841 C TYR B 141 4077 4248 3654 -149 561 239 C ATOM 3842 O TYR B 141 -22.692 13.599 13.916 1.00 31.35 O ANISOU 3842 O TYR B 141 4000 4224 3686 -190 568 318 O ATOM 3843 CB TYR B 141 -23.718 16.562 14.583 1.00 30.83 C ANISOU 3843 CB TYR B 141 3969 4205 3539 -42 724 169 C ATOM 3844 CG TYR B 141 -24.743 17.096 15.558 1.00 30.57 C ANISOU 3844 CG TYR B 141 3941 4238 3434 25 856 168 C ATOM 3845 CD1 TYR B 141 -25.866 16.349 15.892 1.00 29.70 C ANISOU 3845 CD1 TYR B 141 3740 4204 3343 12 946 256 C ATOM 3846 CD2 TYR B 141 -24.586 18.349 16.144 1.00 30.79 C ANISOU 3846 CD2 TYR B 141 4070 4255 3375 97 895 78 C ATOM 3847 CE1 TYR B 141 -26.819 16.838 16.792 1.00 38.49 C ANISOU 3847 CE1 TYR B 141 4843 5396 4386 83 1084 258 C ATOM 3848 CE2 TYR B 141 -25.523 18.851 17.047 1.00 37.99 C ANISOU 3848 CE2 TYR B 141 4996 5229 4211 177 1026 70 C ATOM 3849 CZ TYR B 141 -26.639 18.096 17.362 1.00 38.64 C ANISOU 3849 CZ TYR B 141 4969 5403 4310 177 1125 162 C ATOM 3850 OH TYR B 141 -27.555 18.597 18.246 1.00 42.74 O ANISOU 3850 OH TYR B 141 5490 5998 4749 265 1268 156 O ATOM 3851 N LEU B 142 -21.068 15.126 13.514 1.00 31.88 N ANISOU 3851 N LEU B 142 4146 4250 3715 -152 473 177 N ATOM 3852 CA LEU B 142 -20.393 14.342 12.485 1.00 32.40 C ANISOU 3852 CA LEU B 142 4178 4273 3858 -185 383 197 C ATOM 3853 C LEU B 142 -19.755 13.084 13.075 1.00 33.16 C ANISOU 3853 C LEU B 142 4313 4378 3908 -205 338 258 C ATOM 3854 O LEU B 142 -19.942 11.990 12.556 1.00 32.08 O ANISOU 3854 O LEU B 142 4151 4206 3831 -229 315 318 O ATOM 3855 CB LEU B 142 -19.325 15.188 11.780 1.00 31.20 C ANISOU 3855 CB LEU B 142 4042 4092 3720 -184 316 120 C ATOM 3856 CG LEU B 142 -18.551 14.495 10.658 1.00 32.84 C ANISOU 3856 CG LEU B 142 4214 4267 3996 -202 235 131 C ATOM 3857 CD1 LEU B 142 -19.519 13.906 9.642 1.00 28.73 C ANISOU 3857 CD1 LEU B 142 3631 3712 3573 -209 246 173 C ATOM 3858 CD2 LEU B 142 -17.566 15.472 9.988 1.00 29.98 C ANISOU 3858 CD2 LEU B 142 3857 3889 3643 -210 192 60 C ATOM 3859 N LEU B 143 -18.993 13.260 14.150 1.00 35.27 N ANISOU 3859 N LEU B 143 4652 4687 4063 -190 321 241 N ATOM 3860 CA LEU B 143 -18.358 12.137 14.852 1.00 37.28 C ANISOU 3860 CA LEU B 143 4957 4956 4251 -187 275 305 C ATOM 3861 C LEU B 143 -19.366 11.119 15.339 1.00 37.48 C ANISOU 3861 C LEU B 143 4994 4973 4273 -207 344 406 C ATOM 3862 O LEU B 143 -19.133 9.915 15.233 1.00 36.10 O ANISOU 3862 O LEU B 143 4842 4759 4116 -218 305 477 O ATOM 3863 CB LEU B 143 -17.575 12.634 16.061 1.00 37.32 C ANISOU 3863 CB LEU B 143 5038 5025 4117 -166 249 267 C ATOM 3864 CG LEU B 143 -16.195 13.178 15.738 1.00 43.03 C ANISOU 3864 CG LEU B 143 5750 5767 4832 -166 147 191 C ATOM 3865 CD1 LEU B 143 -15.694 14.014 16.919 1.00 49.28 C ANISOU 3865 CD1 LEU B 143 6615 6624 5487 -164 130 129 C ATOM 3866 CD2 LEU B 143 -15.243 12.023 15.421 1.00 41.19 C ANISOU 3866 CD2 LEU B 143 5499 5532 4617 -143 56 242 C ATOM 3867 N GLU B 144 -20.472 11.620 15.886 1.00 37.46 N ANISOU 3867 N GLU B 144 4981 5009 4245 -211 451 413 N ATOM 3868 CA GLU B 144 -21.536 10.776 16.418 1.00 38.92 C ANISOU 3868 CA GLU B 144 5160 5204 4423 -246 539 513 C ATOM 3869 C GLU B 144 -22.125 9.930 15.302 1.00 37.71 C ANISOU 3869 C GLU B 144 4931 4987 4408 -304 524 561 C ATOM 3870 O GLU B 144 -22.213 8.712 15.428 1.00 36.98 O ANISOU 3870 O GLU B 144 4874 4851 4326 -348 516 648 O ATOM 3871 CB GLU B 144 -22.626 11.631 17.083 1.00 38.10 C ANISOU 3871 CB GLU B 144 5031 5170 4274 -227 668 499 C ATOM 3872 CG GLU B 144 -23.805 10.831 17.637 1.00 43.62 C ANISOU 3872 CG GLU B 144 5700 5903 4969 -274 779 608 C ATOM 3873 CD GLU B 144 -24.843 11.694 18.345 1.00 43.13 C ANISOU 3873 CD GLU B 144 5605 5932 4851 -234 919 592 C ATOM 3874 OE1 GLU B 144 -25.116 12.830 17.898 1.00 45.17 O ANISOU 3874 OE1 GLU B 144 5813 6203 5145 -180 936 506 O ATOM 3875 OE2 GLU B 144 -25.402 11.226 19.353 1.00 50.33 O ANISOU 3875 OE2 GLU B 144 6545 6900 5679 -251 1020 671 O ATOM 3876 N LEU B 145 -22.497 10.577 14.200 1.00 36.92 N ANISOU 3876 N LEU B 145 4744 4874 4410 -303 513 503 N ATOM 3877 CA LEU B 145 -23.059 9.869 13.048 1.00 37.43 C ANISOU 3877 CA LEU B 145 4737 4885 4600 -358 484 532 C ATOM 3878 C LEU B 145 -22.114 8.795 12.523 1.00 35.92 C ANISOU 3878 C LEU B 145 4607 4610 4433 -372 383 552 C ATOM 3879 O LEU B 145 -22.543 7.701 12.185 1.00 38.50 O ANISOU 3879 O LEU B 145 4936 4876 4815 -434 372 613 O ATOM 3880 CB LEU B 145 -23.411 10.846 11.918 1.00 36.69 C ANISOU 3880 CB LEU B 145 4557 4795 4590 -334 469 459 C ATOM 3881 CG LEU B 145 -23.919 10.242 10.595 1.00 38.36 C ANISOU 3881 CG LEU B 145 4698 4958 4920 -385 417 471 C ATOM 3882 CD1 LEU B 145 -22.779 9.624 9.774 1.00 34.31 C ANISOU 3882 CD1 LEU B 145 4244 4364 4427 -381 310 448 C ATOM 3883 CD2 LEU B 145 -25.036 9.208 10.831 1.00 36.01 C ANISOU 3883 CD2 LEU B 145 4351 4665 4664 -475 464 558 C ATOM 3884 N MET B 146 -20.824 9.098 12.460 1.00 35.37 N ANISOU 3884 N MET B 146 4586 4534 4320 -314 311 500 N ATOM 3885 CA MET B 146 -19.879 8.141 11.900 1.00 34.19 C ANISOU 3885 CA MET B 146 4483 4316 4193 -300 220 512 C ATOM 3886 C MET B 146 -19.447 7.090 12.909 1.00 35.85 C ANISOU 3886 C MET B 146 4793 4505 4324 -288 210 592 C ATOM 3887 O MET B 146 -18.688 6.183 12.570 1.00 35.30 O ANISOU 3887 O MET B 146 4776 4372 4263 -258 140 613 O ATOM 3888 CB MET B 146 -18.676 8.865 11.319 1.00 34.11 C ANISOU 3888 CB MET B 146 4459 4323 4177 -244 151 428 C ATOM 3889 CG MET B 146 -19.032 9.689 10.099 1.00 32.55 C ANISOU 3889 CG MET B 146 4187 4118 4063 -253 151 365 C ATOM 3890 SD MET B 146 -17.576 10.235 9.207 1.00 36.86 S ANISOU 3890 SD MET B 146 4721 4670 4615 -207 75 288 S ATOM 3891 CE MET B 146 -16.641 11.005 10.533 1.00 26.62 C ANISOU 3891 CE MET B 146 3456 3453 3204 -184 70 259 C ATOM 3892 N ASP B 147 -19.928 7.214 14.144 1.00 37.12 N ANISOU 3892 N ASP B 147 4986 4720 4399 -300 283 639 N ATOM 3893 CA ASP B 147 -19.653 6.241 15.191 1.00 39.25 C ANISOU 3893 CA ASP B 147 5364 4972 4578 -290 285 732 C ATOM 3894 C ASP B 147 -18.144 6.182 15.396 1.00 38.67 C ANISOU 3894 C ASP B 147 5343 4914 4435 -200 183 704 C ATOM 3895 O ASP B 147 -17.566 5.114 15.616 1.00 37.23 O ANISOU 3895 O ASP B 147 5245 4678 4224 -162 132 769 O ATOM 3896 CB ASP B 147 -20.234 4.867 14.819 1.00 39.43 C ANISOU 3896 CB ASP B 147 5427 4884 4670 -356 291 822 C ATOM 3897 CG ASP B 147 -20.254 3.893 15.986 1.00 43.97 C ANISOU 3897 CG ASP B 147 6126 5431 5150 -363 322 939 C ATOM 3898 OD1 ASP B 147 -20.442 4.325 17.143 1.00 42.00 O ANISOU 3898 OD1 ASP B 147 5902 5267 4789 -352 387 967 O ATOM 3899 OD2 ASP B 147 -20.077 2.683 15.732 1.00 48.49 O ANISOU 3899 OD2 ASP B 147 6784 5887 5752 -376 281 1005 O ATOM 3900 N CYS B 148 -17.526 7.356 15.296 1.00 37.04 N ANISOU 3900 N CYS B 148 5085 4783 4208 -166 153 606 N ATOM 3901 CA CYS B 148 -16.085 7.530 15.462 1.00 37.12 C ANISOU 3901 CA CYS B 148 5107 4840 4158 -96 55 564 C ATOM 3902 C CYS B 148 -15.235 6.690 14.495 1.00 35.08 C ANISOU 3902 C CYS B 148 4839 4523 3968 -47 -29 569 C ATOM 3903 O CYS B 148 -14.090 6.383 14.797 1.00 36.99 O ANISOU 3903 O CYS B 148 5100 4802 4152 27 -108 572 O ATOM 3904 CB CYS B 148 -15.689 7.266 16.920 1.00 38.81 C ANISOU 3904 CB CYS B 148 5412 5113 4221 -55 43 617 C ATOM 3905 SG CYS B 148 -16.442 8.428 18.089 1.00 43.26 S ANISOU 3905 SG CYS B 148 5998 5765 4674 -88 137 583 S ATOM 3906 N CYS B 149 -15.805 6.332 13.344 1.00 33.48 N ANISOU 3906 N CYS B 149 4605 4235 3880 -83 -13 565 N ATOM 3907 CA CYS B 149 -15.092 5.609 12.297 1.00 33.33 C ANISOU 3907 CA CYS B 149 4585 4155 3926 -33 -80 554 C ATOM 3908 C CYS B 149 -14.376 6.645 11.438 1.00 31.53 C ANISOU 3908 C CYS B 149 4259 3988 3734 -17 -111 455 C ATOM 3909 O CYS B 149 -14.980 7.238 10.550 1.00 31.82 O ANISOU 3909 O CYS B 149 4240 4005 3843 -67 -78 409 O ATOM 3910 CB CYS B 149 -16.059 4.792 11.431 1.00 32.59 C ANISOU 3910 CB CYS B 149 4514 3941 3928 -89 -54 585 C ATOM 3911 SG CYS B 149 -16.881 3.422 12.267 1.00 37.25 S ANISOU 3911 SG CYS B 149 5229 4430 4494 -134 -16 712 S ATOM 3912 N LEU B 150 -13.091 6.857 11.709 1.00 31.95 N ANISOU 3912 N LEU B 150 4286 4120 3732 49 -174 427 N ATOM 3913 CA LEU B 150 -12.347 8.004 11.158 1.00 31.50 C ANISOU 3913 CA LEU B 150 4134 4143 3692 40 -194 338 C ATOM 3914 C LEU B 150 -11.325 7.656 10.077 1.00 30.28 C ANISOU 3914 C LEU B 150 3925 3994 3585 103 -244 310 C ATOM 3915 O LEU B 150 -11.092 8.454 9.165 1.00 29.07 O ANISOU 3915 O LEU B 150 3701 3863 3480 73 -232 248 O ATOM 3916 CB LEU B 150 -11.643 8.743 12.283 1.00 29.59 C ANISOU 3916 CB LEU B 150 3879 4012 3351 40 -227 312 C ATOM 3917 CG LEU B 150 -12.560 9.371 13.327 1.00 36.39 C ANISOU 3917 CG LEU B 150 4793 4885 4149 -17 -169 316 C ATOM 3918 CD1 LEU B 150 -11.762 9.801 14.555 1.00 26.85 C ANISOU 3918 CD1 LEU B 150 3602 3783 2818 -2 -222 297 C ATOM 3919 CD2 LEU B 150 -13.326 10.543 12.709 1.00 33.23 C ANISOU 3919 CD2 LEU B 150 4355 4463 3810 -87 -103 252 C ATOM 3920 N ILE B 151 -10.712 6.481 10.171 1.00 32.05 N ANISOU 3920 N ILE B 151 4190 4197 3790 198 -292 359 N ATOM 3921 CA ILE B 151 -9.763 6.042 9.140 1.00 30.26 C ANISOU 3921 CA ILE B 151 3916 3977 3603 282 -327 333 C ATOM 3922 C ILE B 151 -10.526 5.592 7.896 1.00 31.01 C ANISOU 3922 C ILE B 151 4050 3952 3782 263 -291 324 C ATOM 3923 O ILE B 151 -11.379 4.702 7.953 1.00 31.23 O ANISOU 3923 O ILE B 151 4176 3863 3828 251 -277 373 O ATOM 3924 CB ILE B 151 -8.804 4.956 9.671 1.00 33.55 C ANISOU 3924 CB ILE B 151 4367 4415 3966 417 -393 386 C ATOM 3925 CG1 ILE B 151 -7.907 5.566 10.756 1.00 35.42 C ANISOU 3925 CG1 ILE B 151 4537 4805 4117 433 -448 379 C ATOM 3926 CG2 ILE B 151 -7.940 4.377 8.544 1.00 30.28 C ANISOU 3926 CG2 ILE B 151 3915 3996 3593 526 -414 361 C ATOM 3927 CD1 ILE B 151 -6.852 4.635 11.293 1.00 44.92 C ANISOU 3927 CD1 ILE B 151 5747 6061 5259 582 -527 429 C ATOM 3928 N VAL B 152 -10.221 6.242 6.777 1.00 30.20 N ANISOU 3928 N VAL B 152 3871 3880 3724 250 -276 260 N ATOM 3929 CA VAL B 152 -10.821 5.943 5.500 1.00 28.78 C ANISOU 3929 CA VAL B 152 3721 3606 3608 237 -252 239 C ATOM 3930 C VAL B 152 -9.755 5.536 4.480 1.00 31.57 C ANISOU 3930 C VAL B 152 4044 3982 3969 340 -270 205 C ATOM 3931 O VAL B 152 -8.717 6.191 4.344 1.00 31.45 O ANISOU 3931 O VAL B 152 3926 4087 3937 366 -273 173 O ATOM 3932 CB VAL B 152 -11.584 7.168 4.955 1.00 30.41 C ANISOU 3932 CB VAL B 152 3879 3824 3851 134 -207 196 C ATOM 3933 CG1 VAL B 152 -12.334 6.796 3.692 1.00 27.21 C ANISOU 3933 CG1 VAL B 152 3512 3326 3501 119 -196 178 C ATOM 3934 CG2 VAL B 152 -12.554 7.721 6.026 1.00 27.48 C ANISOU 3934 CG2 VAL B 152 3523 3455 3465 51 -177 221 C ATOM 3935 N TYR B 153 -10.041 4.460 3.751 1.00 30.47 N ANISOU 3935 N TYR B 153 3995 3729 3854 393 -278 211 N ATOM 3936 CA TYR B 153 -9.194 3.977 2.668 1.00 30.97 C ANISOU 3936 CA TYR B 153 4054 3795 3920 503 -282 173 C ATOM 3937 C TYR B 153 -9.662 4.552 1.339 1.00 30.97 C ANISOU 3937 C TYR B 153 4038 3776 3952 446 -248 118 C ATOM 3938 O TYR B 153 -10.852 4.777 1.147 1.00 29.97 O ANISOU 3938 O TYR B 153 3951 3579 3858 345 -239 118 O ATOM 3939 CB TYR B 153 -9.236 2.451 2.614 1.00 31.47 C ANISOU 3939 CB TYR B 153 4256 3724 3978 601 -313 202 C ATOM 3940 CG TYR B 153 -8.690 1.799 3.862 1.00 29.14 C ANISOU 3940 CG TYR B 153 3993 3440 3638 684 -351 267 C ATOM 3941 CD1 TYR B 153 -7.438 1.190 3.869 1.00 35.48 C ANISOU 3941 CD1 TYR B 153 4779 4295 4406 856 -379 272 C ATOM 3942 CD2 TYR B 153 -9.428 1.791 5.037 1.00 27.12 C ANISOU 3942 CD2 TYR B 153 3783 3153 3368 602 -356 328 C ATOM 3943 CE1 TYR B 153 -6.948 0.587 5.014 1.00 33.34 C ANISOU 3943 CE1 TYR B 153 4543 4038 4086 946 -425 338 C ATOM 3944 CE2 TYR B 153 -8.953 1.203 6.175 1.00 26.80 C ANISOU 3944 CE2 TYR B 153 3787 3124 3273 680 -393 394 C ATOM 3945 CZ TYR B 153 -7.719 0.606 6.166 1.00 31.26 C ANISOU 3945 CZ TYR B 153 4340 3735 3802 853 -433 400 C ATOM 3946 OH TYR B 153 -7.278 0.030 7.318 1.00 32.75 O ANISOU 3946 OH TYR B 153 4578 3938 3929 940 -479 473 O ATOM 3947 N HIS B 154 -8.722 4.792 0.428 1.00 31.21 N ANISOU 3947 N HIS B 154 4007 3882 3971 516 -228 76 N ATOM 3948 CA HIS B 154 -9.024 5.411 -0.865 1.00 29.47 C ANISOU 3948 CA HIS B 154 3774 3659 3763 473 -192 30 C ATOM 3949 C HIS B 154 -8.317 4.649 -2.003 1.00 31.06 C ANISOU 3949 C HIS B 154 4013 3848 3941 601 -180 -8 C ATOM 3950 O HIS B 154 -7.397 3.864 -1.749 1.00 32.59 O ANISOU 3950 O HIS B 154 4206 4065 4111 731 -192 0 O ATOM 3951 CB HIS B 154 -8.573 6.882 -0.870 1.00 29.29 C ANISOU 3951 CB HIS B 154 3625 3765 3738 400 -153 16 C ATOM 3952 CG HIS B 154 -9.202 7.726 0.199 1.00 31.76 C ANISOU 3952 CG HIS B 154 3912 4090 4063 287 -157 39 C ATOM 3953 ND1 HIS B 154 -10.522 8.132 0.152 1.00 33.25 N ANISOU 3953 ND1 HIS B 154 4149 4205 4281 196 -150 44 N ATOM 3954 CD2 HIS B 154 -8.682 8.274 1.323 1.00 26.10 C ANISOU 3954 CD2 HIS B 154 3128 3461 3329 258 -167 54 C ATOM 3955 CE1 HIS B 154 -10.791 8.866 1.217 1.00 30.26 C ANISOU 3955 CE1 HIS B 154 3739 3859 3899 127 -145 60 C ATOM 3956 NE2 HIS B 154 -9.692 8.969 1.943 1.00 25.73 N ANISOU 3956 NE2 HIS B 154 3104 3378 3293 158 -159 63 N ATOM 3957 N PRO B 155 -8.722 4.894 -3.266 1.00 29.98 N ANISOU 3957 N PRO B 155 3912 3680 3801 579 -156 -50 N ATOM 3958 CA PRO B 155 -8.153 4.141 -4.379 1.00 30.84 C ANISOU 3958 CA PRO B 155 4079 3767 3872 704 -141 -93 C ATOM 3959 C PRO B 155 -6.773 4.590 -4.853 1.00 31.08 C ANISOU 3959 C PRO B 155 3990 3953 3866 791 -80 -109 C ATOM 3960 O PRO B 155 -6.209 3.959 -5.746 1.00 31.71 O ANISOU 3960 O PRO B 155 4111 4032 3906 916 -53 -145 O ATOM 3961 CB PRO B 155 -9.184 4.349 -5.509 1.00 29.43 C ANISOU 3961 CB PRO B 155 3981 3511 3690 633 -144 -130 C ATOM 3962 CG PRO B 155 -10.417 4.847 -4.823 1.00 29.04 C ANISOU 3962 CG PRO B 155 3929 3415 3690 487 -176 -97 C ATOM 3963 CD PRO B 155 -9.883 5.679 -3.713 1.00 29.82 C ANISOU 3963 CD PRO B 155 3907 3622 3803 452 -154 -58 C ATOM 3964 N TYR B 156 -6.236 5.659 -4.277 1.00 31.23 N ANISOU 3964 N TYR B 156 3864 4105 3896 723 -55 -84 N ATOM 3965 CA TYR B 156 -4.973 6.212 -4.745 1.00 32.44 C ANISOU 3965 CA TYR B 156 3883 4420 4023 769 8 -94 C ATOM 3966 C TYR B 156 -3.816 5.252 -4.499 1.00 35.32 C ANISOU 3966 C TYR B 156 4200 4855 4366 944 5 -93 C ATOM 3967 O TYR B 156 -3.004 5.025 -5.388 1.00 35.49 O ANISOU 3967 O TYR B 156 4184 4950 4350 1054 62 -118 O ATOM 3968 CB TYR B 156 -4.692 7.565 -4.085 1.00 32.46 C ANISOU 3968 CB TYR B 156 3751 4535 4048 633 23 -71 C ATOM 3969 CG TYR B 156 -5.772 8.581 -4.363 1.00 32.38 C ANISOU 3969 CG TYR B 156 3790 4457 4057 485 34 -71 C ATOM 3970 CD1 TYR B 156 -5.849 9.230 -5.594 1.00 30.83 C ANISOU 3970 CD1 TYR B 156 3606 4269 3837 453 94 -86 C ATOM 3971 CD2 TYR B 156 -6.738 8.873 -3.404 1.00 31.75 C ANISOU 3971 CD2 TYR B 156 3749 4304 4009 391 -12 -51 C ATOM 3972 CE1 TYR B 156 -6.846 10.159 -5.847 1.00 31.49 C ANISOU 3972 CE1 TYR B 156 3740 4288 3934 338 97 -80 C ATOM 3973 CE2 TYR B 156 -7.737 9.787 -3.651 1.00 24.88 C ANISOU 3973 CE2 TYR B 156 2920 3377 3157 281 -1 -50 C ATOM 3974 CZ TYR B 156 -7.791 10.425 -4.868 1.00 26.06 C ANISOU 3974 CZ TYR B 156 3083 3533 3287 259 48 -64 C ATOM 3975 OH TYR B 156 -8.796 11.325 -5.095 1.00 27.76 O ANISOU 3975 OH TYR B 156 3342 3689 3516 169 52 -57 O ATOM 3976 N ARG B 157 -3.750 4.692 -3.295 1.00 37.42 N ANISOU 3976 N ARG B 157 4471 5102 4646 980 -59 -59 N ATOM 3977 CA ARG B 157 -2.659 3.791 -2.922 1.00 40.03 C ANISOU 3977 CA ARG B 157 4754 5503 4954 1163 -75 -48 C ATOM 3978 C ARG B 157 -2.651 2.525 -3.802 1.00 39.59 C ANISOU 3978 C ARG B 157 4844 5332 4868 1335 -63 -81 C ATOM 3979 O ARG B 157 -1.640 2.242 -4.435 1.00 41.91 O ANISOU 3979 O ARG B 157 5072 5725 5129 1484 -13 -104 O ATOM 3980 CB ARG B 157 -2.724 3.470 -1.419 1.00 41.35 C ANISOU 3980 CB ARG B 157 4924 5656 5130 1162 -154 4 C ATOM 3981 CG ARG B 157 -1.797 2.373 -0.930 1.00 49.28 C ANISOU 3981 CG ARG B 157 5921 6696 6107 1369 -191 28 C ATOM 3982 CD ARG B 157 -2.231 1.832 0.433 1.00 58.74 C ANISOU 3982 CD ARG B 157 7204 7811 7302 1367 -272 87 C ATOM 3983 NE ARG B 157 -2.664 2.890 1.347 1.00 65.37 N ANISOU 3983 NE ARG B 157 7975 8707 8154 1183 -295 108 N ATOM 3984 CZ ARG B 157 -1.851 3.723 1.998 1.00 70.59 C ANISOU 3984 CZ ARG B 157 8462 9554 8804 1141 -314 114 C ATOM 3985 NH1 ARG B 157 -0.528 3.645 1.856 1.00 71.98 N ANISOU 3985 NH1 ARG B 157 8484 9904 8963 1265 -314 108 N ATOM 3986 NH2 ARG B 157 -2.371 4.648 2.801 1.00 73.50 N ANISOU 3986 NH2 ARG B 157 8810 9941 9177 973 -333 122 N ATOM 3987 N PRO B 158 -3.775 1.781 -3.868 1.00 37.15 N ANISOU 3987 N PRO B 158 4732 4815 4568 1311 -105 -87 N ATOM 3988 CA PRO B 158 -3.814 0.625 -4.777 1.00 38.22 C ANISOU 3988 CA PRO B 158 5031 4821 4671 1457 -98 -133 C ATOM 3989 C PRO B 158 -3.536 0.981 -6.242 1.00 38.24 C ANISOU 3989 C PRO B 158 5019 4880 4631 1488 -21 -195 C ATOM 3990 O PRO B 158 -2.817 0.249 -6.929 1.00 39.56 O ANISOU 3990 O PRO B 158 5226 5054 4749 1672 17 -233 O ATOM 3991 CB PRO B 158 -5.240 0.093 -4.624 1.00 36.63 C ANISOU 3991 CB PRO B 158 5020 4401 4497 1347 -158 -131 C ATOM 3992 CG PRO B 158 -5.696 0.581 -3.313 1.00 37.97 C ANISOU 3992 CG PRO B 158 5129 4589 4708 1217 -198 -66 C ATOM 3993 CD PRO B 158 -5.009 1.888 -3.069 1.00 36.48 C ANISOU 3993 CD PRO B 158 4731 4609 4523 1157 -160 -54 C ATOM 3994 N LEU B 159 -4.087 2.098 -6.715 1.00 36.44 N ANISOU 3994 N LEU B 159 4741 4692 4411 1322 6 -201 N ATOM 3995 CA LEU B 159 -3.788 2.567 -8.070 1.00 35.93 C ANISOU 3995 CA LEU B 159 4659 4699 4296 1342 86 -246 C ATOM 3996 C LEU B 159 -2.276 2.713 -8.258 1.00 37.04 C ANISOU 3996 C LEU B 159 4632 5038 4403 1476 166 -243 C ATOM 3997 O LEU B 159 -1.722 2.238 -9.240 1.00 37.92 O ANISOU 3997 O LEU B 159 4778 5176 4453 1621 229 -286 O ATOM 3998 CB LEU B 159 -4.489 3.898 -8.358 1.00 32.95 C ANISOU 3998 CB LEU B 159 4233 4352 3935 1145 102 -233 C ATOM 3999 CG LEU B 159 -4.158 4.568 -9.695 1.00 33.13 C ANISOU 3999 CG LEU B 159 4231 4462 3897 1147 190 -260 C ATOM 4000 CD1 LEU B 159 -4.555 3.670 -10.874 1.00 30.82 C ANISOU 4000 CD1 LEU B 159 4124 4053 3535 1248 189 -326 C ATOM 4001 CD2 LEU B 159 -4.836 5.929 -9.789 1.00 30.35 C ANISOU 4001 CD2 LEU B 159 3837 4129 3566 958 199 -231 C ATOM 4002 N LEU B 160 -1.620 3.370 -7.308 1.00 38.29 N ANISOU 4002 N LEU B 160 4605 5343 4600 1426 164 -194 N ATOM 4003 CA LEU B 160 -0.174 3.544 -7.352 1.00 42.75 C ANISOU 4003 CA LEU B 160 4974 6123 5147 1533 230 -185 C ATOM 4004 C LEU B 160 0.530 2.189 -7.523 1.00 44.94 C ANISOU 4004 C LEU B 160 5302 6387 5384 1795 235 -208 C ATOM 4005 O LEU B 160 1.424 2.046 -8.366 1.00 46.83 O ANISOU 4005 O LEU B 160 5472 6746 5575 1933 325 -234 O ATOM 4006 CB LEU B 160 0.323 4.241 -6.078 1.00 44.87 C ANISOU 4006 CB LEU B 160 5058 6526 5464 1439 189 -133 C ATOM 4007 CG LEU B 160 1.450 5.254 -6.267 1.00 51.39 C ANISOU 4007 CG LEU B 160 5644 7593 6290 1384 265 -119 C ATOM 4008 CD1 LEU B 160 2.646 4.632 -6.965 1.00 60.74 C ANISOU 4008 CD1 LEU B 160 6729 8921 7429 1595 343 -136 C ATOM 4009 CD2 LEU B 160 0.940 6.466 -7.046 1.00 55.65 C ANISOU 4009 CD2 LEU B 160 6193 8123 6827 1193 329 -124 C ATOM 4010 N GLN B 161 0.107 1.200 -6.736 1.00 43.45 N ANISOU 4010 N GLN B 161 5247 6047 5214 1867 146 -196 N ATOM 4011 CA GLN B 161 0.669 -0.151 -6.821 1.00 46.38 C ANISOU 4011 CA GLN B 161 5711 6363 5550 2125 140 -215 C ATOM 4012 C GLN B 161 0.363 -0.806 -8.167 1.00 44.78 C ANISOU 4012 C GLN B 161 5696 6032 5285 2225 191 -290 C ATOM 4013 O GLN B 161 1.227 -1.452 -8.741 1.00 46.00 O ANISOU 4013 O GLN B 161 5849 6242 5387 2447 251 -324 O ATOM 4014 CB GLN B 161 0.152 -1.037 -5.681 1.00 47.60 C ANISOU 4014 CB GLN B 161 6003 6350 5734 2155 33 -176 C ATOM 4015 CG GLN B 161 0.635 -0.616 -4.288 1.00 51.85 C ANISOU 4015 CG GLN B 161 6371 7024 6307 2115 -24 -104 C ATOM 4016 CD GLN B 161 -0.204 -1.198 -3.146 1.00 58.46 C ANISOU 4016 CD GLN B 161 7360 7684 7169 2065 -124 -54 C ATOM 4017 OE1 GLN B 161 -1.287 -1.751 -3.364 1.00 59.50 O ANISOU 4017 OE1 GLN B 161 7706 7591 7308 2007 -149 -69 O ATOM 4018 NE2 GLN B 161 0.293 -1.056 -1.918 1.00 59.25 N ANISOU 4018 NE2 GLN B 161 7344 7893 7278 2077 -181 8 N ATOM 4019 N TYR B 162 -0.854 -0.630 -8.681 1.00 42.18 N ANISOU 4019 N TYR B 162 5527 5544 4958 2069 166 -320 N ATOM 4020 CA TYR B 162 -1.221 -1.252 -9.959 1.00 42.17 C ANISOU 4020 CA TYR B 162 5722 5414 4887 2148 196 -401 C ATOM 4021 C TYR B 162 -0.384 -0.727 -11.131 1.00 44.48 C ANISOU 4021 C TYR B 162 5909 5884 5106 2226 321 -436 C ATOM 4022 O TYR B 162 0.178 -1.518 -11.892 1.00 46.63 O ANISOU 4022 O TYR B 162 6264 6146 5305 2436 377 -493 O ATOM 4023 CB TYR B 162 -2.719 -1.108 -10.261 1.00 38.56 C ANISOU 4023 CB TYR B 162 5432 4773 4445 1951 130 -423 C ATOM 4024 CG TYR B 162 -3.644 -1.894 -9.342 1.00 38.68 C ANISOU 4024 CG TYR B 162 5599 4580 4518 1889 20 -400 C ATOM 4025 CD1 TYR B 162 -3.406 -3.232 -9.046 1.00 41.47 C ANISOU 4025 CD1 TYR B 162 6108 4790 4860 2061 -15 -413 C ATOM 4026 CD2 TYR B 162 -4.780 -1.298 -8.791 1.00 42.85 C ANISOU 4026 CD2 TYR B 162 6124 5050 5108 1660 -41 -362 C ATOM 4027 CE1 TYR B 162 -4.256 -3.950 -8.212 1.00 42.34 C ANISOU 4027 CE1 TYR B 162 6367 4702 5020 1988 -107 -381 C ATOM 4028 CE2 TYR B 162 -5.637 -2.008 -7.958 1.00 39.54 C ANISOU 4028 CE2 TYR B 162 5832 4452 4738 1592 -127 -334 C ATOM 4029 CZ TYR B 162 -5.368 -3.331 -7.674 1.00 44.73 C ANISOU 4029 CZ TYR B 162 6646 4967 5383 1747 -159 -340 C ATOM 4030 OH TYR B 162 -6.214 -4.040 -6.856 1.00 47.87 O ANISOU 4030 OH TYR B 162 7181 5181 5827 1666 -236 -302 O ATOM 4031 N AVAL B 163 -0.290 0.596 -11.274 0.50 43.82 N ANISOU 4031 N AVAL B 163 5653 5959 5037 2062 372 -401 N ATOM 4032 N BVAL B 163 -0.287 0.594 -11.253 0.50 44.38 N ANISOU 4032 N BVAL B 163 5723 6031 5110 2062 371 -401 N ATOM 4033 CA AVAL B 163 0.460 1.190 -12.394 0.50 45.41 C ANISOU 4033 CA AVAL B 163 5755 6333 5167 2106 503 -421 C ATOM 4034 CA BVAL B 163 0.441 1.213 -12.362 0.50 46.50 C ANISOU 4034 CA BVAL B 163 5890 6470 5307 2100 500 -419 C ATOM 4035 C AVAL B 163 1.957 0.893 -12.320 0.50 48.54 C ANISOU 4035 C AVAL B 163 5969 6932 5541 2313 589 -411 C ATOM 4036 C BVAL B 163 1.946 0.922 -12.313 0.50 49.10 C ANISOU 4036 C BVAL B 163 6037 7004 5613 2307 588 -410 C ATOM 4037 O AVAL B 163 2.612 0.751 -13.351 0.50 50.18 O ANISOU 4037 O AVAL B 163 6165 7235 5666 2451 701 -449 O ATOM 4038 O BVAL B 163 2.593 0.810 -13.353 0.50 50.77 O ANISOU 4038 O BVAL B 163 6236 7313 5742 2439 701 -447 O ATOM 4039 CB AVAL B 163 0.276 2.719 -12.490 0.50 43.80 C ANISOU 4039 CB AVAL B 163 5409 6245 4987 1874 541 -373 C ATOM 4040 CB BVAL B 163 0.223 2.733 -12.395 0.50 45.05 C ANISOU 4040 CB BVAL B 163 5568 6397 5153 1863 532 -370 C ATOM 4041 CG1AVAL B 163 -1.121 3.058 -12.985 0.50 40.32 C ANISOU 4041 CG1AVAL B 163 5145 5636 4537 1714 485 -392 C ATOM 4042 CG1BVAL B 163 0.842 3.317 -13.642 0.50 47.10 C ANISOU 4042 CG1BVAL B 163 5765 6803 5329 1889 670 -383 C ATOM 4043 CG2AVAL B 163 0.571 3.381 -11.156 0.50 42.34 C ANISOU 4043 CG2AVAL B 163 5033 6158 4896 1756 496 -304 C ATOM 4044 CG2BVAL B 163 -1.258 3.053 -12.347 0.50 44.02 C ANISOU 4044 CG2BVAL B 163 5590 6084 5052 1677 441 -372 C ATOM 4045 N GLN B 164 2.495 0.806 -11.105 1.00 49.73 N ANISOU 4045 N GLN B 164 5974 7161 5762 2338 536 -359 N ATOM 4046 CA GLN B 164 3.901 0.448 -10.921 1.00 52.47 C ANISOU 4046 CA GLN B 164 6130 7710 6095 2549 598 -345 C ATOM 4047 C GLN B 164 4.146 -0.971 -11.434 1.00 53.62 C ANISOU 4047 C GLN B 164 6454 7745 6174 2841 614 -407 C ATOM 4048 O GLN B 164 5.145 -1.224 -12.106 1.00 53.29 O ANISOU 4048 O GLN B 164 6321 7857 6071 3040 725 -432 O ATOM 4049 CB GLN B 164 4.321 0.587 -9.451 1.00 53.72 C ANISOU 4049 CB GLN B 164 6118 7961 6333 2517 510 -278 C ATOM 4050 CG GLN B 164 4.549 2.048 -9.023 1.00 60.20 C ANISOU 4050 CG GLN B 164 6704 8963 7205 2271 524 -227 C ATOM 4051 CD GLN B 164 4.763 2.228 -7.521 1.00 65.34 C ANISOU 4051 CD GLN B 164 7226 9675 7924 2209 415 -171 C ATOM 4052 OE1 GLN B 164 5.630 2.994 -7.099 1.00 71.61 O ANISOU 4052 OE1 GLN B 164 7766 10697 8745 2139 432 -137 O ATOM 4053 NE2 GLN B 164 3.966 1.537 -6.712 1.00 65.77 N ANISOU 4053 NE2 GLN B 164 7458 9531 8000 2221 302 -161 N ATOM 4054 N ASP B 165 3.209 -1.873 -11.148 1.00 52.60 N ANISOU 4054 N ASP B 165 6587 7347 6054 2861 511 -433 N ATOM 4055 CA ASP B 165 3.284 -3.257 -11.619 1.00 55.38 C ANISOU 4055 CA ASP B 165 7164 7535 6342 3118 512 -499 C ATOM 4056 C ASP B 165 3.292 -3.351 -13.157 1.00 57.71 C ANISOU 4056 C ASP B 165 7576 7820 6529 3197 619 -586 C ATOM 4057 O ASP B 165 4.155 -3.999 -13.740 1.00 58.99 O ANISOU 4057 O ASP B 165 7747 8048 6619 3459 707 -631 O ATOM 4058 CB ASP B 165 2.120 -4.066 -11.040 1.00 53.96 C ANISOU 4058 CB ASP B 165 7253 7049 6199 3054 378 -505 C ATOM 4059 CG ASP B 165 2.188 -5.527 -11.408 1.00 56.15 C ANISOU 4059 CG ASP B 165 7789 7126 6419 3307 367 -571 C ATOM 4060 OD1 ASP B 165 3.215 -6.167 -11.105 1.00 56.10 O ANISOU 4060 OD1 ASP B 165 7722 7198 6397 3567 396 -559 O ATOM 4061 OD2 ASP B 165 1.217 -6.035 -12.002 1.00 57.40 O ANISOU 4061 OD2 ASP B 165 8215 7049 6547 3248 326 -638 O ATOM 4062 N MET B 166 2.334 -2.691 -13.801 1.00 59.28 N ANISOU 4062 N MET B 166 7867 7946 6712 2981 612 -608 N ATOM 4063 CA MET B 166 2.303 -2.560 -15.267 1.00 61.24 C ANISOU 4063 CA MET B 166 8211 8212 6844 3020 711 -680 C ATOM 4064 C MET B 166 3.598 -2.001 -15.860 1.00 62.61 C ANISOU 4064 C MET B 166 8148 8679 6961 3135 878 -664 C ATOM 4065 O MET B 166 3.941 -2.308 -16.999 1.00 64.24 O ANISOU 4065 O MET B 166 8440 8917 7052 3288 983 -731 O ATOM 4066 CB MET B 166 1.179 -1.606 -15.692 1.00 60.19 C ANISOU 4066 CB MET B 166 8134 8020 6715 2740 675 -674 C ATOM 4067 CG MET B 166 -0.226 -2.158 -15.609 1.00 60.18 C ANISOU 4067 CG MET B 166 8394 7737 6733 2626 535 -715 C ATOM 4068 SD MET B 166 -1.371 -1.015 -16.411 1.00 61.34 S ANISOU 4068 SD MET B 166 8585 7869 6854 2359 516 -716 S ATOM 4069 CE MET B 166 -2.864 -2.003 -16.455 1.00 59.64 C ANISOU 4069 CE MET B 166 8680 7335 6646 2284 356 -786 C ATOM 4070 N GLY B 167 4.292 -1.159 -15.098 1.00 63.55 N ANISOU 4070 N GLY B 167 7972 9018 7158 3048 902 -578 N ATOM 4071 CA GLY B 167 5.451 -0.429 -15.602 1.00 65.95 C ANISOU 4071 CA GLY B 167 8014 9619 7425 3088 1059 -548 C ATOM 4072 C GLY B 167 5.016 0.728 -16.484 1.00 66.05 C ANISOU 4072 C GLY B 167 8022 9680 7393 2870 1130 -535 C ATOM 4073 O GLY B 167 5.690 1.063 -17.456 1.00 68.67 O ANISOU 4073 O GLY B 167 8275 10180 7638 2933 1283 -542 O ATOM 4074 N GLN B 168 3.883 1.337 -16.140 1.00 64.77 N ANISOU 4074 N GLN B 168 7948 9373 7288 2620 1024 -512 N ATOM 4075 CA GLN B 168 3.305 2.416 -16.940 1.00 65.14 C ANISOU 4075 CA GLN B 168 8029 9430 7293 2417 1069 -496 C ATOM 4076 C GLN B 168 3.033 3.661 -16.088 1.00 63.21 C ANISOU 4076 C GLN B 168 7625 9236 7156 2146 1021 -411 C ATOM 4077 O GLN B 168 2.076 4.403 -16.343 1.00 61.25 O ANISOU 4077 O GLN B 168 7471 8891 6908 1956 982 -397 O ATOM 4078 CB GLN B 168 2.014 1.927 -17.609 1.00 65.16 C ANISOU 4078 CB GLN B 168 8344 9181 7235 2395 986 -566 C ATOM 4079 CG GLN B 168 2.222 0.790 -18.609 1.00 70.57 C ANISOU 4079 CG GLN B 168 9224 9798 7791 2644 1037 -664 C ATOM 4080 CD GLN B 168 3.101 1.187 -19.784 1.00 73.92 C ANISOU 4080 CD GLN B 168 9573 10425 8090 2741 1221 -670 C ATOM 4081 OE1 GLN B 168 3.169 2.359 -20.154 1.00 78.14 O ANISOU 4081 OE1 GLN B 168 9992 11087 8610 2576 1296 -609 O ATOM 4082 NE2 GLN B 168 3.779 0.208 -20.375 1.00 76.28 N ANISOU 4082 NE2 GLN B 168 9945 10746 8291 3013 1303 -742 N ATOM 4083 N GLU B 169 3.890 3.889 -15.092 1.00 62.92 N ANISOU 4083 N GLU B 169 7349 9356 7202 2139 1020 -359 N ATOM 4084 CA GLU B 169 3.739 5.009 -14.163 1.00 62.50 C ANISOU 4084 CA GLU B 169 7147 9353 7249 1895 968 -290 C ATOM 4085 C GLU B 169 3.646 6.350 -14.890 1.00 62.76 C ANISOU 4085 C GLU B 169 7133 9459 7254 1696 1060 -250 C ATOM 4086 O GLU B 169 2.737 7.134 -14.634 1.00 60.39 O ANISOU 4086 O GLU B 169 6902 9050 6995 1495 994 -225 O ATOM 4087 CB GLU B 169 4.898 5.035 -13.160 1.00 63.66 C ANISOU 4087 CB GLU B 169 7024 9700 7463 1939 969 -249 C ATOM 4088 CG GLU B 169 5.073 3.801 -12.302 0.00 65.87 C ANISOU 4088 CG GLU B 169 7335 9920 7773 2138 873 -270 C ATOM 4089 CD GLU B 169 6.091 2.824 -12.872 0.00 68.18 C ANISOU 4089 CD GLU B 169 7582 10324 7997 2435 963 -305 C ATOM 4090 OE1 GLU B 169 6.145 2.664 -14.110 0.00 68.90 O ANISOU 4090 OE1 GLU B 169 7767 10417 7993 2524 1074 -347 O ATOM 4091 OE2 GLU B 169 6.833 2.210 -12.077 0.00 69.19 O ANISOU 4091 OE2 GLU B 169 7588 10542 8159 2591 924 -291 O ATOM 4092 N ASP B 170 4.568 6.600 -15.814 1.00 65.02 N ANISOU 4092 N ASP B 170 7312 9927 7465 1758 1216 -240 N ATOM 4093 CA ASP B 170 4.622 7.897 -16.500 1.00 65.90 C ANISOU 4093 CA ASP B 170 7372 10121 7545 1567 1320 -186 C ATOM 4094 C ASP B 170 3.504 8.102 -17.537 1.00 63.91 C ANISOU 4094 C ASP B 170 7380 9698 7205 1520 1317 -207 C ATOM 4095 O ASP B 170 3.060 9.233 -17.755 1.00 62.96 O ANISOU 4095 O ASP B 170 7280 9553 7089 1321 1332 -156 O ATOM 4096 CB ASP B 170 5.998 8.097 -17.143 1.00 68.31 C ANISOU 4096 CB ASP B 170 7467 10692 7796 1641 1502 -159 C ATOM 4097 CG ASP B 170 7.121 8.139 -16.116 1.00 72.31 C ANISOU 4097 CG ASP B 170 7675 11404 8397 1645 1499 -126 C ATOM 4098 OD1 ASP B 170 6.846 8.420 -14.928 1.00 72.44 O ANISOU 4098 OD1 ASP B 170 7638 11369 8519 1518 1369 -108 O ATOM 4099 OD2 ASP B 170 8.284 7.886 -16.496 1.00 80.50 O ANISOU 4099 OD2 ASP B 170 8525 12665 9396 1779 1627 -120 O ATOM 4100 N MET B 171 3.047 7.013 -18.154 1.00 62.43 N ANISOU 4100 N MET B 171 7397 9388 6937 1702 1288 -284 N ATOM 4101 CA MET B 171 2.019 7.080 -19.197 1.00 62.26 C ANISOU 4101 CA MET B 171 7622 9218 6815 1678 1272 -315 C ATOM 4102 C MET B 171 0.595 7.212 -18.631 1.00 57.43 C ANISOU 4102 C MET B 171 7158 8389 6274 1538 1100 -321 C ATOM 4103 O MET B 171 -0.175 8.067 -19.068 1.00 55.08 O ANISOU 4103 O MET B 171 6944 8030 5953 1394 1085 -290 O ATOM 4104 CB MET B 171 2.093 5.831 -20.085 1.00 65.82 C ANISOU 4104 CB MET B 171 8244 9620 7144 1923 1300 -408 C ATOM 4105 CG MET B 171 1.411 5.982 -21.447 1.00 73.11 C ANISOU 4105 CG MET B 171 9388 10469 7920 1923 1330 -440 C ATOM 4106 SD MET B 171 0.744 4.429 -22.100 1.00 87.09 S ANISOU 4106 SD MET B 171 11462 12042 9586 2133 1242 -576 S ATOM 4107 CE MET B 171 0.059 4.976 -23.668 1.00 86.90 C ANISOU 4107 CE MET B 171 11645 11990 9381 2086 1282 -592 C ATOM 4108 N LEU B 172 0.265 6.366 -17.657 1.00 53.96 N ANISOU 4108 N LEU B 172 6745 7840 5919 1588 977 -354 N ATOM 4109 CA LEU B 172 -1.115 6.174 -17.209 1.00 50.86 C ANISOU 4109 CA LEU B 172 6510 7236 5578 1495 821 -374 C ATOM 4110 C LEU B 172 -1.468 6.764 -15.837 1.00 46.98 C ANISOU 4110 C LEU B 172 5908 6719 5224 1332 733 -318 C ATOM 4111 O LEU B 172 -2.652 6.946 -15.541 1.00 46.17 O ANISOU 4111 O LEU B 172 5908 6472 5162 1219 629 -317 O ATOM 4112 CB LEU B 172 -1.439 4.678 -17.202 1.00 49.84 C ANISOU 4112 CB LEU B 172 6549 6961 5428 1662 741 -457 C ATOM 4113 CG LEU B 172 -1.435 4.022 -18.581 1.00 53.69 C ANISOU 4113 CG LEU B 172 7216 7414 5768 1812 793 -534 C ATOM 4114 CD1 LEU B 172 -1.335 2.505 -18.452 1.00 57.45 C ANISOU 4114 CD1 LEU B 172 7827 7772 6229 2009 743 -616 C ATOM 4115 CD2 LEU B 172 -2.671 4.424 -19.376 1.00 51.28 C ANISOU 4115 CD2 LEU B 172 7087 6992 5404 1694 727 -552 C ATOM 4116 N LEU B 173 -0.472 7.061 -15.003 1.00 45.22 N ANISOU 4116 N LEU B 173 5475 6641 5065 1320 773 -276 N ATOM 4117 CA LEU B 173 -0.761 7.481 -13.630 1.00 43.72 C ANISOU 4117 CA LEU B 173 5198 6424 4991 1187 683 -236 C ATOM 4118 C LEU B 173 -1.509 8.817 -13.541 1.00 42.43 C ANISOU 4118 C LEU B 173 5039 6222 4860 969 667 -190 C ATOM 4119 O LEU B 173 -2.519 8.895 -12.844 1.00 40.26 O ANISOU 4119 O LEU B 173 4835 5818 4645 882 564 -187 O ATOM 4120 CB LEU B 173 0.493 7.520 -12.747 1.00 43.28 C ANISOU 4120 CB LEU B 173 4914 6544 4987 1220 714 -206 C ATOM 4121 CG LEU B 173 0.231 7.844 -11.268 1.00 46.21 C ANISOU 4121 CG LEU B 173 5210 6888 5459 1100 610 -174 C ATOM 4122 CD1 LEU B 173 -0.881 6.958 -10.673 1.00 37.10 C ANISOU 4122 CD1 LEU B 173 4230 5532 4337 1133 485 -199 C ATOM 4123 CD2 LEU B 173 1.524 7.731 -10.452 1.00 48.32 C ANISOU 4123 CD2 LEU B 173 5254 7342 5763 1158 625 -152 C ATOM 4124 N PRO B 174 -1.017 9.865 -14.228 1.00 42.72 N ANISOU 4124 N PRO B 174 5005 6367 4858 885 776 -150 N ATOM 4125 CA PRO B 174 -1.694 11.162 -14.118 1.00 41.90 C ANISOU 4125 CA PRO B 174 4923 6211 4785 690 763 -103 C ATOM 4126 C PRO B 174 -3.166 11.114 -14.517 1.00 39.82 C ANISOU 4126 C PRO B 174 4860 5769 4502 667 677 -121 C ATOM 4127 O PRO B 174 -4.002 11.688 -13.828 1.00 39.24 O ANISOU 4127 O PRO B 174 4809 5607 4493 551 602 -101 O ATOM 4128 CB PRO B 174 -0.903 12.061 -15.082 1.00 44.02 C ANISOU 4128 CB PRO B 174 5129 6611 4988 638 908 -59 C ATOM 4129 CG PRO B 174 0.434 11.419 -15.185 1.00 46.89 C ANISOU 4129 CG PRO B 174 5340 7148 5328 766 995 -72 C ATOM 4130 CD PRO B 174 0.169 9.944 -15.101 1.00 44.83 C ANISOU 4130 CD PRO B 174 5173 6809 5051 961 922 -141 C ATOM 4131 N LEU B 175 -3.476 10.431 -15.617 1.00 40.17 N ANISOU 4131 N LEU B 175 5043 5768 4451 781 685 -163 N ATOM 4132 CA LEU B 175 -4.858 10.309 -16.070 1.00 37.88 C ANISOU 4132 CA LEU B 175 4932 5326 4136 762 591 -187 C ATOM 4133 C LEU B 175 -5.702 9.478 -15.107 1.00 34.92 C ANISOU 4133 C LEU B 175 4600 4824 3842 766 458 -221 C ATOM 4134 O LEU B 175 -6.785 9.901 -14.724 1.00 35.42 O ANISOU 4134 O LEU B 175 4706 4797 3955 667 377 -205 O ATOM 4135 CB LEU B 175 -4.924 9.707 -17.474 1.00 39.77 C ANISOU 4135 CB LEU B 175 5315 5555 4242 884 622 -235 C ATOM 4136 CG LEU B 175 -6.325 9.556 -18.065 1.00 37.94 C ANISOU 4136 CG LEU B 175 5262 5184 3969 864 513 -266 C ATOM 4137 CD1 LEU B 175 -7.101 10.874 -17.984 1.00 41.54 C ANISOU 4137 CD1 LEU B 175 5715 5614 4456 717 490 -198 C ATOM 4138 CD2 LEU B 175 -6.245 9.058 -19.488 1.00 38.35 C ANISOU 4138 CD2 LEU B 175 5458 5245 3869 980 551 -316 C ATOM 4139 N ALA B 176 -5.205 8.309 -14.707 1.00 36.24 N ANISOU 4139 N ALA B 176 4759 4989 4023 886 440 -263 N ATOM 4140 CA ALA B 176 -5.968 7.405 -13.817 1.00 34.77 C ANISOU 4140 CA ALA B 176 4634 4672 3907 891 322 -288 C ATOM 4141 C ALA B 176 -6.215 8.016 -12.435 1.00 33.39 C ANISOU 4141 C ALA B 176 4352 4497 3839 768 278 -237 C ATOM 4142 O ALA B 176 -7.267 7.807 -11.828 1.00 34.38 O ANISOU 4142 O ALA B 176 4535 4511 4018 705 187 -237 O ATOM 4143 CB ALA B 176 -5.253 6.060 -13.681 1.00 32.06 C ANISOU 4143 CB ALA B 176 4315 4320 3547 1059 323 -334 C ATOM 4144 N TRP B 177 -5.226 8.752 -11.940 1.00 32.89 N ANISOU 4144 N TRP B 177 4131 4566 3801 732 346 -197 N ATOM 4145 CA TRP B 177 -5.329 9.449 -10.666 1.00 33.84 C ANISOU 4145 CA TRP B 177 4154 4701 4005 613 312 -156 C ATOM 4146 C TRP B 177 -6.450 10.492 -10.749 1.00 33.44 C ANISOU 4146 C TRP B 177 4158 4575 3973 476 286 -132 C ATOM 4147 O TRP B 177 -7.279 10.610 -9.850 1.00 32.49 O ANISOU 4147 O TRP B 177 4052 4381 3913 407 218 -121 O ATOM 4148 CB TRP B 177 -3.982 10.117 -10.347 1.00 33.80 C ANISOU 4148 CB TRP B 177 3971 4863 4008 587 392 -127 C ATOM 4149 CG TRP B 177 -3.912 10.883 -9.056 1.00 36.15 C ANISOU 4149 CG TRP B 177 4168 5190 4378 463 358 -95 C ATOM 4150 CD1 TRP B 177 -4.405 12.135 -8.814 1.00 36.80 C ANISOU 4150 CD1 TRP B 177 4251 5245 4487 309 361 -68 C ATOM 4151 CD2 TRP B 177 -3.271 10.465 -7.846 1.00 34.65 C ANISOU 4151 CD2 TRP B 177 3871 5065 4229 490 315 -91 C ATOM 4152 NE1 TRP B 177 -4.129 12.514 -7.523 1.00 37.88 N ANISOU 4152 NE1 TRP B 177 4296 5420 4678 233 323 -56 N ATOM 4153 CE2 TRP B 177 -3.435 11.504 -6.905 1.00 41.81 C ANISOU 4153 CE2 TRP B 177 4723 5981 5182 339 291 -68 C ATOM 4154 CE3 TRP B 177 -2.577 9.310 -7.463 1.00 42.99 C ANISOU 4154 CE3 TRP B 177 4885 6169 5281 639 292 -104 C ATOM 4155 CZ2 TRP B 177 -2.930 11.422 -5.601 1.00 40.66 C ANISOU 4155 CZ2 TRP B 177 4479 5900 5071 323 239 -61 C ATOM 4156 CZ3 TRP B 177 -2.073 9.230 -6.164 1.00 44.03 C ANISOU 4156 CZ3 TRP B 177 4912 6367 5450 630 238 -87 C ATOM 4157 CH2 TRP B 177 -2.256 10.279 -5.251 1.00 41.00 C ANISOU 4157 CH2 TRP B 177 4473 6001 5105 469 210 -67 C ATOM 4158 N ARG B 178 -6.455 11.247 -11.842 1.00 34.70 N ANISOU 4158 N ARG B 178 4352 4758 4074 449 348 -119 N ATOM 4159 CA ARG B 178 -7.467 12.276 -12.082 1.00 34.71 C ANISOU 4159 CA ARG B 178 4417 4692 4080 347 329 -90 C ATOM 4160 C ARG B 178 -8.870 11.653 -12.204 1.00 34.38 C ANISOU 4160 C ARG B 178 4493 4525 4045 364 225 -117 C ATOM 4161 O ARG B 178 -9.847 12.208 -11.705 1.00 32.33 O ANISOU 4161 O ARG B 178 4246 4204 3834 287 175 -97 O ATOM 4162 CB ARG B 178 -7.080 13.082 -13.327 1.00 36.19 C ANISOU 4162 CB ARG B 178 4632 4932 4185 335 420 -64 C ATOM 4163 CG ARG B 178 -8.146 13.986 -13.896 1.00 36.73 C ANISOU 4163 CG ARG B 178 4801 4923 4230 275 397 -34 C ATOM 4164 CD ARG B 178 -8.932 13.311 -15.011 1.00 34.31 C ANISOU 4164 CD ARG B 178 4630 4561 3844 359 346 -68 C ATOM 4165 NE ARG B 178 -10.257 13.915 -15.145 1.00 31.44 N ANISOU 4165 NE ARG B 178 4343 4114 3491 312 272 -47 N ATOM 4166 CZ ARG B 178 -10.619 14.825 -16.048 1.00 32.56 C ANISOU 4166 CZ ARG B 178 4559 4246 3565 297 294 -6 C ATOM 4167 NH1 ARG B 178 -11.867 15.276 -16.031 1.00 33.88 N ANISOU 4167 NH1 ARG B 178 4778 4343 3752 273 212 11 N ATOM 4168 NH2 ARG B 178 -9.774 15.279 -16.972 1.00 31.84 N ANISOU 4168 NH2 ARG B 178 4492 4221 3384 311 398 24 N ATOM 4169 N ILE B 179 -8.971 10.499 -12.859 1.00 34.28 N ANISOU 4169 N ILE B 179 4564 4476 3984 464 195 -167 N ATOM 4170 CA ILE B 179 -10.255 9.798 -12.927 1.00 31.25 C ANISOU 4170 CA ILE B 179 4283 3977 3615 462 88 -198 C ATOM 4171 C ILE B 179 -10.702 9.372 -11.531 1.00 29.36 C ANISOU 4171 C ILE B 179 3999 3684 3472 416 26 -188 C ATOM 4172 O ILE B 179 -11.885 9.441 -11.219 1.00 31.19 O ANISOU 4172 O ILE B 179 4257 3847 3747 351 -43 -181 O ATOM 4173 CB ILE B 179 -10.219 8.590 -13.875 1.00 32.46 C ANISOU 4173 CB ILE B 179 4554 4086 3692 569 62 -263 C ATOM 4174 CG1 ILE B 179 -9.946 9.044 -15.313 1.00 30.36 C ANISOU 4174 CG1 ILE B 179 4352 3872 3311 613 120 -271 C ATOM 4175 CG2 ILE B 179 -11.538 7.836 -13.821 1.00 29.78 C ANISOU 4175 CG2 ILE B 179 4309 3625 3381 535 -59 -296 C ATOM 4176 CD1 ILE B 179 -9.831 7.896 -16.318 1.00 31.75 C ANISOU 4176 CD1 ILE B 179 4662 4010 3392 730 103 -348 C ATOM 4177 N VAL B 180 -9.760 8.959 -10.687 1.00 28.30 N ANISOU 4177 N VAL B 180 3792 3593 3367 454 54 -184 N ATOM 4178 CA VAL B 180 -10.073 8.630 -9.295 1.00 28.50 C ANISOU 4178 CA VAL B 180 3778 3580 3469 413 5 -164 C ATOM 4179 C VAL B 180 -10.690 9.820 -8.561 1.00 28.75 C ANISOU 4179 C VAL B 180 3751 3622 3552 296 3 -123 C ATOM 4180 O VAL B 180 -11.734 9.680 -7.923 1.00 29.20 O ANISOU 4180 O VAL B 180 3828 3612 3656 243 -52 -112 O ATOM 4181 CB VAL B 180 -8.842 8.123 -8.519 1.00 29.37 C ANISOU 4181 CB VAL B 180 3812 3757 3590 484 33 -159 C ATOM 4182 CG1 VAL B 180 -9.123 8.110 -7.033 1.00 24.71 C ANISOU 4182 CG1 VAL B 180 3175 3149 3063 427 -9 -126 C ATOM 4183 CG2 VAL B 180 -8.442 6.724 -9.004 1.00 28.79 C ANISOU 4183 CG2 VAL B 180 3823 3638 3478 621 19 -201 C ATOM 4184 N ASN B 181 -10.055 10.984 -8.664 1.00 27.82 N ANISOU 4184 N ASN B 181 3565 3583 3422 255 70 -100 N ATOM 4185 CA ASN B 181 -10.642 12.214 -8.139 1.00 28.38 C ANISOU 4185 CA ASN B 181 3609 3645 3528 155 74 -68 C ATOM 4186 C ASN B 181 -12.088 12.373 -8.589 1.00 27.76 C ANISOU 4186 C ASN B 181 3606 3487 3456 132 23 -66 C ATOM 4187 O ASN B 181 -12.960 12.679 -7.784 1.00 28.85 O ANISOU 4187 O ASN B 181 3731 3588 3643 82 -8 -50 O ATOM 4188 CB ASN B 181 -9.858 13.452 -8.593 1.00 28.23 C ANISOU 4188 CB ASN B 181 3551 3695 3482 109 154 -46 C ATOM 4189 CG ASN B 181 -8.488 13.547 -7.972 1.00 29.41 C ANISOU 4189 CG ASN B 181 3591 3946 3639 97 200 -44 C ATOM 4190 OD1 ASN B 181 -8.182 12.895 -6.968 1.00 28.58 O ANISOU 4190 OD1 ASN B 181 3435 3861 3564 119 164 -52 O ATOM 4191 ND2 ASN B 181 -7.644 14.363 -8.578 1.00 30.40 N ANISOU 4191 ND2 ASN B 181 3675 4141 3733 59 277 -27 N ATOM 4192 N ASP B 182 -12.340 12.167 -9.876 1.00 29.56 N ANISOU 4192 N ASP B 182 3905 3698 3627 175 14 -82 N ATOM 4193 CA ASP B 182 -13.689 12.355 -10.425 1.00 28.61 C ANISOU 4193 CA ASP B 182 3844 3522 3504 159 -47 -80 C ATOM 4194 C ASP B 182 -14.730 11.363 -9.875 1.00 29.05 C ANISOU 4194 C ASP B 182 3911 3514 3612 143 -132 -98 C ATOM 4195 O ASP B 182 -15.907 11.704 -9.812 1.00 31.25 O ANISOU 4195 O ASP B 182 4186 3769 3920 105 -179 -83 O ATOM 4196 CB ASP B 182 -13.672 12.301 -11.954 1.00 29.26 C ANISOU 4196 CB ASP B 182 4010 3611 3498 212 -47 -98 C ATOM 4197 CG ASP B 182 -12.850 13.420 -12.582 1.00 28.78 C ANISOU 4197 CG ASP B 182 3947 3606 3380 209 45 -64 C ATOM 4198 OD1 ASP B 182 -12.518 14.406 -11.891 1.00 30.78 O ANISOU 4198 OD1 ASP B 182 4142 3878 3673 150 96 -27 O ATOM 4199 OD2 ASP B 182 -12.529 13.313 -13.787 1.00 31.03 O ANISOU 4199 OD2 ASP B 182 4299 3915 3577 262 69 -74 O ATOM 4200 N THR B 183 -14.311 10.161 -9.459 1.00 29.20 N ANISOU 4200 N THR B 183 3943 3509 3644 173 -150 -123 N ATOM 4201 CA THR B 183 -15.254 9.184 -8.868 1.00 29.27 C ANISOU 4201 CA THR B 183 3971 3445 3703 138 -223 -130 C ATOM 4202 C THR B 183 -15.915 9.717 -7.589 1.00 29.13 C ANISOU 4202 C THR B 183 3879 3434 3756 67 -219 -87 C ATOM 4203 O THR B 183 -17.004 9.278 -7.223 1.00 29.78 O ANISOU 4203 O THR B 183 3959 3475 3883 16 -270 -79 O ATOM 4204 CB THR B 183 -14.601 7.791 -8.560 1.00 30.16 C ANISOU 4204 CB THR B 183 4133 3510 3815 191 -236 -156 C ATOM 4205 OG1 THR B 183 -13.601 7.932 -7.551 1.00 27.20 O ANISOU 4205 OG1 THR B 183 3693 3185 3457 213 -184 -130 O ATOM 4206 CG2 THR B 183 -13.969 7.182 -9.811 1.00 27.59 C ANISOU 4206 CG2 THR B 183 3897 3174 3413 280 -234 -209 C ATOM 4207 N TYR B 184 -15.273 10.673 -6.921 1.00 28.00 N ANISOU 4207 N TYR B 184 3674 3346 3619 58 -157 -62 N ATOM 4208 CA TYR B 184 -15.854 11.286 -5.723 1.00 28.09 C ANISOU 4208 CA TYR B 184 3629 3365 3680 2 -145 -30 C ATOM 4209 C TYR B 184 -17.086 12.162 -6.009 1.00 29.32 C ANISOU 4209 C TYR B 184 3771 3515 3852 -27 -159 -14 C ATOM 4210 O TYR B 184 -17.793 12.552 -5.090 1.00 28.12 O ANISOU 4210 O TYR B 184 3577 3367 3740 -61 -150 9 O ATOM 4211 CB TYR B 184 -14.781 12.053 -4.942 1.00 29.70 C ANISOU 4211 CB TYR B 184 3786 3623 3876 -5 -85 -19 C ATOM 4212 CG TYR B 184 -13.824 11.112 -4.252 1.00 26.62 C ANISOU 4212 CG TYR B 184 3384 3250 3482 26 -88 -23 C ATOM 4213 CD1 TYR B 184 -14.137 10.557 -3.013 1.00 29.80 C ANISOU 4213 CD1 TYR B 184 3777 3634 3912 7 -107 -3 C ATOM 4214 CD2 TYR B 184 -12.649 10.717 -4.871 1.00 25.61 C ANISOU 4214 CD2 TYR B 184 3256 3158 3316 88 -70 -43 C ATOM 4215 CE1 TYR B 184 -13.277 9.661 -2.390 1.00 30.41 C ANISOU 4215 CE1 TYR B 184 3855 3723 3978 52 -117 2 C ATOM 4216 CE2 TYR B 184 -11.785 9.819 -4.264 1.00 30.41 C ANISOU 4216 CE2 TYR B 184 3849 3786 3919 141 -78 -44 C ATOM 4217 CZ TYR B 184 -12.094 9.299 -3.024 1.00 28.91 C ANISOU 4217 CZ TYR B 184 3659 3570 3755 125 -107 -20 C ATOM 4218 OH TYR B 184 -11.228 8.412 -2.423 1.00 32.22 O ANISOU 4218 OH TYR B 184 4075 4007 4162 193 -121 -12 O ATOM 4219 N ARG B 185 -17.370 12.429 -7.282 1.00 30.42 N ANISOU 4219 N ARG B 185 3949 3653 3956 -2 -182 -25 N ATOM 4220 CA ARG B 185 -18.625 13.086 -7.663 1.00 31.10 C ANISOU 4220 CA ARG B 185 4021 3739 4055 -9 -215 -8 C ATOM 4221 C ARG B 185 -19.828 12.147 -7.575 1.00 31.91 C ANISOU 4221 C ARG B 185 4101 3824 4200 -44 -291 -13 C ATOM 4222 O ARG B 185 -20.966 12.598 -7.713 1.00 34.41 O ANISOU 4222 O ARG B 185 4374 4159 4539 -51 -325 4 O ATOM 4223 CB ARG B 185 -18.522 13.641 -9.084 1.00 33.82 C ANISOU 4223 CB ARG B 185 4424 4092 4334 35 -224 -11 C ATOM 4224 CG ARG B 185 -17.475 14.720 -9.235 1.00 32.52 C ANISOU 4224 CG ARG B 185 4281 3945 4132 49 -141 7 C ATOM 4225 CD ARG B 185 -16.972 14.838 -10.654 1.00 35.02 C ANISOU 4225 CD ARG B 185 4670 4273 4365 91 -134 1 C ATOM 4226 NE ARG B 185 -18.021 15.207 -11.603 1.00 34.77 N ANISOU 4226 NE ARG B 185 4678 4234 4299 122 -193 14 N ATOM 4227 CZ ARG B 185 -18.212 16.422 -12.125 1.00 37.27 C ANISOU 4227 CZ ARG B 185 5032 4548 4580 147 -169 56 C ATOM 4228 NH1 ARG B 185 -17.440 17.459 -11.795 1.00 35.04 N ANISOU 4228 NH1 ARG B 185 4762 4255 4296 126 -80 87 N ATOM 4229 NH2 ARG B 185 -19.208 16.594 -12.989 1.00 34.25 N ANISOU 4229 NH2 ARG B 185 4682 4169 4161 190 -241 68 N ATOM 4230 N THR B 186 -19.584 10.856 -7.329 1.00 31.01 N ANISOU 4230 N THR B 186 4013 3672 4099 -66 -319 -34 N ATOM 4231 CA THR B 186 -20.646 9.844 -7.300 1.00 30.92 C ANISOU 4231 CA THR B 186 3993 3628 4127 -124 -392 -41 C ATOM 4232 C THR B 186 -20.715 9.134 -5.951 1.00 31.71 C ANISOU 4232 C THR B 186 4067 3701 4279 -176 -370 -15 C ATOM 4233 O THR B 186 -19.933 9.410 -5.054 1.00 30.11 O ANISOU 4233 O THR B 186 3855 3512 4075 -156 -307 3 O ATOM 4234 CB THR B 186 -20.401 8.755 -8.371 1.00 30.19 C ANISOU 4234 CB THR B 186 3999 3481 3992 -112 -458 -93 C ATOM 4235 OG1 THR B 186 -19.269 7.962 -7.981 1.00 29.12 O ANISOU 4235 OG1 THR B 186 3922 3301 3842 -80 -423 -107 O ATOM 4236 CG2 THR B 186 -20.155 9.378 -9.739 1.00 28.43 C ANISOU 4236 CG2 THR B 186 3823 3287 3692 -51 -472 -118 C ATOM 4237 N ASP B 187 -21.655 8.196 -5.844 1.00 32.37 N ANISOU 4237 N ASP B 187 4145 3749 4405 -249 -426 -13 N ATOM 4238 CA ASP B 187 -21.783 7.304 -4.692 1.00 33.09 C ANISOU 4238 CA ASP B 187 4237 3797 4538 -309 -410 19 C ATOM 4239 C ASP B 187 -20.756 6.151 -4.620 1.00 33.28 C ANISOU 4239 C ASP B 187 4374 3733 4536 -281 -416 0 C ATOM 4240 O ASP B 187 -20.796 5.370 -3.673 1.00 34.85 O ANISOU 4240 O ASP B 187 4596 3884 4762 -322 -404 34 O ATOM 4241 CB ASP B 187 -23.183 6.664 -4.702 1.00 33.66 C ANISOU 4241 CB ASP B 187 4265 3858 4668 -419 -468 32 C ATOM 4242 CG ASP B 187 -24.302 7.678 -4.559 1.00 38.68 C ANISOU 4242 CG ASP B 187 4766 4592 5338 -437 -457 61 C ATOM 4243 OD1 ASP B 187 -24.163 8.630 -3.762 1.00 32.71 O ANISOU 4243 OD1 ASP B 187 3956 3892 4581 -393 -379 92 O ATOM 4244 OD2 ASP B 187 -25.339 7.514 -5.247 1.00 44.08 O ANISOU 4244 OD2 ASP B 187 5399 5302 6048 -491 -530 49 O ATOM 4245 N LEU B 188 -19.852 6.030 -5.593 1.00 33.35 N ANISOU 4245 N LEU B 188 4458 3722 4490 -203 -430 -49 N ATOM 4246 CA LEU B 188 -19.001 4.830 -5.712 1.00 32.47 C ANISOU 4246 CA LEU B 188 4463 3522 4353 -156 -445 -75 C ATOM 4247 C LEU B 188 -18.237 4.461 -4.446 1.00 32.71 C ANISOU 4247 C LEU B 188 4499 3538 4390 -126 -396 -32 C ATOM 4248 O LEU B 188 -18.125 3.282 -4.120 1.00 32.82 O ANISOU 4248 O LEU B 188 4603 3455 4412 -129 -419 -26 O ATOM 4249 CB LEU B 188 -18.008 4.963 -6.867 1.00 32.49 C ANISOU 4249 CB LEU B 188 4524 3538 4284 -52 -440 -130 C ATOM 4250 CG LEU B 188 -18.548 4.772 -8.284 1.00 31.76 C ANISOU 4250 CG LEU B 188 4495 3420 4154 -59 -508 -188 C ATOM 4251 CD1 LEU B 188 -17.471 5.171 -9.295 1.00 31.17 C ANISOU 4251 CD1 LEU B 188 4460 3389 3995 54 -471 -227 C ATOM 4252 CD2 LEU B 188 -19.009 3.340 -8.527 1.00 29.20 C ANISOU 4252 CD2 LEU B 188 4288 2967 3839 -106 -585 -226 C ATOM 4253 N CYS B 189 -17.707 5.460 -3.741 1.00 31.47 N ANISOU 4253 N CYS B 189 4258 3473 4226 -96 -335 -3 N ATOM 4254 CA CYS B 189 -16.892 5.209 -2.554 1.00 32.19 C ANISOU 4254 CA CYS B 189 4348 3572 4308 -58 -299 34 C ATOM 4255 C CYS B 189 -17.699 4.665 -1.377 1.00 32.74 C ANISOU 4255 C CYS B 189 4423 3600 4415 -138 -298 92 C ATOM 4256 O CYS B 189 -17.112 4.175 -0.416 1.00 35.54 O ANISOU 4256 O CYS B 189 4809 3940 4754 -105 -282 129 O ATOM 4257 CB CYS B 189 -16.145 6.469 -2.119 1.00 30.46 C ANISOU 4257 CB CYS B 189 4041 3464 4067 -26 -244 41 C ATOM 4258 SG CYS B 189 -17.209 7.732 -1.412 1.00 34.42 S ANISOU 4258 SG CYS B 189 4451 4028 4599 -108 -208 71 S ATOM 4259 N LEU B 190 -19.029 4.754 -1.449 1.00 30.93 N ANISOU 4259 N LEU B 190 4157 3363 4231 -238 -312 105 N ATOM 4260 CA LEU B 190 -19.899 4.165 -0.432 1.00 31.84 C ANISOU 4260 CA LEU B 190 4272 3442 4383 -330 -302 166 C ATOM 4261 C LEU B 190 -20.282 2.714 -0.746 1.00 33.59 C ANISOU 4261 C LEU B 190 4605 3529 4628 -388 -357 167 C ATOM 4262 O LEU B 190 -20.749 1.990 0.133 1.00 34.18 O ANISOU 4262 O LEU B 190 4713 3548 4725 -461 -344 226 O ATOM 4263 CB LEU B 190 -21.171 4.991 -0.284 1.00 31.31 C ANISOU 4263 CB LEU B 190 4089 3451 4356 -411 -281 184 C ATOM 4264 CG LEU B 190 -21.021 6.437 0.170 1.00 31.22 C ANISOU 4264 CG LEU B 190 3986 3550 4325 -366 -221 187 C ATOM 4265 CD1 LEU B 190 -22.392 7.109 0.180 1.00 32.79 C ANISOU 4265 CD1 LEU B 190 4079 3813 4568 -427 -206 203 C ATOM 4266 CD2 LEU B 190 -20.366 6.516 1.522 1.00 28.96 C ANISOU 4266 CD2 LEU B 190 3712 3287 4004 -338 -167 226 C ATOM 4267 N LEU B 191 -20.073 2.293 -1.990 1.00 34.27 N ANISOU 4267 N LEU B 191 4762 3557 4703 -359 -415 102 N ATOM 4268 CA LEU B 191 -20.601 1.016 -2.473 1.00 35.08 C ANISOU 4268 CA LEU B 191 4979 3520 4828 -433 -481 84 C ATOM 4269 C LEU B 191 -19.554 -0.057 -2.763 1.00 35.20 C ANISOU 4269 C LEU B 191 5161 3411 4803 -334 -504 54 C ATOM 4270 O LEU B 191 -19.876 -1.243 -2.713 1.00 36.42 O ANISOU 4270 O LEU B 191 5442 3420 4976 -393 -542 60 O ATOM 4271 CB LEU B 191 -21.434 1.256 -3.729 1.00 34.15 C ANISOU 4271 CB LEU B 191 4830 3420 4724 -494 -547 23 C ATOM 4272 CG LEU B 191 -22.568 2.269 -3.560 1.00 34.30 C ANISOU 4272 CG LEU B 191 4682 3563 4786 -576 -534 51 C ATOM 4273 CD1 LEU B 191 -23.293 2.498 -4.885 1.00 34.60 C ANISOU 4273 CD1 LEU B 191 4694 3629 4825 -612 -616 -9 C ATOM 4274 CD2 LEU B 191 -23.539 1.822 -2.489 1.00 33.62 C ANISOU 4274 CD2 LEU B 191 4547 3465 4761 -708 -510 125 C ATOM 4275 N TYR B 192 -18.317 0.346 -3.058 1.00 34.92 N ANISOU 4275 N TYR B 192 5126 3429 4713 -183 -477 22 N ATOM 4276 CA TYR B 192 -17.274 -0.596 -3.485 1.00 37.41 C ANISOU 4276 CA TYR B 192 5584 3648 4983 -56 -493 -16 C ATOM 4277 C TYR B 192 -15.965 -0.392 -2.734 1.00 36.64 C ANISOU 4277 C TYR B 192 5456 3618 4848 84 -441 17 C ATOM 4278 O TYR B 192 -15.638 0.735 -2.372 1.00 35.42 O ANISOU 4278 O TYR B 192 5165 3606 4686 99 -397 34 O ATOM 4279 CB TYR B 192 -16.996 -0.426 -4.980 1.00 37.81 C ANISOU 4279 CB TYR B 192 5666 3709 4990 6 -521 -108 C ATOM 4280 CG TYR B 192 -18.184 -0.696 -5.881 1.00 39.83 C ANISOU 4280 CG TYR B 192 5966 3903 5267 -117 -595 -156 C ATOM 4281 CD1 TYR B 192 -18.509 -1.995 -6.260 1.00 43.63 C ANISOU 4281 CD1 TYR B 192 6617 4210 5750 -158 -659 -194 C ATOM 4282 CD2 TYR B 192 -18.966 0.347 -6.376 1.00 40.68 C ANISOU 4282 CD2 TYR B 192 5949 4121 5386 -189 -607 -165 C ATOM 4283 CE1 TYR B 192 -19.588 -2.257 -7.095 1.00 41.95 C ANISOU 4283 CE1 TYR B 192 6439 3947 5552 -286 -742 -245 C ATOM 4284 CE2 TYR B 192 -20.051 0.094 -7.218 1.00 38.53 C ANISOU 4284 CE2 TYR B 192 5702 3810 5127 -298 -690 -210 C ATOM 4285 CZ TYR B 192 -20.353 -1.213 -7.574 1.00 42.50 C ANISOU 4285 CZ TYR B 192 6365 4150 5633 -354 -761 -253 C ATOM 4286 OH TYR B 192 -21.422 -1.483 -8.403 1.00 45.09 O ANISOU 4286 OH TYR B 192 6715 4446 5972 -477 -857 -304 O ATOM 4287 N PRO B 193 -15.198 -1.479 -2.514 1.00 38.10 N ANISOU 4287 N PRO B 193 5770 3699 5007 191 -451 24 N ATOM 4288 CA PRO B 193 -13.853 -1.318 -1.975 1.00 38.81 C ANISOU 4288 CA PRO B 193 5818 3874 5055 347 -415 45 C ATOM 4289 C PRO B 193 -12.998 -0.431 -2.877 1.00 38.27 C ANISOU 4289 C PRO B 193 5650 3942 4950 438 -384 -15 C ATOM 4290 O PRO B 193 -13.186 -0.446 -4.093 1.00 36.97 O ANISOU 4290 O PRO B 193 5525 3751 4769 441 -398 -83 O ATOM 4291 CB PRO B 193 -13.308 -2.751 -1.947 1.00 41.14 C ANISOU 4291 CB PRO B 193 6294 4010 5326 463 -443 47 C ATOM 4292 CG PRO B 193 -14.497 -3.599 -1.826 1.00 41.19 C ANISOU 4292 CG PRO B 193 6430 3845 5376 319 -483 67 C ATOM 4293 CD PRO B 193 -15.557 -2.903 -2.639 1.00 41.29 C ANISOU 4293 CD PRO B 193 6366 3901 5421 171 -499 19 C ATOM 4294 N PRO B 194 -12.086 0.366 -2.286 1.00 37.95 N ANISOU 4294 N PRO B 194 5479 4051 4890 500 -344 11 N ATOM 4295 CA PRO B 194 -11.270 1.296 -3.075 1.00 37.23 C ANISOU 4295 CA PRO B 194 5279 4098 4768 561 -304 -35 C ATOM 4296 C PRO B 194 -10.437 0.645 -4.182 1.00 37.50 C ANISOU 4296 C PRO B 194 5385 4108 4755 709 -296 -96 C ATOM 4297 O PRO B 194 -10.276 1.238 -5.249 1.00 35.59 O ANISOU 4297 O PRO B 194 5107 3930 4487 717 -267 -146 O ATOM 4298 CB PRO B 194 -10.352 1.933 -2.032 1.00 38.35 C ANISOU 4298 CB PRO B 194 5292 4379 4899 599 -277 9 C ATOM 4299 CG PRO B 194 -11.087 1.809 -0.754 1.00 38.85 C ANISOU 4299 CG PRO B 194 5373 4400 4988 510 -298 74 C ATOM 4300 CD PRO B 194 -11.861 0.532 -0.838 1.00 38.21 C ANISOU 4300 CD PRO B 194 5456 4137 4926 492 -336 85 C ATOM 4301 N PHE B 195 -9.926 -0.562 -3.945 1.00 38.15 N ANISOU 4301 N PHE B 195 5581 4096 4821 833 -316 -92 N ATOM 4302 CA PHE B 195 -9.076 -1.226 -4.942 1.00 38.14 C ANISOU 4302 CA PHE B 195 5655 4071 4766 1003 -299 -154 C ATOM 4303 C PHE B 195 -9.843 -1.471 -6.243 1.00 38.36 C ANISOU 4303 C PHE B 195 5803 3997 4777 954 -319 -229 C ATOM 4304 O PHE B 195 -9.290 -1.285 -7.327 1.00 39.90 O ANISOU 4304 O PHE B 195 5993 4249 4916 1042 -281 -290 O ATOM 4305 CB PHE B 195 -8.415 -2.508 -4.388 1.00 39.99 C ANISOU 4305 CB PHE B 195 6005 4205 4984 1165 -320 -131 C ATOM 4306 CG PHE B 195 -9.282 -3.746 -4.435 1.00 37.81 C ANISOU 4306 CG PHE B 195 5957 3687 4722 1131 -376 -140 C ATOM 4307 CD1 PHE B 195 -9.268 -4.578 -5.542 1.00 40.18 C ANISOU 4307 CD1 PHE B 195 6425 3856 4984 1214 -388 -221 C ATOM 4308 CD2 PHE B 195 -10.065 -4.107 -3.347 1.00 40.02 C ANISOU 4308 CD2 PHE B 195 6292 3867 5047 1014 -414 -65 C ATOM 4309 CE1 PHE B 195 -10.048 -5.734 -5.582 1.00 41.38 C ANISOU 4309 CE1 PHE B 195 6802 3770 5152 1165 -446 -234 C ATOM 4310 CE2 PHE B 195 -10.839 -5.263 -3.377 1.00 39.73 C ANISOU 4310 CE2 PHE B 195 6467 3601 5027 962 -462 -67 C ATOM 4311 CZ PHE B 195 -10.833 -6.075 -4.498 1.00 38.66 C ANISOU 4311 CZ PHE B 195 6503 3326 4862 1031 -483 -154 C ATOM 4312 N MET B 196 -11.117 -1.842 -6.130 1.00 36.96 N ANISOU 4312 N MET B 196 5722 3682 4640 807 -377 -224 N ATOM 4313 CA MET B 196 -11.979 -2.051 -7.306 1.00 38.44 C ANISOU 4313 CA MET B 196 6015 3779 4811 734 -418 -297 C ATOM 4314 C MET B 196 -12.168 -0.761 -8.118 1.00 36.91 C ANISOU 4314 C MET B 196 5697 3732 4597 676 -390 -322 C ATOM 4315 O MET B 196 -12.140 -0.778 -9.354 1.00 36.14 O ANISOU 4315 O MET B 196 5663 3629 4439 716 -393 -393 O ATOM 4316 CB MET B 196 -13.346 -2.593 -6.877 1.00 39.42 C ANISOU 4316 CB MET B 196 6225 3758 4996 559 -488 -274 C ATOM 4317 CG MET B 196 -13.295 -3.997 -6.286 1.00 43.78 C ANISOU 4317 CG MET B 196 6953 4120 5560 599 -521 -255 C ATOM 4318 SD MET B 196 -14.926 -4.719 -6.036 1.00 54.14 S ANISOU 4318 SD MET B 196 8379 5252 6941 366 -600 -238 S ATOM 4319 CE MET B 196 -14.501 -6.277 -5.256 1.00 56.96 C ANISOU 4319 CE MET B 196 8954 5388 7299 451 -615 -197 C ATOM 4320 N ILE B 197 -12.360 0.345 -7.404 1.00 33.81 N ANISOU 4320 N ILE B 197 5141 3459 4245 587 -364 -261 N ATOM 4321 CA ILE B 197 -12.511 1.663 -8.010 1.00 32.45 C ANISOU 4321 CA ILE B 197 4855 3417 4059 534 -332 -268 C ATOM 4322 C ILE B 197 -11.203 2.023 -8.711 1.00 31.85 C ANISOU 4322 C ILE B 197 4735 3452 3916 672 -260 -296 C ATOM 4323 O ILE B 197 -11.211 2.502 -9.838 1.00 33.09 O ANISOU 4323 O ILE B 197 4901 3652 4019 682 -240 -336 O ATOM 4324 CB ILE B 197 -12.917 2.727 -6.945 1.00 30.88 C ANISOU 4324 CB ILE B 197 4510 3304 3918 425 -314 -198 C ATOM 4325 CG1 ILE B 197 -14.290 2.394 -6.348 1.00 30.88 C ANISOU 4325 CG1 ILE B 197 4540 3212 3979 288 -372 -169 C ATOM 4326 CG2 ILE B 197 -12.963 4.141 -7.529 1.00 31.07 C ANISOU 4326 CG2 ILE B 197 4432 3448 3926 384 -275 -199 C ATOM 4327 CD1 ILE B 197 -14.641 3.225 -5.115 1.00 25.86 C ANISOU 4327 CD1 ILE B 197 3785 2650 3393 206 -345 -101 C ATOM 4328 N ALA B 198 -10.079 1.733 -8.059 1.00 31.70 N ANISOU 4328 N ALA B 198 4669 3483 3894 784 -221 -272 N ATOM 4329 CA ALA B 198 -8.763 1.930 -8.664 1.00 32.42 C ANISOU 4329 CA ALA B 198 4700 3693 3925 924 -146 -296 C ATOM 4330 C ALA B 198 -8.645 1.188 -9.995 1.00 33.03 C ANISOU 4330 C ALA B 198 4921 3703 3926 1030 -141 -375 C ATOM 4331 O ALA B 198 -8.182 1.758 -10.983 1.00 34.11 O ANISOU 4331 O ALA B 198 5024 3937 4001 1071 -80 -403 O ATOM 4332 CB ALA B 198 -7.652 1.485 -7.705 1.00 30.83 C ANISOU 4332 CB ALA B 198 4432 3547 3734 1043 -126 -260 C ATOM 4333 N LEU B 199 -9.072 -0.076 -10.012 1.00 34.36 N ANISOU 4333 N LEU B 199 5264 3699 4094 1069 -203 -410 N ATOM 4334 CA LEU B 199 -9.001 -0.910 -11.218 1.00 36.29 C ANISOU 4334 CA LEU B 199 5680 3851 4258 1174 -209 -499 C ATOM 4335 C LEU B 199 -9.876 -0.366 -12.347 1.00 35.28 C ANISOU 4335 C LEU B 199 5598 3721 4087 1071 -236 -545 C ATOM 4336 O LEU B 199 -9.455 -0.341 -13.506 1.00 36.32 O ANISOU 4336 O LEU B 199 5785 3892 4124 1163 -194 -605 O ATOM 4337 CB LEU B 199 -9.382 -2.368 -10.902 1.00 36.99 C ANISOU 4337 CB LEU B 199 5967 3724 4362 1210 -281 -526 C ATOM 4338 CG LEU B 199 -8.326 -3.166 -10.120 1.00 40.88 C ANISOU 4338 CG LEU B 199 6473 4200 4861 1387 -253 -498 C ATOM 4339 CD1 LEU B 199 -8.763 -4.607 -9.833 1.00 39.70 C ANISOU 4339 CD1 LEU B 199 6553 3807 4725 1415 -324 -518 C ATOM 4340 CD2 LEU B 199 -6.997 -3.163 -10.862 1.00 41.43 C ANISOU 4340 CD2 LEU B 199 6501 4391 4849 1601 -162 -539 C ATOM 4341 N ALA B 200 -11.085 0.065 -11.996 1.00 34.42 N ANISOU 4341 N ALA B 200 5463 3576 4040 890 -303 -515 N ATOM 4342 CA ALA B 200 -11.998 0.684 -12.949 1.00 34.28 C ANISOU 4342 CA ALA B 200 5463 3573 3988 789 -343 -544 C ATOM 4343 C ALA B 200 -11.417 1.965 -13.545 1.00 33.51 C ANISOU 4343 C ALA B 200 5245 3648 3839 815 -257 -523 C ATOM 4344 O ALA B 200 -11.523 2.189 -14.748 1.00 34.57 O ANISOU 4344 O ALA B 200 5446 3806 3884 839 -253 -569 O ATOM 4345 CB ALA B 200 -13.344 0.977 -12.294 1.00 33.23 C ANISOU 4345 CB ALA B 200 5284 3398 3944 604 -421 -501 C ATOM 4346 N CYS B 201 -10.818 2.803 -12.707 1.00 32.22 N ANISOU 4346 N CYS B 201 4917 3601 3725 801 -191 -452 N ATOM 4347 CA CYS B 201 -10.226 4.063 -13.176 1.00 34.22 C ANISOU 4347 CA CYS B 201 5057 4008 3939 803 -104 -422 C ATOM 4348 C CYS B 201 -9.050 3.813 -14.107 1.00 34.71 C ANISOU 4348 C CYS B 201 5145 4140 3901 957 -16 -462 C ATOM 4349 O CYS B 201 -8.899 4.492 -15.123 1.00 36.65 O ANISOU 4349 O CYS B 201 5395 4462 4069 965 37 -469 O ATOM 4350 CB CYS B 201 -9.769 4.924 -11.988 1.00 33.59 C ANISOU 4350 CB CYS B 201 4804 4023 3935 746 -59 -346 C ATOM 4351 SG CYS B 201 -11.141 5.527 -10.985 1.00 35.83 S ANISOU 4351 SG CYS B 201 5041 4256 4316 573 -132 -295 S ATOM 4352 N LEU B 202 -8.218 2.838 -13.746 1.00 35.29 N ANISOU 4352 N LEU B 202 5240 4195 3975 1089 6 -484 N ATOM 4353 CA LEU B 202 -7.061 2.457 -14.552 1.00 35.48 C ANISOU 4353 CA LEU B 202 5283 4291 3906 1264 97 -526 C ATOM 4354 C LEU B 202 -7.487 1.903 -15.919 1.00 37.14 C ANISOU 4354 C LEU B 202 5687 4419 4005 1322 76 -613 C ATOM 4355 O LEU B 202 -6.900 2.242 -16.950 1.00 36.12 O ANISOU 4355 O LEU B 202 5564 4388 3773 1400 163 -635 O ATOM 4356 CB LEU B 202 -6.213 1.437 -13.777 1.00 35.34 C ANISOU 4356 CB LEU B 202 5259 4252 3918 1409 106 -530 C ATOM 4357 CG LEU B 202 -4.973 0.829 -14.446 1.00 36.23 C ANISOU 4357 CG LEU B 202 5386 4435 3943 1630 200 -576 C ATOM 4358 CD1 LEU B 202 -4.034 1.912 -14.988 1.00 30.81 C ANISOU 4358 CD1 LEU B 202 4527 3968 3210 1643 328 -543 C ATOM 4359 CD2 LEU B 202 -4.258 -0.067 -13.448 1.00 34.26 C ANISOU 4359 CD2 LEU B 202 5110 4164 3742 1765 189 -559 C ATOM 4360 N HIS B 203 -8.523 1.069 -15.925 1.00 37.74 N ANISOU 4360 N HIS B 203 5924 4320 4097 1273 -40 -661 N ATOM 4361 CA HIS B 203 -9.078 0.533 -17.171 1.00 38.92 C ANISOU 4361 CA HIS B 203 6271 4377 4140 1301 -88 -753 C ATOM 4362 C HIS B 203 -9.548 1.656 -18.102 1.00 38.49 C ANISOU 4362 C HIS B 203 6190 4417 4019 1217 -78 -740 C ATOM 4363 O HIS B 203 -9.243 1.650 -19.304 1.00 37.98 O ANISOU 4363 O HIS B 203 6218 4391 3821 1306 -34 -793 O ATOM 4364 CB HIS B 203 -10.249 -0.406 -16.865 1.00 40.30 C ANISOU 4364 CB HIS B 203 6593 4352 4367 1205 -230 -794 C ATOM 4365 CG HIS B 203 -10.784 -1.127 -18.065 1.00 44.15 C ANISOU 4365 CG HIS B 203 7300 4727 4746 1230 -300 -904 C ATOM 4366 ND1 HIS B 203 -11.604 -0.523 -18.994 1.00 51.43 N ANISOU 4366 ND1 HIS B 203 8255 5682 5602 1137 -355 -928 N ATOM 4367 CD2 HIS B 203 -10.633 -2.408 -18.475 1.00 52.94 C ANISOU 4367 CD2 HIS B 203 8624 5690 5800 1337 -332 -1001 C ATOM 4368 CE1 HIS B 203 -11.922 -1.396 -19.931 1.00 52.99 C ANISOU 4368 CE1 HIS B 203 8667 5765 5700 1179 -422 -1038 C ATOM 4369 NE2 HIS B 203 -11.346 -2.549 -19.639 1.00 54.30 N ANISOU 4369 NE2 HIS B 203 8952 5811 5870 1297 -407 -1088 N ATOM 4370 N VAL B 204 -10.296 2.609 -17.549 1.00 37.44 N ANISOU 4370 N VAL B 204 5940 4317 3968 1057 -118 -668 N ATOM 4371 CA VAL B 204 -10.800 3.741 -18.335 1.00 37.24 C ANISOU 4371 CA VAL B 204 5891 4371 3887 982 -115 -641 C ATOM 4372 C VAL B 204 -9.634 4.566 -18.880 1.00 38.24 C ANISOU 4372 C VAL B 204 5938 4656 3937 1063 34 -604 C ATOM 4373 O VAL B 204 -9.640 4.967 -20.041 1.00 42.32 O ANISOU 4373 O VAL B 204 6525 5221 4332 1092 65 -620 O ATOM 4374 CB VAL B 204 -11.779 4.615 -17.510 1.00 36.31 C ANISOU 4374 CB VAL B 204 5658 4255 3881 817 -177 -566 C ATOM 4375 CG1 VAL B 204 -12.075 5.933 -18.219 1.00 34.64 C ANISOU 4375 CG1 VAL B 204 5410 4137 3616 767 -151 -519 C ATOM 4376 CG2 VAL B 204 -13.077 3.844 -17.248 1.00 30.96 C ANISOU 4376 CG2 VAL B 204 5063 3441 3259 724 -323 -604 C ATOM 4377 N ALA B 205 -8.622 4.783 -18.048 1.00 38.89 N ANISOU 4377 N ALA B 205 5872 4822 4083 1095 124 -554 N ATOM 4378 CA ALA B 205 -7.408 5.469 -18.477 1.00 38.64 C ANISOU 4378 CA ALA B 205 5740 4950 3990 1160 273 -518 C ATOM 4379 C ALA B 205 -6.751 4.730 -19.641 1.00 40.48 C ANISOU 4379 C ALA B 205 6094 5205 4080 1330 341 -593 C ATOM 4380 O ALA B 205 -6.294 5.352 -20.595 1.00 40.07 O ANISOU 4380 O ALA B 205 6043 5261 3922 1361 440 -578 O ATOM 4381 CB ALA B 205 -6.435 5.603 -17.312 1.00 36.64 C ANISOU 4381 CB ALA B 205 5304 4782 3835 1170 335 -467 C ATOM 4382 N CYS B 206 -6.700 3.404 -19.557 1.00 41.03 N ANISOU 4382 N CYS B 206 6278 5169 4142 1443 293 -671 N ATOM 4383 CA CYS B 206 -6.113 2.600 -20.621 1.00 42.47 C ANISOU 4383 CA CYS B 206 6601 5353 4184 1624 354 -757 C ATOM 4384 C CYS B 206 -6.900 2.749 -21.928 1.00 42.84 C ANISOU 4384 C CYS B 206 6823 5360 4094 1599 310 -809 C ATOM 4385 O CYS B 206 -6.310 2.930 -22.988 1.00 41.18 O ANISOU 4385 O CYS B 206 6661 5245 3742 1699 414 -830 O ATOM 4386 CB CYS B 206 -6.016 1.124 -20.212 1.00 43.10 C ANISOU 4386 CB CYS B 206 6801 5289 4287 1747 296 -834 C ATOM 4387 SG CYS B 206 -4.730 0.784 -18.990 1.00 44.60 S ANISOU 4387 SG CYS B 206 6807 5562 4577 1866 375 -783 S ATOM 4388 N VAL B 207 -8.225 2.688 -21.839 1.00 42.41 N ANISOU 4388 N VAL B 207 6855 5181 4080 1466 156 -826 N ATOM 4389 CA VAL B 207 -9.078 2.864 -23.012 1.00 44.24 C ANISOU 4389 CA VAL B 207 7240 5382 4186 1429 86 -872 C ATOM 4390 C VAL B 207 -8.890 4.260 -23.604 1.00 43.71 C ANISOU 4390 C VAL B 207 7087 5467 4053 1386 176 -787 C ATOM 4391 O VAL B 207 -8.773 4.407 -24.814 1.00 45.27 O ANISOU 4391 O VAL B 207 7399 5714 4087 1453 218 -818 O ATOM 4392 CB VAL B 207 -10.583 2.646 -22.685 1.00 44.68 C ANISOU 4392 CB VAL B 207 7356 5301 4318 1274 -103 -891 C ATOM 4393 CG1 VAL B 207 -11.467 3.018 -23.895 1.00 44.56 C ANISOU 4393 CG1 VAL B 207 7467 5292 4173 1230 -186 -925 C ATOM 4394 CG2 VAL B 207 -10.840 1.204 -22.269 1.00 43.96 C ANISOU 4394 CG2 VAL B 207 7393 5037 4272 1301 -195 -980 C ATOM 4395 N VAL B 208 -8.849 5.278 -22.750 1.00 41.98 N ANISOU 4395 N VAL B 208 6683 5314 3954 1274 208 -681 N ATOM 4396 CA VAL B 208 -8.690 6.653 -23.225 1.00 42.40 C ANISOU 4396 CA VAL B 208 6666 5486 3958 1217 293 -591 C ATOM 4397 C VAL B 208 -7.343 6.843 -23.934 1.00 44.92 C ANISOU 4397 C VAL B 208 6960 5946 4162 1335 478 -577 C ATOM 4398 O VAL B 208 -7.279 7.483 -24.984 1.00 44.44 O ANISOU 4398 O VAL B 208 6964 5954 3965 1347 541 -551 O ATOM 4399 CB VAL B 208 -8.869 7.681 -22.085 1.00 39.76 C ANISOU 4399 CB VAL B 208 6152 5175 3780 1074 292 -489 C ATOM 4400 CG1 VAL B 208 -8.415 9.062 -22.527 1.00 33.39 C ANISOU 4400 CG1 VAL B 208 5279 4484 2924 1027 409 -393 C ATOM 4401 CG2 VAL B 208 -10.327 7.706 -21.633 1.00 36.64 C ANISOU 4401 CG2 VAL B 208 5787 4668 3468 960 125 -491 C ATOM 4402 N GLN B 209 -6.282 6.256 -23.385 1.00 45.54 N ANISOU 4402 N GLN B 209 6943 6072 4287 1429 564 -593 N ATOM 4403 CA GLN B 209 -4.951 6.382 -23.977 1.00 48.98 C ANISOU 4403 CA GLN B 209 7319 6665 4626 1547 749 -579 C ATOM 4404 C GLN B 209 -4.601 5.283 -24.984 1.00 51.19 C ANISOU 4404 C GLN B 209 7772 6931 4748 1742 786 -688 C ATOM 4405 O GLN B 209 -3.451 5.192 -25.417 1.00 53.26 O ANISOU 4405 O GLN B 209 7979 7328 4930 1871 947 -688 O ATOM 4406 CB GLN B 209 -3.890 6.443 -22.879 1.00 50.02 C ANISOU 4406 CB GLN B 209 7226 6893 4885 1556 832 -531 C ATOM 4407 CG GLN B 209 -4.052 7.646 -21.952 1.00 53.68 C ANISOU 4407 CG GLN B 209 7522 7391 5484 1366 821 -426 C ATOM 4408 CD GLN B 209 -2.784 7.998 -21.193 1.00 56.91 C ANISOU 4408 CD GLN B 209 7699 7952 5974 1362 937 -369 C ATOM 4409 OE1 GLN B 209 -2.697 9.051 -20.567 1.00 66.66 O ANISOU 4409 OE1 GLN B 209 8798 9235 7295 1211 954 -288 O ATOM 4410 NE2 GLN B 209 -1.800 7.121 -21.247 1.00 64.25 N ANISOU 4410 NE2 GLN B 209 8581 8959 6872 1531 1012 -414 N ATOM 4411 N GLN B 210 -5.585 4.458 -25.353 1.00 51.98 N ANISOU 4411 N GLN B 210 8079 6871 4799 1761 640 -784 N ATOM 4412 CA GLN B 210 -5.409 3.382 -26.344 1.00 55.58 C ANISOU 4412 CA GLN B 210 8744 7279 5093 1938 651 -907 C ATOM 4413 C GLN B 210 -4.301 2.390 -25.979 1.00 57.49 C ANISOU 4413 C GLN B 210 8951 7541 5352 2126 743 -958 C ATOM 4414 O GLN B 210 -3.623 1.839 -26.860 1.00 58.33 O ANISOU 4414 O GLN B 210 9162 7694 5306 2311 847 -1029 O ATOM 4415 CB GLN B 210 -5.181 3.966 -27.753 1.00 56.29 C ANISOU 4415 CB GLN B 210 8929 7483 4976 1989 756 -901 C ATOM 4416 CG GLN B 210 -6.350 4.816 -28.245 1.00 57.79 C ANISOU 4416 CG GLN B 210 9196 7639 5122 1837 644 -860 C ATOM 4417 CD GLN B 210 -6.133 5.401 -29.627 1.00 60.29 C ANISOU 4417 CD GLN B 210 9622 8065 5221 1892 745 -842 C ATOM 4418 OE1 GLN B 210 -5.348 4.885 -30.422 1.00 67.46 O ANISOU 4418 OE1 GLN B 210 10618 9038 5974 2058 866 -902 O ATOM 4419 NE2 GLN B 210 -6.840 6.482 -29.921 1.00 62.31 N ANISOU 4419 NE2 GLN B 210 9879 8339 5456 1763 698 -757 N ATOM 4420 N LYS B 211 -4.130 2.159 -24.677 1.00 56.43 N ANISOU 4420 N LYS B 211 8675 7373 5395 2092 706 -923 N ATOM 4421 CA LYS B 211 -3.166 1.176 -24.192 1.00 57.21 C ANISOU 4421 CA LYS B 211 8738 7475 5524 2278 767 -964 C ATOM 4422 C LYS B 211 -3.840 -0.189 -24.090 1.00 58.51 C ANISOU 4422 C LYS B 211 9134 7406 5690 2342 625 -1078 C ATOM 4423 O LYS B 211 -4.924 -0.312 -23.511 1.00 58.18 O ANISOU 4423 O LYS B 211 9144 7214 5747 2187 466 -1077 O ATOM 4424 CB LYS B 211 -2.613 1.581 -22.827 1.00 55.02 C ANISOU 4424 CB LYS B 211 8202 7279 5424 2216 789 -866 C ATOM 4425 CG LYS B 211 -1.547 0.624 -22.252 0.00 58.76 C ANISOU 4425 CG LYS B 211 8612 7781 5933 2422 849 -893 C ATOM 4426 CD LYS B 211 -0.328 0.481 -23.157 0.00 60.91 C ANISOU 4426 CD LYS B 211 8850 8225 6068 2635 1034 -921 C ATOM 4427 CE LYS B 211 0.759 -0.353 -22.497 0.00 62.14 C ANISOU 4427 CE LYS B 211 8902 8436 6273 2847 1093 -932 C ATOM 4428 NZ LYS B 211 1.953 -0.510 -23.374 0.00 64.50 N ANISOU 4428 NZ LYS B 211 9148 8921 6438 3071 1285 -959 N ATOM 4429 N ASP B 212 -3.199 -1.203 -24.665 1.00 59.03 N ANISOU 4429 N ASP B 212 9342 7441 5646 2569 688 -1176 N ATOM 4430 CA ASP B 212 -3.660 -2.577 -24.546 1.00 59.84 C ANISOU 4430 CA ASP B 212 9680 7308 5748 2651 570 -1288 C ATOM 4431 C ASP B 212 -3.188 -3.129 -23.205 1.00 58.61 C ANISOU 4431 C ASP B 212 9410 7108 5751 2706 555 -1244 C ATOM 4432 O ASP B 212 -1.991 -3.307 -22.988 1.00 60.02 O ANISOU 4432 O ASP B 212 9465 7412 5927 2892 684 -1224 O ATOM 4433 CB ASP B 212 -3.107 -3.425 -25.704 1.00 63.08 C ANISOU 4433 CB ASP B 212 10307 7696 5965 2895 652 -1415 C ATOM 4434 CG ASP B 212 -3.564 -4.879 -25.653 1.00 66.53 C ANISOU 4434 CG ASP B 212 11026 7863 6390 2983 531 -1543 C ATOM 4435 OD1 ASP B 212 -4.430 -5.224 -24.822 1.00 68.48 O ANISOU 4435 OD1 ASP B 212 11314 7935 6772 2829 375 -1531 O ATOM 4436 OD2 ASP B 212 -3.052 -5.688 -26.458 1.00 73.25 O ANISOU 4436 OD2 ASP B 212 12069 8671 7093 3206 597 -1656 O ATOM 4437 N ALA B 213 -4.132 -3.386 -22.306 1.00 55.30 N ANISOU 4437 N ALA B 213 9025 6521 5464 2545 400 -1225 N ATOM 4438 CA ALA B 213 -3.827 -4.010 -21.025 1.00 54.23 C ANISOU 4438 CA ALA B 213 8826 6313 5466 2590 367 -1184 C ATOM 4439 C ALA B 213 -4.806 -5.142 -20.716 1.00 54.02 C ANISOU 4439 C ALA B 213 9047 5998 5480 2537 207 -1253 C ATOM 4440 O ALA B 213 -5.079 -5.419 -19.553 1.00 53.60 O ANISOU 4440 O ALA B 213 8949 5855 5561 2462 134 -1195 O ATOM 4441 CB ALA B 213 -3.851 -2.967 -19.915 1.00 52.70 C ANISOU 4441 CB ALA B 213 8358 6246 5420 2417 362 -1050 C ATOM 4442 N ARG B 214 -5.316 -5.803 -21.756 1.00 55.94 N ANISOU 4442 N ARG B 214 9557 6097 5601 2571 154 -1377 N ATOM 4443 CA ARG B 214 -6.274 -6.900 -21.590 1.00 57.73 C ANISOU 4443 CA ARG B 214 10040 6039 5857 2499 -1 -1455 C ATOM 4444 C ARG B 214 -5.680 -8.057 -20.790 1.00 58.66 C ANISOU 4444 C ARG B 214 10249 6008 6031 2671 5 -1463 C ATOM 4445 O ARG B 214 -6.273 -8.505 -19.807 1.00 58.30 O ANISOU 4445 O ARG B 214 10236 5807 6110 2552 -97 -1421 O ATOM 4446 CB ARG B 214 -6.754 -7.431 -22.950 1.00 60.68 C ANISOU 4446 CB ARG B 214 10697 6296 6064 2530 -51 -1604 C ATOM 4447 CG ARG B 214 -7.932 -6.672 -23.568 1.00 65.05 C ANISOU 4447 CG ARG B 214 11253 6877 6587 2292 -156 -1611 C ATOM 4448 CD ARG B 214 -7.505 -5.720 -24.681 1.00 70.20 C ANISOU 4448 CD ARG B 214 11837 7748 7088 2354 -47 -1612 C ATOM 4449 NE ARG B 214 -6.758 -6.411 -25.730 1.00 76.05 N ANISOU 4449 NE ARG B 214 12780 8472 7645 2598 42 -1734 N ATOM 4450 CZ ARG B 214 -7.291 -7.216 -26.647 1.00 82.21 C ANISOU 4450 CZ ARG B 214 13861 9085 8291 2623 -49 -1881 C ATOM 4451 NH1 ARG B 214 -8.601 -7.451 -26.677 1.00 86.27 N ANISOU 4451 NH1 ARG B 214 14500 9439 8839 2404 -241 -1926 N ATOM 4452 NH2 ARG B 214 -6.504 -7.796 -27.546 1.00 83.90 N ANISOU 4452 NH2 ARG B 214 14250 9298 8330 2870 54 -1989 N ATOM 4453 N GLN B 215 -4.516 -8.534 -21.229 1.00 59.30 N ANISOU 4453 N GLN B 215 10374 6143 6015 2959 129 -1514 N ATOM 4454 CA GLN B 215 -3.820 -9.641 -20.579 1.00 61.86 C ANISOU 4454 CA GLN B 215 10793 6338 6372 3177 148 -1524 C ATOM 4455 C GLN B 215 -3.582 -9.364 -19.090 1.00 59.96 C ANISOU 4455 C GLN B 215 10322 6160 6298 3120 136 -1380 C ATOM 4456 O GLN B 215 -3.814 -10.232 -18.248 1.00 60.54 O ANISOU 4456 O GLN B 215 10518 6033 6451 3129 56 -1363 O ATOM 4457 CB GLN B 215 -2.486 -9.915 -21.287 1.00 64.22 C ANISOU 4457 CB GLN B 215 11093 6766 6541 3511 312 -1580 C ATOM 4458 CG GLN B 215 -1.753 -11.165 -20.804 1.00 68.15 C ANISOU 4458 CG GLN B 215 11733 7115 7046 3789 332 -1611 C ATOM 4459 CD GLN B 215 -0.519 -11.483 -21.617 0.00 72.08 C ANISOU 4459 CD GLN B 215 12248 7738 7402 4134 497 -1682 C ATOM 4460 OE1 GLN B 215 -0.114 -10.712 -22.488 0.00 72.24 O ANISOU 4460 OE1 GLN B 215 12143 7985 7321 4162 613 -1695 O ATOM 4461 NE2 GLN B 215 0.088 -12.632 -21.342 0.00 74.30 N ANISOU 4461 NE2 GLN B 215 12690 7872 7669 4409 515 -1724 N ATOM 4462 N TRP B 216 -3.127 -8.154 -18.776 1.00 58.14 N ANISOU 4462 N TRP B 216 9773 6202 6113 3056 213 -1277 N ATOM 4463 CA TRP B 216 -2.907 -7.747 -17.387 1.00 57.44 C ANISOU 4463 CA TRP B 216 9455 6200 6169 2985 198 -1145 C ATOM 4464 C TRP B 216 -4.192 -7.853 -16.566 1.00 54.77 C ANISOU 4464 C TRP B 216 9189 5677 5945 2725 48 -1103 C ATOM 4465 O TRP B 216 -4.181 -8.403 -15.470 1.00 54.66 O ANISOU 4465 O TRP B 216 9188 5562 6020 2738 -2 -1044 O ATOM 4466 CB TRP B 216 -2.358 -6.316 -17.318 1.00 56.28 C ANISOU 4466 CB TRP B 216 8978 6362 6044 2910 294 -1056 C ATOM 4467 CG TRP B 216 -1.927 -5.892 -15.934 1.00 56.69 C ANISOU 4467 CG TRP B 216 8787 6528 6223 2868 289 -934 C ATOM 4468 CD1 TRP B 216 -0.692 -6.062 -15.375 1.00 57.46 C ANISOU 4468 CD1 TRP B 216 8726 6770 6337 3072 363 -888 C ATOM 4469 CD2 TRP B 216 -2.726 -5.224 -14.943 1.00 53.68 C ANISOU 4469 CD2 TRP B 216 8297 6139 5961 2614 202 -845 C ATOM 4470 NE1 TRP B 216 -0.673 -5.547 -14.100 1.00 58.00 N ANISOU 4470 NE1 TRP B 216 8601 6915 6521 2952 317 -780 N ATOM 4471 CE2 TRP B 216 -1.907 -5.027 -13.809 1.00 53.37 C ANISOU 4471 CE2 TRP B 216 8048 6233 5997 2674 224 -754 C ATOM 4472 CE3 TRP B 216 -4.055 -4.780 -14.902 1.00 48.76 C ANISOU 4472 CE3 TRP B 216 7727 5417 5383 2351 106 -837 C ATOM 4473 CZ2 TRP B 216 -2.371 -4.402 -12.647 1.00 51.50 C ANISOU 4473 CZ2 TRP B 216 7675 6024 5869 2479 159 -660 C ATOM 4474 CZ3 TRP B 216 -4.516 -4.161 -13.749 1.00 47.71 C ANISOU 4474 CZ3 TRP B 216 7447 5315 5365 2168 52 -740 C ATOM 4475 CH2 TRP B 216 -3.674 -3.978 -12.635 1.00 49.24 C ANISOU 4475 CH2 TRP B 216 7454 5632 5622 2232 80 -656 C ATOM 4476 N PHE B 217 -5.293 -7.323 -17.095 1.00 54.82 N ANISOU 4476 N PHE B 217 9236 5651 5944 2496 -20 -1128 N ATOM 4477 CA PHE B 217 -6.578 -7.367 -16.384 1.00 53.97 C ANISOU 4477 CA PHE B 217 9172 5392 5942 2239 -154 -1089 C ATOM 4478 C PHE B 217 -7.095 -8.809 -16.270 1.00 57.24 C ANISOU 4478 C PHE B 217 9888 5499 6360 2261 -251 -1156 C ATOM 4479 O PHE B 217 -7.618 -9.205 -15.226 1.00 55.80 O ANISOU 4479 O PHE B 217 9731 5187 6284 2149 -325 -1092 O ATOM 4480 CB PHE B 217 -7.621 -6.455 -17.058 1.00 52.37 C ANISOU 4480 CB PHE B 217 8930 5245 5723 2011 -206 -1103 C ATOM 4481 CG PHE B 217 -7.562 -5.018 -16.596 1.00 46.98 C ANISOU 4481 CG PHE B 217 7955 4792 5104 1888 -158 -995 C ATOM 4482 CD1 PHE B 217 -8.239 -4.619 -15.454 1.00 40.27 C ANISOU 4482 CD1 PHE B 217 6986 3932 4383 1702 -220 -902 C ATOM 4483 CD2 PHE B 217 -6.831 -4.070 -17.300 1.00 42.91 C ANISOU 4483 CD2 PHE B 217 7297 4495 4513 1956 -45 -986 C ATOM 4484 CE1 PHE B 217 -8.188 -3.296 -15.021 1.00 40.84 C ANISOU 4484 CE1 PHE B 217 6812 4198 4507 1595 -177 -812 C ATOM 4485 CE2 PHE B 217 -6.770 -2.750 -16.870 1.00 42.55 C ANISOU 4485 CE2 PHE B 217 7005 4636 4526 1834 -3 -889 C ATOM 4486 CZ PHE B 217 -7.450 -2.362 -15.733 1.00 36.21 C ANISOU 4486 CZ PHE B 217 6098 3811 3851 1658 -72 -807 C ATOM 4487 N ALA B 218 -6.921 -9.585 -17.342 1.00 60.26 N ANISOU 4487 N ALA B 218 10511 5763 6622 2406 -245 -1285 N ATOM 4488 CA ALA B 218 -7.347 -10.992 -17.384 1.00 64.71 C ANISOU 4488 CA ALA B 218 11402 6012 7173 2437 -333 -1368 C ATOM 4489 C ALA B 218 -6.765 -11.850 -16.255 1.00 66.57 C ANISOU 4489 C ALA B 218 11687 6125 7481 2582 -324 -1302 C ATOM 4490 O ALA B 218 -7.449 -12.730 -15.732 1.00 67.69 O ANISOU 4490 O ALA B 218 12026 6011 7682 2483 -420 -1301 O ATOM 4491 CB ALA B 218 -6.991 -11.613 -18.736 1.00 65.19 C ANISOU 4491 CB ALA B 218 11704 5996 7071 2624 -301 -1524 C ATOM 4492 N GLU B 219 -5.515 -11.591 -15.876 1.00 68.15 N ANISOU 4492 N GLU B 219 11707 6510 7676 2809 -210 -1243 N ATOM 4493 CA GLU B 219 -4.838 -12.415 -14.863 1.00 71.52 C ANISOU 4493 CA GLU B 219 12179 6842 8152 2993 -201 -1179 C ATOM 4494 C GLU B 219 -4.945 -11.869 -13.430 1.00 70.35 C ANISOU 4494 C GLU B 219 11804 6791 8135 2858 -227 -1024 C ATOM 4495 O GLU B 219 -4.154 -12.240 -12.562 1.00 72.57 O ANISOU 4495 O GLU B 219 12036 7090 8446 3033 -201 -950 O ATOM 4496 CB GLU B 219 -3.376 -12.685 -15.263 1.00 74.53 C ANISOU 4496 CB GLU B 219 12527 7349 8444 3359 -75 -1214 C ATOM 4497 CG GLU B 219 -2.452 -11.463 -15.297 1.00 75.84 C ANISOU 4497 CG GLU B 219 12326 7886 8602 3418 44 -1151 C ATOM 4498 CD GLU B 219 -1.199 -11.675 -16.157 1.00 78.72 C ANISOU 4498 CD GLU B 219 12675 8388 8847 3747 181 -1222 C ATOM 4499 OE1 GLU B 219 -1.110 -12.695 -16.878 1.00 67.59 O ANISOU 4499 OE1 GLU B 219 11553 6786 7343 3931 187 -1337 O ATOM 4500 OE2 GLU B 219 -0.300 -10.804 -16.114 1.00 82.59 O ANISOU 4500 OE2 GLU B 219 12863 9182 9336 3818 286 -1163 O ATOM 4501 N LEU B 220 -5.928 -11.001 -13.190 1.00 68.47 N ANISOU 4501 N LEU B 220 11435 6616 7965 2559 -280 -976 N ATOM 4502 CA LEU B 220 -6.300 -10.587 -11.835 1.00 66.55 C ANISOU 4502 CA LEU B 220 11034 6414 7839 2396 -320 -842 C ATOM 4503 C LEU B 220 -7.350 -11.548 -11.291 1.00 66.95 C ANISOU 4503 C LEU B 220 11323 6167 7948 2242 -427 -829 C ATOM 4504 O LEU B 220 -8.156 -12.082 -12.049 1.00 66.31 O ANISOU 4504 O LEU B 220 11459 5898 7840 2139 -490 -922 O ATOM 4505 CB LEU B 220 -6.881 -9.171 -11.835 1.00 64.07 C ANISOU 4505 CB LEU B 220 10470 6307 7568 2159 -317 -799 C ATOM 4506 CG LEU B 220 -5.954 -8.023 -12.235 1.00 64.01 C ANISOU 4506 CG LEU B 220 10200 6601 7519 2245 -211 -787 C ATOM 4507 CD1 LEU B 220 -6.767 -6.756 -12.503 1.00 64.36 C ANISOU 4507 CD1 LEU B 220 10088 6776 7591 1999 -224 -768 C ATOM 4508 CD2 LEU B 220 -4.905 -7.776 -11.166 1.00 62.59 C ANISOU 4508 CD2 LEU B 220 9818 6582 7381 2373 -160 -688 C ATOM 4509 N SER B 221 -7.349 -11.753 -9.977 1.00 68.22 N ANISOU 4509 N SER B 221 11443 6290 8186 2215 -449 -712 N ATOM 4510 CA SER B 221 -8.367 -12.581 -9.330 1.00 70.40 C ANISOU 4510 CA SER B 221 11923 6301 8526 2040 -537 -674 C ATOM 4511 C SER B 221 -9.397 -11.683 -8.658 1.00 69.09 C ANISOU 4511 C SER B 221 11569 6233 8447 1738 -572 -591 C ATOM 4512 O SER B 221 -9.500 -11.643 -7.428 1.00 70.35 O ANISOU 4512 O SER B 221 11659 6401 8669 1679 -578 -472 O ATOM 4513 CB SER B 221 -7.732 -13.554 -8.328 1.00 72.57 C ANISOU 4513 CB SER B 221 12326 6435 8812 2223 -537 -594 C ATOM 4514 OG SER B 221 -6.929 -12.873 -7.381 1.00 72.98 O ANISOU 4514 OG SER B 221 12121 6721 8885 2319 -490 -486 O ATOM 4515 N VAL B 222 -10.137 -10.949 -9.489 1.00 67.89 N ANISOU 4515 N VAL B 222 11340 6164 8291 1564 -591 -653 N ATOM 4516 CA VAL B 222 -11.227 -10.081 -9.044 1.00 65.67 C ANISOU 4516 CA VAL B 222 10891 5974 8088 1285 -624 -592 C ATOM 4517 C VAL B 222 -12.464 -10.314 -9.905 1.00 65.99 C ANISOU 4517 C VAL B 222 11059 5883 8131 1075 -709 -676 C ATOM 4518 O VAL B 222 -12.361 -10.746 -11.054 1.00 66.07 O ANISOU 4518 O VAL B 222 11229 5812 8063 1149 -729 -796 O ATOM 4519 CB VAL B 222 -10.847 -8.578 -9.134 1.00 63.96 C ANISOU 4519 CB VAL B 222 10372 6064 7867 1283 -560 -565 C ATOM 4520 CG1 VAL B 222 -10.567 -8.146 -10.568 0.00 65.45 C ANISOU 4520 CG1 VAL B 222 10555 6345 7969 1355 -533 -674 C ATOM 4521 CG2 VAL B 222 -11.882 -7.680 -8.481 0.00 63.58 C ANISOU 4521 CG2 VAL B 222 10151 6107 7899 1032 -585 -489 C ATOM 4522 N ASP B 223 -13.632 -10.027 -9.338 1.00 65.21 N ANISOU 4522 N ASP B 223 10884 5775 8115 817 -759 -615 N ATOM 4523 CA ASP B 223 -14.893 -10.124 -10.060 1.00 66.09 C ANISOU 4523 CA ASP B 223 11064 5806 8243 591 -849 -683 C ATOM 4524 C ASP B 223 -14.991 -8.957 -11.049 1.00 64.76 C ANISOU 4524 C ASP B 223 10727 5853 8027 579 -841 -740 C ATOM 4525 O ASP B 223 -15.265 -7.820 -10.655 1.00 61.79 O ANISOU 4525 O ASP B 223 10111 5672 7693 494 -812 -671 O ATOM 4526 CB ASP B 223 -16.067 -10.103 -9.069 1.00 65.92 C ANISOU 4526 CB ASP B 223 10971 5745 8329 330 -889 -586 C ATOM 4527 CG ASP B 223 -17.422 -10.329 -9.734 1.00 69.71 C ANISOU 4527 CG ASP B 223 11511 6138 8837 81 -994 -650 C ATOM 4528 OD1 ASP B 223 -17.478 -10.680 -10.935 1.00 70.67 O ANISOU 4528 OD1 ASP B 223 11777 6184 8888 105 -1052 -776 O ATOM 4529 OD2 ASP B 223 -18.444 -10.158 -9.034 1.00 73.65 O ANISOU 4529 OD2 ASP B 223 11907 6652 9425 -141 -1019 -572 O ATOM 4530 N MET B 224 -14.763 -9.247 -12.330 1.00 65.60 N ANISOU 4530 N MET B 224 10977 5914 8036 669 -864 -866 N ATOM 4531 CA MET B 224 -14.809 -8.221 -13.375 1.00 65.49 C ANISOU 4531 CA MET B 224 10841 6089 7954 674 -855 -920 C ATOM 4532 C MET B 224 -16.226 -7.677 -13.613 1.00 65.13 C ANISOU 4532 C MET B 224 10702 6088 7954 416 -949 -919 C ATOM 4533 O MET B 224 -16.380 -6.614 -14.209 1.00 64.52 O ANISOU 4533 O MET B 224 10478 6193 7842 400 -940 -925 O ATOM 4534 CB MET B 224 -14.217 -8.747 -14.691 1.00 67.59 C ANISOU 4534 CB MET B 224 11306 6290 8086 845 -854 -1057 C ATOM 4535 CG MET B 224 -12.683 -8.817 -14.728 1.00 69.89 C ANISOU 4535 CG MET B 224 11597 6650 8309 1139 -732 -1059 C ATOM 4536 SD MET B 224 -11.824 -7.218 -14.654 1.00 71.00 S ANISOU 4536 SD MET B 224 11412 7128 8437 1227 -606 -979 S ATOM 4537 CE MET B 224 -12.504 -6.373 -16.084 1.00 74.37 C ANISOU 4537 CE MET B 224 11820 7665 8774 1129 -645 -1057 C ATOM 4538 N GLU B 225 -17.252 -8.401 -13.161 1.00 65.29 N ANISOU 4538 N GLU B 225 10807 5948 8053 217 -1037 -907 N ATOM 4539 CA GLU B 225 -18.624 -7.888 -13.191 1.00 64.78 C ANISOU 4539 CA GLU B 225 10613 5950 8052 -32 -1121 -887 C ATOM 4540 C GLU B 225 -18.734 -6.619 -12.347 1.00 61.29 C ANISOU 4540 C GLU B 225 9883 5727 7679 -67 -1051 -766 C ATOM 4541 O GLU B 225 -19.343 -5.636 -12.765 1.00 60.04 O ANISOU 4541 O GLU B 225 9567 5727 7520 -143 -1075 -763 O ATOM 4542 CB GLU B 225 -19.615 -8.928 -12.664 1.00 67.00 C ANISOU 4542 CB GLU B 225 11014 6027 8418 -246 -1208 -876 C ATOM 4543 CG GLU B 225 -21.083 -8.532 -12.853 1.00 70.86 C ANISOU 4543 CG GLU B 225 11371 6586 8967 -508 -1309 -872 C ATOM 4544 CD GLU B 225 -22.015 -9.173 -11.836 1.00 76.54 C ANISOU 4544 CD GLU B 225 12086 7189 9807 -736 -1341 -794 C ATOM 4545 OE1 GLU B 225 -21.814 -8.964 -10.618 1.00 76.59 O ANISOU 4545 OE1 GLU B 225 11986 7234 9880 -725 -1251 -672 O ATOM 4546 OE2 GLU B 225 -22.961 -9.873 -12.261 1.00 82.88 O ANISOU 4546 OE2 GLU B 225 12991 7869 10633 -934 -1457 -854 O ATOM 4547 N LYS B 226 -18.150 -6.655 -11.156 1.00 58.47 N ANISOU 4547 N LYS B 226 9471 5372 7375 -4 -968 -670 N ATOM 4548 CA LYS B 226 -18.160 -5.502 -10.268 1.00 56.20 C ANISOU 4548 CA LYS B 226 8935 5275 7142 -26 -897 -563 C ATOM 4549 C LYS B 226 -17.360 -4.354 -10.876 1.00 52.63 C ANISOU 4549 C LYS B 226 8357 5017 6622 120 -831 -579 C ATOM 4550 O LYS B 226 -17.774 -3.198 -10.803 1.00 49.03 O ANISOU 4550 O LYS B 226 7716 4723 6189 57 -814 -538 O ATOM 4551 CB LYS B 226 -17.587 -5.872 -8.904 1.00 57.67 C ANISOU 4551 CB LYS B 226 9119 5416 7376 28 -830 -466 C ATOM 4552 CG LYS B 226 -18.374 -6.945 -8.156 1.00 62.46 C ANISOU 4552 CG LYS B 226 9847 5832 8053 -128 -878 -422 C ATOM 4553 CD LYS B 226 -19.317 -6.358 -7.116 1.00 65.29 C ANISOU 4553 CD LYS B 226 10023 6285 8501 -307 -861 -317 C ATOM 4554 CE LYS B 226 -19.860 -7.447 -6.196 1.00 69.85 C ANISOU 4554 CE LYS B 226 10722 6678 9139 -439 -877 -249 C ATOM 4555 NZ LYS B 226 -20.526 -6.884 -4.992 1.00 72.00 N ANISOU 4555 NZ LYS B 226 10818 7057 9481 -567 -827 -131 N ATOM 4556 N ILE B 227 -16.228 -4.677 -11.498 1.00 50.56 N ANISOU 4556 N ILE B 227 8202 4736 6273 315 -788 -639 N ATOM 4557 CA ILE B 227 -15.394 -3.657 -12.121 1.00 48.02 C ANISOU 4557 CA ILE B 227 7769 4595 5880 448 -713 -652 C ATOM 4558 C ILE B 227 -16.178 -2.967 -13.235 1.00 47.36 C ANISOU 4558 C ILE B 227 7656 4587 5751 363 -769 -703 C ATOM 4559 O ILE B 227 -16.116 -1.746 -13.373 1.00 44.60 O ANISOU 4559 O ILE B 227 7147 4407 5393 363 -724 -665 O ATOM 4560 CB ILE B 227 -14.069 -4.238 -12.688 1.00 49.26 C ANISOU 4560 CB ILE B 227 8050 4723 5945 679 -653 -714 C ATOM 4561 CG1 ILE B 227 -13.225 -4.869 -11.580 1.00 51.67 C ANISOU 4561 CG1 ILE B 227 8371 4972 6289 791 -603 -655 C ATOM 4562 CG2 ILE B 227 -13.239 -3.143 -13.371 1.00 45.64 C ANISOU 4562 CG2 ILE B 227 7464 4466 5412 792 -564 -719 C ATOM 4563 CD1 ILE B 227 -12.745 -3.873 -10.536 1.00 47.68 C ANISOU 4563 CD1 ILE B 227 7637 4642 5838 795 -530 -550 C ATOM 4564 N LEU B 228 -16.921 -3.756 -14.010 1.00 47.33 N ANISOU 4564 N LEU B 228 7815 4453 5715 287 -873 -789 N ATOM 4565 CA LEU B 228 -17.694 -3.246 -15.141 1.00 48.24 C ANISOU 4565 CA LEU B 228 7925 4632 5771 214 -949 -847 C ATOM 4566 C LEU B 228 -18.841 -2.345 -14.686 1.00 46.47 C ANISOU 4566 C LEU B 228 7507 4516 5633 40 -992 -773 C ATOM 4567 O LEU B 228 -19.102 -1.324 -15.315 1.00 44.06 O ANISOU 4567 O LEU B 228 7105 4350 5287 41 -997 -768 O ATOM 4568 CB LEU B 228 -18.224 -4.400 -16.002 1.00 51.25 C ANISOU 4568 CB LEU B 228 8537 4839 6096 162 -1066 -965 C ATOM 4569 CG LEU B 228 -17.170 -5.067 -16.895 1.00 55.75 C ANISOU 4569 CG LEU B 228 9313 5334 6536 362 -1028 -1067 C ATOM 4570 CD1 LEU B 228 -17.640 -6.446 -17.399 1.00 57.92 C ANISOU 4570 CD1 LEU B 228 9854 5377 6777 305 -1141 -1181 C ATOM 4571 CD2 LEU B 228 -16.796 -4.159 -18.065 1.00 55.23 C ANISOU 4571 CD2 LEU B 228 9212 5430 6343 465 -992 -1105 C ATOM 4572 N GLU B 229 -19.511 -2.713 -13.594 1.00 45.59 N ANISOU 4572 N GLU B 229 7344 4342 5637 -96 -1014 -711 N ATOM 4573 CA GLU B 229 -20.476 -1.809 -12.957 1.00 45.54 C ANISOU 4573 CA GLU B 229 7130 4456 5719 -231 -1024 -628 C ATOM 4574 C GLU B 229 -19.821 -0.465 -12.644 1.00 41.37 C ANISOU 4574 C GLU B 229 6436 4098 5182 -129 -915 -560 C ATOM 4575 O GLU B 229 -20.402 0.581 -12.900 1.00 40.66 O ANISOU 4575 O GLU B 229 6218 4136 5097 -168 -927 -534 O ATOM 4576 CB GLU B 229 -21.042 -2.407 -11.665 1.00 45.55 C ANISOU 4576 CB GLU B 229 7099 4374 5835 -364 -1024 -557 C ATOM 4577 CG GLU B 229 -21.979 -3.579 -11.885 1.00 52.79 C ANISOU 4577 CG GLU B 229 8143 5131 6783 -528 -1139 -607 C ATOM 4578 CD GLU B 229 -22.302 -4.357 -10.613 1.00 57.39 C ANISOU 4578 CD GLU B 229 8742 5600 7464 -642 -1119 -532 C ATOM 4579 OE1 GLU B 229 -23.054 -5.347 -10.721 1.00 64.04 O ANISOU 4579 OE1 GLU B 229 9694 6297 8339 -797 -1205 -564 O ATOM 4580 OE2 GLU B 229 -21.815 -3.992 -9.515 1.00 56.50 O ANISOU 4580 OE2 GLU B 229 8540 5538 7388 -585 -1019 -440 O ATOM 4581 N ILE B 230 -18.606 -0.503 -12.101 1.00 38.55 N ANISOU 4581 N ILE B 230 6091 3744 4815 1 -815 -533 N ATOM 4582 CA ILE B 230 -17.920 0.724 -11.708 1.00 37.25 C ANISOU 4582 CA ILE B 230 5774 3731 4649 77 -715 -470 C ATOM 4583 C ILE B 230 -17.533 1.513 -12.951 1.00 36.44 C ANISOU 4583 C ILE B 230 5673 3726 4448 162 -696 -511 C ATOM 4584 O ILE B 230 -17.725 2.729 -12.997 1.00 35.75 O ANISOU 4584 O ILE B 230 5461 3759 4363 145 -667 -467 O ATOM 4585 CB ILE B 230 -16.686 0.463 -10.820 1.00 36.66 C ANISOU 4585 CB ILE B 230 5696 3650 4583 190 -625 -433 C ATOM 4586 CG1 ILE B 230 -17.086 -0.299 -9.550 1.00 37.10 C ANISOU 4586 CG1 ILE B 230 5765 3608 4725 109 -641 -378 C ATOM 4587 CG2 ILE B 230 -16.031 1.789 -10.417 1.00 31.85 C ANISOU 4587 CG2 ILE B 230 4925 3202 3976 237 -533 -374 C ATOM 4588 CD1 ILE B 230 -15.913 -0.871 -8.775 1.00 34.74 C ANISOU 4588 CD1 ILE B 230 5507 3272 4420 235 -581 -351 C ATOM 4589 N ILE B 231 -17.034 0.817 -13.969 1.00 36.23 N ANISOU 4589 N ILE B 231 5801 3638 4326 253 -713 -595 N ATOM 4590 CA ILE B 231 -16.678 1.469 -15.229 1.00 37.39 C ANISOU 4590 CA ILE B 231 5973 3874 4360 335 -691 -635 C ATOM 4591 C ILE B 231 -17.878 2.197 -15.843 1.00 37.40 C ANISOU 4591 C ILE B 231 5925 3934 4351 231 -777 -632 C ATOM 4592 O ILE B 231 -17.728 3.319 -16.320 1.00 37.64 O ANISOU 4592 O ILE B 231 5887 4081 4335 268 -734 -600 O ATOM 4593 CB ILE B 231 -16.082 0.483 -16.258 1.00 37.78 C ANISOU 4593 CB ILE B 231 6221 3839 4297 451 -702 -738 C ATOM 4594 CG1 ILE B 231 -14.706 -0.005 -15.794 1.00 39.70 C ANISOU 4594 CG1 ILE B 231 6485 4067 4531 603 -596 -734 C ATOM 4595 CG2 ILE B 231 -15.927 1.161 -17.612 1.00 36.07 C ANISOU 4595 CG2 ILE B 231 6040 3718 3949 516 -689 -776 C ATOM 4596 CD1 ILE B 231 -14.162 -1.156 -16.605 1.00 43.01 C ANISOU 4596 CD1 ILE B 231 7114 4376 4853 731 -604 -837 C ATOM 4597 N ARG B 232 -19.054 1.569 -15.818 1.00 38.46 N ANISOU 4597 N ARG B 232 6092 3989 4531 102 -898 -660 N ATOM 4598 CA ARG B 232 -20.270 2.191 -16.365 1.00 40.36 C ANISOU 4598 CA ARG B 232 6268 4300 4769 6 -997 -657 C ATOM 4599 C ARG B 232 -20.652 3.478 -15.626 1.00 38.31 C ANISOU 4599 C ARG B 232 5810 4162 4585 -28 -947 -555 C ATOM 4600 O ARG B 232 -21.096 4.441 -16.248 1.00 37.94 O ANISOU 4600 O ARG B 232 5707 4211 4496 -18 -971 -536 O ATOM 4601 CB ARG B 232 -21.451 1.213 -16.361 1.00 41.52 C ANISOU 4601 CB ARG B 232 6462 4350 4965 -146 -1137 -704 C ATOM 4602 CG ARG B 232 -21.353 0.153 -17.439 1.00 50.52 C ANISOU 4602 CG ARG B 232 7816 5377 6001 -127 -1222 -824 C ATOM 4603 CD ARG B 232 -22.620 -0.699 -17.544 1.00 58.69 C ANISOU 4603 CD ARG B 232 8890 6326 7083 -309 -1379 -875 C ATOM 4604 NE ARG B 232 -22.319 -2.006 -18.133 1.00 64.10 N ANISOU 4604 NE ARG B 232 9816 6839 7699 -298 -1437 -989 N ATOM 4605 CZ ARG B 232 -22.143 -3.141 -17.453 1.00 64.04 C ANISOU 4605 CZ ARG B 232 9918 6659 7754 -343 -1431 -1004 C ATOM 4606 NH1 ARG B 232 -22.261 -3.184 -16.125 1.00 60.79 N ANISOU 4606 NH1 ARG B 232 9393 6230 7474 -412 -1372 -907 N ATOM 4607 NH2 ARG B 232 -21.859 -4.257 -18.117 1.00 68.94 N ANISOU 4607 NH2 ARG B 232 10781 7116 8297 -315 -1486 -1117 N ATOM 4608 N VAL B 233 -20.491 3.494 -14.305 1.00 36.42 N ANISOU 4608 N VAL B 233 5478 3910 4448 -61 -880 -491 N ATOM 4609 CA VAL B 233 -20.755 4.706 -13.539 1.00 34.96 C ANISOU 4609 CA VAL B 233 5126 3829 4327 -80 -822 -404 C ATOM 4610 C VAL B 233 -19.757 5.812 -13.928 1.00 35.99 C ANISOU 4610 C VAL B 233 5240 4046 4389 35 -723 -379 C ATOM 4611 O VAL B 233 -20.148 6.962 -14.114 1.00 35.92 O ANISOU 4611 O VAL B 233 5152 4121 4374 37 -713 -336 O ATOM 4612 CB VAL B 233 -20.745 4.439 -12.023 1.00 35.13 C ANISOU 4612 CB VAL B 233 5072 3820 4455 -135 -770 -346 C ATOM 4613 CG1 VAL B 233 -20.843 5.747 -11.242 1.00 33.78 C ANISOU 4613 CG1 VAL B 233 4752 3753 4331 -133 -696 -269 C ATOM 4614 CG2 VAL B 233 -21.899 3.499 -11.651 1.00 32.01 C ANISOU 4614 CG2 VAL B 233 4677 3353 4133 -276 -861 -353 C ATOM 4615 N ILE B 234 -18.483 5.453 -14.089 1.00 35.26 N ANISOU 4615 N ILE B 234 5223 3933 4243 131 -649 -404 N ATOM 4616 CA ILE B 234 -17.463 6.415 -14.508 1.00 34.74 C ANISOU 4616 CA ILE B 234 5137 3952 4110 223 -548 -380 C ATOM 4617 C ILE B 234 -17.778 6.987 -15.888 1.00 36.39 C ANISOU 4617 C ILE B 234 5405 4208 4213 255 -583 -401 C ATOM 4618 O ILE B 234 -17.746 8.200 -16.083 1.00 33.55 O ANISOU 4618 O ILE B 234 4989 3925 3834 268 -537 -347 O ATOM 4619 CB ILE B 234 -16.060 5.782 -14.539 1.00 34.42 C ANISOU 4619 CB ILE B 234 5157 3896 4025 328 -467 -410 C ATOM 4620 CG1 ILE B 234 -15.542 5.568 -13.114 1.00 36.01 C ANISOU 4620 CG1 ILE B 234 5278 4087 4318 317 -416 -367 C ATOM 4621 CG2 ILE B 234 -15.104 6.656 -15.299 1.00 33.28 C ANISOU 4621 CG2 ILE B 234 5006 3848 3792 410 -371 -397 C ATOM 4622 CD1 ILE B 234 -14.421 4.540 -13.008 1.00 37.62 C ANISOU 4622 CD1 ILE B 234 5551 4249 4496 422 -375 -403 C ATOM 4623 N LEU B 235 -18.071 6.111 -16.847 1.00 37.54 N ANISOU 4623 N LEU B 235 5678 4301 4283 270 -666 -479 N ATOM 4624 CA LEU B 235 -18.431 6.557 -18.188 1.00 38.82 C ANISOU 4624 CA LEU B 235 5913 4510 4327 303 -716 -503 C ATOM 4625 C LEU B 235 -19.637 7.500 -18.135 1.00 38.27 C ANISOU 4625 C LEU B 235 5744 4498 4299 234 -787 -447 C ATOM 4626 O LEU B 235 -19.651 8.532 -18.808 1.00 36.47 O ANISOU 4626 O LEU B 235 5516 4341 4000 280 -766 -408 O ATOM 4627 CB LEU B 235 -18.713 5.362 -19.104 1.00 40.30 C ANISOU 4627 CB LEU B 235 6261 4621 4431 311 -819 -608 C ATOM 4628 CG LEU B 235 -17.480 4.525 -19.456 1.00 43.78 C ANISOU 4628 CG LEU B 235 6828 5012 4793 423 -742 -671 C ATOM 4629 CD1 LEU B 235 -17.827 3.414 -20.443 1.00 44.44 C ANISOU 4629 CD1 LEU B 235 7098 5007 4778 434 -850 -787 C ATOM 4630 CD2 LEU B 235 -16.370 5.409 -20.015 1.00 44.36 C ANISOU 4630 CD2 LEU B 235 6894 5189 4773 535 -605 -634 C ATOM 4631 N LYS B 236 -20.623 7.151 -17.311 1.00 35.59 N ANISOU 4631 N LYS B 236 5320 4129 4073 132 -861 -438 N ATOM 4632 CA LYS B 236 -21.816 7.978 -17.130 1.00 38.07 C ANISOU 4632 CA LYS B 236 5516 4509 4441 77 -924 -384 C ATOM 4633 C LYS B 236 -21.520 9.346 -16.503 1.00 35.01 C ANISOU 4633 C LYS B 236 5028 4182 4093 114 -815 -294 C ATOM 4634 O LYS B 236 -22.119 10.347 -16.895 1.00 33.62 O ANISOU 4634 O LYS B 236 4812 4067 3893 138 -840 -250 O ATOM 4635 CB LYS B 236 -22.851 7.241 -16.272 1.00 38.47 C ANISOU 4635 CB LYS B 236 5482 4523 4611 -46 -1003 -389 C ATOM 4636 CG LYS B 236 -24.144 8.003 -16.053 1.00 42.84 C ANISOU 4636 CG LYS B 236 5891 5161 5226 -95 -1067 -337 C ATOM 4637 CD LYS B 236 -25.202 7.124 -15.405 1.00 54.39 C ANISOU 4637 CD LYS B 236 7273 6600 6792 -232 -1151 -350 C ATOM 4638 CE LYS B 236 -26.563 7.806 -15.387 1.00 58.50 C ANISOU 4638 CE LYS B 236 7637 7230 7362 -269 -1229 -307 C ATOM 4639 NZ LYS B 236 -27.649 6.882 -14.953 1.00 60.36 N ANISOU 4639 NZ LYS B 236 7787 7459 7689 -421 -1322 -324 N ATOM 4640 N LEU B 237 -20.614 9.390 -15.530 1.00 35.68 N ANISOU 4640 N LEU B 237 5078 4246 4233 119 -703 -269 N ATOM 4641 CA LEU B 237 -20.302 10.654 -14.848 1.00 33.77 C ANISOU 4641 CA LEU B 237 4753 4048 4031 137 -604 -195 C ATOM 4642 C LEU B 237 -19.717 11.689 -15.818 1.00 33.44 C ANISOU 4642 C LEU B 237 4771 4049 3886 212 -548 -167 C ATOM 4643 O LEU B 237 -19.922 12.884 -15.630 1.00 31.53 O ANISOU 4643 O LEU B 237 4486 3836 3659 223 -510 -106 O ATOM 4644 CB LEU B 237 -19.416 10.438 -13.609 1.00 32.20 C ANISOU 4644 CB LEU B 237 4507 3825 3901 120 -510 -180 C ATOM 4645 CG LEU B 237 -17.885 10.326 -13.669 1.00 33.32 C ANISOU 4645 CG LEU B 237 4693 3971 3997 177 -410 -191 C ATOM 4646 CD1 LEU B 237 -17.212 11.668 -13.840 1.00 32.00 C ANISOU 4646 CD1 LEU B 237 4505 3858 3795 205 -316 -141 C ATOM 4647 CD2 LEU B 237 -17.374 9.659 -12.403 1.00 26.49 C ANISOU 4647 CD2 LEU B 237 3781 3077 3209 153 -375 -190 C ATOM 4648 N TYR B 238 -19.040 11.238 -16.875 1.00 34.29 N ANISOU 4648 N TYR B 238 4991 4155 3884 266 -541 -210 N ATOM 4649 CA TYR B 238 -18.525 12.170 -17.880 1.00 33.85 C ANISOU 4649 CA TYR B 238 5002 4142 3716 331 -483 -176 C ATOM 4650 C TYR B 238 -19.608 12.719 -18.801 1.00 34.51 C ANISOU 4650 C TYR B 238 5124 4254 3734 354 -582 -157 C ATOM 4651 O TYR B 238 -19.522 13.874 -19.225 1.00 32.42 O ANISOU 4651 O TYR B 238 4883 4017 3418 393 -536 -92 O ATOM 4652 CB TYR B 238 -17.339 11.581 -18.664 1.00 34.10 C ANISOU 4652 CB TYR B 238 5133 4180 3642 394 -416 -221 C ATOM 4653 CG TYR B 238 -16.114 11.459 -17.788 1.00 34.39 C ANISOU 4653 CG TYR B 238 5109 4222 3736 393 -296 -212 C ATOM 4654 CD1 TYR B 238 -15.538 12.591 -17.202 1.00 34.73 C ANISOU 4654 CD1 TYR B 238 5077 4299 3821 368 -194 -142 C ATOM 4655 CD2 TYR B 238 -15.553 10.217 -17.506 1.00 30.11 C ANISOU 4655 CD2 TYR B 238 4586 3647 3208 416 -293 -275 C ATOM 4656 CE1 TYR B 238 -14.425 12.483 -16.367 1.00 35.93 C ANISOU 4656 CE1 TYR B 238 5156 4470 4024 358 -100 -136 C ATOM 4657 CE2 TYR B 238 -14.444 10.101 -16.669 1.00 30.49 C ANISOU 4657 CE2 TYR B 238 4564 3714 3308 427 -196 -262 C ATOM 4658 CZ TYR B 238 -13.883 11.230 -16.110 1.00 35.13 C ANISOU 4658 CZ TYR B 238 5060 4354 3934 394 -104 -194 C ATOM 4659 OH TYR B 238 -12.790 11.098 -15.280 1.00 38.53 O ANISOU 4659 OH TYR B 238 5410 4819 4412 399 -24 -186 O ATOM 4660 N GLU B 239 -20.631 11.914 -19.089 1.00 34.70 N ANISOU 4660 N GLU B 239 5153 4270 3761 325 -722 -210 N ATOM 4661 CA GLU B 239 -21.784 12.402 -19.850 1.00 34.81 C ANISOU 4661 CA GLU B 239 5173 4330 3725 345 -840 -192 C ATOM 4662 C GLU B 239 -22.617 13.377 -19.018 1.00 33.99 C ANISOU 4662 C GLU B 239 4937 4252 3726 330 -843 -117 C ATOM 4663 O GLU B 239 -23.087 14.397 -19.529 1.00 34.80 O ANISOU 4663 O GLU B 239 5051 4393 3780 391 -864 -60 O ATOM 4664 CB GLU B 239 -22.658 11.245 -20.338 1.00 37.38 C ANISOU 4664 CB GLU B 239 5523 4648 4031 298 -1000 -275 C ATOM 4665 CG GLU B 239 -21.927 10.252 -21.242 1.00 40.94 C ANISOU 4665 CG GLU B 239 6131 5062 4362 327 -1009 -363 C ATOM 4666 CD GLU B 239 -21.266 10.918 -22.437 1.00 46.76 C ANISOU 4666 CD GLU B 239 6995 5841 4932 431 -953 -342 C ATOM 4667 OE1 GLU B 239 -21.922 11.774 -23.071 1.00 52.00 O ANISOU 4667 OE1 GLU B 239 7665 6562 5531 469 -1012 -293 O ATOM 4668 OE2 GLU B 239 -20.093 10.589 -22.737 1.00 46.84 O ANISOU 4668 OE2 GLU B 239 7094 5832 4871 480 -847 -370 O ATOM 4669 N GLN B 240 -22.790 13.059 -17.739 1.00 32.64 N ANISOU 4669 N GLN B 240 4655 4058 3690 261 -818 -117 N ATOM 4670 CA GLN B 240 -23.425 13.959 -16.778 1.00 33.16 C ANISOU 4670 CA GLN B 240 4600 4143 3856 256 -790 -53 C ATOM 4671 C GLN B 240 -22.625 15.274 -16.664 1.00 32.90 C ANISOU 4671 C GLN B 240 4606 4096 3797 313 -662 13 C ATOM 4672 O GLN B 240 -23.194 16.364 -16.632 1.00 32.35 O ANISOU 4672 O GLN B 240 4514 4043 3736 362 -660 72 O ATOM 4673 CB GLN B 240 -23.521 13.274 -15.406 1.00 34.95 C ANISOU 4673 CB GLN B 240 4725 4344 4211 170 -763 -68 C ATOM 4674 CG GLN B 240 -24.493 12.072 -15.338 1.00 42.67 C ANISOU 4674 CG GLN B 240 5648 5326 5237 87 -884 -118 C ATOM 4675 CD GLN B 240 -24.503 11.380 -13.964 1.00 45.41 C ANISOU 4675 CD GLN B 240 5916 5638 5701 1 -841 -120 C ATOM 4676 OE1 GLN B 240 -23.457 11.016 -13.422 1.00 42.53 O ANISOU 4676 OE1 GLN B 240 5597 5219 5345 -5 -756 -130 O ATOM 4677 NE2 GLN B 240 -25.694 11.204 -13.401 1.00 44.92 N ANISOU 4677 NE2 GLN B 240 5728 5615 5723 -63 -898 -104 N ATOM 4678 N TRP B 241 -21.301 15.159 -16.613 1.00 31.81 N ANISOU 4678 N TRP B 241 4529 3928 3630 305 -557 3 N ATOM 4679 CA TRP B 241 -20.414 16.324 -16.544 1.00 30.36 C ANISOU 4679 CA TRP B 241 4386 3730 3422 330 -433 60 C ATOM 4680 C TRP B 241 -20.681 17.232 -17.741 1.00 31.70 C ANISOU 4680 C TRP B 241 4652 3913 3480 404 -453 110 C ATOM 4681 O TRP B 241 -20.901 18.429 -17.584 1.00 32.49 O ANISOU 4681 O TRP B 241 4761 3993 3590 434 -415 177 O ATOM 4682 CB TRP B 241 -18.962 15.853 -16.544 1.00 30.52 C ANISOU 4682 CB TRP B 241 4443 3743 3412 310 -335 33 C ATOM 4683 CG TRP B 241 -17.901 16.880 -16.232 1.00 29.73 C ANISOU 4683 CG TRP B 241 4353 3634 3311 295 -202 83 C ATOM 4684 CD1 TRP B 241 -17.802 18.157 -16.711 1.00 29.71 C ANISOU 4684 CD1 TRP B 241 4414 3618 3257 317 -149 151 C ATOM 4685 CD2 TRP B 241 -16.743 16.666 -15.430 1.00 31.37 C ANISOU 4685 CD2 TRP B 241 4510 3845 3563 248 -110 69 C ATOM 4686 NE1 TRP B 241 -16.668 18.758 -16.226 1.00 33.53 N ANISOU 4686 NE1 TRP B 241 4888 4092 3760 266 -28 177 N ATOM 4687 CE2 TRP B 241 -15.998 17.864 -15.436 1.00 34.53 C ANISOU 4687 CE2 TRP B 241 4934 4240 3945 225 -6 126 C ATOM 4688 CE3 TRP B 241 -16.263 15.577 -14.698 1.00 29.53 C ANISOU 4688 CE3 TRP B 241 4217 3620 3384 224 -110 18 C ATOM 4689 CZ2 TRP B 241 -14.803 18.005 -14.731 1.00 32.82 C ANISOU 4689 CZ2 TRP B 241 4663 4041 3765 168 89 125 C ATOM 4690 CZ3 TRP B 241 -15.078 15.721 -13.995 1.00 29.49 C ANISOU 4690 CZ3 TRP B 241 4161 3635 3410 190 -16 23 C ATOM 4691 CH2 TRP B 241 -14.363 16.924 -14.017 1.00 31.39 C ANISOU 4691 CH2 TRP B 241 4407 3886 3634 157 79 73 C ATOM 4692 N LYS B 242 -20.673 16.635 -18.929 1.00 31.06 N ANISOU 4692 N LYS B 242 4657 3859 3287 439 -514 77 N ATOM 4693 CA LYS B 242 -20.952 17.326 -20.183 1.00 33.00 C ANISOU 4693 CA LYS B 242 5010 4126 3401 516 -548 122 C ATOM 4694 C LYS B 242 -22.288 18.081 -20.172 1.00 35.84 C ANISOU 4694 C LYS B 242 5327 4503 3788 567 -645 172 C ATOM 4695 O LYS B 242 -22.353 19.235 -20.601 1.00 33.86 O ANISOU 4695 O LYS B 242 5146 4238 3480 632 -614 250 O ATOM 4696 CB LYS B 242 -20.931 16.303 -21.319 1.00 32.93 C ANISOU 4696 CB LYS B 242 5089 4150 3272 540 -629 54 C ATOM 4697 CG LYS B 242 -21.479 16.767 -22.660 1.00 36.97 C ANISOU 4697 CG LYS B 242 5712 4701 3633 623 -711 85 C ATOM 4698 CD LYS B 242 -22.194 15.601 -23.340 1.00 41.26 C ANISOU 4698 CD LYS B 242 6278 5280 4118 620 -872 -5 C ATOM 4699 CE LYS B 242 -22.694 15.954 -24.702 1.00 43.75 C ANISOU 4699 CE LYS B 242 6710 5646 4265 704 -967 16 C ATOM 4700 NZ LYS B 242 -23.434 14.815 -25.307 1.00 47.30 N ANISOU 4700 NZ LYS B 242 7179 6131 4662 683 -1141 -84 N ATOM 4701 N ASN B 243 -23.338 17.427 -19.670 1.00 36.01 N ANISOU 4701 N ASN B 243 5230 4556 3895 537 -756 131 N ATOM 4702 CA ASN B 243 -24.701 17.966 -19.734 1.00 36.57 C ANISOU 4702 CA ASN B 243 5232 4675 3990 594 -865 169 C ATOM 4703 C ASN B 243 -25.051 18.956 -18.629 1.00 36.62 C ANISOU 4703 C ASN B 243 5151 4655 4106 615 -797 227 C ATOM 4704 O ASN B 243 -26.054 19.648 -18.721 1.00 39.44 O ANISOU 4704 O ASN B 243 5466 5049 4473 696 -861 274 O ATOM 4705 CB ASN B 243 -25.717 16.818 -19.736 1.00 36.30 C ANISOU 4705 CB ASN B 243 5093 4700 3998 541 -1016 100 C ATOM 4706 CG ASN B 243 -25.675 16.009 -21.023 1.00 38.47 C ANISOU 4706 CG ASN B 243 5474 5002 4139 543 -1121 40 C ATOM 4707 OD1 ASN B 243 -25.598 14.780 -21.004 1.00 38.09 O ANISOU 4707 OD1 ASN B 243 5423 4944 4106 462 -1171 -44 O ATOM 4708 ND2 ASN B 243 -25.703 16.700 -22.144 1.00 34.17 N ANISOU 4708 ND2 ASN B 243 5043 4485 3456 640 -1153 83 N ATOM 4709 N PHE B 244 -24.211 19.026 -17.603 1.00 36.03 N ANISOU 4709 N PHE B 244 5058 4524 4109 552 -671 222 N ATOM 4710 CA PHE B 244 -24.466 19.814 -16.399 1.00 34.58 C ANISOU 4710 CA PHE B 244 4800 4309 4030 557 -602 256 C ATOM 4711 C PHE B 244 -23.737 21.158 -16.484 1.00 35.61 C ANISOU 4711 C PHE B 244 5050 4362 4118 600 -489 322 C ATOM 4712 O PHE B 244 -22.515 21.174 -16.606 1.00 34.76 O ANISOU 4712 O PHE B 244 5020 4214 3973 547 -396 318 O ATOM 4713 CB PHE B 244 -23.959 19.004 -15.198 1.00 32.89 C ANISOU 4713 CB PHE B 244 4503 4079 3913 452 -543 205 C ATOM 4714 CG PHE B 244 -24.082 19.692 -13.861 1.00 33.23 C ANISOU 4714 CG PHE B 244 4481 4091 4052 445 -463 226 C ATOM 4715 CD1 PHE B 244 -25.198 20.448 -13.530 1.00 37.91 C ANISOU 4715 CD1 PHE B 244 5013 4705 4686 522 -489 263 C ATOM 4716 CD2 PHE B 244 -23.097 19.520 -12.906 1.00 33.07 C ANISOU 4716 CD2 PHE B 244 4458 4031 4077 369 -366 203 C ATOM 4717 CE1 PHE B 244 -25.306 21.041 -12.279 1.00 36.53 C ANISOU 4717 CE1 PHE B 244 4791 4500 4588 524 -409 273 C ATOM 4718 CE2 PHE B 244 -23.198 20.105 -11.660 1.00 36.60 C ANISOU 4718 CE2 PHE B 244 4857 4451 4597 359 -299 213 C ATOM 4719 CZ PHE B 244 -24.312 20.865 -11.344 1.00 36.53 C ANISOU 4719 CZ PHE B 244 4803 4454 4622 437 -316 245 C ATOM 4720 N ASP B 245 -24.473 22.271 -16.446 1.00 37.57 N ANISOU 4720 N ASP B 245 5314 4589 4370 696 -496 383 N ATOM 4721 CA ASP B 245 -23.844 23.590 -16.261 1.00 37.99 C ANISOU 4721 CA ASP B 245 5486 4540 4408 720 -381 442 C ATOM 4722 C ASP B 245 -24.059 24.041 -14.824 1.00 36.52 C ANISOU 4722 C ASP B 245 5227 4313 4335 706 -318 431 C ATOM 4723 O ASP B 245 -25.069 24.662 -14.484 1.00 40.02 O ANISOU 4723 O ASP B 245 5633 4758 4815 803 -346 458 O ATOM 4724 CB ASP B 245 -24.350 24.642 -17.259 1.00 39.41 C ANISOU 4724 CB ASP B 245 5787 4692 4495 851 -415 525 C ATOM 4725 CG ASP B 245 -23.474 25.921 -17.271 1.00 46.00 C ANISOU 4725 CG ASP B 245 6788 5396 5294 846 -287 590 C ATOM 4726 OD1 ASP B 245 -22.784 26.217 -16.261 1.00 46.90 O ANISOU 4726 OD1 ASP B 245 6897 5444 5481 760 -184 569 O ATOM 4727 OD2 ASP B 245 -23.459 26.629 -18.305 1.00 54.01 O ANISOU 4727 OD2 ASP B 245 7946 6372 6202 921 -291 665 O ATOM 4728 N GLU B 246 -23.084 23.705 -13.993 1.00 35.73 N ANISOU 4728 N GLU B 246 5106 4186 4282 591 -234 389 N ATOM 4729 CA GLU B 246 -23.110 23.961 -12.557 1.00 36.97 C ANISOU 4729 CA GLU B 246 5201 4311 4534 556 -173 364 C ATOM 4730 C GLU B 246 -23.419 25.417 -12.237 1.00 36.56 C ANISOU 4730 C GLU B 246 5239 4166 4486 637 -119 411 C ATOM 4731 O GLU B 246 -24.294 25.701 -11.427 1.00 37.02 O ANISOU 4731 O GLU B 246 5231 4230 4603 700 -124 404 O ATOM 4732 CB GLU B 246 -21.760 23.550 -11.960 1.00 36.67 C ANISOU 4732 CB GLU B 246 5166 4254 4514 426 -92 324 C ATOM 4733 CG GLU B 246 -21.531 23.853 -10.501 1.00 43.39 C ANISOU 4733 CG GLU B 246 5979 5068 5438 375 -25 294 C ATOM 4734 CD GLU B 246 -20.170 23.348 -10.028 1.00 51.90 C ANISOU 4734 CD GLU B 246 7045 6150 6524 252 32 256 C ATOM 4735 OE1 GLU B 246 -19.985 22.115 -9.948 1.00 54.01 O ANISOU 4735 OE1 GLU B 246 7229 6485 6806 213 -4 220 O ATOM 4736 OE2 GLU B 246 -19.282 24.179 -9.736 1.00 60.73 O ANISOU 4736 OE2 GLU B 246 8237 7204 7634 195 109 264 O ATOM 4737 N ARG B 247 -22.719 26.329 -12.900 1.00 36.13 N ANISOU 4737 N ARG B 247 5343 4021 4364 638 -64 460 N ATOM 4738 CA ARG B 247 -22.799 27.742 -12.558 1.00 37.68 C ANISOU 4738 CA ARG B 247 5664 4091 4562 694 0 501 C ATOM 4739 C ARG B 247 -24.148 28.367 -12.910 1.00 36.08 C ANISOU 4739 C ARG B 247 5475 3886 4347 875 -64 550 C ATOM 4740 O ARG B 247 -24.581 29.309 -12.257 1.00 36.61 O ANISOU 4740 O ARG B 247 5595 3871 4446 954 -24 562 O ATOM 4741 CB ARG B 247 -21.641 28.508 -13.203 1.00 37.73 C ANISOU 4741 CB ARG B 247 5841 3994 4500 623 81 547 C ATOM 4742 CG ARG B 247 -20.302 28.101 -12.618 1.00 41.28 C ANISOU 4742 CG ARG B 247 6259 4448 4977 449 156 498 C ATOM 4743 CD ARG B 247 -19.115 28.550 -13.438 1.00 47.41 C ANISOU 4743 CD ARG B 247 7157 5175 5683 360 231 544 C ATOM 4744 NE ARG B 247 -17.870 28.327 -12.704 1.00 52.60 N ANISOU 4744 NE ARG B 247 7765 5842 6380 198 304 497 N ATOM 4745 CZ ARG B 247 -17.222 29.242 -11.979 1.00 57.00 C ANISOU 4745 CZ ARG B 247 8394 6297 6968 102 379 492 C ATOM 4746 NH1 ARG B 247 -17.669 30.491 -11.874 1.00 58.46 N ANISOU 4746 NH1 ARG B 247 8728 6338 7148 152 405 532 N ATOM 4747 NH2 ARG B 247 -16.102 28.904 -11.351 1.00 60.22 N ANISOU 4747 NH2 ARG B 247 8727 6745 7408 -43 425 445 N ATOM 4748 N LYS B 248 -24.802 27.827 -13.931 1.00 35.58 N ANISOU 4748 N LYS B 248 5366 3919 4235 948 -168 574 N ATOM 4749 CA LYS B 248 -26.124 28.280 -14.344 1.00 35.63 C ANISOU 4749 CA LYS B 248 5351 3960 4226 1128 -252 622 C ATOM 4750 C LYS B 248 -27.253 27.669 -13.512 1.00 33.60 C ANISOU 4750 C LYS B 248 4885 3820 4061 1172 -308 577 C ATOM 4751 O LYS B 248 -28.304 28.280 -13.347 1.00 35.13 O ANISOU 4751 O LYS B 248 5043 4031 4276 1325 -337 607 O ATOM 4752 CB LYS B 248 -26.364 27.943 -15.815 1.00 35.34 C ANISOU 4752 CB LYS B 248 5348 3993 4087 1182 -355 664 C ATOM 4753 CG LYS B 248 -25.482 28.703 -16.792 1.00 43.43 C ANISOU 4753 CG LYS B 248 6592 4911 5001 1177 -300 734 C ATOM 4754 CD LYS B 248 -25.948 28.452 -18.231 1.00 46.98 C ANISOU 4754 CD LYS B 248 7079 5439 5331 1267 -415 781 C ATOM 4755 CE LYS B 248 -25.270 29.378 -19.234 1.00 51.05 C ANISOU 4755 CE LYS B 248 7830 5846 5722 1295 -357 874 C ATOM 4756 NZ LYS B 248 -23.849 29.022 -19.458 1.00 46.53 N ANISOU 4756 NZ LYS B 248 7324 5245 5112 1128 -256 855 N ATOM 4757 N GLU B 249 -27.040 26.471 -12.990 1.00 33.57 N ANISOU 4757 N GLU B 249 4744 3900 4112 1042 -319 509 N ATOM 4758 CA GLU B 249 -28.125 25.691 -12.400 1.00 34.88 C ANISOU 4758 CA GLU B 249 4703 4195 4355 1058 -383 476 C ATOM 4759 C GLU B 249 -28.167 25.683 -10.877 1.00 34.77 C ANISOU 4759 C GLU B 249 4610 4170 4431 1016 -294 434 C ATOM 4760 O GLU B 249 -29.226 25.483 -10.309 1.00 36.18 O ANISOU 4760 O GLU B 249 4637 4441 4669 1073 -318 428 O ATOM 4761 CB GLU B 249 -28.052 24.241 -12.890 1.00 33.94 C ANISOU 4761 CB GLU B 249 4487 4178 4232 945 -470 433 C ATOM 4762 CG GLU B 249 -28.389 24.058 -14.353 1.00 38.01 C ANISOU 4762 CG GLU B 249 5038 4747 4657 1001 -590 461 C ATOM 4763 CD GLU B 249 -28.171 22.627 -14.815 1.00 46.30 C ANISOU 4763 CD GLU B 249 6029 5868 5694 879 -667 403 C ATOM 4764 OE1 GLU B 249 -28.653 21.699 -14.129 1.00 44.11 O ANISOU 4764 OE1 GLU B 249 5599 5660 5498 803 -697 357 O ATOM 4765 OE2 GLU B 249 -27.513 22.428 -15.860 1.00 51.98 O ANISOU 4765 OE2 GLU B 249 6867 6568 6317 860 -692 404 O ATOM 4766 N MET B 250 -27.034 25.882 -10.211 1.00 36.35 N ANISOU 4766 N MET B 250 4903 4272 4635 915 -194 406 N ATOM 4767 CA MET B 250 -26.960 25.541 -8.791 1.00 35.17 C ANISOU 4767 CA MET B 250 4670 4136 4556 846 -127 356 C ATOM 4768 C MET B 250 -27.770 26.434 -7.856 1.00 35.90 C ANISOU 4768 C MET B 250 4747 4208 4685 965 -70 360 C ATOM 4769 O MET B 250 -28.284 25.948 -6.851 1.00 33.85 O ANISOU 4769 O MET B 250 4358 4022 4481 949 -46 330 O ATOM 4770 CB MET B 250 -25.508 25.426 -8.314 1.00 35.62 C ANISOU 4770 CB MET B 250 4816 4115 4604 702 -52 319 C ATOM 4771 CG MET B 250 -24.845 24.100 -8.681 1.00 36.80 C ANISOU 4771 CG MET B 250 4908 4326 4749 578 -95 291 C ATOM 4772 SD MET B 250 -25.842 22.646 -8.345 1.00 39.51 S ANISOU 4772 SD MET B 250 5052 4805 5153 547 -173 265 S ATOM 4773 CE MET B 250 -26.119 22.791 -6.581 1.00 37.92 C ANISOU 4773 CE MET B 250 4781 4608 5017 534 -86 240 C ATOM 4774 N ALA B 251 -27.898 27.721 -8.178 1.00 36.46 N ANISOU 4774 N ALA B 251 4958 4178 4719 1091 -42 399 N ATOM 4775 CA ALA B 251 -28.725 28.625 -7.368 1.00 38.25 C ANISOU 4775 CA ALA B 251 5186 4377 4971 1238 13 400 C ATOM 4776 C ALA B 251 -30.159 28.097 -7.272 1.00 38.93 C ANISOU 4776 C ALA B 251 5054 4633 5105 1342 -46 413 C ATOM 4777 O ALA B 251 -30.711 27.996 -6.182 1.00 38.05 O ANISOU 4777 O ALA B 251 4837 4579 5041 1368 10 384 O ATOM 4778 CB ALA B 251 -28.716 30.053 -7.941 1.00 38.31 C ANISOU 4778 CB ALA B 251 5395 4236 4924 1377 36 451 C ATOM 4779 N THR B 252 -30.745 27.752 -8.417 1.00 40.10 N ANISOU 4779 N THR B 252 5131 4871 5235 1394 -159 455 N ATOM 4780 CA THR B 252 -32.097 27.192 -8.456 1.00 42.45 C ANISOU 4780 CA THR B 252 5199 5350 5579 1470 -235 469 C ATOM 4781 C THR B 252 -32.176 25.859 -7.710 1.00 40.81 C ANISOU 4781 C THR B 252 4814 5255 5436 1306 -234 422 C ATOM 4782 O THR B 252 -33.097 25.637 -6.930 1.00 41.67 O ANISOU 4782 O THR B 252 4752 5476 5604 1344 -209 417 O ATOM 4783 CB THR B 252 -32.582 26.994 -9.908 1.00 43.38 C ANISOU 4783 CB THR B 252 5287 5545 5652 1529 -378 515 C ATOM 4784 OG1 THR B 252 -32.660 28.266 -10.556 1.00 50.35 O ANISOU 4784 OG1 THR B 252 6332 6328 6471 1706 -379 573 O ATOM 4785 CG2 THR B 252 -33.956 26.331 -9.952 1.00 42.29 C ANISOU 4785 CG2 THR B 252 4887 5613 5569 1576 -472 523 C ATOM 4786 N ILE B 253 -31.211 24.976 -7.943 1.00 37.83 N ANISOU 4786 N ILE B 253 4481 4848 5047 1129 -254 392 N ATOM 4787 CA ILE B 253 -31.222 23.676 -7.280 1.00 37.14 C ANISOU 4787 CA ILE B 253 4254 4843 5014 975 -257 354 C ATOM 4788 C ILE B 253 -31.097 23.818 -5.751 1.00 36.39 C ANISOU 4788 C ILE B 253 4143 4727 4957 951 -131 326 C ATOM 4789 O ILE B 253 -31.871 23.207 -5.021 1.00 37.94 O ANISOU 4789 O ILE B 253 4173 5035 5209 925 -116 323 O ATOM 4790 CB ILE B 253 -30.151 22.734 -7.857 1.00 36.51 C ANISOU 4790 CB ILE B 253 4246 4721 4904 816 -300 326 C ATOM 4791 CG1 ILE B 253 -30.512 22.390 -9.309 1.00 35.87 C ANISOU 4791 CG1 ILE B 253 4152 4694 4781 837 -434 345 C ATOM 4792 CG2 ILE B 253 -30.031 21.458 -7.006 1.00 31.77 C ANISOU 4792 CG2 ILE B 253 3542 4170 4359 663 -285 290 C ATOM 4793 CD1 ILE B 253 -29.497 21.526 -10.028 1.00 30.08 C ANISOU 4793 CD1 ILE B 253 3507 3919 4003 712 -475 315 C ATOM 4794 N LEU B 254 -30.168 24.655 -5.282 1.00 34.61 N ANISOU 4794 N LEU B 254 4090 4365 4697 958 -43 308 N ATOM 4795 CA LEU B 254 -30.019 24.957 -3.849 1.00 34.08 C ANISOU 4795 CA LEU B 254 4039 4267 4644 951 72 275 C ATOM 4796 C LEU B 254 -31.289 25.549 -3.224 1.00 38.31 C ANISOU 4796 C LEU B 254 4474 4877 5207 1112 121 290 C ATOM 4797 O LEU B 254 -31.600 25.277 -2.065 1.00 39.00 O ANISOU 4797 O LEU B 254 4481 5020 5317 1093 197 269 O ATOM 4798 CB LEU B 254 -28.831 25.904 -3.597 1.00 32.61 C ANISOU 4798 CB LEU B 254 4070 3914 4408 933 141 249 C ATOM 4799 CG LEU B 254 -27.426 25.330 -3.832 1.00 33.20 C ANISOU 4799 CG LEU B 254 4226 3931 4459 765 126 225 C ATOM 4800 CD1 LEU B 254 -26.379 26.443 -3.864 1.00 34.43 C ANISOU 4800 CD1 LEU B 254 4584 3932 4568 754 180 212 C ATOM 4801 CD2 LEU B 254 -27.071 24.282 -2.773 1.00 31.88 C ANISOU 4801 CD2 LEU B 254 3976 3819 4317 638 154 189 C ATOM 4802 N SER B 255 -32.028 26.357 -3.976 1.00 42.28 N ANISOU 4802 N SER B 255 4979 5386 5699 1281 83 329 N ATOM 4803 CA SER B 255 -33.293 26.881 -3.461 1.00 45.99 C ANISOU 4803 CA SER B 255 5328 5948 6196 1458 127 346 C ATOM 4804 C SER B 255 -34.326 25.757 -3.289 1.00 46.05 C ANISOU 4804 C SER B 255 5063 6165 6270 1408 86 363 C ATOM 4805 O SER B 255 -35.201 25.856 -2.444 1.00 48.61 O ANISOU 4805 O SER B 255 5254 6591 6625 1489 159 366 O ATOM 4806 CB SER B 255 -33.839 28.010 -4.341 1.00 46.98 C ANISOU 4806 CB SER B 255 5523 6034 6292 1671 87 391 C ATOM 4807 OG SER B 255 -34.235 27.533 -5.614 1.00 52.59 O ANISOU 4807 OG SER B 255 6145 6833 7003 1671 -50 435 O ATOM 4808 N LYS B 256 -34.206 24.688 -4.073 1.00 45.59 N ANISOU 4808 N LYS B 256 4929 6165 6229 1267 -24 371 N ATOM 4809 CA LYS B 256 -35.112 23.537 -3.962 1.00 45.70 C ANISOU 4809 CA LYS B 256 4698 6359 6307 1178 -73 384 C ATOM 4810 C LYS B 256 -34.796 22.577 -2.804 1.00 44.33 C ANISOU 4810 C LYS B 256 4476 6203 6164 1008 6 358 C ATOM 4811 O LYS B 256 -35.667 21.807 -2.406 1.00 44.40 O ANISOU 4811 O LYS B 256 4283 6357 6230 949 6 376 O ATOM 4812 CB LYS B 256 -35.128 22.735 -5.263 1.00 44.95 C ANISOU 4812 CB LYS B 256 4562 6306 6212 1087 -229 394 C ATOM 4813 CG LYS B 256 -35.837 23.412 -6.418 1.00 47.55 C ANISOU 4813 CG LYS B 256 4863 6687 6516 1250 -333 433 C ATOM 4814 CD LYS B 256 -36.011 22.419 -7.566 1.00 51.82 C ANISOU 4814 CD LYS B 256 5331 7303 7055 1138 -495 432 C ATOM 4815 CE LYS B 256 -36.630 23.057 -8.791 1.00 53.19 C ANISOU 4815 CE LYS B 256 5494 7530 7184 1298 -616 472 C ATOM 4816 NZ LYS B 256 -36.671 22.095 -9.920 1.00 53.72 N ANISOU 4816 NZ LYS B 256 5527 7656 7229 1179 -777 458 N ATOM 4817 N MET B 257 -33.563 22.599 -2.291 1.00 42.71 N ANISOU 4817 N MET B 257 4449 5858 5919 925 66 322 N ATOM 4818 CA MET B 257 -33.181 21.769 -1.141 1.00 43.46 C ANISOU 4818 CA MET B 257 4525 5960 6027 784 140 303 C ATOM 4819 C MET B 257 -34.112 22.003 0.031 1.00 44.90 C ANISOU 4819 C MET B 257 4583 6246 6230 859 253 315 C ATOM 4820 O MET B 257 -34.442 23.151 0.321 1.00 48.67 O ANISOU 4820 O MET B 257 5103 6706 6684 1031 321 310 O ATOM 4821 CB MET B 257 -31.797 22.137 -0.611 1.00 41.82 C ANISOU 4821 CB MET B 257 4528 5599 5763 739 200 261 C ATOM 4822 CG MET B 257 -30.633 21.518 -1.290 1.00 43.14 C ANISOU 4822 CG MET B 257 4800 5681 5910 610 129 244 C ATOM 4823 SD MET B 257 -29.157 21.652 -0.258 1.00 42.32 S ANISOU 4823 SD MET B 257 4866 5460 5756 528 210 198 S ATOM 4824 CE MET B 257 -29.248 23.329 0.388 1.00 33.59 C ANISOU 4824 CE MET B 257 3876 4278 4607 682 309 175 C ATOM 4825 N PRO B 258 -34.483 20.931 0.749 1.00 45.26 N ANISOU 4825 N PRO B 258 4496 6388 6313 733 284 331 N ATOM 4826 CA PRO B 258 -35.246 21.135 1.978 1.00 48.14 C ANISOU 4826 CA PRO B 258 4758 6850 6682 795 416 344 C ATOM 4827 C PRO B 258 -34.381 21.840 3.018 1.00 49.32 C ANISOU 4827 C PRO B 258 5101 6883 6757 837 527 299 C ATOM 4828 O PRO B 258 -33.207 21.499 3.169 1.00 47.45 O ANISOU 4828 O PRO B 258 5011 6533 6484 723 509 270 O ATOM 4829 CB PRO B 258 -35.588 19.708 2.418 1.00 46.74 C ANISOU 4829 CB PRO B 258 4437 6771 6552 608 416 377 C ATOM 4830 CG PRO B 258 -34.498 18.882 1.873 1.00 45.93 C ANISOU 4830 CG PRO B 258 4459 6552 6441 452 323 358 C ATOM 4831 CD PRO B 258 -34.083 19.523 0.577 1.00 42.67 C ANISOU 4831 CD PRO B 258 4142 6059 6012 528 218 336 C ATOM 4832 N LYS B 259 -34.950 22.828 3.704 1.00 54.57 N ANISOU 4832 N LYS B 259 5764 7575 7393 1006 634 288 N ATOM 4833 CA LYS B 259 -34.204 23.607 4.696 1.00 57.41 C ANISOU 4833 CA LYS B 259 6320 7820 7672 1056 734 233 C ATOM 4834 C LYS B 259 -34.601 23.208 6.120 1.00 59.22 C ANISOU 4834 C LYS B 259 6482 8146 7872 1033 865 237 C ATOM 4835 O LYS B 259 -35.688 22.667 6.335 1.00 59.08 O ANISOU 4835 O LYS B 259 6253 8295 7902 1035 905 287 O ATOM 4836 CB LYS B 259 -34.429 25.112 4.492 1.00 59.75 C ANISOU 4836 CB LYS B 259 6726 8040 7937 1274 769 205 C ATOM 4837 CG LYS B 259 -34.062 25.642 3.097 1.00 59.60 C ANISOU 4837 CG LYS B 259 6797 7918 7932 1315 652 212 C ATOM 4838 CD LYS B 259 -32.633 25.283 2.675 1.00 54.81 C ANISOU 4838 CD LYS B 259 6348 7174 7302 1143 579 187 C ATOM 4839 CE LYS B 259 -32.219 26.021 1.397 1.00 54.09 C ANISOU 4839 CE LYS B 259 6381 6967 7203 1200 495 194 C ATOM 4840 NZ LYS B 259 -33.226 25.883 0.294 1.00 51.40 N ANISOU 4840 NZ LYS B 259 5887 6732 6910 1285 407 250 N ATOM 4841 N PRO B 260 -33.706 23.456 7.093 1.00 60.66 N ANISOU 4841 N PRO B 260 6843 8231 7972 1002 929 187 N ATOM 4842 CA PRO B 260 -33.974 23.188 8.507 1.00 63.66 C ANISOU 4842 CA PRO B 260 7202 8691 8296 993 1059 185 C ATOM 4843 C PRO B 260 -35.248 23.850 9.060 1.00 67.08 C ANISOU 4843 C PRO B 260 7521 9247 8720 1183 1188 194 C ATOM 4844 O PRO B 260 -35.459 25.052 8.878 1.00 70.69 O ANISOU 4844 O PRO B 260 8059 9644 9155 1369 1214 154 O ATOM 4845 CB PRO B 260 -32.740 23.756 9.209 1.00 63.29 C ANISOU 4845 CB PRO B 260 7405 8493 8150 974 1079 110 C ATOM 4846 CG PRO B 260 -31.640 23.652 8.202 1.00 62.49 C ANISOU 4846 CG PRO B 260 7405 8264 8076 871 945 96 C ATOM 4847 CD PRO B 260 -32.281 23.753 6.844 1.00 60.09 C ANISOU 4847 CD PRO B 260 6989 7986 7858 928 864 135 C ATOM 4848 N LYS B 261 -36.087 23.050 9.717 1.00 67.93 N ANISOU 4848 N LYS B 261 7443 9523 8843 1137 1271 250 N ATOM 4849 CA LYS B 261 -37.255 23.547 10.449 1.00 69.54 C ANISOU 4849 CA LYS B 261 7523 9873 9026 1307 1421 261 C ATOM 4850 C LYS B 261 -36.779 24.313 11.691 1.00 68.89 C ANISOU 4850 C LYS B 261 7652 9712 8811 1399 1545 188 C ATOM 4851 O LYS B 261 -35.879 23.851 12.395 1.00 65.14 O ANISOU 4851 O LYS B 261 7313 9171 8265 1265 1548 168 O ATOM 4852 CB LYS B 261 -38.143 22.362 10.866 1.00 71.23 C ANISOU 4852 CB LYS B 261 7489 10288 9288 1187 1482 348 C ATOM 4853 CG LYS B 261 -39.365 22.694 11.736 1.00 75.77 C ANISOU 4853 CG LYS B 261 7902 11051 9838 1338 1661 373 C ATOM 4854 CD LYS B 261 -39.757 21.508 12.626 1.00 77.20 C ANISOU 4854 CD LYS B 261 7946 11374 10012 1169 1759 447 C ATOM 4855 CE LYS B 261 -40.796 21.891 13.671 1.00 81.85 C ANISOU 4855 CE LYS B 261 8411 12144 10546 1320 1966 466 C ATOM 4856 NZ LYS B 261 -41.030 20.807 14.682 1.00 80.23 N ANISOU 4856 NZ LYS B 261 8125 12055 10304 1152 2081 541 N ATOM 4857 N PRO B 262 -37.386 25.483 11.972 1.00 71.32 N ANISOU 4857 N PRO B 262 7992 10028 9077 1637 1643 145 N ATOM 4858 CA PRO B 262 -37.002 26.221 13.170 1.00 71.58 C ANISOU 4858 CA PRO B 262 8237 9987 8974 1729 1762 65 C ATOM 4859 C PRO B 262 -37.663 25.626 14.412 1.00 72.10 C ANISOU 4859 C PRO B 262 8187 10230 8976 1720 1923 101 C ATOM 4860 O PRO B 262 -38.620 24.860 14.286 1.00 71.24 O ANISOU 4860 O PRO B 262 7813 10311 8944 1681 1961 190 O ATOM 4861 CB PRO B 262 -37.554 27.619 12.897 1.00 73.62 C ANISOU 4861 CB PRO B 262 8559 10193 9222 2001 1808 14 C ATOM 4862 CG PRO B 262 -38.790 27.369 12.098 1.00 74.70 C ANISOU 4862 CG PRO B 262 8399 10508 9475 2086 1796 98 C ATOM 4863 CD PRO B 262 -38.525 26.122 11.282 1.00 72.72 C ANISOU 4863 CD PRO B 262 8007 10300 9324 1841 1655 171 C ATOM 4864 N PRO B 263 -37.156 25.964 15.609 1.00 72.50 N ANISOU 4864 N PRO B 263 8438 10226 8885 1744 2018 34 N ATOM 4865 CA PRO B 263 -37.880 25.590 16.820 1.00 74.69 C ANISOU 4865 CA PRO B 263 8623 10676 9080 1778 2197 65 C ATOM 4866 C PRO B 263 -39.321 26.104 16.776 1.00 77.51 C ANISOU 4866 C PRO B 263 8772 11204 9475 2004 2328 93 C ATOM 4867 O PRO B 263 -39.543 27.255 16.409 1.00 78.82 O ANISOU 4867 O PRO B 263 9014 11293 9640 2218 2333 31 O ATOM 4868 CB PRO B 263 -37.086 26.283 17.927 1.00 74.52 C ANISOU 4868 CB PRO B 263 8900 10531 8884 1831 2259 -43 C ATOM 4869 CG PRO B 263 -35.702 26.351 17.401 1.00 73.31 C ANISOU 4869 CG PRO B 263 8945 10169 8738 1689 2084 -95 C ATOM 4870 CD PRO B 263 -35.831 26.534 15.911 1.00 72.06 C ANISOU 4870 CD PRO B 263 8689 9958 8733 1700 1955 -66 C ATOM 4871 N PRO B 264 -40.298 25.252 17.126 1.00 79.92 N ANISOU 4871 N PRO B 264 8811 11740 9816 1956 2434 191 N ATOM 4872 CA PRO B 264 -41.701 25.651 17.046 1.00 83.20 C ANISOU 4872 CA PRO B 264 8979 12354 10280 2161 2556 228 C ATOM 4873 C PRO B 264 -42.108 26.600 18.176 1.00 85.40 C ANISOU 4873 C PRO B 264 9367 12670 10411 2410 2759 157 C ATOM 4874 O PRO B 264 -42.917 27.506 17.960 1.00 88.00 O ANISOU 4874 O PRO B 264 9623 13056 10758 2671 2827 133 O ATOM 4875 CB PRO B 264 -42.444 24.320 17.169 1.00 84.22 C ANISOU 4875 CB PRO B 264 8807 12709 10484 1974 2603 356 C ATOM 4876 CG PRO B 264 -41.548 23.475 18.000 1.00 82.44 C ANISOU 4876 CG PRO B 264 8744 12414 10165 1756 2611 368 C ATOM 4877 CD PRO B 264 -40.145 23.884 17.655 1.00 79.57 C ANISOU 4877 CD PRO B 264 8685 11784 9763 1709 2451 276 C TER 4878 PRO B 264 HETATM 4879 C1 BAX A 465 -3.479 3.317 22.868 1.00 40.55 C HETATM 4880 C2 BAX A 465 -4.004 4.602 22.970 1.00 33.62 C HETATM 4881 C3 BAX A 465 -3.696 5.545 22.001 1.00 36.59 C HETATM 4882 C4 BAX A 465 -2.871 5.220 20.944 1.00 36.07 C HETATM 4883 C13 BAX A 465 -4.966 4.410 25.294 1.00 32.07 C HETATM 4884 C16 BAX A 465 -6.176 4.577 27.475 1.00 33.31 C HETATM 4885 C17 BAX A 465 -6.617 5.542 28.366 1.00 34.96 C HETATM 4886 C18 BAX A 465 -6.925 5.206 29.671 1.00 35.40 C HETATM 4887 C19 BAX A 465 -6.787 3.893 30.096 1.00 41.04 C HETATM 4888 C20 BAX A 465 -6.346 2.919 29.207 1.00 36.26 C HETATM 4889 C21 BAX A 465 -6.049 3.263 27.902 1.00 37.16 C HETATM 4890 O22 BAX A 465 -7.100 3.609 31.390 1.00 39.20 O HETATM 4891 C24 BAX A 465 -7.965 1.355 31.541 1.00 38.64 C HETATM 4892 C25 BAX A 465 -8.009 0.159 32.241 1.00 39.14 C HETATM 4893 C27 BAX A 465 -6.495 1.063 33.886 1.00 47.73 C HETATM 4894 C28 BAX A 465 -6.458 2.255 33.185 1.00 42.39 C HETATM 4895 N30 BAX A 465 -5.796 -0.177 35.938 1.00 56.86 N HETATM 4896 C31 BAX A 465 -5.015 -0.354 37.173 1.00 60.17 C HETATM 4897 C5 BAX A 465 -2.359 3.935 20.848 1.00 40.45 C HETATM 4898 C6 BAX A 465 -2.657 2.974 21.801 1.00 40.51 C HETATM 4899 C7 BAX A 465 -2.063 1.578 21.678 1.00 40.59 C HETATM 4900 F8 BAX A 465 -2.512 0.720 22.618 1.00 39.99 F HETATM 4901 F9 BAX A 465 -2.357 1.029 20.487 1.00 40.31 F HETATM 4902 F10 BAX A 465 -0.718 1.698 21.789 1.00 41.80 F HETATM 4903 CL11 BAX A 465 -1.338 3.559 19.525 1.00 48.55 CL HETATM 4904 N12 BAX A 465 -4.854 4.978 24.037 1.00 34.98 N HETATM 4905 N14 BAX A 465 -5.889 4.979 26.147 1.00 33.25 N HETATM 4906 O15 BAX A 465 -4.304 3.460 25.638 1.00 32.89 O HETATM 4907 C23 BAX A 465 -7.187 2.399 32.019 1.00 41.51 C HETATM 4908 N26 BAX A 465 -7.269 0.013 33.406 1.00 43.02 N HETATM 4909 C29 BAX A 465 -5.696 0.936 35.126 1.00 52.29 C HETATM 4910 O32 BAX A 465 -4.929 1.825 35.422 1.00 53.65 O HETATM 4911 C1 EDO A 466 21.663 6.046 12.981 1.00 51.27 C HETATM 4912 O1 EDO A 466 21.441 6.668 14.253 1.00 48.78 O HETATM 4913 C2 EDO A 466 21.194 4.599 13.061 1.00 52.00 C HETATM 4914 O2 EDO A 466 22.038 3.652 12.394 1.00 49.82 O HETATM 4915 C1 EDO A 467 0.904 -17.059 23.926 1.00 71.31 C HETATM 4916 O1 EDO A 467 0.648 -15.852 24.652 1.00 68.07 O HETATM 4917 C2 EDO A 467 0.622 -18.258 24.824 1.00 71.49 C HETATM 4918 O2 EDO A 467 0.712 -19.487 24.094 1.00 73.55 O HETATM 4919 C1 EDO A 468 17.989 -15.696 33.463 1.00 68.86 C HETATM 4920 O1 EDO A 468 16.626 -15.672 33.906 1.00 69.47 O HETATM 4921 C2 EDO A 468 18.841 -16.442 34.487 1.00 68.17 C HETATM 4922 O2 EDO A 468 20.162 -16.682 33.992 1.00 64.72 O HETATM 4923 C1 EDO A 469 -9.379 -8.478 20.485 1.00 69.78 C HETATM 4924 O1 EDO A 469 -9.126 -8.543 21.895 1.00 71.42 O HETATM 4925 C2 EDO A 469 -9.227 -9.868 19.870 1.00 69.70 C HETATM 4926 O2 EDO A 469 -8.885 -9.786 18.479 1.00 67.66 O HETATM 4927 C1 EDO B 284 -20.283 14.822 -1.771 1.00 46.13 C HETATM 4928 O1 EDO B 284 -19.147 14.576 -2.609 1.00 49.12 O HETATM 4929 C2 EDO B 284 -21.503 14.153 -2.385 1.00 45.73 C HETATM 4930 O2 EDO B 284 -22.638 14.158 -1.505 1.00 55.68 O HETATM 4931 C1 EDO B 285 -33.721 15.275 8.931 1.00 64.35 C HETATM 4932 O1 EDO B 285 -34.421 15.854 10.048 1.00 70.24 O HETATM 4933 C2 EDO B 285 -33.036 13.961 9.319 1.00 57.07 C HETATM 4934 O2 EDO B 285 -32.926 13.051 8.204 1.00 49.26 O HETATM 4935 C1 GOL B 286 -17.121 22.018 -13.534 1.00 74.58 C HETATM 4936 O1 GOL B 286 -15.760 21.731 -13.782 1.00 73.97 O HETATM 4937 C2 GOL B 286 -17.908 20.722 -13.323 1.00 72.86 C HETATM 4938 O2 GOL B 286 -18.094 20.489 -11.947 1.00 69.46 O HETATM 4939 C3 GOL B 286 -19.280 20.776 -14.000 1.00 74.43 C HETATM 4940 O3 GOL B 286 -19.874 19.498 -14.024 1.00 68.52 O HETATM 4941 C1 EDO B 287 -4.305 20.081 -3.564 1.00 62.44 C HETATM 4942 O1 EDO B 287 -4.756 20.908 -2.488 1.00 60.99 O HETATM 4943 C2 EDO B 287 -5.225 18.874 -3.681 1.00 61.50 C HETATM 4944 O2 EDO B 287 -4.729 17.953 -4.657 1.00 63.70 O HETATM 4945 C1 EDO B 288 -23.074 1.626 11.264 1.00 87.70 C HETATM 4946 O1 EDO B 288 -22.341 1.986 12.441 1.00 91.27 O HETATM 4947 C2 EDO B 288 -22.709 2.583 10.136 1.00 85.47 C HETATM 4948 O2 EDO B 288 -23.380 2.230 8.918 1.00 82.21 O HETATM 4949 C1 EDO B 289 -24.015 32.935 16.667 1.00 92.21 C HETATM 4950 O1 EDO B 289 -22.777 32.707 17.349 1.00 91.67 O HETATM 4951 C2 EDO B 289 -25.048 31.902 17.112 1.00 91.77 C HETATM 4952 O2 EDO B 289 -26.080 31.735 16.128 1.00 91.37 O HETATM 4953 C1 EDO B 290 -29.367 9.857 -7.915 1.00 62.09 C HETATM 4954 O1 EDO B 290 -29.358 11.261 -7.659 1.00 52.72 O HETATM 4955 C2 EDO B 290 -29.947 9.129 -6.703 1.00 62.32 C HETATM 4956 O2 EDO B 290 -31.330 8.783 -6.874 1.00 67.08 O HETATM 4957 C1 EDO B 291 -5.112 3.801 5.739 1.00 56.93 C HETATM 4958 O1 EDO B 291 -3.709 3.864 5.457 1.00 57.87 O HETATM 4959 C2 EDO B 291 -5.699 5.201 5.652 1.00 55.57 C HETATM 4960 O2 EDO B 291 -5.553 5.715 4.320 1.00 60.95 O HETATM 4961 O HOH A 470 8.439 4.661 18.450 1.00 23.95 O HETATM 4962 O HOH A 471 15.272 4.882 15.599 1.00 26.05 O HETATM 4963 O HOH A 472 14.205 -0.779 32.637 1.00 22.68 O HETATM 4964 O HOH A 473 16.904 3.864 27.940 1.00 25.23 O HETATM 4965 O HOH A 474 12.841 4.002 23.469 1.00 26.17 O HETATM 4966 O HOH A 475 -11.428 1.976 8.545 1.00 10.40 O HETATM 4967 O HOH A 476 -18.625 3.997 20.240 1.00 32.36 O HETATM 4968 O HOH A 477 -21.998 6.375 22.333 1.00 29.77 O HETATM 4969 O HOH A 478 19.210 -20.553 28.465 1.00 21.71 O HETATM 4970 O HOH A 479 12.954 1.035 12.939 1.00 22.31 O HETATM 4971 O HOH A 480 0.472 -13.176 22.930 1.00 21.88 O HETATM 4972 O HOH A 481 -1.356 -20.919 27.368 1.00 43.24 O HETATM 4973 O HOH A 482 -23.449 11.793 25.643 1.00 25.98 O HETATM 4974 O HOH A 483 9.033 2.541 35.472 1.00 29.46 O HETATM 4975 O HOH A 484 17.008 -18.321 29.367 1.00 28.52 O HETATM 4976 O HOH A 485 6.531 -4.316 11.353 1.00 27.66 O HETATM 4977 O HOH A 486 11.441 6.947 29.279 1.00 28.21 O HETATM 4978 O HOH A 487 -8.929 -7.044 35.110 1.00 15.93 O HETATM 4979 O HOH A 488 9.006 -4.332 15.230 1.00 23.28 O HETATM 4980 O HOH A 489 24.880 2.736 11.679 1.00 25.43 O HETATM 4981 O HOH A 490 10.429 2.474 11.636 1.00 26.71 O HETATM 4982 O HOH A 491 18.887 -14.733 20.890 1.00 23.37 O HETATM 4983 O HOH A 492 18.150 -16.566 23.022 1.00 19.61 O HETATM 4984 O HOH A 493 -2.607 -4.907 8.399 1.00 37.74 O HETATM 4985 O HOH A 494 8.296 3.369 23.090 1.00 27.16 O HETATM 4986 O HOH A 495 10.159 5.324 23.664 1.00 31.59 O HETATM 4987 O HOH A 496 27.302 -4.125 26.473 1.00 28.87 O HETATM 4988 O HOH A 497 17.871 -3.919 35.389 1.00 31.38 O HETATM 4989 O HOH A 498 -28.240 7.575 28.393 1.00 38.39 O HETATM 4990 O HOH A 499 -22.144 11.453 27.855 1.00 21.06 O HETATM 4991 O HOH A 500 -10.569 -4.722 19.789 1.00 35.88 O HETATM 4992 O HOH A 501 1.905 7.226 27.538 1.00 29.93 O HETATM 4993 O HOH A 502 15.452 1.588 32.143 1.00 20.23 O HETATM 4994 O HOH A 503 17.134 17.303 17.092 1.00 29.91 O HETATM 4995 O HOH A 504 25.164 5.249 36.618 1.00 35.69 O HETATM 4996 O HOH A 505 26.002 -5.521 24.313 1.00 32.55 O HETATM 4997 O HOH A 506 -22.775 9.415 23.259 1.00 31.04 O HETATM 4998 O HOH A 507 -4.329 19.920 18.975 1.00 30.31 O HETATM 4999 O HOH A 508 -7.982 -6.267 23.613 1.00 22.69 O HETATM 5000 O HOH A 509 -11.244 -2.881 26.824 1.00 28.28 O HETATM 5001 O HOH A 510 -7.660 -9.876 40.010 1.00 30.96 O HETATM 5002 O HOH A 511 33.005 0.767 26.732 1.00 29.17 O HETATM 5003 O HOH A 512 -20.335 -3.003 35.781 1.00 29.05 O HETATM 5004 O HOH A 513 -11.108 4.866 12.582 1.00 16.22 O HETATM 5005 O HOH A 514 3.783 -18.459 32.220 1.00 33.39 O HETATM 5006 O HOH A 515 -3.674 -6.359 11.154 1.00 43.05 O HETATM 5007 O HOH A 516 26.221 15.643 35.754 1.00 37.18 O HETATM 5008 O HOH A 517 28.250 -2.293 32.995 1.00 24.84 O HETATM 5009 O HOH A 518 14.208 -26.363 26.843 1.00 25.88 O HETATM 5010 O HOH A 519 -28.111 9.934 19.503 1.00 36.52 O HETATM 5011 O HOH A 520 -4.565 -20.321 33.662 1.00 37.72 O HETATM 5012 O HOH A 521 32.256 -8.032 28.906 1.00 35.53 O HETATM 5013 O HOH A 522 13.649 -20.516 29.706 1.00 26.12 O HETATM 5014 O HOH A 523 33.695 10.648 30.187 1.00 24.24 O HETATM 5015 O HOH A 524 34.941 1.884 33.063 1.00 33.96 O HETATM 5016 O HOH A 525 -2.300 7.680 9.125 1.00 31.09 O HETATM 5017 O HOH A 526 7.795 10.893 14.563 1.00 38.65 O HETATM 5018 O HOH A 527 27.165 -13.639 26.446 1.00 34.50 O HETATM 5019 O HOH A 528 -2.462 -20.019 29.932 1.00 30.56 O HETATM 5020 O HOH A 529 11.814 -1.313 39.217 1.00 43.03 O HETATM 5021 O HOH A 530 6.495 3.336 34.068 1.00 23.95 O HETATM 5022 O HOH A 531 -37.864 14.601 16.036 1.00 23.83 O HETATM 5023 O HOH A 532 5.363 6.309 34.863 1.00 40.86 O HETATM 5024 O HOH A 533 -0.622 2.383 35.166 1.00 34.99 O HETATM 5025 O HOH A 534 30.294 7.499 34.893 1.00 42.13 O HETATM 5026 O HOH A 535 -8.950 -4.315 26.791 1.00 21.42 O HETATM 5027 O HOH A 536 6.431 -25.374 29.094 1.00 30.75 O HETATM 5028 O HOH A 537 1.900 5.942 14.940 1.00 29.10 O HETATM 5029 O HOH A 538 38.732 8.060 25.816 1.00 22.57 O HETATM 5030 O HOH A 539 25.688 -14.463 36.856 1.00 36.04 O HETATM 5031 O HOH A 540 5.350 -6.400 13.031 1.00 37.29 O HETATM 5032 O HOH A 541 -8.515 -4.073 29.375 1.00 25.99 O HETATM 5033 O HOH A 542 16.260 4.000 13.267 1.00 32.71 O HETATM 5034 O HOH A 543 26.650 0.189 13.053 1.00 28.11 O HETATM 5035 O HOH A 544 28.398 -3.502 35.333 1.00 30.54 O HETATM 5036 O HOH A 545 22.717 -11.714 21.904 1.00 40.70 O HETATM 5037 O HOH A 546 23.869 -4.879 22.836 1.00 29.83 O HETATM 5038 O HOH A 547 10.090 -18.408 19.317 1.00 21.42 O HETATM 5039 O HOH A 548 15.389 7.816 15.066 1.00 43.74 O HETATM 5040 O HOH A 549 -27.602 14.820 24.784 1.00 22.54 O HETATM 5041 O HOH A 550 20.389 -7.228 17.466 1.00 33.10 O HETATM 5042 O HOH A 551 9.010 -1.848 9.128 1.00 34.75 O HETATM 5043 O HOH A 552 -7.386 -4.452 20.519 1.00 22.81 O HETATM 5044 O HOH A 553 14.027 -2.868 15.865 1.00 28.09 O HETATM 5045 O HOH A 554 15.992 -2.232 14.033 1.00 26.88 O HETATM 5046 O HOH A 555 31.366 10.664 31.610 1.00 29.20 O HETATM 5047 O HOH A 556 24.981 -1.210 18.132 1.00 36.14 O HETATM 5048 O HOH A 557 25.326 -2.322 21.147 1.00 27.33 O HETATM 5049 O HOH A 558 26.276 0.336 10.062 1.00 44.45 O HETATM 5050 O AHOH A 559 3.885 -20.216 22.961 0.50 26.32 O HETATM 5051 O BHOH A 559 6.367 -20.610 22.317 0.50 16.64 O HETATM 5052 O HOH B 292 -13.972 4.267 8.581 1.00 29.13 O HETATM 5053 O HOH B 293 -8.314 -0.507 9.831 1.00 21.50 O HETATM 5054 O HOH B 294 -30.404 10.394 3.034 1.00 34.98 O HETATM 5055 O HOH B 295 -7.508 32.889 3.385 1.00 38.60 O HETATM 5056 O HOH B 296 -6.731 31.652 14.610 1.00 32.16 O HETATM 5057 O HOH B 297 -26.527 29.430 -10.431 1.00 23.01 O HETATM 5058 O HOH B 298 -5.349 5.909 -1.057 1.00 26.34 O HETATM 5059 O HOH B 299 -5.859 4.444 1.226 1.00 24.65 O HETATM 5060 O HOH B 300 -14.848 2.705 -0.819 1.00 27.66 O HETATM 5061 O HOH B 301 -7.529 -2.411 -21.359 1.00 39.27 O HETATM 5062 O HOH B 302 -6.813 -6.276 5.291 1.00 28.58 O HETATM 5063 O HOH B 303 -29.258 8.107 1.570 1.00 29.16 O HETATM 5064 O HOH B 304 -34.693 17.605 -12.798 1.00 24.55 O HETATM 5065 O HOH B 305 -17.425 8.177 -4.643 1.00 32.74 O HETATM 5066 O HOH B 306 -23.196 12.917 -9.224 1.00 27.36 O HETATM 5067 O HOH B 307 -4.704 29.617 4.111 1.00 40.44 O HETATM 5068 O HOH B 308 -2.558 12.662 -1.422 1.00 35.96 O HETATM 5069 O HOH B 309 -1.819 15.506 -3.015 1.00 35.97 O HETATM 5070 O HOH B 310 -10.710 13.281 -3.438 1.00 35.09 O HETATM 5071 O HOH B 311 -26.420 28.533 3.795 1.00 31.73 O HETATM 5072 O HOH B 312 -25.210 12.918 14.738 1.00 21.41 O HETATM 5073 O HOH B 313 -28.919 16.705 19.489 1.00 19.81 O HETATM 5074 O HOH B 314 -8.957 -1.455 -0.912 1.00 31.66 O HETATM 5075 O HOH B 315 -14.055 16.770 -3.058 1.00 24.62 O HETATM 5076 O HOH B 316 -3.586 26.576 10.609 1.00 23.82 O HETATM 5077 O HOH B 317 -8.355 8.568 7.083 1.00 34.93 O HETATM 5078 O HOH B 318 -18.667 8.817 -21.196 1.00 29.22 O HETATM 5079 O HOH B 319 -22.229 -1.998 -1.785 1.00 22.31 O HETATM 5080 O HOH B 320 -5.015 15.378 -7.062 1.00 34.92 O HETATM 5081 O HOH B 321 -20.221 13.961 -13.179 1.00 27.63 O HETATM 5082 O HOH B 322 -9.821 27.054 -4.066 1.00 42.17 O HETATM 5083 O HOH B 323 -29.659 13.312 1.579 1.00 28.92 O HETATM 5084 O HOH B 324 -8.904 25.603 15.427 1.00 27.84 O HETATM 5085 O HOH B 325 -10.707 16.292 -12.348 1.00 29.23 O HETATM 5086 O HOH B 326 -29.699 28.680 -11.110 1.00 26.15 O HETATM 5087 O HOH B 327 -16.018 19.721 18.490 1.00 11.42 O HETATM 5088 O HOH B 328 -5.670 -2.547 3.173 1.00 35.36 O HETATM 5089 O HOH B 329 -31.871 19.064 -13.428 1.00 33.12 O HETATM 5090 O HOH B 330 -26.111 10.451 14.210 1.00 27.08 O HETATM 5091 O HOH B 331 -13.523 22.871 -7.201 1.00 40.47 O HETATM 5092 O HOH B 332 -18.247 34.082 1.822 1.00 28.51 O HETATM 5093 O HOH B 333 -29.926 22.194 4.615 1.00 40.24 O HETATM 5094 O HOH B 334 -34.217 13.040 -12.632 1.00 32.44 O HETATM 5095 O HOH B 335 -19.749 23.641 -15.252 1.00 37.30 O HETATM 5096 O HOH B 336 -20.132 -2.501 5.535 1.00 30.59 O HETATM 5097 O HOH B 337 -36.532 11.894 -10.800 1.00 29.46 O HETATM 5098 O HOH B 338 -4.521 29.328 -1.005 1.00 39.84 O HETATM 5099 O HOH B 339 -14.829 32.043 14.392 1.00 30.89 O HETATM 5100 O HOH B 340 -6.864 1.948 0.136 1.00 32.38 O HETATM 5101 O HOH B 341 -1.638 9.795 -18.077 1.00 31.31 O HETATM 5102 O HOH B 342 -6.766 8.233 4.268 1.00 40.47 O HETATM 5103 O HOH B 343 -17.245 31.409 17.911 1.00 39.46 O HETATM 5104 O HOH B 344 -26.257 -0.194 4.227 1.00 47.44 O HETATM 5105 O HOH B 345 -22.029 12.397 -11.598 1.00 35.23 O HETATM 5106 O HOH B 346 -20.246 33.774 -0.172 1.00 37.37 O HETATM 5107 O HOH B 347 -17.041 4.897 3.630 1.00 39.55 O HETATM 5108 O HOH B 348 -26.833 13.304 -18.502 1.00 35.24 O HETATM 5109 O HOH B 349 -23.889 1.179 -8.847 1.00 39.68 O HETATM 5110 O HOH B 350 -19.039 -4.226 -3.058 1.00 42.09 O HETATM 5111 O HOH B 351 -24.124 10.604 0.377 1.00 38.05 O HETATM 5112 O HOH B 352 -3.712 13.643 -12.058 1.00 38.43 O HETATM 5113 O HOH B 353 -37.543 24.109 -0.107 1.00 41.89 O HETATM 5114 O HOH B 354 -37.749 12.809 -7.252 1.00 33.65 O HETATM 5115 O HOH B 355 -12.408 20.064 18.111 1.00 26.07 O HETATM 5116 O HOH B 356 -27.372 23.816 10.154 1.00 25.54 O HETATM 5117 O HOH B 357 -10.896 36.128 -0.761 1.00 37.33 O HETATM 5118 O HOH B 358 -19.645 6.833 18.642 1.00 38.02 O HETATM 5119 O HOH B 359 -4.049 11.893 -21.035 1.00 46.02 O HETATM 5120 O HOH B 360 -15.656 5.349 1.334 1.00 36.28 O HETATM 5121 O HOH B 361 -7.796 20.536 11.121 1.00 43.21 O HETATM 5122 O HOH B 362 -27.750 26.730 1.756 1.00 49.46 O HETATM 5123 O HOH B 363 -12.778 -2.809 13.724 1.00 41.67 O HETATM 5124 O HOH B 364 -24.351 6.105 12.968 1.00 42.62 O HETATM 5125 O HOH B 365 -6.819 14.764 -17.363 1.00 27.61 O HETATM 5126 O HOH B 366 -7.219 15.804 -20.088 1.00 30.51 O HETATM 5127 O HOH B 367 -15.849 -2.395 12.914 1.00 38.71 O HETATM 5128 O HOH B 368 -22.587 -4.798 -6.793 1.00 36.11 O HETATM 5129 O HOH B 369 -4.276 13.861 -17.401 1.00 43.99 O HETATM 5130 O AHOH B 370 -13.525 15.926 -10.122 0.50 14.82 O HETATM 5131 O BHOH B 370 -13.503 15.570 -7.698 0.50 25.08 O HETATM 5132 O AHOH B 371 -15.024 17.749 -10.426 0.50 19.84 O HETATM 5133 O BHOH B 371 -14.733 19.401 -11.040 0.50 21.83 O HETATM 5134 O HOH B 372 -12.199 18.829 -11.713 1.00 42.38 O HETATM 5135 O HOH B 373 -12.345 15.533 -4.704 1.00 38.83 O HETATM 5136 O HOH B 374 -8.575 16.089 -10.758 1.00 37.94 O HETATM 5137 O HOH B 376 -28.251 18.023 -17.128 1.00 44.45 O HETATM 5138 O HOH B 377 -28.265 20.659 -17.536 1.00 39.28 O CONECT 4879 4880 4898 CONECT 4880 4879 4881 4904 CONECT 4881 4880 4882 CONECT 4882 4881 4897 CONECT 4883 4904 4905 4906 CONECT 4884 4885 4889 4905 CONECT 4885 4884 4886 CONECT 4886 4885 4887 CONECT 4887 4886 4888 4890 CONECT 4888 4887 4889 CONECT 4889 4884 4888 CONECT 4890 4887 4907 CONECT 4891 4892 4907 CONECT 4892 4891 4908 CONECT 4893 4894 4908 4909 CONECT 4894 4893 4907 CONECT 4895 4896 4909 CONECT 4896 4895 CONECT 4897 4882 4898 4903 CONECT 4898 4879 4897 4899 CONECT 4899 4898 4900 4901 4902 CONECT 4900 4899 CONECT 4901 4899 CONECT 4902 4899 CONECT 4903 4897 CONECT 4904 4880 4883 CONECT 4905 4883 4884 CONECT 4906 4883 CONECT 4907 4890 4891 4894 CONECT 4908 4892 4893 CONECT 4909 4893 4895 4910 CONECT 4910 4909 CONECT 4911 4912 4913 CONECT 4912 4911 CONECT 4913 4911 4914 CONECT 4914 4913 CONECT 4915 4916 4917 CONECT 4916 4915 CONECT 4917 4915 4918 CONECT 4918 4917 CONECT 4919 4920 4921 CONECT 4920 4919 CONECT 4921 4919 4922 CONECT 4922 4921 CONECT 4923 4924 4925 CONECT 4924 4923 CONECT 4925 4923 4926 CONECT 4926 4925 CONECT 4927 4928 4929 CONECT 4928 4927 CONECT 4929 4927 4930 CONECT 4930 4929 CONECT 4931 4932 4933 CONECT 4932 4931 CONECT 4933 4931 4934 CONECT 4934 4933 CONECT 4935 4936 4937 CONECT 4936 4935 CONECT 4937 4935 4938 4939 CONECT 4938 4937 CONECT 4939 4937 4940 CONECT 4940 4939 CONECT 4941 4942 4943 CONECT 4942 4941 CONECT 4943 4941 4944 CONECT 4944 4943 CONECT 4945 4946 4947 CONECT 4946 4945 CONECT 4947 4945 4948 CONECT 4948 4947 CONECT 4949 4950 4951 CONECT 4950 4949 CONECT 4951 4949 4952 CONECT 4952 4951 CONECT 4953 4954 4955 CONECT 4954 4953 CONECT 4955 4953 4956 CONECT 4956 4955 CONECT 4957 4958 4959 CONECT 4958 4957 CONECT 4959 4957 4960 CONECT 4960 4959 MASTER 506 0 13 33 8 0 22 6 5126 2 82 54 END
Display Options:
Goto PDB code:
3D presentation of molecule is powered by
3Dmol
, which supports all modern browsers and mobile devices via WebGL.
Hold mouse button:
left to rotate,middle to shift,right to zoom
Related entries of code: 3rgf
Entries with 90% protein sequence similarity cutoff in PDBbind
PDB Code
Check Database
Protein Sequence Similarity
4crl
RCSB PDB
PDBbind
285aa, >4CRL_2|Chain... at 100%
4f6s
RCSB PDB
PDBbind
287aa, >4F6S_2|Chain... *
4f6u
RCSB PDB
PDBbind
287aa, >4F6U_2|Chain... at 100%
4f6w
RCSB PDB
PDBbind
287aa, >4F6W_2|Chain... at 100%
4f70
RCSB PDB
PDBbind
287aa, >4F70_2|Chain... at 100%
4f7j
RCSB PDB
PDBbind
287aa, >4F7J_2|Chain... at 100%
4f7l
RCSB PDB
PDBbind
287aa, >4F7L_2|Chain... at 100%
4f7n
RCSB PDB
PDBbind
287aa, >4F7N_2|Chain... at 100%
5bnj
RCSB PDB
PDBbind
285aa, >5BNJ_2|Chain... at 100%
5cei
RCSB PDB
PDBbind
287aa, >5CEI_2|Chain... at 100%
5fgk
RCSB PDB
PDBbind
266aa, >5FGK_2|Chain... at 100%
5hbe
RCSB PDB
PDBbind
266aa, >5HBE_2|Chain... at 100%
5hbh
RCSB PDB
PDBbind
270aa, >5HBH_2|Chain... at 99%
5hbj
RCSB PDB
PDBbind
270aa, >5HBJ_2|Chain... at 99%
5hvy
RCSB PDB
PDBbind
287aa, >5HVY_2|Chain... at 100%
5i5z
RCSB PDB
PDBbind
266aa, >5I5Z_2|Chain... at 100%
5icp
RCSB PDB
PDBbind
267aa, >5ICP_2|Chain... at 100%
5idn
RCSB PDB
PDBbind
267aa, >5IDN_2|Chain... at 100%
5idp
RCSB PDB
PDBbind
268aa, >5IDP_2|Chain... at 100%
5xqx
RCSB PDB
PDBbind
263aa, >5XQX_2|Chain... at 100%
5xs2
RCSB PDB
PDBbind
263aa, >5XS2_2|Chain... at 100%
Complexes with the same small molecule ligand
PDB Code
Check Database
Ligand Name
No complexes with the same small molecule ligand are found!
Entry Information
PDB ID
3rgf
Complex Type
Protein-Protein
PDBbind Subset
general set
Protein Name
human Cyclin-dependent kinase 8, CDK8
Ligand Name
Cyclin-C
EC.Number
E.C.2.7.11.22
Resolution
2.2(Å)
Affinity (Kd/Ki/IC50)
Kd=7.05nM
Release Year
2011
Protein/NA Sequence
Check fasta file
Primary Reference
(2011) J.Mol.Biol. Vol. 412: pp. 251-266
Links to External Databases
RCSB PDB
The mother database
PDBsum
Enhanced annotations on PDB entries
Pubchem
Comprehensive collection of chemical and biological data
UniProtKB AC
UniProt accession number (AC):
P24863
P49336
Entrez Gene ID
NCBI Entrez Gene ID:
892
1024
ASD
Information of known allosteric effects of PDB entries
This site has been visited
times since Nov 2007.
Copyright ©2007-2025 涓婃捣鐩堣禌鎬濅俊鎭鎶鏈夐檺鍏徃 缃戠珯澶囨鍙凤細
娌狪CP澶2021015625鍙-3
娌叕缃戝畨澶囷細
姝ｅ湪鐢宠涓
Technical Support锛堟妧鏈敮鎸侊級:
yingsaisi@foxmail.com
times since Nov 2007. 
娌叕缃戝畨澶囷細姝ｅ湪鐢宠涓