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*** MEMBRANE PROTEIN 26-MAR-24 8YU7 ***elNémo ID: 2603180307243691338Job options:ID = 2603180307243691338 JOBID = MEMBRANE PROTEIN 26-MAR-24 8YU7 USERID = unknown PRIVAT = 0 NMODES = 5 DQMIN = -100 DQMAX = 100 DQSTEP = 20 DOGRAPHS = on DOPROJMODS = 0 DORMSD = 0 NRBL = 0 CUTOFF = 0 CAONLY = 0 Input data for this run:REMARK File generated by Swiss-PdbViewer 4.00b0 REMARK http://www.expasy.org/spdbv/ REMARK File generated by Swiss-PdbViewer 4.00b0 REMARK http://www.expasy.org/spdbv/ HEADER MEMBRANE PROTEIN 26-MAR-24 8YU7 TITLE CRYO-EM STRUCTURE OF CXCR4 TETRAMER COMPND MOL_ID: 1; COMPND 2 MOLECULE: C-X-C CHEMOKINE RECEPTOR TYPE 4; COMPND 3 CHAIN: A, B, C, D; COMPND 4 SYNONYM: CXC-R4,CXCR-4,FB22,FUSIN,HM89,LCR1,LEUKOCYTE-DERIVED SEVEN COMPND 5 TRANSMEMBRANE DOMAIN RECEPTOR,LESTR,LIPOPOLYSACCHARIDE-ASSOCIATED COMPND 6 PROTEIN 3,LAP-3,LPS-ASSOCIATED PROTEIN 3,NPYRL,STROMAL CELL-DERIVED COMPND 7 FACTOR 1 RECEPTOR,SDF-1 RECEPTOR; COMPND 8 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: CXCR4; SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7108 KEYWDS CHEMOKINE RECEPTOR, CXCR4, G PROTEIN-COUPLED RECEPTOR, MEMBRANE KEYWDS 2 PROTEIN EXPDTA ELECTRON MICROSCOPY AUTHOR A.LIU,Y.LIU REVDAT 1 05-MAR-25 8YU7 0 REMARK 2 REMARK 2 RESOLUTION. 3.01 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 SOFTWARE PACKAGES : NULL REMARK 3 RECONSTRUCTION SCHEMA : NULL REMARK 3 REMARK 3 EM MAP-MODEL FITTING AND REFINEMENT REMARK 3 PDB ENTRY : NULL REMARK 3 REFINEMENT SPACE : NULL REMARK 3 REFINEMENT PROTOCOL : NULL REMARK 3 REFINEMENT TARGET : NULL REMARK 3 OVERALL ANISOTROPIC B VALUE : NULL REMARK 3 REMARK 3 FITTING PROCEDURE : NULL REMARK 3 REMARK 3 EM IMAGE RECONSTRUCTION STATISTICS REMARK 3 NOMINAL PIXEL SIZE (ANGSTROMS) : NULL REMARK 3 ACTUAL PIXEL SIZE (ANGSTROMS) : NULL REMARK 3 EFFECTIVE RESOLUTION (ANGSTROMS) : 3.010 REMARK 3 NUMBER OF PARTICLES : 162668 REMARK 3 CTF CORRECTION METHOD : PHASE FLIPPING AND AMPLITUDE REMARK 3 CORRECTION REMARK 3 REMARK 3 EM RECONSTRUCTION MAGNIFICATION CALIBRATION: NULL REMARK 3 REMARK 3 OTHER DETAILS: NULL REMARK 4 REMARK 4 8YU7 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 02-APR-24. REMARK 100 THE DEPOSITION ID IS D_1300046367. REMARK 245 REMARK 245 EXPERIMENTAL DETAILS REMARK 245 RECONSTRUCTION METHOD : SINGLE PARTICLE REMARK 245 SPECIMEN TYPE : NULL REMARK 245 REMARK 245 ELECTRON MICROSCOPE SAMPLE REMARK 245 SAMPLE TYPE : PARTICLE REMARK 245 PARTICLE TYPE : POINT REMARK 245 NAME OF SAMPLE : TETRAMER OF CXC CHEMOKINE REMARK 245 RECEPTOR TYPE 4 REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : NULL REMARK 245 SAMPLE SUPPORT DETAILS : NULL REMARK 245 SAMPLE VITRIFICATION DETAILS : NULL REMARK 245 SAMPLE BUFFER : NULL REMARK 245 PH : 7.40 REMARK 245 SAMPLE DETAILS : NULL REMARK 245 REMARK 245 DATA ACQUISITION REMARK 245 DATE OF EXPERIMENT : NULL REMARK 245 NUMBER OF MICROGRAPHS-IMAGES : NULL REMARK 245 TEMPERATURE (KELVIN) : NULL REMARK 245 MICROSCOPE MODEL : FEI TITAN KRIOS REMARK 245 DETECTOR TYPE : GATAN K3 BIOQUANTUM (6K X REMARK 245 4K) REMARK 245 MINIMUM DEFOCUS (NM) : 1200.00 REMARK 245 MAXIMUM DEFOCUS (NM) : 2500.00 REMARK 245 MINIMUM TILT ANGLE (DEGREES) : NULL REMARK 245 MAXIMUM TILT ANGLE (DEGREES) : NULL REMARK 245 NOMINAL CS : NULL REMARK 245 IMAGING MODE : BRIGHT FIELD REMARK 245 ELECTRON DOSE (ELECTRONS NM**-2) : 5200.00 REMARK 245 ILLUMINATION MODE : FLOOD BEAM REMARK 245 NOMINAL MAGNIFICATION : NULL REMARK 245 CALIBRATED MAGNIFICATION : NULL REMARK 245 SOURCE : FIELD EMISSION GUN REMARK 245 ACCELERATION VOLTAGE (KV) : 300 REMARK 245 IMAGING DETAILS : NULL REMARK 247 REMARK 247 ELECTRON MICROSCOPY REMARK 247 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM ELECTRON REMARK 247 MICROSCOPY DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE REMARK 247 THAT CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES REMARK 247 ON THESE RECORDS ARE MEANINGLESS EXCEPT FOR THE CALCULATION REMARK 247 OF THE STRUCTURE FACTORS. 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: TETRAMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 GLU A 2 REMARK 465 GLY A 3 REMARK 465 ILE A 4 REMARK 465 SER A 5 REMARK 465 ILE A 6 REMARK 465 TYR A 7 REMARK 465 THR A 8 REMARK 465 SER A 9 REMARK 465 ASP A 10 REMARK 465 ASN A 11 REMARK 465 TYR A 12 REMARK 465 THR A 13 REMARK 465 GLU A 14 REMARK 465 GLU A 15 REMARK 465 MET A 16 REMARK 465 GLY A 17 REMARK 465 SER A 18 REMARK 465 GLY A 19 REMARK 465 ASP A 20 REMARK 465 TYR A 21 REMARK 465 ASP A 22 REMARK 465 SER A 23 REMARK 465 MET A 24 REMARK 465 LYS A 25 REMARK 465 GLY A 306 REMARK 465 ALA A 307 REMARK 465 LYS A 308 REMARK 465 PHE A 309 REMARK 465 LYS A 310 REMARK 465 THR A 311 REMARK 465 SER A 312 REMARK 465 ALA A 313 REMARK 465 GLN A 314 REMARK 465 HIS A 315 REMARK 465 ALA A 316 REMARK 465 LEU A 317 REMARK 465 THR A 318 REMARK 465 SER A 319 REMARK 465 VAL A 320 REMARK 465 SER A 321 REMARK 465 ARG A 322 REMARK 465 GLY A 323 REMARK 465 SER A 324 REMARK 465 SER A 325 REMARK 465 LEU A 326 REMARK 465 LYS A 327 REMARK 465 ILE A 328 REMARK 465 LEU A 329 REMARK 465 SER A 330 REMARK 465 LYS A 331 REMARK 465 GLY A 332 REMARK 465 LYS A 333 REMARK 465 ARG A 334 REMARK 465 GLY A 335 REMARK 465 GLY A 336 REMARK 465 HIS A 337 REMARK 465 SER A 338 REMARK 465 SER A 339 REMARK 465 VAL A 340 REMARK 465 SER A 341 REMARK 465 THR A 342 REMARK 465 GLU A 343 REMARK 465 SER A 344 REMARK 465 GLU A 345 REMARK 465 SER A 346 REMARK 465 SER A 347 REMARK 465 SER A 348 REMARK 465 PHE A 349 REMARK 465 HIS A 350 REMARK 465 SER A 351 REMARK 465 SER A 352 REMARK 465 GLU B 2 REMARK 465 GLY B 3 REMARK 465 ILE B 4 REMARK 465 SER B 5 REMARK 465 ILE B 6 REMARK 465 TYR B 7 REMARK 465 THR B 8 REMARK 465 SER B 9 REMARK 465 ASP B 10 REMARK 465 ASN B 11 REMARK 465 TYR B 12 REMARK 465 THR B 13 REMARK 465 GLU B 14 REMARK 465 GLU B 15 REMARK 465 MET B 16 REMARK 465 GLY B 17 REMARK 465 SER B 18 REMARK 465 GLY B 19 REMARK 465 ASP B 20 REMARK 465 TYR B 21 REMARK 465 ASP B 22 REMARK 465 SER B 23 REMARK 465 MET B 24 REMARK 465 LYS B 25 REMARK 465 GLY B 306 REMARK 465 ALA B 307 REMARK 465 LYS B 308 REMARK 465 PHE B 309 REMARK 465 LYS B 310 REMARK 465 THR B 311 REMARK 465 SER B 312 REMARK 465 ALA B 313 REMARK 465 GLN B 314 REMARK 465 HIS B 315 REMARK 465 ALA B 316 REMARK 465 LEU B 317 REMARK 465 THR B 318 REMARK 465 SER B 319 REMARK 465 VAL B 320 REMARK 465 SER B 321 REMARK 465 ARG B 322 REMARK 465 GLY B 323 REMARK 465 SER B 324 REMARK 465 SER B 325 REMARK 465 LEU B 326 REMARK 465 LYS B 327 REMARK 465 ILE B 328 REMARK 465 LEU B 329 REMARK 465 SER B 330 REMARK 465 LYS B 331 REMARK 465 GLY B 332 REMARK 465 LYS B 333 REMARK 465 ARG B 334 REMARK 465 GLY B 335 REMARK 465 GLY B 336 REMARK 465 HIS B 337 REMARK 465 SER B 338 REMARK 465 SER B 339 REMARK 465 VAL B 340 REMARK 465 SER B 341 REMARK 465 THR B 342 REMARK 465 GLU B 343 REMARK 465 SER B 344 REMARK 465 GLU B 345 REMARK 465 SER B 346 REMARK 465 SER B 347 REMARK 465 SER B 348 REMARK 465 PHE B 349 REMARK 465 HIS B 350 REMARK 465 SER B 351 REMARK 465 SER B 352 REMARK 465 GLU C 2 REMARK 465 GLY C 3 REMARK 465 ILE C 4 REMARK 465 SER C 5 REMARK 465 ILE C 6 REMARK 465 TYR C 7 REMARK 465 THR C 8 REMARK 465 SER C 9 REMARK 465 ASP C 10 REMARK 465 ASN C 11 REMARK 465 TYR C 12 REMARK 465 THR C 13 REMARK 465 GLU C 14 REMARK 465 GLU C 15 REMARK 465 MET C 16 REMARK 465 GLY C 17 REMARK 465 SER C 18 REMARK 465 GLY C 19 REMARK 465 ASP C 20 REMARK 465 TYR C 21 REMARK 465 ASP C 22 REMARK 465 SER C 23 REMARK 465 MET C 24 REMARK 465 LYS C 25 REMARK 465 GLY C 306 REMARK 465 ALA C 307 REMARK 465 LYS C 308 REMARK 465 PHE C 309 REMARK 465 LYS C 310 REMARK 465 THR C 311 REMARK 465 SER C 312 REMARK 465 ALA C 313 REMARK 465 GLN C 314 REMARK 465 HIS C 315 REMARK 465 ALA C 316 REMARK 465 LEU C 317 REMARK 465 THR C 318 REMARK 465 SER C 319 REMARK 465 VAL C 320 REMARK 465 SER C 321 REMARK 465 ARG C 322 REMARK 465 GLY C 323 REMARK 465 SER C 324 REMARK 465 SER C 325 REMARK 465 LEU C 326 REMARK 465 LYS C 327 REMARK 465 ILE C 328 REMARK 465 LEU C 329 REMARK 465 SER C 330 REMARK 465 LYS C 331 REMARK 465 GLY C 332 REMARK 465 LYS C 333 REMARK 465 ARG C 334 REMARK 465 GLY C 335 REMARK 465 GLY C 336 REMARK 465 HIS C 337 REMARK 465 SER C 338 REMARK 465 SER C 339 REMARK 465 VAL C 340 REMARK 465 SER C 341 REMARK 465 THR C 342 REMARK 465 GLU C 343 REMARK 465 SER C 344 REMARK 465 GLU C 345 REMARK 465 SER C 346 REMARK 465 SER C 347 REMARK 465 SER C 348 REMARK 465 PHE C 349 REMARK 465 HIS C 350 REMARK 465 SER C 351 REMARK 465 SER C 352 REMARK 465 GLU D 2 REMARK 465 GLY D 3 REMARK 465 ILE D 4 REMARK 465 SER D 5 REMARK 465 ILE D 6 REMARK 465 TYR D 7 REMARK 465 THR D 8 REMARK 465 SER D 9 REMARK 465 ASP D 10 REMARK 465 ASN D 11 REMARK 465 TYR D 12 REMARK 465 THR D 13 REMARK 465 GLU D 14 REMARK 465 GLU D 15 REMARK 465 MET D 16 REMARK 465 GLY D 17 REMARK 465 SER D 18 REMARK 465 GLY D 19 REMARK 465 ASP D 20 REMARK 465 TYR D 21 REMARK 465 ASP D 22 REMARK 465 SER D 23 REMARK 465 MET D 24 REMARK 465 LYS D 25 REMARK 465 GLY D 306 REMARK 465 ALA D 307 REMARK 465 LYS D 308 REMARK 465 PHE D 309 REMARK 465 LYS D 310 REMARK 465 THR D 311 REMARK 465 SER D 312 REMARK 465 ALA D 313 REMARK 465 GLN D 314 REMARK 465 HIS D 315 REMARK 465 ALA D 316 REMARK 465 LEU D 317 REMARK 465 THR D 318 REMARK 465 SER D 319 REMARK 465 VAL D 320 REMARK 465 SER D 321 REMARK 465 ARG D 322 REMARK 465 GLY D 323 REMARK 465 SER D 324 REMARK 465 SER D 325 REMARK 465 LEU D 326 REMARK 465 LYS D 327 REMARK 465 ILE D 328 REMARK 465 LEU D 329 REMARK 465 SER D 330 REMARK 465 LYS D 331 REMARK 465 GLY D 332 REMARK 465 LYS D 333 REMARK 465 ARG D 334 REMARK 465 GLY D 335 REMARK 465 GLY D 336 REMARK 465 HIS D 337 REMARK 465 SER D 338 REMARK 465 SER D 339 REMARK 465 VAL D 340 REMARK 465 SER D 341 REMARK 465 THR D 342 REMARK 465 GLU D 343 REMARK 465 SER D 344 REMARK 465 GLU D 345 REMARK 465 SER D 346 REMARK 465 SER D 347 REMARK 465 SER D 348 REMARK 465 PHE D 349 REMARK 465 HIS D 350 REMARK 465 SER D 351 REMARK 465 SER D 352 REMARK 470 REMARK 470 MISSING ATOM REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 470 I=INSERTION CODE): REMARK 470 M RES CSSEQI ATOMS REMARK 470 LYS A 67 CG CD CE NZ REMARK 470 LYS A 68 CG CD CE NZ REMARK 470 SER A 229 OG REMARK 470 LYS B 67 CG CD CE NZ REMARK 470 LYS B 68 CG CD CE NZ REMARK 470 SER B 229 OG REMARK 470 LYS C 67 CG CD CE NZ REMARK 470 LYS C 68 CG CD CE NZ REMARK 470 SER C 229 OG REMARK 470 LYS D 67 CG CD CE NZ REMARK 470 LYS D 68 CG CD CE NZ REMARK 470 SER D 229 OG REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT REMARK 500 REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT. REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE REMARK 500 O ALA B 291 ND1 HIS B 294 2.11 REMARK 500 O ALA A 291 ND1 HIS A 294 2.11 REMARK 500 O ALA C 291 ND1 HIS C 294 2.11 REMARK 500 O ALA D 291 ND1 HIS D 294 2.11 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 SER A 229 -118.64 59.06 REMARK 500 HIS A 232 -168.17 -160.61 REMARK 500 LEU A 267 47.82 -91.92 REMARK 500 GLU A 268 48.51 38.39 REMARK 500 SER B 229 -118.74 58.97 REMARK 500 HIS B 232 -168.17 -160.60 REMARK 500 LEU B 267 47.78 -91.80 REMARK 500 GLU B 268 48.54 38.41 REMARK 500 SER C 229 -118.72 59.09 REMARK 500 HIS C 232 -168.17 -160.63 REMARK 500 LEU C 267 47.79 -91.87 REMARK 500 GLU C 268 48.53 38.39 REMARK 500 SER D 229 -118.74 59.08 REMARK 500 HIS D 232 -168.21 -160.58 REMARK 500 LEU D 267 47.73 -91.76 REMARK 500 GLU D 268 48.46 38.41 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-39573 RELATED DB: EMDB REMARK 900 CRYO-EM STRUCTURE OF CXCR4 TETRAMER DBREF 8YU7 A 2 352 UNP P61073 CXCR4_HUMAN 2 352 DBREF 8YU7 B 2 352 UNP P61073 CXCR4_HUMAN 2 352 DBREF 8YU7 C 2 352 UNP P61073 CXCR4_HUMAN 2 352 DBREF 8YU7 D 2 352 UNP P61073 CXCR4_HUMAN 2 352 CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1 1 ATOM 1 N GLU A 26 157.761 154.522 99.596 1.00 73.56 ATOM 2 CA GLU A 26 156.483 154.877 98.987 1.00 73.56 ATOM 3 C GLU A 26 155.330 154.631 99.954 1.00 73.56 ATOM 4 O GLU A 26 155.037 153.483 100.294 1.00 73.56 ATOM 5 CB GLU A 26 156.267 154.087 97.695 1.00 73.56 ATOM 6 CG GLU A 26 154.990 154.446 96.954 1.00 73.56 ATOM 7 CD GLU A 26 153.765 153.779 97.547 1.00 73.56 ATOM 8 OE1 GLU A 26 153.918 152.717 98.186 1.00 73.56 ATOM 9 OE2 GLU A 26 152.651 154.319 97.376 1.00 73.56 ATOM 10 N PRO A 27 154.687 155.707 100.402 1.00 73.35 ATOM 11 CA PRO A 27 153.552 155.560 101.323 1.00 73.35 ATOM 12 C PRO A 27 152.421 154.764 100.690 1.00 73.35 ATOM 13 O PRO A 27 152.147 154.879 99.492 1.00 73.35 ATOM 14 CB PRO A 27 153.185 157.009 101.650 1.00 73.35 ATOM 15 CG PRO A 27 154.485 157.765 101.493 1.00 73.35 ATOM 16 CD PRO A 27 155.114 157.109 100.276 1.00 73.35 ATOM 17 N CYS A 28 151.760 153.953 101.511 1.00 72.54 ATOM 18 CA CYS A 28 150.658 153.125 101.046 1.00 72.54 ATOM 19 C CYS A 28 149.351 153.917 101.081 1.00 72.54 ATOM 20 O CYS A 28 149.318 155.107 101.400 1.00 72.54 ATOM 21 CB CYS A 28 150.544 151.858 101.896 1.00 72.54 ATOM 22 SG CYS A 28 151.968 150.730 101.760 1.00 72.54 ATOM 23 N PHE A 29 148.255 153.242 100.746 1.00 73.10 ATOM 24 CA PHE A 29 146.941 153.867 100.690 1.00 73.10 ATOM 25 C PHE A 29 145.930 152.922 101.332 1.00 73.10 ATOM 26 O PHE A 29 146.296 151.960 102.013 1.00 73.10 ATOM 27 CB PHE A 29 146.565 154.196 99.244 1.00 73.10 ATOM 28 CG PHE A 29 147.450 155.228 98.607 1.00 73.10 ATOM 29 CD1 PHE A 29 147.199 156.579 98.779 1.00 73.10 ATOM 30 CD2 PHE A 29 148.537 154.851 97.838 1.00 73.10 ATOM 31 CE1 PHE A 29 148.013 157.529 98.194 1.00 73.10 ATOM 32 CE2 PHE A 29 149.353 155.799 97.250 1.00 73.10 ATOM 33 CZ PHE A 29 149.091 157.139 97.429 1.00 73.10 ATOM 34 N ARG A 30 144.644 153.221 101.120 1.00 71.90 ATOM 35 CA ARG A 30 143.535 152.419 101.640 1.00 71.90 ATOM 36 C ARG A 30 143.524 152.411 103.168 1.00 71.90 ATOM 37 O ARG A 30 143.387 151.367 103.808 1.00 71.90 ATOM 38 CB ARG A 30 143.614 150.987 101.109 1.00 71.90 ATOM 39 CG ARG A 30 144.870 150.239 101.526 1.00 71.90 ATOM 40 CD ARG A 30 144.882 148.826 100.965 1.00 71.90 ATOM 41 NE ARG A 30 146.082 148.092 101.357 1.00 71.90 ATOM 42 CZ ARG A 30 147.242 148.154 100.710 1.00 71.90 ATOM 43 NH1 ARG A 30 147.359 148.919 99.633 1.00 71.90 ATOM 44 NH2 ARG A 30 148.279 147.451 101.140 1.00 71.90 ATOM 45 N GLU A 31 143.667 153.598 103.752 1.00 69.21 ATOM 46 CA GLU A 31 143.607 153.780 105.198 1.00 69.21 ATOM 47 C GLU A 31 142.252 154.386 105.547 1.00 69.21 ATOM 48 O GLU A 31 141.958 155.524 105.170 1.00 69.21 ATOM 49 CB GLU A 31 144.761 154.663 105.675 1.00 69.21 ATOM 50 CG GLU A 31 146.137 154.049 105.476 1.00 69.21 ATOM 51 CD GLU A 31 146.345 152.802 106.313 1.00 69.21 ATOM 52 OE1 GLU A 31 145.903 152.790 107.481 1.00 69.21 ATOM 53 OE2 GLU A 31 146.948 151.835 105.800 1.00 69.21 ATOM 54 N GLU A 32 141.431 153.627 106.269 1.00 63.29 ATOM 55 CA GLU A 32 140.116 154.102 106.677 1.00 63.29 ATOM 56 C GLU A 32 139.674 153.323 107.905 1.00 63.29 ATOM 57 O GLU A 32 140.189 152.240 108.195 1.00 63.29 ATOM 58 CB GLU A 32 139.113 153.954 105.531 1.00 63.29 ATOM 59 CG GLU A 32 139.419 154.824 104.323 1.00 63.29 ATOM 60 CD GLU A 32 139.311 156.304 104.628 1.00 63.29 ATOM 61 OE1 GLU A 32 138.379 156.693 105.362 1.00 63.29 ATOM 62 OE2 GLU A 32 140.162 157.076 104.136 1.00 63.29 ATOM 63 N ASN A 33 138.710 153.891 108.622 1.00 37.52 ATOM 64 CA ASN A 33 138.192 153.258 109.827 1.00 37.52 ATOM 65 C ASN A 33 137.168 152.188 109.473 1.00 37.52 ATOM 66 O ASN A 33 136.366 152.353 108.551 1.00 37.52 ATOM 67 CB ASN A 33 137.573 154.303 110.757 1.00 37.52 ATOM 68 CG ASN A 33 137.147 153.718 112.090 1.00 37.52 ATOM 69 OD1 ASN A 33 136.948 152.510 112.212 1.00 37.52 ATOM 70 ND2 ASN A 33 137.012 154.575 113.094 1.00 37.52 ATOM 71 N ALA A 34 137.206 151.083 110.213 1.00 22.83 ATOM 72 CA ALA A 34 136.263 150.000 109.988 1.00 22.83 ATOM 73 C ALA A 34 134.874 150.386 110.484 1.00 22.83 ATOM 74 O ALA A 34 134.720 151.202 111.396 1.00 22.83 ATOM 75 CB ALA A 34 136.741 148.715 110.681 1.00 22.83 ATOM 76 N ASN A 35 133.855 149.782 109.870 1.00 14.80 ATOM 77 CA ASN A 35 132.478 150.096 110.241 1.00 14.80 ATOM 78 C ASN A 35 132.180 149.679 111.675 1.00 14.80 ATOM 79 O ASN A 35 131.469 150.385 112.397 1.00 14.80 ATOM 80 CB ASN A 35 131.497 149.417 109.284 1.00 14.80 ATOM 81 CG ASN A 35 131.520 150.025 107.896 1.00 14.80 ATOM 82 OD1 ASN A 35 131.828 149.348 106.916 1.00 14.80 ATOM 83 ND2 ASN A 35 131.192 151.308 107.808 1.00 14.80 ATOM 84 N PHE A 36 132.709 148.532 112.105 1.00 10.37 ATOM 85 CA PHE A 36 132.481 148.095 113.478 1.00 10.37 ATOM 86 C PHE A 36 133.168 149.012 114.481 1.00 10.37 ATOM 87 O PHE A 36 132.652 149.210 115.589 1.00 10.37 ATOM 88 CB PHE A 36 132.967 146.657 113.671 1.00 10.37 ATOM 89 CG PHE A 36 132.703 146.107 115.042 1.00 10.37 ATOM 90 CD1 PHE A 36 131.450 145.626 115.382 1.00 10.37 ATOM 91 CD2 PHE A 36 133.705 146.068 115.994 1.00 10.37 ATOM 92 CE1 PHE A 36 131.206 145.120 116.645 1.00 10.37 ATOM 93 CE2 PHE A 36 133.465 145.564 117.258 1.00 10.37 ATOM 94 CZ PHE A 36 132.215 145.088 117.583 1.00 10.37 ATOM 95 N ASN A 37 134.326 149.567 114.123 1.00 11.03 ATOM 96 CA ASN A 37 135.033 150.459 115.036 1.00 11.03 ATOM 97 C ASN A 37 134.241 151.735 115.287 1.00 11.03 ATOM 98 O ASN A 37 134.219 152.246 116.415 1.00 11.03 ATOM 99 CB ASN A 37 136.418 150.801 114.485 1.00 11.03 ATOM 100 CG ASN A 37 137.224 151.669 115.432 1.00 11.03 ATOM 101 OD1 ASN A 37 137.486 151.284 116.570 1.00 11.03 ATOM 102 ND2 ASN A 37 137.621 152.845 114.961 1.00 11.03 ATOM 103 N LYS A 38 133.567 152.250 114.255 1.00 7.77 ATOM 104 CA LYS A 38 132.799 153.483 114.383 1.00 7.77 ATOM 105 C LYS A 38 131.684 153.371 115.411 1.00 7.77 ATOM 106 O LYS A 38 131.183 154.400 115.879 1.00 7.77 ATOM 107 CB LYS A 38 132.205 153.887 113.032 1.00 7.77 ATOM 108 CG LYS A 38 133.240 154.296 111.997 1.00 7.77 ATOM 109 CD LYS A 38 132.583 154.685 110.682 1.00 7.77 ATOM 110 CE LYS A 38 133.618 155.093 109.647 1.00 7.77 ATOM 111 NZ LYS A 38 134.501 153.956 109.266 1.00 7.77 ATOM 112 N ILE A 39 131.273 152.155 115.762 1.00 4.04 ATOM 113 CA ILE A 39 130.295 151.951 116.813 1.00 4.04 ATOM 114 C ILE A 39 130.928 151.429 118.098 1.00 4.04 ATOM 115 O ILE A 39 130.401 151.690 119.185 1.00 4.04 ATOM 116 CB ILE A 39 129.194 150.967 116.376 1.00 4.04 ATOM 117 CG1 ILE A 39 128.379 151.557 115.223 1.00 4.04 ATOM 118 CG2 ILE A 39 128.251 150.674 117.533 1.00 4.04 ATOM 119 CD1 ILE A 39 127.435 150.569 114.574 1.00 4.04 ATOM 120 N PHE A 40 132.041 150.698 118.009 1.00 4.15 ATOM 121 CA PHE A 40 132.671 150.167 119.213 1.00 4.15 ATOM 122 C PHE A 40 133.365 151.263 120.011 1.00 4.15 ATOM 123 O PHE A 40 133.247 151.311 121.241 1.00 4.15 ATOM 124 CB PHE A 40 133.674 149.069 118.854 1.00 4.15 ATOM 125 CG PHE A 40 134.316 148.421 120.046 1.00 4.15 ATOM 126 CD1 PHE A 40 133.649 147.442 120.762 1.00 4.15 ATOM 127 CD2 PHE A 40 135.586 148.787 120.452 1.00 4.15 ATOM 128 CE1 PHE A 40 134.239 146.844 121.860 1.00 4.15 ATOM 129 CE2 PHE A 40 136.178 148.193 121.550 1.00 4.15 ATOM 130 CZ PHE A 40 135.505 147.219 122.254 1.00 4.15 ATOM 131 N LEU A 41 134.108 152.143 119.336 1.00 2.30 ATOM 132 CA LEU A 41 134.852 153.182 120.046 1.00 2.30 ATOM 133 C LEU A 41 133.953 154.157 120.800 1.00 2.30 ATOM 134 O LEU A 41 134.242 154.439 121.978 1.00 2.30 ATOM 135 CB LEU A 41 135.735 153.968 119.075 1.00 2.30 ATOM 136 CG LEU A 41 136.866 153.187 118.402 1.00 2.30 ATOM 137 CD1 LEU A 41 137.566 154.045 117.360 1.00 2.30 ATOM 138 CD2 LEU A 41 137.899 152.749 119.429 1.00 2.30 ATOM 139 N PRO A 42 132.880 154.708 120.215 1.00 1.55 ATOM 140 CA PRO A 42 132.018 155.608 120.995 1.00 1.55 ATOM 141 C PRO A 42 131.419 154.971 122.233 1.00 1.55 ATOM 142 O PRO A 42 131.203 155.674 123.225 1.00 1.55 ATOM 143 CB PRO A 42 130.959 156.037 119.978 1.00 1.55 ATOM 144 CG PRO A 42 131.668 155.945 118.645 1.00 1.55 ATOM 145 CD PRO A 42 132.507 154.688 118.793 1.00 1.55 ATOM 146 N THR A 43 131.140 153.666 122.216 1.00 1.35 ATOM 147 CA THR A 43 130.619 153.011 123.413 1.00 1.35 ATOM 148 C THR A 43 131.627 153.076 124.552 1.00 1.35 ATOM 149 O THR A 43 131.283 153.430 125.690 1.00 1.35 ATOM 150 CB THR A 43 130.258 151.540 123.139 1.00 1.35 ATOM 151 OG1 THR A 43 131.436 150.820 122.752 1.00 1.35 ATOM 152 CG2 THR A 43 129.232 151.442 122.020 1.00 1.35 ATOM 153 N ILE A 44 132.887 152.750 124.256 1.00 0.91 ATOM 154 CA ILE A 44 133.942 152.812 125.264 1.00 0.91 ATOM 155 C ILE A 44 134.112 154.242 125.757 1.00 0.91 ATOM 156 O ILE A 44 134.220 154.498 126.964 1.00 0.91 ATOM 157 CB ILE A 44 135.281 152.291 124.711 1.00 0.91 ATOM 158 CG1 ILE A 44 135.178 150.802 124.377 1.00 0.91 ATOM 159 CG2 ILE A 44 136.390 152.480 125.736 1.00 0.91 ATOM 160 CD1 ILE A 44 136.365 150.263 123.610 1.00 0.91 ATOM 161 N TYR A 45 134.125 155.197 124.822 1.00 0.06 ATOM 162 CA TYR A 45 134.318 156.594 125.196 1.00 0.06 ATOM 163 C TYR A 45 133.189 157.093 126.089 1.00 0.06 ATOM 164 O TYR A 45 133.433 157.824 127.051 1.00 0.06 ATOM 165 CB TYR A 45 134.425 157.473 123.949 1.00 0.06 ATOM 166 CG TYR A 45 134.699 158.930 124.247 1.00 0.06 ATOM 167 CD1 TYR A 45 135.983 159.367 124.542 1.00 0.06 ATOM 168 CD2 TYR A 45 133.671 159.865 124.232 1.00 0.06 ATOM 169 CE1 TYR A 45 136.241 160.695 124.817 1.00 0.06 ATOM 170 CE2 TYR A 45 133.910 161.197 124.503 1.00 0.06 ATOM 171 CZ TYR A 45 135.197 161.612 124.795 1.00 0.06 ATOM 172 OH TYR A 45 135.446 162.936 125.067 1.00 0.06 ATOM 173 N SER A 46 131.946 156.705 125.794 1.00 0.13 ATOM 174 CA SER A 46 130.814 157.161 126.594 1.00 0.13 ATOM 175 C SER A 46 130.804 156.516 127.973 1.00 0.13 ATOM 176 O SER A 46 130.508 157.184 128.976 1.00 0.13 ATOM 177 CB SER A 46 129.496 156.868 125.874 1.00 0.13 ATOM 178 OG SER A 46 129.319 155.476 125.682 1.00 0.13 ATOM 179 N ILE A 47 131.117 155.220 128.051 1.00 0.71 ATOM 180 CA ILE A 47 131.201 154.574 129.356 1.00 0.71 ATOM 181 C ILE A 47 132.269 155.248 130.205 1.00 0.71 ATOM 182 O ILE A 47 132.067 155.511 131.400 1.00 0.71 ATOM 183 CB ILE A 47 131.515 153.073 129.223 1.00 0.71 ATOM 184 CG1 ILE A 47 130.362 152.347 128.525 1.00 0.71 ATOM 185 CG2 ILE A 47 131.719 152.447 130.594 1.00 0.71 ATOM 186 CD1 ILE A 47 130.683 150.920 128.139 1.00 0.71 ATOM 187 N ILE A 48 133.418 155.557 129.596 1.00 1.19 ATOM 188 CA ILE A 48 134.489 156.210 130.337 1.00 1.19 ATOM 189 C ILE A 48 134.081 157.624 130.742 1.00 1.19 ATOM 190 O ILE A 48 134.322 158.045 131.875 1.00 1.19 ATOM 191 CB ILE A 48 135.789 156.270 129.514 1.00 1.19 ATOM 192 CG1 ILE A 48 136.324 154.859 129.259 1.00 1.19 ATOM 193 CG2 ILE A 48 136.854 157.062 130.257 1.00 1.19 ATOM 194 CD1 ILE A 48 137.460 154.807 128.262 1.00 1.19 ATOM 195 N PHE A 49 133.452 158.369 129.836 1.00 0.49 ATOM 196 CA PHE A 49 132.841 159.654 130.148 1.00 0.49 ATOM 197 C PHE A 49 132.074 159.572 131.458 1.00 0.49 ATOM 198 O PHE A 49 132.434 160.230 132.444 1.00 0.49 ATOM 199 CB PHE A 49 131.918 160.098 129.012 1.00 0.49 ATOM 200 CG PHE A 49 131.302 161.451 129.226 1.00 0.49 ATOM 201 CD1 PHE A 49 132.020 162.604 128.962 1.00 0.49 ATOM 202 CD2 PHE A 49 130.004 161.573 129.689 1.00 0.49 ATOM 203 CE1 PHE A 49 131.455 163.850 129.159 1.00 0.49 ATOM 204 CE2 PHE A 49 129.435 162.816 129.888 1.00 0.49 ATOM 205 CZ PHE A 49 130.161 163.956 129.621 1.00 0.49 ATOM 206 N LEU A 50 131.039 158.731 131.482 1.00 0.65 ATOM 207 CA LEU A 50 130.144 158.697 132.637 1.00 0.65 ATOM 208 C LEU A 50 130.883 158.271 133.901 1.00 0.65 ATOM 209 O LEU A 50 130.837 158.967 134.929 1.00 0.65 ATOM 210 CB LEU A 50 128.968 157.755 132.376 1.00 0.65 ATOM 211 CG LEU A 50 128.007 158.163 131.256 1.00 0.65 ATOM 212 CD1 LEU A 50 126.977 157.072 131.008 1.00 0.65 ATOM 213 CD2 LEU A 50 127.267 159.439 131.623 1.00 0.65 ATOM 214 N THR A 51 131.587 157.135 133.839 1.00 1.75 ATOM 215 CA THR A 51 132.212 156.591 135.041 1.00 1.75 ATOM 216 C THR A 51 133.278 157.534 135.586 1.00 1.75 ATOM 217 O THR A 51 133.316 157.814 136.791 1.00 1.75 ATOM 218 CB THR A 51 132.848 155.215 134.772 1.00 1.75 ATOM 219 OG1 THR A 51 133.885 155.348 133.791 1.00 1.75 ATOM 220 CG2 THR A 51 131.805 154.236 134.256 1.00 1.75 ATOM 221 N GLY A 52 134.152 158.035 134.712 1.00 2.25 ATOM 222 CA GLY A 52 135.210 158.919 135.158 1.00 2.25 ATOM 223 C GLY A 52 134.682 160.213 135.737 1.00 2.25 ATOM 224 O GLY A 52 135.130 160.652 136.797 1.00 2.25 ATOM 225 N ILE A 53 133.715 160.841 135.060 1.00 1.12 ATOM 226 CA ILE A 53 133.190 162.102 135.575 1.00 1.12 ATOM 227 C ILE A 53 132.580 161.895 136.953 1.00 1.12 ATOM 228 O ILE A 53 132.910 162.612 137.905 1.00 1.12 ATOM 229 CB ILE A 53 132.135 162.703 134.628 1.00 1.12 ATOM 230 CG1 ILE A 53 132.775 163.087 133.292 1.00 1.12 ATOM 231 CG2 ILE A 53 131.514 163.948 135.242 1.00 1.12 ATOM 232 CD1 ILE A 53 131.775 163.462 132.221 1.00 1.12 ATOM 233 N VAL A 54 131.723 160.879 137.101 1.00 2.36 ATOM 234 CA VAL A 54 131.054 160.682 138.384 1.00 2.36 ATOM 235 C VAL A 54 132.069 160.367 139.479 1.00 2.36 ATOM 236 O VAL A 54 132.068 160.989 140.550 1.00 2.36 ATOM 237 CB VAL A 54 130.015 159.549 138.310 1.00 2.36 ATOM 238 CG1 VAL A 54 129.420 159.279 139.684 1.00 2.36 ATOM 239 CG2 VAL A 54 128.884 159.923 137.363 1.00 2.36 ATOM 240 N GLY A 55 132.966 159.412 139.218 1.00 3.45 ATOM 241 CA GLY A 55 133.906 158.997 140.249 1.00 3.45 ATOM 242 C GLY A 55 134.868 160.097 140.650 1.00 3.45 ATOM 243 O GLY A 55 135.091 160.338 141.839 1.00 3.45 ATOM 244 N ASN A 56 135.453 160.781 139.664 1.00 3.30 ATOM 245 CA ASN A 56 136.418 161.829 139.964 1.00 3.30 ATOM 246 C ASN A 56 135.754 163.015 140.648 1.00 3.30 ATOM 247 O ASN A 56 136.323 163.592 141.582 1.00 3.30 ATOM 248 CB ASN A 56 137.124 162.289 138.687 1.00 3.30 ATOM 249 CG ASN A 56 138.273 163.238 138.966 1.00 3.30 ATOM 250 OD1 ASN A 56 138.076 164.318 139.524 1.00 3.30 ATOM 251 ND2 ASN A 56 139.476 162.838 138.579 1.00 3.30 ATOM 252 N GLY A 57 134.550 163.399 140.209 1.00 2.79 ATOM 253 CA GLY A 57 133.843 164.465 140.895 1.00 2.79 ATOM 254 C GLY A 57 133.545 164.122 142.340 1.00 2.79 ATOM 255 O GLY A 57 133.744 164.948 143.236 1.00 2.79 ATOM 256 N LEU A 58 133.078 162.896 142.593 1.00 4.94 ATOM 257 CA LEU A 58 132.791 162.500 143.967 1.00 4.94 ATOM 258 C LEU A 58 134.059 162.470 144.811 1.00 4.94 ATOM 259 O LEU A 58 134.051 162.904 145.970 1.00 4.94 ATOM 260 CB LEU A 58 132.107 161.132 143.999 1.00 4.94 ATOM 261 CG LEU A 58 130.719 161.052 143.361 1.00 4.94 ATOM 262 CD1 LEU A 58 130.222 159.615 143.331 1.00 4.94 ATOM 263 CD2 LEU A 58 129.718 161.884 144.149 1.00 4.94 ATOM 264 N VAL A 59 135.161 161.967 144.248 1.00 5.43 ATOM 265 CA VAL A 59 136.417 161.910 144.994 1.00 5.43 ATOM 266 C VAL A 59 136.899 163.315 145.337 1.00 5.43 ATOM 267 O VAL A 59 137.313 163.583 146.472 1.00 5.43 ATOM 268 CB VAL A 59 137.511 161.171 144.201 1.00 5.43 ATOM 269 CG1 VAL A 59 138.839 161.232 144.941 1.00 5.43 ATOM 270 CG2 VAL A 59 137.134 159.710 144.008 1.00 5.43 ATOM 271 N ILE A 60 136.845 164.232 144.367 1.00 5.40 ATOM 272 CA ILE A 60 137.268 165.608 144.616 1.00 5.40 ATOM 273 C ILE A 60 136.398 166.242 145.692 1.00 5.40 ATOM 274 O ILE A 60 136.901 166.855 146.639 1.00 5.40 ATOM 275 CB ILE A 60 137.205 166.458 143.334 1.00 5.40 ATOM 276 CG1 ILE A 60 138.211 165.944 142.302 1.00 5.40 ATOM 277 CG2 ILE A 60 137.530 167.912 143.642 1.00 5.40 ATOM 278 CD1 ILE A 60 138.053 166.564 140.932 1.00 5.40 ATOM 279 N LEU A 61 135.077 166.075 145.580 1.00 8.56 ATOM 280 CA LEU A 61 134.168 166.671 146.553 1.00 8.56 ATOM 281 C LEU A 61 134.427 166.137 147.956 1.00 8.56 ATOM 282 O LEU A 61 134.422 166.901 148.928 1.00 8.56 ATOM 283 CB LEU A 61 132.713 166.413 146.156 1.00 8.56 ATOM 284 CG LEU A 61 132.240 167.066 144.855 1.00 8.56 ATOM 285 CD1 LEU A 61 130.831 166.610 144.507 1.00 8.56 ATOM 286 CD2 LEU A 61 132.230 168.580 144.987 1.00 8.56 ATOM 287 N VAL A 62 134.652 164.829 148.086 1.00 10.01 ATOM 288 CA VAL A 62 134.856 164.248 149.409 1.00 10.01 ATOM 289 C VAL A 62 136.205 164.667 149.987 1.00 10.01 ATOM 290 O VAL A 62 136.312 164.971 151.181 1.00 10.01 ATOM 291 CB VAL A 62 134.777 162.711 149.368 1.00 10.01 ATOM 292 CG1 VAL A 62 135.114 162.123 150.730 1.00 10.01 ATOM 293 CG2 VAL A 62 133.376 162.260 148.983 1.00 10.01 ATOM 294 N MET A 63 137.250 164.701 149.159 1.00 13.79 ATOM 295 CA MET A 63 138.606 164.901 149.664 1.00 13.79 ATOM 296 C MET A 63 138.973 166.378 149.801 1.00 13.79 ATOM 297 O MET A 63 139.331 166.833 150.891 1.00 13.79 ATOM 298 CB MET A 63 139.624 164.210 148.755 1.00 13.79 ATOM 299 CG MET A 63 139.651 164.747 147.332 1.00 13.79 ATOM 300 SD MET A 63 140.861 163.908 146.294 1.00 13.79 ATOM 301 CE MET A 63 142.385 164.626 146.902 1.00 13.79 ATOM 302 N GLY A 64 138.903 167.134 148.703 1.00 16.99 ATOM 303 CA GLY A 64 139.372 168.509 148.741 1.00 16.99 ATOM 304 C GLY A 64 138.438 169.433 149.501 1.00 16.99 ATOM 305 O GLY A 64 138.857 170.129 150.430 1.00 16.99 ATOM 306 N TYR A 65 137.159 169.455 149.114 1.00 19.27 ATOM 307 CA TYR A 65 136.218 170.394 149.719 1.00 19.27 ATOM 308 C TYR A 65 136.045 170.126 151.209 1.00 19.27 ATOM 309 O TYR A 65 136.016 171.064 152.016 1.00 19.27 ATOM 310 CB TYR A 65 134.862 170.323 149.014 1.00 19.27 ATOM 311 CG TYR A 65 134.898 170.771 147.570 1.00 19.27 ATOM 312 CD1 TYR A 65 134.781 172.115 147.239 1.00 19.27 ATOM 313 CD2 TYR A 65 135.047 169.849 146.543 1.00 19.27 ATOM 314 CE1 TYR A 65 134.813 172.533 145.924 1.00 19.27 ATOM 315 CE2 TYR A 65 135.081 170.248 145.220 1.00 19.27 ATOM 316 CZ TYR A 65 134.965 171.591 144.913 1.00 19.27 ATOM 317 OH TYR A 65 134.997 172.000 143.600 1.00 19.27 ATOM 318 N GLN A 66 135.929 168.863 151.596 1.00 20.24 ATOM 319 CA GLN A 66 135.802 168.504 152.998 1.00 20.24 ATOM 320 C GLN A 66 137.183 168.169 153.559 1.00 20.24 ATOM 321 O GLN A 66 138.209 168.365 152.901 1.00 20.24 ATOM 322 CB GLN A 66 134.838 167.328 153.165 1.00 20.24 ATOM 323 CG GLN A 66 133.404 167.641 152.772 1.00 20.24 ATOM 324 CD GLN A 66 133.156 167.469 151.285 1.00 20.24 ATOM 325 OE1 GLN A 66 134.062 167.112 150.533 1.00 20.24 ATOM 326 NE2 GLN A 66 131.924 167.721 150.860 1.00 20.24 ATOM 327 N LYS A 67 137.230 167.669 154.789 1.00 28.02 ATOM 328 CA LYS A 67 138.481 167.336 155.466 1.00 28.02 ATOM 329 C LYS A 67 138.540 165.822 155.641 1.00 28.02 ATOM 330 O LYS A 67 138.086 165.279 156.649 1.00 28.02 ATOM 331 CB LYS A 67 138.575 168.065 156.808 1.00 28.02 ATOM 332 CG LYS A 67 139.880 167.833 157.551 0.00 99.99 ATOM 333 CD LYS A 67 141.051 168.476 156.824 0.00 99.99 ATOM 334 CE LYS A 67 142.356 168.243 157.567 0.00 99.99 ATOM 335 NZ LYS A 67 142.726 166.801 157.602 0.00 99.99 ATOM 336 N LYS A 68 139.108 165.139 154.645 1.00 23.45 ATOM 337 CA LYS A 68 139.234 163.688 154.677 1.00 23.45 ATOM 338 C LYS A 68 140.643 163.213 154.340 1.00 23.45 ATOM 339 O LYS A 68 140.843 162.010 154.132 1.00 23.45 ATOM 340 CB LYS A 68 138.238 163.042 153.712 1.00 23.45 ATOM 341 CG LYS A 68 138.449 163.423 152.256 0.00 99.99 ATOM 342 CD LYS A 68 137.428 162.747 151.355 0.00 99.99 ATOM 343 CE LYS A 68 137.639 163.128 149.899 0.00 99.99 ATOM 344 NZ LYS A 68 136.645 162.473 149.003 0.00 99.99 ATOM 345 N LEU A 69 141.620 164.116 154.277 1.00 21.68 ATOM 346 CA LEU A 69 143.002 163.748 153.976 1.00 21.68 ATOM 347 C LEU A 69 143.690 163.386 155.284 1.00 21.68 ATOM 348 O LEU A 69 144.228 164.241 155.988 1.00 21.68 ATOM 349 CB LEU A 69 143.717 164.893 153.257 1.00 21.68 ATOM 350 CG LEU A 69 143.188 165.257 151.868 1.00 21.68 ATOM 351 CD1 LEU A 69 143.888 166.497 151.334 1.00 21.68 ATOM 352 CD2 LEU A 69 143.425 164.119 150.888 1.00 21.68 ATOM 353 N ARG A 70 143.674 162.096 155.615 1.00 26.57 ATOM 354 CA ARG A 70 144.351 161.614 156.813 1.00 26.57 ATOM 355 C ARG A 70 145.791 161.201 156.533 1.00 26.57 ATOM 356 O ARG A 70 146.677 161.459 157.353 1.00 26.57 ATOM 357 CB ARG A 70 143.589 160.436 157.422 1.00 26.57 ATOM 358 CG ARG A 70 142.180 160.777 157.877 1.00 26.57 ATOM 359 CD ARG A 70 142.199 161.717 159.071 1.00 26.57 ATOM 360 NE ARG A 70 140.852 162.057 159.522 1.00 26.57 ATOM 361 CZ ARG A 70 140.115 163.034 159.006 1.00 26.57 ATOM 362 NH1 ARG A 70 140.595 163.775 158.017 1.00 26.57 ATOM 363 NH2 ARG A 70 138.900 163.270 159.482 1.00 26.57 ATOM 364 N SER A 71 146.039 160.572 155.390 1.00 17.35 ATOM 365 CA SER A 71 147.366 160.124 155.008 1.00 17.35 ATOM 366 C SER A 71 147.971 161.100 154.001 1.00 17.35 ATOM 367 O SER A 71 147.403 162.156 153.705 1.00 17.35 ATOM 368 CB SER A 71 147.308 158.709 154.429 1.00 17.35 ATOM 369 OG SER A 71 146.516 158.672 153.254 1.00 17.35 ATOM 370 N MET A 72 149.139 160.749 153.465 1.00 14.00 ATOM 371 CA MET A 72 149.816 161.583 152.482 1.00 14.00 ATOM 372 C MET A 72 149.587 161.127 151.047 1.00 14.00 ATOM 373 O MET A 72 149.876 161.893 150.123 1.00 14.00 ATOM 374 CB MET A 72 151.320 161.623 152.758 1.00 14.00 ATOM 375 CG MET A 72 152.099 162.530 151.820 1.00 14.00 ATOM 376 SD MET A 72 153.866 162.549 152.176 1.00 14.00 ATOM 377 CE MET A 72 153.902 163.561 153.654 1.00 14.00 ATOM 378 N THR A 73 149.091 159.906 150.842 1.00 10.43 ATOM 379 CA THR A 73 148.759 159.448 149.499 1.00 10.43 ATOM 380 C THR A 73 147.492 160.105 148.967 1.00 10.43 ATOM 381 O THR A 73 147.291 160.148 147.747 1.00 10.43 ATOM 382 CB THR A 73 148.577 157.920 149.453 1.00 10.43 ATOM 383 OG1 THR A 73 147.485 157.540 150.302 1.00 10.43 ATOM 384 CG2 THR A 73 149.839 157.218 149.931 1.00 10.43 ATOM 385 N ASP A 74 146.644 160.623 149.856 1.00 13.58 ATOM 386 CA ASP A 74 145.382 161.214 149.433 1.00 13.58 ATOM 387 C ASP A 74 145.593 162.464 148.590 1.00 13.58 ATOM 388 O ASP A 74 144.817 162.719 147.666 1.00 13.58 ATOM 389 CB ASP A 74 144.514 161.551 150.647 1.00 13.58 ATOM 390 CG ASP A 74 144.083 160.319 151.416 1.00 13.58 ATOM 391 OD1 ASP A 74 143.405 159.454 150.820 1.00 13.58 ATOM 392 OD2 ASP A 74 144.423 160.216 152.613 1.00 13.58 ATOM 393 N LYS A 75 146.627 163.252 148.884 1.00 8.65 ATOM 394 CA LYS A 75 146.887 164.453 148.093 1.00 8.65 ATOM 395 C LYS A 75 147.302 164.104 146.668 1.00 8.65 ATOM 396 O LYS A 75 146.828 164.720 145.702 1.00 8.65 ATOM 397 CB LYS A 75 147.968 165.308 148.757 1.00 8.65 ATOM 398 CG LYS A 75 148.252 166.617 148.038 1.00 8.65 ATOM 399 CD LYS A 75 149.333 167.414 148.750 1.00 8.65 ATOM 400 CE LYS A 75 149.617 168.723 148.030 1.00 8.65 ATOM 401 NZ LYS A 75 150.192 168.498 146.675 1.00 8.65 ATOM 402 N TYR A 76 148.178 163.111 146.511 1.00 6.30 ATOM 403 CA TYR A 76 148.549 162.669 145.172 1.00 6.30 ATOM 404 C TYR A 76 147.351 162.071 144.447 1.00 6.30 ATOM 405 O TYR A 76 147.188 162.261 143.235 1.00 6.30 ATOM 406 CB TYR A 76 149.690 161.652 145.240 1.00 6.30 ATOM 407 CG TYR A 76 150.185 161.195 143.886 1.00 6.30 ATOM 408 CD1 TYR A 76 151.062 161.978 143.147 1.00 6.30 ATOM 409 CD2 TYR A 76 149.775 159.980 143.351 1.00 6.30 ATOM 410 CE1 TYR A 76 151.518 161.569 141.910 1.00 6.30 ATOM 411 CE2 TYR A 76 150.221 159.554 142.116 1.00 6.30 ATOM 412 CZ TYR A 76 151.094 160.349 141.396 1.00 6.30 ATOM 413 OH TYR A 76 151.544 159.934 140.165 1.00 6.30 ATOM 414 N ARG A 77 146.503 161.339 145.172 1.00 7.69 ATOM 415 CA ARG A 77 145.296 160.804 144.552 1.00 7.69 ATOM 416 C ARG A 77 144.345 161.917 144.126 1.00 7.69 ATOM 417 O ARG A 77 143.658 161.789 143.109 1.00 7.69 ATOM 418 CB ARG A 77 144.582 159.846 145.507 1.00 7.69 ATOM 419 CG ARG A 77 145.352 158.567 145.794 1.00 7.69 ATOM 420 CD ARG A 77 144.472 157.534 146.479 1.00 7.69 ATOM 421 NE ARG A 77 144.044 157.972 147.804 1.00 7.69 ATOM 422 CZ ARG A 77 144.762 157.811 148.911 1.00 7.69 ATOM 423 NH1 ARG A 77 145.948 157.222 148.854 1.00 7.69 ATOM 424 NH2 ARG A 77 144.290 158.242 150.074 1.00 7.69 ATOM 425 N LEU A 78 144.302 163.015 144.881 1.00 5.35 ATOM 426 CA LEU A 78 143.510 164.174 144.481 1.00 5.35 ATOM 427 C LEU A 78 144.056 164.805 143.204 1.00 5.35 ATOM 428 O LEU A 78 143.283 165.202 142.320 1.00 5.35 ATOM 429 CB LEU A 78 143.473 165.212 145.604 1.00 5.35 ATOM 430 CG LEU A 78 142.617 166.454 145.352 1.00 5.35 ATOM 431 CD1 LEU A 78 141.147 166.079 145.239 1.00 5.35 ATOM 432 CD2 LEU A 78 142.768 167.452 146.490 1.00 5.35 ATOM 433 N HIS A 79 145.381 164.915 143.094 1.00 5.01 ATOM 434 CA HIS A 79 145.972 165.412 141.850 1.00 5.01 ATOM 435 C HIS A 79 145.612 164.506 140.676 1.00 5.01 ATOM 436 O HIS A 79 145.260 164.983 139.583 1.00 5.01 ATOM 437 CB HIS A 79 147.492 165.524 141.986 1.00 5.01 ATOM 438 CG HIS A 79 148.166 166.094 140.777 1.00 5.01 ATOM 439 ND1 HIS A 79 147.914 167.367 140.315 1.00 5.01 ATOM 440 CD2 HIS A 79 149.083 165.565 139.935 1.00 5.01 ATOM 441 CE1 HIS A 79 148.648 167.595 139.240 1.00 5.01 ATOM 442 NE2 HIS A 79 149.367 166.519 138.989 1.00 5.01 ATOM 443 N LEU A 80 145.693 163.190 140.891 1.00 3.20 ATOM 444 CA LEU A 80 145.305 162.234 139.860 1.00 3.20 ATOM 445 C LEU A 80 143.847 162.417 139.462 1.00 3.20 ATOM 446 O LEU A 80 143.505 162.372 138.274 1.00 3.20 ATOM 447 CB LEU A 80 145.544 160.801 140.340 1.00 3.20 ATOM 448 CG LEU A 80 147.000 160.405 140.593 1.00 3.20 ATOM 449 CD1 LEU A 80 147.080 159.013 141.202 1.00 3.20 ATOM 450 CD2 LEU A 80 147.788 160.399 139.293 1.00 3.20 ATOM 451 N SER A 81 142.972 162.618 140.451 1.00 3.20 ATOM 452 CA SER A 81 141.555 162.811 140.174 1.00 3.20 ATOM 453 C SER A 81 141.322 164.063 139.343 1.00 3.20 ATOM 454 O SER A 81 140.503 164.056 138.421 1.00 3.20 ATOM 455 CB SER A 81 140.760 162.890 141.478 1.00 3.20 ATOM 456 OG SER A 81 141.172 163.998 142.260 1.00 3.20 ATOM 457 N VAL A 82 142.031 165.148 139.656 1.00 2.31 ATOM 458 CA VAL A 82 141.868 166.383 138.891 1.00 2.31 ATOM 459 C VAL A 82 142.271 166.168 137.436 1.00 2.31 ATOM 460 O VAL A 82 141.549 166.555 136.502 1.00 2.31 ATOM 461 CB VAL A 82 142.701 167.531 139.490 1.00 2.31 ATOM 462 CG1 VAL A 82 142.613 168.769 138.609 1.00 2.31 ATOM 463 CG2 VAL A 82 142.191 167.892 140.877 1.00 2.31 ATOM 464 N ALA A 83 143.429 165.534 137.219 1.00 2.56 ATOM 465 CA ALA A 83 143.882 165.306 135.848 1.00 2.56 ATOM 466 C ALA A 83 142.911 164.410 135.081 1.00 2.56 ATOM 467 O ALA A 83 142.566 164.691 133.919 1.00 2.56 ATOM 468 CB ALA A 83 145.287 164.685 135.840 1.00 2.56 ATOM 469 N ASP A 84 142.443 163.337 135.722 1.00 2.37 ATOM 470 CA ASP A 84 141.512 162.429 135.060 1.00 2.37 ATOM 471 C ASP A 84 140.182 163.113 134.771 1.00 2.37 ATOM 472 O ASP A 84 139.560 162.854 133.735 1.00 2.37 ATOM 473 CB ASP A 84 141.284 161.179 135.913 1.00 2.37 ATOM 474 CG ASP A 84 140.380 160.169 135.236 1.00 2.37 ATOM 475 OD1 ASP A 84 140.735 159.695 134.136 1.00 2.37 ATOM 476 OD2 ASP A 84 139.314 159.850 135.806 1.00 2.37 ATOM 477 N LEU A 85 139.725 163.982 135.677 1.00 1.50 ATOM 478 CA LEU A 85 138.487 164.719 135.447 1.00 1.50 ATOM 479 C LEU A 85 138.606 165.621 134.229 1.00 1.50 ATOM 480 O LEU A 85 137.692 165.679 133.397 1.00 1.50 ATOM 481 CB LEU A 85 138.118 165.544 136.681 1.00 1.50 ATOM 482 CG LEU A 85 137.774 164.756 137.947 1.00 1.50 ATOM 483 CD1 LEU A 85 137.571 165.695 139.126 1.00 1.50 ATOM 484 CD2 LEU A 85 136.495 163.958 137.750 1.00 1.50 ATOM 485 N LEU A 86 139.735 166.320 134.095 1.00 1.01 ATOM 486 CA LEU A 86 139.931 167.148 132.909 1.00 1.01 ATOM 487 C LEU A 86 139.919 166.304 131.638 1.00 1.01 ATOM 488 O LEU A 86 139.279 166.669 130.639 1.00 1.01 ATOM 489 CB LEU A 86 141.244 167.927 133.010 1.00 1.01 ATOM 490 CG LEU A 86 141.330 168.969 134.128 1.00 1.01 ATOM 491 CD1 LEU A 86 142.729 169.559 134.206 1.00 1.01 ATOM 492 CD2 LEU A 86 140.349 170.103 133.881 1.00 1.01 ATOM 493 N PHE A 87 140.598 165.154 131.662 1.00 0.50 ATOM 494 CA PHE A 87 140.633 164.324 130.459 1.00 0.50 ATOM 495 C PHE A 87 139.247 163.794 130.090 1.00 0.50 ATOM 496 O PHE A 87 138.852 163.819 128.915 1.00 0.50 ATOM 497 CB PHE A 87 141.601 163.154 130.643 1.00 0.50 ATOM 498 CG PHE A 87 141.748 162.291 129.424 1.00 0.50 ATOM 499 CD1 PHE A 87 142.569 162.678 128.378 1.00 0.50 ATOM 500 CD2 PHE A 87 141.067 161.091 129.319 1.00 0.50 ATOM 501 CE1 PHE A 87 142.704 161.885 127.255 1.00 0.50 ATOM 502 CE2 PHE A 87 141.199 160.296 128.197 1.00 0.50 ATOM 503 CZ PHE A 87 142.020 160.693 127.164 1.00 0.50 ATOM 504 N VAL A 88 138.492 163.303 131.078 1.00 0.53 ATOM 505 CA VAL A 88 137.177 162.748 130.770 1.00 0.53 ATOM 506 C VAL A 88 136.221 163.846 130.330 1.00 0.53 ATOM 507 O VAL A 88 135.294 163.592 129.552 1.00 0.53 ATOM 508 CB VAL A 88 136.581 162.005 131.980 1.00 0.53 ATOM 509 CG1 VAL A 88 135.163 161.543 131.677 1.00 0.53 ATOM 510 CG2 VAL A 88 137.421 160.784 132.322 1.00 0.53 ATOM 511 N ILE A 89 136.418 165.079 130.806 1.00 0.37 ATOM 512 CA ILE A 89 135.668 166.203 130.254 1.00 0.37 ATOM 513 C ILE A 89 136.001 166.384 128.779 1.00 0.37 ATOM 514 O ILE A 89 135.123 166.670 127.957 1.00 0.37 ATOM 515 CB ILE A 89 135.965 167.508 131.015 1.00 0.37 ATOM 516 CG1 ILE A 89 135.470 167.407 132.460 1.00 0.37 ATOM 517 CG2 ILE A 89 135.270 168.685 130.348 1.00 0.37 ATOM 518 CD1 ILE A 89 135.930 168.545 133.344 1.00 0.37 ATOM 519 N THR A 90 137.276 166.218 128.420 1.00 0.85 ATOM 520 CA THR A 90 137.671 166.357 127.018 1.00 0.85 ATOM 521 C THR A 90 137.085 165.250 126.135 1.00 0.85 ATOM 522 O THR A 90 136.795 165.487 124.957 1.00 0.85 ATOM 523 CB THR A 90 139.202 166.347 126.860 1.00 0.85 ATOM 524 OG1 THR A 90 139.725 165.092 127.315 1.00 0.85 ATOM 525 CG2 THR A 90 139.830 167.467 127.677 1.00 0.85 ATOM 526 N LEU A 91 136.863 164.064 126.700 1.00 1.18 ATOM 527 CA LEU A 91 136.573 162.866 125.901 1.00 1.18 ATOM 528 C LEU A 91 135.432 162.953 124.876 1.00 1.18 ATOM 529 O LEU A 91 135.572 162.340 123.800 1.00 1.18 ATOM 530 CB LEU A 91 136.251 161.679 126.811 1.00 1.18 ATOM 531 CG LEU A 91 137.389 161.183 127.706 1.00 1.18 ATOM 532 CD1 LEU A 91 136.894 160.104 128.657 1.00 1.18 ATOM 533 CD2 LEU A 91 138.514 160.596 126.867 1.00 1.18 ATOM 534 N PRO A 92 134.290 163.603 125.135 1.00 2.21 ATOM 535 CA PRO A 92 133.198 163.551 124.143 1.00 2.21 ATOM 536 C PRO A 92 133.590 164.048 122.762 1.00 2.21 ATOM 537 O PRO A 92 133.010 163.599 121.767 1.00 2.21 ATOM 538 CB PRO A 92 132.104 164.402 124.791 1.00 2.21 ATOM 539 CG PRO A 92 132.356 164.262 126.275 1.00 2.21 ATOM 540 CD PRO A 92 133.872 164.286 126.366 1.00 2.21 ATOM 541 N PHE A 93 134.556 164.963 122.664 1.00 5.03 ATOM 542 CA PHE A 93 135.063 165.348 121.351 1.00 5.03 ATOM 543 C PHE A 93 135.752 164.176 120.667 1.00 5.03 ATOM 544 O PHE A 93 135.609 163.985 119.453 1.00 5.03 ATOM 545 CB PHE A 93 136.027 166.529 121.474 1.00 5.03 ATOM 546 CG PHE A 93 135.379 167.792 121.962 1.00 5.03 ATOM 547 CD1 PHE A 93 134.744 168.649 121.079 1.00 5.03 ATOM 548 CD2 PHE A 93 135.400 168.126 123.305 1.00 5.03 ATOM 549 CE1 PHE A 93 134.147 169.811 121.528 1.00 5.03 ATOM 550 CE2 PHE A 93 134.806 169.288 123.757 1.00 5.03 ATOM 551 CZ PHE A 93 134.177 170.131 122.867 1.00 5.03 ATOM 552 N TRP A 94 136.499 163.371 121.430 1.00 3.45 ATOM 553 CA TRP A 94 137.055 162.136 120.887 1.00 3.45 ATOM 554 C TRP A 94 135.948 161.231 120.370 1.00 3.45 ATOM 555 O TRP A 94 136.051 160.659 119.277 1.00 3.45 ATOM 556 CB TRP A 94 137.885 161.410 121.947 1.00 3.45 ATOM 557 CG TRP A 94 139.106 162.166 122.374 1.00 3.45 ATOM 558 CD1 TRP A 94 139.221 162.996 123.451 1.00 3.45 ATOM 559 CD2 TRP A 94 140.386 162.159 121.729 1.00 3.45 ATOM 560 NE1 TRP A 94 140.494 163.510 123.521 1.00 3.45 ATOM 561 CE2 TRP A 94 141.229 163.009 122.473 1.00 3.45 ATOM 562 CE3 TRP A 94 140.899 161.518 120.599 1.00 3.45 ATOM 563 CZ2 TRP A 94 142.559 163.237 122.122 1.00 3.45 ATOM 564 CZ3 TRP A 94 142.218 161.743 120.252 1.00 3.45 ATOM 565 CH2 TRP A 94 143.038 162.596 121.010 1.00 3.45 ATOM 566 N ALA A 95 134.879 161.079 121.158 1.00 4.00 ATOM 567 CA ALA A 95 133.787 160.194 120.759 1.00 4.00 ATOM 568 C ALA A 95 133.123 160.672 119.473 1.00 4.00 ATOM 569 O ALA A 95 132.813 159.867 118.588 1.00 4.00 ATOM 570 CB ALA A 95 132.742 160.087 121.879 1.00 4.00 ATOM 571 N VAL A 96 132.895 161.980 119.354 1.00 6.19 ATOM 572 CA VAL A 96 132.283 162.528 118.146 1.00 6.19 ATOM 573 C VAL A 96 133.212 162.361 116.949 1.00 6.19 ATOM 574 O VAL A 96 132.769 162.020 115.847 1.00 6.19 ATOM 575 CB VAL A 96 131.933 164.017 118.317 1.00 6.19 ATOM 576 CG1 VAL A 96 131.412 164.597 117.010 1.00 6.19 ATOM 577 CG2 VAL A 96 130.860 164.193 119.382 1.00 6.19 ATOM 578 N ASP A 97 134.511 162.602 117.143 1.00 10.89 ATOM 579 CA ASP A 97 135.460 162.499 116.037 1.00 10.89 ATOM 580 C ASP A 97 135.567 161.063 115.541 1.00 10.89 ATOM 581 O ASP A 97 135.698 160.825 114.334 1.00 10.89 ATOM 582 CB ASP A 97 136.836 163.015 116.462 1.00 10.89 ATOM 583 CG ASP A 97 137.841 162.998 115.327 1.00 10.89 ATOM 584 OD1 ASP A 97 137.595 163.670 114.304 1.00 10.89 ATOM 585 OD2 ASP A 97 138.876 162.311 115.460 1.00 10.89 ATOM 586 N ALA A 98 135.500 160.092 116.455 1.00 8.70 ATOM 587 CA ALA A 98 135.691 158.695 116.075 1.00 8.70 ATOM 588 C ALA A 98 134.636 158.191 115.100 1.00 8.70 ATOM 589 O ALA A 98 134.867 157.181 114.430 1.00 8.70 ATOM 590 CB ALA A 98 135.696 157.793 117.318 1.00 8.70 ATOM 591 N VAL A 99 133.492 158.866 114.996 1.00 7.58 ATOM 592 CA VAL A 99 132.392 158.381 114.171 1.00 7.58 ATOM 593 C VAL A 99 132.577 158.811 112.722 1.00 7.58 ATOM 594 O VAL A 99 132.694 157.966 111.828 1.00 7.58 ATOM 595 CB VAL A 99 131.034 158.891 114.686 1.00 7.58 ATOM 596 CG1 VAL A 99 129.915 158.475 113.742 1.00 7.58 ATOM 597 CG2 VAL A 99 130.737 158.317 116.064 1.00 7.58 ATOM 598 N ALA A 100 132.602 160.120 112.468 1.00 14.25 ATOM 599 CA ALA A 100 132.624 160.623 111.102 1.00 14.25 ATOM 600 C ALA A 100 133.923 161.342 110.752 1.00 14.25 ATOM 601 O ALA A 100 134.641 160.900 109.850 1.00 14.25 ATOM 602 CB ALA A 100 131.442 161.573 110.857 1.00 14.25 ATOM 603 N ASN A 101 134.261 162.418 111.464 1.00 21.45 ATOM 604 CA ASN A 101 135.405 163.253 111.104 1.00 21.45 ATOM 605 C ASN A 101 135.614 164.374 112.113 1.00 21.45 ATOM 606 O ASN A 101 134.808 164.548 113.033 1.00 21.45 ATOM 607 CB ASN A 101 135.222 163.838 109.702 1.00 21.45 ATOM 608 CG ASN A 101 136.444 164.595 109.222 1.00 21.45 ATOM 609 OD1 ASN A 101 137.275 165.023 110.023 1.00 21.45 ATOM 610 ND2 ASN A 101 136.558 164.759 107.910 1.00 21.45 ATOM 611 N TRP A 102 136.689 165.140 111.947 1.00 22.50 ATOM 612 CA TRP A 102 136.922 166.361 112.716 1.00 22.50 ATOM 613 C TRP A 102 136.782 167.540 111.761 1.00 22.50 ATOM 614 O TRP A 102 137.718 167.871 111.026 1.00 22.50 ATOM 615 CB TRP A 102 138.299 166.321 113.381 1.00 22.50 ATOM 616 CG TRP A 102 138.582 167.511 114.246 1.00 22.50 ATOM 617 CD1 TRP A 102 139.405 168.560 113.954 1.00 22.50 ATOM 618 CD2 TRP A 102 138.038 167.771 115.548 1.00 22.50 ATOM 619 NE1 TRP A 102 139.410 169.461 114.991 1.00 22.50 ATOM 620 CE2 TRP A 102 138.579 168.997 115.983 1.00 22.50 ATOM 621 CE3 TRP A 102 137.151 167.087 116.382 1.00 22.50 ATOM 622 CZ2 TRP A 102 138.260 169.556 117.220 1.00 22.50 ATOM 623 CZ3 TRP A 102 136.837 167.642 117.608 1.00 22.50 ATOM 624 CH2 TRP A 102 137.387 168.867 118.020 1.00 22.50 ATOM 625 N TYR A 103 135.630 168.206 111.806 1.00 24.12 ATOM 626 CA TYR A 103 135.380 169.352 110.933 1.00 24.12 ATOM 627 C TYR A 103 134.683 170.470 111.695 1.00 24.12 ATOM 628 O TYR A 103 133.993 171.293 111.096 1.00 24.12 ATOM 629 CB TYR A 103 134.543 168.932 109.723 1.00 24.12 ATOM 630 CG TYR A 103 135.243 167.958 108.802 1.00 24.12 ATOM 631 CD1 TYR A 103 136.101 168.410 107.807 1.00 24.12 ATOM 632 CD2 TYR A 103 135.045 166.589 108.930 1.00 24.12 ATOM 633 CE1 TYR A 103 136.744 167.528 106.962 1.00 24.12 ATOM 634 CE2 TYR A 103 135.680 165.691 108.093 1.00 24.12 ATOM 635 CZ TYR A 103 136.530 166.163 107.111 1.00 24.12 ATOM 636 OH TYR A 103 137.167 165.278 106.272 1.00 24.12 ATOM 637 N PHE A 104 134.854 170.504 113.011 1.00 24.95 ATOM 638 CA PHE A 104 134.222 171.517 113.848 1.00 24.95 ATOM 639 C PHE A 104 135.245 172.411 114.543 1.00 24.95 ATOM 640 O PHE A 104 135.108 172.738 115.721 1.00 24.95 ATOM 641 CB PHE A 104 133.320 170.861 114.895 1.00 24.95 ATOM 642 CG PHE A 104 132.144 170.133 114.311 1.00 24.95 ATOM 643 CD1 PHE A 104 130.974 170.808 114.005 1.00 24.95 ATOM 644 CD2 PHE A 104 132.205 168.772 114.065 1.00 24.95 ATOM 645 CE1 PHE A 104 129.893 170.138 113.467 1.00 24.95 ATOM 646 CE2 PHE A 104 131.124 168.099 113.528 1.00 24.95 ATOM 647 CZ PHE A 104 129.967 168.784 113.229 1.00 24.95 ATOM 648 N GLY A 105 136.291 172.808 113.825 1.00 22.99 ATOM 649 CA GLY A 105 137.193 173.837 114.290 1.00 22.99 ATOM 650 C GLY A 105 138.644 173.444 114.129 1.00 22.99 ATOM 651 O GLY A 105 138.984 172.371 113.632 1.00 22.99 ATOM 652 N ASN A 106 139.512 174.357 114.558 1.00 18.30 ATOM 653 CA ASN A 106 140.959 174.178 114.575 1.00 18.30 ATOM 654 C ASN A 106 141.557 174.365 115.959 1.00 18.30 ATOM 655 O ASN A 106 142.466 173.627 116.340 1.00 18.30 ATOM 656 CB ASN A 106 141.630 175.146 113.600 1.00 18.30 ATOM 657 CG ASN A 106 143.132 174.951 113.525 1.00 18.30 ATOM 658 OD1 ASN A 106 143.635 173.849 113.733 1.00 18.30 ATOM 659 ND2 ASN A 106 143.853 176.025 113.225 1.00 18.30 ATOM 660 N PHE A 107 141.061 175.341 116.725 1.00 16.34 ATOM 661 CA PHE A 107 141.569 175.573 118.073 1.00 16.34 ATOM 662 C PHE A 107 141.153 174.460 119.027 1.00 16.34 ATOM 663 O PHE A 107 141.871 174.170 119.996 1.00 16.34 ATOM 664 CB PHE A 107 141.083 176.923 118.604 1.00 16.34 ATOM 665 CG PHE A 107 141.617 178.101 117.842 1.00 16.34 ATOM 666 CD1 PHE A 107 142.855 178.641 118.148 1.00 16.34 ATOM 667 CD2 PHE A 107 140.884 178.671 116.815 1.00 16.34 ATOM 668 CE1 PHE A 107 143.345 179.725 117.447 1.00 16.34 ATOM 669 CE2 PHE A 107 141.372 179.756 116.112 1.00 16.34 ATOM 670 CZ PHE A 107 142.605 180.283 116.428 1.00 16.34 ATOM 671 N LEU A 108 140.015 173.815 118.763 1.00 12.89 ATOM 672 CA LEU A 108 139.578 172.709 119.609 1.00 12.89 ATOM 673 C LEU A 108 140.514 171.512 119.502 1.00 12.89 ATOM 674 O LEU A 108 140.726 170.808 120.494 1.00 12.89 ATOM 675 CB LEU A 108 138.153 172.287 119.246 1.00 12.89 ATOM 676 CG LEU A 108 137.054 173.320 119.501 1.00 12.89 ATOM 677 CD1 LEU A 108 135.719 172.829 118.962 1.00 12.89 ATOM 678 CD2 LEU A 108 136.898 173.581 120.991 1.00 12.89 ATOM 679 N CYS A 109 141.076 171.263 118.319 1.00 12.77 ATOM 680 CA CYS A 109 142.057 170.190 118.170 1.00 12.77 ATOM 681 C CYS A 109 143.274 170.445 119.051 1.00 12.77 ATOM 682 O CYS A 109 143.738 169.547 119.773 1.00 12.77 ATOM 683 CB CYS A 109 142.480 170.050 116.707 1.00 12.77 ATOM 684 SG CYS A 109 143.640 168.681 116.385 1.00 12.77 ATOM 685 N LYS A 110 143.789 171.678 119.028 1.00 8.73 ATOM 686 CA LYS A 110 144.927 172.026 119.872 1.00 8.73 ATOM 687 C LYS A 110 144.582 171.881 121.346 1.00 8.73 ATOM 688 O LYS A 110 145.379 171.341 122.125 1.00 8.73 ATOM 689 CB LYS A 110 145.395 173.452 119.579 1.00 8.73 ATOM 690 CG LYS A 110 145.882 173.665 118.155 1.00 8.73 ATOM 691 CD LYS A 110 147.176 172.910 117.896 1.00 8.73 ATOM 692 CE LYS A 110 147.664 173.122 116.472 1.00 8.73 ATOM 693 NZ LYS A 110 146.723 172.546 115.471 1.00 8.73 ATOM 694 N ALA A 111 143.402 172.351 121.751 1.00 6.84 ATOM 695 CA ALA A 111 143.013 172.240 123.154 1.00 6.84 ATOM 696 C ALA A 111 142.925 170.779 123.586 1.00 6.84 ATOM 697 O ALA A 111 143.460 170.396 124.636 1.00 6.84 ATOM 698 CB ALA A 111 141.671 172.946 123.400 1.00 6.84 ATOM 699 N VAL A 112 142.261 169.950 122.780 1.00 5.93 ATOM 700 CA VAL A 112 142.099 168.540 123.120 1.00 5.93 ATOM 701 C VAL A 112 143.458 167.876 123.268 1.00 5.93 ATOM 702 O VAL A 112 143.709 167.145 124.238 1.00 5.93 ATOM 703 CB VAL A 112 141.272 167.795 122.056 1.00 5.93 ATOM 704 CG1 VAL A 112 141.221 166.306 122.367 1.00 5.93 ATOM 705 CG2 VAL A 112 139.847 168.327 122.020 1.00 5.93 ATOM 706 N HIS A 113 144.369 168.138 122.324 1.00 5.73 ATOM 707 CA HIS A 113 145.713 167.586 122.436 1.00 5.73 ATOM 708 C HIS A 113 146.422 168.084 123.692 1.00 5.73 ATOM 709 O HIS A 113 147.176 167.328 124.316 1.00 5.73 ATOM 710 CB HIS A 113 146.541 167.935 121.198 1.00 5.73 ATOM 711 CG HIS A 113 146.032 167.314 119.935 1.00 5.73 ATOM 712 ND1 HIS A 113 145.008 167.862 119.195 1.00 5.73 ATOM 713 CD2 HIS A 113 146.405 166.188 119.282 1.00 5.73 ATOM 714 CE1 HIS A 113 144.774 167.100 118.140 1.00 5.73 ATOM 715 NE2 HIS A 113 145.608 166.079 118.169 1.00 5.73 ATOM 716 N VAL A 114 146.181 169.336 124.086 1.00 3.55 ATOM 717 CA VAL A 114 146.871 169.892 125.248 1.00 3.55 ATOM 718 C VAL A 114 146.445 169.176 126.527 1.00 3.55 ATOM 719 O VAL A 114 147.292 168.745 127.319 1.00 3.55 ATOM 720 CB VAL A 114 146.601 171.401 125.396 1.00 3.55 ATOM 721 CG1 VAL A 114 147.226 171.931 126.677 1.00 3.55 ATOM 722 CG2 VAL A 114 147.192 172.165 124.220 1.00 3.55 ATOM 723 N ILE A 115 145.132 169.037 126.759 1.00 1.99 ATOM 724 CA ILE A 115 144.753 168.317 127.983 1.00 1.99 ATOM 725 C ILE A 115 145.131 166.841 127.896 1.00 1.99 ATOM 726 O ILE A 115 145.507 166.234 128.912 1.00 1.99 ATOM 727 CB ILE A 115 143.243 168.434 128.262 1.00 1.99 ATOM 728 CG1 ILE A 115 142.866 169.887 128.557 1.00 1.99 ATOM 729 CG2 ILE A 115 142.854 167.582 129.460 1.00 1.99 ATOM 730 CD1 ILE A 115 141.375 170.134 128.606 1.00 1.99 ATOM 731 N TYR A 116 145.051 166.236 126.707 1.00 1.80 ATOM 732 CA TYR A 116 145.504 164.856 126.561 1.00 1.80 ATOM 733 C TYR A 116 146.939 164.702 127.049 1.00 1.80 ATOM 734 O TYR A 116 147.231 163.852 127.901 1.00 1.80 ATOM 735 CB TYR A 116 145.388 164.405 125.104 1.00 1.80 ATOM 736 CG TYR A 116 143.966 164.345 124.592 1.00 1.80 ATOM 737 CD1 TYR A 116 143.182 163.217 124.801 1.00 1.80 ATOM 738 CD2 TYR A 116 143.412 165.415 123.903 1.00 1.80 ATOM 739 CE1 TYR A 116 141.883 163.154 124.337 1.00 1.80 ATOM 740 CE2 TYR A 116 142.113 165.370 123.431 1.00 1.80 ATOM 741 CZ TYR A 116 141.351 164.239 123.650 1.00 1.80 ATOM 742 OH TYR A 116 140.057 164.182 123.186 1.00 1.80 ATOM 743 N THR A 117 147.842 165.543 126.542 1.00 2.13 ATOM 744 CA THR A 117 149.249 165.438 126.911 1.00 2.13 ATOM 745 C THR A 117 149.466 165.759 128.385 1.00 2.13 ATOM 746 O THR A 117 150.281 165.110 129.053 1.00 2.13 ATOM 747 CB THR A 117 150.126 166.376 126.062 1.00 2.13 ATOM 748 OG1 THR A 117 149.738 167.736 126.291 1.00 2.13 ATOM 749 CG2 THR A 117 149.965 166.061 124.582 1.00 2.13 ATOM 750 N VAL A 118 148.744 166.753 128.915 1.00 1.26 ATOM 751 CA VAL A 118 148.901 167.111 130.325 1.00 1.26 ATOM 752 C VAL A 118 148.580 165.918 131.214 1.00 1.26 ATOM 753 O VAL A 118 149.372 165.539 132.086 1.00 1.26 ATOM 754 CB VAL A 118 147.998 168.297 130.710 1.00 1.26 ATOM 755 CG1 VAL A 118 148.086 168.572 132.203 1.00 1.26 ATOM 756 CG2 VAL A 118 148.424 169.554 129.964 1.00 1.26 ATOM 757 N ASN A 119 147.419 165.294 130.994 1.00 1.61 ATOM 758 CA ASN A 119 147.045 164.139 131.806 1.00 1.61 ATOM 759 C ASN A 119 148.021 162.988 131.607 1.00 1.61 ATOM 760 O ASN A 119 148.447 162.342 132.580 1.00 1.61 ATOM 761 CB ASN A 119 145.622 163.687 131.472 1.00 1.61 ATOM 762 CG ASN A 119 145.113 162.617 132.417 1.00 1.61 ATOM 763 OD1 ASN A 119 145.687 161.531 132.508 1.00 1.61 ATOM 764 ND2 ASN A 119 144.034 162.921 133.126 1.00 1.61 ATOM 765 N LEU A 120 148.406 162.735 130.351 1.00 1.59 ATOM 766 CA LEU A 120 149.247 161.588 130.032 1.00 1.59 ATOM 767 C LEU A 120 150.606 161.688 130.710 1.00 1.59 ATOM 768 O LEU A 120 151.122 160.692 131.230 1.00 1.59 ATOM 769 CB LEU A 120 149.427 161.460 128.518 1.00 1.59 ATOM 770 CG LEU A 120 148.165 161.149 127.709 1.00 1.59 ATOM 771 CD1 LEU A 120 148.459 161.194 126.218 1.00 1.59 ATOM 772 CD2 LEU A 120 147.639 159.763 128.048 1.00 1.59 ATOM 773 N TYR A 121 151.204 162.878 130.724 1.00 1.98 ATOM 774 CA TYR A 121 152.509 163.043 131.346 1.00 1.98 ATOM 775 C TYR A 121 152.437 163.394 132.824 1.00 1.98 ATOM 776 O TYR A 121 153.478 163.402 133.486 1.00 1.98 ATOM 777 CB TYR A 121 153.316 164.122 130.621 1.00 1.98 ATOM 778 CG TYR A 121 152.683 165.495 130.666 1.00 1.98 ATOM 779 CD1 TYR A 121 152.973 166.379 131.696 1.00 1.98 ATOM 780 CD2 TYR A 121 151.796 165.901 129.677 1.00 1.98 ATOM 781 CE1 TYR A 121 152.400 167.633 131.745 1.00 1.98 ATOM 782 CE2 TYR A 121 151.212 167.153 129.709 1.00 1.98 ATOM 783 CZ TYR A 121 151.516 168.019 130.744 1.00 1.98 ATOM 784 OH TYR A 121 150.939 169.266 130.785 1.00 1.98 ATOM 785 N SER A 122 151.254 163.682 133.364 1.00 1.98 ATOM 786 CA SER A 122 151.147 163.978 134.786 1.00 1.98 ATOM 787 C SER A 122 150.796 162.770 135.638 1.00 1.98 ATOM 788 O SER A 122 151.249 162.686 136.787 1.00 1.98 ATOM 789 CB SER A 122 150.103 165.070 135.029 1.00 1.98 ATOM 790 OG SER A 122 148.818 164.649 134.607 1.00 1.98 ATOM 791 N SER A 123 150.000 161.831 135.114 1.00 1.33 ATOM 792 CA SER A 123 149.599 160.684 135.926 1.00 1.33 ATOM 793 C SER A 123 150.796 159.825 136.327 1.00 1.33 ATOM 794 O SER A 123 150.905 159.395 137.486 1.00 1.33 ATOM 795 CB SER A 123 148.576 159.828 135.177 1.00 1.33 ATOM 796 OG SER A 123 149.129 159.303 133.982 1.00 1.33 ATOM 797 N VAL A 124 151.713 159.572 135.390 1.00 0.95 ATOM 798 CA VAL A 124 152.877 158.740 135.688 1.00 0.95 ATOM 799 C VAL A 124 153.775 159.413 136.718 1.00 0.95 ATOM 800 O VAL A 124 154.321 158.754 137.610 1.00 0.95 ATOM 801 CB VAL A 124 153.695 158.439 134.419 1.00 0.95 ATOM 802 CG1 VAL A 124 154.965 157.678 134.770 1.00 0.95 ATOM 803 CG2 VAL A 124 152.882 157.596 133.448 1.00 0.95 ATOM 804 N LEU A 125 153.958 160.730 136.604 1.00 1.06 ATOM 805 CA LEU A 125 154.785 161.439 137.573 1.00 1.06 ATOM 806 C LEU A 125 154.143 161.434 138.955 1.00 1.06 ATOM 807 O LEU A 125 154.843 161.331 139.969 1.00 1.06 ATOM 808 CB LEU A 125 155.034 162.877 137.115 1.00 1.06 ATOM 809 CG LEU A 125 155.851 163.048 135.832 1.00 1.06 ATOM 810 CD1 LEU A 125 155.897 164.510 135.415 1.00 1.06 ATOM 811 CD2 LEU A 125 157.279 162.568 136.037 1.00 1.06 ATOM 812 N ILE A 126 152.813 161.530 139.017 1.00 1.93 ATOM 813 CA ILE A 126 152.139 161.422 140.309 1.00 1.93 ATOM 814 C ILE A 126 152.363 160.040 140.914 1.00 1.93 ATOM 815 O ILE A 126 152.604 159.902 142.120 1.00 1.93 ATOM 816 CB ILE A 126 150.628 161.688 140.181 1.00 1.93 ATOM 817 CG1 ILE A 126 150.375 163.135 139.753 1.00 1.93 ATOM 818 CG2 ILE A 126 149.930 161.450 141.511 1.00 1.93 ATOM 819 CD1 ILE A 126 148.939 163.418 139.372 1.00 1.93 ATOM 820 N LEU A 127 152.292 158.994 140.083 1.00 1.39 ATOM 821 CA LEU A 127 152.556 157.643 140.580 1.00 1.39 ATOM 822 C LEU A 127 153.985 157.508 141.096 1.00 1.39 ATOM 823 O LEU A 127 154.226 156.884 142.138 1.00 1.39 ATOM 824 CB LEU A 127 152.296 156.608 139.484 1.00 1.39 ATOM 825 CG LEU A 127 150.850 156.480 139.001 1.00 1.39 ATOM 826 CD1 LEU A 127 150.761 155.529 137.818 1.00 1.39 ATOM 827 CD2 LEU A 127 149.960 155.942 140.111 1.00 1.39 ATOM 828 N ALA A 128 154.949 158.079 140.369 1.00 1.41 ATOM 829 CA ALA A 128 156.338 158.035 140.813 1.00 1.41 ATOM 830 C ALA A 128 156.514 158.759 142.139 1.00 1.41 ATOM 831 O ALA A 128 157.286 158.318 142.999 1.00 1.41 ATOM 832 CB ALA A 128 157.264 158.646 139.751 1.00 1.41 ATOM 833 N PHE A 129 155.812 159.879 142.325 1.00 2.90 ATOM 834 CA PHE A 129 155.884 160.585 143.599 1.00 2.90 ATOM 835 C PHE A 129 155.273 159.764 144.727 1.00 2.90 ATOM 836 O PHE A 129 155.773 159.782 145.857 1.00 2.90 ATOM 837 CB PHE A 129 155.182 161.941 143.501 1.00 2.90 ATOM 838 CG PHE A 129 155.273 162.762 144.754 1.00 2.90 ATOM 839 CD1 PHE A 129 156.418 163.485 145.044 1.00 2.90 ATOM 840 CD2 PHE A 129 154.216 162.815 145.644 1.00 2.90 ATOM 841 CE1 PHE A 129 156.503 164.242 146.198 1.00 2.90 ATOM 842 CE2 PHE A 129 154.298 163.569 146.799 1.00 2.90 ATOM 843 CZ PHE A 129 155.441 164.284 147.075 1.00 2.90 ATOM 844 N ILE A 130 154.184 159.041 144.445 1.00 2.54 ATOM 845 CA ILE A 130 153.609 158.153 145.456 1.00 2.54 ATOM 846 C ILE A 130 154.618 157.084 145.857 1.00 2.54 ATOM 847 O ILE A 130 154.797 156.785 147.048 1.00 2.54 ATOM 848 CB ILE A 130 152.320 157.481 144.949 1.00 2.54 ATOM 849 CG1 ILE A 130 151.229 158.529 144.715 1.00 2.54 ATOM 850 CG2 ILE A 130 151.809 156.472 145.966 1.00 2.54 ATOM 851 CD1 ILE A 130 150.012 157.993 143.994 1.00 2.54 ATOM 852 N SER A 131 155.293 156.493 144.868 1.00 3.15 ATOM 853 CA SER A 131 156.305 155.480 145.155 1.00 3.15 ATOM 854 C SER A 131 157.453 156.055 145.976 1.00 3.15 ATOM 855 O SER A 131 157.938 155.416 146.919 1.00 3.15 ATOM 856 CB SER A 131 156.843 154.877 143.856 1.00 3.15 ATOM 857 OG SER A 131 157.475 155.863 143.060 1.00 3.15 ATOM 858 N LEU A 132 157.904 157.263 145.630 1.00 3.78 ATOM 859 CA LEU A 132 158.977 157.905 146.383 1.00 3.78 ATOM 860 C LEU A 132 158.559 158.172 147.824 1.00 3.78 ATOM 861 O LEU A 132 159.353 157.990 148.754 1.00 3.78 ATOM 862 CB LEU A 132 159.398 159.212 145.708 1.00 3.78 ATOM 863 CG LEU A 132 160.031 159.086 144.321 1.00 3.78 ATOM 864 CD1 LEU A 132 160.264 160.459 143.709 1.00 3.78 ATOM 865 CD2 LEU A 132 161.370 158.370 144.405 1.00 3.78 ATOM 866 N ASP A 133 157.318 158.619 148.026 1.00 7.71 ATOM 867 CA ASP A 133 156.833 158.843 149.381 1.00 7.71 ATOM 868 C ASP A 133 156.782 157.540 150.166 1.00 7.71 ATOM 869 O ASP A 133 157.124 157.513 151.353 1.00 7.71 ATOM 870 CB ASP A 133 155.451 159.498 149.354 1.00 7.71 ATOM 871 CG ASP A 133 154.931 159.819 150.741 1.00 7.71 ATOM 872 OD1 ASP A 133 155.593 160.597 151.459 1.00 7.71 ATOM 873 OD2 ASP A 133 153.859 159.293 151.111 1.00 7.71 ATOM 874 N ARG A 134 156.352 156.451 149.524 1.00 7.82 ATOM 875 CA ARG A 134 156.345 155.156 150.203 1.00 7.82 ATOM 876 C ARG A 134 157.754 154.742 150.604 1.00 7.82 ATOM 877 O ARG A 134 157.976 154.248 151.720 1.00 7.82 ATOM 878 CB ARG A 134 155.714 154.086 149.310 1.00 7.82 ATOM 879 CG ARG A 134 156.462 153.844 148.009 1.00 7.82 ATOM 880 CD ARG A 134 155.781 152.771 147.174 1.00 7.82 ATOM 881 NE ARG A 134 156.487 152.525 145.919 1.00 7.82 ATOM 882 CZ ARG A 134 156.309 153.234 144.809 1.00 7.82 ATOM 883 NH1 ARG A 134 155.441 154.236 144.796 1.00 7.82 ATOM 884 NH2 ARG A 134 156.995 152.936 143.715 1.00 7.82 ATOM 885 N TYR A 135 158.723 154.935 149.705 1.00 7.75 ATOM 886 CA TYR A 135 160.107 154.593 150.013 1.00 7.75 ATOM 887 C TYR A 135 160.623 155.398 151.199 1.00 7.75 ATOM 888 O TYR A 135 161.227 154.844 152.125 1.00 7.75 ATOM 889 CB TYR A 135 161.000 154.823 148.793 1.00 7.75 ATOM 890 CG TYR A 135 160.686 153.918 147.623 1.00 7.75 ATOM 891 CD1 TYR A 135 161.235 152.644 147.541 1.00 7.75 ATOM 892 CD2 TYR A 135 159.842 154.339 146.604 1.00 7.75 ATOM 893 CE1 TYR A 135 160.953 151.811 146.477 1.00 7.75 ATOM 894 CE2 TYR A 135 159.548 153.519 145.531 1.00 7.75 ATOM 895 CZ TYR A 135 160.104 152.256 145.470 1.00 7.75 ATOM 896 OH TYR A 135 159.819 151.431 144.407 1.00 7.75 ATOM 897 N LEU A 136 160.383 156.712 151.193 1.00 8.20 ATOM 898 CA LEU A 136 160.845 157.544 152.300 1.00 8.20 ATOM 899 C LEU A 136 160.130 157.206 153.600 1.00 8.20 ATOM 900 O LEU A 136 160.715 157.340 154.678 1.00 8.20 ATOM 901 CB LEU A 136 160.651 159.026 151.974 1.00 8.20 ATOM 902 CG LEU A 136 161.478 159.578 150.810 1.00 8.20 ATOM 903 CD1 LEU A 136 161.081 161.014 150.503 1.00 8.20 ATOM 904 CD2 LEU A 136 162.960 159.557 151.148 1.00 8.20 ATOM 905 N ALA A 137 158.872 156.774 153.522 1.00 10.46 ATOM 906 CA ALA A 137 158.120 156.451 154.727 1.00 10.46 ATOM 907 C ALA A 137 158.542 155.121 155.332 1.00 10.46 ATOM 908 O ALA A 137 158.496 154.963 156.557 1.00 10.46 ATOM 909 CB ALA A 137 156.613 156.424 154.432 1.00 10.46 ATOM 910 N ILE A 138 158.940 154.158 154.507 1.00 10.75 ATOM 911 CA ILE A 138 159.270 152.827 155.010 1.00 10.75 ATOM 912 C ILE A 138 160.753 152.698 155.339 1.00 10.75 ATOM 913 O ILE A 138 161.119 152.256 156.431 1.00 10.75 ATOM 914 CB ILE A 138 158.890 151.731 153.997 1.00 10.75 ATOM 915 CG1 ILE A 138 157.373 151.687 153.804 1.00 10.75 ATOM 916 CG2 ILE A 138 159.354 150.368 154.488 1.00 10.75 ATOM 917 CD1 ILE A 138 156.929 150.808 152.656 1.00 10.75 ATOM 918 N VAL A 139 161.632 153.073 154.407 1.00 11.18 ATOM 919 CA VAL A 139 163.062 152.855 154.607 1.00 11.18 ATOM 920 C VAL A 139 163.615 153.786 155.682 1.00 11.18 ATOM 921 O VAL A 139 164.405 153.366 156.536 1.00 11.18 ATOM 922 CB VAL A 139 163.852 153.065 153.302 1.00 11.18 ATOM 923 CG1 VAL A 139 165.347 152.954 153.561 1.00 11.18 ATOM 924 CG2 VAL A 139 163.464 152.016 152.270 1.00 11.18 ATOM 925 N HIS A 140 163.203 155.053 155.672 1.00 16.14 ATOM 926 CA HIS A 140 163.753 156.038 156.595 1.00 16.14 ATOM 927 C HIS A 140 162.701 156.499 157.594 1.00 16.14 ATOM 928 O HIS A 140 162.570 157.698 157.858 1.00 16.14 ATOM 929 CB HIS A 140 164.314 157.237 155.828 1.00 16.14 ATOM 930 CG HIS A 140 164.962 158.265 156.702 1.00 16.14 ATOM 931 ND1 HIS A 140 164.244 159.215 157.394 1.00 16.14 ATOM 932 CD2 HIS A 140 166.264 158.489 156.998 1.00 16.14 ATOM 933 CE1 HIS A 140 165.077 159.981 158.076 1.00 16.14 ATOM 934 NE2 HIS A 140 166.307 159.563 157.854 1.00 16.14 ATOM 935 N ALA A 141 161.950 155.552 158.156 1.00 18.93 ATOM 936 CA ALA A 141 160.883 155.884 159.091 1.00 18.93 ATOM 937 C ALA A 141 161.394 156.467 160.400 1.00 18.93 ATOM 938 O ALA A 141 160.584 156.972 161.185 1.00 18.93 ATOM 939 CB ALA A 141 160.027 154.646 159.396 1.00 18.93 ATOM 940 N THR A 142 162.702 156.406 160.656 1.00 26.69 ATOM 941 CA THR A 142 163.265 156.884 161.913 1.00 26.69 ATOM 942 C THR A 142 162.943 158.354 162.150 1.00 26.69 ATOM 943 O THR A 142 162.216 158.689 163.089 1.00 26.69 ATOM 944 CB THR A 142 164.793 156.696 161.954 1.00 26.69 ATOM 945 OG1 THR A 142 165.400 157.467 160.909 1.00 26.69 ATOM 946 CG2 THR A 142 165.155 155.232 161.761 1.00 26.69 ATOM 947 N ASN A 143 163.480 159.240 161.311 1.00 27.35 ATOM 948 CA ASN A 143 163.200 160.674 161.393 1.00 27.35 ATOM 949 C ASN A 143 163.013 161.246 159.989 1.00 27.35 ATOM 950 O ASN A 143 163.960 161.721 159.355 1.00 27.35 ATOM 951 CB ASN A 143 164.327 161.399 162.131 1.00 27.35 ATOM 952 CG ASN A 143 165.660 161.280 161.419 1.00 27.35 ATOM 953 OD1 ASN A 143 165.807 160.497 160.481 1.00 27.35 ATOM 954 ND2 ASN A 143 166.638 162.060 161.862 1.00 27.35 ATOM 955 N SER A 144 161.773 161.222 159.506 1.00 26.12 ATOM 956 CA SER A 144 161.456 161.813 158.210 1.00 26.12 ATOM 957 C SER A 144 159.979 162.178 158.197 1.00 26.12 ATOM 958 O SER A 144 159.140 161.330 157.881 1.00 26.12 ATOM 959 CB SER A 144 161.807 160.845 157.079 1.00 26.12 ATOM 960 OG SER A 144 161.047 159.653 157.175 1.00 26.12 ATOM 961 N GLN A 145 159.663 163.422 158.552 1.00 27.33 ATOM 962 CA GLN A 145 158.318 163.947 158.347 1.00 27.33 ATOM 963 C GLN A 145 158.397 165.276 157.608 1.00 27.33 ATOM 964 O GLN A 145 157.589 165.556 156.716 1.00 27.33 ATOM 965 CB GLN A 145 157.595 164.106 159.686 1.00 27.33 ATOM 966 CG GLN A 145 157.332 162.796 160.409 1.00 27.33 ATOM 967 CD GLN A 145 158.515 162.344 161.245 1.00 27.33 ATOM 968 OE1 GLN A 145 159.547 163.013 161.290 1.00 27.33 ATOM 969 NE2 GLN A 145 158.365 161.207 161.912 1.00 27.33 ATOM 970 N ARG A 146 159.387 166.094 157.974 1.00 29.03 ATOM 971 CA ARG A 146 159.626 167.347 157.259 1.00 29.03 ATOM 972 C ARG A 146 160.036 167.107 155.812 1.00 29.03 ATOM 973 O ARG A 146 159.521 167.803 154.917 1.00 29.03 ATOM 974 CB ARG A 146 160.700 168.173 157.969 1.00 29.03 ATOM 975 CG ARG A 146 160.327 168.592 159.382 1.00 29.03 ATOM 976 CD ARG A 146 159.189 169.598 159.376 1.00 29.03 ATOM 977 NE ARG A 146 158.816 170.011 160.727 1.00 29.03 ATOM 978 CZ ARG A 146 157.852 170.883 161.003 1.00 29.03 ATOM 979 NH1 ARG A 146 157.156 171.434 160.019 1.00 29.03 ATOM 980 NH2 ARG A 146 157.585 171.198 162.262 1.00 29.03 ATOM 981 N PRO A 147 160.967 166.189 155.506 1.00 22.91 ATOM 982 CA PRO A 147 161.234 165.890 154.090 1.00 22.91 ATOM 983 C PRO A 147 159.992 165.459 153.335 1.00 22.91 ATOM 984 O PRO A 147 159.773 165.915 152.209 1.00 22.91 ATOM 985 CB PRO A 147 162.307 164.802 154.165 1.00 22.91 ATOM 986 CG PRO A 147 163.024 165.078 155.467 1.00 22.91 ATOM 987 CD PRO A 147 161.894 165.478 156.399 1.00 22.91 ATOM 988 N ARG A 148 159.150 164.614 153.939 1.00 20.48 ATOM 989 CA ARG A 148 157.951 164.161 153.241 1.00 20.48 ATOM 990 C ARG A 148 156.994 165.314 152.975 1.00 20.48 ATOM 991 O ARG A 148 156.463 165.437 151.868 1.00 20.48 ATOM 992 CB ARG A 148 157.243 163.069 154.045 1.00 20.48 ATOM 993 CG ARG A 148 158.025 161.770 154.150 1.00 20.48 ATOM 994 CD ARG A 148 157.266 160.731 154.960 1.00 20.48 ATOM 995 NE ARG A 148 158.004 159.478 155.072 1.00 20.48 ATOM 996 CZ ARG A 148 157.974 158.510 154.162 1.00 20.48 ATOM 997 NH1 ARG A 148 157.239 158.651 153.068 1.00 20.48 ATOM 998 NH2 ARG A 148 158.679 157.401 154.350 1.00 20.48 ATOM 999 N LYS A 149 156.772 166.177 153.969 1.00 21.43 ATOM 1000 CA LYS A 149 155.847 167.291 153.780 1.00 21.43 ATOM 1001 C LYS A 149 156.356 168.258 152.714 1.00 21.43 ATOM 1002 O LYS A 149 155.614 168.634 151.792 1.00 21.43 ATOM 1003 CB LYS A 149 155.625 168.033 155.099 1.00 21.43 ATOM 1004 CG LYS A 149 154.890 167.221 156.152 1.00 21.43 ATOM 1005 CD LYS A 149 154.703 168.016 157.434 1.00 21.43 ATOM 1006 CE LYS A 149 156.034 168.262 158.128 1.00 21.43 ATOM 1007 NZ LYS A 149 155.868 169.042 159.386 1.00 21.43 ATOM 1008 N LEU A 150 157.619 168.678 152.830 1.00 17.54 ATOM 1009 CA LEU A 150 158.172 169.625 151.870 1.00 17.54 ATOM 1010 C LEU A 150 158.180 169.037 150.466 1.00 17.54 ATOM 1011 O LEU A 150 157.772 169.698 149.497 1.00 17.54 ATOM 1012 CB LEU A 150 159.587 170.037 152.278 1.00 17.54 ATOM 1013 CG LEU A 150 159.715 170.819 153.588 1.00 17.54 ATOM 1014 CD1 LEU A 150 161.178 171.035 153.944 1.00 17.54 ATOM 1015 CD2 LEU A 150 159.050 172.181 153.466 1.00 17.54 ATOM 1016 N LEU A 151 158.660 167.805 150.344 1.00 15.33 ATOM 1017 CA LEU A 151 158.657 167.143 149.049 1.00 15.33 ATOM 1018 C LEU A 151 157.248 167.121 148.512 1.00 15.33 ATOM 1019 O LEU A 151 156.991 167.567 147.394 1.00 15.33 ATOM 1020 CB LEU A 151 159.228 165.729 149.169 1.00 15.33 ATOM 1021 CG LEU A 151 160.703 165.624 149.563 1.00 15.33 ATOM 1022 CD1 LEU A 151 161.097 164.172 149.787 1.00 15.33 ATOM 1023 CD2 LEU A 151 161.592 166.193 148.469 1.00 15.33 ATOM 1024 N ALA A 152 156.326 166.603 149.312 1.00 16.36 ATOM 1025 CA ALA A 152 154.941 166.508 148.877 1.00 16.36 ATOM 1026 C ALA A 152 154.451 167.807 148.268 1.00 16.36 ATOM 1027 O ALA A 152 154.150 167.849 147.088 1.00 16.36 ATOM 1028 CB ALA A 152 154.033 166.110 150.050 1.00 16.36 ATOM 1029 N GLU A 153 154.390 168.874 149.054 1.00 16.89 ATOM 1030 CA GLU A 153 153.831 170.132 148.561 1.00 16.89 ATOM 1031 C GLU A 153 154.630 170.686 147.383 1.00 16.89 ATOM 1032 O GLU A 153 154.189 170.633 146.219 1.00 16.89 ATOM 1033 CB GLU A 153 153.777 171.170 149.683 1.00 16.89 ATOM 1034 CG GLU A 153 152.831 170.810 150.817 1.00 16.89 ATOM 1035 CD GLU A 153 153.480 169.910 151.852 1.00 16.89 ATOM 1036 OE1 GLU A 153 154.669 169.570 151.681 1.00 16.89 ATOM 1037 OE2 GLU A 153 152.798 169.549 152.834 1.00 16.89 ATOM 1038 N LYS A 154 155.853 171.136 147.668 1.00 15.23 ATOM 1039 CA LYS A 154 156.534 171.978 146.695 1.00 15.23 ATOM 1040 C LYS A 154 156.988 171.171 145.490 1.00 15.23 ATOM 1041 O LYS A 154 156.817 171.606 144.340 1.00 15.23 ATOM 1042 CB LYS A 154 157.731 172.680 147.338 1.00 15.23 ATOM 1043 CG LYS A 154 158.461 173.638 146.412 1.00 15.23 ATOM 1044 CD LYS A 154 157.600 174.847 146.078 1.00 15.23 ATOM 1045 CE LYS A 154 158.330 175.804 145.151 1.00 15.23 ATOM 1046 NZ LYS A 154 158.594 175.195 143.818 1.00 15.23 ATOM 1047 N VAL A 155 157.573 169.998 145.725 1.00 12.03 ATOM 1048 CA VAL A 155 158.040 169.197 144.614 1.00 12.03 ATOM 1049 C VAL A 155 156.902 168.621 143.782 1.00 12.03 ATOM 1050 O VAL A 155 157.056 168.524 142.559 1.00 12.03 ATOM 1051 CB VAL A 155 158.924 168.031 145.092 1.00 12.03 ATOM 1052 CG1 VAL A 155 159.301 167.133 143.923 1.00 12.03 ATOM 1053 CG2 VAL A 155 160.204 168.557 145.725 1.00 12.03 ATOM 1054 N VAL A 156 155.749 168.262 144.374 1.00 10.72 ATOM 1055 CA VAL A 156 154.666 167.801 143.514 1.00 10.72 ATOM 1056 C VAL A 156 154.267 168.929 142.578 1.00 10.72 ATOM 1057 O VAL A 156 154.214 168.740 141.358 1.00 10.72 ATOM 1058 CB VAL A 156 153.452 167.334 144.337 1.00 10.72 ATOM 1059 CG1 VAL A 156 152.292 166.974 143.421 1.00 10.72 ATOM 1060 CG2 VAL A 156 153.809 166.107 145.164 1.00 10.72 ATOM 1061 N TYR A 157 154.120 170.151 143.120 1.00 10.80 ATOM 1062 CA TYR A 157 153.773 171.255 142.229 1.00 10.80 ATOM 1063 C TYR A 157 154.790 171.376 141.103 1.00 10.80 ATOM 1064 O TYR A 157 154.450 171.135 139.937 1.00 10.80 ATOM 1065 CB TYR A 157 153.684 172.567 143.011 1.00 10.80 ATOM 1066 CG TYR A 157 154.985 172.982 143.662 1.00 10.80 ATOM 1067 CD1 TYR A 157 155.896 173.782 142.986 1.00 10.80 ATOM 1068 CD2 TYR A 157 155.297 172.570 144.952 1.00 10.80 ATOM 1069 CE1 TYR A 157 157.085 174.165 143.573 1.00 10.80 ATOM 1070 CE2 TYR A 157 156.481 172.943 145.556 1.00 10.80 ATOM 1071 CZ TYR A 157 157.375 173.742 144.865 1.00 10.80 ATOM 1072 OH TYR A 157 158.558 174.118 145.457 1.00 10.80 ATOM 1073 N VAL A 158 156.031 171.720 141.406 1.00 10.99 ATOM 1074 CA VAL A 158 156.989 171.913 140.325 1.00 10.99 ATOM 1075 C VAL A 158 157.211 170.627 139.531 1.00 10.99 ATOM 1076 O VAL A 158 156.804 170.538 138.367 1.00 10.99 ATOM 1077 CB VAL A 158 158.346 172.410 140.856 1.00 10.99 ATOM 1078 CG1 VAL A 158 159.365 172.486 139.729 1.00 10.99 ATOM 1079 CG2 VAL A 158 158.204 173.795 141.469 1.00 10.99 ATOM 1080 N GLY A 159 157.804 169.616 140.157 1.00 10.02 ATOM 1081 CA GLY A 159 158.136 168.387 139.450 1.00 10.02 ATOM 1082 C GLY A 159 157.048 167.670 138.680 1.00 10.02 ATOM 1083 O GLY A 159 157.334 167.038 137.666 1.00 10.02 ATOM 1084 N VAL A 160 155.810 167.732 139.152 1.00 8.36 ATOM 1085 CA VAL A 160 154.739 166.990 138.492 1.00 8.36 ATOM 1086 C VAL A 160 153.998 167.822 137.452 1.00 8.36 ATOM 1087 O VAL A 160 153.394 167.271 136.531 1.00 8.36 ATOM 1088 CB VAL A 160 153.710 166.462 139.508 1.00 8.36 ATOM 1089 CG1 VAL A 160 152.543 165.801 138.790 1.00 8.36 ATOM 1090 CG2 VAL A 160 154.350 165.435 140.430 1.00 8.36 ATOM 1091 N TRP A 161 154.052 169.144 137.569 1.00 8.05 ATOM 1092 CA TRP A 161 153.269 169.977 136.654 1.00 8.05 ATOM 1093 C TRP A 161 154.096 170.691 135.592 1.00 8.05 ATOM 1094 O TRP A 161 153.840 170.533 134.401 1.00 8.05 ATOM 1095 CB TRP A 161 152.473 171.026 137.432 1.00 8.05 ATOM 1096 CG TRP A 161 153.334 171.984 138.198 1.00 8.05 ATOM 1097 CD1 TRP A 161 153.775 171.844 139.482 1.00 8.05 ATOM 1098 CD2 TRP A 161 153.857 173.232 137.725 1.00 8.05 ATOM 1099 NE1 TRP A 161 154.541 172.925 139.842 1.00 8.05 ATOM 1100 CE2 TRP A 161 154.607 173.793 138.778 1.00 8.05 ATOM 1101 CE3 TRP A 161 153.765 173.925 136.516 1.00 8.05 ATOM 1102 CZ2 TRP A 161 155.262 175.018 138.659 1.00 8.05 ATOM 1103 CZ3 TRP A 161 154.415 175.139 136.398 1.00 8.05 ATOM 1104 CH2 TRP A 161 155.156 175.678 137.464 1.00 8.05 ATOM 1105 N ILE A 162 155.082 171.474 136.008 1.00 7.49 ATOM 1106 CA ILE A 162 155.860 172.259 135.054 1.00 7.49 ATOM 1107 C ILE A 162 156.314 171.390 133.881 1.00 7.49 ATOM 1108 O ILE A 162 156.116 171.792 132.723 1.00 7.49 ATOM 1109 CB ILE A 162 157.091 172.899 135.721 1.00 7.49 ATOM 1110 CG1 ILE A 162 156.656 173.922 136.773 1.00 7.49 ATOM 1111 CG2 ILE A 162 157.951 173.608 134.686 1.00 7.49 ATOM 1112 CD1 ILE A 162 157.788 174.424 137.642 1.00 7.49 ATOM 1113 N PRO A 163 156.925 170.215 134.103 1.00 6.46 ATOM 1114 CA PRO A 163 157.344 169.401 132.948 1.00 6.46 ATOM 1115 C PRO A 163 156.197 168.985 132.046 1.00 6.46 ATOM 1116 O PRO A 163 156.390 168.853 130.830 1.00 6.46 ATOM 1117 CB PRO A 163 158.050 168.212 133.603 1.00 6.46 ATOM 1118 CG PRO A 163 158.576 168.767 134.907 1.00 6.46 ATOM 1119 CD PRO A 163 157.453 169.681 135.366 1.00 6.46 ATOM 1120 N ALA A 164 155.002 168.773 132.602 1.00 5.24 ATOM 1121 CA ALA A 164 153.851 168.444 131.768 1.00 5.24 ATOM 1122 C ALA A 164 153.556 169.565 130.779 1.00 5.24 ATOM 1123 O ALA A 164 153.360 169.322 129.585 1.00 5.24 ATOM 1124 CB ALA A 164 152.616 168.165 132.638 1.00 5.24 ATOM 1125 N LEU A 165 153.548 170.812 131.257 1.00 5.73 ATOM 1126 CA LEU A 165 153.337 171.945 130.359 1.00 5.73 ATOM 1127 C LEU A 165 154.480 172.073 129.358 1.00 5.73 ATOM 1128 O LEU A 165 154.257 172.387 128.179 1.00 5.73 ATOM 1129 CB LEU A 165 153.188 173.241 131.157 1.00 5.73 ATOM 1130 CG LEU A 165 151.962 173.340 132.068 1.00 5.73 ATOM 1131 CD1 LEU A 165 152.016 174.608 132.906 1.00 5.73 ATOM 1132 CD2 LEU A 165 150.684 173.369 131.245 1.00 5.73 ATOM 1133 N LEU A 166 155.713 171.840 129.809 1.00 5.50 ATOM 1134 CA LEU A 166 156.846 171.925 128.896 1.00 5.50 ATOM 1135 C LEU A 166 156.756 170.883 127.788 1.00 5.50 ATOM 1136 O LEU A 166 157.226 171.128 126.672 1.00 5.50 ATOM 1137 CB LEU A 166 158.162 171.760 129.658 1.00 5.50 ATOM 1138 CG LEU A 166 158.502 172.856 130.670 1.00 5.50 ATOM 1139 CD1 LEU A 166 159.753 172.494 131.455 1.00 5.50 ATOM 1140 CD2 LEU A 166 158.751 174.180 129.964 1.00 5.50 ATOM 1141 N LEU A 167 156.168 169.719 128.073 1.00 4.61 ATOM 1142 CA LEU A 167 155.995 168.716 127.025 1.00 4.61 ATOM 1143 C LEU A 167 154.716 168.945 126.225 1.00 4.61 ATOM 1144 O LEU A 167 154.549 168.353 125.153 1.00 4.61 ATOM 1145 CB LEU A 167 155.984 167.309 127.626 1.00 4.61 ATOM 1146 CG LEU A 167 157.284 166.843 128.285 1.00 4.61 ATOM 1147 CD1 LEU A 167 157.089 165.496 128.964 1.00 4.61 ATOM 1148 CD2 LEU A 167 158.387 166.696 127.249 1.00 4.61 ATOM 1149 N THR A 168 153.796 169.768 126.733 1.00 5.37 ATOM 1150 CA THR A 168 152.668 170.193 125.904 1.00 5.37 ATOM 1151 C THR A 168 153.054 171.341 124.986 1.00 5.37 ATOM 1152 O THR A 168 152.297 171.683 124.071 1.00 5.37 ATOM 1153 CB THR A 168 151.466 170.623 126.765 1.00 5.37 ATOM 1154 OG1 THR A 168 150.966 169.493 127.492 1.00 5.37 ATOM 1155 CG2 THR A 168 150.353 171.176 125.888 1.00 5.37 ATOM 1156 N ILE A 169 154.197 171.969 125.238 1.00 6.66 ATOM 1157 CA ILE A 169 154.692 173.051 124.383 1.00 6.66 ATOM 1158 C ILE A 169 154.702 172.643 122.909 1.00 6.66 ATOM 1159 O ILE A 169 154.253 173.432 122.064 1.00 6.66 ATOM 1160 CB ILE A 169 156.112 173.486 124.789 1.00 6.66 ATOM 1161 CG1 ILE A 169 156.101 174.099 126.191 1.00 6.66 ATOM 1162 CG2 ILE A 169 156.652 174.522 123.814 1.00 6.66 ATOM 1163 CD1 ILE A 169 157.480 174.336 126.766 1.00 6.66 ATOM 1164 N PRO A 170 155.193 171.444 122.530 1.00 8.26 ATOM 1165 CA PRO A 170 155.129 171.048 121.115 1.00 8.26 ATOM 1166 C PRO A 170 153.718 170.929 120.563 1.00 8.26 ATOM 1167 O PRO A 170 153.515 171.018 119.349 1.00 8.26 ATOM 1168 CB PRO A 170 155.885 169.718 121.095 1.00 8.26 ATOM 1169 CG PRO A 170 156.861 169.830 122.245 1.00 8.26 ATOM 1170 CD PRO A 170 156.047 170.539 123.314 1.00 8.26 ATOM 1171 N ASP A 171 152.734 170.707 121.440 1.00 9.18 ATOM 1172 CA ASP A 171 151.359 170.530 120.984 1.00 9.18 ATOM 1173 C ASP A 171 150.798 171.822 120.403 1.00 9.18 ATOM 1174 O ASP A 171 150.080 171.804 119.396 1.00 9.18 ATOM 1175 CB ASP A 171 150.472 170.042 122.131 1.00 9.18 ATOM 1176 CG ASP A 171 149.097 169.612 121.662 1.00 9.18 ATOM 1177 OD1 ASP A 171 148.610 170.171 120.657 1.00 9.18 ATOM 1178 OD2 ASP A 171 148.505 168.716 122.299 1.00 9.18 ATOM 1179 N PHE A 172 151.108 172.956 121.028 1.00 7.48 ATOM 1180 CA PHE A 172 150.648 174.249 120.536 1.00 7.48 ATOM 1181 C PHE A 172 151.183 174.510 119.137 1.00 7.48 ATOM 1182 O PHE A 172 150.455 174.980 118.259 1.00 7.48 ATOM 1183 CB PHE A 172 151.075 175.368 121.488 1.00 7.48 ATOM 1184 CG PHE A 172 150.578 176.727 121.088 1.00 7.48 ATOM 1185 CD1 PHE A 172 149.279 177.116 121.369 1.00 7.48 ATOM 1186 CD2 PHE A 172 151.406 177.618 120.432 1.00 7.48 ATOM 1187 CE1 PHE A 172 148.820 178.366 121.001 1.00 7.48 ATOM 1188 CE2 PHE A 172 150.951 178.869 120.061 1.00 7.48 ATOM 1189 CZ PHE A 172 149.658 179.244 120.348 1.00 7.48 ATOM 1190 N ILE A 173 152.461 174.209 118.929 1.00 9.20 ATOM 1191 CA ILE A 173 153.146 174.500 117.675 1.00 9.20 ATOM 1192 C ILE A 173 152.657 173.587 116.559 1.00 9.20 ATOM 1193 O ILE A 173 152.444 174.036 115.426 1.00 9.20 ATOM 1194 CB ILE A 173 154.672 174.351 117.818 1.00 9.20 ATOM 1195 CG1 ILE A 173 155.221 175.397 118.790 1.00 9.20 ATOM 1196 CG2 ILE A 173 155.354 174.538 116.471 1.00 9.20 ATOM 1197 CD1 ILE A 173 156.667 175.175 119.174 1.00 9.20 ATOM 1198 N PHE A 174 152.472 172.303 116.864 1.00 13.18 ATOM 1199 CA PHE A 174 152.364 171.290 115.824 1.00 13.18 ATOM 1200 C PHE A 174 150.949 170.781 115.580 1.00 13.18 ATOM 1201 O PHE A 174 150.648 170.372 114.454 1.00 13.18 ATOM 1202 CB PHE A 174 153.255 170.090 116.150 1.00 13.18 ATOM 1203 CG PHE A 174 154.723 170.408 116.152 1.00 13.18 ATOM 1204 CD1 PHE A 174 155.453 170.388 114.975 1.00 13.18 ATOM 1205 CD2 PHE A 174 155.376 170.729 117.328 1.00 13.18 ATOM 1206 CE1 PHE A 174 156.802 170.681 114.976 1.00 13.18 ATOM 1207 CE2 PHE A 174 156.726 171.022 117.333 1.00 13.18 ATOM 1208 CZ PHE A 174 157.440 170.998 116.155 1.00 13.18 ATOM 1209 N ALA A 175 150.078 170.784 116.588 1.00 12.53 ATOM 1210 CA ALA A 175 148.736 170.256 116.395 1.00 12.53 ATOM 1211 C ALA A 175 147.955 171.126 115.412 1.00 12.53 ATOM 1212 O ALA A 175 147.951 172.356 115.488 1.00 12.53 ATOM 1213 CB ALA A 175 147.994 170.163 117.737 1.00 12.53 ATOM 1214 N ASN A 176 147.276 170.459 114.480 1.00 17.53 ATOM 1215 CA ASN A 176 146.552 171.149 113.420 1.00 17.53 ATOM 1216 C ASN A 176 145.596 170.196 112.715 1.00 17.53 ATOM 1217 O ASN A 176 145.723 168.974 112.846 1.00 17.53 ATOM 1218 CB ASN A 176 147.529 171.764 112.416 1.00 17.53 ATOM 1219 CG ASN A 176 148.382 170.723 111.721 1.00 17.53 ATOM 1220 OD1 ASN A 176 147.962 169.581 111.542 1.00 17.53 ATOM 1221 ND2 ASN A 176 149.587 171.116 111.324 1.00 17.53 ATOM 1222 N VAL A 177 144.639 170.739 111.967 1.00 23.53 ATOM 1223 CA VAL A 177 143.723 169.949 111.155 1.00 23.53 ATOM 1224 C VAL A 177 143.914 170.344 109.697 1.00 23.53 ATOM 1225 O VAL A 177 143.854 171.531 109.355 1.00 23.53 ATOM 1226 CB VAL A 177 142.261 170.160 111.588 1.00 23.53 ATOM 1227 CG1 VAL A 177 141.315 169.423 110.650 1.00 23.53 ATOM 1228 CG2 VAL A 177 142.042 169.635 112.999 1.00 23.53 ATOM 1229 N SER A 178 144.166 169.352 108.846 1.00 32.05 ATOM 1230 CA SER A 178 144.392 169.591 107.428 1.00 32.05 ATOM 1231 C SER A 178 143.604 168.577 106.618 1.00 32.05 ATOM 1232 O SER A 178 143.634 167.381 106.920 1.00 32.05 ATOM 1233 CB SER A 178 145.885 169.517 107.103 1.00 32.05 ATOM 1234 OG SER A 178 146.404 168.229 107.383 1.00 32.05 ATOM 1235 N GLU A 179 142.906 169.056 105.595 1.00 47.48 ATOM 1236 CA GLU A 179 142.128 168.192 104.722 1.00 47.48 ATOM 1237 C GLU A 179 142.987 167.691 103.567 1.00 47.48 ATOM 1238 O GLU A 179 143.918 168.364 103.117 1.00 47.48 ATOM 1239 CB GLU A 179 140.897 168.932 104.194 1.00 47.48 ATOM 1240 CG GLU A 179 139.891 169.309 105.269 1.00 47.48 ATOM 1241 CD GLU A 179 139.257 168.097 105.923 1.00 47.48 ATOM 1242 OE1 GLU A 179 138.952 167.125 105.203 1.00 47.48 ATOM 1243 OE2 GLU A 179 139.068 168.120 107.159 1.00 47.48 ATOM 1244 N ALA A 180 142.671 166.483 103.101 1.00 60.26 ATOM 1245 CA ALA A 180 143.361 165.860 101.969 1.00 60.26 ATOM 1246 C ALA A 180 142.303 165.117 101.158 1.00 60.26 ATOM 1247 O ALA A 180 141.985 163.960 101.450 1.00 60.26 ATOM 1248 CB ALA A 180 144.478 164.929 102.463 1.00 60.26 ATOM 1249 N ASP A 181 141.763 165.793 100.142 1.00 68.90 ATOM 1250 CA ASP A 181 140.668 165.271 99.326 1.00 68.90 ATOM 1251 C ASP A 181 139.464 164.915 100.202 1.00 68.90 ATOM 1252 O ASP A 181 139.006 163.771 100.249 1.00 68.90 ATOM 1253 CB ASP A 181 141.128 164.049 98.530 1.00 68.90 ATOM 1254 CG ASP A 181 141.559 162.901 99.422 1.00 68.90 ATOM 1255 OD1 ASP A 181 142.370 163.136 100.343 1.00 68.90 ATOM 1256 OD2 ASP A 181 141.088 161.766 99.201 1.00 68.90 ATOM 1257 N ASP A 182 138.965 165.932 100.907 1.00 64.41 ATOM 1258 CA ASP A 182 137.825 165.797 101.816 1.00 64.41 ATOM 1259 C ASP A 182 138.106 164.764 102.908 1.00 64.41 ATOM 1260 O ASP A 182 137.301 163.869 103.175 1.00 64.41 ATOM 1261 CB ASP A 182 136.564 165.412 101.041 1.00 64.41 ATOM 1262 CG ASP A 182 135.337 165.330 101.927 1.00 64.41 ATOM 1263 OD1 ASP A 182 134.925 166.377 102.471 1.00 64.41 ATOM 1264 OD2 ASP A 182 134.785 164.219 102.077 1.00 64.41 ATOM 1265 N ARG A 183 139.269 164.897 103.546 1.00 56.43 ATOM 1266 CA ARG A 183 139.667 164.049 104.671 1.00 56.43 ATOM 1267 C ARG A 183 140.227 164.962 105.759 1.00 56.43 ATOM 1268 O ARG A 183 141.434 165.212 105.814 1.00 56.43 ATOM 1269 CB ARG A 183 140.686 163.002 104.219 1.00 56.43 ATOM 1270 CG ARG A 183 140.127 161.966 103.258 1.00 56.43 ATOM 1271 CD ARG A 183 141.190 160.958 102.850 1.00 56.43 ATOM 1272 NE ARG A 183 141.646 160.156 103.981 1.00 56.43 ATOM 1273 CZ ARG A 183 141.037 159.053 104.406 1.00 56.43 ATOM 1274 NH1 ARG A 183 139.945 158.619 103.792 1.00 56.43 ATOM 1275 NH2 ARG A 183 141.525 158.386 105.444 1.00 56.43 ATOM 1276 N TYR A 184 139.346 165.448 106.630 1.00 40.98 ATOM 1277 CA TYR A 184 139.724 166.378 107.690 1.00 40.98 ATOM 1278 C TYR A 184 140.181 165.576 108.902 1.00 40.98 ATOM 1279 O TYR A 184 139.373 164.905 109.552 1.00 40.98 ATOM 1280 CB TYR A 184 138.553 167.299 108.037 1.00 40.98 ATOM 1281 CG TYR A 184 138.884 168.344 109.080 1.00 40.98 ATOM 1282 CD1 TYR A 184 139.564 169.505 108.734 1.00 40.98 ATOM 1283 CD2 TYR A 184 138.514 168.167 110.407 1.00 40.98 ATOM 1284 CE1 TYR A 184 139.870 170.462 109.679 1.00 40.98 ATOM 1285 CE2 TYR A 184 138.811 169.115 111.366 1.00 40.98 ATOM 1286 CZ TYR A 184 139.489 170.263 111.001 1.00 40.98 ATOM 1287 OH TYR A 184 139.790 171.213 111.948 1.00 40.98 ATOM 1288 N ILE A 185 141.474 165.644 109.209 1.00 30.35 ATOM 1289 CA ILE A 185 142.075 164.877 110.295 1.00 30.35 ATOM 1290 C ILE A 185 142.752 165.840 111.259 1.00 30.35 ATOM 1291 O ILE A 185 143.573 166.666 110.844 1.00 30.35 ATOM 1292 CB ILE A 185 143.089 163.847 109.764 1.00 30.35 ATOM 1293 CG1 ILE A 185 142.381 162.790 108.914 1.00 30.35 ATOM 1294 CG2 ILE A 185 143.791 163.147 110.918 1.00 30.35 ATOM 1295 CD1 ILE A 185 143.324 161.880 108.159 1.00 30.35 ATOM 1296 N CYS A 186 142.414 165.727 112.543 1.00 21.74 ATOM 1297 CA CYS A 186 143.108 166.456 113.605 1.00 21.74 ATOM 1298 C CYS A 186 144.294 165.597 114.023 1.00 21.74 ATOM 1299 O CYS A 186 144.190 164.722 114.884 1.00 21.74 ATOM 1300 CB CYS A 186 142.156 166.745 114.767 1.00 21.74 ATOM 1301 SG CYS A 186 142.889 167.727 116.116 1.00 21.74 ATOM 1302 N ASP A 187 145.438 165.834 113.381 1.00 20.37 ATOM 1303 CA ASP A 187 146.632 165.032 113.590 1.00 20.37 ATOM 1304 C ASP A 187 147.852 165.939 113.644 1.00 20.37 ATOM 1305 O ASP A 187 147.964 166.899 112.878 1.00 20.37 ATOM 1306 CB ASP A 187 146.776 163.986 112.483 1.00 20.37 ATOM 1307 CG ASP A 187 146.934 164.609 111.110 1.00 20.37 ATOM 1308 OD1 ASP A 187 146.119 165.488 110.758 1.00 20.37 ATOM 1309 OD2 ASP A 187 147.872 164.218 110.384 1.00 20.37 ATOM 1310 N ARG A 188 148.768 165.624 114.559 1.00 17.09 ATOM 1311 CA ARG A 188 150.027 166.352 114.642 1.00 17.09 ATOM 1312 C ARG A 188 150.815 166.170 113.352 1.00 17.09 ATOM 1313 O ARG A 188 150.981 165.048 112.867 1.00 17.09 ATOM 1314 CB ARG A 188 150.841 165.880 115.848 1.00 17.09 ATOM 1315 CG ARG A 188 150.161 166.117 117.187 1.00 17.09 ATOM 1316 CD ARG A 188 150.068 167.600 117.502 1.00 17.09 ATOM 1317 NE ARG A 188 149.416 167.847 118.786 1.00 17.09 ATOM 1318 CZ ARG A 188 149.208 169.056 119.299 1.00 17.09 ATOM 1319 NH1 ARG A 188 149.601 170.133 118.635 1.00 17.09 ATOM 1320 NH2 ARG A 188 148.608 169.182 120.473 1.00 17.09 ATOM 1321 N PHE A 189 151.306 167.274 112.796 1.00 16.28 ATOM 1322 CA PHE A 189 151.998 167.262 111.516 1.00 16.28 ATOM 1323 C PHE A 189 153.410 167.798 111.688 1.00 16.28 ATOM 1324 O PHE A 189 153.613 168.836 112.326 1.00 16.28 ATOM 1325 CB PHE A 189 151.226 168.083 110.482 1.00 16.28 ATOM 1326 CG PHE A 189 149.881 167.514 110.136 1.00 16.28 ATOM 1327 CD1 PHE A 189 149.756 166.531 109.168 1.00 16.28 ATOM 1328 CD2 PHE A 189 148.738 167.956 110.779 1.00 16.28 ATOM 1329 CE1 PHE A 189 148.518 166.006 108.851 1.00 16.28 ATOM 1330 CE2 PHE A 189 147.499 167.433 110.463 1.00 16.28 ATOM 1331 CZ PHE A 189 147.389 166.457 109.498 1.00 16.28 ATOM 1332 N TYR A 190 154.379 167.091 111.114 1.00 16.29 ATOM 1333 CA TYR A 190 155.784 167.456 111.157 1.00 16.29 ATOM 1334 C TYR A 190 156.338 167.502 109.742 1.00 16.29 ATOM 1335 O TYR A 190 155.849 166.793 108.856 1.00 16.29 ATOM 1336 CB TYR A 190 156.568 166.468 112.023 1.00 16.29 ATOM 1337 CG TYR A 190 156.175 166.485 113.483 1.00 16.29 ATOM 1338 CD1 TYR A 190 154.881 166.810 113.867 1.00 16.29 ATOM 1339 CD2 TYR A 190 157.100 166.179 114.472 1.00 16.29 ATOM 1340 CE1 TYR A 190 154.512 166.830 115.197 1.00 16.29 ATOM 1341 CE2 TYR A 190 156.751 166.191 115.808 1.00 16.29 ATOM 1342 CZ TYR A 190 155.456 166.518 116.169 1.00 16.29 ATOM 1343 OH TYR A 190 155.099 166.534 117.497 1.00 16.29 ATOM 1344 N PRO A 191 157.351 168.335 109.497 1.00 17.27 ATOM 1345 CA PRO A 191 157.941 168.387 108.148 1.00 17.27 ATOM 1346 C PRO A 191 158.553 167.074 107.689 1.00 17.27 ATOM 1347 O PRO A 191 158.485 166.759 106.493 1.00 17.27 ATOM 1348 CB PRO A 191 158.971 169.512 108.266 1.00 17.27 ATOM 1349 CG PRO A 191 158.412 170.414 109.344 1.00 17.27 ATOM 1350 CD PRO A 191 157.840 169.428 110.348 1.00 17.27 ATOM 1351 N ASN A 192 159.149 166.294 108.591 1.00 17.04 ATOM 1352 CA ASN A 192 159.818 165.055 108.221 1.00 17.04 ATOM 1353 C ASN A 192 159.431 163.951 109.196 1.00 17.04 ATOM 1354 O ASN A 192 158.858 164.200 110.259 1.00 17.04 ATOM 1355 CB ASN A 192 161.335 165.252 108.194 1.00 17.04 ATOM 1356 CG ASN A 192 162.072 164.033 107.675 1.00 17.04 ATOM 1357 OD1 ASN A 192 162.299 163.074 108.411 1.00 17.04 ATOM 1358 ND2 ASN A 192 162.446 164.069 106.402 1.00 17.04 ATOM 1359 N ASP A 193 159.759 162.713 108.818 1.00 17.00 ATOM 1360 CA ASP A 193 159.532 161.566 109.686 1.00 17.00 ATOM 1361 C ASP A 193 160.540 161.481 110.824 1.00 17.00 ATOM 1362 O ASP A 193 160.297 160.760 111.799 1.00 17.00 ATOM 1363 CB ASP A 193 159.571 160.267 108.879 1.00 17.00 ATOM 1364 CG ASP A 193 159.268 159.046 109.725 1.00 17.00 ATOM 1365 OD1 ASP A 193 158.128 158.936 110.224 1.00 17.00 ATOM 1366 OD2 ASP A 193 160.169 158.197 109.887 1.00 17.00 ATOM 1367 N LEU A 194 161.666 162.192 110.718 1.00 15.12 ATOM 1368 CA LEU A 194 162.633 162.209 111.808 1.00 15.12 ATOM 1369 C LEU A 194 162.020 162.807 113.067 1.00 15.12 ATOM 1370 O LEU A 194 162.226 162.294 114.172 1.00 15.12 ATOM 1371 CB LEU A 194 163.883 162.992 111.403 1.00 15.12 ATOM 1372 CG LEU A 194 164.716 162.399 110.264 1.00 15.12 ATOM 1373 CD1 LEU A 194 165.838 163.346 109.869 1.00 15.12 ATOM 1374 CD2 LEU A 194 165.338 161.077 110.687 1.00 15.12 ATOM 1375 N TRP A 195 161.252 163.888 112.915 1.00 14.86 ATOM 1376 CA TRP A 195 160.529 164.442 114.052 1.00 14.86 ATOM 1377 C TRP A 195 159.554 163.421 114.620 1.00 14.86 ATOM 1378 O TRP A 195 159.412 163.298 115.843 1.00 14.86 ATOM 1379 CB TRP A 195 159.788 165.717 113.646 1.00 14.86 ATOM 1380 CG TRP A 195 158.750 165.496 112.589 1.00 14.86 ATOM 1381 CD1 TRP A 195 158.928 165.563 111.237 1.00 14.86 ATOM 1382 CD2 TRP A 195 157.369 165.171 112.799 1.00 14.86 ATOM 1383 NE1 TRP A 195 157.747 165.301 110.590 1.00 14.86 ATOM 1384 CE2 TRP A 195 156.772 165.057 111.528 1.00 14.86 ATOM 1385 CE3 TRP A 195 156.584 164.967 113.936 1.00 14.86 ATOM 1386 CZ2 TRP A 195 155.424 164.746 111.361 1.00 14.86 ATOM 1387 CZ3 TRP A 195 155.247 164.659 113.770 1.00 14.86 ATOM 1388 CH2 TRP A 195 154.675 164.551 112.491 1.00 14.86 ATOM 1389 N VAL A 196 158.878 162.674 113.744 1.00 12.41 ATOM 1390 CA VAL A 196 157.905 161.683 114.193 1.00 12.41 ATOM 1391 C VAL A 196 158.578 160.631 115.064 1.00 12.41 ATOM 1392 O VAL A 196 158.123 160.339 116.177 1.00 12.41 ATOM 1393 CB VAL A 196 157.210 160.996 113.003 1.00 12.41 ATOM 1394 CG1 VAL A 196 156.293 159.884 113.491 1.00 12.41 ATOM 1395 CG2 VAL A 196 156.374 162.000 112.223 1.00 12.41 ATOM 1396 N VAL A 197 159.680 160.056 114.578 1.00 10.25 ATOM 1397 CA VAL A 197 160.331 158.989 115.331 1.00 10.25 ATOM 1398 C VAL A 197 160.952 159.537 116.612 1.00 10.25 ATOM 1399 O VAL A 197 160.906 158.886 117.662 1.00 10.25 ATOM 1400 CB VAL A 197 161.418 158.290 114.494 1.00 10.25 ATOM 1401 CG1 VAL A 197 162.165 157.267 115.337 1.00 10.25 ATOM 1402 CG2 VAL A 197 160.795 157.571 113.306 1.00 10.25 ATOM 1403 N VAL A 198 161.516 160.748 116.558 1.00 9.84 ATOM 1404 CA VAL A 198 162.112 161.339 117.753 1.00 9.84 ATOM 1405 C VAL A 198 161.053 161.548 118.825 1.00 9.84 ATOM 1406 O VAL A 198 161.265 161.227 120.000 1.00 9.84 ATOM 1407 CB VAL A 198 162.797 162.681 117.437 1.00 9.84 ATOM 1408 CG1 VAL A 198 163.302 163.336 118.714 1.00 9.84 ATOM 1409 CG2 VAL A 198 163.981 162.469 116.505 1.00 9.84 ATOM 1410 N PHE A 199 159.886 162.068 118.437 1.00 10.84 ATOM 1411 CA PHE A 199 158.849 162.335 119.426 1.00 10.84 ATOM 1412 C PHE A 199 158.201 161.053 119.932 1.00 10.84 ATOM 1413 O PHE A 199 157.830 160.981 121.107 1.00 10.84 ATOM 1414 CB PHE A 199 157.778 163.259 118.844 1.00 10.84 ATOM 1415 CG PHE A 199 156.708 163.640 119.825 1.00 10.84 ATOM 1416 CD1 PHE A 199 156.926 164.641 120.756 1.00 10.84 ATOM 1417 CD2 PHE A 199 155.481 163.001 119.818 1.00 10.84 ATOM 1418 CE1 PHE A 199 155.941 164.992 121.660 1.00 10.84 ATOM 1419 CE2 PHE A 199 154.495 163.348 120.721 1.00 10.84 ATOM 1420 CZ PHE A 199 154.725 164.346 121.642 1.00 10.84 ATOM 1421 N GLN A 200 158.069 160.027 119.084 1.00 7.97 ATOM 1422 CA GLN A 200 157.571 158.744 119.576 1.00 7.97 ATOM 1423 C GLN A 200 158.533 158.126 120.585 1.00 7.97 ATOM 1424 O GLN A 200 158.108 157.605 121.625 1.00 7.97 ATOM 1425 CB GLN A 200 157.339 157.778 118.413 1.00 7.97 ATOM 1426 CG GLN A 200 158.596 157.436 117.628 1.00 7.97 ATOM 1427 CD GLN A 200 158.327 156.478 116.487 1.00 7.97 ATOM 1428 OE1 GLN A 200 157.547 156.776 115.583 1.00 7.97 ATOM 1429 NE2 GLN A 200 158.977 155.320 116.523 1.00 7.97 ATOM 1430 N PHE A 201 159.836 158.174 120.295 1.00 6.25 ATOM 1431 CA PHE A 201 160.814 157.638 121.235 1.00 6.25 ATOM 1432 C PHE A 201 160.821 158.432 122.533 1.00 6.25 ATOM 1433 O PHE A 201 160.951 157.855 123.619 1.00 6.25 ATOM 1434 CB PHE A 201 162.211 157.636 120.612 1.00 6.25 ATOM 1435 CG PHE A 201 163.266 157.032 121.492 1.00 6.25 ATOM 1436 CD1 PHE A 201 163.411 155.658 121.583 1.00 6.25 ATOM 1437 CD2 PHE A 201 164.117 157.835 122.231 1.00 6.25 ATOM 1438 CE1 PHE A 201 164.382 155.101 122.393 1.00 6.25 ATOM 1439 CE2 PHE A 201 165.088 157.282 123.043 1.00 6.25 ATOM 1440 CZ PHE A 201 165.222 155.913 123.123 1.00 6.25 ATOM 1441 N GLN A 202 160.682 159.757 122.445 1.00 5.49 ATOM 1442 CA GLN A 202 160.590 160.567 123.654 1.00 5.49 ATOM 1443 C GLN A 202 159.345 160.215 124.459 1.00 5.49 ATOM 1444 O GLN A 202 159.394 160.137 125.693 1.00 5.49 ATOM 1445 CB GLN A 202 160.586 162.056 123.303 1.00 5.49 ATOM 1446 CG GLN A 202 159.405 162.489 122.448 1.00 5.49 ATOM 1447 CD GLN A 202 159.434 163.968 122.122 1.00 5.49 ATOM 1448 OE1 GLN A 202 160.480 164.612 122.202 1.00 5.49 ATOM 1449 NE2 GLN A 202 158.282 164.513 121.749 1.00 5.49 ATOM 1450 N HIS A 203 158.218 160.005 123.776 1.00 3.63 ATOM 1451 CA HIS A 203 156.994 159.606 124.459 1.00 3.63 ATOM 1452 C HIS A 203 157.200 158.298 125.209 1.00 3.63 ATOM 1453 O HIS A 203 156.846 158.185 126.387 1.00 3.63 ATOM 1454 CB HIS A 203 155.842 159.473 123.461 1.00 3.63 ATOM 1455 CG HIS A 203 155.453 160.764 122.811 1.00 3.63 ATOM 1456 ND1 HIS A 203 156.115 161.277 121.718 1.00 3.63 ATOM 1457 CD2 HIS A 203 154.469 161.648 123.103 1.00 3.63 ATOM 1458 CE1 HIS A 203 155.555 162.421 121.364 1.00 3.63 ATOM 1459 NE2 HIS A 203 154.554 162.668 122.187 1.00 3.63 ATOM 1460 N ILE A 204 157.804 157.310 124.548 1.00 3.31 ATOM 1461 CA ILE A 204 158.056 156.026 125.202 1.00 3.31 ATOM 1462 C ILE A 204 158.965 156.218 126.411 1.00 3.31 ATOM 1463 O ILE A 204 158.681 155.722 127.510 1.00 3.31 ATOM 1464 CB ILE A 204 158.694 155.015 124.232 1.00 3.31 ATOM 1465 CG1 ILE A 204 157.718 154.669 123.104 1.00 3.31 ATOM 1466 CG2 ILE A 204 159.059 153.732 124.963 1.00 3.31 ATOM 1467 CD1 ILE A 204 158.341 153.871 121.980 1.00 3.31 ATOM 1468 N MET A 205 160.059 156.963 126.229 1.00 2.84 ATOM 1469 CA MET A 205 161.060 157.097 127.280 1.00 2.84 ATOM 1470 C MET A 205 160.497 157.793 128.512 1.00 2.84 ATOM 1471 O MET A 205 160.753 157.365 129.642 1.00 2.84 ATOM 1472 CB MET A 205 162.279 157.863 126.764 1.00 2.84 ATOM 1473 CG MET A 205 161.977 159.288 126.325 1.00 2.84 ATOM 1474 SD MET A 205 163.437 160.156 125.724 1.00 2.84 ATOM 1475 CE MET A 205 164.283 160.503 127.266 1.00 2.84 ATOM 1476 N VAL A 206 159.726 158.867 128.321 1.00 3.04 ATOM 1477 CA VAL A 206 159.191 159.592 129.472 1.00 3.04 ATOM 1478 C VAL A 206 157.895 158.995 129.998 1.00 3.04 ATOM 1479 O VAL A 206 157.483 159.324 131.117 1.00 3.04 ATOM 1480 CB VAL A 206 158.935 161.073 129.137 1.00 3.04 ATOM 1481 CG1 VAL A 206 158.265 161.777 130.307 1.00 3.04 ATOM 1482 CG2 VAL A 206 160.246 161.784 128.834 1.00 3.04 ATOM 1483 N GLY A 207 157.251 158.102 129.246 1.00 1.72 ATOM 1484 CA GLY A 207 156.016 157.513 129.717 1.00 1.72 ATOM 1485 C GLY A 207 156.179 156.185 130.420 1.00 1.72 ATOM 1486 O GLY A 207 155.469 155.913 131.392 1.00 1.72 ATOM 1487 N LEU A 208 157.102 155.343 129.957 1.00 0.72 ATOM 1488 CA LEU A 208 157.244 154.006 130.519 1.00 0.72 ATOM 1489 C LEU A 208 158.587 153.776 131.192 1.00 0.72 ATOM 1490 O LEU A 208 158.627 153.352 132.351 1.00 0.72 ATOM 1491 CB LEU A 208 157.043 152.945 129.435 1.00 0.72 ATOM 1492 CG LEU A 208 155.648 152.868 128.812 1.00 0.72 ATOM 1493 CD1 LEU A 208 155.629 151.879 127.656 1.00 0.72 ATOM 1494 CD2 LEU A 208 154.624 152.415 129.841 1.00 0.72 ATOM 1495 N ILE A 209 159.691 154.054 130.499 1.00 0.48 ATOM 1496 CA ILE A 209 160.996 153.597 130.967 1.00 0.48 ATOM 1497 C ILE A 209 161.474 154.430 132.152 1.00 0.48 ATOM 1498 O ILE A 209 161.874 153.886 133.187 1.00 0.48 ATOM 1499 CB ILE A 209 162.050 153.658 129.847 1.00 0.48 ATOM 1500 CG1 ILE A 209 161.696 152.678 128.726 1.00 0.48 ATOM 1501 CG2 ILE A 209 163.425 153.296 130.387 1.00 0.48 ATOM 1502 CD1 ILE A 209 162.540 152.840 127.482 1.00 0.48 ATOM 1503 N LEU A 210 161.451 155.754 132.017 1.00 0.06 ATOM 1504 CA LEU A 210 162.035 156.611 133.049 1.00 0.06 ATOM 1505 C LEU A 210 161.334 156.506 134.401 1.00 0.06 ATOM 1506 O LEU A 210 162.034 156.368 135.418 1.00 0.06 ATOM 1507 CB LEU A 210 162.023 158.074 132.601 1.00 0.06 ATOM 1508 CG LEU A 210 162.892 158.419 131.389 1.00 0.06 ATOM 1509 CD1 LEU A 210 162.673 159.863 130.965 1.00 0.06 ATOM 1510 CD2 LEU A 210 164.366 158.238 131.716 1.00 0.06 ATOM 1511 N PRO A 211 159.991 156.572 134.505 1.00 0.27 ATOM 1512 CA PRO A 211 159.370 156.446 135.831 1.00 0.27 ATOM 1513 C PRO A 211 159.274 155.003 136.297 1.00 0.27 ATOM 1514 O PRO A 211 159.242 154.728 137.504 1.00 0.27 ATOM 1515 CB PRO A 211 158.008 157.115 135.638 1.00 0.27 ATOM 1516 CG PRO A 211 158.245 158.126 134.538 1.00 0.27 ATOM 1517 CD PRO A 211 159.175 157.387 133.592 1.00 0.27 ATOM 1518 N GLY A 212 159.218 154.072 135.342 1.00 0.96 ATOM 1519 CA GLY A 212 159.168 152.664 135.697 1.00 0.96 ATOM 1520 C GLY A 212 160.396 152.217 136.463 1.00 0.96 ATOM 1521 O GLY A 212 160.296 151.446 137.422 1.00 0.96 ATOM 1522 N ILE A 213 161.571 152.698 136.055 1.00 0.96 ATOM 1523 CA ILE A 213 162.805 152.356 136.756 1.00 0.96 ATOM 1524 C ILE A 213 162.765 152.868 138.189 1.00 0.96 ATOM 1525 O ILE A 213 163.154 152.161 139.126 1.00 0.96 ATOM 1526 CB ILE A 213 164.039 152.933 136.039 1.00 0.96 ATOM 1527 CG1 ILE A 213 164.207 152.289 134.662 1.00 0.96 ATOM 1528 CG2 ILE A 213 165.299 152.671 136.851 1.00 0.96 ATOM 1529 CD1 ILE A 213 165.247 152.962 133.794 1.00 0.96 ATOM 1530 N VAL A 214 162.295 154.101 138.384 1.00 1.00 ATOM 1531 CA VAL A 214 162.228 154.673 139.728 1.00 1.00 ATOM 1532 C VAL A 214 161.271 153.871 140.601 1.00 1.00 ATOM 1533 O VAL A 214 161.577 153.548 141.758 1.00 1.00 ATOM 1534 CB VAL A 214 161.780 156.146 139.693 1.00 1.00 ATOM 1535 CG1 VAL A 214 161.599 156.682 141.104 1.00 1.00 ATOM 1536 CG2 VAL A 214 162.818 157.001 138.983 1.00 1.00 ATOM 1537 N ILE A 215 160.101 153.531 140.056 1.00 1.31 ATOM 1538 CA ILE A 215 159.116 152.769 140.823 1.00 1.31 ATOM 1539 C ILE A 215 159.679 151.403 141.200 1.00 1.31 ATOM 1540 O ILE A 215 159.575 150.961 142.354 1.00 1.31 ATOM 1541 CB ILE A 215 157.806 152.587 140.035 1.00 1.31 ATOM 1542 CG1 ILE A 215 157.129 153.940 139.806 1.00 1.31 ATOM 1543 CG2 ILE A 215 156.844 151.690 140.799 1.00 1.31 ATOM 1544 CD1 ILE A 215 155.966 153.886 138.841 1.00 1.31 ATOM 1545 N LEU A 216 160.295 150.719 140.230 1.00 1.85 ATOM 1546 CA LEU A 216 160.844 149.395 140.486 1.00 1.85 ATOM 1547 C LEU A 216 161.954 149.445 141.526 1.00 1.85 ATOM 1548 O LEU A 216 162.004 148.601 142.425 1.00 1.85 ATOM 1549 CB LEU A 216 161.369 148.773 139.191 1.00 1.85 ATOM 1550 CG LEU A 216 160.326 148.468 138.113 1.00 1.85 ATOM 1551 CD1 LEU A 216 160.997 147.994 136.834 1.00 1.85 ATOM 1552 CD2 LEU A 216 159.373 147.380 138.581 1.00 1.85 ATOM 1553 N SER A 217 162.851 150.428 141.424 1.00 2.84 ATOM 1554 CA SER A 217 163.940 150.536 142.388 1.00 2.84 ATOM 1555 C SER A 217 163.405 150.794 143.789 1.00 2.84 ATOM 1556 O SER A 217 163.829 150.149 144.758 1.00 2.84 ATOM 1557 CB SER A 217 164.909 151.647 141.980 1.00 2.84 ATOM 1558 OG SER A 217 164.261 152.907 141.961 1.00 2.84 ATOM 1559 N CYS A 218 162.457 151.726 143.914 1.00 4.88 ATOM 1560 CA CYS A 218 161.913 152.044 145.229 1.00 4.88 ATOM 1561 C CYS A 218 161.243 150.827 145.850 1.00 4.88 ATOM 1562 O CYS A 218 161.476 150.505 147.021 1.00 4.88 ATOM 1563 CB CYS A 218 160.919 153.203 145.132 1.00 4.88 ATOM 1564 SG CYS A 218 159.461 152.860 144.095 1.00 4.88 ATOM 1565 N TYR A 219 160.430 150.111 145.068 1.00 5.82 ATOM 1566 CA TYR A 219 159.705 148.984 145.643 1.00 5.82 ATOM 1567 C TYR A 219 160.616 147.793 145.913 1.00 5.82 ATOM 1568 O TYR A 219 160.399 147.065 146.888 1.00 5.82 ATOM 1569 CB TYR A 219 158.561 148.557 144.722 1.00 5.82 ATOM 1570 CG TYR A 219 157.479 149.601 144.562 1.00 5.82 ATOM 1571 CD1 TYR A 219 156.443 149.700 145.482 1.00 5.82 ATOM 1572 CD2 TYR A 219 157.498 150.486 143.491 1.00 5.82 ATOM 1573 CE1 TYR A 219 155.452 150.651 145.343 1.00 5.82 ATOM 1574 CE2 TYR A 219 156.515 151.445 143.336 1.00 5.82 ATOM 1575 CZ TYR A 219 155.493 151.525 144.264 1.00 5.82 ATOM 1576 OH TYR A 219 154.509 152.476 144.120 1.00 5.82 ATOM 1577 N CYS A 220 161.647 147.584 145.092 1.00 4.94 ATOM 1578 CA CYS A 220 162.609 146.524 145.375 1.00 4.94 ATOM 1579 C CYS A 220 163.376 146.805 146.660 1.00 4.94 ATOM 1580 O CYS A 220 163.593 145.899 147.474 1.00 4.94 ATOM 1581 CB CYS A 220 163.583 146.358 144.207 1.00 4.94 ATOM 1582 SG CYS A 220 164.599 147.829 143.860 1.00 4.94 ATOM 1583 N ILE A 221 163.793 148.058 146.866 1.00 5.14 ATOM 1584 CA ILE A 221 164.487 148.396 148.105 1.00 5.14 ATOM 1585 C ILE A 221 163.550 148.253 149.299 1.00 5.14 ATOM 1586 O ILE A 221 163.959 147.794 150.375 1.00 5.14 ATOM 1587 CB ILE A 221 165.050 149.828 148.063 1.00 5.14 ATOM 1588 CG1 ILE A 221 166.134 149.945 146.990 1.00 5.14 ATOM 1589 CG2 ILE A 221 165.659 150.201 149.407 1.00 5.14 ATOM 1590 CD1 ILE A 221 166.573 151.366 146.716 1.00 5.14 ATOM 1591 N ILE A 222 162.278 148.627 149.133 1.00 7.82 ATOM 1592 CA ILE A 222 161.308 148.447 150.212 1.00 7.82 ATOM 1593 C ILE A 222 161.160 146.970 150.558 1.00 7.82 ATOM 1594 O ILE A 222 161.146 146.592 151.735 1.00 7.82 ATOM 1595 CB ILE A 222 159.932 149.026 149.836 1.00 7.82 ATOM 1596 CG1 ILE A 222 160.019 150.544 149.668 1.00 7.82 ATOM 1597 CG2 ILE A 222 158.909 148.718 150.919 1.00 7.82 ATOM 1598 CD1 ILE A 222 158.778 151.165 149.068 1.00 7.82 ATOM 1599 N ILE A 223 161.045 146.116 149.537 1.00 8.11 ATOM 1600 CA ILE A 223 160.885 144.684 149.772 1.00 8.11 ATOM 1601 C ILE A 223 162.110 144.114 150.473 1.00 8.11 ATOM 1602 O ILE A 223 161.992 143.312 151.406 1.00 8.11 ATOM 1603 CB ILE A 223 160.647 143.920 148.457 1.00 8.11 ATOM 1604 CG1 ILE A 223 159.318 144.341 147.828 1.00 8.11 ATOM 1605 CG2 ILE A 223 160.607 142.420 148.711 1.00 8.11 ATOM 1606 CD1 ILE A 223 159.115 143.822 146.422 1.00 8.11 ATOM 1607 N SER A 224 163.306 144.524 150.041 1.00 8.31 ATOM 1608 CA SER A 224 164.522 144.045 150.691 1.00 8.31 ATOM 1609 C SER A 224 164.576 144.486 152.148 1.00 8.31 ATOM 1610 O SER A 224 165.016 143.724 153.016 1.00 8.31 ATOM 1611 CB SER A 224 165.761 144.542 149.944 1.00 8.31 ATOM 1612 OG SER A 224 165.828 145.957 149.955 1.00 8.31 ATOM 1613 N LYS A 225 164.132 145.708 152.439 1.00 11.81 ATOM 1614 CA LYS A 225 164.141 146.195 153.814 1.00 11.81 ATOM 1615 C LYS A 225 162.938 145.727 154.623 1.00 11.81 ATOM 1616 O LYS A 225 162.889 145.992 155.830 1.00 11.81 ATOM 1617 CB LYS A 225 164.197 147.724 153.841 1.00 11.81 ATOM 1618 CG LYS A 225 165.498 148.307 153.318 1.00 11.81 ATOM 1619 CD LYS A 225 165.486 149.826 153.373 1.00 11.81 ATOM 1620 CE LYS A 225 164.486 150.405 152.384 1.00 11.81 ATOM 1621 NZ LYS A 225 164.461 151.894 152.427 1.00 11.81 ATOM 1622 N LEU A 226 161.978 145.044 154.005 1.00 20.14 ATOM 1623 CA LEU A 226 160.774 144.590 154.705 1.00 20.14 ATOM 1624 C LEU A 226 160.999 143.216 155.336 1.00 20.14 ATOM 1625 O LEU A 226 160.355 142.224 154.995 1.00 20.14 ATOM 1626 CB LEU A 226 159.582 144.546 153.748 1.00 20.14 ATOM 1627 CG LEU A 226 159.118 145.890 153.180 1.00 20.14 ATOM 1628 CD1 LEU A 226 158.029 145.686 152.138 1.00 20.14 ATOM 1629 CD2 LEU A 226 158.559 146.774 154.284 1.00 20.14 ATOM 1630 N SER A 227 161.938 143.169 156.277 1.00 33.55 ATOM 1631 CA SER A 227 162.280 141.931 156.972 1.00 33.55 ATOM 1632 C SER A 227 162.465 142.188 158.461 1.00 33.55 ATOM 1633 O SER A 227 163.413 141.696 159.083 1.00 33.55 ATOM 1634 CB SER A 227 163.545 141.313 156.375 1.00 33.55 ATOM 1635 OG SER A 227 163.331 140.907 155.034 1.00 33.55 ATOM 1636 N HIS A 228 161.563 142.965 159.054 1.00 49.23 ATOM 1637 CA HIS A 228 161.600 143.276 160.476 1.00 49.23 ATOM 1638 C HIS A 228 160.291 142.839 161.117 1.00 49.23 ATOM 1639 O HIS A 228 159.212 143.116 160.582 1.00 49.23 ATOM 1640 CB HIS A 228 161.850 144.770 160.692 1.00 49.23 ATOM 1641 CG HIS A 228 160.778 145.649 160.128 1.00 49.23 ATOM 1642 ND1 HIS A 228 160.649 145.892 158.778 1.00 49.23 ATOM 1643 CD2 HIS A 228 159.785 146.344 160.731 1.00 49.23 ATOM 1644 CE1 HIS A 228 159.622 146.700 158.576 1.00 49.23 ATOM 1645 NE2 HIS A 228 159.081 146.988 159.743 1.00 49.23 ATOM 1646 N SER A 229 160.395 142.155 162.258 1.00 49.82 ATOM 1647 CA SER A 229 159.245 141.652 163.018 1.00 49.82 ATOM 1648 C SER A 229 158.455 140.715 162.112 1.00 49.82 ATOM 1649 O SER A 229 159.015 139.694 161.676 1.00 49.82 ATOM 1650 CB SER A 229 158.386 142.813 163.522 1.00 49.82 ATOM 1651 OG SER A 229 157.859 143.563 162.442 0.00 99.99 ATOM 1652 N LYS A 230 157.194 140.998 161.801 1.00 49.09 ATOM 1653 CA LYS A 230 156.384 140.130 160.958 1.00 49.09 ATOM 1654 C LYS A 230 155.308 140.977 160.290 1.00 49.09 ATOM 1655 O LYS A 230 155.377 142.210 160.290 1.00 49.09 ATOM 1656 CB LYS A 230 155.776 138.996 161.785 1.00 49.09 ATOM 1657 CG LYS A 230 154.971 137.997 160.970 1.00 49.09 ATOM 1658 CD LYS A 230 154.397 136.900 161.853 1.00 49.09 ATOM 1659 CE LYS A 230 153.591 135.901 161.037 1.00 49.09 ATOM 1660 NZ LYS A 230 152.381 136.524 160.433 1.00 49.09 ATOM 1661 N GLY A 231 154.311 140.308 159.713 1.00 51.51 ATOM 1662 CA GLY A 231 153.221 140.987 159.041 1.00 51.51 ATOM 1663 C GLY A 231 152.454 141.935 159.940 1.00 51.51 ATOM 1664 O GLY A 231 152.031 141.560 161.037 1.00 51.51 ATOM 1665 N HIS A 232 152.270 143.168 159.480 1.00 51.39 ATOM 1666 CA HIS A 232 151.592 144.202 160.252 1.00 51.39 ATOM 1667 C HIS A 232 151.135 145.287 159.283 1.00 51.39 ATOM 1668 O HIS A 232 151.158 145.099 158.062 1.00 51.39 ATOM 1669 CB HIS A 232 152.520 144.758 161.334 1.00 51.39 ATOM 1670 CG HIS A 232 153.750 145.418 160.794 1.00 51.39 ATOM 1671 ND1 HIS A 232 154.814 144.706 160.284 1.00 51.39 ATOM 1672 CD2 HIS A 232 154.086 146.725 160.683 1.00 51.39 ATOM 1673 CE1 HIS A 232 155.751 145.548 159.885 1.00 51.39 ATOM 1674 NE2 HIS A 232 155.335 146.777 160.115 1.00 51.39 ATOM 1675 N GLN A 233 150.712 146.429 159.831 1.00 47.44 ATOM 1676 CA GLN A 233 150.316 147.550 158.985 1.00 47.44 ATOM 1677 C GLN A 233 151.473 148.036 158.123 1.00 47.44 ATOM 1678 O GLN A 233 151.254 148.517 157.006 1.00 47.44 ATOM 1679 CB GLN A 233 149.781 148.702 159.837 1.00 47.44 ATOM 1680 CG GLN A 233 149.278 149.888 159.032 1.00 47.44 ATOM 1681 CD GLN A 233 148.064 149.547 158.189 1.00 47.44 ATOM 1682 OE1 GLN A 233 148.179 149.307 156.988 1.00 47.44 ATOM 1683 NE2 GLN A 233 146.897 149.523 158.820 1.00 47.44 ATOM 1684 N LYS A 234 152.706 147.912 158.620 1.00 40.68 ATOM 1685 CA LYS A 234 153.878 148.262 157.826 1.00 40.68 ATOM 1686 C LYS A 234 153.995 147.412 156.568 1.00 40.68 ATOM 1687 O LYS A 234 154.602 147.852 155.587 1.00 40.68 ATOM 1688 CB LYS A 234 155.152 148.121 158.660 1.00 40.68 ATOM 1689 CG LYS A 234 156.420 148.535 157.932 1.00 40.68 ATOM 1690 CD LYS A 234 157.645 148.370 158.818 1.00 40.68 ATOM 1691 CE LYS A 234 158.913 148.784 158.088 1.00 40.68 ATOM 1692 NZ LYS A 234 159.204 147.895 156.930 1.00 40.68 ATOM 1693 N ARG A 235 153.426 146.207 156.573 1.00 42.93 ATOM 1694 CA ARG A 235 153.434 145.337 155.404 1.00 42.93 ATOM 1695 C ARG A 235 152.163 145.439 154.574 1.00 42.93 ATOM 1696 O ARG A 235 152.206 145.185 153.365 1.00 42.93 ATOM 1697 CB ARG A 235 153.642 143.880 155.822 1.00 42.93 ATOM 1698 CG ARG A 235 154.968 143.617 156.516 1.00 42.93 ATOM 1699 CD ARG A 235 156.135 143.780 155.557 1.00 42.93 ATOM 1700 NE ARG A 235 157.419 143.531 156.208 1.00 42.93 ATOM 1701 CZ ARG A 235 158.595 143.607 155.594 1.00 42.93 ATOM 1702 NH1 ARG A 235 158.652 143.926 154.309 1.00 42.93 ATOM 1703 NH2 ARG A 235 159.709 143.363 156.268 1.00 42.93 ATOM 1704 N LYS A 236 151.038 145.798 155.187 1.00 39.23 ATOM 1705 CA LYS A 236 149.766 145.895 154.485 1.00 39.23 ATOM 1706 C LYS A 236 149.452 147.303 153.998 1.00 39.23 ATOM 1707 O LYS A 236 148.405 147.507 153.376 1.00 39.23 ATOM 1708 CB LYS A 236 148.622 145.412 155.379 1.00 39.23 ATOM 1709 CG LYS A 236 148.666 143.927 155.695 1.00 39.23 ATOM 1710 CD LYS A 236 147.504 143.515 156.585 1.00 39.23 ATOM 1711 CE LYS A 236 147.635 144.117 157.976 1.00 39.23 ATOM 1712 NZ LYS A 236 148.825 143.588 158.699 1.00 39.23 ATOM 1713 N ALA A 237 150.323 148.279 154.265 1.00 31.82 ATOM 1714 CA ALA A 237 150.084 149.640 153.805 1.00 31.82 ATOM 1715 C ALA A 237 150.380 149.828 152.324 1.00 31.82 ATOM 1716 O ALA A 237 149.931 150.817 151.738 1.00 31.82 ATOM 1717 CB ALA A 237 150.923 150.639 154.616 1.00 31.82 ATOM 1718 N LEU A 238 151.118 148.907 151.709 1.00 20.89 ATOM 1719 CA LEU A 238 151.530 149.034 150.319 1.00 20.89 ATOM 1720 C LEU A 238 150.549 148.409 149.339 1.00 20.89 ATOM 1721 O LEU A 238 150.750 148.535 148.126 1.00 20.89 ATOM 1722 CB LEU A 238 152.909 148.406 150.109 1.00 20.89 ATOM 1723 CG LEU A 238 154.077 149.074 150.837 1.00 20.89 ATOM 1724 CD1 LEU A 238 155.354 148.267 150.660 1.00 20.89 ATOM 1725 CD2 LEU A 238 154.320 150.472 150.290 1.00 20.89 ATOM 1726 N LYS A 239 149.504 147.738 149.828 1.00 15.62 ATOM 1727 CA LYS A 239 148.637 146.963 148.946 1.00 15.62 ATOM 1728 C LYS A 239 147.909 147.860 147.951 1.00 15.62 ATOM 1729 O LYS A 239 147.922 147.603 146.742 1.00 15.62 ATOM 1730 CB LYS A 239 147.624 146.158 149.762 1.00 15.62 ATOM 1731 CG LYS A 239 148.242 145.054 150.604 1.00 15.62 ATOM 1732 CD LYS A 239 147.182 144.296 151.387 1.00 15.62 ATOM 1733 CE LYS A 239 147.801 143.193 152.230 1.00 15.62 ATOM 1734 NZ LYS A 239 148.688 143.738 153.294 1.00 15.62 ATOM 1735 N THR A 240 147.267 148.922 148.444 1.00 11.92 ATOM 1736 CA THR A 240 146.510 149.801 147.559 1.00 11.92 ATOM 1737 C THR A 240 147.422 150.476 146.542 1.00 11.92 ATOM 1738 O THR A 240 147.095 150.538 145.349 1.00 11.92 ATOM 1739 CB THR A 240 145.751 150.882 148.351 1.00 11.92 ATOM 1740 OG1 THR A 240 146.688 151.708 149.054 1.00 11.92 ATOM 1741 CG2 THR A 240 144.808 150.241 149.358 1.00 11.92 ATOM 1742 N THR A 241 148.573 150.977 146.995 1.00 11.11 ATOM 1743 CA THR A 241 149.488 151.667 146.093 1.00 11.11 ATOM 1744 C THR A 241 150.004 150.729 145.011 1.00 11.11 ATOM 1745 O THR A 241 150.036 151.085 143.825 1.00 11.11 ATOM 1746 CB THR A 241 150.685 152.266 146.854 1.00 11.11 ATOM 1747 OG1 THR A 241 151.433 151.215 147.478 1.00 11.11 ATOM 1748 CG2 THR A 241 150.205 153.233 147.926 1.00 11.11 ATOM 1749 N VAL A 242 150.402 149.512 145.395 1.00 9.45 ATOM 1750 CA VAL A 242 150.955 148.594 144.408 1.00 9.45 ATOM 1751 C VAL A 242 149.872 148.139 143.436 1.00 9.45 ATOM 1752 O VAL A 242 150.124 148.014 142.234 1.00 9.45 ATOM 1753 CB VAL A 242 151.594 147.364 145.078 1.00 9.45 ATOM 1754 CG1 VAL A 242 152.053 146.363 144.028 1.00 9.45 ATOM 1755 CG2 VAL A 242 152.799 147.775 145.909 1.00 9.45 ATOM 1756 N ILE A 243 148.646 147.923 143.922 1.00 8.87 ATOM 1757 CA ILE A 243 147.561 147.537 143.023 1.00 8.87 ATOM 1758 C ILE A 243 147.296 148.647 142.015 1.00 8.87 ATOM 1759 O ILE A 243 147.140 148.393 140.813 1.00 8.87 ATOM 1760 CB ILE A 243 146.270 147.223 143.800 1.00 8.87 ATOM 1761 CG1 ILE A 243 146.467 145.993 144.689 1.00 8.87 ATOM 1762 CG2 ILE A 243 145.123 146.944 142.839 1.00 8.87 ATOM 1763 CD1 ILE A 243 145.335 145.754 145.663 1.00 8.87 ATOM 1764 N LEU A 244 147.269 149.897 142.487 1.00 6.76 ATOM 1765 CA LEU A 244 147.052 151.025 141.589 1.00 6.76 ATOM 1766 C LEU A 244 148.143 151.108 140.529 1.00 6.76 ATOM 1767 O LEU A 244 147.855 151.298 139.341 1.00 6.76 ATOM 1768 CB LEU A 244 146.988 152.334 142.378 1.00 6.76 ATOM 1769 CG LEU A 244 145.814 152.484 143.348 1.00 6.76 ATOM 1770 CD1 LEU A 244 145.953 153.758 144.167 1.00 6.76 ATOM 1771 CD2 LEU A 244 144.497 152.549 142.590 1.00 6.76 ATOM 1772 N ILE A 245 149.404 150.942 140.936 1.00 5.13 ATOM 1773 CA ILE A 245 150.513 151.081 139.994 1.00 5.13 ATOM 1774 C ILE A 245 150.487 149.964 138.953 1.00 5.13 ATOM 1775 O ILE A 245 150.637 150.213 137.748 1.00 5.13 ATOM 1776 CB ILE A 245 151.872 151.070 140.717 1.00 5.13 ATOM 1777 CG1 ILE A 245 152.004 152.294 141.625 1.00 5.13 ATOM 1778 CG2 ILE A 245 153.012 151.091 139.710 1.00 5.13 ATOM 1779 CD1 ILE A 245 153.198 152.243 142.551 1.00 5.13 ATOM 1780 N LEU A 246 150.307 148.713 139.399 1.00 5.49 ATOM 1781 CA LEU A 246 150.268 147.609 138.442 1.00 5.49 ATOM 1782 C LEU A 246 149.091 147.735 137.488 1.00 5.49 ATOM 1783 O LEU A 246 149.224 147.439 136.299 1.00 5.49 ATOM 1784 CB LEU A 246 150.203 146.267 139.174 1.00 5.49 ATOM 1785 CG LEU A 246 151.422 145.896 140.020 1.00 5.49 ATOM 1786 CD1 LEU A 246 151.164 144.618 140.803 1.00 5.49 ATOM 1787 CD2 LEU A 246 152.640 145.674 139.137 1.00 5.49 ATOM 1788 N ALA A 247 147.925 148.166 137.981 1.00 4.39 ATOM 1789 CA ALA A 247 146.793 148.363 137.083 1.00 4.39 ATOM 1790 C ALA A 247 147.095 149.444 136.052 1.00 4.39 ATOM 1791 O ALA A 247 146.837 149.270 134.851 1.00 4.39 ATOM 1792 CB ALA A 247 145.530 148.727 137.878 1.00 4.39 ATOM 1793 N PHE A 248 147.670 150.563 136.506 1.00 3.00 ATOM 1794 CA PHE A 248 147.998 151.658 135.599 1.00 3.00 ATOM 1795 C PHE A 248 148.924 151.189 134.487 1.00 3.00 ATOM 1796 O PHE A 248 148.712 151.503 133.312 1.00 3.00 ATOM 1797 CB PHE A 248 148.639 152.816 136.366 1.00 3.00 ATOM 1798 CG PHE A 248 148.943 154.013 135.514 1.00 3.00 ATOM 1799 CD1 PHE A 248 147.947 154.915 135.180 1.00 3.00 ATOM 1800 CD2 PHE A 248 150.224 154.242 135.045 1.00 3.00 ATOM 1801 CE1 PHE A 248 148.225 156.017 134.395 1.00 3.00 ATOM 1802 CE2 PHE A 248 150.506 155.343 134.258 1.00 3.00 ATOM 1803 CZ PHE A 248 149.506 156.232 133.934 1.00 3.00 ATOM 1804 N PHE A 249 149.962 150.431 134.841 1.00 2.77 ATOM 1805 CA PHE A 249 150.913 150.006 133.818 1.00 2.77 ATOM 1806 C PHE A 249 150.371 148.870 132.954 1.00 2.77 ATOM 1807 O PHE A 249 150.716 148.779 131.768 1.00 2.77 ATOM 1808 CB PHE A 249 152.232 149.572 134.460 1.00 2.77 ATOM 1809 CG PHE A 249 152.965 150.685 135.151 1.00 2.77 ATOM 1810 CD1 PHE A 249 153.807 151.526 134.442 1.00 2.77 ATOM 1811 CD2 PHE A 249 152.813 150.897 136.510 1.00 2.77 ATOM 1812 CE1 PHE A 249 154.480 152.551 135.078 1.00 2.77 ATOM 1813 CE2 PHE A 249 153.486 151.920 137.149 1.00 2.77 ATOM 1814 CZ PHE A 249 154.321 152.748 136.432 1.00 2.77 ATOM 1815 N ALA A 250 149.530 148.002 133.524 1.00 3.39 ATOM 1816 CA ALA A 250 148.962 146.900 132.759 1.00 3.39 ATOM 1817 C ALA A 250 148.017 147.396 131.678 1.00 3.39 ATOM 1818 O ALA A 250 148.013 146.852 130.569 1.00 3.39 ATOM 1819 CB ALA A 250 148.225 145.922 133.686 1.00 3.39 ATOM 1820 N CYS A 251 147.209 148.417 131.971 1.00 4.65 ATOM 1821 CA CYS A 251 146.345 148.930 130.911 1.00 4.65 ATOM 1822 C CYS A 251 147.097 149.734 129.859 1.00 4.65 ATOM 1823 O CYS A 251 146.498 150.084 128.836 1.00 4.65 ATOM 1824 CB CYS A 251 145.232 149.799 131.500 1.00 4.65 ATOM 1825 SG CYS A 251 144.037 150.426 130.275 1.00 4.65 ATOM 1826 N TRP A 252 148.383 150.031 130.066 1.00 2.13 ATOM 1827 CA TRP A 252 149.143 150.837 129.121 1.00 2.13 ATOM 1828 C TRP A 252 150.158 150.059 128.294 1.00 2.13 ATOM 1829 O TRP A 252 150.474 150.496 127.185 1.00 2.13 ATOM 1830 CB TRP A 252 149.881 151.962 129.848 1.00 2.13 ATOM 1831 CG TRP A 252 150.886 151.472 130.846 1.00 2.13 ATOM 1832 CD1 TRP A 252 150.668 151.207 132.167 1.00 2.13 ATOM 1833 CD2 TRP A 252 152.270 151.190 130.599 1.00 2.13 ATOM 1834 NE1 TRP A 252 151.828 150.776 132.762 1.00 2.13 ATOM 1835 CE2 TRP A 252 152.828 150.757 131.819 1.00 2.13 ATOM 1836 CE3 TRP A 252 153.087 151.260 129.469 1.00 2.13 ATOM 1837 CZ2 TRP A 252 154.169 150.395 131.940 1.00 2.13 ATOM 1838 CZ3 TRP A 252 154.416 150.902 129.589 1.00 2.13 ATOM 1839 CH2 TRP A 252 154.948 150.473 130.817 1.00 2.13 ATOM 1840 N LEU A 253 150.676 148.936 128.799 1.00 1.94 ATOM 1841 CA LEU A 253 151.738 148.215 128.089 1.00 1.94 ATOM 1842 C LEU A 253 151.437 147.888 126.627 1.00 1.94 ATOM 1843 O LEU A 253 152.310 148.145 125.779 1.00 1.94 ATOM 1844 CB LEU A 253 152.068 146.905 128.806 1.00 1.94 ATOM 1845 CG LEU A 253 152.668 147.031 130.208 1.00 1.94 ATOM 1846 CD1 LEU A 253 152.809 145.663 130.857 1.00 1.94 ATOM 1847 CD2 LEU A 253 154.046 147.671 130.146 1.00 1.94 ATOM 1848 N PRO A 254 150.283 147.316 126.258 1.00 1.38 ATOM 1849 CA PRO A 254 150.086 146.954 124.842 1.00 1.38 ATOM 1850 C PRO A 254 150.138 148.140 123.888 1.00 1.38 ATOM 1851 O PRO A 254 150.642 148.000 122.765 1.00 1.38 ATOM 1852 CB PRO A 254 148.724 146.258 124.851 1.00 1.38 ATOM 1853 CG PRO A 254 148.615 145.676 126.243 1.00 1.38 ATOM 1854 CD PRO A 254 149.225 146.761 127.113 1.00 1.38 ATOM 1855 N TYR A 255 149.645 149.306 124.307 1.00 1.46 ATOM 1856 CA TYR A 255 149.749 150.498 123.469 1.00 1.46 ATOM 1857 C TYR A 255 151.205 150.883 123.241 1.00 1.46 ATOM 1858 O TYR A 255 151.593 151.256 122.126 1.00 1.46 ATOM 1859 CB TYR A 255 148.988 151.665 124.100 1.00 1.46 ATOM 1860 CG TYR A 255 149.522 152.086 125.451 1.00 1.46 ATOM 1861 CD1 TYR A 255 150.513 153.054 125.554 1.00 1.46 ATOM 1862 CD2 TYR A 255 149.035 151.514 126.619 1.00 1.46 ATOM 1863 CE1 TYR A 255 151.006 153.444 126.782 1.00 1.46 ATOM 1864 CE2 TYR A 255 149.516 151.891 127.857 1.00 1.46 ATOM 1865 CZ TYR A 255 150.503 152.858 127.938 1.00 1.46 ATOM 1866 OH TYR A 255 150.989 153.240 129.165 1.00 1.46 ATOM 1867 N TYR A 256 152.024 150.799 124.292 1.00 0.91 ATOM 1868 CA TYR A 256 153.442 151.110 124.158 1.00 0.91 ATOM 1869 C TYR A 256 154.139 150.120 123.235 1.00 0.91 ATOM 1870 O TYR A 256 154.992 150.511 122.429 1.00 0.91 ATOM 1871 CB TYR A 256 154.121 151.118 125.529 1.00 0.91 ATOM 1872 CG TYR A 256 153.627 152.209 126.452 1.00 0.91 ATOM 1873 CD1 TYR A 256 154.165 153.488 126.394 1.00 0.91 ATOM 1874 CD2 TYR A 256 152.623 151.957 127.378 1.00 0.91 ATOM 1875 CE1 TYR A 256 153.719 154.490 127.233 1.00 0.91 ATOM 1876 CE2 TYR A 256 152.164 152.947 128.226 1.00 0.91 ATOM 1877 CZ TYR A 256 152.713 154.213 128.151 1.00 0.91 ATOM 1878 OH TYR A 256 152.264 155.207 128.989 1.00 0.91 ATOM 1879 N ILE A 257 153.785 148.837 123.329 1.00 1.09 ATOM 1880 CA ILE A 257 154.348 147.850 122.412 1.00 1.09 ATOM 1881 C ILE A 257 153.979 148.189 120.973 1.00 1.09 ATOM 1882 O ILE A 257 154.824 148.148 120.068 1.00 1.09 ATOM 1883 CB ILE A 257 153.862 146.428 122.746 1.00 1.09 ATOM 1884 CG1 ILE A 257 154.382 145.995 124.119 1.00 1.09 ATOM 1885 CG2 ILE A 257 154.361 145.436 121.707 1.00 1.09 ATOM 1886 CD1 ILE A 257 153.762 144.714 124.631 1.00 1.09 ATOM 1887 N GLY A 258 152.713 148.546 120.742 1.00 2.26 ATOM 1888 CA GLY A 258 152.289 148.894 119.395 1.00 2.26 ATOM 1889 C GLY A 258 153.020 150.100 118.834 1.00 2.26 ATOM 1890 O GLY A 258 153.468 150.086 117.682 1.00 2.26 ATOM 1891 N ILE A 259 153.155 151.160 119.637 1.00 2.01 ATOM 1892 CA ILE A 259 153.819 152.361 119.134 1.00 2.01 ATOM 1893 C ILE A 259 155.307 152.112 118.925 1.00 2.01 ATOM 1894 O ILE A 259 155.907 152.647 117.986 1.00 2.01 ATOM 1895 CB ILE A 259 153.633 153.552 120.092 1.00 2.01 ATOM 1896 CG1 ILE A 259 152.157 153.950 120.168 1.00 2.01 ATOM 1897 CG2 ILE A 259 154.433 154.753 119.612 1.00 2.01 ATOM 1898 CD1 ILE A 259 151.849 154.949 121.261 1.00 2.01 ATOM 1899 N SER A 260 155.931 151.298 119.785 1.00 2.35 ATOM 1900 CA SER A 260 157.334 150.953 119.576 1.00 2.35 ATOM 1901 C SER A 260 157.521 150.195 118.270 1.00 2.35 ATOM 1902 O SER A 260 158.446 150.485 117.499 1.00 2.35 ATOM 1903 CB SER A 260 157.863 150.124 120.748 1.00 2.35 ATOM 1904 OG SER A 260 157.159 148.900 120.864 1.00 2.35 ATOM 1905 N ILE A 261 156.639 149.231 117.997 1.00 3.82 ATOM 1906 CA ILE A 261 156.732 148.487 116.745 1.00 3.82 ATOM 1907 C ILE A 261 156.543 149.420 115.555 1.00 3.82 ATOM 1908 O ILE A 261 157.280 149.337 114.565 1.00 3.82 ATOM 1909 CB ILE A 261 155.689 147.356 116.682 1.00 3.82 ATOM 1910 CG1 ILE A 261 155.975 146.306 117.758 1.00 3.82 ATOM 1911 CG2 ILE A 261 155.722 146.675 115.322 1.00 3.82 ATOM 1912 CD1 ILE A 261 154.870 145.287 117.926 1.00 3.82 ATOM 1913 N ASP A 262 155.568 150.331 115.634 1.00 5.56 ATOM 1914 CA ASP A 262 155.335 151.251 114.522 1.00 5.56 ATOM 1915 C ASP A 262 156.544 152.152 114.293 1.00 5.56 ATOM 1916 O ASP A 262 156.964 152.364 113.147 1.00 5.56 ATOM 1917 CB ASP A 262 154.087 152.098 114.779 1.00 5.56 ATOM 1918 CG ASP A 262 152.818 151.269 114.820 1.00 5.56 ATOM 1919 OD1 ASP A 262 152.505 150.613 113.804 1.00 5.56 ATOM 1920 OD2 ASP A 262 152.138 151.275 115.867 1.00 5.56 ATOM 1921 N SER A 263 157.131 152.677 115.372 1.00 5.68 ATOM 1922 CA SER A 263 158.303 153.534 115.233 1.00 5.68 ATOM 1923 C SER A 263 159.465 152.772 114.614 1.00 5.68 ATOM 1924 O SER A 263 160.218 153.326 113.803 1.00 5.68 ATOM 1925 CB SER A 263 158.711 154.109 116.591 1.00 5.68 ATOM 1926 OG SER A 263 157.711 154.973 117.100 1.00 5.68 ATOM 1927 N PHE A 264 159.631 151.501 114.983 1.00 6.12 ATOM 1928 CA PHE A 264 160.662 150.687 114.345 1.00 6.12 ATOM 1929 C PHE A 264 160.372 150.486 112.862 1.00 6.12 ATOM 1930 O PHE A 264 161.295 150.485 112.041 1.00 6.12 ATOM 1931 CB PHE A 264 160.783 149.331 115.043 1.00 6.12 ATOM 1932 CG PHE A 264 161.873 148.460 114.490 1.00 6.12 ATOM 1933 CD1 PHE A 264 163.193 148.658 114.859 1.00 6.12 ATOM 1934 CD2 PHE A 264 161.582 147.441 113.602 1.00 6.12 ATOM 1935 CE1 PHE A 264 164.197 147.857 114.350 1.00 6.12 ATOM 1936 CE2 PHE A 264 162.584 146.638 113.090 1.00 6.12 ATOM 1937 CZ PHE A 264 163.892 146.845 113.466 1.00 6.12 ATOM 1938 N ILE A 265 159.098 150.307 112.499 1.00 8.20 ATOM 1939 CA ILE A 265 158.742 150.241 111.081 1.00 8.20 ATOM 1940 C ILE A 265 159.116 151.534 110.377 1.00 8.20 ATOM 1941 O ILE A 265 159.479 151.527 109.194 1.00 8.20 ATOM 1942 CB ILE A 265 157.239 149.969 110.889 1.00 8.20 ATOM 1943 CG1 ILE A 265 156.875 148.583 111.426 1.00 8.20 ATOM 1944 CG2 ILE A 265 156.870 150.027 109.414 1.00 8.20 ATOM 1945 CD1 ILE A 265 155.386 148.326 111.497 1.00 8.20 ATOM 1946 N LEU A 266 159.030 152.664 111.083 1.00 9.01 ATOM 1947 CA LEU A 266 159.319 153.948 110.453 1.00 9.01 ATOM 1948 C LEU A 266 160.779 154.050 110.021 1.00 9.01 ATOM 1949 O LEU A 266 161.077 154.601 108.955 1.00 9.01 ATOM 1950 CB LEU A 266 158.977 155.099 111.401 1.00 9.01 ATOM 1951 CG LEU A 266 157.500 155.262 111.765 1.00 9.01 ATOM 1952 CD1 LEU A 266 157.322 156.343 112.820 1.00 9.01 ATOM 1953 CD2 LEU A 266 156.686 155.656 110.541 1.00 9.01 ATOM 1954 N LEU A 267 161.704 153.534 110.829 1.00 8.89 ATOM 1955 CA LEU A 267 163.127 153.610 110.489 1.00 8.89 ATOM 1956 C LEU A 267 163.600 152.382 109.717 1.00 8.89 ATOM 1957 O LEU A 267 164.647 151.815 110.022 1.00 8.89 ATOM 1958 CB LEU A 267 163.972 153.778 111.753 1.00 8.89 ATOM 1959 CG LEU A 267 163.774 155.080 112.533 1.00 8.89 ATOM 1960 CD1 LEU A 267 164.560 155.051 113.835 1.00 8.89 ATOM 1961 CD2 LEU A 267 164.249 156.272 111.718 1.00 8.89 ATOM 1962 N GLU A 268 162.841 151.997 108.690 1.00 12.54 ATOM 1963 CA GLU A 268 163.202 150.938 107.741 1.00 12.54 ATOM 1964 C GLU A 268 163.905 149.760 108.417 1.00 12.54 ATOM 1965 O GLU A 268 164.952 149.285 107.970 1.00 12.54 ATOM 1966 CB GLU A 268 164.097 151.494 106.632 1.00 12.54 ATOM 1967 CG GLU A 268 165.495 151.873 107.094 1.00 12.54 ATOM 1968 CD GLU A 268 165.536 153.224 107.781 1.00 12.54 ATOM 1969 OE1 GLU A 268 164.470 153.864 107.897 1.00 12.54 ATOM 1970 OE2 GLU A 268 166.633 153.641 108.206 1.00 12.54 ATOM 1971 N ILE A 269 163.319 149.284 109.513 1.00 10.34 ATOM 1972 CA ILE A 269 163.849 148.148 110.251 1.00 10.34 ATOM 1973 C ILE A 269 162.949 146.924 110.126 1.00 10.34 ATOM 1974 O ILE A 269 163.440 145.806 109.960 1.00 10.34 ATOM 1975 CB ILE A 269 164.031 148.480 111.743 1.00 10.34 ATOM 1976 CG1 ILE A 269 165.094 149.565 111.923 1.00 10.34 ATOM 1977 CG2 ILE A 269 164.467 147.244 112.516 1.00 10.34 ATOM 1978 CD1 ILE A 269 165.169 150.122 113.327 1.00 10.34 ATOM 1979 N ILE A 270 161.633 147.118 110.162 1.00 12.61 ATOM 1980 CA ILE A 270 160.687 146.008 110.131 1.00 12.61 ATOM 1981 C ILE A 270 159.910 146.086 108.824 1.00 12.61 ATOM 1982 O ILE A 270 158.703 145.821 108.783 1.00 12.61 ATOM 1983 CB ILE A 270 159.732 146.047 111.338 1.00 12.61 ATOM 1984 CG1 ILE A 270 160.508 145.834 112.640 1.00 12.61 ATOM 1985 CG2 ILE A 270 158.679 144.956 111.220 1.00 12.61 ATOM 1986 CD1 ILE A 270 159.692 146.094 113.887 1.00 12.61 ATOM 1987 N LYS A 271 160.586 146.498 107.753 1.00 20.08 ATOM 1988 CA LYS A 271 159.944 146.559 106.446 1.00 20.08 ATOM 1989 C LYS A 271 159.383 145.197 106.062 1.00 20.08 ATOM 1990 O LYS A 271 160.138 144.260 105.782 1.00 20.08 ATOM 1991 CB LYS A 271 160.932 147.048 105.386 1.00 20.08 ATOM 1992 CG LYS A 271 161.460 148.453 105.630 1.00 20.08 ATOM 1993 CD LYS A 271 160.363 149.491 105.460 1.00 20.08 ATOM 1994 CE LYS A 271 160.890 150.896 105.705 1.00 20.08 ATOM 1995 NZ LYS A 271 161.328 151.087 107.116 1.00 20.08 ATOM 1996 N GLN A 272 158.052 145.080 106.045 1.00 23.10 ATOM 1997 CA GLN A 272 157.402 143.807 105.765 1.00 23.10 ATOM 1998 C GLN A 272 156.183 143.957 104.865 1.00 23.10 ATOM 1999 O GLN A 272 155.418 142.994 104.724 1.00 23.10 ATOM 2000 CB GLN A 272 156.988 143.119 107.067 1.00 23.10 ATOM 2001 CG GLN A 272 155.843 143.804 107.795 1.00 23.10 ATOM 2002 CD GLN A 272 156.277 145.076 108.497 1.00 23.10 ATOM 2003 OE1 GLN A 272 157.446 145.457 108.445 1.00 23.10 ATOM 2004 NE2 GLN A 272 155.333 145.738 109.155 1.00 23.10 ATOM 2005 N GLY A 273 155.971 145.117 104.263 1.00 28.78 ATOM 2006 CA GLY A 273 154.818 145.360 103.419 1.00 28.78 ATOM 2007 C GLY A 273 153.881 146.386 104.033 1.00 28.78 ATOM 2008 O GLY A 273 154.091 146.889 105.138 1.00 28.78 ATOM 2009 N CYS A 274 152.827 146.689 103.277 1.00 34.71 ATOM 2010 CA CYS A 274 151.843 147.679 103.686 1.00 34.71 ATOM 2011 C CYS A 274 150.737 147.107 104.564 1.00 34.71 ATOM 2012 O CYS A 274 149.941 147.879 105.107 1.00 34.71 ATOM 2013 CB CYS A 274 151.210 148.343 102.462 1.00 34.71 ATOM 2014 SG CYS A 274 150.020 149.666 102.853 1.00 34.71 ATOM 2015 N GLU A 275 150.665 145.788 104.717 1.00 31.72 ATOM 2016 CA GLU A 275 149.596 145.165 105.486 1.00 31.72 ATOM 2017 C GLU A 275 149.905 145.064 106.974 1.00 31.72 ATOM 2018 O GLU A 275 149.026 144.664 107.745 1.00 31.72 ATOM 2019 CB GLU A 275 149.291 143.767 104.945 1.00 31.72 ATOM 2020 CG GLU A 275 148.732 143.756 103.532 1.00 31.72 ATOM 2021 CD GLU A 275 149.820 143.791 102.475 1.00 31.72 ATOM 2022 OE1 GLU A 275 151.011 143.823 102.850 1.00 31.72 ATOM 2023 OE2 GLU A 275 149.480 143.784 101.273 1.00 31.72 ATOM 2024 N PHE A 276 151.121 145.405 107.393 1.00 21.90 ATOM 2025 CA PHE A 276 151.477 145.407 108.808 1.00 21.90 ATOM 2026 C PHE A 276 151.136 146.725 109.493 1.00 21.90 ATOM 2027 O PHE A 276 150.753 146.732 110.675 1.00 21.90 ATOM 2028 CB PHE A 276 152.967 145.112 108.986 1.00 21.90 ATOM 2029 CG PHE A 276 153.401 145.027 110.421 1.00 21.90 ATOM 2030 CD1 PHE A 276 153.185 143.874 111.157 1.00 21.90 ATOM 2031 CD2 PHE A 276 154.026 146.096 111.036 1.00 21.90 ATOM 2032 CE1 PHE A 276 153.583 143.795 112.478 1.00 21.90 ATOM 2033 CE2 PHE A 276 154.425 146.020 112.357 1.00 21.90 ATOM 2034 CZ PHE A 276 154.205 144.868 113.078 1.00 21.90 ATOM 2035 N GLU A 277 151.262 147.840 108.767 1.00 22.03 ATOM 2036 CA GLU A 277 150.998 149.150 109.347 1.00 22.03 ATOM 2037 C GLU A 277 149.536 149.299 109.750 1.00 22.03 ATOM 2038 O GLU A 277 149.235 149.862 110.809 1.00 22.03 ATOM 2039 CB GLU A 277 151.384 150.258 108.366 1.00 22.03 ATOM 2040 CG GLU A 277 150.596 150.238 107.065 1.00 22.03 ATOM 2041 CD GLU A 277 151.004 151.350 106.120 1.00 22.03 ATOM 2042 OE1 GLU A 277 152.190 151.391 105.727 1.00 22.03 ATOM 2043 OE2 GLU A 277 150.139 152.180 105.768 1.00 22.03 ATOM 2044 N ASN A 278 148.611 148.812 108.922 1.00 20.51 ATOM 2045 CA ASN A 278 147.197 148.913 109.269 1.00 20.51 ATOM 2046 C ASN A 278 146.883 148.124 110.533 1.00 20.51 ATOM 2047 O ASN A 278 146.149 148.598 111.414 1.00 20.51 ATOM 2048 CB ASN A 278 146.325 148.422 108.112 1.00 20.51 ATOM 2049 CG ASN A 278 146.352 149.361 106.923 1.00 20.51 ATOM 2050 OD1 ASN A 278 145.652 150.373 106.903 1.00 20.51 ATOM 2051 ND2 ASN A 278 147.163 149.027 105.926 1.00 20.51 ATOM 2052 N THR A 279 147.440 146.915 110.644 1.00 14.40 ATOM 2053 CA THR A 279 147.209 146.098 111.829 1.00 14.40 ATOM 2054 C THR A 279 147.756 146.773 113.079 1.00 14.40 ATOM 2055 O THR A 279 147.088 146.809 114.122 1.00 14.40 ATOM 2056 CB THR A 279 147.850 144.705 111.688 1.00 14.40 ATOM 2057 OG1 THR A 279 149.270 144.842 111.549 1.00 14.40 ATOM 2058 CG2 THR A 279 147.303 143.988 110.463 1.00 14.40 ATOM 2059 N VAL A 280 148.968 147.327 112.994 1.00 11.61 ATOM 2060 CA VAL A 280 149.525 147.967 114.182 1.00 11.61 ATOM 2061 C VAL A 280 148.748 149.237 114.528 1.00 11.61 ATOM 2062 O VAL A 280 148.580 149.563 115.708 1.00 11.61 ATOM 2063 CB VAL A 280 151.012 148.316 113.990 1.00 11.61 ATOM 2064 CG1 VAL A 280 151.538 149.090 115.189 1.00 11.61 ATOM 2065 CG2 VAL A 280 151.841 147.049 113.835 1.00 11.61 ATOM 2066 N HIS A 281 148.228 149.955 113.523 1.00 10.22 ATOM 2067 CA HIS A 281 147.403 151.129 113.802 1.00 10.22 ATOM 2068 C HIS A 281 146.129 150.749 114.549 1.00 10.22 ATOM 2069 O HIS A 281 145.733 151.424 115.512 1.00 10.22 ATOM 2070 CB HIS A 281 147.051 151.857 112.504 1.00 10.22 ATOM 2071 CG HIS A 281 148.234 152.444 111.799 1.00 10.22 ATOM 2072 ND1 HIS A 281 148.943 153.514 112.300 1.00 10.22 ATOM 2073 CD2 HIS A 281 148.834 152.111 110.632 1.00 10.22 ATOM 2074 CE1 HIS A 281 149.927 153.813 111.470 1.00 10.22 ATOM 2075 NE2 HIS A 281 149.884 152.978 110.453 1.00 10.22 ATOM 2076 N LYS A 282 145.462 149.679 114.109 1.00 7.74 ATOM 2077 CA LYS A 282 144.259 149.230 114.808 1.00 7.74 ATOM 2078 C LYS A 282 144.581 148.792 116.233 1.00 7.74 ATOM 2079 O LYS A 282 143.818 149.075 117.174 1.00 7.74 ATOM 2080 CB LYS A 282 143.591 148.086 114.044 1.00 7.74 ATOM 2081 CG LYS A 282 143.117 148.463 112.650 1.00 7.74 ATOM 2082 CD LYS A 282 141.960 149.446 112.708 1.00 7.74 ATOM 2083 CE LYS A 282 141.486 149.824 111.314 1.00 7.74 ATOM 2084 NZ LYS A 282 140.350 150.788 111.355 1.00 7.74 ATOM 2085 N TRP A 283 145.709 148.096 116.408 1.00 3.88 ATOM 2086 CA TRP A 283 146.175 147.746 117.745 1.00 3.88 ATOM 2087 C TRP A 283 146.309 148.989 118.619 1.00 3.88 ATOM 2088 O TRP A 283 145.841 149.019 119.767 1.00 3.88 ATOM 2089 CB TRP A 283 147.511 147.005 117.670 1.00 3.88 ATOM 2090 CG TRP A 283 148.020 146.550 119.003 1.00 3.88 ATOM 2091 CD1 TRP A 283 149.039 147.103 119.725 1.00 3.88 ATOM 2092 CD2 TRP A 283 147.530 145.444 119.775 1.00 3.88 ATOM 2093 NE1 TRP A 283 149.217 146.412 120.899 1.00 3.88 ATOM 2094 CE2 TRP A 283 148.302 145.388 120.952 1.00 3.88 ATOM 2095 CE3 TRP A 283 146.518 144.501 119.582 1.00 3.88 ATOM 2096 CZ2 TRP A 283 148.092 144.423 121.936 1.00 3.88 ATOM 2097 CZ3 TRP A 283 146.312 143.545 120.557 1.00 3.88 ATOM 2098 CH2 TRP A 283 147.093 143.510 121.725 1.00 3.88 ATOM 2099 N ILE A 284 146.931 150.038 118.071 1.00 3.95 ATOM 2100 CA ILE A 284 147.132 151.280 118.811 1.00 3.95 ATOM 2101 C ILE A 284 145.799 151.886 119.226 1.00 3.95 ATOM 2102 O ILE A 284 145.632 152.329 120.369 1.00 3.95 ATOM 2103 CB ILE A 284 147.922 152.309 117.982 1.00 3.95 ATOM 2104 CG1 ILE A 284 149.342 151.804 117.716 1.00 3.95 ATOM 2105 CG2 ILE A 284 148.012 153.635 118.723 1.00 3.95 ATOM 2106 CD1 ILE A 284 150.109 152.636 116.713 1.00 3.95 ATOM 2107 N SER A 285 144.829 151.917 118.309 1.00 3.83 ATOM 2108 CA SER A 285 143.537 152.531 118.620 1.00 3.83 ATOM 2109 C SER A 285 142.829 151.799 119.761 1.00 3.83 ATOM 2110 O SER A 285 142.393 152.420 120.748 1.00 3.83 ATOM 2111 CB SER A 285 142.642 152.554 117.380 1.00 3.83 ATOM 2112 OG SER A 285 142.365 151.240 116.927 1.00 3.83 ATOM 2113 N ILE A 286 142.711 150.473 119.645 1.00 3.55 ATOM 2114 CA ILE A 286 141.993 149.725 120.675 1.00 3.55 ATOM 2115 C ILE A 286 142.707 149.842 122.019 1.00 3.55 ATOM 2116 O ILE A 286 142.070 149.964 123.078 1.00 3.55 ATOM 2117 CB ILE A 286 141.852 148.239 120.298 1.00 3.55 ATOM 2118 CG1 ILE A 286 140.976 148.086 119.052 1.00 3.55 ATOM 2119 CG2 ILE A 286 141.212 147.458 121.436 1.00 3.55 ATOM 2120 CD1 ILE A 286 140.977 146.689 118.472 1.00 3.55 ATOM 2121 N THR A 287 144.042 149.837 121.999 1.00 2.79 ATOM 2122 CA THR A 287 144.776 149.926 123.255 1.00 2.79 ATOM 2123 C THR A 287 144.677 151.316 123.877 1.00 2.79 ATOM 2124 O THR A 287 144.700 151.445 125.109 1.00 2.79 ATOM 2125 CB THR A 287 146.263 149.576 123.065 1.00 2.79 ATOM 2126 OG1 THR A 287 146.867 150.514 122.165 1.00 2.79 ATOM 2127 CG2 THR A 287 146.412 148.176 122.489 1.00 2.79 ATOM 2128 N GLU A 288 144.546 152.364 123.057 1.00 3.78 ATOM 2129 CA GLU A 288 144.241 153.687 123.596 1.00 3.78 ATOM 2130 C GLU A 288 142.907 153.677 124.327 1.00 3.78 ATOM 2131 O GLU A 288 142.775 154.252 125.422 1.00 3.78 ATOM 2132 CB GLU A 288 144.227 154.731 122.478 1.00 3.78 ATOM 2133 CG GLU A 288 145.577 154.947 121.814 1.00 3.78 ATOM 2134 CD GLU A 288 145.847 153.948 120.705 1.00 3.78 ATOM 2135 OE1 GLU A 288 144.978 153.086 120.458 1.00 3.78 ATOM 2136 OE2 GLU A 288 146.928 154.028 120.084 1.00 3.78 ATOM 2137 N ALA A 289 141.901 153.035 123.730 1.00 2.68 ATOM 2138 CA ALA A 289 140.606 152.939 124.401 1.00 2.68 ATOM 2139 C ALA A 289 140.737 152.244 125.756 1.00 2.68 ATOM 2140 O ALA A 289 140.163 152.691 126.759 1.00 2.68 ATOM 2141 CB ALA A 289 139.595 152.191 123.519 1.00 2.68 ATOM 2142 N LEU A 290 141.512 151.160 125.811 1.00 4.23 ATOM 2143 CA LEU A 290 141.672 150.461 127.087 1.00 4.23 ATOM 2144 C LEU A 290 142.471 151.284 128.104 1.00 4.23 ATOM 2145 O LEU A 290 142.236 151.186 129.319 1.00 4.23 ATOM 2146 CB LEU A 290 142.354 149.108 126.875 1.00 4.23 ATOM 2147 CG LEU A 290 141.575 148.076 126.057 1.00 4.23 ATOM 2148 CD1 LEU A 290 142.424 146.841 125.801 1.00 4.23 ATOM 2149 CD2 LEU A 290 140.318 147.644 126.795 1.00 4.23 ATOM 2150 N ALA A 291 143.407 152.111 127.642 1.00 3.62 ATOM 2151 CA ALA A 291 144.080 153.022 128.566 1.00 3.62 ATOM 2152 C ALA A 291 143.089 154.008 129.184 1.00 3.62 ATOM 2153 O ALA A 291 143.126 154.282 130.393 1.00 3.62 ATOM 2154 CB ALA A 291 145.206 153.782 127.850 1.00 3.62 ATOM 2155 N PHE A 292 142.186 154.549 128.370 1.00 2.60 ATOM 2156 CA PHE A 292 141.148 155.400 128.947 1.00 2.60 ATOM 2157 C PHE A 292 140.297 154.610 129.945 1.00 2.60 ATOM 2158 O PHE A 292 139.829 155.159 130.958 1.00 2.60 ATOM 2159 CB PHE A 292 140.267 155.993 127.846 1.00 2.60 ATOM 2160 CG PHE A 292 139.217 156.938 128.352 1.00 2.60 ATOM 2161 CD1 PHE A 292 139.537 158.248 128.667 1.00 2.60 ATOM 2162 CD2 PHE A 292 137.908 156.521 128.515 1.00 2.60 ATOM 2163 CE1 PHE A 292 138.571 159.119 129.134 1.00 2.60 ATOM 2164 CE2 PHE A 292 136.940 157.388 128.983 1.00 2.60 ATOM 2165 CZ PHE A 292 137.271 158.689 129.291 1.00 2.60 ATOM 2166 N PHE A 293 140.109 153.313 129.686 1.00 4.88 ATOM 2167 CA PHE A 293 139.477 152.454 130.685 1.00 4.88 ATOM 2168 C PHE A 293 140.236 152.482 132.006 1.00 4.88 ATOM 2169 O PHE A 293 139.625 152.451 133.075 1.00 4.88 ATOM 2170 CB PHE A 293 139.378 151.017 130.170 1.00 4.88 ATOM 2171 CG PHE A 293 138.674 150.083 131.112 1.00 4.88 ATOM 2172 CD1 PHE A 293 137.292 150.052 131.176 1.00 4.88 ATOM 2173 CD2 PHE A 293 139.392 149.234 131.935 1.00 4.88 ATOM 2174 CE1 PHE A 293 136.643 149.193 132.043 1.00 4.88 ATOM 2175 CE2 PHE A 293 138.748 148.375 132.804 1.00 4.88 ATOM 2176 CZ PHE A 293 137.372 148.353 132.857 1.00 4.88 ATOM 2177 N HIS A 294 141.570 152.516 131.959 1.00 5.68 ATOM 2178 CA HIS A 294 142.326 152.656 133.213 1.00 5.68 ATOM 2179 C HIS A 294 142.006 153.984 133.893 1.00 5.68 ATOM 2180 O HIS A 294 141.912 154.072 135.135 1.00 5.68 ATOM 2181 CB HIS A 294 143.828 152.543 132.949 1.00 5.68 ATOM 2182 CG HIS A 294 144.256 151.196 132.453 1.00 5.68 ATOM 2183 ND1 HIS A 294 145.486 150.970 131.876 1.00 5.68 ATOM 2184 CD2 HIS A 294 143.615 150.003 132.449 1.00 5.68 ATOM 2185 CE1 HIS A 294 145.582 149.697 131.538 1.00 5.68 ATOM 2186 NE2 HIS A 294 144.462 149.088 131.875 1.00 5.68 ATOM 2187 N CYS A 295 141.902 155.042 133.083 1.00 4.86 ATOM 2188 CA CYS A 295 141.578 156.361 133.618 1.00 4.86 ATOM 2189 C CYS A 295 140.284 156.312 134.415 1.00 4.86 ATOM 2190 O CYS A 295 140.145 156.990 135.438 1.00 4.86 ATOM 2191 CB CYS A 295 141.471 157.386 132.488 1.00 4.86 ATOM 2192 SG CYS A 295 143.031 157.695 131.600 1.00 4.86 ATOM 2193 N CYS A 296 139.326 155.508 133.955 1.00 6.17 ATOM 2194 CA CYS A 296 138.136 155.250 134.769 1.00 6.17 ATOM 2195 C CYS A 296 138.384 154.275 135.914 1.00 6.17 ATOM 2196 O CYS A 296 137.694 154.345 136.934 1.00 6.17 ATOM 2197 CB CYS A 296 136.998 154.713 133.899 1.00 6.17 ATOM 2198 SG CYS A 296 136.377 155.894 132.658 1.00 6.17 ATOM 2199 N LEU A 297 139.325 153.346 135.754 1.00 11.85 ATOM 2200 CA LEU A 297 139.525 152.309 136.759 1.00 11.85 ATOM 2201 C LEU A 297 140.083 152.862 138.060 1.00 11.85 ATOM 2202 O LEU A 297 139.965 152.200 139.097 1.00 11.85 ATOM 2203 CB LEU A 297 140.458 151.220 136.227 1.00 11.85 ATOM 2204 CG LEU A 297 139.940 150.402 135.042 1.00 11.85 ATOM 2205 CD1 LEU A 297 141.019 149.462 134.525 1.00 11.85 ATOM 2206 CD2 LEU A 297 138.739 149.565 135.452 1.00 11.85 ATOM 2207 N ASN A 298 140.709 154.037 138.030 1.00 9.44 ATOM 2208 CA ASN A 298 141.247 154.588 139.276 1.00 9.44 ATOM 2209 C ASN A 298 140.184 154.794 140.358 1.00 9.44 ATOM 2210 O ASN A 298 140.337 154.246 141.468 1.00 9.44 ATOM 2211 CB ASN A 298 141.951 155.920 139.013 1.00 9.44 ATOM 2212 CG ASN A 298 142.590 156.498 140.260 1.00 9.44 ATOM 2213 OD1 ASN A 298 143.448 155.870 140.878 1.00 9.44 ATOM 2214 ND2 ASN A 298 142.173 157.702 140.633 1.00 9.44 ATOM 2215 N PRO A 299 139.104 155.561 140.132 1.00 9.57 ATOM 2216 CA PRO A 299 138.109 155.735 141.211 1.00 9.57 ATOM 2217 C PRO A 299 137.419 154.444 141.616 1.00 9.57 ATOM 2218 O PRO A 299 136.969 154.323 142.763 1.00 9.57 ATOM 2219 CB PRO A 299 137.146 156.770 140.627 1.00 9.57 ATOM 2220 CG PRO A 299 138.000 157.572 139.670 1.00 9.57 ATOM 2221 CD PRO A 299 138.885 156.513 139.037 1.00 9.57 ATOM 2222 N ILE A 300 137.310 153.476 140.704 1.00 9.00 ATOM 2223 CA ILE A 300 136.759 152.174 141.062 1.00 9.00 ATOM 2224 C ILE A 300 137.623 151.515 142.129 1.00 9.00 ATOM 2225 O ILE A 300 137.112 150.970 143.114 1.00 9.00 ATOM 2226 CB ILE A 300 136.654 151.249 139.835 1.00 9.00 ATOM 2227 CG1 ILE A 300 135.649 151.811 138.828 1.00 9.00 ATOM 2228 CG2 ILE A 300 136.195 149.860 140.252 1.00 9.00 ATOM 2229 CD1 ILE A 300 135.657 151.099 137.494 1.00 9.00 ATOM 2230 N LEU A 301 138.945 151.562 141.949 1.00 10.32 ATOM 2231 CA LEU A 301 139.848 151.100 142.997 1.00 10.32 ATOM 2232 C LEU A 301 139.675 151.916 144.267 1.00 10.32 ATOM 2233 O LEU A 301 139.832 151.385 145.372 1.00 10.32 ATOM 2234 CB LEU A 301 141.300 151.167 142.521 1.00 10.32 ATOM 2235 CG LEU A 301 141.678 150.241 141.362 1.00 10.32 ATOM 2236 CD1 LEU A 301 143.100 150.515 140.897 1.00 10.32 ATOM 2237 CD2 LEU A 301 141.589 148.785 141.788 1.00 10.32 ATOM 2238 N TYR A 302 139.275 153.174 144.117 1.00 11.19 ATOM 2239 CA TYR A 302 139.039 154.032 145.271 1.00 11.19 ATOM 2240 C TYR A 302 137.751 153.656 145.998 1.00 11.19 ATOM 2241 O TYR A 302 137.567 154.019 147.159 1.00 11.19 ATOM 2242 CB TYR A 302 138.986 155.500 144.845 1.00 11.19 ATOM 2243 CG TYR A 302 140.294 156.028 144.300 1.00 11.19 ATOM 2244 CD1 TYR A 302 141.277 156.513 145.153 1.00 11.19 ATOM 2245 CD2 TYR A 302 140.541 156.041 142.933 1.00 11.19 ATOM 2246 CE1 TYR A 302 142.474 156.996 144.663 1.00 11.19 ATOM 2247 CE2 TYR A 302 141.734 156.521 142.425 1.00 11.19 ATOM 2248 CZ TYR A 302 142.698 156.997 143.292 1.00 11.19 ATOM 2249 OH TYR A 302 143.889 157.478 142.797 1.00 11.19 ATOM 2250 N ALA A 303 136.857 152.933 145.327 1.00 11.52 ATOM 2251 CA ALA A 303 135.571 152.583 145.928 1.00 11.52 ATOM 2252 C ALA A 303 135.681 151.388 146.872 1.00 11.52 ATOM 2253 O ALA A 303 135.113 151.408 147.971 1.00 11.52 ATOM 2254 CB ALA A 303 134.530 152.283 144.839 1.00 11.52 ATOM 2255 N PHE A 304 136.392 150.335 146.458 1.00 14.49 ATOM 2256 CA PHE A 304 136.395 149.090 147.223 1.00 14.49 ATOM 2257 C PHE A 304 137.024 149.271 148.600 1.00 14.49 ATOM 2258 O PHE A 304 136.480 148.793 149.603 1.00 14.49 ATOM 2259 CB PHE A 304 137.135 147.992 146.457 1.00 14.49 ATOM 2260 CG PHE A 304 136.466 147.591 145.175 1.00 14.49 ATOM 2261 CD1 PHE A 304 135.453 146.647 145.170 1.00 14.49 ATOM 2262 CD2 PHE A 304 136.845 148.158 143.971 1.00 14.49 ATOM 2263 CE1 PHE A 304 134.837 146.278 143.990 1.00 14.49 ATOM 2264 CE2 PHE A 304 136.231 147.791 142.788 1.00 14.49 ATOM 2265 CZ PHE A 304 135.226 146.850 142.798 1.00 14.49 ATOM 2266 N LEU A 305 138.162 149.956 148.665 1.00 14.61 ATOM 2267 CA LEU A 305 138.909 150.147 149.906 1.00 14.61 ATOM 2268 C LEU A 305 139.225 148.807 150.568 1.00 14.61 ATOM 2269 O LEU A 305 140.389 148.462 150.765 1.00 14.61 ATOM 2270 CB LEU A 305 138.127 151.041 150.870 1.00 14.61 ATOM 2271 CG LEU A 305 137.901 152.487 150.423 1.00 14.61 ATOM 2272 CD1 LEU A 305 136.992 153.216 151.400 1.00 14.61 ATOM 2273 CD2 LEU A 305 139.221 153.238 150.352 1.00 14.61 END If you find results from this site helpful for your research, please cite one of our papers:
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