HEADER TRANSFERASE 17-JUL-02 1M6Y TITLE CRYSTAL STRUCTURE ANALYSIS OF TM0872, A PUTATIVE SAM- TITLE 2 DEPENDENT METHYLTRANSFERASE, COMPLEXED WITH SAH COMPND MOL_ID: 1; COMPND 2 MOLECULE: S-ADENOSYL-METHYLTRANSFERASE MRAW; COMPND 3 CHAIN: A, B; COMPND 4 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: THERMOTOGA MARITIMA; SOURCE 3 ORGANISM_TAXID: 2336; SOURCE 4 GENE: TM0872; SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3); SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008; SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3) KEYWDS SAM-DEPENDENT METHYLTRANSFERASE FOLD, PROTEIN-COFACTOR KEYWDS 2 PRODUCT COMPLEX, STRUCTURAL GENOMICS, PSI, PROTEIN KEYWDS 3 STRUCTURE INITIATIVE, MIDWEST CENTER FOR STRUCTURAL KEYWDS 4 GENOMICS, MCSG EXPDTA X-RAY DIFFRACTION AUTHOR D.J.MILLER,W.F.ANDERSON,MIDWEST CENTER FOR STRUCTURAL AUTHOR 2 GENOMICS (MCSG) REVDAT 4 24-FEB-09 1M6Y 1 VERSN REVDAT 3 18-JAN-05 1M6Y 1 AUTHOR KEYWDS REMARK REVDAT 2 11-NOV-03 1M6Y 1 JRNL REVDAT 1 28-JAN-03 1M6Y 0 JRNL AUTH D.J.MILLER,N.OUELLETTE,E.EVDOKIMOVA,A.SAVCHENKO, JRNL AUTH 2 A.EDWARDS,W.F.ANDERSON JRNL TITL CRYSTAL COMPLEXES OF A PREDICTED JRNL TITL 2 S-ADENOSYLMETHIONINE-DEPENDENT METHYLTRANSFERASE JRNL TITL 3 REVEAL A TYPICAL ADOMET BINDING DOMAIN AND A JRNL TITL 4 SUBSTRATE RECOGNITION DOMAIN JRNL REF PROTEIN SCI. V. 12 1432 2003 JRNL REFN ISSN 0961-8368 JRNL PMID 12824489 JRNL DOI 10.1110/PS.0302403 REMARK 1 REMARK 2 REMARK 2 RESOLUTION. 1.90 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : CNS 1.0 REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE- REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU, REMARK 3 : READ,RICE,SIMONSON,WARREN REMARK 3 REMARK 3 REFINEMENT TARGET : ENGH & HUBER REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.89 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000 REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 3472061.430 REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 97.3 REMARK 3 NUMBER OF REFLECTIONS : 60592 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM REMARK 3 R VALUE (WORKING SET) : 0.197 REMARK 3 FREE R VALUE : 0.212 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000 REMARK 3 FREE R VALUE TEST SET COUNT : 3057 REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.004 REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : 10 REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.90 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.97 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 89.00 REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 5198 REMARK 3 BIN R VALUE (WORKING SET) : 0.2010 REMARK 3 BIN FREE R VALUE : 0.2230 REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.90 REMARK 3 BIN FREE R VALUE TEST SET COUNT : 267 REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.014 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 4635 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 62 REMARK 3 SOLVENT ATOMS : 367 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 18.30 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 37.20 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 0.00000 REMARK 3 B22 (A**2) : 0.00000 REMARK 3 B33 (A**2) : 0.00000 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : 0.00000 REMARK 3 B23 (A**2) : 0.00000 REMARK 3 REMARK 3 ESTIMATED COORDINATE ERROR. REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.20 REMARK 3 ESD FROM SIGMAA (A) : -0.06 REMARK 3 LOW RESOLUTION CUTOFF (A) : 6.00 REMARK 3 REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR. REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.21 REMARK 3 ESD FROM C-V SIGMAA (A) : NULL REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. REMARK 3 BOND LENGTHS (A) : 0.008 REMARK 3 BOND ANGLES (DEGREES) : 1.30 REMARK 3 DIHEDRAL ANGLES (DEGREES) : 22.30 REMARK 3 IMPROPER ANGLES (DEGREES) : 0.88 REMARK 3 REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED REMARK 3 REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA REMARK 3 MAIN-CHAIN BOND (A**2) : 1.470 ; 1.500 REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.100 ; 2.000 REMARK 3 SIDE-CHAIN BOND (A**2) : 2.790 ; 2.000 REMARK 3 SIDE-CHAIN ANGLE (A**2) : 4.150 ; 2.500 REMARK 3 REMARK 3 BULK SOLVENT MODELING. REMARK 3 METHOD USED : FLAT MODEL REMARK 3 KSOL : 0.38 REMARK 3 BSOL : 46.60 REMARK 3 REMARK 3 NCS MODEL : NULL REMARK 3 REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL REMARK 3 REMARK 3 PARAMETER FILE 1 : PROTEIN_REP.PARAM REMARK 3 PARAMETER FILE 2 : DNA-RNA-MULTI-ENDO_REP.PARAM REMARK 3 PARAMETER FILE 3 : ION.PARAM REMARK 3 PARAMETER FILE 4 : WATER_REP.PARAM REMARK 3 PARAMETER FILE 5 : NULL REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP REMARK 3 TOPOLOGY FILE 2 : DNA-RNA.TOP REMARK 3 TOPOLOGY FILE 3 : ION.TOP REMARK 3 TOPOLOGY FILE 4 : WATER.TOP REMARK 3 TOPOLOGY FILE 5 : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1M6Y COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 19-JUL-02. REMARK 100 THE RCSB ID CODE IS RCSB016672. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 03-APR-02 REMARK 200 TEMPERATURE (KELVIN) : 170 REMARK 200 PH : 6.5 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : APS REMARK 200 BEAMLINE : 5ID-B REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.9787, 0.9785, 0.9537 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO REMARK 200 DATA SCALING SOFTWARE : SCALEPACK REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 62185 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900 REMARK 200 RESOLUTION RANGE LOW (A) : 19.890 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9 REMARK 200 DATA REDUNDANCY : 13.700 REMARK 200 R MERGE (I) : 0.07200 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 22.0000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.97 REMARK 200 COMPLETENESS FOR SHELL (%) : 99.7 REMARK 200 DATA REDUNDANCY IN SHELL : 3.40 REMARK 200 R MERGE FOR SHELL (I) : 0.34100 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 4.700 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: MAD REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD REMARK 200 SOFTWARE USED: SOLVE V. 2.02 REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 55.98 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.79 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: DROP: 50MM NA CACODYLATE PH 6.5, REMARK 280 5MM HEPES PH 7.5, 0.1M AMMONIUM SULFATE, 9% PEG 8000, 0.25M REMARK 280 NACL, 1MM BME, 0.3MM S-ADENOSYL-L-HOMOCYSTEINE, 10MG/ML REMARK 280 PROTEIN. WELL: 0.1M NA CACODYLATE PH 6.5, 0.1M AMMONIUM REMARK 280 SULFATE, 18 % PEG 8000, VAPOR DIFFUSION, HANGING DROP, REMARK 280 TEMPERATURE 277K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 3 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X+1/2,-Y,Z+1/2 REMARK 290 3555 -X,Y+1/2,-Z+1/2 REMARK 290 4555 X+1/2,-Y+1/2,-Z REMARK 290 5555 Z,X,Y REMARK 290 6555 Z+1/2,-X+1/2,-Y REMARK 290 7555 -Z+1/2,-X,Y+1/2 REMARK 290 8555 -Z,X+1/2,-Y+1/2 REMARK 290 9555 Y,Z,X REMARK 290 10555 -Y,Z+1/2,-X+1/2 REMARK 290 11555 Y+1/2,-Z+1/2,-X REMARK 290 12555 -Y+1/2,-Z,X+1/2 REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 66.70000 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 66.70000 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 66.70000 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 66.70000 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 66.70000 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 66.70000 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 5 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY2 5 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY3 5 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY1 6 0.000000 0.000000 1.000000 66.70000 REMARK 290 SMTRY2 6 -1.000000 0.000000 0.000000 66.70000 REMARK 290 SMTRY3 6 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY1 7 0.000000 0.000000 -1.000000 66.70000 REMARK 290 SMTRY2 7 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY3 7 0.000000 1.000000 0.000000 66.70000 REMARK 290 SMTRY1 8 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY2 8 1.000000 0.000000 0.000000 66.70000 REMARK 290 SMTRY3 8 0.000000 -1.000000 0.000000 66.70000 REMARK 290 SMTRY1 9 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY2 9 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY3 9 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY1 10 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY2 10 0.000000 0.000000 1.000000 66.70000 REMARK 290 SMTRY3 10 -1.000000 0.000000 0.000000 66.70000 REMARK 290 SMTRY1 11 0.000000 1.000000 0.000000 66.70000 REMARK 290 SMTRY2 11 0.000000 0.000000 -1.000000 66.70000 REMARK 290 SMTRY3 11 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY1 12 0.000000 -1.000000 0.000000 66.70000 REMARK 290 SMTRY2 12 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY3 12 1.000000 0.000000 0.000000 66.70000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE REMARK 300 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT REMARK 300 WHICH CONSISTS OF 2 CHAINS. THE BIOLOGICAL UNIT IS A REMARK 300 TRIMER ACCORDING TO DYNAMIC LIGHT SCATTERING DATA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 GLY A -1 REMARK 465 HIS A 0 REMARK 465 MSE A 1 REMARK 465 GLU A 295 REMARK 465 GLU A 296 REMARK 465 GLY A 297 REMARK 465 GLY A 298 REMARK 465 ASP A 299 REMARK 465 GLY B -1 REMARK 465 HIS B 0 REMARK 465 MSE B 1 REMARK 465 ARG B 2 REMARK 465 LYS B 3 REMARK 465 TYR B 4 REMARK 465 SER B 5 REMARK 465 GLN B 6 REMARK 465 ARG B 7 REMARK 465 GLU B 274 REMARK 465 GLU B 275 REMARK 465 GLU B 276 REMARK 465 ILE B 277 REMARK 465 ARG B 278 REMARK 465 GLU B 279 REMARK 465 ASN B 280 REMARK 465 ARG B 293 REMARK 465 ILE B 294 REMARK 465 GLU B 295 REMARK 465 GLU B 296 REMARK 465 GLY B 297 REMARK 465 GLY B 298 REMARK 465 ASP B 299 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 ARG A 2 CG CD NE CZ NH1 NH2 REMARK 470 ARG B 14 CG CD NE CZ NH1 NH2 REMARK 470 GLU B 15 CG CD OE1 OE2 REMARK 470 GLU B 23 CG CD OE1 OE2 REMARK 470 ASP B 24 CG OD1 OD2 REMARK 470 GLU B 25 CG CD OE1 OE2 REMARK 470 LYS B 26 CG CD CE NZ REMARK 470 GLU B 35 CG CD OE1 OE2 REMARK 470 LYS B 69 CG CD CE NZ REMARK 470 ARG B 238 CG CD NE CZ NH1 NH2 REMARK 470 PRO B 272 CG CD REMARK 470 ARG B 282 CG CD NE CZ NH1 NH2 REMARK 470 ARG B 284 CG CD NE CZ NH1 NH2 REMARK 470 ARG B 287 CG CD NE CZ NH1 NH2 REMARK 470 GLU B 292 CG CD OE1 OE2 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 ASP A 24 -121.74 52.39 REMARK 500 LEU A 104 31.32 -85.80 REMARK 500 PHE B 19 -34.86 -131.50 REMARK 500 GLU B 23 -162.12 44.10 REMARK 500 GLU B 25 81.97 44.25 REMARK 500 GLU B 44 45.51 -83.86 REMARK 500 HIS B 45 -18.31 -161.35 REMARK 500 SER B 72 -73.82 -42.07 REMARK 500 ASP B 73 9.27 -54.37 REMARK 500 TYR B 82 5.07 -68.51 REMARK 500 ASP B 231 25.54 -79.84 REMARK 500 THR B 266 114.88 179.61 REMARK 500 PRO B 272 -137.73 -113.71 REMARK 500 ARG B 282 -77.23 -55.18 REMARK 500 ARG B 284 -75.67 -112.94 REMARK 500 SER B 285 41.04 -84.00 REMARK 500 REMARK 500 REMARK: NULL REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 500 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 501 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SAH A 401 REMARK 800 SITE_IDENTIFIER: AC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SAH B 402 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: APC038 RELATED DB: TARGETDB DBREF 1M6Y A 1 299 UNP Q9WZX6 MRAW_THEMA 1 299 DBREF 1M6Y B 1 299 UNP Q9WZX6 MRAW_THEMA 1 299 SEQADV 1M6Y GLY A -1 UNP Q9WZX6 CLONING ARTIFACT SEQADV 1M6Y HIS A 0 UNP Q9WZX6 CLONING ARTIFACT SEQADV 1M6Y MSE A 1 UNP Q9WZX6 MET 1 MODIFIED RESIDUE SEQADV 1M6Y MSE A 12 UNP Q9WZX6 MET 12 MODIFIED RESIDUE SEQADV 1M6Y MSE A 102 UNP Q9WZX6 MET 102 MODIFIED RESIDUE SEQADV 1M6Y MSE A 128 UNP Q9WZX6 MET 128 MODIFIED RESIDUE SEQADV 1M6Y MSE A 130 UNP Q9WZX6 MET 130 MODIFIED RESIDUE SEQADV 1M6Y GLY B -1 UNP Q9WZX6 CLONING ARTIFACT SEQADV 1M6Y HIS B 0 UNP Q9WZX6 CLONING ARTIFACT SEQADV 1M6Y MSE B 1 UNP Q9WZX6 MET 1 MODIFIED RESIDUE SEQADV 1M6Y MSE B 12 UNP Q9WZX6 MET 12 MODIFIED RESIDUE SEQADV 1M6Y MSE B 102 UNP Q9WZX6 MET 102 MODIFIED RESIDUE SEQADV 1M6Y MSE B 128 UNP Q9WZX6 MET 128 MODIFIED RESIDUE SEQADV 1M6Y MSE B 130 UNP Q9WZX6 MET 130 MODIFIED RESIDUE SEQRES 1 A 301 GLY HIS MSE ARG LYS TYR SER GLN ARG HIS ILE PRO VAL SEQRES 2 A 301 MSE VAL ARG GLU VAL ILE GLU PHE LEU LYS PRO GLU ASP SEQRES 3 A 301 GLU LYS ILE ILE LEU ASP CYS THR VAL GLY GLU GLY GLY SEQRES 4 A 301 HIS SER ARG ALA ILE LEU GLU HIS CYS PRO GLY CYS ARG SEQRES 5 A 301 ILE ILE GLY ILE ASP VAL ASP SER GLU VAL LEU ARG ILE SEQRES 6 A 301 ALA GLU GLU LYS LEU LYS GLU PHE SER ASP ARG VAL SER SEQRES 7 A 301 LEU PHE LYS VAL SER TYR ARG GLU ALA ASP PHE LEU LEU SEQRES 8 A 301 LYS THR LEU GLY ILE GLU LYS VAL ASP GLY ILE LEU MSE SEQRES 9 A 301 ASP LEU GLY VAL SER THR TYR GLN LEU LYS GLY GLU ASN SEQRES 10 A 301 ARG GLY PHE THR PHE GLU ARG GLU GLU PRO LEU ASP MSE SEQRES 11 A 301 ARG MSE ASP LEU GLU SER GLU VAL THR ALA GLN LYS VAL SEQRES 12 A 301 LEU ASN GLU LEU PRO GLU GLU GLU LEU ALA ARG ILE ILE SEQRES 13 A 301 PHE GLU TYR GLY GLU GLU LYS ARG PHE ALA ARG ARG ILE SEQRES 14 A 301 ALA ARG LYS ILE VAL GLU ASN ARG PRO LEU ASN THR THR SEQRES 15 A 301 LEU ASP LEU VAL LYS ALA VAL ARG GLU ALA LEU PRO SER SEQRES 16 A 301 TYR GLU ILE ARG ARG ARG LYS ARG HIS PHE ALA THR LYS SEQRES 17 A 301 THR PHE GLN ALA ILE ARG ILE TYR VAL ASN ARG GLU LEU SEQRES 18 A 301 GLU ASN LEU LYS GLU PHE LEU LYS LYS ALA GLU ASP LEU SEQRES 19 A 301 LEU ASN PRO GLY GLY ARG ILE VAL VAL ILE SER PHE HIS SEQRES 20 A 301 SER LEU GLU ASP ARG ILE VAL LYS GLU THR PHE ARG ASN SEQRES 21 A 301 SER LYS LYS LEU ARG ILE LEU THR GLU LYS PRO VAL ARG SEQRES 22 A 301 PRO SER GLU GLU GLU ILE ARG GLU ASN PRO ARG ALA ARG SEQRES 23 A 301 SER GLY ARG LEU ARG ALA ALA GLU ARG ILE GLU GLU GLY SEQRES 24 A 301 GLY ASP SEQRES 1 B 301 GLY HIS MSE ARG LYS TYR SER GLN ARG HIS ILE PRO VAL SEQRES 2 B 301 MSE VAL ARG GLU VAL ILE GLU PHE LEU LYS PRO GLU ASP SEQRES 3 B 301 GLU LYS ILE ILE LEU ASP CYS THR VAL GLY GLU GLY GLY SEQRES 4 B 301 HIS SER ARG ALA ILE LEU GLU HIS CYS PRO GLY CYS ARG SEQRES 5 B 301 ILE ILE GLY ILE ASP VAL ASP SER GLU VAL LEU ARG ILE SEQRES 6 B 301 ALA GLU GLU LYS LEU LYS GLU PHE SER ASP ARG VAL SER SEQRES 7 B 301 LEU PHE LYS VAL SER TYR ARG GLU ALA ASP PHE LEU LEU SEQRES 8 B 301 LYS THR LEU GLY ILE GLU LYS VAL ASP GLY ILE LEU MSE SEQRES 9 B 301 ASP LEU GLY VAL SER THR TYR GLN LEU LYS GLY GLU ASN SEQRES 10 B 301 ARG GLY PHE THR PHE GLU ARG GLU GLU PRO LEU ASP MSE SEQRES 11 B 301 ARG MSE ASP LEU GLU SER GLU VAL THR ALA GLN LYS VAL SEQRES 12 B 301 LEU ASN GLU LEU PRO GLU GLU GLU LEU ALA ARG ILE ILE SEQRES 13 B 301 PHE GLU TYR GLY GLU GLU LYS ARG PHE ALA ARG ARG ILE SEQRES 14 B 301 ALA ARG LYS ILE VAL GLU ASN ARG PRO LEU ASN THR THR SEQRES 15 B 301 LEU ASP LEU VAL LYS ALA VAL ARG GLU ALA LEU PRO SER SEQRES 16 B 301 TYR GLU ILE ARG ARG ARG LYS ARG HIS PHE ALA THR LYS SEQRES 17 B 301 THR PHE GLN ALA ILE ARG ILE TYR VAL ASN ARG GLU LEU SEQRES 18 B 301 GLU ASN LEU LYS GLU PHE LEU LYS LYS ALA GLU ASP LEU SEQRES 19 B 301 LEU ASN PRO GLY GLY ARG ILE VAL VAL ILE SER PHE HIS SEQRES 20 B 301 SER LEU GLU ASP ARG ILE VAL LYS GLU THR PHE ARG ASN SEQRES 21 B 301 SER LYS LYS LEU ARG ILE LEU THR GLU LYS PRO VAL ARG SEQRES 22 B 301 PRO SER GLU GLU GLU ILE ARG GLU ASN PRO ARG ALA ARG SEQRES 23 B 301 SER GLY ARG LEU ARG ALA ALA GLU ARG ILE GLU GLU GLY SEQRES 24 B 301 GLY ASP MODRES 1M6Y MSE A 12 MET SELENOMETHIONINE MODRES 1M6Y MSE A 102 MET SELENOMETHIONINE MODRES 1M6Y MSE A 128 MET SELENOMETHIONINE MODRES 1M6Y MSE A 130 MET SELENOMETHIONINE MODRES 1M6Y MSE B 12 MET SELENOMETHIONINE MODRES 1M6Y MSE B 102 MET SELENOMETHIONINE MODRES 1M6Y MSE B 128 MET SELENOMETHIONINE MODRES 1M6Y MSE B 130 MET SELENOMETHIONINE HET MSE A 12 8 HET MSE A 102 8 HET MSE A 128 8 HET MSE A 130 8 HET MSE B 12 8 HET MSE B 102 8 HET MSE B 128 8 HET MSE B 130 8 HET SO4 A 500 5 HET SO4 B 501 5 HET SAH A 401 26 HET SAH B 402 26 HETNAM MSE SELENOMETHIONINE HETNAM SO4 SULFATE ION HETNAM SAH S-ADENOSYL-L-HOMOCYSTEINE FORMUL 1 MSE 8(C5 H11 N O2 SE) FORMUL 3 SO4 2(O4 S 2-) FORMUL 5 SAH 2(C14 H20 N6 O5 S) FORMUL 7 HOH *367(H2 O) HELIX 103 103 SER A 107 GLY A 113 1 7 HELIX 104 104 THR A 137 TYR A 157 1 21 HELIX 105 105 PHE A 163 ASN A 174 1 12 HELIX 106 106 THR A 179 ARG A 199 1 21 SHEET 111 111 1 VAL A 97 ASP A 103 0 SSBOND 1 CYS A 46 CYS A 49 1555 1555 2.07 SSBOND 2 CYS B 46 CYS B 49 1555 1555 2.03 LINK C VAL A 11 N MSE A 12 1555 1555 1.34 LINK C MSE A 12 N AVAL A 13 1555 1555 1.33 LINK C MSE A 12 N BVAL A 13 1555 1555 1.33 LINK C LEU A 101 N MSE A 102 1555 1555 1.34 LINK C MSE A 102 N ASP A 103 1555 1555 1.33 LINK C ASP A 127 N MSE A 128 1555 1555 1.33 LINK C MSE A 128 N ARG A 129 1555 1555 1.33 LINK C ARG A 129 N MSE A 130 1555 1555 1.33 LINK C MSE A 130 N ASP A 131 1555 1555 1.33 LINK C VAL B 11 N MSE B 12 1555 1555 1.33 LINK C MSE B 12 N VAL B 13 1555 1555 1.33 LINK C LEU B 101 N MSE B 102 1555 1555 1.33 LINK C MSE B 102 N ASP B 103 1555 1555 1.33 LINK C ASP B 127 N MSE B 128 1555 1555 1.33 LINK C MSE B 128 N ARG B 129 1555 1555 1.33 LINK C ARG B 129 N MSE B 130 1555 1555 1.33 LINK C MSE B 130 N ASP B 131 1555 1555 1.33 CISPEP 1 ARG A 175 PRO A 176 0 -0.36 CISPEP 2 ARG B 175 PRO B 176 0 0.16 SITE 1 AC1 5 ARG A 199 LYS A 200 ARG A 201 HOH A 556 SITE 2 AC1 5 HOH A 600 SITE 1 AC2 4 ARG B 199 LYS B 200 ARG B 201 HOH B 507 SITE 1 AC3 21 HIS A 8 CYS A 31 THR A 32 VAL A 33 SITE 2 AC3 21 GLY A 34 GLU A 35 GLY A 36 GLY A 37 SITE 3 AC3 21 HIS A 38 ASP A 55 VAL A 56 SER A 81 SITE 4 AC3 21 TYR A 82 ASP A 103 GLY A 105 GLN A 110 SITE 5 AC3 21 MSE A 130 ASN A 221 HOH A 508 HOH A 524 SITE 6 AC3 21 HOH A 563 SITE 1 AC4 20 HIS B 8 CYS B 31 THR B 32 VAL B 33 SITE 2 AC4 20 GLY B 34 GLU B 35 GLY B 36 GLY B 37 SITE 3 AC4 20 HIS B 38 ASP B 55 VAL B 56 VAL B 60 SITE 4 AC4 20 VAL B 80 SER B 81 TYR B 82 ASP B 103 SITE 5 AC4 20 GLY B 105 SER B 107 GLN B 110 MSE B 130 CRYST1 133.400 133.400 133.400 90.00 90.00 90.00 P 21 3 24 ORIGX1 1.000000 0.000000 0.000000 0.00000 ORIGX2 0.000000 1.000000 0.000000 0.00000 ORIGX3 0.000000 0.000000 1.000000 0.00000 SCALE1 0.007496 0.000000 0.000000 0.00000 SCALE2 0.000000 0.007496 0.000000 0.00000 SCALE3 0.000000 0.000000 0.007496 0.00000 ATOM 1 N LYS A 96 85.565 213.810 849.564 1.00 23.97 N ATOM 2 CA LYS A 96 86.120 214.971 848.885 1.00 22.93 C ATOM 3 C LYS A 96 86.358 216.094 849.868 1.00 18.23 C ATOM 4 O LYS A 96 85.768 216.116 850.947 1.00 18.25 O ATOM 5 CB LYS A 96 85.171 215.450 847.783 1.00 27.55 C ATOM 6 CG LYS A 96 85.160 214.523 846.561 1.00 30.63 C ATOM 7 CD LYS A 96 84.200 215.008 845.502 1.00 34.01 C ATOM 8 CE LYS A 96 84.284 214.140 844.259 1.00 36.09 C ATOM 9 NZ LYS A 96 84.270 212.701 844.634 1.00 39.30 N ATOM 10 N VAL A 97 87.216 217.029 849.491 1.00 15.27 N ATOM 11 CA VAL A 97 87.503 218.161 850.364 1.00 15.56 C ATOM 12 C VAL A 97 87.277 219.461 849.598 1.00 15.94 C ATOM 13 O VAL A 97 87.123 219.451 848.374 1.00 16.00 O ATOM 14 CB VAL A 97 88.954 218.108 850.905 1.00 15.19 C ATOM 15 CG1 VAL A 97 89.141 216.837 851.742 1.00 13.88 C ATOM 16 CG2 VAL A 97 89.967 218.137 849.751 1.00 15.63 C ATOM 17 N ASP A 98 87.265 220.575 850.320 1.00 13.75 N ATOM 18 CA ASP A 98 87.030 221.878 849.708 1.00 14.92 C ATOM 19 C ASP A 98 88.307 222.631 849.391 1.00 18.01 C ATOM 20 O ASP A 98 88.294 223.639 848.668 1.00 16.97 O ATOM 21 CB ASP A 98 86.147 222.699 850.643 1.00 13.75 C ATOM 22 CG ASP A 98 84.844 221.994 850.939 1.00 18.84 C ATOM 23 OD1 ASP A 98 84.069 221.783 849.977 1.00 17.87 O ATOM 24 OD2 ASP A 98 84.607 221.620 852.107 1.00 18.22 O ATOM 25 N GLY A 99 89.421 222.147 849.929 1.00 15.64 N ATOM 26 CA GLY A 99 90.673 222.823 849.676 1.00 13.86 C ATOM 27 C GLY A 99 91.833 221.866 849.821 1.00 15.42 C ATOM 28 O GLY A 99 91.777 220.940 850.634 1.00 14.33 O ATOM 29 N ILE A 100 92.858 222.072 848.999 1.00 13.65 N ATOM 30 CA ILE A 100 94.068 221.261 849.037 1.00 14.24 C ATOM 31 C ILE A 100 95.242 222.230 849.021 1.00 13.56 C ATOM 32 O ILE A 100 95.322 223.095 848.161 1.00 16.61 O ATOM 33 CB ILE A 100 94.162 220.323 847.803 1.00 15.08 C ATOM 34 CG1 ILE A 100 93.010 219.323 847.846 1.00 15.77 C ATOM 35 CD1 ILE A 100 92.925 218.442 846.591 1.00 20.83 C ATOM 36 CG2 ILE A 100 95.519 219.602 847.782 1.00 17.82 C ATOM 37 N LEU A 101 96.136 222.098 849.995 1.00 12.95 N ATOM 38 CA LEU A 101 97.296 222.967 850.080 1.00 12.50 C ATOM 39 C LEU A 101 98.581 222.153 850.040 1.00 15.99 C ATOM 40 O LEU A 101 98.678 221.131 850.718 1.00 14.23 O ATOM 41 CB LEU A 101 97.265 223.761 851.396 1.00 14.06 C ATOM 42 CG LEU A 101 98.512 224.593 851.715 1.00 17.50 C ATOM 43 CD1 LEU A 101 98.654 225.727 850.678 1.00 15.93 C ATOM 44 CD2 LEU A 101 98.401 225.170 853.148 1.00 16.61 C ATOM 45 N MSE A 102 99.553 222.591 849.233 1.00 12.72 N ATOM 46 CA MSE A 102 100.854 221.919 849.182 1.00 15.45 C ATOM 47 C MSE A 102 101.942 222.991 849.265 1.00 14.91 C ATOM 48 O MSE A 102 101.875 223.990 848.561 1.00 15.44 O ATOM 49 CB MSE A 102 101.047 221.141 847.870 1.00 13.91 C ATOM 50 CG MSE A 102 99.887 220.244 847.471 1.00 15.94 C ATOM 51 SE MSE A 102 100.412 219.273 845.829 1.00 27.56 Se ATOM 52 CE MSE A 102 101.480 217.886 846.658 1.00 17.32 C ATOM 53 N ASP A 103 102.931 222.770 850.133 1.00 12.95 N ATOM 54 CA ASP A 103 104.072 223.676 850.322 1.00 16.63 C ATOM 55 C ASP A 103 105.254 222.715 850.131 1.00 18.84 C ATOM 56 O ASP A 103 105.588 221.941 851.024 1.00 19.94 O ATOM 57 CB ASP A 103 103.988 224.258 851.746 1.00 19.66 C ATOM 58 CG ASP A 103 105.236 225.033 852.169 1.00 24.26 C ATOM 59 OD1 ASP A 103 106.225 225.094 851.413 1.00 24.17 O ATOM 60 OD2 ASP A 103 105.215 225.578 853.297 1.00 22.26 O ATOM 61 N LEU A 104 105.885 222.757 848.958 1.00 18.85 N ATOM 62 CA LEU A 104 106.941 221.807 848.625 1.00 20.71 C ATOM 63 C LEU A 104 108.385 222.092 849.051 1.00 22.07 C ATOM 64 O LEU A 104 109.327 221.664 848.387 1.00 23.44 O ATOM 65 CB LEU A 104 106.898 221.536 847.113 1.00 19.77 C ATOM 66 CG LEU A 104 105.489 221.242 846.556 1.00 22.61 C ATOM 67 CD1 LEU A 104 105.503 221.322 845.033 1.00 21.74 C ATOM 68 CD2 LEU A 104 105.003 219.876 847.034 1.00 21.95 C ATOM 69 N GLY A 105 108.566 222.770 850.172 1.00 23.54 N ATOM 70 CA GLY A 105 109.913 223.073 850.625 1.00 23.91 C ATOM 71 C GLY A 105 110.450 222.152 851.712 1.00 22.00 C ATOM 72 O GLY A 105 110.211 220.938 851.712 1.00 18.88 O ATOM 73 N VAL A 106 111.196 222.754 852.635 1.00 21.15 N ATOM 74 CA VAL A 106 111.796 222.047 853.760 1.00 20.13 C ATOM 75 C VAL A 106 111.429 222.868 854.978 1.00 19.30 C ATOM 76 O VAL A 106 111.456 224.096 854.930 1.00 20.99 O ATOM 77 CB VAL A 106 113.338 221.983 853.604 1.00 22.27 C ATOM 78 CG1 VAL A 106 113.951 221.131 854.715 1.00 23.57 C ATOM 79 CG2 VAL A 106 113.695 221.407 852.251 1.00 23.97 C ATOM 80 N SER A 107 111.078 222.212 856.074 1.00 17.52 N ATOM 81 CA SER A 107 110.679 222.962 857.263 1.00 19.86 C ATOM 82 C SER A 107 111.900 223.479 858.026 1.00 22.63 C ATOM 83 O SER A 107 113.021 222.966 857.874 1.00 23.24 O ATOM 84 CB SER A 107 109.814 222.090 858.180 1.00 22.12 C ATOM 85 OG SER A 107 110.599 221.532 859.225 1.00 25.76 O ATOM 86 N THR A 108 111.676 224.512 858.828 1.00 21.63 N ATOM 87 CA THR A 108 112.726 225.128 859.627 1.00 22.94 C ATOM 88 C THR A 108 113.411 224.113 860.502 1.00 22.42 C ATOM 89 O THR A 108 114.654 224.058 860.563 1.00 22.33 O ATOM 90 CB THR A 108 112.137 226.243 860.534 1.00 25.31 C ATOM 91 OG1 THR A 108 111.665 227.313 859.708 1.00 26.45 O ATOM 92 CG2 THR A 108 113.187 226.760 861.532 1.00 24.61 C ATOM 93 N TYR A 109 112.606 223.314 861.192 1.00 21.28 N ATOM 94 CA TYR A 109 113.158 222.305 862.073 1.00 22.51 C ATOM 95 C TYR A 109 113.961 221.286 861.266 1.00 20.30 C ATOM 96 O TYR A 109 114.962 220.782 861.744 1.00 19.08 O ATOM 97 CB TYR A 109 112.057 221.592 862.860 1.00 22.14 C ATOM 98 CG TYR A 109 112.619 220.689 863.928 1.00 22.21 C ATOM 99 CD1 TYR A 109 113.333 221.216 865.004 1.00 24.67 C ATOM 100 CE1 TYR A 109 113.911 220.376 865.969 1.00 26.79 C ATOM 101 CZ TYR A 109 113.768 219.000 865.850 1.00 26.62 C ATOM 102 OH TYR A 109 114.362 218.159 866.769 1.00 28.75 O ATOM 103 CE2 TYR A 109 113.056 218.460 864.796 1.00 26.12 C ATOM 104 CD2 TYR A 109 112.486 219.307 863.838 1.00 22.29 C ATOM 105 N GLN A 110 113.518 220.975 860.049 1.00 18.24 N ATOM 106 CA GLN A 110 114.270 220.019 859.247 1.00 17.33 C ATOM 107 C GLN A 110 115.649 220.587 858.913 1.00 16.16 C ATOM 108 O GLN A 110 116.654 219.887 859.001 1.00 15.91 O ATOM 109 CB GLN A 110 113.491 219.659 857.971 1.00 19.03 C ATOM 110 CG GLN A 110 112.183 218.920 858.302 1.00 16.86 C ATOM 111 CD GLN A 110 111.345 218.595 857.073 1.00 17.68 C ATOM 112 OE1 GLN A 110 111.195 219.426 856.177 1.00 17.62 O ATOM 113 NE2 GLN A 110 110.778 217.389 857.037 1.00 16.17 N ATOM 114 N LEU A 111 115.684 221.858 858.532 1.00 15.93 N ATOM 115 CA LEU A 111 116.945 222.526 858.191 1.00 20.13 C ATOM 116 C LEU A 111 117.887 222.738 859.383 1.00 22.89 C ATOM 117 O LEU A 111 119.096 222.474 859.300 1.00 20.41 O ATOM 118 CB LEU A 111 116.645 223.892 857.575 1.00 20.00 C ATOM 119 CG LEU A 111 115.895 223.892 856.246 1.00 23.19 C ATOM 120 CD1 LEU A 111 115.304 225.271 855.986 1.00 26.68 C ATOM 121 CD2 LEU A 111 116.855 223.481 855.119 1.00 24.12 C ATOM 122 N LYS A 112 117.332 223.195 860.501 1.00 23.27 N ATOM 123 CA LYS A 112 118.155 223.515 861.666 1.00 27.12 C ATOM 124 C LYS A 112 118.195 222.615 862.889 1.00 28.24 C ATOM 125 O LYS A 112 119.149 222.700 863.666 1.00 29.59 O ATOM 126 CB LYS A 112 117.813 224.934 862.137 1.00 31.06 C ATOM 127 CG LYS A 112 118.127 226.009 861.114 1.00 36.78 C ATOM 128 CD LYS A 112 117.844 227.389 861.687 1.00 41.88 C ATOM 129 CE LYS A 112 118.488 228.481 860.851 1.00 45.57 C ATOM 130 NZ LYS A 112 119.971 228.521 860.974 1.00 47.40 N ATOM 131 N GLY A 113 117.202 221.757 863.091 1.00 26.40 N ATOM 132 CA GLY A 113 117.239 220.950 864.300 1.00 24.70 C ATOM 133 C GLY A 113 117.288 219.448 864.200 1.00 25.04 C ATOM 134 O GLY A 113 117.550 218.772 865.203 1.00 25.16 O ATOM 135 N GLU A 114 117.059 218.902 863.009 1.00 19.24 N ATOM 136 CA GLU A 114 117.059 217.462 862.870 1.00 20.37 C ATOM 137 C GLU A 114 118.419 216.801 862.715 1.00 18.92 C ATOM 138 O GLU A 114 118.522 215.586 862.848 1.00 19.05 O ATOM 139 CB GLU A 114 116.142 217.061 861.710 1.00 19.94 C ATOM 140 CG GLU A 114 114.668 217.337 862.029 1.00 20.00 C ATOM 141 CD GLU A 114 113.734 216.833 860.948 1.00 21.06 C ATOM 142 OE1 GLU A 114 114.214 216.598 859.821 1.00 14.48 O ATOM 143 OE2 GLU A 114 112.523 216.684 861.223 1.00 19.11 O ATOM 144 N ASN A 115 119.454 217.596 862.454 1.00 18.91 N ATOM 145 CA ASN A 115 120.813 217.062 862.259 1.00 19.52 C ATOM 146 C ASN A 115 120.814 215.997 861.143 1.00 17.34 C ATOM 147 O ASN A 115 121.456 214.944 861.256 1.00 16.54 O ATOM 148 CB ASN A 115 121.357 216.450 863.567 1.00 21.68 C ATOM 149 CG ASN A 115 122.866 216.202 863.513 1.00 22.55 C ATOM 150 OD1 ASN A 115 123.607 217.021 862.979 1.00 21.03 O ATOM 151 ND2 ASN A 115 123.320 215.073 864.067 1.00 23.12 N ATOM 152 N ARG A 116 120.092 216.276 860.064 1.00 14.83 N ATOM 153 CA ARG A 116 120.010 215.335 858.942 1.00 15.13 C ATOM 154 C ARG A 116 120.751 215.811 857.694 1.00 13.55 C ATOM 155 O ARG A 116 120.643 215.194 856.643 1.00 16.18 O ATOM 156 CB ARG A 116 118.544 215.050 858.584 1.00 15.58 C ATOM 157 CG ARG A 116 117.797 214.224 859.652 1.00 16.39 C ATOM 158 CD ARG A 116 116.363 213.906 859.227 1.00 19.54 C ATOM 159 NE ARG A 116 115.514 213.657 860.391 1.00 16.42 N ATOM 160 CZ ARG A 116 114.197 213.452 860.338 1.00 20.61 C ATOM 161 NH1 ARG A 116 113.559 213.433 859.169 1.00 15.54 N ATOM 162 NH2 ARG A 116 113.500 213.356 861.469 1.00 21.90 N ATOM 163 N GLY A 117 121.470 216.918 857.811 1.00 15.91 N ATOM 164 CA GLY A 117 122.245 217.429 856.688 1.00 17.12 C ATOM 165 C GLY A 117 121.487 217.973 855.483 1.00 18.29 C ATOM 166 O GLY A 117 121.981 217.882 854.351 1.00 17.26 O ATOM 167 N PHE A 118 120.293 218.522 855.710 1.00 15.49 N ATOM 168 CA PHE A 118 119.510 219.134 854.633 1.00 16.06 C ATOM 169 C PHE A 118 120.246 220.379 854.154 1.00 18.66 C ATOM 170 O PHE A 118 120.156 220.774 852.988 1.00 17.70 O ATOM 171 CB PHE A 118 118.102 219.524 855.134 1.00 14.97 C ATOM 172 CG PHE A 118 117.151 218.371 855.193 1.00 17.55 C ATOM 173 CD1 PHE A 118 116.723 217.754 854.021 1.00 16.19 C ATOM 174 CE1 PHE A 118 115.871 216.665 854.056 1.00 18.48 C ATOM 175 CZ PHE A 118 115.429 216.168 855.273 1.00 17.77 C ATOM 176 CE2 PHE A 118 115.851 216.774 856.458 1.00 15.38 C ATOM 177 CD2 PHE A 118 116.708 217.872 856.413 1.00 18.00 C ATOM 178 N THR A 119 120.964 221.035 855.057 1.00 19.92 N ATOM 179 CA THR A 119 121.704 222.205 854.614 1.00 23.94 C ATOM 180 C THR A 119 123.144 222.126 855.094 1.00 25.79 C ATOM 181 O THR A 119 123.537 221.154 855.739 1.00 26.53 O ATOM 182 CB THR A 119 121.025 223.533 855.049 1.00 28.46 C ATOM 183 OG1 THR A 119 121.642 224.632 854.350 1.00 29.57 O ATOM 184 CG2 THR A 119 121.138 223.734 856.548 1.00 29.74 C ATOM 185 N PHE A 120 123.935 223.133 854.762 1.00 28.47 N ATOM 186 CA PHE A 120 125.350 223.123 855.123 1.00 30.75 C ATOM 187 C PHE A 120 125.805 224.265 856.024 1.00 33.66 C ATOM 188 O PHE A 120 126.955 224.680 855.975 1.00 34.76 O ATOM 189 CB PHE A 120 126.222 223.126 853.839 1.00 28.38 C ATOM 190 CG PHE A 120 125.589 224.007 852.819 1.00 26.58 C ATOM 191 CD1 PHE A 120 125.821 225.377 852.867 1.00 29.50 C ATOM 192 CE1 PHE A 120 125.190 226.234 851.960 1.00 29.54 C ATOM 193 CZ PHE A 120 124.308 225.717 851.014 1.00 31.26 C ATOM 194 CE2 PHE A 120 124.079 224.356 850.955 1.00 26.35 C ATOM 195 CD2 PHE A 120 124.722 223.510 851.837 1.00 26.30 C ATOM 196 N GLU A 121 124.907 224.771 856.855 1.00 37.06 N ATOM 197 CA GLU A 121 125.286 225.835 857.774 1.00 38.09 C ATOM 198 C GLU A 121 126.261 225.202 858.769 1.00 37.05 C ATOM 199 O GLU A 121 127.144 225.873 859.306 1.00 36.51 O ATOM 200 CB GLU A 121 124.058 226.375 858.505 1.00 40.31 C ATOM 201 CG GLU A 121 123.069 227.092 857.598 1.00 47.10 C ATOM 202 CD GLU A 121 121.789 227.475 858.314 1.00 49.83 C ATOM 203 OE1 GLU A 121 120.948 228.161 857.693 1.00 53.72 O ATOM 204 OE2 GLU A 121 121.623 227.090 859.491 1.00 50.82 O ATOM 205 N ARG A 122 126.096 223.901 859.008 1.00 32.67 N ATOM 206 CA ARG A 122 126.968 223.183 859.926 1.00 30.91 C ATOM 207 C ARG A 122 127.291 221.770 859.461 1.00 27.19 C ATOM 208 O ARG A 122 126.680 221.250 858.525 1.00 24.04 O ATOM 209 CB ARG A 122 126.354 223.149 861.334 1.00 34.77 C ATOM 210 CG ARG A 122 124.940 222.615 861.422 1.00 37.52 C ATOM 211 CD ARG A 122 124.295 222.960 862.775 1.00 41.68 C ATOM 212 NE ARG A 122 124.924 222.275 863.910 1.00 44.96 N ATOM 213 CZ ARG A 122 124.662 221.023 864.284 1.00 45.13 C ATOM 214 NH1 ARG A 122 123.772 220.296 863.620 1.00 42.40 N ATOM 215 NH2 ARG A 122 125.295 220.493 865.326 1.00 45.93 N ATOM 216 N GLU A 123 128.270 221.160 860.118 1.00 22.54 N ATOM 217 CA GLU A 123 128.683 219.805 859.787 1.00 22.75 C ATOM 218 C GLU A 123 127.662 218.824 860.362 1.00 22.77 C ATOM 219 O GLU A 123 127.488 218.745 861.582 1.00 20.75 O ATOM 220 CB GLU A 123 130.071 219.524 860.377 1.00 24.86 C ATOM 221 CG GLU A 123 130.625 218.136 860.067 1.00 29.15 C ATOM 222 CD GLU A 123 131.994 217.913 860.702 1.00 34.34 C ATOM 223 OE1 GLU A 123 132.614 218.903 861.123 1.00 38.61 O ATOM 224 OE2 GLU A 123 132.453 216.755 860.776 1.00 36.39 O ATOM 225 N GLU A 124 126.993 218.075 859.488 1.00 18.89 N ATOM 226 CA GLU A 124 125.985 217.108 859.910 1.00 18.93 C ATOM 227 C GLU A 124 126.084 215.876 859.017 1.00 19.75 C ATOM 228 O GLU A 124 126.679 215.936 857.935 1.00 19.19 O ATOM 229 CB GLU A 124 124.576 217.719 859.763 1.00 17.06 C ATOM 230 CG GLU A 124 124.382 219.027 860.512 1.00 18.48 C ATOM 231 CD GLU A 124 122.947 219.550 860.471 1.00 23.03 C ATOM 232 OE1 GLU A 124 122.126 219.073 859.640 1.00 19.94 O ATOM 233 OE2 GLU A 124 122.651 220.463 861.273 1.00 20.07 O ATOM 234 N PRO A 125 125.525 214.739 859.463 1.00 19.21 N ATOM 235 CA PRO A 125 125.593 213.544 858.615 1.00 18.96 C ATOM 236 C PRO A 125 124.794 213.763 857.323 1.00 19.18 C ATOM 237 O PRO A 125 123.877 214.596 857.279 1.00 15.66 O ATOM 238 CB PRO A 125 124.993 212.431 859.493 1.00 22.55 C ATOM 239 CG PRO A 125 124.234 213.156 860.578 1.00 23.75 C ATOM 240 CD PRO A 125 124.977 214.438 860.804 1.00 20.80 C ATOM 241 N LEU A 126 125.173 213.041 856.267 1.00 15.77 N ATOM 242 CA LEU A 126 124.482 213.140 854.982 1.00 16.72 C ATOM 243 C LEU A 126 123.300 212.174 855.030 1.00 15.51 C ATOM 244 O LEU A 126 123.396 211.032 854.598 1.00 16.81 O ATOM 245 CB LEU A 126 125.441 212.764 853.844 1.00 16.78 C ATOM 246 CG LEU A 126 126.543 213.806 853.614 1.00 17.06 C ATOM 247 CD1 LEU A 126 127.648 213.212 852.721 1.00 17.74 C ATOM 248 CD2 LEU A 126 125.928 215.053 852.993 1.00 16.71 C ATOM 249 N ASP A 127 122.175 212.649 855.556 1.00 15.19 N ATOM 250 CA ASP A 127 120.987 211.809 855.712 1.00 13.69 C ATOM 251 C ASP A 127 119.911 212.282 854.746 1.00 12.64 C ATOM 252 O ASP A 127 119.578 211.599 853.781 1.00 12.88 O ATOM 253 CB ASP A 127 120.490 211.918 857.171 1.00 16.08 C ATOM 254 CG ASP A 127 119.435 210.900 857.498 1.00 19.57 C ATOM 255 OD1 ASP A 127 118.486 210.760 856.698 1.00 16.50 O ATOM 256 OD2 ASP A 127 119.550 210.237 858.561 1.00 21.84 O ATOM 257 N MSE A 128 119.372 213.459 855.031 1.00 12.63 N ATOM 258 CA MSE A 128 118.354 214.109 854.213 1.00 14.14 C ATOM 259 C MSE A 128 117.031 213.377 854.028 1.00 14.59 C ATOM 260 O MSE A 128 116.256 213.731 853.149 1.00 15.51 O ATOM 261 CB MSE A 128 118.936 214.457 852.826 1.00 17.29 C ATOM 262 CG MSE A 128 120.096 215.440 852.886 1.00 15.70 C ATOM 263 SE MSE A 128 120.548 216.047 851.060 1.00 23.25 Se ATOM 264 CE MSE A 128 122.463 216.328 851.344 1.00 16.76 C ATOM 265 N ARG A 129 116.769 212.356 854.834 1.00 14.59 N ATOM 266 CA ARG A 129 115.482 211.673 854.724 1.00 15.75 C ATOM 267 C ARG A 129 114.429 212.481 855.483 1.00 17.23 C ATOM 268 O ARG A 129 114.661 212.859 856.628 1.00 16.71 O ATOM 269 CB ARG A 129 115.545 210.290 855.363 1.00 17.58 C ATOM 270 CG ARG A 129 116.364 209.269 854.604 1.00 19.14 C ATOM 271 CD ARG A 129 116.490 208.002 855.435 1.00 19.36 C ATOM 272 NE ARG A 129 117.277 208.221 856.645 1.00 19.08 N ATOM 273 CZ ARG A 129 117.622 207.255 857.492 1.00 20.80 C ATOM 274 NH1 ARG A 129 117.238 206.004 857.258 1.00 23.42 N ATOM 275 NH2 ARG A 129 118.372 207.531 858.555 1.00 24.27 N ATOM 276 N MSE A 130 113.295 212.765 854.850 1.00 14.78 N ATOM 277 CA MSE A 130 112.222 213.465 855.563 1.00 16.70 C ATOM 278 C MSE A 130 111.489 212.389 856.374 1.00 17.41 C ATOM 279 O MSE A 130 111.002 212.646 857.475 1.00 17.56 O ATOM 280 CB MSE A 130 111.309 214.176 854.557 1.00 14.66 C ATOM 281 CG MSE A 130 112.023 215.406 853.997 1.00 16.66 C ATOM 282 SE MSE A 130 111.185 216.102 852.416 1.00 27.93 Se ATOM 283 CE MSE A 130 112.011 217.846 852.450 1.00 26.28 C ATOM 284 N ASP A 131 111.431 211.174 855.838 1.00 17.19 N ATOM 285 CA ASP A 131 110.837 210.057 856.578 1.00 17.43 C ATOM 286 C ASP A 131 111.992 209.159 857.038 1.00 20.13 C ATOM 287 O ASP A 131 112.585 208.435 856.228 1.00 17.59 O ATOM 288 CB ASP A 131 109.886 209.257 855.699 1.00 16.97 C ATOM 289 CG ASP A 131 109.236 208.090 856.450 1.00 21.35 C ATOM 290 OD1 ASP A 131 109.610 207.807 857.618 1.00 22.74 O ATOM 291 OD2 ASP A 131 108.355 207.459 855.861 1.00 24.79 O ATOM 292 N LEU A 132 112.319 209.197 858.331 1.00 20.67 N ATOM 293 CA LEU A 132 113.433 208.384 858.828 1.00 24.40 C ATOM 294 C LEU A 132 113.235 206.886 858.688 1.00 25.47 C ATOM 295 O LEU A 132 114.183 206.113 858.871 1.00 26.03 O ATOM 296 CB LEU A 132 113.768 208.717 860.291 1.00 26.18 C ATOM 297 CG LEU A 132 114.450 210.067 860.524 1.00 28.29 C ATOM 298 CD1 LEU A 132 114.767 210.242 862.011 1.00 30.72 C ATOM 299 CD2 LEU A 132 115.732 210.142 859.688 1.00 28.02 C ATOM 300 N GLU A 133 112.020 206.479 858.346 1.00 25.50 N ATOM 301 CA GLU A 133 111.720 205.067 858.158 1.00 28.43 C ATOM 302 C GLU A 133 112.175 204.569 856.785 1.00 30.32 C ATOM 303 O GLU A 133 112.253 203.366 856.561 1.00 30.34 O ATOM 304 CB GLU A 133 110.221 204.815 858.323 1.00 33.58 C ATOM 305 CG GLU A 133 109.679 205.094 859.728 1.00 37.53 C ATOM 306 CD GLU A 133 110.221 204.136 860.770 1.00 44.19 C ATOM 307 OE1 GLU A 133 111.342 204.356 861.287 1.00 45.49 O ATOM 308 OE2 GLU A 133 109.525 203.143 861.067 1.00 48.17 O ATOM 309 N SER A 134 112.466 205.476 855.855 1.00 27.46 N ATOM 310 CA SER A 134 112.923 205.032 854.538 1.00 27.67 C ATOM 311 C SER A 134 114.376 204.578 854.647 1.00 25.68 C ATOM 312 O SER A 134 115.113 205.013 855.534 1.00 23.90 O ATOM 313 CB SER A 134 112.772 206.142 853.482 1.00 29.29 C ATOM 314 OG SER A 134 113.421 207.328 853.882 1.00 35.22 O ATOM 315 N GLU A 135 114.788 203.697 853.747 1.00 25.63 N ATOM 316 CA GLU A 135 116.137 203.149 853.790 1.00 28.95 C ATOM 317 C GLU A 135 117.215 203.961 853.086 1.00 26.71 C ATOM 318 O GLU A 135 118.360 203.968 853.517 1.00 28.38 O ATOM 319 CB GLU A 135 116.136 201.731 853.213 1.00 35.67 C ATOM 320 CG GLU A 135 115.251 200.751 853.977 1.00 43.80 C ATOM 321 CD GLU A 135 115.565 200.728 855.462 1.00 48.84 C ATOM 322 OE1 GLU A 135 116.736 200.460 855.820 1.00 51.78 O ATOM 323 OE2 GLU A 135 114.641 200.978 856.269 1.00 52.12 O ATOM 324 N VAL A 136 116.847 204.657 852.022 1.00 21.48 N ATOM 325 CA VAL A 136 117.842 205.412 851.254 1.00 23.27 C ATOM 326 C VAL A 136 118.243 206.752 851.862 1.00 19.06 C ATOM 327 O VAL A 136 117.398 207.603 852.080 1.00 17.96 O ATOM 328 CB VAL A 136 117.342 205.670 849.827 1.00 25.55 C ATOM 329 CG1 VAL A 136 118.437 206.391 849.012 1.00 29.35 C ATOM 330 CG2 VAL A 136 116.949 204.344 849.163 1.00 29.11 C ATOM 331 N THR A 137 119.537 206.930 852.110 1.00 18.14 N ATOM 332 CA THR A 137 120.074 208.172 852.670 1.00 16.64 C ATOM 333 C THR A 137 120.907 208.897 851.620 1.00 17.18 C ATOM 334 O THR A 137 121.357 208.287 850.637 1.00 15.86 O ATOM 335 CB THR A 137 121.021 207.931 853.852 1.00 18.58 C ATOM 336 OG1 THR A 137 122.089 207.074 853.420 1.00 18.70 O ATOM 337 CG2 THR A 137 120.265 207.294 855.055 1.00 20.14 C ATOM 338 N ALA A 138 121.128 210.186 851.840 1.00 14.73 N ATOM 339 CA ALA A 138 121.947 210.954 850.906 1.00 15.51 C ATOM 340 C ALA A 138 123.343 210.322 850.877 1.00 16.39 C ATOM 341 O ALA A 138 123.960 210.243 849.820 1.00 14.13 O ATOM 342 CB ALA A 138 122.038 212.419 851.350 1.00 12.21 C ATOM 343 N GLN A 139 123.842 209.854 852.025 1.00 17.19 N ATOM 344 CA GLN A 139 125.184 209.250 852.041 1.00 17.81 C ATOM 345 C GLN A 139 125.282 208.056 851.097 1.00 17.72 C ATOM 346 O GLN A 139 126.224 207.954 850.296 1.00 16.81 O ATOM 347 CB GLN A 139 125.592 208.787 853.452 1.00 18.76 C ATOM 348 CG GLN A 139 127.088 208.392 853.526 1.00 21.24 C ATOM 349 CD GLN A 139 127.521 207.763 854.861 1.00 26.74 C ATOM 350 OE1 GLN A 139 128.656 207.957 855.305 1.00 27.92 O ATOM 351 NE2 GLN A 139 126.634 206.996 855.479 1.00 20.76 N ATOM 352 N LYS A 140 124.307 207.155 851.183 1.00 15.92 N ATOM 353 CA LYS A 140 124.295 205.969 850.348 1.00 18.59 C ATOM 354 C LYS A 140 124.229 206.349 848.869 1.00 18.02 C ATOM 355 O LYS A 140 124.924 205.760 848.032 1.00 15.83 O ATOM 356 CB LYS A 140 123.106 205.076 850.716 1.00 21.73 C ATOM 357 CG LYS A 140 123.014 203.783 849.908 1.00 33.63 C ATOM 358 CD LYS A 140 121.721 203.033 850.220 1.00 39.32 C ATOM 359 CE LYS A 140 121.534 201.803 849.336 1.00 42.65 C ATOM 360 NZ LYS A 140 122.543 200.744 849.625 1.00 43.86 N ATOM 361 N VAL A 141 123.400 207.344 848.558 1.00 14.52 N ATOM 362 CA VAL A 141 123.245 207.811 847.183 1.00 16.93 C ATOM 363 C VAL A 141 124.562 208.383 846.668 1.00 14.71 C ATOM 364 O VAL A 141 125.014 208.053 845.572 1.00 16.39 O ATOM 365 CB VAL A 141 122.166 208.929 847.096 1.00 17.73 C ATOM 366 CG1 VAL A 141 122.241 209.631 845.745 1.00 20.02 C ATOM 367 CG2 VAL A 141 120.779 208.313 847.301 1.00 19.79 C ATOM 368 N LEU A 142 125.175 209.238 847.477 1.00 13.33 N ATOM 369 CA LEU A 142 126.421 209.876 847.072 1.00 13.29 C ATOM 370 C LEU A 142 127.593 208.902 846.960 1.00 15.29 C ATOM 371 O LEU A 142 128.459 209.067 846.102 1.00 14.69 O ATOM 372 CB LEU A 142 126.759 211.003 848.045 1.00 12.01 C ATOM 373 CG LEU A 142 125.785 212.193 847.985 1.00 14.54 C ATOM 374 CD1 LEU A 142 125.951 213.049 849.266 1.00 12.24 C ATOM 375 CD2 LEU A 142 126.076 213.036 846.704 1.00 13.22 C ATOM 376 N ASN A 143 127.612 207.871 847.794 1.00 14.78 N ATOM 377 CA ASN A 143 128.716 206.923 847.733 1.00 17.01 C ATOM 378 C ASN A 143 128.512 205.713 846.845 1.00 17.01 C ATOM 379 O ASN A 143 129.483 205.053 846.470 1.00 18.75 O ATOM 380 CB ASN A 143 129.083 206.412 849.136 1.00 17.34 C ATOM 381 CG ASN A 143 129.631 207.488 850.024 1.00 17.83 C ATOM 382 OD1 ASN A 143 130.264 208.429 849.557 1.00 18.53 O ATOM 383 ND2 ASN A 143 129.399 207.353 851.333 1.00 20.42 N ATOM 384 N GLU A 144 127.271 205.407 846.493 1.00 16.97 N ATOM 385 CA GLU A 144 127.036 204.196 845.709 1.00 17.85 C ATOM 386 C GLU A 144 126.403 204.314 844.339 1.00 17.18 C ATOM 387 O GLU A 144 126.542 203.397 843.522 1.00 16.34 O ATOM 388 CB GLU A 144 126.211 203.208 846.539 1.00 21.08 C ATOM 389 CG GLU A 144 126.788 202.969 847.924 1.00 28.13 C ATOM 390 CD GLU A 144 125.956 202.001 848.756 1.00 34.70 C ATOM 391 OE1 GLU A 144 124.847 201.609 848.317 1.00 35.10 O ATOM 392 OE2 GLU A 144 126.417 201.643 849.862 1.00 35.48 O ATOM 393 N LEU A 145 125.695 205.399 844.067 1.00 15.13 N ATOM 394 CA LEU A 145 125.066 205.515 842.750 1.00 17.08 C ATOM 395 C LEU A 145 126.082 205.640 841.624 1.00 17.22 C ATOM 396 O LEU A 145 127.152 206.216 841.810 1.00 15.65 O ATOM 397 CB LEU A 145 124.148 206.736 842.667 1.00 21.51 C ATOM 398 CG LEU A 145 122.695 206.662 843.152 1.00 27.71 C ATOM 399 CD1 LEU A 145 121.966 207.859 842.552 1.00 27.14 C ATOM 400 CD2 LEU A 145 122.014 205.371 842.711 1.00 28.46 C ATOM 401 N PRO A 146 125.754 205.094 840.443 1.00 16.95 N ATOM 402 CA PRO A 146 126.669 205.188 839.296 1.00 15.77 C ATOM 403 C PRO A 146 126.880 206.679 839.034 1.00 16.28 C ATOM 404 O PRO A 146 125.962 207.493 839.213 1.00 13.23 O ATOM 405 CB PRO A 146 125.884 204.533 838.166 1.00 17.01 C ATOM 406 CG PRO A 146 125.096 203.449 838.910 1.00 20.73 C ATOM 407 CD PRO A 146 124.627 204.187 840.158 1.00 17.02 C ATOM 408 N GLU A 147 128.083 207.040 838.604 1.00 13.56 N ATOM 409 CA GLU A 147 128.390 208.444 838.344 1.00 13.41 C ATOM 410 C GLU A 147 127.449 209.095 837.328 1.00 12.86 C ATOM 411 O GLU A 147 127.068 210.258 837.472 1.00 13.02 O ATOM 412 CB GLU A 147 129.843 208.566 837.854 1.00 13.03 C ATOM 413 CG GLU A 147 130.327 210.024 837.672 1.00 11.91 C ATOM 414 CD GLU A 147 131.821 210.084 837.365 1.00 16.61 C ATOM 415 OE1 GLU A 147 132.508 209.063 837.593 1.00 15.20 O ATOM 416 OE2 GLU A 147 132.299 211.145 836.916 1.00 17.29 O ATOM 417 N GLU A 148 127.053 208.351 836.301 1.00 13.00 N ATOM 418 CA GLU A 148 126.172 208.930 835.285 1.00 11.89 C ATOM 419 C GLU A 148 124.797 209.242 835.869 1.00 13.75 C ATOM 420 O GLU A 148 124.124 210.184 835.442 1.00 12.13 O ATOM 421 CB GLU A 148 126.040 207.982 834.093 1.00 12.22 C ATOM 422 CG GLU A 148 127.326 207.822 833.271 1.00 15.76 C ATOM 423 CD GLU A 148 127.771 209.110 832.606 1.00 16.75 C ATOM 424 OE1 GLU A 148 126.927 210.010 832.417 1.00 17.96 O ATOM 425 OE2 GLU A 148 128.968 209.223 832.258 1.00 16.86 O ATOM 426 N GLU A 149 124.378 208.451 836.849 1.00 13.57 N ATOM 427 CA GLU A 149 123.075 208.720 837.471 1.00 14.25 C ATOM 428 C GLU A 149 123.176 209.940 838.368 1.00 12.02 C ATOM 429 O GLU A 149 122.232 210.728 838.451 1.00 14.19 O ATOM 430 CB GLU A 149 122.569 207.504 838.263 1.00 19.15 C ATOM 431 CG GLU A 149 121.124 207.685 838.712 1.00 26.18 C ATOM 432 CD GLU A 149 120.482 206.418 839.273 1.00 30.90 C ATOM 433 OE1 GLU A 149 119.285 206.506 839.644 1.00 30.85 O ATOM 434 OE2 GLU A 149 121.156 205.355 839.344 1.00 27.60 O ATOM 435 N LEU A 150 124.308 210.108 839.057 1.00 10.93 N ATOM 436 CA LEU A 150 124.502 211.298 839.884 1.00 12.74 C ATOM 437 C LEU A 150 124.487 212.517 838.974 1.00 13.26 C ATOM 438 O LEU A 150 123.909 213.563 839.307 1.00 13.26 O ATOM 439 CB LEU A 150 125.850 211.245 840.614 1.00 13.60 C ATOM 440 CG LEU A 150 125.912 210.319 841.828 1.00 15.97 C ATOM 441 CD1 LEU A 150 127.351 210.275 842.345 1.00 17.36 C ATOM 442 CD2 LEU A 150 124.972 210.838 842.923 1.00 17.09 C ATOM 443 N ALA A 151 125.136 212.399 837.815 1.00 12.22 N ATOM 444 CA ALA A 151 125.165 213.526 836.882 1.00 11.42 C ATOM 445 C ALA A 151 123.745 213.877 836.433 1.00 11.24 C ATOM 446 O ALA A 151 123.389 215.043 836.345 1.00 12.65 O ATOM 447 CB ALA A 151 126.042 213.191 835.666 1.00 14.15 C ATOM 448 N ARG A 152 122.947 212.858 836.140 1.00 11.66 N ATOM 449 CA ARG A 152 121.570 213.072 835.695 1.00 14.01 C ATOM 450 C ARG A 152 120.760 213.783 836.787 1.00 13.50 C ATOM 451 O ARG A 152 120.009 214.733 836.520 1.00 13.77 O ATOM 452 CB ARG A 152 120.919 211.719 835.368 1.00 16.92 C ATOM 453 CG ARG A 152 119.566 211.825 834.707 1.00 27.82 C ATOM 454 CD ARG A 152 118.412 211.391 835.607 1.00 37.50 C ATOM 455 NE ARG A 152 117.381 210.746 834.794 1.00 46.11 N ATOM 456 CZ ARG A 152 116.106 210.607 835.147 1.00 50.53 C ATOM 457 NH1 ARG A 152 115.669 211.072 836.314 1.00 55.01 N ATOM 458 NH2 ARG A 152 115.265 210.002 834.325 1.00 51.21 N ATOM 459 N ILE A 153 120.915 213.309 838.016 1.00 12.64 N ATOM 460 CA ILE A 153 120.204 213.895 839.168 1.00 14.43 C ATOM 461 C ILE A 153 120.551 215.365 839.386 1.00 14.69 C ATOM 462 O ILE A 153 119.665 216.208 839.574 1.00 14.66 O ATOM 463 CB ILE A 153 120.533 213.094 840.457 1.00 16.28 C ATOM 464 CG1 ILE A 153 119.847 211.720 840.392 1.00 17.10 C ATOM 465 CD1 ILE A 153 120.383 210.716 841.450 1.00 19.30 C ATOM 466 CG2 ILE A 153 120.133 213.892 841.716 1.00 17.33 C ATOM 467 N ILE A 154 121.840 215.674 839.344 1.00 13.10 N ATOM 468 CA ILE A 154 122.300 217.033 839.564 1.00 12.13 C ATOM 469 C ILE A 154 121.852 217.948 838.421 1.00 13.72 C ATOM 470 O ILE A 154 121.516 219.107 838.633 1.00 12.69 O ATOM 471 CB ILE A 154 123.823 217.029 839.757 1.00 13.37 C ATOM 472 CG1 ILE A 154 124.151 216.322 841.084 1.00 16.10 C ATOM 473 CD1 ILE A 154 125.604 215.892 841.230 1.00 17.24 C ATOM 474 CG2 ILE A 154 124.366 218.459 839.764 1.00 14.44 C ATOM 475 N PHE A 155 121.807 217.409 837.212 1.00 13.06 N ATOM 476 CA PHE A 155 121.337 218.197 836.073 1.00 12.67 C ATOM 477 C PHE A 155 119.827 218.452 836.157 1.00 14.12 C ATOM 478 O PHE A 155 119.366 219.593 836.067 1.00 14.78 O ATOM 479 CB PHE A 155 121.617 217.452 834.757 1.00 14.76 C ATOM 480 CG PHE A 155 120.991 218.100 833.551 1.00 17.41 C ATOM 481 CD1 PHE A 155 121.612 219.166 832.912 1.00 21.13 C ATOM 482 CE1 PHE A 155 120.988 219.829 831.852 1.00 22.07 C ATOM 483 CZ PHE A 155 119.719 219.414 831.422 1.00 22.99 C ATOM 484 CE2 PHE A 155 119.096 218.350 832.043 1.00 20.58 C ATOM 485 CD2 PHE A 155 119.735 217.692 833.106 1.00 20.35 C ATOM 486 N GLU A 156 119.068 217.376 836.332 1.00 13.24 N ATOM 487 CA GLU A 156 117.620 217.452 836.336 1.00 14.55 C ATOM 488 C GLU A 156 117.002 218.049 837.601 1.00 17.57 C ATOM 489 O GLU A 156 116.150 218.938 837.518 1.00 15.14 O ATOM 490 CB GLU A 156 117.023 216.057 836.069 1.00 15.64 C ATOM 491 CG GLU A 156 115.480 216.064 835.999 1.00 19.40 C ATOM 492 CD GLU A 156 114.860 214.684 835.801 1.00 22.67 C ATOM 493 OE1 GLU A 156 115.508 213.674 836.120 1.00 23.31 O ATOM 494 OE2 GLU A 156 113.700 214.609 835.335 1.00 27.40 O ATOM 495 N TYR A 157 117.427 217.571 838.764 1.00 14.95 N ATOM 496 CA TYR A 157 116.858 218.085 840.010 1.00 17.99 C ATOM 497 C TYR A 157 117.590 219.291 840.560 1.00 18.30 C ATOM 498 O TYR A 157 116.994 220.124 841.241 1.00 17.58 O ATOM 499 CB TYR A 157 116.867 216.983 841.060 1.00 15.87 C ATOM 500 CG TYR A 157 115.953 215.820 840.763 1.00 16.68 C ATOM 501 CD1 TYR A 157 114.951 215.900 839.790 1.00 18.40 C ATOM 502 CE1 TYR A 157 114.104 214.820 839.539 1.00 20.65 C ATOM 503 CZ TYR A 157 114.252 213.651 840.262 1.00 22.97 C ATOM 504 OH TYR A 157 113.418 212.574 840.041 1.00 24.50 O ATOM 505 CE2 TYR A 157 115.249 213.550 841.224 1.00 20.83 C ATOM 506 CD2 TYR A 157 116.091 214.636 841.467 1.00 16.11 C ATOM 507 N GLY A 158 118.886 219.385 840.287 1.00 14.97 N ATOM 508 CA GLY A 158 119.630 220.523 840.791 1.00 16.55 C ATOM 509 C GLY A 158 119.590 221.692 839.829 1.00 19.22 C ATOM 510 O GLY A 158 119.851 222.827 840.209 1.00 20.61 O ATOM 511 N GLU A 159 119.236 221.412 838.582 1.00 19.12 N ATOM 512 CA GLU A 159 119.221 222.428 837.544 1.00 20.64 C ATOM 513 C GLU A 159 120.614 223.019 837.319 1.00 20.35 C ATOM 514 O GLU A 159 120.764 224.210 837.038 1.00 19.66 O ATOM 515 CB GLU A 159 118.191 223.528 837.863 1.00 26.56 C ATOM 516 CG GLU A 159 116.757 223.010 837.835 1.00 31.38 C ATOM 517 CD GLU A 159 115.721 224.117 837.998 1.00 39.09 C ATOM 518 OE1 GLU A 159 115.761 224.830 839.026 1.00 40.97 O ATOM 519 OE2 GLU A 159 114.867 224.270 837.097 1.00 40.84 O ATOM 520 N GLU A 160 121.643 222.188 837.474 1.00 19.83 N ATOM 521 CA GLU A 160 123.025 222.619 837.200 1.00 17.97 C ATOM 522 C GLU A 160 123.170 222.274 835.721 1.00 18.41 C ATOM 523 O GLU A 160 123.606 221.188 835.361 1.00 19.35 O ATOM 524 CB GLU A 160 124.033 221.818 838.029 1.00 16.88 C ATOM 525 CG GLU A 160 124.099 222.246 839.515 1.00 16.88 C ATOM 526 CD GLU A 160 124.825 223.573 839.737 1.00 21.94 C ATOM 527 OE1 GLU A 160 125.181 224.243 838.738 1.00 21.53 O ATOM 528 OE2 GLU A 160 125.040 223.953 840.914 1.00 19.84 O ATOM 529 N LYS A 161 122.792 223.213 834.871 1.00 17.89 N ATOM 530 CA LYS A 161 122.793 222.989 833.425 1.00 20.47 C ATOM 531 C LYS A 161 124.142 222.988 832.729 1.00 21.48 C ATOM 532 O LYS A 161 124.228 222.632 831.555 1.00 25.62 O ATOM 533 CB LYS A 161 121.866 224.010 832.765 1.00 22.72 C ATOM 534 CG LYS A 161 120.421 223.841 833.216 1.00 29.41 C ATOM 535 CD LYS A 161 119.514 224.906 832.633 1.00 35.30 C ATOM 536 CE LYS A 161 118.090 224.756 833.158 1.00 40.66 C ATOM 537 NZ LYS A 161 117.228 225.918 832.770 1.00 45.76 N ATOM 538 N ARG A 162 125.190 223.375 833.435 1.00 16.45 N ATOM 539 CA ARG A 162 126.508 223.373 832.836 1.00 17.87 C ATOM 540 C ARG A 162 127.506 222.509 833.594 1.00 15.97 C ATOM 541 O ARG A 162 128.312 221.802 832.988 1.00 17.12 O ATOM 542 CB ARG A 162 127.059 224.806 832.738 1.00 17.09 C ATOM 543 CG ARG A 162 128.408 224.896 831.998 1.00 18.57 C ATOM 544 CD ARG A 162 128.879 226.361 831.843 1.00 16.34 C ATOM 545 NE ARG A 162 127.960 227.171 831.042 1.00 17.51 N ATOM 546 CZ ARG A 162 127.857 227.109 829.714 1.00 20.03 C ATOM 547 NH1 ARG A 162 128.618 226.270 829.013 1.00 18.05 N ATOM 548 NH2 ARG A 162 126.995 227.889 829.082 1.00 21.38 N ATOM 549 N PHE A 163 127.449 222.551 834.921 1.00 13.05 N ATOM 550 CA PHE A 163 128.424 221.822 835.729 1.00 12.31 C ATOM 551 C PHE A 163 128.003 220.490 836.339 1.00 12.49 C ATOM 552 O PHE A 163 128.748 219.936 837.134 1.00 12.80 O ATOM 553 CB PHE A 163 128.934 222.756 836.837 1.00 14.64 C ATOM 554 CG PHE A 163 129.717 223.945 836.316 1.00 16.51 C ATOM 555 CD1 PHE A 163 131.064 223.813 835.978 1.00 18.35 C ATOM 556 CE1 PHE A 163 131.786 224.900 835.471 1.00 20.45 C ATOM 557 CZ PHE A 163 131.162 226.130 835.294 1.00 21.06 C ATOM 558 CE2 PHE A 163 129.812 226.280 835.628 1.00 20.70 C ATOM 559 CD2 PHE A 163 129.098 225.181 836.139 1.00 18.10 C ATOM 560 N ALA A 164 126.842 219.956 835.960 1.00 12.15 N ATOM 561 CA ALA A 164 126.388 218.684 836.533 1.00 13.87 C ATOM 562 C ALA A 164 127.409 217.543 836.437 1.00 13.37 C ATOM 563 O ALA A 164 127.651 216.834 837.414 1.00 11.65 O ATOM 564 CB ALA A 164 125.065 218.241 835.874 1.00 12.26 C ATOM 565 N ARG A 165 128.002 217.344 835.263 1.00 12.95 N ATOM 566 CA ARG A 165 128.958 216.251 835.123 1.00 10.78 C ATOM 567 C ARG A 165 130.202 216.434 835.988 1.00 10.58 C ATOM 568 O ARG A 165 130.708 215.481 836.574 1.00 13.28 O ATOM 569 CB ARG A 165 129.358 216.076 833.642 1.00 11.97 C ATOM 570 CG ARG A 165 128.174 215.721 832.710 1.00 12.21 C ATOM 571 CD ARG A 165 128.673 215.270 831.317 1.00 12.05 C ATOM 572 NE ARG A 165 129.487 214.067 831.467 1.00 12.64 N ATOM 573 CZ ARG A 165 128.991 212.843 831.657 1.00 15.09 C ATOM 574 NH1 ARG A 165 127.676 212.639 831.696 1.00 14.68 N ATOM 575 NH2 ARG A 165 129.816 211.825 831.876 1.00 13.96 N ATOM 576 N ARG A 166 130.709 217.655 836.069 1.00 10.89 N ATOM 577 CA ARG A 166 131.903 217.889 836.875 1.00 12.49 C ATOM 578 C ARG A 166 131.600 217.725 838.361 1.00 11.98 C ATOM 579 O ARG A 166 132.435 217.229 839.112 1.00 12.45 O ATOM 580 CB ARG A 166 132.455 219.284 836.608 1.00 17.84 C ATOM 581 CG ARG A 166 133.872 219.457 837.133 1.00 24.79 C ATOM 582 CD ARG A 166 134.419 220.801 836.719 1.00 26.50 C ATOM 583 NE ARG A 166 135.514 221.213 837.585 1.00 29.65 N ATOM 584 CZ ARG A 166 136.735 220.699 837.555 1.00 30.55 C ATOM 585 NH1 ARG A 166 137.040 219.737 836.684 1.00 29.83 N ATOM 586 NH2 ARG A 166 137.651 221.157 838.400 1.00 28.92 N ATOM 587 N ILE A 167 130.405 218.132 838.787 1.00 11.67 N ATOM 588 CA ILE A 167 130.053 217.966 840.199 1.00 11.39 C ATOM 589 C ILE A 167 129.956 216.468 840.503 1.00 11.27 C ATOM 590 O ILE A 167 130.441 215.999 841.527 1.00 12.21 O ATOM 591 CB ILE A 167 128.705 218.675 840.531 1.00 11.96 C ATOM 592 CG1 ILE A 167 128.878 220.200 840.390 1.00 12.39 C ATOM 593 CD1 ILE A 167 127.538 220.984 840.346 1.00 14.47 C ATOM 594 CG2 ILE A 167 128.272 218.340 841.985 1.00 11.28 C ATOM 595 N ALA A 168 129.340 215.705 839.604 1.00 11.74 N ATOM 596 CA ALA A 168 129.230 214.266 839.825 1.00 12.93 C ATOM 597 C ALA A 168 130.632 213.660 839.911 1.00 12.41 C ATOM 598 O ALA A 168 130.902 212.805 840.751 1.00 11.46 O ATOM 599 CB ALA A 168 128.434 213.600 838.688 1.00 9.75 C ATOM 600 N ARG A 169 131.529 214.109 839.038 1.00 10.79 N ATOM 601 CA ARG A 169 132.910 213.590 839.048 1.00 10.97 C ATOM 602 C ARG A 169 133.617 213.887 840.378 1.00 13.39 C ATOM 603 O ARG A 169 134.292 213.022 840.951 1.00 12.05 O ATOM 604 CB ARG A 169 133.702 214.216 837.882 1.00 12.46 C ATOM 605 CG ARG A 169 135.201 213.863 837.868 1.00 13.58 C ATOM 606 CD ARG A 169 135.499 212.634 836.993 1.00 12.69 C ATOM 607 NE ARG A 169 134.974 211.354 837.476 1.00 12.30 N ATOM 608 CZ ARG A 169 135.681 210.472 838.178 1.00 13.43 C ATOM 609 NH1 ARG A 169 136.943 210.740 838.510 1.00 15.51 N ATOM 610 NH2 ARG A 169 135.166 209.280 838.472 1.00 12.14 N ATOM 611 N LYS A 170 133.463 215.104 840.878 1.00 11.40 N ATOM 612 CA LYS A 170 134.099 215.461 842.143 1.00 13.65 C ATOM 613 C LYS A 170 133.489 214.721 843.314 1.00 13.42 C ATOM 614 O LYS A 170 134.173 214.434 844.288 1.00 14.57 O ATOM 615 CB LYS A 170 134.024 216.968 842.366 1.00 13.50 C ATOM 616 CG LYS A 170 134.881 217.759 841.366 1.00 17.07 C ATOM 617 CD LYS A 170 136.322 217.292 841.437 1.00 21.14 C ATOM 618 CE LYS A 170 137.190 217.978 840.385 1.00 26.69 C ATOM 619 NZ LYS A 170 138.574 217.404 840.388 1.00 29.37 N ATOM 620 N ILE A 171 132.197 214.423 843.241 1.00 12.60 N ATOM 621 CA ILE A 171 131.581 213.656 844.324 1.00 12.27 C ATOM 622 C ILE A 171 132.248 212.279 844.328 1.00 13.16 C ATOM 623 O ILE A 171 132.681 211.786 845.368 1.00 12.73 O ATOM 624 CB ILE A 171 130.077 213.498 844.094 1.00 12.53 C ATOM 625 CG1 ILE A 171 129.381 214.839 844.379 1.00 14.18 C ATOM 626 CD1 ILE A 171 127.958 214.886 843.888 1.00 14.42 C ATOM 627 CG2 ILE A 171 129.510 212.377 844.977 1.00 13.54 C ATOM 628 N VAL A 172 132.327 211.644 843.157 1.00 11.65 N ATOM 629 CA VAL A 172 132.956 210.336 843.088 1.00 12.67 C ATOM 630 C VAL A 172 134.413 210.431 843.568 1.00 12.74 C ATOM 631 O VAL A 172 134.890 209.563 844.308 1.00 14.54 O ATOM 632 CB VAL A 172 132.907 209.759 841.635 1.00 13.68 C ATOM 633 CG1 VAL A 172 133.745 208.458 841.531 1.00 11.97 C ATOM 634 CG2 VAL A 172 131.462 209.481 841.242 1.00 11.86 C ATOM 635 N GLU A 173 135.120 211.485 843.173 1.00 12.41 N ATOM 636 CA GLU A 173 136.517 211.619 843.591 1.00 14.14 C ATOM 637 C GLU A 173 136.686 211.798 845.093 1.00 16.62 C ATOM 638 O GLU A 173 137.740 211.480 845.645 1.00 16.31 O ATOM 639 CB GLU A 173 137.187 212.777 842.840 1.00 15.63 C ATOM 640 CG GLU A 173 137.531 212.360 841.407 1.00 15.70 C ATOM 641 CD GLU A 173 138.067 213.478 840.522 1.00 16.09 C ATOM 642 OE1 GLU A 173 138.505 214.534 841.022 1.00 16.22 O ATOM 643 OE2 GLU A 173 138.066 213.273 839.292 1.00 17.72 O ATOM 644 N ASN A 174 135.639 212.293 845.756 1.00 15.02 N ATOM 645 CA ASN A 174 135.683 212.509 847.201 1.00 16.51 C ATOM 646 C ASN A 174 135.135 211.363 848.054 1.00 17.76 C ATOM 647 O ASN A 174 135.047 211.490 849.276 1.00 20.17 O ATOM 648 CB ASN A 174 134.936 213.811 847.561 1.00 15.23 C ATOM 649 CG ASN A 174 135.782 215.043 847.353 1.00 19.63 C ATOM 650 OD1 ASN A 174 135.832 215.618 846.259 1.00 22.83 O ATOM 651 ND2 ASN A 174 136.468 215.457 848.404 1.00 18.04 N ATOM 652 N ARG A 175 134.760 210.252 847.427 1.00 17.70 N ATOM 653 CA ARG A 175 134.229 209.108 848.169 1.00 16.15 C ATOM 654 C ARG A 175 135.284 208.493 849.092 1.00 21.22 C ATOM 655 O ARG A 175 136.473 208.436 848.752 1.00 20.09 O ATOM 656 CB ARG A 175 133.718 208.030 847.206 1.00 15.53 C ATOM 657 CG ARG A 175 132.491 208.466 846.442 1.00 13.63 C ATOM 658 CD ARG A 175 132.064 207.431 845.442 1.00 12.89 C ATOM 659 NE ARG A 175 130.721 207.725 844.974 1.00 14.90 N ATOM 660 CZ ARG A 175 130.135 207.097 843.972 1.00 14.62 C ATOM 661 NH1 ARG A 175 130.789 206.147 843.307 1.00 13.98 N ATOM 662 NH2 ARG A 175 128.869 207.375 843.674 1.00 14.85 N ATOM 663 N PRO A 176 134.858 208.026 850.275 1.00 22.23 N ATOM 664 CA PRO A 176 133.462 208.070 850.746 1.00 21.78 C ATOM 665 C PRO A 176 133.137 209.403 851.403 1.00 19.50 C ATOM 666 O PRO A 176 133.951 209.944 852.142 1.00 20.19 O ATOM 667 CB PRO A 176 133.384 206.925 851.768 1.00 25.59 C ATOM 668 CG PRO A 176 134.800 206.281 851.780 1.00 28.86 C ATOM 669 CD PRO A 176 135.721 207.330 851.247 1.00 25.85 C ATOM 670 N LEU A 177 131.961 209.956 851.117 1.00 16.62 N ATOM 671 CA LEU A 177 131.565 211.205 851.752 1.00 15.29 C ATOM 672 C LEU A 177 130.851 210.817 853.050 1.00 18.99 C ATOM 673 O LEU A 177 130.178 209.791 853.101 1.00 18.11 O ATOM 674 CB LEU A 177 130.597 212.006 850.872 1.00 17.44 C ATOM 675 CG LEU A 177 131.233 212.743 849.678 1.00 17.36 C ATOM 676 CD1 LEU A 177 131.561 211.707 848.591 1.00 18.55 C ATOM 677 CD2 LEU A 177 130.257 213.806 849.133 1.00 16.78 C ATOM 678 N ASN A 178 130.996 211.636 854.083 1.00 19.58 N ATOM 679 CA ASN A 178 130.361 211.337 855.366 1.00 22.24 C ATOM 680 C ASN A 178 129.528 212.468 855.924 1.00 20.55 C ATOM 681 O ASN A 178 128.522 212.228 856.581 1.00 23.23 O ATOM 682 CB ASN A 178 131.422 210.955 856.408 1.00 23.49 C ATOM 683 CG ASN A 178 132.084 209.635 856.090 1.00 26.84 C ATOM 684 OD1 ASN A 178 131.427 208.607 856.052 1.00 29.28 O ATOM 685 ND2 ASN A 178 133.386 209.662 855.840 1.00 31.62 N ATOM 686 N THR A 179 129.931 213.703 855.657 1.00 18.52 N ATOM 687 CA THR A 179 129.217 214.842 856.207 1.00 16.89 C ATOM 688 C THR A 179 128.855 215.886 855.177 1.00 18.34 C ATOM 689 O THR A 179 129.335 215.864 854.044 1.00 18.58 O ATOM 690 CB THR A 179 130.066 215.584 857.262 1.00 18.48 C ATOM 691 OG1 THR A 179 131.022 216.411 856.586 1.00 19.00 O ATOM 692 CG2 THR A 179 130.809 214.592 858.165 1.00 19.06 C ATOM 693 N THR A 180 128.026 216.828 855.603 1.00 15.43 N ATOM 694 CA THR A 180 127.623 217.939 854.760 1.00 15.27 C ATOM 695 C THR A 180 128.849 218.702 854.257 1.00 18.35 C ATOM 696 O THR A 180 128.856 219.210 853.136 1.00 15.25 O ATOM 697 CB THR A 180 126.746 218.909 855.549 1.00 18.23 C ATOM 698 OG1 THR A 180 127.370 219.170 856.815 1.00 18.43 O ATOM 699 CG2 THR A 180 125.349 218.298 855.787 1.00 13.53 C ATOM 700 N LEU A 181 129.886 218.798 855.082 1.00 16.71 N ATOM 701 CA LEU A 181 131.075 219.525 854.649 1.00 18.01 C ATOM 702 C LEU A 181 131.817 218.773 853.546 1.00 17.32 C ATOM 703 O LEU A 181 132.500 219.401 852.736 1.00 16.76 O ATOM 704 CB LEU A 181 132.008 219.807 855.836 1.00 22.05 C ATOM 705 CG LEU A 181 131.347 220.638 856.960 1.00 25.88 C ATOM 706 CD1 LEU A 181 132.393 221.011 858.002 1.00 28.66 C ATOM 707 CD2 LEU A 181 130.717 221.898 856.384 1.00 26.64 C ATOM 708 N ASP A 182 131.692 217.447 853.512 1.00 16.27 N ATOM 709 CA ASP A 182 132.340 216.660 852.459 1.00 17.88 C ATOM 710 C ASP A 182 131.661 216.944 851.120 1.00 17.65 C ATOM 711 O ASP A 182 132.315 217.016 850.080 1.00 18.10 O ATOM 712 CB ASP A 182 132.257 215.151 852.738 1.00 17.95 C ATOM 713 CG ASP A 182 133.027 214.739 853.992 1.00 19.60 C ATOM 714 OD1 ASP A 182 134.002 215.425 854.337 1.00 20.05 O ATOM 715 OD2 ASP A 182 132.658 213.726 854.623 1.00 17.86 O ATOM 716 N LEU A 183 130.335 217.097 851.140 1.00 16.11 N ATOM 717 CA LEU A 183 129.605 217.388 849.905 1.00 16.27 C ATOM 718 C LEU A 183 129.926 218.814 849.448 1.00 14.92 C ATOM 719 O LEU A 183 130.128 219.057 848.253 1.00 14.99 O ATOM 720 CB LEU A 183 128.079 217.214 850.099 1.00 13.25 C ATOM 721 CG LEU A 183 127.214 217.448 848.842 1.00 15.30 C ATOM 722 CD1 LEU A 183 127.741 216.554 847.683 1.00 15.23 C ATOM 723 CD2 LEU A 183 125.741 217.101 849.120 1.00 15.64 C ATOM 724 N VAL A 184 129.993 219.762 850.380 1.00 13.80 N ATOM 725 CA VAL A 184 130.329 221.134 849.998 1.00 14.08 C ATOM 726 C VAL A 184 131.727 221.159 849.330 1.00 14.43 C ATOM 727 O VAL A 184 131.940 221.876 848.343 1.00 13.60 O ATOM 728 CB VAL A 184 130.334 222.088 851.234 1.00 15.56 C ATOM 729 CG1 VAL A 184 130.921 223.449 850.854 1.00 15.78 C ATOM 730 CG2 VAL A 184 128.884 222.276 851.754 1.00 13.36 C ATOM 731 N LYS A 185 132.667 220.387 849.880 1.00 14.43 N ATOM 732 CA LYS A 185 134.030 220.321 849.339 1.00 17.24 C ATOM 733 C LYS A 185 134.019 219.846 847.878 1.00 17.12 C ATOM 734 O LYS A 185 134.719 220.406 847.033 1.00 16.92 O ATOM 735 CB LYS A 185 134.894 219.373 850.199 1.00 18.32 C ATOM 736 CG LYS A 185 136.337 219.108 849.676 1.00 19.92 C ATOM 737 CD LYS A 185 137.151 218.259 850.670 1.00 22.27 C ATOM 738 CE LYS A 185 138.610 218.001 850.214 1.00 21.58 C ATOM 739 NZ LYS A 185 138.706 217.122 848.989 1.00 24.80 N ATOM 740 N ALA A 186 133.227 218.813 847.598 1.00 13.80 N ATOM 741 CA ALA A 186 133.103 218.256 846.246 1.00 16.09 C ATOM 742 C ALA A 186 132.543 219.301 845.283 1.00 15.81 C ATOM 743 O ALA A 186 133.066 219.487 844.177 1.00 13.81 O ATOM 744 CB ALA A 186 132.191 217.026 846.266 1.00 14.73 C ATOM 745 N VAL A 187 131.487 220.001 845.691 1.00 14.47 N ATOM 746 CA VAL A 187 130.938 221.001 844.798 1.00 14.53 C ATOM 747 C VAL A 187 131.951 222.138 844.590 1.00 16.18 C ATOM 748 O VAL A 187 132.095 222.648 843.470 1.00 15.52 O ATOM 749 CB VAL A 187 129.591 221.592 845.323 1.00 14.88 C ATOM 750 CG1 VAL A 187 129.015 222.556 844.276 1.00 13.95 C ATOM 751 CG2 VAL A 187 128.579 220.466 845.596 1.00 14.89 C ATOM 752 N ARG A 188 132.653 222.526 845.656 1.00 14.56 N ATOM 753 CA ARG A 188 133.627 223.615 845.558 1.00 17.21 C ATOM 754 C ARG A 188 134.743 223.269 844.568 1.00 17.98 C ATOM 755 O ARG A 188 135.193 224.125 843.799 1.00 16.80 O ATOM 756 CB ARG A 188 134.254 223.929 846.926 1.00 18.14 C ATOM 757 CG ARG A 188 135.239 225.124 846.863 1.00 20.70 C ATOM 758 CD ARG A 188 136.014 225.339 848.169 1.00 27.30 C ATOM 759 NE ARG A 188 135.149 225.778 849.260 1.00 30.82 N ATOM 760 CZ ARG A 188 134.651 227.006 849.386 1.00 35.47 C ATOM 761 NH1 ARG A 188 134.931 227.946 848.485 1.00 37.35 N ATOM 762 NH2 ARG A 188 133.853 227.289 850.410 1.00 38.04 N ATOM 763 N GLU A 189 135.193 222.019 844.605 1.00 15.19 N ATOM 764 CA GLU A 189 136.248 221.573 843.691 1.00 19.00 C ATOM 765 C GLU A 189 135.755 221.497 842.240 1.00 18.93 C ATOM 766 O GLU A 189 136.550 221.573 841.301 1.00 17.61 O ATOM 767 CB GLU A 189 136.791 220.207 844.152 1.00 17.80 C ATOM 768 CG GLU A 189 137.430 220.294 845.536 1.00 22.30 C ATOM 769 CD GLU A 189 137.954 218.978 846.070 1.00 22.47 C ATOM 770 OE1 GLU A 189 137.621 217.907 845.510 1.00 22.23 O ATOM 771 OE2 GLU A 189 138.704 219.021 847.072 1.00 26.25 O ATOM 772 N ALA A 190 134.446 221.370 842.050 1.00 15.46 N ATOM 773 CA ALA A 190 133.891 221.286 840.702 1.00 17.07 C ATOM 774 C ALA A 190 133.671 222.642 840.039 1.00 18.18 C ATOM 775 O ALA A 190 133.624 222.732 838.812 1.00 21.87 O ATOM 776 CB ALA A 190 132.563 220.545 840.736 1.00 15.20 C ATOM 777 N LEU A 191 133.505 223.688 840.841 1.00 16.51 N ATOM 778 CA LEU A 191 133.232 225.024 840.306 1.00 18.28 C ATOM 779 C LEU A 191 134.423 225.977 840.390 1.00 19.22 C ATOM 780 O LEU A 191 135.080 226.073 841.422 1.00 21.30 O ATOM 781 CB LEU A 191 132.030 225.643 841.049 1.00 17.11 C ATOM 782 CG LEU A 191 130.741 224.812 841.052 1.00 18.53 C ATOM 783 CD1 LEU A 191 129.651 225.532 841.862 1.00 19.97 C ATOM 784 CD2 LEU A 191 130.269 224.593 839.604 1.00 17.85 C ATOM 785 N PRO A 192 134.719 226.695 839.294 1.00 19.82 N ATOM 786 CA PRO A 192 135.838 227.643 839.258 1.00 20.24 C ATOM 787 C PRO A 192 135.550 228.792 840.213 1.00 19.03 C ATOM 788 O PRO A 192 134.393 229.121 840.439 1.00 19.77 O ATOM 789 CB PRO A 192 135.833 228.149 837.814 1.00 21.26 C ATOM 790 CG PRO A 192 135.134 227.072 837.061 1.00 24.77 C ATOM 791 CD PRO A 192 134.049 226.623 837.984 1.00 19.59 C ATOM 792 N SER A 193 136.594 229.423 840.739 1.00 23.31 N ATOM 793 CA SER A 193 136.407 230.547 841.655 1.00 23.78 C ATOM 794 C SER A 193 135.492 231.624 841.096 1.00 22.55 C ATOM 795 O SER A 193 134.640 232.146 841.813 1.00 21.59 O ATOM 796 CB SER A 193 137.753 231.189 842.019 1.00 23.97 C ATOM 797 OG SER A 193 138.569 230.272 842.709 1.00 33.66 O ATOM 798 N TYR A 194 135.648 231.972 839.820 1.00 22.96 N ATOM 799 CA TYR A 194 134.794 233.018 839.266 1.00 21.35 C ATOM 800 C TYR A 194 133.320 232.624 839.248 1.00 22.56 C ATOM 801 O TYR A 194 132.446 233.489 839.339 1.00 22.02 O ATOM 802 CB TYR A 194 135.248 233.417 837.843 1.00 22.35 C ATOM 803 CG TYR A 194 134.824 232.433 836.784 1.00 20.75 C ATOM 804 CD1 TYR A 194 133.542 232.480 836.224 1.00 20.89 C ATOM 805 CE1 TYR A 194 133.116 231.583 835.275 1.00 22.76 C ATOM 806 CZ TYR A 194 134.000 230.598 834.852 1.00 21.32 C ATOM 807 OH TYR A 194 133.600 229.664 833.919 1.00 24.19 O ATOM 808 CE2 TYR A 194 135.285 230.541 835.349 1.00 18.97 C ATOM 809 CD2 TYR A 194 135.687 231.469 836.295 1.00 20.30 C ATOM 810 N GLU A 195 133.039 231.325 839.120 1.00 21.94 N ATOM 811 CA GLU A 195 131.655 230.840 839.083 1.00 20.04 C ATOM 812 C GLU A 195 131.028 230.893 840.478 1.00 20.39 C ATOM 813 O GLU A 195 129.853 231.214 840.628 1.00 22.67 O ATOM 814 CB GLU A 195 131.618 229.397 838.536 1.00 19.66 C ATOM 815 CG GLU A 195 130.253 228.705 838.536 1.00 22.01 C ATOM 816 CD GLU A 195 129.231 229.372 837.645 1.00 24.32 C ATOM 817 OE1 GLU A 195 129.618 230.182 836.766 1.00 27.23 O ATOM 818 OE2 GLU A 195 128.031 229.075 837.814 1.00 25.47 O ATOM 819 N ILE A 196 131.812 230.557 841.490 1.00 22.58 N ATOM 820 CA ILE A 196 131.318 230.598 842.859 1.00 24.61 C ATOM 821 C ILE A 196 130.994 232.049 843.227 1.00 27.21 C ATOM 822 O ILE A 196 129.938 232.341 843.787 1.00 26.12 O ATOM 823 CB ILE A 196 132.366 230.022 843.824 1.00 24.26 C ATOM 824 CG1 ILE A 196 132.452 228.504 843.614 1.00 20.95 C ATOM 825 CD1 ILE A 196 133.600 227.847 844.350 1.00 23.00 C ATOM 826 CG2 ILE A 196 132.030 230.410 845.273 1.00 24.43 C ATOM 827 N ARG A 197 131.893 232.964 842.883 1.00 27.42 N ATOM 828 CA ARG A 197 131.674 234.372 843.192 1.00 30.34 C ATOM 829 C ARG A 197 130.507 234.957 842.417 1.00 30.81 C ATOM 830 O ARG A 197 129.794 235.824 842.922 1.00 31.17 O ATOM 831 CB ARG A 197 132.935 235.179 842.893 1.00 35.03 C ATOM 832 CG ARG A 197 134.099 234.815 843.781 1.00 41.88 C ATOM 833 CD ARG A 197 135.354 235.569 843.378 1.00 49.39 C ATOM 834 NE ARG A 197 136.494 235.183 844.201 1.00 53.35 N ATOM 835 CZ ARG A 197 137.759 235.455 843.898 1.00 57.06 C ATOM 836 NH1 ARG A 197 138.052 236.117 842.781 1.00 57.62 N ATOM 837 NH2 ARG A 197 138.734 235.070 844.715 1.00 57.21 N ATOM 838 N ARG A 198 130.302 234.475 841.195 1.00 29.73 N ATOM 839 CA ARG A 198 129.228 234.970 840.332 1.00 29.79 C ATOM 840 C ARG A 198 127.827 234.624 840.828 1.00 29.83 C ATOM 841 O ARG A 198 126.876 235.388 840.622 1.00 29.29 O ATOM 842 CB ARG A 198 129.406 234.400 838.918 1.00 30.32 C ATOM 843 CG ARG A 198 128.386 234.877 837.896 1.00 34.22 C ATOM 844 CD ARG A 198 128.514 234.111 836.574 1.00 35.20 C ATOM 845 NE ARG A 198 127.971 232.751 836.649 1.00 35.71 N ATOM 846 CZ ARG A 198 126.669 232.464 836.687 1.00 37.71 C ATOM 847 NH1 ARG A 198 125.770 233.439 836.657 1.00 34.59 N ATOM 848 NH2 ARG A 198 126.259 231.200 836.752 1.00 36.83 N ATOM 849 N ARG A 199 127.689 233.468 841.470 1.00 28.25 N ATOM 850 CA ARG A 199 126.389 233.021 841.958 1.00 28.93 C ATOM 851 C ARG A 199 125.827 233.828 843.118 1.00 29.15 C ATOM 852 O ARG A 199 126.559 234.240 844.009 1.00 30.56 O ATOM 853 CB ARG A 199 126.462 231.551 842.363 1.00 28.88 C ATOM 854 CG ARG A 199 126.737 230.647 841.190 1.00 28.25 C ATOM 855 CD ARG A 199 126.816 229.199 841.599 1.00 29.24 C ATOM 856 NE ARG A 199 127.067 228.369 840.429 1.00 25.03 N ATOM 857 CZ ARG A 199 126.625 227.129 840.294 1.00 24.55 C ATOM 858 NH1 ARG A 199 125.905 226.569 841.263 1.00 24.50 N ATOM 859 NH2 ARG A 199 126.886 226.460 839.181 1.00 18.77 N ATOM 860 N LYS A 200 124.515 234.023 843.099 1.00 29.36 N ATOM 861 CA LYS A 200 123.822 234.760 844.147 1.00 33.48 C ATOM 862 C LYS A 200 123.742 233.903 845.410 1.00 33.04 C ATOM 863 O LYS A 200 124.152 234.322 846.488 1.00 33.75 O ATOM 864 CB LYS A 200 122.404 235.124 843.680 1.00 37.22 C ATOM 865 CG LYS A 200 121.545 235.862 844.716 1.00 44.83 C ATOM 866 CD LYS A 200 122.081 237.262 845.038 1.00 50.08 C ATOM 867 CE LYS A 200 123.305 237.213 845.951 1.00 52.85 C ATOM 868 NZ LYS A 200 124.264 238.320 845.656 1.00 57.40 N ATOM 869 N ARG A 201 123.219 232.694 845.257 1.00 30.07 N ATOM 870 CA ARG A 201 123.075 231.765 846.368 1.00 29.45 C ATOM 871 C ARG A 201 124.356 230.961 846.574 1.00 27.74 C ATOM 872 O ARG A 201 125.164 230.816 845.649 1.00 26.67 O ATOM 873 CB ARG A 201 121.917 230.816 846.084 1.00 31.34 C ATOM 874 CG ARG A 201 120.559 231.494 845.965 1.00 35.93 C ATOM 875 CD ARG A 201 119.491 230.500 845.535 1.00 39.62 C ATOM 876 NE ARG A 201 119.635 230.134 844.128 1.00 43.69 N ATOM 877 CZ ARG A 201 118.901 229.210 843.516 1.00 45.72 C ATOM 878 NH1 ARG A 201 117.970 228.544 844.187 1.00 46.07 N ATOM 879 NH2 ARG A 201 119.087 228.966 842.223 1.00 47.09 N ATOM 880 N HIS A 202 124.545 230.446 847.787 1.00 23.46 N ATOM 881 CA HIS A 202 125.720 229.644 848.089 1.00 22.24 C ATOM 882 C HIS A 202 125.831 228.579 846.993 1.00 20.69 C ATOM 883 O HIS A 202 124.833 227.951 846.621 1.00 18.51 O ATOM 884 CB HIS A 202 125.577 228.981 849.458 1.00 22.64 C ATOM 885 CG HIS A 202 126.801 228.242 849.901 1.00 23.69 C ATOM 886 ND1 HIS A 202 127.171 227.026 849.366 1.00 20.45 N ATOM 887 CE1 HIS A 202 128.284 226.611 849.949 1.00 23.39 C ATOM 888 NE2 HIS A 202 128.648 227.516 850.842 1.00 23.86 N ATOM 889 CD2 HIS A 202 127.738 228.546 850.832 1.00 21.14 C ATOM 890 N PHE A 203 127.049 228.384 846.499 1.00 19.09 N ATOM 891 CA PHE A 203 127.324 227.446 845.412 1.00 19.93 C ATOM 892 C PHE A 203 126.868 225.998 845.594 1.00 18.41 C ATOM 893 O PHE A 203 126.633 225.304 844.606 1.00 18.38 O ATOM 894 CB PHE A 203 128.821 227.472 845.075 1.00 17.52 C ATOM 895 CG PHE A 203 129.707 226.973 846.186 1.00 18.03 C ATOM 896 CD1 PHE A 203 129.947 225.609 846.340 1.00 17.15 C ATOM 897 CE1 PHE A 203 130.773 225.128 847.366 1.00 15.94 C ATOM 898 CZ PHE A 203 131.380 226.043 848.259 1.00 18.43 C ATOM 899 CE2 PHE A 203 131.141 227.413 848.107 1.00 17.02 C ATOM 900 CD2 PHE A 203 130.308 227.870 847.074 1.00 17.35 C ATOM 901 N ALA A 204 126.735 225.532 846.833 1.00 16.75 N ATOM 902 CA ALA A 204 126.313 224.149 847.043 1.00 14.39 C ATOM 903 C ALA A 204 124.798 223.960 847.104 1.00 15.18 C ATOM 904 O ALA A 204 124.317 222.835 847.165 1.00 13.91 O ATOM 905 CB ALA A 204 126.944 223.593 848.322 1.00 16.28 C ATOM 906 N THR A 205 124.058 225.058 847.094 1.00 15.63 N ATOM 907 CA THR A 205 122.602 225.011 847.187 1.00 16.18 C ATOM 908 C THR A 205 121.910 224.032 846.234 1.00 16.76 C ATOM 909 O THR A 205 121.130 223.188 846.667 1.00 14.92 O ATOM 910 CB THR A 205 121.997 226.422 846.957 1.00 17.87 C ATOM 911 OG1 THR A 205 122.555 227.339 847.907 1.00 21.05 O ATOM 912 CG2 THR A 205 120.472 226.393 847.107 1.00 21.86 C ATOM 913 N LYS A 206 122.188 224.154 844.938 1.00 14.82 N ATOM 914 CA LYS A 206 121.538 223.292 843.951 1.00 15.23 C ATOM 915 C LYS A 206 121.858 221.819 844.061 1.00 14.47 C ATOM 916 O LYS A 206 120.980 220.985 843.851 1.00 15.03 O ATOM 917 CB LYS A 206 121.849 223.764 842.526 1.00 17.07 C ATOM 918 CG LYS A 206 121.217 225.087 842.147 1.00 21.73 C ATOM 919 CD LYS A 206 121.690 225.505 840.755 1.00 27.14 C ATOM 920 CE LYS A 206 120.808 226.601 840.190 1.00 33.17 C ATOM 921 NZ LYS A 206 121.068 226.816 838.744 1.00 34.98 N ATOM 922 N THR A 207 123.107 221.487 844.384 1.00 13.96 N ATOM 923 CA THR A 207 123.489 220.085 844.509 1.00 13.40 C ATOM 924 C THR A 207 122.793 219.475 845.736 1.00 15.55 C ATOM 925 O THR A 207 122.289 218.356 845.674 1.00 12.21 O ATOM 926 CB THR A 207 125.028 219.954 844.649 1.00 14.06 C ATOM 927 OG1 THR A 207 125.656 220.441 843.446 1.00 14.51 O ATOM 928 CG2 THR A 207 125.432 218.517 844.892 1.00 13.59 C ATOM 929 N PHE A 208 122.767 220.200 846.853 1.00 14.30 N ATOM 930 CA PHE A 208 122.081 219.674 848.040 1.00 14.01 C ATOM 931 C PHE A 208 120.606 219.453 847.710 1.00 13.40 C ATOM 932 O PHE A 208 120.023 218.442 848.090 1.00 14.03 O ATOM 933 CB PHE A 208 122.208 220.642 849.233 1.00 13.17 C ATOM 934 CG PHE A 208 123.418 220.382 850.088 1.00 15.49 C ATOM 935 CD1 PHE A 208 124.701 220.600 849.583 1.00 14.35 C ATOM 936 CE1 PHE A 208 125.837 220.336 850.363 1.00 16.94 C ATOM 937 CZ PHE A 208 125.691 219.848 851.666 1.00 16.50 C ATOM 938 CE2 PHE A 208 124.422 219.624 852.180 1.00 15.81 C ATOM 939 CD2 PHE A 208 123.285 219.894 851.390 1.00 16.58 C ATOM 940 N GLN A 209 120.008 220.391 846.985 1.00 15.02 N ATOM 941 CA GLN A 209 118.597 220.265 846.637 1.00 16.77 C ATOM 942 C GLN A 209 118.353 219.045 845.753 1.00 15.94 C ATOM 943 O GLN A 209 117.390 218.311 845.946 1.00 15.34 O ATOM 944 CB GLN A 209 118.116 221.542 845.939 1.00 17.66 C ATOM 945 CG GLN A 209 116.735 221.453 845.326 1.00 25.83 C ATOM 946 CD GLN A 209 116.256 222.807 844.835 1.00 28.57 C ATOM 947 OE1 GLN A 209 116.949 223.470 844.088 1.00 31.24 O ATOM 948 NE2 GLN A 209 115.065 223.215 845.260 1.00 34.54 N ATOM 949 N ALA A 210 119.241 218.828 844.785 1.00 15.12 N ATOM 950 CA ALA A 210 119.132 217.688 843.879 1.00 14.31 C ATOM 951 C ALA A 210 119.103 216.358 844.633 1.00 14.32 C ATOM 952 O ALA A 210 118.259 215.503 844.359 1.00 12.87 O ATOM 953 CB ALA A 210 120.331 217.682 842.898 1.00 13.96 C ATOM 954 N ILE A 211 120.050 216.175 845.553 1.00 12.44 N ATOM 955 CA ILE A 211 120.144 214.939 846.314 1.00 11.93 C ATOM 956 C ILE A 211 118.899 214.784 847.207 1.00 11.37 C ATOM 957 O ILE A 211 118.341 213.697 847.314 1.00 13.78 O ATOM 958 CB ILE A 211 121.442 214.915 847.180 1.00 12.94 C ATOM 959 CG1 ILE A 211 122.678 215.077 846.272 1.00 15.61 C ATOM 960 CD1 ILE A 211 122.814 213.953 845.219 1.00 17.02 C ATOM 961 CG2 ILE A 211 121.551 213.591 847.939 1.00 16.55 C ATOM 962 N ARG A 212 118.469 215.871 847.833 1.00 12.28 N ATOM 963 CA ARG A 212 117.274 215.833 848.691 1.00 12.89 C ATOM 964 C ARG A 212 116.032 215.372 847.925 1.00 12.87 C ATOM 965 O ARG A 212 115.294 214.490 848.371 1.00 13.35 O ATOM 966 CB ARG A 212 117.009 217.224 849.270 1.00 14.91 C ATOM 967 CG ARG A 212 115.917 217.254 850.326 1.00 16.89 C ATOM 968 CD ARG A 212 115.451 218.685 850.497 1.00 17.88 C ATOM 969 NE ARG A 212 114.410 218.990 849.527 1.00 20.95 N ATOM 970 CZ ARG A 212 114.286 220.138 848.872 1.00 21.72 C ATOM 971 NH1 ARG A 212 115.158 221.125 849.052 1.00 19.72 N ATOM 972 NH2 ARG A 212 113.246 220.311 848.064 1.00 24.95 N ATOM 973 N ILE A 213 115.801 215.975 846.763 1.00 13.16 N ATOM 974 CA ILE A 213 114.650 215.631 845.945 1.00 13.52 C ATOM 975 C ILE A 213 114.699 214.140 845.569 1.00 13.97 C ATOM 976 O ILE A 213 113.693 213.422 845.636 1.00 15.18 O ATOM 977 CB ILE A 213 114.613 216.565 844.671 1.00 13.47 C ATOM 978 CG1 ILE A 213 114.247 217.994 845.100 1.00 14.52 C ATOM 979 CD1 ILE A 213 114.332 219.040 843.970 1.00 16.82 C ATOM 980 CG2 ILE A 213 113.616 216.040 843.624 1.00 16.30 C ATOM 981 N TYR A 214 115.884 213.661 845.191 1.00 13.02 N ATOM 982 CA TYR A 214 116.039 212.267 844.817 1.00 12.37 C ATOM 983 C TYR A 214 115.745 211.328 845.985 1.00 13.97 C ATOM 984 O TYR A 214 114.995 210.356 845.855 1.00 15.11 O ATOM 985 CB TYR A 214 117.462 212.011 844.324 1.00 15.66 C ATOM 986 CG TYR A 214 117.685 210.585 843.927 1.00 16.66 C ATOM 987 CD1 TYR A 214 117.255 210.109 842.680 1.00 19.44 C ATOM 988 CE1 TYR A 214 117.442 208.773 842.323 1.00 18.90 C ATOM 989 CZ TYR A 214 118.050 207.904 843.219 1.00 21.35 C ATOM 990 OH TYR A 214 118.246 206.588 842.873 1.00 22.80 O ATOM 991 CE2 TYR A 214 118.472 208.349 844.461 1.00 21.26 C ATOM 992 CD2 TYR A 214 118.295 209.691 844.805 1.00 20.00 C ATOM 993 N VAL A 215 116.355 211.621 847.122 1.00 13.04 N ATOM 994 CA VAL A 215 116.185 210.807 848.330 1.00 13.22 C ATOM 995 C VAL A 215 114.722 210.740 848.756 1.00 13.77 C ATOM 996 O VAL A 215 114.236 209.695 849.188 1.00 13.29 O ATOM 997 CB VAL A 215 117.032 211.393 849.506 1.00 14.14 C ATOM 998 CG1 VAL A 215 116.617 210.754 850.856 1.00 15.39 C ATOM 999 CG2 VAL A 215 118.534 211.096 849.264 1.00 13.95 C ATOM 1000 N ASN A 216 114.015 211.848 848.599 1.00 14.32 N ATOM 1001 CA ASN A 216 112.622 211.904 849.037 1.00 15.40 C ATOM 1002 C ASN A 216 111.570 211.770 847.952 1.00 17.23 C ATOM 1003 O ASN A 216 110.369 211.956 848.220 1.00 15.57 O ATOM 1004 CB ASN A 216 112.431 213.191 849.845 1.00 14.90 C ATOM 1005 CG ASN A 216 113.265 213.181 851.109 1.00 16.94 C ATOM 1006 OD1 ASN A 216 112.940 212.479 852.076 1.00 15.03 O ATOM 1007 ND2 ASN A 216 114.375 213.921 851.100 1.00 14.16 N CONECT 47 46 48 53 CONECT 45 39 46 CONECT 259 258 260 265 CONECT 257 251 258 CONECT 278 277 279 284 CONECT 276 267 277 END