REMARK File generated by pHLA3D REMARK http://www.phla3d.com.br HEADER IMMUNE SYSTEM/PEPTIDE 22-MAR-06 2CIK TITLE INSIGHTS INTO CROSSREACTIVITY IN HUMAN ALLORECOGNITION: THE TITLE 2 STRUCTURE OF HLA-B35011 PRESENTING AN EPITOPE DERIVED FROM TITLE 3 CYTOCHROME P450. COMPND MOL_ID: 1; COMPND 2 MOLECULE: HLA CLASS I HISTOCOMPATIBILITY ANTIGEN B-35 COMPND 3 ALPHA CHAIN; COMPND 4 CHAIN: A; COMPND 5 FRAGMENT: RESIDUES 25-300; COMPND 6 SYNONYM: HLA-B3501, MHC CLASS I ANTIGEN B*35, HLA CLASS I COMPND 7 HISTOCOMPATIBILITY ANTIGEN B3501 HEAVY CHAIN, B350101, COMPND 8 B35011, B35, B35, B3501; COMPND 9 ENGINEERED: YES; COMPND 10 MOL_ID: 2; COMPND 11 MOLECULE: BETA-2-MICROGLOBULIN; COMPND 12 CHAIN: B; COMPND 13 SYNONYM: B2M; COMPND 14 ENGINEERED: YES; COMPND 15 MOL_ID: 3; COMPND 16 MOLECULE: PEPTIDE; COMPND 17 CHAIN: C SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606; SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL-21; SOURCE 8 EXPRESSION_SYSTEM_VARIANT: (DE3)PLYSS; SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PGM-T7; SOURCE 10 MOL_ID: 2; SOURCE 11 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 12 ORGANISM_COMMON: HUMAN; SOURCE 13 ORGANISM_TAXID: 9606; SOURCE 14 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 15 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 16 EXPRESSION_SYSTEM_STRAIN: BL-21; SOURCE 17 EXPRESSION_SYSTEM_VARIANT: (DE3)PLYSS; SOURCE 18 EXPRESSION_SYSTEM_PLASMID: PGM-T7; SOURCE 19 MOL_ID: 3; SOURCE 20 SYNTHETIC: YES; SOURCE 21 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 22 ORGANISM_COMMON: HUMAN; SOURCE 23 ORGANISM_TAXID: 9606; SOURCE 24 OTHER_DETAILS: PEPTIDE EPITOPE FROM HUMAN CYTOCHROME P450 SOURCE 25 ISOFORMS IIC8, IIC9, IIC10 AND IIC18 KEYWDS IMMUNE SYSTEM/PEPTIDE, ANTIGEN/PEPTIDE COMPLEX, MAJOR KEYWDS 2 HISTOCOMPATIBILITY ANTIGEN, HUMAN, MHC, HLA, HLA-B3501, KEYWDS 3 EBV, ALLO-LIGAND, GLYCOPROTEIN, IMMUNE RESPONSE, MEMBRANE, KEYWDS 4 MHC I, POLYMORPHISM, TRANSMEMBRANE, IMMUNOGLOBULIN DOMAIN, KEYWDS 5 PYRROLIDONE CARBOXYLIC ACID EXPDTA X-RAY DIFFRACTION AUTHOR C.S.HOURIGAN,M.HARKIOLAKI,N.A.PETERSON,J.I.BELL,E.Y.JONES, AUTHOR 2 C.A.O'CALLAGHAN REVDAT 4 24-FEB-09 2CIK 1 VERSN REVDAT 3 20-DEC-06 2CIK 1 JRNL REVDAT 2 22-NOV-06 2CIK 1 JRNL REVDAT 1 25-OCT-06 2CIK 0 REMARK 2 REMARK 2 RESOLUTION. 1.75 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC 5.2.0019 REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON REMARK 3 REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.75 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.62 REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL REMARK 3 COMPLETENESS FOR RANGE (%) : 97.0 REMARK 3 NUMBER OF REFLECTIONS : 44265 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM REMARK 3 R VALUE (WORKING + TEST SET) : 0.198 REMARK 3 R VALUE (WORKING SET) : 0.197 REMARK 3 FREE R VALUE : 0.227 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.000 REMARK 3 FREE R VALUE TEST SET COUNT : 1852 REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : 20 REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.75 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.80 REMARK 3 REFLECTION IN BIN (WORKING SET) : 2954 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL REMARK 3 BIN R VALUE (WORKING SET) : 0.2250 REMARK 3 BIN FREE R VALUE SET COUNT : 123 REMARK 3 BIN FREE R VALUE : 0.2440 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 3156 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 18 REMARK 3 SOLVENT ATOMS : 325 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 15.58 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : -0.73000 REMARK 3 B22 (A**2) : -0.27000 REMARK 3 B33 (A**2) : 1.00000 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 OVERALL COORDINATE ERROR. REMARK 3 ESU BASED ON R VALUE (A): 0.120 REMARK 3 ESU BASED ON FREE R VALUE (A): 0.114 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.074 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.236 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.945 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.937 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3265 ; 0.011 ; 0.021 REMARK 3 BOND LENGTHS OTHERS (A): 2272 ; 0.002 ; 0.020 REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4434 ; 1.272 ; 1.940 REMARK 3 BOND ANGLES OTHERS (DEGREES): 5456 ; 0.866 ; 3.002 REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 381 ; 6.010 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 176 ;32.238 ;23.182 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 525 ;12.737 ;15.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 31 ;17.799 ;15.000 REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 451 ; 0.082 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3651 ; 0.005 ; 0.020 REMARK 3 GENERAL PLANES OTHERS (A): 709 ; 0.001 ; 0.020 REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 528 ; 0.213 ; 0.200 REMARK 3 NON-BONDED CONTACTS OTHERS (A): 2330 ; 0.205 ; 0.200 REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 1510 ; 0.178 ; 0.200 REMARK 3 NON-BONDED TORSION OTHERS (A): 1717 ; 0.082 ; 0.200 REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 227 ; 0.129 ; 0.200 REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 4 ; 0.096 ; 0.200 REMARK 3 SYMMETRY VDW OTHERS (A): 38 ; 0.282 ; 0.200 REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 9 ; 0.130 ; 0.200 REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL REMARK 3 REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 2484 ; 1.184 ; 1.500 REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3107 ; 1.269 ; 2.000 REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1611 ; 2.134 ; 3.000 REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1327 ; 3.045 ; 4.500 REMARK 3 REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 REMARK 3 NCS RESTRAINTS STATISTICS REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : NULL REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : MASK REMARK 3 PARAMETERS FOR MASK CALCULATION REMARK 3 VDW PROBE RADIUS : 1.20 REMARK 3 ION PROBE RADIUS : 0.80 REMARK 3 SHRINKAGE RADIUS : 0.80 REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE REMARK 3 RIDING POSITIONS. REMARK 4 REMARK 4 2CIK COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 22-MAR-06. REMARK 100 THE PDBE ID CODE IS EBI-28198. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 30-MAY-01 REMARK 200 TEMPERATURE (KELVIN) : 100.0 REMARK 200 PH : 5.60 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : ESRF REMARK 200 BEAMLINE : ID14-3 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.93 REMARK 200 MONOCHROMATOR : DIAMOND REMARK 200 OPTICS : MIRRORS 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 : 47620 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.750 REMARK 200 RESOLUTION RANGE LOW (A) : 20.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0 REMARK 200 DATA REDUNDANCY : 7.800 REMARK 200 R MERGE (I) : 0.07000 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 23.9000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.75 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.81 REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0 REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : 0.58000 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 4.000 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: AMORE REMARK 200 STARTING MODEL: PDB ENTRY 1A1N REMARK 200 REMARK 200 REMARK: MODEL 1A1N WITH CHAIN C AND WATERS REMOVED. REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 53 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.6 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.105M AMMONIUM ACETATE, REMARK 280 0.0525M TRI-SODIUM CITRATE DIHYDRATE PH 5.6 AND 15.75% W/V REMARK 280 PEG 4000 REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21 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 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 25.66000 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 54.92500 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 41.12500 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 54.92500 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 25.66000 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 41.12500 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 GENERATING THE BIOMOLECULE 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: TRIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC REMARK 350 SOFTWARE USED: PQS REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C 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 400 REMARK 400 COMPOUND REMARK 400 INVOLVED IN THE PRESENTATION OF FOREIGN ANTIGENS TO THE REMARK 400 IMMUNE SYSTEM REMARK 400 BETA-2-MICROGLOBULIN IS THE BETA-CHAIN OF MAJOR REMARK 400 HISTOCOMPATIBILITY COMPLEX CLASS I MOLECULES 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 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 ARG A 14 67.84 -160.54 REMARK 500 ASP A 29 -129.17 51.96 REMARK 500 GLN A 224 52.28 -106.76 REMARK 500 ARG A 239 -22.65 89.81 REMARK 500 TRP B 60 -5.18 75.10 REMARK 500 REMARK 500 REMARK: NULL REMARK 525 REMARK 525 SOLVENT REMARK 525 REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER; REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE REMARK 525 NUMBER; I=INSERTION CODE): REMARK 700 REMARK 700 SHEET REMARK 700 THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN REMARK 700 ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW, REMARK 700 TWO SHEETS ARE DEFINED. REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A1277 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B1100 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B1101 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1A1M RELATED DB: PDB REMARK 900 MHC CLASS I MOLECULE B*5301 COMPLEXED WITH REMARK 900 PEPTIDETYPDINQML FROM GAG PROTEIN OF HIV2 REMARK 900 RELATED ID: 1A1N RELATED DB: PDB REMARK 900 MHC CLASS I MOLECULE B*3501 COMPLEXED WITH REMARK 900 PEPTIDE VPLRPMTYFROM THE NEF PROTEIN (75- REMARK 900 82) OF HIV1 REMARK 900 RELATED ID: 1A1O RELATED DB: PDB REMARK 900 MHC CLASS I MOLECULE B5301 COMPLEXED WITH REMARK 900 PEPTIDE LS6 (KPIVQYDNF) FROM THE MALARIA REMARK 900 PARASITE P. FALCIPARUM REMARK 900 RELATED ID: 1A6Z RELATED DB: PDB REMARK 900 HFE (HUMAN) HEMOCHROMATOSIS PROTEIN REMARK 900 RELATED ID: 1A9B RELATED DB: PDB REMARK 900 DECAMER-LIKE CONFORMATION OF A NANO-PEPTIDE REMARK 900 BOUND TO HLA-B 3501 DUE TO NONSTANDARD REMARK 900 POSITIONING OF THE C-TERMINUS REMARK 900 RELATED ID: 1A9E RELATED DB: PDB REMARK 900 DECAMER-LIKE CONFORMATION OF A NANO-PEPTIDE REMARK 900 BOUND TO HLA-B 3501 DUE TO NONSTANDARD REMARK 900 POSITIONING OF THE C-TERMINUS REMARK 900 RELATED ID: 1AGB RELATED DB: PDB REMARK 900 ANTAGONIST HIV-1 GAG PEPTIDES INDUCE REMARK 900 STRUCTURAL CHANGES IN HLA B8 - HIV-1 GAG REMARK 900 PEPTIDE (GGRKKYKL - 3R MUTATION) REMARK 900 RELATED ID: 1AGC RELATED DB: PDB REMARK 900 ANTAGONIST HIV-1 GAG PEPTIDES INDUCE REMARK 900 STRUCTURAL CHANGES IN HLA B8 - HIV-1 GAG REMARK 900 PEPTIDE (GGKKKYQL - 7Q MUTATION) REMARK 900 RELATED ID: 1AGD RELATED DB: PDB REMARK 900 ANTAGONIST HIV-1 GAG PEPTIDES INDUCE REMARK 900 STRUCTURAL CHANGES IN HLA B8 - HIV-1 GAG REMARK 900 PEPTIDE (GGKKKYKL - INDEX PEPTIDE) REMARK 900 RELATED ID: 1AGE RELATED DB: PDB REMARK 900 ANTAGONIST HIV-1 GAG PEPTIDES INDUCE REMARK 900 STRUCTURAL CHANGES IN HLA B8 - HIV-1 GAG REMARK 900 PEPTIDE (GGKKKYRL - 7R MUTATION) REMARK 900 RELATED ID: 1AGF RELATED DB: PDB REMARK 900 ANTAGONIST HIV-1 GAG PEPTIDES INDUCE REMARK 900 STRUCTURAL CHANGES IN HLA B8 - HIV-1 GAG REMARK 900 PEPTIDE (GGKKRYKL - 5R MUTATION) REMARK 900 RELATED ID: 1AKJ RELATED DB: PDB REMARK 900 COMPLEX OF THE HUMAN MHC CLASS I REMARK 900 GLYCOPROTEIN HLA-A2 ANDTHE T CELL CORECEPTOR REMARK 900 CD8 REMARK 900 RELATED ID: 1AO7 RELATED DB: PDB REMARK 900 COMPLEX BETWEEN HUMAN T-CELL RECEPTOR, VIRAL REMARK 900 PEPTIDE (TAX), AND HLA-A 0201 REMARK 900 RELATED ID: 1B0G RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF HUMAN CLASS I MHC ( REMARK 900 HLA-A2.1) COMPLEXED WITH BETA 2- REMARK 900 MICROGLOBULIN AND HUMAN PEPTIDE P1049 REMARK 900 RELATED ID: 1B0R RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF HLA-A0201 COMPLEXED REMARK 900 WITH A PEPTIDE WITH THE CARBOXYL-TERMINAL REMARK 900 GROUP SUBSTITUTED BY A METHYL GROUP REMARK 900 RELATED ID: 1BD2 RELATED DB: PDB REMARK 900 COMPLEX BETWEEN HUMAN T-CELL RECEPTOR B7, REMARK 900 VIRAL PEPTIDE (TAX) AND MHC CLASS I REMARK 900 MOLECULE HLA-A 0201 REMARK 900 RELATED ID: 1C16 RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE ANALYSIS OF THE GAMMA/ REMARK 900 DELTA T CELL LIGAND T22 REMARK 900 RELATED ID: 1CE6 RELATED DB: PDB REMARK 900 MHC CLASS I H-2DB COMPLEXED WITH A REMARK 900 SENDAI VIRUSNUCLEOPROTEIN PEPTIDE REMARK 900 RELATED ID: 1CG9 RELATED DB: PDB REMARK 900 COMPLEX RECOGNITION OF THE SUPERTYPIC BW6- REMARK 900 DETERMINANT ONHLA-B AND-C MOLECULES BY THE REMARK 900 MONOCLONAL ANTIBODY SFR8-B6 REMARK 900 RELATED ID: 1DE4 RELATED DB: PDB REMARK 900 HEMOCHROMATOSIS PROTEIN HFE COMPLEXED WITH REMARK 900 TRANSFERRINRECEPTOR REMARK 900 RELATED ID: 1DUY RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF HLA-A0201/OCTAMERIC TAX REMARK 900 PEPTIDE COMPLEX REMARK 900 RELATED ID: 1DUZ RELATED DB: PDB REMARK 900 HUMAN CLASS I HISTOCOMPATIBILITY ANTIGEN (HLA REMARK 900 -A 0201) INCOMPLEX WITH A NONAMERIC PEPTIDE REMARK 900 FROM HTLV-1 TAX PROTEIN REMARK 900 RELATED ID: 1E27 RELATED DB: PDB REMARK 900 NONSTANDARD PEPTIDE BINDING OF HLA-B*5101 REMARK 900 COMPLEXED WITH HIV IMMUNODOMINANT EPITOPE KM1 REMARK 900 (LPPVVAKEI) REMARK 900 RELATED ID: 1E28 RELATED DB: PDB REMARK 900 NONSTANDARD PEPTIDE BINDING OF HLA-B*5101 REMARK 900 COMPLEXED WITH HIV IMMUNODOMINANT EPITOPE KM2 REMARK 900 (TAFTIPSI) REMARK 900 RELATED ID: 1EEY RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE DETERMINATION OF HLA A2 REMARK 900 COMPLEXED TOPEPTIDE GP2 WITH THE SUBSTITUTION REMARK 900 (I2L/V5L/L9V) REMARK 900 RELATED ID: 1EEZ RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE DETERMINATION OF HLA-A2.1 REMARK 900 COMPLEXED TOGP2 PEPTIDE VARIANT(I2L/V5L) REMARK 900 RELATED ID: 1EFX RELATED DB: PDB REMARK 900 STRUCTURE OF A COMPLEX BETWEEN THE HUMAN REMARK 900 NATURAL KILLER CELL RECEPTOR KIR2DL2 AND A REMARK 900 CLASS I MHC LIGAND HLA-CW3 REMARK 900 RELATED ID: 1EXU RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF THE HUMAN MHC-RELATED REMARK 900 FC RECEPTOR REMARK 900 RELATED ID: 1GZP RELATED DB: PDB REMARK 900 CD1B IN COMPLEX WITH GM2 GANGLIOSIDE REMARK 900 RELATED ID: 1GZQ RELATED DB: PDB REMARK 900 CD1B IN COMPLEX WITH PHOPHATIDYLINOSITOL REMARK 900 RELATED ID: 1HHG RELATED DB: PDB REMARK 900 REMARK 900 RELATED ID: 1HHH RELATED DB: PDB REMARK 900 REMARK 900 RELATED ID: 1HHI RELATED DB: PDB REMARK 900 REMARK 900 RELATED ID: 1HHJ RELATED DB: PDB REMARK 900 HUMAN CLASS I HISTOCOMPATIBILITY ANTIGEN (HLA REMARK 900 -A 0201) COMPLEX WITH A NONAMERIC PEPTIDE REMARK 900 FROM HIV-1 REVERSE TRANSCRIPTASE (RESIDUES REMARK 900 309-317) REMARK 900 RELATED ID: 1HHK RELATED DB: PDB REMARK 900 REMARK 900 RELATED ID: 1HLA RELATED DB: PDB REMARK 900 HUMAN CLASS I HISTOCOMPATIBILITY ANTIGEN A2 ( REMARK 900 HLA-A2, HUMAN LEUCOCYTE ANTIGEN) REMARK 900 RELATED ID: 1HSA RELATED DB: PDB REMARK 900 HUMAN CLASS I HISTOCOMPATIBILITY ANTIGEN HLA- REMARK 900 B(ASTERISK)2705 REMARK 900 RELATED ID: 1HSB RELATED DB: PDB REMARK 900 CLASS I HISTOCOMPATIBILITY ANTIGEN AW68.1 ( REMARK 900 LEUCOCYTE ANTIGEN) REMARK 900 RELATED ID: 1I1F RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF HUMAN CLASS I MHC ( REMARK 900 HLA-A2.1) COMPLEXED WITH BETA 2- REMARK 900 MICROGLOBULIN AND HIV-RT VARIANT PEPTIDE I1Y REMARK 900 RELATED ID: 1I1Y RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF HUMAN CLASS I MHC ( REMARK 900 HLA-A2.1) COMPLEXED WITH BETA 2- REMARK 900 MICROGLOBULIN AND HIV-RT VARIANT PEPTIDE I1Y REMARK 900 RELATED ID: 1I4F RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF HLA-A*0201/MAGE-A4- REMARK 900 PEPTIDE COMPLEX REMARK 900 RELATED ID: 1I7R RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF CLASS I MHC A2 IN REMARK 900 COMPLEX WITH PEPTIDEP1058 REMARK 900 RELATED ID: 1I7T RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF CLASS I MHC A2 IN REMARK 900 COMPLEX WITH PEPTIDEP1049-5V REMARK 900 RELATED ID: 1I7U RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF CLASS I MHC A2 IN REMARK 900 COMPLEX WITH PEPTIDEP1049-6V REMARK 900 RELATED ID: 1IM3 RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF THE HUMAN CYTOMEGALOVIRUS REMARK 900 PROTEIN US2BOUND TO THE MHC CLASS I REMARK 900 MOLECULE HLA-A2/TAX REMARK 900 RELATED ID: 1IM9 RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF THE HUMAN NATURAL REMARK 900 KILLER CELLINHIBITORY RECEPTOR KIR2DL1 BOUND REMARK 900 TO ITS MHC LIGAND HLA-CW4 REMARK 900 RELATED ID: 1JF1 RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF HLA-A2*0201 IN REMARK 900 COMPLEX WITH ADECAMERIC ALTERED PEPTIDE LIGAND REMARK 900 FROM THE MART-1/MELAN-A REMARK 900 RELATED ID: 1JGD RELATED DB: PDB REMARK 900 HLA-B*2709 BOUND TO DECA-PEPTIDE S10R REMARK 900 RELATED ID: 1JGE RELATED DB: PDB REMARK 900 HLA-B*2705 BOUND TO NONA-PEPTIDE M9 REMARK 900 RELATED ID: 1JHT RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF HLA-A2*0201 IN REMARK 900 COMPLEX WITH ANONAMERIC ALTERED PEPTIDE LIGAND REMARK 900 (ALGIGILTV) FROM THE MART-1/MELAN-A. REMARK 900 RELATED ID: 1JNJ RELATED DB: PDB REMARK 900 NMR SOLUTION STRUCTURE OF THE HUMAN BETA2- REMARK 900 MICROGLOBULIN REMARK 900 RELATED ID: 1K5N RELATED DB: PDB REMARK 900 HLA-B*2709 BOUND TO NONA-PEPTIDE M9 REMARK 900 RELATED ID: 1KPR RELATED DB: PDB REMARK 900 THE HUMAN NON-CLASSICAL MAJOR REMARK 900 HISTOCOMPATIBILITY COMPLEXMOLECULE HLA-E REMARK 900 RELATED ID: 1KTL RELATED DB: PDB REMARK 900 THE HUMAN NON-CLASSICAL MAJOR REMARK 900 HISTOCOMPATIBILITY COMPLEXMOLECULE HLA-E REMARK 900 RELATED ID: 1LDS RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF MONOMERIC HUMAN BETA-2 REMARK 900 -MICROGLOBULIN REMARK 900 RELATED ID: 1LP9 RELATED DB: PDB REMARK 900 XENOREACTIVE COMPLEX AHIII 12.2 TCR BOUND REMARK 900 TO P1049/HLA-A2.1 REMARK 900 RELATED ID: 1M05 RELATED DB: PDB REMARK 900 HLA B8 IN COMPLEX WITH AN EPSTEIN BARR REMARK 900 VIRUS DETERMINANT REMARK 900 RELATED ID: 1M6O RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF HLA B*4402 IN COMPLEX REMARK 900 WITH HLADPA*0201 PEPTIDE REMARK 900 RELATED ID: 1MHE RELATED DB: PDB REMARK 900 THE HUMAN NON-CLASSICAL MAJOR REMARK 900 HISTOCOMPATIBILITY COMPLEX MOLECULE HLA-E REMARK 900 RELATED ID: 1MI5 RELATED DB: PDB REMARK 900 THE CRYSTAL STRUCTURE OF LC13 TCR IN REMARK 900 COMPLEX WITH HLAB8-EBVPEPTIDE COMPLEX REMARK 900 RELATED ID: 1N2R RELATED DB: PDB REMARK 900 A NATURAL SELECTED DIMORPHISM IN HLA B*44 REMARK 900 ALTERS SELF,PEPTIDE REPORTOIRE AND T CELL REMARK 900 RECOGNITION. REMARK 900 RELATED ID: 1OF2 RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF HLA-B*2709 COMPLEXED REMARK 900 WITH THE VASOACTIVE INTESTINAL PEPTIDE TYPE REMARK 900 1 RECEPTOR (VPAC1) PEPTIDE (RESIDUES 400-408 REMARK 900 ) REMARK 900 RELATED ID: 1OGA RELATED DB: PDB REMARK 900 A STRUCTURAL BASIS FOR IMMUNODOMINANT HUMAN REMARK 900 T-CELL RECEPTOR RECOGNITION. REMARK 900 RELATED ID: 1OGT RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF HLA-B*2709 COMPLEXED REMARK 900 WITH THE VASOACTIVE INTESTINAL PEPTIDE TYPE REMARK 900 1 RECEPTOR (VPAC1) PEPTIDE (RESIDUES 400-408 REMARK 900 ) REMARK 900 RELATED ID: 1ONQ RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF CD1A IN COMPLEX WITH REMARK 900 A SULFATIDE REMARK 900 RELATED ID: 1P7Q RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF HLA-A2 BOUND TO LIR- REMARK 900 1, A HOST ANDVIRAL MHC RECEPTOR REMARK 900 RELATED ID: 1PY4 RELATED DB: PDB REMARK 900 BETA2 MICROGLOBULIN MUTANT H31Y DISPLAYS HINTS REMARK 900 FOR AMYLOIDFORMATIONS REMARK 900 RELATED ID: 1Q94 RELATED DB: PDB REMARK 900 STRUCTURES OF HLA-A*1101 IN COMPLEX WITH REMARK 900 IMMUNODOMINANTNONAMER AND DECAMER HIV-1 REMARK 900 EPITOPES CLEARLY REVEAL THEPRESENCE OF A REMARK 900 MIDDLE ANCHOR RESIDUE REMARK 900 RELATED ID: 1QEW RELATED DB: PDB REMARK 900 HUMAN CLASS I HISTOCOMPATIBILITY ANTIGEN (HLA REMARK 900 -A 0201)COMPLEX WITH A NONAMERIC PEPTIDE REMARK 900 FROM MELANOMA-ASSOCIATEDANTIGEN 3 (RESIDUES REMARK 900 271-279) REMARK 900 RELATED ID: 1QLF RELATED DB: PDB REMARK 900 MHC CLASS I H-2DB COMPLEXED WITH REMARK 900 GLYCOPEPTIDE K3G REMARK 900 RELATED ID: 1QQD RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF HLA-CW4, A LIGAND FOR REMARK 900 THE KIR2D NATURAL KILLER CELL INHIBITORY REMARK 900 RECEPTOR REMARK 900 RELATED ID: 1QR1 RELATED DB: PDB REMARK 900 POOR BINDING OF A HER-2/NEU EPITOPE (GP2 REMARK 900 ) TO HLA-A2.1 IS DUE TO A LACK OF REMARK 900 INTERACTIONS IN THE CENTER OF THE PEPTIDE REMARK 900 RELATED ID: 1QRN RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF HUMAN A6 TCR COMPLEXED REMARK 900 WITH HLA-A2 BOUND TO ALTERED HTLV-1 REMARK 900 TAX PEPTIDE P6A REMARK 900 RELATED ID: 1QSE RELATED DB: PDB REMARK 900 STRUCTURE OF HUMAN A6-TCR BOUND TO HLA- REMARK 900 A2 COMPLEXED WITH ALTERED HTLV-1 TAX REMARK 900 PEPTIDE V7R REMARK 900 RELATED ID: 1QSF RELATED DB: PDB REMARK 900 STRUCTURE OF A6-TCR BOUND TO HLA-A2 REMARK 900 COMPLEXED WITH ALTERED HTLV-1 TAX PEPTIDE REMARK 900 Y8A REMARK 900 RELATED ID: 1QVO RELATED DB: PDB REMARK 900 STRUCTURES OF HLA-A*1101 IN COMPLEX WITH REMARK 900 IMMUNODOMINANTNONAMER AND DECAMER HIV-1 REMARK 900 EPITOPES CLEARLY REVEAL THEPRESENCE OF A REMARK 900 MIDDLE ANCHOR RESIDUE REMARK 900 RELATED ID: 1R3H RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF T10 REMARK 900 RELATED ID: 1S9W RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE ANALYSIS OF NY-ESO-1 REMARK 900 EPITOPE, SLLMWITQC,IN COMPLEX WITH HLA-A2 REMARK 900 RELATED ID: 1S9X RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE ANALYSIS OF NY-ESO-1 REMARK 900 EPITOPE ANALOGUE,SLLMWITQA, IN COMPLEX WITH REMARK 900 HLA-A2 REMARK 900 RELATED ID: 1S9Y RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE ANALYSIS OF NY-ESO-1 REMARK 900 EPITOPE ANALOGUE,SLLMWITQS, IN COMPLEX WITH REMARK 900 HLA-A2 REMARK 900 RELATED ID: 1SYS RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF HLA, B*4403, AND REMARK 900 PEPTIDE EEPTVIKKY REMARK 900 RELATED ID: 1SYV RELATED DB: PDB REMARK 900 HLA-B*4405 COMPLEXED TO THE DOMINANT SELF REMARK 900 LIGAND EEFGRAYGF REMARK 900 RELATED ID: 1TMC RELATED DB: PDB REMARK 900 TRUNCATED HUMAN CLASS I HISTOCOMPATIBILITY REMARK 900 ANTIGEN HLA-AW68 COMPLEXED WITH A DECAMERIC REMARK 900 PEPTIDE (EVAPPEYHRK) REMARK 900 RELATED ID: 1TVB RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF MELANOMA ANTIGEN GP100( REMARK 900 209-217) BOUNDTO HUMAN CLASS I MHC HLA- REMARK 900 A2 REMARK 900 RELATED ID: 1TVH RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF MODIFIED MELANOMA ANTIGEN REMARK 900 GP100(209-T2M) BOUND TO HUMAN CLASS I REMARK 900 MHC HLA-A2 REMARK 900 RELATED ID: 1UQS RELATED DB: PDB REMARK 900 THE CRYSTAL STRUCTURE OF HUMAN CD1B WITH A REMARK 900 BOUND BACTERIAL GLYCOLIPID REMARK 900 RELATED ID: 1UR7 RELATED DB: PDB REMARK 900 MOLECULAR REFINEMENT OF ANTI-HLA-A2 USING REMARK 900 LIGHT CHAIN SHUFFLING: A STRUCTURAL MODEL REMARK 900 FOR HLA ANTIBODY BINDING REMARK 900 RELATED ID: 1UXS RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF HLA-B*2705 COMPLEXED REMARK 900 WITH THE LATENT MEMBRANE PROTEIN 2 PEPTIDE REMARK 900 (LMP2)OF EPSTEIN-BARR VIRUS REMARK 900 RELATED ID: 1UXW RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF HLA-B*2709 COMPLEXED REMARK 900 WITH THE LATENT MEMBRANE PROTEIN 2 PEPTIDE REMARK 900 (LMP2) OF EPSTEIN-BARR VIRUS REMARK 900 RELATED ID: 1VGK RELATED DB: PDB REMARK 900 THE CRYSTAL STRUCTURE OF CLASS I MAJOR REMARK 900 HISTOCOMPATIBILITYCOMPLEX, H-2KD AT 2.0 A REMARK 900 RESOLUTION REMARK 900 RELATED ID: 1W0V RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF HLA-B*2705 COMPLEXED REMARK 900 WITH THE SELF-PEPTIDE TIS FROM EGF- REMARK 900 RESPONSE FACTOR 1 REMARK 900 RELATED ID: 1W0W RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF HLA-B*2709 COMPLEXED REMARK 900 WITH THE SELF-PEPTIDE TIS FROM EGF- REMARK 900 RESPONSE FACTOR 1 REMARK 900 RELATED ID: 1W72 RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF HLA-A1:MAGE-A1 IN REMARK 900 COMPLEX WITH FAB-HYB3 REMARK 900 RELATED ID: 1X7Q RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF HLA-A*1101 WITH SARS REMARK 900 NUCLEOCAPSIDPEPTIDE REMARK 900 RELATED ID: 1XH3 RELATED DB: PDB REMARK 900 CONFORMATIONAL RESTRAINTS AND FLEXIBILITY OF REMARK 900 14-MERICPEPTIDES IN COMPLEX WITH HLA-B* REMARK 900 3501 REMARK 900 RELATED ID: 1XR8 RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURES OF HLA-B*1501 IN REMARK 900 COMPLEX WITH PEPTIDESFROM HUMAN UBCH6 AND REMARK 900 EPSTEIN-BARR VIRUS EBNA-3 REMARK 900 RELATED ID: 1XR9 RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURES OF HLA-B*1501 IN REMARK 900 COMPLEX WITH PEPTIDESFROM HUMAN UBCH6 AND REMARK 900 EPSTEIN-BARR VIRUS EBNA-3 REMARK 900 RELATED ID: 1XZ0 RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF CD1A IN COMPLEX WITH REMARK 900 A SYNTHETICMYCOBACTIN LIPOPEPTIDE REMARK 900 RELATED ID: 1YDP RELATED DB: PDB REMARK 900 1.9A CRYSTAL STRUCTURE OF HLA-G REMARK 900 RELATED ID: 1YPZ RELATED DB: PDB REMARK 900 IMMUNE RECEPTOR REMARK 900 RELATED ID: 1ZS8 RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF THE MURINE MHC CLASS REMARK 900 IB MOLECULE M10.5 REMARK 900 RELATED ID: 1ZSD RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF HLA-B*3501 PRESENTING REMARK 900 AN 11-MER EBVANTIGEN EPLPQGQLTAY REMARK 900 RELATED ID: 1ZT4 RELATED DB: PDB REMARK 900 THE CRYSTAL STRUCTURE OF HUMAN CD1D WITH REMARK 900 AND WITHOUT ALPHA-GALACTOSYLCERAMIDE REMARK 900 RELATED ID: 2A83 RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF HLA-B*2705 COMPLEXED REMARK 900 WITH THE GLUCAGONRECEPTOR (GR) PEPTIDE ( REMARK 900 RESIDUES 412-420) REMARK 900 RELATED ID: 2AK4 RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF SB27 TCR IN COMPLEX REMARK 900 WITH HLA-B*3508-13MER PEPTIDE REMARK 900 RELATED ID: 2AV7 RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF HTLV-1 TAX PEPTIDE REMARK 900 BOUND TO HUMANCLASS I MHC HLA-A2 WITH REMARK 900 THE K66A MUTATION IN THE HEAVYCHAIN. REMARK 900 RELATED ID: 2AXF RELATED DB: PDB REMARK 900 THE IMMUNOGENICITY OF A VIRAL CYTOTOXIC T REMARK 900 CELL EPITOPE ISCONTROLLED BY ITS MHC-BOUND REMARK 900 CONFORMATION REMARK 900 RELATED ID: 2AXG RELATED DB: PDB REMARK 900 THE IMMUNOGENICITY OF A VIRAL CYTOTOXIC T REMARK 900 CELL EPITOPE ISCONTROLLED BY ITS MHC-BOUND REMARK 900 CONFORMATION REMARK 900 RELATED ID: 2BCK RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF HLA-A*2402 COMPLEXED REMARK 900 WITH A TELOMERASEPEPTIDE REMARK 900 RELATED ID: 2BNQ RELATED DB: PDB REMARK 900 STRUCTURAL AND KINETIC BASIS FOR HIGHTENED REMARK 900 IMMUNOGENICITY OF T CELL VACCINES REMARK 900 RELATED ID: 2BNR RELATED DB: PDB REMARK 900 STRUCTURAL AND KINETIC BASIS FOR HIGHTENED REMARK 900 IMMUNOGENICITY OF T CELL VACCINES REMARK 900 RELATED ID: 2BSR RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURES AND KIR3DL1 RECOGNITION OF REMARK 900 THREE IMMUNODOMINANT VIRAL PEPTIDES COMPLEXED REMARK 900 TO HLA-B2705 REMARK 900 RELATED ID: 2BSS RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURES AND KIR3DL1 RECOGNITION OF REMARK 900 THREE IMMUNODOMINANT VIRAL PEPTIDES COMPLEXED REMARK 900 TO HLA-B2705 REMARK 900 RELATED ID: 2BST RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURES AND KIR3DL1 RECOGNITION OF REMARK 900 THREE IMMUNODOMINANT VIRAL PEPTIDES COMPLEXED REMARK 900 TO HLA-B2705 REMARK 900 RELATED ID: 2BSU RELATED DB: PDB REMARK 900 T CELL CROSS-REACTIVITY AND CONFORMATIONAL REMARK 900 CHANGES DURING TCR ENGAGEMENT REMARK 900 RELATED ID: 2BSV RELATED DB: PDB REMARK 900 T CELL CROSS-REACTIVITY AND CONFORMATIONAL REMARK 900 CHANGES DURING TCR ENGAGEMENT REMARK 900 RELATED ID: 2BVQ RELATED DB: PDB REMARK 900 STRUCTURES OF THREE HIV-1 HLA-B5703- REMARK 900 PEPTIDE COMPLEXES AND IDENTIFICATION OF REMARK 900 RELATED HLAS POTENTIALLY ASSOCIATED WITH LONG REMARK 900 -TERM NON-PROGRESSION REMARK 900 RELATED ID: 2C7U RELATED DB: PDB REMARK 900 CONFLICTING SELECTIVE FORCES AFFECT CD8 T- REMARK 900 CELL RECEPTOR CONTACT SITES IN AN HLA-A2 REMARK 900 IMMUNODOMINANT HIV EPITOPE. REMARK 900 RELATED ID: 2CLR RELATED DB: PDB REMARK 900 HUMAN CLASS I HISTOCOMPATIBILITY ANTIGEN (HLA REMARK 900 -A 0201) COMPLEXED WITH A DECAMERIC PEPTIDE REMARK 900 FROM CALRETICULIN REMARK 900 RELATED ID: 2D31 RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF DISULFIDE-LINKED HLA-G REMARK 900 DIMER REMARK 900 RELATED ID: 2F74 RELATED DB: PDB REMARK 900 MURINE MHC CLASS I H-2DB IN COMPLEX WITH REMARK 900 HUMAN B2-MICROGLOBULIN AND LCMV-DERIVED REMARK 900 IMMUNODMINANT PEPTIDE GP33 REMARK 900 RELATED ID: 2F8O RELATED DB: PDB REMARK 900 A NATIVE TO AMYLOIDOGENIC TRANSITION REGULATED REMARK 900 BY ABACKBONE TRIGGER REMARK 900 RELATED ID: 2HLA RELATED DB: PDB REMARK 900 HUMAN CLASS I HISTOCOMPATIBILITY ANTIGEN AW REMARK 900 68.1 (HLA-AW 68.1, HUMAN LEUCOCYTE REMARK 900 ANTIGEN) REMARK 900 RELATED ID: 3HLA RELATED DB: PDB REMARK 900 HUMAN CLASS I HISTOCOMPATIBILITY ANTIGEN A2. REMARK 900 1 (HLA-A2.1 HUMAN LEUCOCYTE ANTIGEN) DBREF 2CIK A 1 276 UNP P30685 1B35_HUMAN 25 300 DBREF 2CIK B 1 99 UNP P61769 B2MG_HUMAN 21 119 DBREF 2CIK C 1 9 PDB 2CIK 2CIK 1 9 CRYST1 51.320 82.250 109.850 90.00 90.00 90.00 P 21 21 21 4 ATOM 1 N GLY A 1 42.181 56.404 88.477 1.00 13.97 ATOM 2 CA GLY A 1 42.862 55.983 87.232 1.00 13.97 ATOM 3 C GLY A 1 44.066 56.828 86.978 1.00 13.97 ATOM 4 O GLY A 1 44.344 57.775 87.714 1.00 13.97 ATOM 5 N SER A 2 44.823 56.478 85.921 1.00 41.78 ATOM 6 CA SER A 2 46.028 57.169 85.565 1.00 41.78 ATOM 7 C SER A 2 45.716 58.567 85.114 1.00 41.78 ATOM 8 O SER A 2 46.299 59.525 85.618 1.00 41.78 ATOM 9 CB SER A 2 46.777 56.476 84.413 1.00 41.78 ATOM 10 OG SER A 2 47.962 57.191 84.095 1.00 41.78 ATOM 11 N HIS A 3 44.783 58.728 84.149 1.00 52.57 ATOM 12 CA HIS A 3 44.516 60.046 83.642 1.00 52.57 ATOM 13 C HIS A 3 43.068 60.177 83.291 1.00 52.57 ATOM 14 O HIS A 3 42.368 59.184 83.100 1.00 52.57 ATOM 15 CB HIS A 3 45.305 60.397 82.366 1.00 52.57 ATOM 16 CG HIS A 3 46.780 60.560 82.590 1.00 52.57 ATOM 17 ND1 HIS A 3 47.363 61.731 83.015 1.00 52.57 ATOM 18 CD2 HIS A 3 47.801 59.672 82.434 1.00 52.57 ATOM 19 CE1 HIS A 3 48.698 61.499 83.095 1.00 52.57 ATOM 20 NE2 HIS A 3 49.012 60.263 82.752 1.00 52.57 ATOM 21 N SER A 4 42.583 61.436 83.211 1.00 38.99 ATOM 22 CA SER A 4 41.207 61.653 82.878 1.00 38.99 ATOM 23 C SER A 4 41.068 62.956 82.160 1.00 38.99 ATOM 24 O SER A 4 41.942 63.821 82.223 1.00 38.99 ATOM 25 CB SER A 4 40.288 61.726 84.107 1.00 38.99 ATOM 26 OG SER A 4 40.622 62.861 84.891 1.00 38.99 ATOM 27 N MET A 5 39.950 63.104 81.420 1.00 48.94 ATOM 28 CA MET A 5 39.641 64.331 80.747 1.00 48.94 ATOM 29 C MET A 5 38.244 64.678 81.155 1.00 48.94 ATOM 30 O MET A 5 37.383 63.803 81.235 1.00 48.94 ATOM 31 CB MET A 5 39.686 64.218 79.214 1.00 48.94 ATOM 32 CG MET A 5 39.501 65.554 78.495 1.00 48.94 ATOM 33 SD MET A 5 39.918 65.517 76.725 1.00 48.94 ATOM 34 CE MET A 5 38.494 64.502 76.238 1.00 48.94 ATOM 35 N ARG A 6 37.988 65.970 81.447 1.00 84.03 ATOM 36 CA ARG A 6 36.678 66.362 81.879 1.00 84.03 ATOM 37 C ARG A 6 36.348 67.693 81.298 1.00 84.03 ATOM 38 O ARG A 6 37.216 68.542 81.098 1.00 84.03 ATOM 39 CB ARG A 6 36.562 66.557 83.400 1.00 84.03 ATOM 40 CG ARG A 6 36.756 65.285 84.221 1.00 84.03 ATOM 41 CD ARG A 6 35.468 64.496 84.463 1.00 84.03 ATOM 42 NE ARG A 6 35.792 63.480 85.502 1.00 84.03 ATOM 43 CZ ARG A 6 36.234 62.242 85.142 1.00 84.03 ATOM 44 NH1 ARG A 6 36.230 61.854 83.834 1.00 84.03 ATOM 45 NH2 ARG A 6 36.700 61.391 86.100 1.00 84.03 ATOM 46 N TYR A 7 35.052 67.895 81.001 1.00 65.22 ATOM 47 CA TYR A 7 34.575 69.168 80.563 1.00 65.22 ATOM 48 C TYR A 7 33.521 69.553 81.545 1.00 65.22 ATOM 49 O TYR A 7 32.706 68.722 81.946 1.00 65.22 ATOM 50 CB TYR A 7 33.934 69.165 79.161 1.00 65.22 ATOM 51 CG TYR A 7 35.009 69.074 78.128 1.00 65.22 ATOM 52 CD1 TYR A 7 35.602 70.222 77.650 1.00 65.22 ATOM 53 CD2 TYR A 7 35.423 67.859 77.632 1.00 65.22 ATOM 54 CE1 TYR A 7 36.590 70.161 76.696 1.00 65.22 ATOM 55 CE2 TYR A 7 36.411 67.791 76.677 1.00 65.22 ATOM 56 CZ TYR A 7 36.995 68.943 76.206 1.00 65.22 ATOM 57 OH TYR A 7 38.008 68.879 75.225 1.00 65.22 ATOM 58 N PHE A 8 33.543 70.824 81.987 1.00 51.21 ATOM 59 CA PHE A 8 32.578 71.281 82.940 1.00 51.21 ATOM 60 C PHE A 8 31.816 72.388 82.277 1.00 51.21 ATOM 61 O PHE A 8 32.401 73.325 81.736 1.00 51.21 ATOM 62 CB PHE A 8 33.229 71.851 84.211 1.00 51.21 ATOM 63 CG PHE A 8 34.039 70.757 84.826 1.00 51.21 ATOM 64 CD1 PHE A 8 35.320 70.513 84.387 1.00 51.21 ATOM 65 CD2 PHE A 8 33.525 69.977 85.836 1.00 51.21 ATOM 66 CE1 PHE A 8 36.078 69.509 84.946 1.00 51.21 ATOM 67 CE2 PHE A 8 34.276 68.971 86.400 1.00 51.21 ATOM 68 CZ PHE A 8 35.555 68.737 85.954 1.00 51.21 ATOM 69 N TYR A 9 30.473 72.299 82.310 1.00122.58 ATOM 70 CA TYR A 9 29.624 73.271 81.679 1.00122.58 ATOM 71 C TYR A 9 28.771 73.889 82.742 1.00122.58 ATOM 72 O TYR A 9 28.227 73.184 83.592 1.00122.58 ATOM 73 CB TYR A 9 28.621 72.633 80.698 1.00122.58 ATOM 74 CG TYR A 9 29.303 72.148 79.464 1.00122.58 ATOM 75 CD1 TYR A 9 30.378 71.292 79.526 1.00122.58 ATOM 76 CD2 TYR A 9 28.818 72.510 78.228 1.00122.58 ATOM 77 CE1 TYR A 9 30.981 70.845 78.372 1.00122.58 ATOM 78 CE2 TYR A 9 29.417 72.063 77.074 1.00122.58 ATOM 79 CZ TYR A 9 30.506 71.231 77.144 1.00122.58 ATOM 80 OH TYR A 9 31.127 70.768 75.966 1.00122.58 ATOM 81 N THR A 10 28.651 75.234 82.733 1.00 45.76 ATOM 82 CA THR A 10 27.801 75.902 83.679 1.00 45.76 ATOM 83 C THR A 10 26.965 76.893 82.919 1.00 45.76 ATOM 84 O THR A 10 27.493 77.674 82.129 1.00 45.76 ATOM 85 CB THR A 10 28.563 76.674 84.714 1.00 45.76 ATOM 86 OG1 THR A 10 29.438 75.808 85.421 1.00 45.76 ATOM 87 CG2 THR A 10 27.562 77.327 85.683 1.00 45.76 ATOM 88 N ALA A 11 25.628 76.870 83.134 1.00 44.24 ATOM 89 CA ALA A 11 24.738 77.812 82.501 1.00 44.24 ATOM 90 C ALA A 11 23.986 78.489 83.603 1.00 44.24 ATOM 91 O ALA A 11 23.462 77.826 84.498 1.00 44.24 ATOM 92 CB ALA A 11 23.692 77.154 81.585 1.00 44.24 ATOM 93 N MET A 12 23.887 79.834 83.558 1.00 69.29 ATOM 94 CA MET A 12 23.274 80.522 84.660 1.00 69.29 ATOM 95 C MET A 12 22.312 81.544 84.136 1.00 69.29 ATOM 96 O MET A 12 22.674 82.400 83.331 1.00 69.29 ATOM 97 CB MET A 12 24.326 81.276 85.484 1.00 69.29 ATOM 98 CG MET A 12 25.361 80.333 86.098 1.00 69.29 ATOM 99 SD MET A 12 26.991 81.085 86.371 1.00 69.29 ATOM 100 CE MET A 12 27.482 80.934 84.627 1.00 69.29 ATOM 101 N SER A 13 21.047 81.476 84.600 1.00 94.48 ATOM 102 CA SER A 13 20.040 82.421 84.206 1.00 94.48 ATOM 103 C SER A 13 20.161 83.628 85.078 1.00 94.48 ATOM 104 O SER A 13 20.619 83.543 86.217 1.00 94.48 ATOM 105 CB SER A 13 18.599 81.919 84.405 1.00 94.48 ATOM 106 OG SER A 13 18.329 80.817 83.555 1.00 94.48 ATOM 107 N ARG A 14 19.764 84.797 84.535 1.00199.49 ATOM 108 CA ARG A 14 19.723 86.013 85.292 1.00199.49 ATOM 109 C ARG A 14 18.556 86.764 84.734 1.00199.49 ATOM 110 O ARG A 14 18.654 87.350 83.658 1.00199.49 ATOM 111 CB ARG A 14 20.919 86.940 85.040 1.00199.49 ATOM 112 CG ARG A 14 22.309 86.349 85.272 1.00199.49 ATOM 113 CD ARG A 14 23.395 87.368 84.923 1.00199.49 ATOM 114 NE ARG A 14 24.694 86.658 84.783 1.00199.49 ATOM 115 CZ ARG A 14 25.372 86.735 83.600 1.00199.49 ATOM 116 NH1 ARG A 14 24.813 87.358 82.522 1.00199.49 ATOM 117 NH2 ARG A 14 26.616 86.187 83.495 1.00199.49 ATOM 118 N PRO A 15 17.455 86.799 85.417 1.00 80.63 ATOM 119 CA PRO A 15 16.344 87.501 84.840 1.00 80.63 ATOM 120 C PRO A 15 16.548 88.981 84.828 1.00 80.63 ATOM 121 O PRO A 15 16.955 89.532 85.851 1.00 80.63 ATOM 122 CB PRO A 15 15.111 87.035 85.607 1.00 80.63 ATOM 123 CG PRO A 15 15.489 85.610 86.049 1.00 80.63 ATOM 124 CD PRO A 15 17.021 85.639 86.178 1.00 80.63 ATOM 125 N GLY A 16 16.261 89.632 83.681 1.00 35.51 ATOM 126 CA GLY A 16 16.349 91.060 83.541 1.00 35.51 ATOM 127 C GLY A 16 17.734 91.419 83.094 1.00 35.51 ATOM 128 O GLY A 16 17.963 92.480 82.515 1.00 35.51 ATOM 129 N ARG A 17 18.693 90.530 83.401 1.00181.54 ATOM 130 CA ARG A 17 20.094 90.646 83.109 1.00181.54 ATOM 131 C ARG A 17 20.397 90.365 81.663 1.00181.54 ATOM 132 O ARG A 17 21.456 90.739 81.168 1.00181.54 ATOM 133 CB ARG A 17 20.946 89.668 83.925 1.00181.54 ATOM 134 CG ARG A 17 22.432 90.015 83.924 1.00181.54 ATOM 135 CD ARG A 17 22.773 91.197 84.834 1.00181.54 ATOM 136 NE ARG A 17 22.687 90.701 86.237 1.00181.54 ATOM 137 CZ ARG A 17 21.490 90.723 86.892 1.00181.54 ATOM 138 NH1 ARG A 17 20.385 91.227 86.271 1.00181.54 ATOM 139 NH2 ARG A 17 21.394 90.238 88.164 1.00181.54 ATOM 140 N GLY A 18 19.539 89.603 80.964 1.00 43.65 ATOM 141 CA GLY A 18 19.854 89.262 79.606 1.00 43.65 ATOM 142 C GLY A 18 19.669 87.780 79.509 1.00 43.65 ATOM 143 O GLY A 18 18.976 87.182 80.331 1.00 43.65 ATOM 144 N GLU A 19 20.287 87.147 78.492 1.00 83.15 ATOM 145 CA GLU A 19 20.163 85.728 78.322 1.00 83.15 ATOM 146 C GLU A 19 21.122 85.052 79.257 1.00 83.15 ATOM 147 O GLU A 19 22.065 85.660 79.760 1.00 83.15 ATOM 148 CB GLU A 19 20.494 85.243 76.899 1.00 83.15 ATOM 149 CG GLU A 19 19.505 85.735 75.840 1.00 83.15 ATOM 150 CD GLU A 19 18.180 85.013 76.041 1.00 83.15 ATOM 151 OE1 GLU A 19 18.140 84.058 76.860 1.00 83.15 ATOM 152 OE2 GLU A 19 17.188 85.410 75.373 1.00 83.15 ATOM 153 N PRO A 20 20.894 83.786 79.498 1.00 74.55 ATOM 154 CA PRO A 20 21.718 83.049 80.414 1.00 74.55 ATOM 155 C PRO A 20 23.126 82.928 79.928 1.00 74.55 ATOM 156 O PRO A 20 23.347 82.806 78.724 1.00 74.55 ATOM 157 CB PRO A 20 21.012 81.711 80.624 1.00 74.55 ATOM 158 CG PRO A 20 19.528 82.046 80.389 1.00 74.55 ATOM 159 CD PRO A 20 19.554 83.228 79.401 1.00 74.55 ATOM 160 N ARG A 21 24.089 82.977 80.867 1.00 87.60 ATOM 161 CA ARG A 21 25.487 82.883 80.571 1.00 87.60 ATOM 162 C ARG A 21 25.845 81.433 80.489 1.00 87.60 ATOM 163 O ARG A 21 25.335 80.612 81.252 1.00 87.60 ATOM 164 CB ARG A 21 26.346 83.519 81.679 1.00 87.60 ATOM 165 CG ARG A 21 27.847 83.613 81.400 1.00 87.60 ATOM 166 CD ARG A 21 28.596 84.248 82.576 1.00 87.60 ATOM 167 NE ARG A 21 30.035 84.389 82.217 1.00 87.60 ATOM 168 CZ ARG A 21 30.853 85.132 83.018 1.00 87.60 ATOM 169 NH1 ARG A 21 30.348 85.735 84.134 1.00 87.60 ATOM 170 NH2 ARG A 21 32.175 85.270 82.714 1.00 87.60 ATOM 171 N PHE A 22 26.733 81.089 79.536 1.00 71.77 ATOM 172 CA PHE A 22 27.195 79.742 79.352 1.00 71.77 ATOM 173 C PHE A 22 28.696 79.767 79.412 1.00 71.77 ATOM 174 O PHE A 22 29.341 80.531 78.694 1.00 71.77 ATOM 175 CB PHE A 22 26.782 79.196 77.974 1.00 71.77 ATOM 176 CG PHE A 22 27.337 77.831 77.785 1.00 71.77 ATOM 177 CD1 PHE A 22 26.710 76.736 78.327 1.00 71.77 ATOM 178 CD2 PHE A 22 28.481 77.651 77.043 1.00 71.77 ATOM 179 CE1 PHE A 22 27.230 75.477 78.144 1.00 71.77 ATOM 180 CE2 PHE A 22 29.005 76.396 76.855 1.00 71.77 ATOM 181 CZ PHE A 22 28.377 75.308 77.406 1.00 71.77 ATOM 182 N ILE A 23 29.296 78.930 80.287 1.00 45.16 ATOM 183 CA ILE A 23 30.728 78.869 80.390 1.00 45.16 ATOM 184 C ILE A 23 31.133 77.430 80.332 1.00 45.16 ATOM 185 O ILE A 23 30.479 76.565 80.915 1.00 45.16 ATOM 186 CB ILE A 23 31.266 79.426 81.678 1.00 45.16 ATOM 187 CG1 ILE A 23 30.938 80.923 81.793 1.00 45.16 ATOM 188 CG2 ILE A 23 32.774 79.124 81.737 1.00 45.16 ATOM 189 CD1 ILE A 23 31.204 81.498 83.183 1.00 45.16 ATOM 190 N ALA A 24 32.226 77.132 79.600 1.00 35.92 ATOM 191 CA ALA A 24 32.687 75.777 79.532 1.00 35.92 ATOM 192 C ALA A 24 34.167 75.784 79.744 1.00 35.92 ATOM 193 O ALA A 24 34.867 76.693 79.299 1.00 35.92 ATOM 194 CB ALA A 24 32.413 75.096 78.179 1.00 35.92 ATOM 195 N VAL A 25 34.672 74.759 80.457 1.00 36.41 ATOM 196 CA VAL A 25 36.079 74.635 80.715 1.00 36.41 ATOM 197 C VAL A 25 36.439 73.196 80.497 1.00 36.41 ATOM 198 O VAL A 25 35.597 72.311 80.645 1.00 36.41 ATOM 199 CB VAL A 25 36.447 74.980 82.128 1.00 36.41 ATOM 200 CG1 VAL A 25 36.143 76.469 82.359 1.00 36.41 ATOM 201 CG2 VAL A 25 35.675 74.044 83.077 1.00 36.41 ATOM 202 N GLY A 26 37.709 72.924 80.125 1.00 27.85 ATOM 203 CA GLY A 26 38.126 71.566 79.901 1.00 27.85 ATOM 204 C GLY A 26 39.373 71.326 80.693 1.00 27.85 ATOM 205 O GLY A 26 40.234 72.198 80.795 1.00 27.85 ATOM 206 N TYR A 27 39.496 70.110 81.267 1.00 73.85 ATOM 207 CA TYR A 27 40.636 69.770 82.072 1.00 73.85 ATOM 208 C TYR A 27 41.169 68.435 81.661 1.00 73.85 ATOM 209 O TYR A 27 40.431 67.550 81.229 1.00 73.85 ATOM 210 CB TYR A 27 40.329 69.559 83.569 1.00 73.85 ATOM 211 CG TYR A 27 40.046 70.832 84.290 1.00 73.85 ATOM 212 CD1 TYR A 27 38.813 71.438 84.216 1.00 73.85 ATOM 213 CD2 TYR A 27 41.024 71.401 85.075 1.00 73.85 ATOM 214 CE1 TYR A 27 38.569 72.604 84.905 1.00 73.85 ATOM 215 CE2 TYR A 27 40.785 72.565 85.765 1.00 73.85 ATOM 216 CZ TYR A 27 39.554 73.170 85.676 1.00 73.85 ATOM 217 OH TYR A 27 39.302 74.365 86.382 1.00 73.85 ATOM 218 N VAL A 28 42.503 68.289 81.759 1.00 76.45 ATOM 219 CA VAL A 28 43.129 67.005 81.667 1.00 76.45 ATOM 220 C VAL A 28 43.727 66.870 83.029 1.00 76.45 ATOM 221 O VAL A 28 44.588 67.663 83.406 1.00 76.45 ATOM 222 CB VAL A 28 44.249 66.943 80.668 1.00 76.45 ATOM 223 CG1 VAL A 28 44.957 65.585 80.807 1.00 76.45 ATOM 224 CG2 VAL A 28 43.662 67.187 79.268 1.00 76.45 ATOM 225 N ASP A 29 43.289 65.857 83.803 1.00125.66 ATOM 226 CA ASP A 29 43.737 65.757 85.161 1.00125.66 ATOM 227 C ASP A 29 43.466 67.078 85.821 1.00125.66 ATOM 228 O ASP A 29 42.383 67.646 85.703 1.00125.66 ATOM 229 CB ASP A 29 45.234 65.437 85.292 1.00125.66 ATOM 230 CG ASP A 29 45.458 64.012 84.804 1.00125.66 ATOM 231 OD1 ASP A 29 44.454 63.335 84.449 1.00125.66 ATOM 232 OD2 ASP A 29 46.641 63.581 84.790 1.00125.66 ATOM 233 N ASP A 30 44.460 67.569 86.572 1.00116.67 ATOM 234 CA ASP A 30 44.438 68.781 87.337 1.00116.67 ATOM 235 C ASP A 30 44.624 70.028 86.515 1.00116.67 ATOM 236 O ASP A 30 44.534 71.120 87.078 1.00116.67 ATOM 237 CB ASP A 30 45.498 68.773 88.446 1.00116.67 ATOM 238 CG ASP A 30 45.069 67.706 89.442 1.00116.67 ATOM 239 OD1 ASP A 30 44.024 67.906 90.115 1.00116.67 ATOM 240 OD2 ASP A 30 45.781 66.672 89.538 1.00116.67 ATOM 241 N THR A 31 44.995 69.925 85.215 1.00147.96 ATOM 242 CA THR A 31 45.269 71.115 84.445 1.00147.96 ATOM 243 C THR A 31 44.166 71.456 83.488 1.00147.96 ATOM 244 O THR A 31 43.683 70.611 82.737 1.00147.96 ATOM 245 CB THR A 31 46.527 71.042 83.627 1.00147.96 ATOM 246 OG1 THR A 31 46.546 69.841 82.873 1.00147.96 ATOM 247 CG2 THR A 31 47.754 71.140 84.534 1.00147.96 ATOM 248 N GLN A 32 43.763 72.747 83.486 1.00 84.05 ATOM 249 CA GLN A 32 42.726 73.230 82.616 1.00 84.05 ATOM 250 C GLN A 32 43.365 73.686 81.336 1.00 84.05 ATOM 251 O GLN A 32 44.331 74.448 81.367 1.00 84.05 ATOM 252 CB GLN A 32 41.956 74.432 83.192 1.00 84.05 ATOM 253 CG GLN A 32 40.854 74.938 82.261 1.00 84.05 ATOM 254 CD GLN A 32 40.265 76.214 82.842 1.00 84.05 ATOM 255 OE1 GLN A 32 40.554 76.592 83.976 1.00 84.05 ATOM 256 NE2 GLN A 32 39.420 76.907 82.033 1.00 84.05 ATOM 257 N PHE A 33 42.932 73.103 80.192 1.00138.11 ATOM 258 CA PHE A 33 43.393 73.465 78.876 1.00138.11 ATOM 259 C PHE A 33 42.612 74.503 78.101 1.00138.11 ATOM 260 O PHE A 33 43.205 75.191 77.274 1.00138.11 ATOM 261 CB PHE A 33 43.733 72.270 77.959 1.00138.11 ATOM 262 CG PHE A 33 42.554 71.433 77.613 1.00138.11 ATOM 263 CD1 PHE A 33 42.029 70.548 78.524 1.00138.11 ATOM 264 CD2 PHE A 33 42.001 71.503 76.354 1.00138.11 ATOM 265 CE1 PHE A 33 40.949 69.764 78.191 1.00138.11 ATOM 266 CE2 PHE A 33 40.923 70.722 76.016 1.00138.11 ATOM 267 CZ PHE A 33 40.394 69.850 76.936 1.00138.11 ATOM 268 N VAL A 34 41.271 74.620 78.265 1.00 58.99 ATOM 269 CA VAL A 34 40.545 75.539 77.415 1.00 58.99 ATOM 270 C VAL A 34 39.403 76.163 78.155 1.00 58.99 ATOM 271 O VAL A 34 39.001 75.692 79.219 1.00 58.99 ATOM 272 CB VAL A 34 39.972 74.885 76.192 1.00 58.99 ATOM 273 CG1 VAL A 34 41.133 74.397 75.309 1.00 58.99 ATOM 274 CG2 VAL A 34 39.015 73.762 76.635 1.00 58.99 ATOM 275 N ARG A 35 38.865 77.276 77.600 1.00 79.66 ATOM 276 CA ARG A 35 37.750 77.946 78.212 1.00 79.66 ATOM 277 C ARG A 35 36.895 78.554 77.137 1.00 79.66 ATOM 278 O ARG A 35 37.351 78.784 76.016 1.00 79.66 ATOM 279 CB ARG A 35 38.163 79.105 79.129 1.00 79.66 ATOM 280 CG ARG A 35 38.887 80.221 78.379 1.00 79.66 ATOM 281 CD ARG A 35 39.310 81.370 79.289 1.00 79.66 ATOM 282 NE ARG A 35 39.982 82.390 78.438 1.00 79.66 ATOM 283 CZ ARG A 35 40.541 83.487 79.025 1.00 79.66 ATOM 284 NH1 ARG A 35 40.533 83.604 80.385 1.00 79.66 ATOM 285 NH2 ARG A 35 41.108 84.460 78.255 1.00 79.66 ATOM 286 N PHE A 36 35.606 78.794 77.467 1.00121.71 ATOM 287 CA PHE A 36 34.655 79.440 76.601 1.00121.71 ATOM 288 C PHE A 36 33.745 80.227 77.501 1.00121.71 ATOM 289 O PHE A 36 33.332 79.737 78.551 1.00121.71 ATOM 290 CB PHE A 36 33.784 78.431 75.823 1.00121.71 ATOM 291 CG PHE A 36 32.756 79.136 74.999 1.00121.71 ATOM 292 CD1 PHE A 36 31.547 79.498 75.550 1.00121.71 ATOM 293 CD2 PHE A 36 32.984 79.425 73.671 1.00121.71 ATOM 294 CE1 PHE A 36 30.588 80.139 74.800 1.00121.71 ATOM 295 CE2 PHE A 36 32.029 80.066 72.915 1.00121.71 ATOM 296 CZ PHE A 36 30.828 80.428 73.479 1.00121.71 ATOM 297 N ASP A 37 33.422 81.479 77.114 1.00 76.08 ATOM 298 CA ASP A 37 32.563 82.318 77.910 1.00 76.08 ATOM 299 C ASP A 37 31.659 83.059 76.968 1.00 76.08 ATOM 300 O ASP A 37 32.123 83.834 76.133 1.00 76.08 ATOM 301 CB ASP A 37 33.358 83.369 78.704 1.00 76.08 ATOM 302 CG ASP A 37 32.396 84.209 79.526 1.00 76.08 ATOM 303 OD1 ASP A 37 31.179 83.885 79.548 1.00 76.08 ATOM 304 OD2 ASP A 37 32.876 85.195 80.147 1.00 76.08 ATOM 305 N SER A 38 30.332 82.846 77.089 1.00 51.85 ATOM 306 CA SER A 38 29.372 83.462 76.211 1.00 51.85 ATOM 307 C SER A 38 29.327 84.952 76.420 1.00 51.85 ATOM 308 O SER A 38 28.918 85.689 75.524 1.00 51.85 ATOM 309 CB SER A 38 27.946 82.914 76.407 1.00 51.85 ATOM 310 OG SER A 38 27.473 83.225 77.708 1.00 51.85 ATOM 311 N ASP A 39 29.709 85.432 77.619 1.00 65.71 ATOM 312 CA ASP A 39 29.696 86.837 77.945 1.00 65.71 ATOM 313 C ASP A 39 30.757 87.603 77.204 1.00 65.71 ATOM 314 O ASP A 39 30.583 88.792 76.941 1.00 65.71 ATOM 315 CB ASP A 39 29.868 87.124 79.448 1.00 65.71 ATOM 316 CG ASP A 39 28.538 86.855 80.142 1.00 65.71 ATOM 317 OD1 ASP A 39 27.524 86.644 79.427 1.00 65.71 ATOM 318 OD2 ASP A 39 28.517 86.876 81.401 1.00 65.71 ATOM 319 N ALA A 40 31.879 86.949 76.844 1.00 40.35 ATOM 320 CA ALA A 40 33.009 87.626 76.257 1.00 40.35 ATOM 321 C ALA A 40 32.582 88.465 75.089 1.00 40.35 ATOM 322 O ALA A 40 31.566 88.205 74.448 1.00 40.35 ATOM 323 CB ALA A 40 34.114 86.665 75.776 1.00 40.35 ATOM 324 N ALA A 41 33.369 89.526 74.795 1.00 31.13 ATOM 325 CA ALA A 41 33.030 90.432 73.735 1.00 31.13 ATOM 326 C ALA A 41 32.955 89.629 72.481 1.00 31.13 ATOM 327 O ALA A 41 32.024 89.783 71.691 1.00 31.13 ATOM 328 CB ALA A 41 34.084 91.530 73.526 1.00 31.13 ATOM 329 N SER A 42 33.943 88.745 72.260 1.00 95.79 ATOM 330 CA SER A 42 33.851 87.862 71.138 1.00 95.79 ATOM 331 C SER A 42 34.010 86.486 71.703 1.00 95.79 ATOM 332 O SER A 42 35.110 86.070 72.065 1.00 95.79 ATOM 333 CB SER A 42 34.952 88.098 70.089 1.00 95.79 ATOM 334 OG SER A 42 36.233 87.931 70.677 1.00 95.79 ATOM 335 N PRO A 43 32.922 85.764 71.780 1.00 79.94 ATOM 336 CA PRO A 43 32.987 84.462 72.376 1.00 79.94 ATOM 337 C PRO A 43 33.781 83.538 71.524 1.00 79.94 ATOM 338 O PRO A 43 33.492 83.426 70.334 1.00 79.94 ATOM 339 CB PRO A 43 31.541 84.030 72.606 1.00 79.94 ATOM 340 CG PRO A 43 30.796 85.365 72.789 1.00 79.94 ATOM 341 CD PRO A 43 31.618 86.379 71.970 1.00 79.94 ATOM 342 N ARG A 44 34.760 82.838 72.124 1.00199.57 ATOM 343 CA ARG A 44 35.587 81.976 71.344 1.00199.57 ATOM 344 C ARG A 44 36.296 81.069 72.290 1.00199.57 ATOM 345 O ARG A 44 36.584 81.447 73.423 1.00199.57 ATOM 346 CB ARG A 44 36.673 82.775 70.613 1.00199.57 ATOM 347 CG ARG A 44 37.608 81.934 69.758 1.00199.57 ATOM 348 CD ARG A 44 38.872 82.689 69.349 1.00199.57 ATOM 349 NE ARG A 44 38.454 83.848 68.516 1.00199.57 ATOM 350 CZ ARG A 44 39.399 84.695 68.014 1.00199.57 ATOM 351 NH1 ARG A 44 40.719 84.489 68.295 1.00199.57 ATOM 352 NH2 ARG A 44 39.024 85.744 67.226 1.00199.57 ATOM 353 N THR A 45 36.608 79.838 71.840 1.00 47.60 ATOM 354 CA THR A 45 37.328 78.932 72.680 1.00 47.60 ATOM 355 C THR A 45 38.738 79.441 72.739 1.00 47.60 ATOM 356 O THR A 45 39.321 79.769 71.708 1.00 47.60 ATOM 357 CB THR A 45 37.362 77.537 72.130 1.00 47.60 ATOM 358 OG1 THR A 45 36.037 77.059 71.944 1.00 47.60 ATOM 359 CG2 THR A 45 38.119 76.631 73.114 1.00 47.60 ATOM 360 N GLU A 46 39.323 79.536 73.953 1.00 67.55 ATOM 361 CA GLU A 46 40.662 80.055 74.053 1.00 67.55 ATOM 362 C GLU A 46 41.518 79.112 74.854 1.00 67.55 ATOM 363 O GLU A 46 41.032 78.391 75.723 1.00 67.55 ATOM 364 CB GLU A 46 40.715 81.458 74.676 1.00 67.55 ATOM 365 CG GLU A 46 40.093 82.500 73.742 1.00 67.55 ATOM 366 CD GLU A 46 40.137 83.863 74.409 1.00 67.55 ATOM 367 OE1 GLU A 46 40.211 83.907 75.666 1.00 67.55 ATOM 368 OE2 GLU A 46 40.089 84.879 73.664 1.00 67.55 ATOM 369 N PRO A 47 42.792 79.076 74.529 1.00106.63 ATOM 370 CA PRO A 47 43.725 78.195 75.195 1.00106.63 ATOM 371 C PRO A 47 44.139 78.595 76.585 1.00106.63 ATOM 372 O PRO A 47 44.447 79.764 76.813 1.00106.63 ATOM 373 CB PRO A 47 44.905 78.019 74.235 1.00106.63 ATOM 374 CG PRO A 47 44.751 79.161 73.215 1.00106.63 ATOM 375 CD PRO A 47 43.237 79.427 73.193 1.00106.63 ATOM 376 N ARG A 48 44.029 77.646 77.536 1.00188.70 ATOM 377 CA ARG A 48 44.448 77.690 78.912 1.00188.70 ATOM 378 C ARG A 48 45.835 77.164 79.181 1.00188.70 ATOM 379 O ARG A 48 46.427 77.514 80.201 1.00188.70 ATOM 380 CB ARG A 48 43.462 76.958 79.832 1.00188.70 ATOM 381 CG ARG A 48 42.041 77.513 79.698 1.00188.70 ATOM 382 CD ARG A 48 41.974 79.038 79.550 1.00188.70 ATOM 383 NE ARG A 48 42.397 79.654 80.839 1.00188.70 ATOM 384 CZ ARG A 48 42.994 80.881 80.830 1.00188.70 ATOM 385 NH1 ARG A 48 43.221 81.518 79.644 1.00188.70 ATOM 386 NH2 ARG A 48 43.368 81.474 82.002 1.00188.70 ATOM 387 N ALA A 49 46.354 76.228 78.349 1.00 51.38 ATOM 388 CA ALA A 49 47.647 75.641 78.616 1.00 51.38 ATOM 389 C ALA A 49 48.453 75.707 77.347 1.00 51.38 ATOM 390 O ALA A 49 47.898 75.714 76.252 1.00 51.38 ATOM 391 CB ALA A 49 47.570 74.166 79.048 1.00 51.38 ATOM 392 N PRO A 50 49.757 75.765 77.461 1.00 75.24 ATOM 393 CA PRO A 50 50.588 75.909 76.293 1.00 75.24 ATOM 394 C PRO A 50 50.550 74.779 75.305 1.00 75.24 ATOM 395 O PRO A 50 50.696 75.036 74.112 1.00 75.24 ATOM 396 CB PRO A 50 51.986 76.226 76.815 1.00 75.24 ATOM 397 CG PRO A 50 51.715 76.941 78.151 1.00 75.24 ATOM 398 CD PRO A 50 50.379 76.355 78.638 1.00 75.24 ATOM 399 N TRP A 51 50.348 73.533 75.767 1.00102.18 ATOM 400 CA TRP A 51 50.367 72.370 74.924 1.00102.18 ATOM 401 C TRP A 51 49.242 72.364 73.928 1.00102.18 ATOM 402 O TRP A 51 49.367 71.763 72.862 1.00102.18 ATOM 403 CB TRP A 51 50.408 71.054 75.729 1.00102.18 ATOM 404 CG TRP A 51 49.575 71.013 76.993 1.00102.18 ATOM 405 CD1 TRP A 51 49.967 71.328 78.263 1.00102.18 ATOM 406 CD2 TRP A 51 48.203 70.600 77.086 1.00102.18 ATOM 407 NE1 TRP A 51 48.929 71.132 79.140 1.00102.18 ATOM 408 CE2 TRP A 51 47.837 70.683 78.431 1.00102.18 ATOM 409 CE3 TRP A 51 47.324 70.177 76.133 1.00102.18 ATOM 410 CZ2 TRP A 51 46.579 70.346 78.842 1.00102.18 ATOM 411 CZ3 TRP A 51 46.055 69.844 76.551 1.00102.18 ATOM 412 CH2 TRP A 51 45.690 69.927 77.878 1.00102.18 ATOM 413 N ILE A 52 48.098 72.973 74.278 1.00113.29 ATOM 414 CA ILE A 52 46.929 73.058 73.440 1.00113.29 ATOM 415 C ILE A 52 47.132 73.960 72.247 1.00113.29 ATOM 416 O ILE A 52 46.518 73.756 71.202 1.00113.29 ATOM 417 CB ILE A 52 45.704 73.521 74.182 1.00113.29 ATOM 418 CG1 ILE A 52 44.438 73.215 73.361 1.00113.29 ATOM 419 CG2 ILE A 52 45.874 75.009 74.529 1.00113.29 ATOM 420 CD1 ILE A 52 44.154 71.719 73.223 1.00113.29 ATOM 421 N GLU A 53 47.988 74.992 72.378 1.00 59.63 ATOM 422 CA GLU A 53 48.140 76.046 71.404 1.00 59.63 ATOM 423 C GLU A 53 48.476 75.520 70.035 1.00 59.63 ATOM 424 O GLU A 53 48.109 76.130 69.031 1.00 59.63 ATOM 425 CB GLU A 53 49.217 77.068 71.809 1.00 59.63 ATOM 426 CG GLU A 53 48.815 77.896 73.032 1.00 59.63 ATOM 427 CD GLU A 53 49.934 78.873 73.358 1.00 59.63 ATOM 428 OE1 GLU A 53 51.016 78.770 72.722 1.00 59.63 ATOM 429 OE2 GLU A 53 49.720 79.738 74.247 1.00 59.63 ATOM 430 N GLN A 54 49.161 74.370 69.952 1.00137.46 ATOM 431 CA GLN A 54 49.618 73.803 68.711 1.00137.46 ATOM 432 C GLN A 54 48.461 73.554 67.788 1.00137.46 ATOM 433 O GLN A 54 48.607 73.703 66.577 1.00137.46 ATOM 434 CB GLN A 54 50.268 72.430 68.927 1.00137.46 ATOM 435 CG GLN A 54 51.470 72.452 69.866 1.00137.46 ATOM 436 CD GLN A 54 51.787 71.006 70.208 1.00137.46 ATOM 437 OE1 GLN A 54 52.800 70.456 69.780 1.00137.46 ATOM 438 NE2 GLN A 54 50.883 70.370 71.000 1.00137.46 ATOM 439 N GLU A 55 47.289 73.173 68.331 1.00103.53 ATOM 440 CA GLU A 55 46.152 72.775 67.540 1.00103.53 ATOM 441 C GLU A 55 45.866 73.806 66.485 1.00103.53 ATOM 442 O GLU A 55 46.041 75.004 66.693 1.00103.53 ATOM 443 CB GLU A 55 44.872 72.592 68.376 1.00103.53 ATOM 444 CG GLU A 55 45.005 71.560 69.502 1.00103.53 ATOM 445 CD GLU A 55 45.123 70.160 68.906 1.00103.53 ATOM 446 OE1 GLU A 55 45.307 70.044 67.665 1.00103.53 ATOM 447 OE2 GLU A 55 45.028 69.185 69.697 1.00103.53 ATOM 448 N GLY A 56 45.412 73.331 65.301 1.00 24.92 ATOM 449 CA GLY A 56 45.165 74.165 64.154 1.00 24.92 ATOM 450 C GLY A 56 43.856 74.878 64.298 1.00 24.92 ATOM 451 O GLY A 56 43.084 74.655 65.229 1.00 24.92 ATOM 452 N PRO A 57 43.608 75.740 63.346 1.00 60.13 ATOM 453 CA PRO A 57 42.422 76.552 63.350 1.00 60.13 ATOM 454 C PRO A 57 41.149 75.775 63.256 1.00 60.13 ATOM 455 O PRO A 57 40.127 76.251 63.749 1.00 60.13 ATOM 456 CB PRO A 57 42.615 77.574 62.233 1.00 60.13 ATOM 457 CG PRO A 57 44.145 77.738 62.160 1.00 60.13 ATOM 458 CD PRO A 57 44.699 76.381 62.629 1.00 60.13 ATOM 459 N GLU A 58 41.180 74.591 62.622 1.00 34.43 ATOM 460 CA GLU A 58 40.002 73.789 62.460 1.00 34.43 ATOM 461 C GLU A 58 39.533 73.362 63.815 1.00 34.43 ATOM 462 O GLU A 58 38.336 73.354 64.098 1.00 34.43 ATOM 463 CB GLU A 58 40.294 72.532 61.620 1.00 34.43 ATOM 464 CG GLU A 58 41.446 71.698 62.187 1.00 34.43 ATOM 465 CD GLU A 58 41.844 70.652 61.156 1.00 34.43 ATOM 466 OE1 GLU A 58 41.079 69.666 60.982 1.00 34.43 ATOM 467 OE2 GLU A 58 42.923 70.830 60.530 1.00 34.43 ATOM 468 N TYR A 59 40.489 73.013 64.692 1.00 60.60 ATOM 469 CA TYR A 59 40.215 72.530 66.014 1.00 60.60 ATOM 470 C TYR A 59 39.497 73.592 66.784 1.00 60.60 ATOM 471 O TYR A 59 38.477 73.333 67.424 1.00 60.60 ATOM 472 CB TYR A 59 41.542 72.202 66.735 1.00 60.60 ATOM 473 CG TYR A 59 41.330 71.837 68.166 1.00 60.60 ATOM 474 CD1 TYR A 59 40.967 70.560 68.527 1.00 60.60 ATOM 475 CD2 TYR A 59 41.522 72.778 69.152 1.00 60.60 ATOM 476 CE1 TYR A 59 40.787 70.229 69.850 1.00 60.60 ATOM 477 CE2 TYR A 59 41.343 72.454 70.477 1.00 60.60 ATOM 478 CZ TYR A 59 40.971 71.179 70.827 1.00 60.60 ATOM 479 OH TYR A 59 40.787 70.846 72.187 1.00 60.60 ATOM 480 N TRP A 60 40.006 74.833 66.719 1.00 57.98 ATOM 481 CA TRP A 60 39.435 75.912 67.468 1.00 57.98 ATOM 482 C TRP A 60 38.059 76.204 66.961 1.00 57.98 ATOM 483 O TRP A 60 37.137 76.416 67.746 1.00 57.98 ATOM 484 CB TRP A 60 40.274 77.192 67.370 1.00 57.98 ATOM 485 CG TRP A 60 41.673 76.994 67.900 1.00 57.98 ATOM 486 CD1 TRP A 60 42.861 77.011 67.229 1.00 57.98 ATOM 487 CD2 TRP A 60 41.981 76.676 69.266 1.00 57.98 ATOM 488 NE1 TRP A 60 43.893 76.736 68.094 1.00 57.98 ATOM 489 CE2 TRP A 60 43.365 76.524 69.351 1.00 57.98 ATOM 490 CE3 TRP A 60 41.175 76.519 70.358 1.00 57.98 ATOM 491 CZ2 TRP A 60 43.968 76.212 70.536 1.00 57.98 ATOM 492 CZ3 TRP A 60 41.786 76.209 71.553 1.00 57.98 ATOM 493 CH2 TRP A 60 43.157 76.059 71.638 1.00 57.98 ATOM 494 N ASP A 61 37.884 76.217 65.626 1.00 29.87 ATOM 495 CA ASP A 61 36.600 76.532 65.067 1.00 29.87 ATOM 496 C ASP A 61 35.613 75.494 65.494 1.00 29.87 ATOM 497 O ASP A 61 34.462 75.813 65.789 1.00 29.87 ATOM 498 CB ASP A 61 36.594 76.584 63.530 1.00 29.87 ATOM 499 CG ASP A 61 37.275 77.878 63.097 1.00 29.87 ATOM 500 OD1 ASP A 61 37.036 78.922 63.762 1.00 29.87 ATOM 501 OD2 ASP A 61 38.042 77.835 62.100 1.00 29.87 ATOM 502 N ARG A 62 36.036 74.217 65.541 1.00117.76 ATOM 503 CA ARG A 62 35.139 73.156 65.900 1.00117.76 ATOM 504 C ARG A 62 34.677 73.356 67.310 1.00117.76 ATOM 505 O ARG A 62 33.493 73.214 67.608 1.00117.76 ATOM 506 CB ARG A 62 35.805 71.769 65.798 1.00117.76 ATOM 507 CG ARG A 62 34.840 70.588 65.926 1.00117.76 ATOM 508 CD ARG A 62 33.744 70.594 64.857 1.00117.76 ATOM 509 NE ARG A 62 33.074 69.263 64.860 1.00117.76 ATOM 510 CZ ARG A 62 32.196 68.957 65.856 1.00117.76 ATOM 511 NH1 ARG A 62 32.130 69.764 66.951 1.00117.76 ATOM 512 NH2 ARG A 62 31.400 67.852 65.774 1.00117.76 ATOM 513 N ASN A 63 35.606 73.710 68.218 1.00 46.36 ATOM 514 CA ASN A 63 35.262 73.887 69.602 1.00 46.36 ATOM 515 C ASN A 63 34.299 75.020 69.742 1.00 46.36 ATOM 516 O ASN A 63 33.304 74.915 70.456 1.00 46.36 ATOM 517 CB ASN A 63 36.470 74.247 70.484 1.00 46.36 ATOM 518 CG ASN A 63 37.332 73.012 70.665 1.00 46.36 ATOM 519 OD1 ASN A 63 36.932 72.052 71.320 1.00 46.36 ATOM 520 ND2 ASN A 63 38.555 73.039 70.071 1.00 46.36 ATOM 521 N THR A 64 34.573 76.135 69.045 1.00 33.89 ATOM 522 CA THR A 64 33.760 77.308 69.174 1.00 33.89 ATOM 523 C THR A 64 32.375 77.005 68.695 1.00 33.89 ATOM 524 O THR A 64 31.399 77.463 69.284 1.00 33.89 ATOM 525 CB THR A 64 34.296 78.477 68.398 1.00 33.89 ATOM 526 OG1 THR A 64 35.617 78.777 68.829 1.00 33.89 ATOM 527 CG2 THR A 64 33.384 79.692 68.642 1.00 33.89 ATOM 528 N GLN A 65 32.249 76.218 67.609 1.00 77.05 ATOM 529 CA GLN A 65 30.947 75.903 67.086 1.00 77.05 ATOM 530 C GLN A 65 30.179 75.165 68.133 1.00 77.05 ATOM 531 O GLN A 65 29.015 75.469 68.392 1.00 77.05 ATOM 532 CB GLN A 65 31.012 74.995 65.839 1.00 77.05 ATOM 533 CG GLN A 65 29.647 74.531 65.314 1.00 77.05 ATOM 534 CD GLN A 65 29.236 73.261 66.054 1.00 77.05 ATOM 535 OE1 GLN A 65 28.337 73.278 66.894 1.00 77.05 ATOM 536 NE2 GLN A 65 29.908 72.124 65.728 1.00 77.05 ATOM 537 N ILE A 66 30.830 74.191 68.793 1.00 95.26 ATOM 538 CA ILE A 66 30.143 73.392 69.763 1.00 95.26 ATOM 539 C ILE A 66 29.685 74.239 70.908 1.00 95.26 ATOM 540 O ILE A 66 28.545 74.123 71.352 1.00 95.26 ATOM 541 CB ILE A 66 30.998 72.296 70.336 1.00 95.26 ATOM 542 CG1 ILE A 66 31.303 71.245 69.260 1.00 95.26 ATOM 543 CG2 ILE A 66 30.274 71.714 71.563 1.00 95.26 ATOM 544 CD1 ILE A 66 30.044 70.550 68.745 1.00 95.26 ATOM 545 N PHE A 67 30.561 75.120 71.421 1.00 63.33 ATOM 546 CA PHE A 67 30.218 75.907 72.571 1.00 63.33 ATOM 547 C PHE A 67 29.139 76.894 72.247 1.00 63.33 ATOM 548 O PHE A 67 28.264 77.152 73.073 1.00 63.33 ATOM 549 CB PHE A 67 31.415 76.661 73.177 1.00 63.33 ATOM 550 CG PHE A 67 32.339 75.627 73.729 1.00 63.33 ATOM 551 CD1 PHE A 67 31.993 74.903 74.847 1.00 63.33 ATOM 552 CD2 PHE A 67 33.564 75.392 73.146 1.00 63.33 ATOM 553 CE1 PHE A 67 32.840 73.948 75.361 1.00 63.33 ATOM 554 CE2 PHE A 67 34.416 74.440 73.655 1.00 63.33 ATOM 555 CZ PHE A 67 34.056 73.714 74.766 1.00 63.33 ATOM 556 N LYS A 68 29.191 77.506 71.050 1.00 37.89 ATOM 557 CA LYS A 68 28.181 78.464 70.703 1.00 37.89 ATOM 558 C LYS A 68 26.853 77.782 70.617 1.00 37.89 ATOM 559 O LYS A 68 25.843 78.323 71.068 1.00 37.89 ATOM 560 CB LYS A 68 28.447 79.190 69.373 1.00 37.89 ATOM 561 CG LYS A 68 29.568 80.225 69.479 1.00 37.89 ATOM 562 CD LYS A 68 29.998 80.831 68.141 1.00 37.89 ATOM 563 CE LYS A 68 31.053 81.931 68.291 1.00 37.89 ATOM 564 NZ LYS A 68 31.426 82.466 66.963 1.00 37.89 ATOM 565 N THR A 69 26.810 76.567 70.039 1.00 99.42 ATOM 566 CA THR A 69 25.553 75.889 69.909 1.00 99.42 ATOM 567 C THR A 69 25.043 75.548 71.279 1.00 99.42 ATOM 568 O THR A 69 23.849 75.671 71.555 1.00 99.42 ATOM 569 CB THR A 69 25.640 74.633 69.083 1.00 99.42 ATOM 570 OG1 THR A 69 24.340 74.224 68.688 1.00 99.42 ATOM 571 CG2 THR A 69 26.305 73.513 69.897 1.00 99.42 ATOM 572 N ASN A 70 25.950 75.133 72.185 1.00 61.01 ATOM 573 CA ASN A 70 25.584 74.739 73.518 1.00 61.01 ATOM 574 C ASN A 70 24.984 75.898 74.247 1.00 61.01 ATOM 575 O ASN A 70 24.069 75.716 75.049 1.00 61.01 ATOM 576 CB ASN A 70 26.772 74.239 74.362 1.00 61.01 ATOM 577 CG ASN A 70 27.159 72.844 73.889 1.00 61.01 ATOM 578 OD1 ASN A 70 28.296 72.606 73.486 1.00 61.01 ATOM 579 ND2 ASN A 70 26.190 71.891 73.948 1.00 61.01 ATOM 580 N THR A 71 25.482 77.127 74.006 1.00132.63 ATOM 581 CA THR A 71 24.920 78.224 74.733 1.00132.63 ATOM 582 C THR A 71 23.459 78.314 74.421 1.00132.63 ATOM 583 O THR A 71 22.649 78.553 75.315 1.00132.63 ATOM 584 CB THR A 71 25.572 79.559 74.482 1.00132.63 ATOM 585 OG1 THR A 71 25.579 79.881 73.103 1.00132.63 ATOM 586 CG2 THR A 71 27.004 79.528 75.024 1.00132.63 ATOM 587 N GLN A 72 23.079 78.118 73.146 1.00 52.32 ATOM 588 CA GLN A 72 21.698 78.213 72.758 1.00 52.32 ATOM 589 C GLN A 72 20.903 77.098 73.381 1.00 52.32 ATOM 590 O GLN A 72 19.816 77.321 73.915 1.00 52.32 ATOM 591 CB GLN A 72 21.514 78.087 71.235 1.00 52.32 ATOM 592 CG GLN A 72 22.383 79.062 70.437 1.00 52.32 ATOM 593 CD GLN A 72 22.121 80.470 70.946 1.00 52.32 ATOM 594 OE1 GLN A 72 23.046 81.262 71.117 1.00 52.32 ATOM 595 NE2 GLN A 72 20.824 80.796 71.190 1.00 52.32 ATOM 596 N THR A 73 21.442 75.862 73.346 1.00 30.13 ATOM 597 CA THR A 73 20.741 74.702 73.826 1.00 30.13 ATOM 598 C THR A 73 20.473 74.843 75.293 1.00 30.13 ATOM 599 O THR A 73 19.374 74.557 75.767 1.00 30.13 ATOM 600 CB THR A 73 21.530 73.436 73.641 1.00 30.13 ATOM 601 OG1 THR A 73 21.828 73.236 72.267 1.00 30.13 ATOM 602 CG2 THR A 73 20.711 72.252 74.184 1.00 30.13 ATOM 603 N TYR A 74 21.480 75.303 76.054 1.00 68.62 ATOM 604 CA TYR A 74 21.355 75.432 77.478 1.00 68.62 ATOM 605 C TYR A 74 20.320 76.445 77.847 1.00 68.62 ATOM 606 O TYR A 74 19.638 76.291 78.857 1.00 68.62 ATOM 607 CB TYR A 74 22.681 75.748 78.197 1.00 68.62 ATOM 608 CG TYR A 74 23.406 74.451 78.356 1.00 68.62 ATOM 609 CD1 TYR A 74 23.186 73.684 79.478 1.00 68.62 ATOM 610 CD2 TYR A 74 24.285 73.987 77.402 1.00 68.62 ATOM 611 CE1 TYR A 74 23.833 72.484 79.656 1.00 68.62 ATOM 612 CE2 TYR A 74 24.936 72.785 77.575 1.00 68.62 ATOM 613 CZ TYR A 74 24.711 72.031 78.702 1.00 68.62 ATOM 614 OH TYR A 74 25.376 70.799 78.884 1.00 68.62 ATOM 615 N ARG A 75 20.192 77.531 77.068 1.00 81.05 ATOM 616 CA ARG A 75 19.216 78.529 77.398 1.00 81.05 ATOM 617 C ARG A 75 17.850 77.915 77.328 1.00 81.05 ATOM 618 O ARG A 75 17.007 78.162 78.189 1.00 81.05 ATOM 619 CB ARG A 75 19.304 79.741 76.456 1.00 81.05 ATOM 620 CG ARG A 75 20.641 80.471 76.626 1.00 81.05 ATOM 621 CD ARG A 75 20.945 81.544 75.578 1.00 81.05 ATOM 622 NE ARG A 75 22.278 82.117 75.927 1.00 81.05 ATOM 623 CZ ARG A 75 22.978 82.866 75.026 1.00 81.05 ATOM 624 NH1 ARG A 75 22.460 83.122 73.790 1.00 81.05 ATOM 625 NH2 ARG A 75 24.208 83.357 75.363 1.00 81.05 ATOM 626 N GLU A 76 17.601 77.077 76.307 1.00 69.30 ATOM 627 CA GLU A 76 16.318 76.452 76.163 1.00 69.30 ATOM 628 C GLU A 76 16.104 75.542 77.336 1.00 69.30 ATOM 629 O GLU A 76 15.005 75.461 77.882 1.00 69.30 ATOM 630 CB GLU A 76 16.230 75.605 74.881 1.00 69.30 ATOM 631 CG GLU A 76 14.808 75.226 74.469 1.00 69.30 ATOM 632 CD GLU A 76 14.217 76.411 73.715 1.00 69.30 ATOM 633 OE1 GLU A 76 13.739 77.365 74.384 1.00 69.30 ATOM 634 OE2 GLU A 76 14.241 76.380 72.455 1.00 69.30 ATOM 635 N SER A 77 17.170 74.838 77.762 1.00 34.44 ATOM 636 CA SER A 77 17.079 73.884 78.832 1.00 34.44 ATOM 637 C SER A 77 16.718 74.565 80.121 1.00 34.44 ATOM 638 O SER A 77 15.954 74.018 80.914 1.00 34.44 ATOM 639 CB SER A 77 18.392 73.118 79.065 1.00 34.44 ATOM 640 OG SER A 77 18.700 72.328 77.925 1.00 34.44 ATOM 641 N LEU A 78 17.260 75.772 80.376 1.00 96.13 ATOM 642 CA LEU A 78 16.929 76.459 81.598 1.00 96.13 ATOM 643 C LEU A 78 15.468 76.760 81.608 1.00 96.13 ATOM 644 O LEU A 78 14.817 76.667 82.647 1.00 96.13 ATOM 645 CB LEU A 78 17.658 77.806 81.795 1.00 96.13 ATOM 646 CG LEU A 78 19.094 77.719 82.357 1.00 96.13 ATOM 647 CD1 LEU A 78 19.083 77.311 83.836 1.00 96.13 ATOM 648 CD2 LEU A 78 20.000 76.810 81.522 1.00 96.13 ATOM 649 N ARG A 79 14.918 77.150 80.446 1.00100.67 ATOM 650 CA ARG A 79 13.529 77.491 80.361 1.00100.67 ATOM 651 C ARG A 79 12.732 76.271 80.696 1.00100.67 ATOM 652 O ARG A 79 11.760 76.338 81.448 1.00100.67 ATOM 653 CB ARG A 79 13.146 77.934 78.940 1.00100.67 ATOM 654 CG ARG A 79 13.995 79.111 78.457 1.00100.67 ATOM 655 CD ARG A 79 13.792 79.475 76.986 1.00100.67 ATOM 656 NE ARG A 79 14.943 80.337 76.598 1.00100.67 ATOM 657 CZ ARG A 79 15.284 80.481 75.285 1.00100.67 ATOM 658 NH1 ARG A 79 14.523 79.908 74.309 1.00100.67 ATOM 659 NH2 ARG A 79 16.395 81.195 74.945 1.00100.67 ATOM 660 N ASN A 80 13.146 75.112 80.154 1.00 44.78 ATOM 661 CA ASN A 80 12.416 73.894 80.355 1.00 44.78 ATOM 662 C ASN A 80 12.425 73.525 81.808 1.00 44.78 ATOM 663 O ASN A 80 11.384 73.189 82.371 1.00 44.78 ATOM 664 CB ASN A 80 13.028 72.700 79.603 1.00 44.78 ATOM 665 CG ASN A 80 12.898 72.927 78.102 1.00 44.78 ATOM 666 OD1 ASN A 80 11.797 73.042 77.566 1.00 44.78 ATOM 667 ND2 ASN A 80 14.063 72.993 77.405 1.00 44.78 ATOM 668 N LEU A 81 13.600 73.591 82.464 1.00 81.38 ATOM 669 CA LEU A 81 13.687 73.148 83.827 1.00 81.38 ATOM 670 C LEU A 81 12.876 74.009 84.732 1.00 81.38 ATOM 671 O LEU A 81 12.305 73.514 85.704 1.00 81.38 ATOM 672 CB LEU A 81 15.110 73.042 84.401 1.00 81.38 ATOM 673 CG LEU A 81 15.927 71.927 83.728 1.00 81.38 ATOM 674 CD1 LEU A 81 17.129 71.523 84.589 1.00 81.38 ATOM 675 CD2 LEU A 81 15.044 70.736 83.330 1.00 81.38 ATOM 676 N ARG A 82 12.801 75.321 84.457 1.00 76.70 ATOM 677 CA ARG A 82 12.041 76.154 85.339 1.00 76.70 ATOM 678 C ARG A 82 10.628 75.649 85.323 1.00 76.70 ATOM 679 O ARG A 82 9.981 75.560 86.365 1.00 76.70 ATOM 680 CB ARG A 82 12.013 77.635 84.924 1.00 76.70 ATOM 681 CG ARG A 82 11.484 78.540 86.039 1.00 76.70 ATOM 682 CD ARG A 82 11.192 79.979 85.608 1.00 76.70 ATOM 683 NE ARG A 82 9.839 79.978 84.991 1.00 76.70 ATOM 684 CZ ARG A 82 9.706 79.852 83.638 1.00 76.70 ATOM 685 NH1 ARG A 82 10.815 79.838 82.843 1.00 76.70 ATOM 686 NH2 ARG A 82 8.466 79.738 83.082 1.00 76.70 ATOM 687 N GLY A 83 10.126 75.282 84.128 1.00 28.55 ATOM 688 CA GLY A 83 8.779 74.812 83.952 1.00 28.55 ATOM 689 C GLY A 83 8.553 73.518 84.681 1.00 28.55 ATOM 690 O GLY A 83 7.482 73.306 85.249 1.00 28.55 ATOM 691 N TYR A 84 9.548 72.608 84.687 1.00 91.39 ATOM 692 CA TYR A 84 9.351 71.314 85.288 1.00 91.39 ATOM 693 C TYR A 84 9.043 71.492 86.740 1.00 91.39 ATOM 694 O TYR A 84 8.246 70.747 87.310 1.00 91.39 ATOM 695 CB TYR A 84 10.580 70.385 85.213 1.00 91.39 ATOM 696 CG TYR A 84 10.869 70.058 83.787 1.00 91.39 ATOM 697 CD1 TYR A 84 9.949 69.382 83.020 1.00 91.39 ATOM 698 CD2 TYR A 84 12.080 70.391 83.228 1.00 91.39 ATOM 699 CE1 TYR A 84 10.222 69.071 81.708 1.00 91.39 ATOM 700 CE2 TYR A 84 12.360 70.081 81.918 1.00 91.39 ATOM 701 CZ TYR A 84 11.428 69.423 81.154 1.00 91.39 ATOM 702 OH TYR A 84 11.712 69.106 79.808 1.00 91.39 ATOM 703 N TYR A 85 9.760 72.432 87.380 1.00108.34 ATOM 704 CA TYR A 85 9.649 72.827 88.757 1.00108.34 ATOM 705 C TYR A 85 8.451 73.703 89.014 1.00108.34 ATOM 706 O TYR A 85 7.972 73.773 90.144 1.00108.34 ATOM 707 CB TYR A 85 10.946 73.468 89.278 1.00108.34 ATOM 708 CG TYR A 85 11.935 72.350 89.215 1.00108.34 ATOM 709 CD1 TYR A 85 11.905 71.355 90.166 1.00108.34 ATOM 710 CD2 TYR A 85 12.878 72.281 88.213 1.00108.34 ATOM 711 CE1 TYR A 85 12.799 70.313 90.122 1.00108.34 ATOM 712 CE2 TYR A 85 13.776 71.239 88.165 1.00108.34 ATOM 713 CZ TYR A 85 13.738 70.252 89.121 1.00108.34 ATOM 714 OH TYR A 85 14.655 69.180 89.079 1.00108.34 ATOM 715 N ASN A 86 7.946 74.430 87.995 1.00 78.38 ATOM 716 CA ASN A 86 6.860 75.351 88.208 1.00 78.38 ATOM 717 C ASN A 86 7.397 76.500 88.996 1.00 78.38 ATOM 718 O ASN A 86 6.699 77.108 89.806 1.00 78.38 ATOM 719 CB ASN A 86 5.679 74.738 88.982 1.00 78.38 ATOM 720 CG ASN A 86 4.992 73.731 88.071 1.00 78.38 ATOM 721 OD1 ASN A 86 4.312 72.816 88.532 1.00 78.38 ATOM 722 ND2 ASN A 86 5.181 73.900 86.735 1.00 78.38 ATOM 723 N GLN A 87 8.682 76.824 88.751 1.00 54.92 ATOM 724 CA GLN A 87 9.337 77.915 89.411 1.00 54.92 ATOM 725 C GLN A 87 9.030 79.180 88.670 1.00 54.92 ATOM 726 O GLN A 87 8.690 79.160 87.488 1.00 54.92 ATOM 727 CB GLN A 87 10.858 77.722 89.490 1.00 54.92 ATOM 728 CG GLN A 87 11.223 76.509 90.347 1.00 54.92 ATOM 729 CD GLN A 87 12.708 76.231 90.192 1.00 54.92 ATOM 730 OE1 GLN A 87 13.277 76.420 89.120 1.00 54.92 ATOM 731 NE2 GLN A 87 13.352 75.758 91.292 1.00 54.92 ATOM 732 N SER A 88 9.127 80.325 89.376 1.00 70.77 ATOM 733 CA SER A 88 8.817 81.605 88.806 1.00 70.77 ATOM 734 C SER A 88 9.930 82.044 87.906 1.00 70.77 ATOM 735 O SER A 88 11.065 81.583 88.008 1.00 70.77 ATOM 736 CB SER A 88 8.600 82.698 89.864 1.00 70.77 ATOM 737 OG SER A 88 8.288 83.934 89.240 1.00 70.77 ATOM 738 N GLU A 89 9.593 82.961 86.980 1.00 63.87 ATOM 739 CA GLU A 89 10.490 83.519 86.006 1.00 63.87 ATOM 740 C GLU A 89 11.497 84.405 86.678 1.00 63.87 ATOM 741 O GLU A 89 12.569 84.666 86.134 1.00 63.87 ATOM 742 CB GLU A 89 9.764 84.318 84.911 1.00 63.87 ATOM 743 CG GLU A 89 8.951 83.418 83.975 1.00 63.87 ATOM 744 CD GLU A 89 8.322 84.290 82.898 1.00 63.87 ATOM 745 OE1 GLU A 89 7.326 84.999 83.206 1.00 63.87 ATOM 746 OE2 GLU A 89 8.840 84.261 81.749 1.00 63.87 ATOM 747 N ALA A 90 11.150 84.933 87.862 1.00 43.07 ATOM 748 CA ALA A 90 11.960 85.880 88.578 1.00 43.07 ATOM 749 C ALA A 90 13.297 85.343 89.020 1.00 43.07 ATOM 750 O ALA A 90 14.283 86.076 88.971 1.00 43.07 ATOM 751 CB ALA A 90 11.258 86.422 89.835 1.00 43.07 ATOM 752 N GLY A 91 13.390 84.077 89.475 1.00 31.07 ATOM 753 CA GLY A 91 14.621 83.603 90.066 1.00 31.07 ATOM 754 C GLY A 91 15.663 83.238 89.049 1.00 31.07 ATOM 755 O GLY A 91 15.381 83.038 87.868 1.00 31.07 ATOM 756 N SER A 92 16.924 83.116 89.528 1.00 41.16 ATOM 757 CA SER A 92 18.030 82.744 88.694 1.00 41.16 ATOM 758 C SER A 92 18.362 81.324 89.029 1.00 41.16 ATOM 759 O SER A 92 18.278 80.916 90.187 1.00 41.16 ATOM 760 CB SER A 92 19.301 83.580 88.921 1.00 41.16 ATOM 761 OG SER A 92 19.063 84.934 88.570 1.00 41.16 ATOM 762 N HIS A 93 18.741 80.525 88.010 1.00 56.37 ATOM 763 CA HIS A 93 18.993 79.136 88.255 1.00 56.37 ATOM 764 C HIS A 93 20.206 78.724 87.491 1.00 56.37 ATOM 765 O HIS A 93 20.616 79.391 86.541 1.00 56.37 ATOM 766 CB HIS A 93 17.828 78.244 87.808 1.00 56.37 ATOM 767 CG HIS A 93 16.579 78.563 88.574 1.00 56.37 ATOM 768 ND1 HIS A 93 15.667 79.525 88.203 1.00 56.37 ATOM 769 CD2 HIS A 93 16.104 78.026 89.731 1.00 56.37 ATOM 770 CE1 HIS A 93 14.694 79.526 89.149 1.00 56.37 ATOM 771 NE2 HIS A 93 14.916 78.634 90.096 1.00 56.37 ATOM 772 N ILE A 94 20.824 77.599 87.910 1.00 48.84 ATOM 773 CA ILE A 94 22.021 77.144 87.269 1.00 48.84 ATOM 774 C ILE A 94 21.898 75.691 86.930 1.00 48.84 ATOM 775 O ILE A 94 21.379 74.895 87.711 1.00 48.84 ATOM 776 CB ILE A 94 23.245 77.280 88.133 1.00 48.84 ATOM 777 CG1 ILE A 94 23.525 78.759 88.454 1.00 48.84 ATOM 778 CG2 ILE A 94 24.412 76.564 87.433 1.00 48.84 ATOM 779 CD1 ILE A 94 24.597 78.959 89.524 1.00 48.84 ATOM 780 N ILE A 95 22.368 75.324 85.719 1.00 49.99 ATOM 781 CA ILE A 95 22.440 73.948 85.315 1.00 49.99 ATOM 782 C ILE A 95 23.895 73.672 85.104 1.00 49.99 ATOM 783 O ILE A 95 24.600 74.468 84.486 1.00 49.99 ATOM 784 CB ILE A 95 21.731 73.644 84.026 1.00 49.99 ATOM 785 CG1 ILE A 95 20.219 73.883 84.175 1.00 49.99 ATOM 786 CG2 ILE A 95 22.091 72.208 83.612 1.00 49.99 ATOM 787 CD1 ILE A 95 19.460 73.834 82.851 1.00 49.99 ATOM 788 N GLN A 96 24.394 72.548 85.655 1.00 47.40 ATOM 789 CA GLN A 96 25.786 72.236 85.502 1.00 47.40 ATOM 790 C GLN A 96 25.896 70.843 84.973 1.00 47.40 ATOM 791 O GLN A 96 25.100 69.969 85.313 1.00 47.40 ATOM 792 CB GLN A 96 26.566 72.351 86.821 1.00 47.40 ATOM 793 CG GLN A 96 26.626 73.801 87.312 1.00 47.40 ATOM 794 CD GLN A 96 27.317 73.844 88.663 1.00 47.40 ATOM 795 OE1 GLN A 96 27.532 72.811 89.295 1.00 47.40 ATOM 796 NE2 GLN A 96 27.665 75.073 89.129 1.00 47.40 ATOM 797 N ARG A 97 26.880 70.610 84.083 1.00 79.97 ATOM 798 CA ARG A 97 27.038 69.301 83.527 1.00 79.97 ATOM 799 C ARG A 97 28.498 69.008 83.435 1.00 79.97 ATOM 800 O ARG A 97 29.306 69.887 83.141 1.00 79.97 ATOM 801 CB ARG A 97 26.458 69.188 82.107 1.00 79.97 ATOM 802 CG ARG A 97 26.416 67.766 81.547 1.00 79.97 ATOM 803 CD ARG A 97 25.831 67.710 80.135 1.00 79.97 ATOM 804 NE ARG A 97 25.574 66.279 79.805 1.00 79.97 ATOM 805 CZ ARG A 97 24.563 65.959 78.947 1.00 79.97 ATOM 806 NH1 ARG A 97 23.815 66.950 78.377 1.00 79.97 ATOM 807 NH2 ARG A 97 24.294 64.651 78.662 1.00 79.97 ATOM 808 N MET A 98 28.881 67.748 83.712 1.00133.72 ATOM 809 CA MET A 98 30.261 67.396 83.575 1.00133.72 ATOM 810 C MET A 98 30.320 66.055 82.924 1.00133.72 ATOM 811 O MET A 98 29.531 65.170 83.251 1.00133.72 ATOM 812 CB MET A 98 31.022 67.303 84.905 1.00133.72 ATOM 813 CG MET A 98 30.628 66.106 85.767 1.00133.72 ATOM 814 SD MET A 98 31.680 65.912 87.232 1.00133.72 ATOM 815 CE MET A 98 33.198 65.716 86.256 1.00133.72 ATOM 816 N TYR A 99 31.239 65.883 81.949 1.00 64.74 ATOM 817 CA TYR A 99 31.373 64.602 81.317 1.00 64.74 ATOM 818 C TYR A 99 32.812 64.368 80.984 1.00 64.74 ATOM 819 O TYR A 99 33.610 65.304 80.932 1.00 64.74 ATOM 820 CB TYR A 99 30.546 64.442 80.025 1.00 64.74 ATOM 821 CG TYR A 99 31.007 65.418 78.996 1.00 64.74 ATOM 822 CD1 TYR A 99 30.578 66.725 79.030 1.00 64.74 ATOM 823 CD2 TYR A 99 31.856 65.021 77.988 1.00 64.74 ATOM 824 CE1 TYR A 99 30.995 67.626 78.079 1.00 64.74 ATOM 825 CE2 TYR A 99 32.277 65.917 77.033 1.00 64.74 ATOM 826 CZ TYR A 99 31.846 67.221 77.078 1.00 64.74 ATOM 827 OH TYR A 99 32.275 68.143 76.100 1.00 64.74 ATOM 828 N GLY A 100 33.190 63.088 80.769 1.00 31.57 ATOM 829 CA GLY A 100 34.552 62.828 80.403 1.00 31.57 ATOM 830 C GLY A 100 34.870 61.379 80.563 1.00 31.57 ATOM 831 O GLY A 100 34.020 60.569 80.932 1.00 31.57 ATOM 832 N CYS A 101 36.147 61.034 80.290 1.00 54.90 ATOM 833 CA CYS A 101 36.584 59.667 80.313 1.00 54.90 ATOM 834 C CYS A 101 37.767 59.506 81.231 1.00 54.90 ATOM 835 O CYS A 101 38.543 60.438 81.441 1.00 54.90 ATOM 836 CB CYS A 101 36.956 59.146 78.902 1.00 54.90 ATOM 837 SG CYS A 101 38.132 60.215 78.011 1.00 54.90 ATOM 838 N ASP A 102 37.900 58.295 81.824 1.00 63.51 ATOM 839 CA ASP A 102 38.963 57.948 82.733 1.00 63.51 ATOM 840 C ASP A 102 39.770 56.856 82.099 1.00 63.51 ATOM 841 O ASP A 102 39.210 55.898 81.564 1.00 63.51 ATOM 842 CB ASP A 102 38.465 57.335 84.057 1.00 63.51 ATOM 843 CG ASP A 102 37.674 58.368 84.841 1.00 63.51 ATOM 844 OD1 ASP A 102 37.679 59.560 84.437 1.00 63.51 ATOM 845 OD2 ASP A 102 37.048 57.970 85.861 1.00 63.51 ATOM 846 N LEU A 103 41.114 56.974 82.134 1.00103.09 ATOM 847 CA LEU A 103 41.939 55.932 81.586 1.00103.09 ATOM 848 C LEU A 103 42.865 55.432 82.653 1.00103.09 ATOM 849 O LEU A 103 43.223 56.160 83.577 1.00103.09 ATOM 850 CB LEU A 103 42.784 56.365 80.377 1.00103.09 ATOM 851 CG LEU A 103 41.916 56.821 79.190 1.00103.09 ATOM 852 CD1 LEU A 103 41.234 58.161 79.488 1.00103.09 ATOM 853 CD2 LEU A 103 42.692 56.831 77.873 1.00103.09 ATOM 854 N GLY A 104 43.239 54.138 82.561 1.00 28.34 ATOM 855 CA GLY A 104 44.143 53.537 83.505 1.00 28.34 ATOM 856 C GLY A 104 45.535 53.720 82.977 1.00 28.34 ATOM 857 O GLY A 104 45.741 54.256 81.888 1.00 28.34 ATOM 858 N PRO A 105 46.494 53.249 83.732 1.00146.98 ATOM 859 CA PRO A 105 47.890 53.373 83.400 1.00146.98 ATOM 860 C PRO A 105 48.169 52.801 82.039 1.00146.98 ATOM 861 O PRO A 105 49.091 53.277 81.378 1.00146.98 ATOM 862 CB PRO A 105 48.632 52.604 84.490 1.00146.98 ATOM 863 CG PRO A 105 47.620 51.521 84.906 1.00146.98 ATOM 864 CD PRO A 105 46.252 52.190 84.698 1.00146.98 ATOM 865 N ASP A 106 47.425 51.755 81.625 1.00 58.04 ATOM 866 CA ASP A 106 47.607 51.142 80.339 1.00 58.04 ATOM 867 C ASP A 106 47.144 52.089 79.274 1.00 58.04 ATOM 868 O ASP A 106 47.628 52.045 78.144 1.00 58.04 ATOM 869 CB ASP A 106 46.887 49.785 80.176 1.00 58.04 ATOM 870 CG ASP A 106 45.377 49.936 80.320 1.00 58.04 ATOM 871 OD1 ASP A 106 44.930 50.856 81.055 1.00 58.04 ATOM 872 OD2 ASP A 106 44.650 49.119 79.696 1.00 58.04 ATOM 873 N GLY A 107 46.187 52.980 79.606 1.00 29.83 ATOM 874 CA GLY A 107 45.681 53.911 78.636 1.00 29.83 ATOM 875 C GLY A 107 44.336 53.439 78.163 1.00 29.83 ATOM 876 O GLY A 107 43.755 54.023 77.249 1.00 29.83 ATOM 877 N ARG A 108 43.813 52.353 78.770 1.00147.72 ATOM 878 CA ARG A 108 42.524 51.821 78.409 1.00147.72 ATOM 879 C ARG A 108 41.461 52.591 79.137 1.00147.72 ATOM 880 O ARG A 108 41.715 53.166 80.193 1.00147.72 ATOM 881 CB ARG A 108 42.361 50.340 78.788 1.00147.72 ATOM 882 CG ARG A 108 41.044 49.718 78.329 1.00147.72 ATOM 883 CD ARG A 108 40.894 48.250 78.737 1.00147.72 ATOM 884 NE ARG A 108 40.128 48.222 80.014 1.00147.72 ATOM 885 CZ ARG A 108 40.779 48.338 81.209 1.00147.72 ATOM 886 NH1 ARG A 108 42.138 48.452 81.236 1.00147.72 ATOM 887 NH2 ARG A 108 40.069 48.337 82.374 1.00147.72 ATOM 888 N LEU A 109 40.229 52.614 78.582 1.00 81.45 ATOM 889 CA LEU A 109 39.151 53.358 79.176 1.00 81.45 ATOM 890 C LEU A 109 38.616 52.609 80.359 1.00 81.45 ATOM 891 O LEU A 109 38.051 51.525 80.218 1.00 81.45 ATOM 892 CB LEU A 109 37.992 53.597 78.191 1.00 81.45 ATOM 893 CG LEU A 109 36.828 54.408 78.785 1.00 81.45 ATOM 894 CD1 LEU A 109 37.276 55.836 79.135 1.00 81.45 ATOM 895 CD2 LEU A 109 35.601 54.384 77.855 1.00 81.45 ATOM 896 N LEU A 110 38.855 53.144 81.576 1.00107.07 ATOM 897 CA LEU A 110 38.303 52.572 82.773 1.00107.07 ATOM 898 C LEU A 110 36.833 52.846 82.881 1.00107.07 ATOM 899 O LEU A 110 36.049 51.923 83.091 1.00107.07 ATOM 900 CB LEU A 110 38.977 53.077 84.061 1.00107.07 ATOM 901 CG LEU A 110 40.298 52.354 84.369 1.00107.07 ATOM 902 CD1 LEU A 110 40.027 50.954 84.941 1.00107.07 ATOM 903 CD2 LEU A 110 41.194 52.284 83.127 1.00107.07 ATOM 904 N ARG A 111 36.415 54.122 82.720 1.00246.49 ATOM 905 CA ARG A 111 35.022 54.461 82.875 1.00246.49 ATOM 906 C ARG A 111 34.739 55.728 82.138 1.00246.49 ATOM 907 O ARG A 111 35.646 56.476 81.783 1.00246.49 ATOM 908 CB ARG A 111 34.593 54.892 84.284 1.00246.49 ATOM 909 CG ARG A 111 34.365 53.819 85.330 1.00246.49 ATOM 910 CD ARG A 111 33.453 54.358 86.430 1.00246.49 ATOM 911 NE ARG A 111 32.114 54.559 85.800 1.00246.49 ATOM 912 CZ ARG A 111 31.201 55.413 86.348 1.00246.49 ATOM 913 NH1 ARG A 111 31.560 56.211 87.392 1.00246.49 ATOM 914 NH2 ARG A 111 29.936 55.475 85.839 1.00246.49 ATOM 915 N GLY A 112 33.432 56.010 81.949 1.00 34.90 ATOM 916 CA GLY A 112 32.984 57.218 81.316 1.00 34.90 ATOM 917 C GLY A 112 32.045 57.884 82.275 1.00 34.90 ATOM 918 O GLY A 112 31.458 57.224 83.132 1.00 34.90 ATOM 919 N HIS A 113 31.873 59.219 82.152 1.00 75.07 ATOM 920 CA HIS A 113 31.018 59.899 83.082 1.00 75.07 ATOM 921 C HIS A 113 30.200 60.928 82.360 1.00 75.07 ATOM 922 O HIS A 113 30.633 61.508 81.366 1.00 75.07 ATOM 923 CB HIS A 113 31.808 60.641 84.173 1.00 75.07 ATOM 924 CG HIS A 113 32.731 59.734 84.934 1.00 75.07 ATOM 925 ND1 HIS A 113 32.396 59.079 86.097 1.00 75.07 ATOM 926 CD2 HIS A 113 34.014 59.372 84.662 1.00 75.07 ATOM 927 CE1 HIS A 113 33.486 58.359 86.468 1.00 75.07 ATOM 928 NE2 HIS A 113 34.492 58.505 85.627 1.00 75.07 ATOM 929 N ASP A 114 28.956 61.143 82.843 1.00 71.77 ATOM 930 CA ASP A 114 28.078 62.165 82.338 1.00 71.77 ATOM 931 C ASP A 114 27.115 62.473 83.449 1.00 71.77 ATOM 932 O ASP A 114 26.261 61.647 83.770 1.00 71.77 ATOM 933 CB ASP A 114 27.232 61.723 81.133 1.00 71.77 ATOM 934 CG ASP A 114 26.490 62.948 80.619 1.00 71.77 ATOM 935 OD1 ASP A 114 27.139 64.021 80.485 1.00 71.77 ATOM 936 OD2 ASP A 114 25.259 62.832 80.380 1.00 71.77 ATOM 937 N GLN A 115 27.224 63.668 84.068 1.00 51.57 ATOM 938 CA GLN A 115 26.358 63.975 85.174 1.00 51.57 ATOM 939 C GLN A 115 25.845 65.378 85.040 1.00 51.57 ATOM 940 O GLN A 115 26.497 66.236 84.446 1.00 51.57 ATOM 941 CB GLN A 115 27.074 63.875 86.530 1.00 51.57 ATOM 942 CG GLN A 115 27.569 62.458 86.830 1.00 51.57 ATOM 943 CD GLN A 115 28.262 62.469 88.182 1.00 51.57 ATOM 944 OE1 GLN A 115 29.457 62.184 88.282 1.00 51.57 ATOM 945 NE2 GLN A 115 27.496 62.810 89.251 1.00 51.57 ATOM 946 N SER A 116 24.638 65.644 85.592 1.00 31.24 ATOM 947 CA SER A 116 24.080 66.968 85.527 1.00 31.24 ATOM 948 C SER A 116 23.469 67.306 86.854 1.00 31.24 ATOM 949 O SER A 116 23.018 66.424 87.584 1.00 31.24 ATOM 950 CB SER A 116 22.970 67.124 84.471 1.00 31.24 ATOM 951 OG SER A 116 23.505 66.943 83.167 1.00 31.24 ATOM 952 N ALA A 117 23.452 68.616 87.192 1.00 28.54 ATOM 953 CA ALA A 117 22.892 69.084 88.432 1.00 28.54 ATOM 954 C ALA A 117 22.113 70.335 88.151 1.00 28.54 ATOM 955 O ALA A 117 22.429 71.088 87.230 1.00 28.54 ATOM 956 CB ALA A 117 23.953 69.451 89.485 1.00 28.54 ATOM 957 N TYR A 118 21.050 70.572 88.950 1.00 70.33 ATOM 958 CA TYR A 118 20.236 71.747 88.810 1.00 70.33 ATOM 959 C TYR A 118 20.254 72.434 90.142 1.00 70.33 ATOM 960 O TYR A 118 19.886 71.853 91.161 1.00 70.33 ATOM 961 CB TYR A 118 18.779 71.389 88.449 1.00 70.33 ATOM 962 CG TYR A 118 17.956 72.620 88.274 1.00 70.33 ATOM 963 CD1 TYR A 118 18.125 73.419 87.168 1.00 70.33 ATOM 964 CD2 TYR A 118 16.992 72.957 89.196 1.00 70.33 ATOM 965 CE1 TYR A 118 17.364 74.550 86.992 1.00 70.33 ATOM 966 CE2 TYR A 118 16.226 74.086 89.026 1.00 70.33 ATOM 967 CZ TYR A 118 16.413 74.884 87.924 1.00 70.33 ATOM 968 OH TYR A 118 15.627 76.040 87.747 1.00 70.33 ATOM 969 N ASP A 119 20.702 73.703 90.164 1.00 54.75 ATOM 970 CA ASP A 119 20.767 74.459 91.382 1.00 54.75 ATOM 971 C ASP A 119 21.591 73.723 92.398 1.00 54.75 ATOM 972 O ASP A 119 21.352 73.842 93.600 1.00 54.75 ATOM 973 CB ASP A 119 19.384 74.762 91.990 1.00 54.75 ATOM 974 CG ASP A 119 18.707 75.818 91.125 1.00 54.75 ATOM 975 OD1 ASP A 119 19.437 76.651 90.525 1.00 54.75 ATOM 976 OD2 ASP A 119 17.450 75.803 91.052 1.00 54.75 ATOM 977 N GLY A 120 22.599 72.952 91.943 1.00 28.33 ATOM 978 CA GLY A 120 23.513 72.330 92.862 1.00 28.33 ATOM 979 C GLY A 120 23.050 70.974 93.309 1.00 28.33 ATOM 980 O GLY A 120 23.713 70.352 94.139 1.00 28.33 ATOM 981 N LYS A 121 21.914 70.464 92.796 1.00107.59 ATOM 982 CA LYS A 121 21.503 69.151 93.219 1.00107.59 ATOM 983 C LYS A 121 21.539 68.229 92.037 1.00107.59 ATOM 984 O LYS A 121 21.228 68.630 90.918 1.00107.59 ATOM 985 CB LYS A 121 20.089 69.097 93.820 1.00107.59 ATOM 986 CG LYS A 121 20.044 69.552 95.280 1.00107.59 ATOM 987 CD LYS A 121 20.383 71.026 95.494 1.00107.59 ATOM 988 CE LYS A 121 20.463 71.419 96.970 1.00107.59 ATOM 989 NZ LYS A 121 21.736 70.939 97.551 1.00107.59 ATOM 990 N ASP A 122 21.926 66.954 92.264 1.00122.80 ATOM 991 CA ASP A 122 22.074 66.015 91.182 1.00122.80 ATOM 992 C ASP A 122 20.747 65.740 90.540 1.00122.80 ATOM 993 O ASP A 122 19.815 65.266 91.190 1.00122.80 ATOM 994 CB ASP A 122 22.711 64.678 91.602 1.00122.80 ATOM 995 CG ASP A 122 21.798 64.001 92.609 1.00122.80 ATOM 996 OD1 ASP A 122 21.362 64.684 93.573 1.00122.80 ATOM 997 OD2 ASP A 122 21.535 62.782 92.431 1.00122.80 ATOM 998 N TYR A 123 20.613 66.173 89.265 1.00112.90 ATOM 999 CA TYR A 123 19.462 66.007 88.416 1.00112.90 ATOM 1000 C TYR A 123 19.382 64.677 87.706 1.00112.90 ATOM 1001 O TYR A 123 18.404 63.944 87.846 1.00112.90 ATOM 1002 CB TYR A 123 19.476 67.123 87.353 1.00112.90 ATOM 1003 CG TYR A 123 18.210 67.190 86.573 1.00112.90 ATOM 1004 CD1 TYR A 123 17.103 67.808 87.105 1.00112.90 ATOM 1005 CD2 TYR A 123 18.138 66.670 85.303 1.00112.90 ATOM 1006 CE1 TYR A 123 15.934 67.897 86.387 1.00112.90 ATOM 1007 CE2 TYR A 123 16.972 66.753 84.579 1.00112.90 ATOM 1008 CZ TYR A 123 15.866 67.364 85.123 1.00112.90 ATOM 1009 OH TYR A 123 14.668 67.453 84.382 1.00112.90 ATOM 1010 N ILE A 124 20.431 64.324 86.922 1.00129.58 ATOM 1011 CA ILE A 124 20.364 63.122 86.129 1.00129.58 ATOM 1012 C ILE A 124 21.773 62.695 85.832 1.00129.58 ATOM 1013 O ILE A 124 22.661 63.532 85.671 1.00129.58 ATOM 1014 CB ILE A 124 19.620 63.357 84.835 1.00129.58 ATOM 1015 CG1 ILE A 124 19.123 62.054 84.175 1.00129.58 ATOM 1016 CG2 ILE A 124 20.524 64.210 83.930 1.00129.58 ATOM 1017 CD1 ILE A 124 20.215 61.163 83.597 1.00129.58 ATOM 1018 N ALA A 125 22.027 61.373 85.755 1.00 38.12 ATOM 1019 CA ALA A 125 23.367 60.950 85.473 1.00 38.12 ATOM 1020 C ALA A 125 23.328 59.720 84.626 1.00 38.12 ATOM 1021 O ALA A 125 22.415 58.902 84.725 1.00 38.12 ATOM 1022 CB ALA A 125 24.169 60.597 86.737 1.00 38.12 ATOM 1023 N LEU A 126 24.331 59.582 83.737 1.00 51.70 ATOM 1024 CA LEU A 126 24.433 58.406 82.924 1.00 51.70 ATOM 1025 C LEU A 126 25.038 57.352 83.800 1.00 51.70 ATOM 1026 O LEU A 126 25.975 57.621 84.550 1.00 51.70 ATOM 1027 CB LEU A 126 25.331 58.614 81.692 1.00 51.70 ATOM 1028 CG LEU A 126 25.449 57.387 80.770 1.00 51.70 ATOM 1029 CD1 LEU A 126 24.085 57.004 80.174 1.00 51.70 ATOM 1030 CD2 LEU A 126 26.514 57.611 79.683 1.00 51.70 ATOM 1031 N ASN A 127 24.512 56.115 83.728 1.00 47.31 ATOM 1032 CA ASN A 127 25.008 55.050 84.551 1.00 47.31 ATOM 1033 C ASN A 127 26.323 54.602 83.999 1.00 47.31 ATOM 1034 O ASN A 127 26.718 54.982 82.899 1.00 47.31 ATOM 1035 CB ASN A 127 24.080 53.826 84.615 1.00 47.31 ATOM 1036 CG ASN A 127 22.856 54.226 85.423 1.00 47.31 ATOM 1037 OD1 ASN A 127 22.860 55.245 86.110 1.00 47.31 ATOM 1038 ND2 ASN A 127 21.782 53.396 85.356 1.00 47.31 ATOM 1039 N GLU A 128 27.029 53.760 84.776 1.00 59.26 ATOM 1040 CA GLU A 128 28.344 53.288 84.450 1.00 59.26 ATOM 1041 C GLU A 128 28.281 52.519 83.168 1.00 59.26 ATOM 1042 O GLU A 128 29.251 52.478 82.414 1.00 59.26 ATOM 1043 CB GLU A 128 28.934 52.373 85.537 1.00 59.26 ATOM 1044 CG GLU A 128 30.423 52.079 85.347 1.00 59.26 ATOM 1045 CD GLU A 128 30.872 51.219 86.519 1.00 59.26 ATOM 1046 OE1 GLU A 128 30.219 50.170 86.759 1.00 59.26 ATOM 1047 OE2 GLU A 128 31.865 51.603 87.194 1.00 59.26 ATOM 1048 N ASP A 129 27.131 51.875 82.898 1.00 70.71 ATOM 1049 CA ASP A 129 26.939 51.079 81.719 1.00 70.71 ATOM 1050 C ASP A 129 26.999 51.931 80.480 1.00 70.71 ATOM 1051 O ASP A 129 27.235 51.413 79.390 1.00 70.71 ATOM 1052 CB ASP A 129 25.632 50.257 81.740 1.00 70.71 ATOM 1053 CG ASP A 129 24.420 51.169 81.847 1.00 70.71 ATOM 1054 OD1 ASP A 129 24.590 52.415 81.823 1.00 70.71 ATOM 1055 OD2 ASP A 129 23.293 50.619 81.968 1.00 70.71 ATOM 1056 N LEU A 130 26.752 53.251 80.606 1.00 84.42 ATOM 1057 CA LEU A 130 26.796 54.157 79.490 1.00 84.42 ATOM 1058 C LEU A 130 25.582 53.921 78.647 1.00 84.42 ATOM 1059 O LEU A 130 25.445 54.508 77.574 1.00 84.42 ATOM 1060 CB LEU A 130 28.034 53.944 78.602 1.00 84.42 ATOM 1061 CG LEU A 130 29.366 54.185 79.339 1.00 84.42 ATOM 1062 CD1 LEU A 130 30.571 54.000 78.401 1.00 84.42 ATOM 1063 CD2 LEU A 130 29.364 55.542 80.063 1.00 84.42 ATOM 1064 N SER A 131 24.729 52.967 79.072 1.00 88.23 ATOM 1065 CA SER A 131 23.493 52.654 78.407 1.00 88.23 ATOM 1066 C SER A 131 22.264 53.269 79.030 1.00 88.23 ATOM 1067 O SER A 131 21.307 53.572 78.319 1.00 88.23 ATOM 1068 CB SER A 131 23.256 51.139 78.334 1.00 88.23 ATOM 1069 OG SER A 131 24.313 50.528 77.608 1.00 88.23 ATOM 1070 N SER A 132 22.232 53.468 80.371 1.00 53.20 ATOM 1071 CA SER A 132 20.982 53.839 80.998 1.00 53.20 ATOM 1072 C SER A 132 21.150 55.053 81.863 1.00 53.20 ATOM 1073 O SER A 132 22.263 55.535 82.068 1.00 53.20 ATOM 1074 CB SER A 132 20.399 52.716 81.870 1.00 53.20 ATOM 1075 OG SER A 132 21.320 52.376 82.895 1.00 53.20 ATOM 1076 N TRP A 133 20.022 55.584 82.398 1.00 74.36 ATOM 1077 CA TRP A 133 20.078 56.823 83.128 1.00 74.36 ATOM 1078 C TRP A 133 19.484 56.659 84.495 1.00 74.36 ATOM 1079 O TRP A 133 18.656 55.781 84.736 1.00 74.36 ATOM 1080 CB TRP A 133 19.254 57.933 82.453 1.00 74.36 ATOM 1081 CG TRP A 133 19.639 58.202 81.019 1.00 74.36 ATOM 1082 CD1 TRP A 133 19.086 57.689 79.883 1.00 74.36 ATOM 1083 CD2 TRP A 133 20.705 59.068 80.596 1.00 74.36 ATOM 1084 NE1 TRP A 133 19.740 58.177 78.778 1.00 74.36 ATOM 1085 CE2 TRP A 133 20.739 59.028 79.202 1.00 74.36 ATOM 1086 CE3 TRP A 133 21.585 59.830 81.309 1.00 74.36 ATOM 1087 CZ2 TRP A 133 21.658 59.750 78.497 1.00 74.36 ATOM 1088 CZ3 TRP A 133 22.508 60.563 80.594 1.00 74.36 ATOM 1089 CH2 TRP A 133 22.543 60.523 79.215 1.00 74.36 ATOM 1090 N THR A 134 19.938 57.513 85.440 1.00 44.64 ATOM 1091 CA THR A 134 19.391 57.574 86.767 1.00 44.64 ATOM 1092 C THR A 134 18.846 58.965 86.917 1.00 44.64 ATOM 1093 O THR A 134 19.597 59.938 86.846 1.00 44.64 ATOM 1094 CB THR A 134 20.416 57.388 87.850 1.00 44.64 ATOM 1095 OG1 THR A 134 21.045 56.122 87.722 1.00 44.64 ATOM 1096 CG2 THR A 134 19.725 57.502 89.219 1.00 44.64 ATOM 1097 N ALA A 135 17.519 59.090 87.137 1.00 35.10 ATOM 1098 CA ALA A 135 16.904 60.387 87.250 1.00 35.10 ATOM 1099 C ALA A 135 16.525 60.615 88.682 1.00 35.10 ATOM 1100 O ALA A 135 15.964 59.742 89.341 1.00 35.10 ATOM 1101 CB ALA A 135 15.622 60.534 86.411 1.00 35.10 ATOM 1102 N ALA A 136 16.849 61.817 89.201 1.00 45.70 ATOM 1103 CA ALA A 136 16.606 62.168 90.572 1.00 45.70 ATOM 1104 C ALA A 136 15.141 62.256 90.892 1.00 45.70 ATOM 1105 O ALA A 136 14.707 61.743 91.923 1.00 45.70 ATOM 1106 CB ALA A 136 17.236 63.519 90.954 1.00 45.70 ATOM 1107 N ASP A 137 14.333 62.906 90.027 1.00 77.57 ATOM 1108 CA ASP A 137 12.954 63.106 90.378 1.00 77.57 ATOM 1109 C ASP A 137 12.082 63.054 89.158 1.00 77.57 ATOM 1110 O ASP A 137 12.507 62.644 88.080 1.00 77.57 ATOM 1111 CB ASP A 137 12.718 64.439 91.120 1.00 77.57 ATOM 1112 CG ASP A 137 13.191 65.608 90.260 1.00 77.57 ATOM 1113 OD1 ASP A 137 13.516 65.390 89.064 1.00 77.57 ATOM 1114 OD2 ASP A 137 13.243 66.744 90.804 1.00 77.57 ATOM 1115 N THR A 138 10.810 63.471 89.327 1.00 97.43 ATOM 1116 CA THR A 138 9.818 63.435 88.291 1.00 97.43 ATOM 1117 C THR A 138 10.212 64.338 87.161 1.00 97.43 ATOM 1118 O THR A 138 9.972 64.013 86.000 1.00 97.43 ATOM 1119 CB THR A 138 8.464 63.867 88.772 1.00 97.43 ATOM 1120 OG1 THR A 138 7.497 63.666 87.752 1.00 97.43 ATOM 1121 CG2 THR A 138 8.521 65.349 89.169 1.00 97.43 ATOM 1122 N ALA A 139 10.791 65.515 87.468 1.00 35.67 ATOM 1123 CA ALA A 139 11.191 66.437 86.440 1.00 35.67 ATOM 1124 C ALA A 139 12.275 65.814 85.609 1.00 35.67 ATOM 1125 O ALA A 139 12.257 65.885 84.381 1.00 35.67 ATOM 1126 CB ALA A 139 11.743 67.759 87.002 1.00 35.67 ATOM 1127 N ALA A 140 13.237 65.148 86.269 1.00 41.10 ATOM 1128 CA ALA A 140 14.361 64.537 85.611 1.00 41.10 ATOM 1129 C ALA A 140 13.859 63.487 84.670 1.00 41.10 ATOM 1130 O ALA A 140 14.475 63.221 83.639 1.00 41.10 ATOM 1131 CB ALA A 140 15.335 63.858 86.590 1.00 41.10 ATOM 1132 N GLN A 141 12.730 62.848 85.021 1.00 45.27 ATOM 1133 CA GLN A 141 12.149 61.793 84.239 1.00 45.27 ATOM 1134 C GLN A 141 11.821 62.320 82.873 1.00 45.27 ATOM 1135 O GLN A 141 11.953 61.605 81.882 1.00 45.27 ATOM 1136 CB GLN A 141 10.840 61.276 84.858 1.00 45.27 ATOM 1137 CG GLN A 141 11.026 60.616 86.227 1.00 45.27 ATOM 1138 CD GLN A 141 9.646 60.359 86.820 1.00 45.27 ATOM 1139 OE1 GLN A 141 8.635 60.824 86.294 1.00 45.27 ATOM 1140 NE2 GLN A 141 9.597 59.607 87.953 1.00 45.27 ATOM 1141 N ILE A 142 11.365 63.584 82.779 1.00100.16 ATOM 1142 CA ILE A 142 11.004 64.160 81.512 1.00100.16 ATOM 1143 C ILE A 142 12.232 64.211 80.657 1.00100.16 ATOM 1144 O ILE A 142 12.209 63.828 79.488 1.00100.16 ATOM 1145 CB ILE A 142 10.565 65.591 81.647 1.00100.16 ATOM 1146 CG1 ILE A 142 9.388 65.732 82.625 1.00100.16 ATOM 1147 CG2 ILE A 142 10.243 66.109 80.235 1.00100.16 ATOM 1148 CD1 ILE A 142 8.097 65.098 82.129 1.00100.16 ATOM 1149 N THR A 143 13.349 64.678 81.242 1.00 37.18 ATOM 1150 CA THR A 143 14.584 64.827 80.529 1.00 37.18 ATOM 1151 C THR A 143 15.017 63.481 80.057 1.00 37.18 ATOM 1152 O THR A 143 15.501 63.332 78.937 1.00 37.18 ATOM 1153 CB THR A 143 15.678 65.378 81.396 1.00 37.18 ATOM 1154 OG1 THR A 143 15.306 66.657 81.888 1.00 37.18 ATOM 1155 CG2 THR A 143 16.975 65.474 80.576 1.00 37.18 ATOM 1156 N GLN A 144 14.840 62.455 80.905 1.00 35.61 ATOM 1157 CA GLN A 144 15.283 61.144 80.548 1.00 35.61 ATOM 1158 C GLN A 144 14.533 60.687 79.337 1.00 35.61 ATOM 1159 O GLN A 144 15.118 60.100 78.429 1.00 35.61 ATOM 1160 CB GLN A 144 15.075 60.113 81.670 1.00 35.61 ATOM 1161 CG GLN A 144 15.553 58.706 81.305 1.00 35.61 ATOM 1162 CD GLN A 144 15.298 57.798 82.499 1.00 35.61 ATOM 1163 OE1 GLN A 144 15.385 58.227 83.649 1.00 35.61 ATOM 1164 NE2 GLN A 144 14.973 56.505 82.223 1.00 35.61 ATOM 1165 N ARG A 145 13.217 60.964 79.275 1.00 54.07 ATOM 1166 CA ARG A 145 12.431 60.499 78.167 1.00 54.07 ATOM 1167 C ARG A 145 12.948 61.117 76.906 1.00 54.07 ATOM 1168 O ARG A 145 13.095 60.436 75.893 1.00 54.07 ATOM 1169 CB ARG A 145 10.947 60.888 78.267 1.00 54.07 ATOM 1170 CG ARG A 145 10.232 60.329 79.498 1.00 54.07 ATOM 1171 CD ARG A 145 8.719 60.555 79.462 1.00 54.07 ATOM 1172 NE ARG A 145 8.499 61.997 79.158 1.00 54.07 ATOM 1173 CZ ARG A 145 7.337 62.612 79.523 1.00 54.07 ATOM 1174 NH1 ARG A 145 6.399 61.939 80.249 1.00 54.07 ATOM 1175 NH2 ARG A 145 7.112 63.910 79.161 1.00 54.07 ATOM 1176 N LYS A 146 13.241 62.431 76.936 1.00 30.19 ATOM 1177 CA LYS A 146 13.683 63.110 75.751 1.00 30.19 ATOM 1178 C LYS A 146 14.995 62.547 75.304 1.00 30.19 ATOM 1179 O LYS A 146 15.214 62.337 74.113 1.00 30.19 ATOM 1180 CB LYS A 146 13.868 64.625 75.947 1.00 30.19 ATOM 1181 CG LYS A 146 12.546 65.382 76.091 1.00 30.19 ATOM 1182 CD LYS A 146 12.709 66.830 76.556 1.00 30.19 ATOM 1183 CE LYS A 146 11.392 67.606 76.615 1.00 30.19 ATOM 1184 NZ LYS A 146 11.644 68.998 77.046 1.00 30.19 ATOM 1185 N TRP A 147 15.905 62.286 76.257 1.00 65.11 ATOM 1186 CA TRP A 147 17.218 61.804 75.942 1.00 65.11 ATOM 1187 C TRP A 147 17.143 60.425 75.362 1.00 65.11 ATOM 1188 O TRP A 147 17.959 60.060 74.517 1.00 65.11 ATOM 1189 CB TRP A 147 18.180 61.869 77.144 1.00 65.11 ATOM 1190 CG TRP A 147 18.547 63.306 77.457 1.00 65.11 ATOM 1191 CD1 TRP A 147 18.076 64.437 76.857 1.00 65.11 ATOM 1192 CD2 TRP A 147 19.492 63.742 78.451 1.00 65.11 ATOM 1193 NE1 TRP A 147 18.665 65.548 77.410 1.00 65.11 ATOM 1194 CE2 TRP A 147 19.539 65.136 78.392 1.00 65.11 ATOM 1195 CE3 TRP A 147 20.259 63.043 79.340 1.00 65.11 ATOM 1196 CZ2 TRP A 147 20.356 65.853 79.220 1.00 65.11 ATOM 1197 CZ3 TRP A 147 21.081 63.770 80.175 1.00 65.11 ATOM 1198 CH2 TRP A 147 21.129 65.148 80.117 1.00 65.11 ATOM 1199 N GLU A 148 16.184 59.605 75.829 1.00 35.05 ATOM 1200 CA GLU A 148 16.027 58.275 75.315 1.00 35.05 ATOM 1201 C GLU A 148 15.599 58.341 73.876 1.00 35.05 ATOM 1202 O GLU A 148 16.096 57.589 73.039 1.00 35.05 ATOM 1203 CB GLU A 148 14.987 57.469 76.115 1.00 35.05 ATOM 1204 CG GLU A 148 15.457 57.180 77.543 1.00 35.05 ATOM 1205 CD GLU A 148 14.373 56.406 78.277 1.00 35.05 ATOM 1206 OE1 GLU A 148 13.181 56.533 77.880 1.00 35.05 ATOM 1207 OE2 GLU A 148 14.719 55.680 79.244 1.00 35.05 ATOM 1208 N ALA A 149 14.665 59.252 73.544 1.00 24.90 ATOM 1209 CA ALA A 149 14.194 59.366 72.191 1.00 24.90 ATOM 1210 C ALA A 149 15.344 59.787 71.324 1.00 24.90 ATOM 1211 O ALA A 149 15.501 59.311 70.200 1.00 24.90 ATOM 1212 CB ALA A 149 13.084 60.418 72.034 1.00 24.90 ATOM 1213 N ALA A 150 16.164 60.711 71.857 1.00 54.82 ATOM 1214 CA ALA A 150 17.320 61.317 71.250 1.00 54.82 ATOM 1215 C ALA A 150 18.404 60.300 71.024 1.00 54.82 ATOM 1216 O ALA A 150 19.214 60.451 70.113 1.00 54.82 ATOM 1217 CB ALA A 150 17.912 62.448 72.109 1.00 54.82 ATOM 1218 N ARG A 151 18.468 59.240 71.856 1.00124.04 ATOM 1219 CA ARG A 151 19.540 58.283 71.760 1.00124.04 ATOM 1220 C ARG A 151 20.799 58.944 72.232 1.00124.04 ATOM 1221 O ARG A 151 21.883 58.715 71.696 1.00124.04 ATOM 1222 CB ARG A 151 19.785 57.776 70.324 1.00124.04 ATOM 1223 CG ARG A 151 18.606 56.999 69.734 1.00124.04 ATOM 1224 CD ARG A 151 18.781 55.479 69.751 1.00124.04 ATOM 1225 NE ARG A 151 17.521 54.879 69.226 1.00124.04 ATOM 1226 CZ ARG A 151 17.329 54.743 67.881 1.00124.04 ATOM 1227 NH1 ARG A 151 18.298 55.143 67.008 1.00124.04 ATOM 1228 NH2 ARG A 151 16.164 54.212 67.407 1.00124.04 ATOM 1229 N VAL A 152 20.667 59.783 73.279 1.00 34.74 ATOM 1230 CA VAL A 152 21.753 60.510 73.878 1.00 34.74 ATOM 1231 C VAL A 152 22.755 59.561 74.476 1.00 34.74 ATOM 1232 O VAL A 152 23.960 59.760 74.341 1.00 34.74 ATOM 1233 CB VAL A 152 21.287 61.424 74.974 1.00 34.74 ATOM 1234 CG1 VAL A 152 22.515 62.065 75.640 1.00 34.74 ATOM 1235 CG2 VAL A 152 20.299 62.441 74.378 1.00 34.74 ATOM 1236 N ALA A 153 22.289 58.498 75.157 1.00 28.16 ATOM 1237 CA ALA A 153 23.192 57.587 75.814 1.00 28.16 ATOM 1238 C ALA A 153 24.073 56.945 74.791 1.00 28.16 ATOM 1239 O ALA A 153 25.266 56.749 75.023 1.00 28.16 ATOM 1240 CB ALA A 153 22.465 56.458 76.564 1.00 28.16 ATOM 1241 N GLU A 154 23.497 56.593 73.629 1.00 33.73 ATOM 1242 CA GLU A 154 24.214 55.933 72.577 1.00 33.73 ATOM 1243 C GLU A 154 25.299 56.843 72.094 1.00 33.73 ATOM 1244 O GLU A 154 26.436 56.417 71.894 1.00 33.73 ATOM 1245 CB GLU A 154 23.286 55.631 71.387 1.00 33.73 ATOM 1246 CG GLU A 154 23.927 54.864 70.231 1.00 33.73 ATOM 1247 CD GLU A 154 22.839 54.683 69.180 1.00 33.73 ATOM 1248 OE1 GLU A 154 21.749 55.292 69.358 1.00 33.73 ATOM 1249 OE2 GLU A 154 23.074 53.938 68.193 1.00 33.73 ATOM 1250 N GLN A 155 24.977 58.137 71.911 1.00 31.74 ATOM 1251 CA GLN A 155 25.934 59.074 71.399 1.00 31.74 ATOM 1252 C GLN A 155 27.062 59.219 72.368 1.00 31.74 ATOM 1253 O GLN A 155 28.226 59.255 71.972 1.00 31.74 ATOM 1254 CB GLN A 155 25.318 60.467 71.166 1.00 31.74 ATOM 1255 CG GLN A 155 24.251 60.464 70.071 1.00 31.74 ATOM 1256 CD GLN A 155 23.706 61.874 69.921 1.00 31.74 ATOM 1257 OE1 GLN A 155 23.220 62.472 70.882 1.00 31.74 ATOM 1258 NE2 GLN A 155 23.786 62.422 68.678 1.00 31.74 ATOM 1259 N LEU A 156 26.745 59.295 73.676 1.00 48.98 ATOM 1260 CA LEU A 156 27.752 59.463 74.690 1.00 48.98 ATOM 1261 C LEU A 156 28.653 58.271 74.725 1.00 48.98 ATOM 1262 O LEU A 156 29.865 58.411 74.875 1.00 48.98 ATOM 1263 CB LEU A 156 27.168 59.630 76.106 1.00 48.98 ATOM 1264 CG LEU A 156 26.499 60.994 76.350 1.00 48.98 ATOM 1265 CD1 LEU A 156 25.939 61.095 77.774 1.00 48.98 ATOM 1266 CD2 LEU A 156 27.469 62.144 76.022 1.00 48.98 ATOM 1267 N ARG A 157 28.085 57.063 74.584 1.00 52.95 ATOM 1268 CA ARG A 157 28.895 55.883 74.672 1.00 52.95 ATOM 1269 C ARG A 157 29.917 55.939 73.585 1.00 52.95 ATOM 1270 O ARG A 157 31.093 55.654 73.812 1.00 52.95 ATOM 1271 CB ARG A 157 28.090 54.588 74.467 1.00 52.95 ATOM 1272 CG ARG A 157 28.939 53.318 74.554 1.00 52.95 ATOM 1273 CD ARG A 157 28.140 52.030 74.339 1.00 52.95 ATOM 1274 NE ARG A 157 29.106 50.896 74.334 1.00 52.95 ATOM 1275 CZ ARG A 157 28.657 49.614 74.197 1.00 52.95 ATOM 1276 NH1 ARG A 157 27.320 49.365 74.081 1.00 52.95 ATOM 1277 NH2 ARG A 157 29.549 48.579 74.183 1.00 52.95 ATOM 1278 N ALA A 158 29.496 56.324 72.370 1.00 25.87 ATOM 1279 CA ALA A 158 30.409 56.338 71.267 1.00 25.87 ATOM 1280 C ALA A 158 31.509 57.319 71.533 1.00 25.87 ATOM 1281 O ALA A 158 32.679 57.023 71.299 1.00 25.87 ATOM 1282 CB ALA A 158 29.738 56.745 69.944 1.00 25.87 ATOM 1283 N TYR A 159 31.158 58.515 72.040 1.00 55.03 ATOM 1284 CA TYR A 159 32.118 59.556 72.283 1.00 55.03 ATOM 1285 C TYR A 159 33.084 59.140 73.345 1.00 55.03 ATOM 1286 O TYR A 159 34.300 59.233 73.173 1.00 55.03 ATOM 1287 CB TYR A 159 31.420 60.848 72.753 1.00 55.03 ATOM 1288 CG TYR A 159 32.429 61.886 73.108 1.00 55.03 ATOM 1289 CD1 TYR A 159 33.027 62.650 72.133 1.00 55.03 ATOM 1290 CD2 TYR A 159 32.765 62.108 74.424 1.00 55.03 ATOM 1291 CE1 TYR A 159 33.953 63.612 72.467 1.00 55.03 ATOM 1292 CE2 TYR A 159 33.689 63.066 74.765 1.00 55.03 ATOM 1293 CZ TYR A 159 34.286 63.821 73.784 1.00 55.03 ATOM 1294 OH TYR A 159 35.235 64.807 74.128 1.00 55.03 ATOM 1295 N LEU A 160 32.555 58.621 74.468 1.00 50.11 ATOM 1296 CA LEU A 160 33.370 58.296 75.603 1.00 50.11 ATOM 1297 C LEU A 160 34.334 57.222 75.231 1.00 50.11 ATOM 1298 O LEU A 160 35.498 57.258 75.628 1.00 50.11 ATOM 1299 CB LEU A 160 32.524 57.793 76.789 1.00 50.11 ATOM 1300 CG LEU A 160 31.557 58.860 77.338 1.00 50.11 ATOM 1301 CD1 LEU A 160 30.732 58.333 78.521 1.00 50.11 ATOM 1302 CD2 LEU A 160 32.300 60.163 77.675 1.00 50.11 ATOM 1303 N GLU A 161 33.864 56.200 74.499 1.00 72.62 ATOM 1304 CA GLU A 161 34.767 55.154 74.142 1.00 72.62 ATOM 1305 C GLU A 161 35.747 55.597 73.093 1.00 72.62 ATOM 1306 O GLU A 161 36.928 55.276 73.193 1.00 72.62 ATOM 1307 CB GLU A 161 34.050 53.897 73.619 1.00 72.62 ATOM 1308 CG GLU A 161 33.219 53.201 74.699 1.00 72.62 ATOM 1309 CD GLU A 161 32.560 51.973 74.087 1.00 72.62 ATOM 1310 OE1 GLU A 161 32.008 52.089 72.959 1.00 72.62 ATOM 1311 OE2 GLU A 161 32.606 50.898 74.741 1.00 72.62 ATOM 1312 N GLY A 162 35.276 56.225 71.990 1.00 89.46 ATOM 1313 CA GLY A 162 36.210 56.589 70.952 1.00 89.46 ATOM 1314 C GLY A 162 36.976 57.886 71.061 1.00 89.46 ATOM 1315 O GLY A 162 38.167 57.907 71.366 1.00 89.46 ATOM 1316 N LEU A 163 36.258 59.018 70.869 1.00107.20 ATOM 1317 CA LEU A 163 36.855 60.322 70.703 1.00107.20 ATOM 1318 C LEU A 163 37.481 60.818 71.958 1.00107.20 ATOM 1319 O LEU A 163 38.585 61.362 71.938 1.00107.20 ATOM 1320 CB LEU A 163 35.847 61.391 70.240 1.00107.20 ATOM 1321 CG LEU A 163 35.432 61.273 68.760 1.00107.20 ATOM 1322 CD1 LEU A 163 36.591 61.659 67.827 1.00107.20 ATOM 1323 CD2 LEU A 163 34.856 59.883 68.443 1.00107.20 ATOM 1324 N CYS A 164 36.791 60.630 73.093 1.00 45.74 ATOM 1325 CA CYS A 164 37.279 61.170 74.325 1.00 45.74 ATOM 1326 C CYS A 164 38.625 60.592 74.589 1.00 45.74 ATOM 1327 O CYS A 164 39.563 61.311 74.928 1.00 45.74 ATOM 1328 CB CYS A 164 36.395 60.812 75.541 1.00 45.74 ATOM 1329 SG CYS A 164 36.961 61.604 77.084 1.00 45.74 ATOM 1330 N VAL A 165 38.755 59.263 74.438 1.00121.82 ATOM 1331 CA VAL A 165 40.012 58.643 74.724 1.00121.82 ATOM 1332 C VAL A 165 41.048 59.077 73.738 1.00121.82 ATOM 1333 O VAL A 165 42.169 59.400 74.121 1.00121.82 ATOM 1334 CB VAL A 165 39.969 57.137 74.770 1.00121.82 ATOM 1335 CG1 VAL A 165 39.181 56.711 76.015 1.00121.82 ATOM 1336 CG2 VAL A 165 39.345 56.603 73.476 1.00121.82 ATOM 1337 N GLU A 166 40.700 59.145 72.442 1.00 51.60 ATOM 1338 CA GLU A 166 41.692 59.447 71.452 1.00 51.60 ATOM 1339 C GLU A 166 42.287 60.790 71.729 1.00 51.60 ATOM 1340 O GLU A 166 43.508 60.939 71.744 1.00 51.60 ATOM 1341 CB GLU A 166 41.094 59.485 70.037 1.00 51.60 ATOM 1342 CG GLU A 166 40.608 58.119 69.542 1.00 51.60 ATOM 1343 CD GLU A 166 39.744 58.344 68.308 1.00 51.60 ATOM 1344 OE1 GLU A 166 38.548 58.701 68.483 1.00 51.60 ATOM 1345 OE2 GLU A 166 40.264 58.163 67.175 1.00 51.60 ATOM 1346 N TRP A 167 41.441 61.806 71.971 1.00 77.36 ATOM 1347 CA TRP A 167 41.955 63.122 72.204 1.00 77.36 ATOM 1348 C TRP A 167 42.707 63.184 73.495 1.00 77.36 ATOM 1349 O TRP A 167 43.721 63.874 73.588 1.00 77.36 ATOM 1350 CB TRP A 167 40.890 64.230 72.142 1.00 77.36 ATOM 1351 CG TRP A 167 40.492 64.522 70.713 1.00 77.36 ATOM 1352 CD1 TRP A 167 39.425 64.077 69.987 1.00 77.36 ATOM 1353 CD2 TRP A 167 41.275 65.342 69.831 1.00 77.36 ATOM 1354 NE1 TRP A 167 39.497 64.566 68.703 1.00 77.36 ATOM 1355 CE2 TRP A 167 40.631 65.347 68.594 1.00 77.36 ATOM 1356 CE3 TRP A 167 42.438 66.031 70.034 1.00 77.36 ATOM 1357 CZ2 TRP A 167 41.144 66.045 67.537 1.00 77.36 ATOM 1358 CZ3 TRP A 167 42.950 66.736 68.967 1.00 77.36 ATOM 1359 CH2 TRP A 167 42.315 66.743 67.743 1.00 77.36 ATOM 1360 N LEU A 168 42.244 62.468 74.535 1.00 50.95 ATOM 1361 CA LEU A 168 42.941 62.528 75.787 1.00 50.95 ATOM 1362 C LEU A 168 44.337 62.014 75.602 1.00 50.95 ATOM 1363 O LEU A 168 45.289 62.595 76.122 1.00 50.95 ATOM 1364 CB LEU A 168 42.290 61.697 76.906 1.00 50.95 ATOM 1365 CG LEU A 168 43.091 61.754 78.222 1.00 50.95 ATOM 1366 CD1 LEU A 168 43.228 63.195 78.735 1.00 50.95 ATOM 1367 CD2 LEU A 168 42.508 60.807 79.279 1.00 50.95 ATOM 1368 N ARG A 169 44.505 60.915 74.845 1.00120.94 ATOM 1369 CA ARG A 169 45.814 60.352 74.654 1.00120.94 ATOM 1370 C ARG A 169 46.672 61.347 73.941 1.00120.94 ATOM 1371 O ARG A 169 47.861 61.472 74.227 1.00120.94 ATOM 1372 CB ARG A 169 45.828 59.067 73.799 1.00120.94 ATOM 1373 CG ARG A 169 45.487 57.754 74.521 1.00120.94 ATOM 1374 CD ARG A 169 44.046 57.633 75.015 1.00120.94 ATOM 1375 NE ARG A 169 43.765 56.188 75.244 1.00120.94 ATOM 1376 CZ ARG A 169 43.302 55.430 74.206 1.00120.94 ATOM 1377 NH1 ARG A 169 43.117 55.997 72.977 1.00120.94 ATOM 1378 NH2 ARG A 169 43.026 54.108 74.396 1.00120.94 ATOM 1379 N ARG A 170 46.088 62.073 72.972 1.00 64.33 ATOM 1380 CA ARG A 170 46.817 63.019 72.181 1.00 64.33 ATOM 1381 C ARG A 170 47.344 64.105 73.069 1.00 64.33 ATOM 1382 O ARG A 170 48.513 64.476 72.983 1.00 64.33 ATOM 1383 CB ARG A 170 45.910 63.688 71.138 1.00 64.33 ATOM 1384 CG ARG A 170 46.638 64.501 70.067 1.00 64.33 ATOM 1385 CD ARG A 170 45.663 65.228 69.138 1.00 64.33 ATOM 1386 NE ARG A 170 46.405 65.669 67.925 1.00 64.33 ATOM 1387 CZ ARG A 170 47.047 66.872 67.901 1.00 64.33 ATOM 1388 NH1 ARG A 170 47.091 67.643 69.025 1.00 64.33 ATOM 1389 NH2 ARG A 170 47.630 67.305 66.746 1.00 64.33 ATOM 1390 N TYR A 171 46.489 64.625 73.970 1.00 72.59 ATOM 1391 CA TYR A 171 46.881 65.712 74.820 1.00 72.59 ATOM 1392 C TYR A 171 47.977 65.254 75.725 1.00 72.59 ATOM 1393 O TYR A 171 48.935 65.985 75.972 1.00 72.59 ATOM 1394 CB TYR A 171 45.754 66.270 75.710 1.00 72.59 ATOM 1395 CG TYR A 171 44.684 66.824 74.831 1.00 72.59 ATOM 1396 CD1 TYR A 171 44.960 67.835 73.938 1.00 72.59 ATOM 1397 CD2 TYR A 171 43.392 66.363 74.934 1.00 72.59 ATOM 1398 CE1 TYR A 171 43.971 68.351 73.134 1.00 72.59 ATOM 1399 CE2 TYR A 171 42.399 66.876 74.135 1.00 72.59 ATOM 1400 CZ TYR A 171 42.689 67.867 73.230 1.00 72.59 ATOM 1401 OH TYR A 171 41.668 68.391 72.410 1.00 72.59 ATOM 1402 N LEU A 172 47.877 64.014 76.236 1.00 55.72 ATOM 1403 CA LEU A 172 48.855 63.530 77.162 1.00 55.72 ATOM 1404 C LEU A 172 50.201 63.553 76.505 1.00 55.72 ATOM 1405 O LEU A 172 51.183 63.959 77.123 1.00 55.72 ATOM 1406 CB LEU A 172 48.570 62.086 77.626 1.00 55.72 ATOM 1407 CG LEU A 172 47.303 61.958 78.496 1.00 55.72 ATOM 1408 CD1 LEU A 172 47.065 60.504 78.934 1.00 55.72 ATOM 1409 CD2 LEU A 172 47.350 62.919 79.695 1.00 55.72 ATOM 1410 N GLU A 173 50.293 63.115 75.235 1.00 80.31 ATOM 1411 CA GLU A 173 51.575 63.083 74.589 1.00 80.31 ATOM 1412 C GLU A 173 52.105 64.468 74.342 1.00 80.31 ATOM 1413 O GLU A 173 53.269 64.745 74.624 1.00 80.31 ATOM 1414 CB GLU A 173 51.575 62.328 73.251 1.00 80.31 ATOM 1415 CG GLU A 173 52.970 62.245 72.626 1.00 80.31 ATOM 1416 CD GLU A 173 53.840 61.366 73.517 1.00 80.31 ATOM 1417 OE1 GLU A 173 53.279 60.728 74.448 1.00 80.31 ATOM 1418 OE2 GLU A 173 55.075 61.322 73.279 1.00 80.31 ATOM 1419 N ASN A 174 51.267 65.390 73.823 1.00 58.20 ATOM 1420 CA ASN A 174 51.750 66.709 73.504 1.00 58.20 ATOM 1421 C ASN A 174 52.180 67.420 74.755 1.00 58.20 ATOM 1422 O ASN A 174 53.174 68.142 74.763 1.00 58.20 ATOM 1423 CB ASN A 174 50.699 67.585 72.800 1.00 58.20 ATOM 1424 CG ASN A 174 50.571 67.100 71.361 1.00 58.20 ATOM 1425 OD1 ASN A 174 51.452 66.415 70.843 1.00 58.20 ATOM 1426 ND2 ASN A 174 49.449 67.477 70.690 1.00 58.20 ATOM 1427 N GLY A 175 51.371 67.264 75.815 1.00 81.86 ATOM 1428 CA GLY A 175 51.456 67.775 77.159 1.00 81.86 ATOM 1429 C GLY A 175 52.462 67.069 78.026 1.00 81.86 ATOM 1430 O GLY A 175 52.695 67.494 79.155 1.00 81.86 ATOM 1431 N LYS A 176 53.046 65.952 77.560 1.00153.96 ATOM 1432 CA LYS A 176 53.746 65.008 78.393 1.00153.96 ATOM 1433 C LYS A 176 54.702 65.633 79.364 1.00153.96 ATOM 1434 O LYS A 176 54.816 65.125 80.480 1.00153.96 ATOM 1435 CB LYS A 176 54.538 63.964 77.585 1.00153.96 ATOM 1436 CG LYS A 176 55.737 64.538 76.827 1.00153.96 ATOM 1437 CD LYS A 176 56.711 63.471 76.319 1.00153.96 ATOM 1438 CE LYS A 176 56.489 63.073 74.860 1.00153.96 ATOM 1439 NZ LYS A 176 56.815 64.210 73.970 1.00153.96 ATOM 1440 N GLU A 177 55.420 66.715 79.015 1.00 67.07 ATOM 1441 CA GLU A 177 56.368 67.216 79.972 1.00 67.07 ATOM 1442 C GLU A 177 55.678 67.600 81.253 1.00 67.07 ATOM 1443 O GLU A 177 56.163 67.242 82.325 1.00 67.07 ATOM 1444 CB GLU A 177 57.155 68.442 79.472 1.00 67.07 ATOM 1445 CG GLU A 177 58.137 68.114 78.345 1.00 67.07 ATOM 1446 CD GLU A 177 58.993 69.347 78.090 1.00 67.07 ATOM 1447 OE1 GLU A 177 58.406 70.441 77.878 1.00 67.07 ATOM 1448 OE2 GLU A 177 60.246 69.210 78.107 1.00 67.07 ATOM 1449 N THR A 178 54.587 68.396 81.196 1.00 70.28 ATOM 1450 CA THR A 178 53.849 68.767 82.380 1.00 70.28 ATOM 1451 C THR A 178 52.850 67.738 82.860 1.00 70.28 ATOM 1452 O THR A 178 52.834 67.392 84.040 1.00 70.28 ATOM 1453 CB THR A 178 53.114 70.063 82.213 1.00 70.28 ATOM 1454 OG1 THR A 178 52.171 69.969 81.155 1.00 70.28 ATOM 1455 CG2 THR A 178 54.141 71.170 81.920 1.00 70.28 ATOM 1456 N LEU A 179 51.993 67.213 81.954 1.00 69.98 ATOM 1457 CA LEU A 179 50.893 66.353 82.332 1.00 69.98 ATOM 1458 C LEU A 179 51.383 65.059 82.902 1.00 69.98 ATOM 1459 O LEU A 179 50.810 64.529 83.850 1.00 69.98 ATOM 1460 CB LEU A 179 49.971 66.030 81.144 1.00 69.98 ATOM 1461 CG LEU A 179 49.270 67.276 80.568 1.00 69.98 ATOM 1462 CD1 LEU A 179 48.357 66.916 79.388 1.00 69.98 ATOM 1463 CD2 LEU A 179 48.541 68.067 81.669 1.00 69.98 ATOM 1464 N GLN A 180 52.416 64.491 82.264 1.00142.21 ATOM 1465 CA GLN A 180 53.080 63.271 82.616 1.00142.21 ATOM 1466 C GLN A 180 54.016 63.420 83.771 1.00142.21 ATOM 1467 O GLN A 180 54.414 62.405 84.332 1.00142.21 ATOM 1468 CB GLN A 180 53.848 62.614 81.458 1.00142.21 ATOM 1469 CG GLN A 180 52.985 61.686 80.595 1.00142.21 ATOM 1470 CD GLN A 180 52.096 62.479 79.651 1.00142.21 ATOM 1471 OE1 GLN A 180 51.845 63.667 79.846 1.00142.21 ATOM 1472 NE2 GLN A 180 51.594 61.785 78.596 1.00142.21 ATOM 1473 N ARG A 181 54.475 64.648 84.093 1.00114.51 ATOM 1474 CA ARG A 181 55.479 64.828 85.112 1.00114.51 ATOM 1475 C ARG A 181 54.851 65.103 86.444 1.00114.51 ATOM 1476 O ARG A 181 54.048 66.022 86.603 1.00114.51 ATOM 1477 CB ARG A 181 56.418 66.005 84.807 1.00114.51 ATOM 1478 CG ARG A 181 57.537 66.199 85.830 1.00114.51 ATOM 1479 CD ARG A 181 58.351 67.470 85.585 1.00114.51 ATOM 1480 NE ARG A 181 57.550 68.613 86.104 1.00114.51 ATOM 1481 CZ ARG A 181 57.553 69.817 85.460 1.00114.51 ATOM 1482 NH1 ARG A 181 58.249 69.974 84.297 1.00114.51 ATOM 1483 NH2 ARG A 181 56.851 70.866 85.979 1.00114.51 ATOM 1484 N ALA A 182 55.234 64.306 87.461 1.00 38.95 ATOM 1485 CA ALA A 182 54.698 64.523 88.769 1.00 38.95 ATOM 1486 C ALA A 182 55.737 65.260 89.554 1.00 38.95 ATOM 1487 O ALA A 182 56.893 64.846 89.623 1.00 38.95 ATOM 1488 CB ALA A 182 54.380 63.219 89.523 1.00 38.95 ATOM 1489 N ASP A 183 55.336 66.393 90.165 1.00 53.46 ATOM 1490 CA ASP A 183 56.238 67.193 90.943 1.00 53.46 ATOM 1491 C ASP A 183 56.009 66.816 92.375 1.00 53.46 ATOM 1492 O ASP A 183 54.881 66.867 92.859 1.00 53.46 ATOM 1493 CB ASP A 183 55.955 68.701 90.826 1.00 53.46 ATOM 1494 CG ASP A 183 56.222 69.120 89.387 1.00 53.46 ATOM 1495 OD1 ASP A 183 57.033 68.435 88.710 1.00 53.46 ATOM 1496 OD2 ASP A 183 55.612 70.131 88.944 1.00 53.46 ATOM 1497 N PRO A 184 57.053 66.436 93.067 1.00 77.35 ATOM 1498 CA PRO A 184 56.945 66.029 94.444 1.00 77.35 ATOM 1499 C PRO A 184 56.711 67.190 95.358 1.00 77.35 ATOM 1500 O PRO A 184 57.049 68.317 95.003 1.00 77.35 ATOM 1501 CB PRO A 184 58.231 65.263 94.759 1.00 77.35 ATOM 1502 CG PRO A 184 59.193 65.625 93.614 1.00 77.35 ATOM 1503 CD PRO A 184 58.254 65.921 92.434 1.00 77.35 ATOM 1504 N PRO A 185 56.123 66.943 96.499 1.00 89.83 ATOM 1505 CA PRO A 185 55.871 67.992 97.446 1.00 89.83 ATOM 1506 C PRO A 185 57.098 68.348 98.217 1.00 89.83 ATOM 1507 O PRO A 185 57.926 67.473 98.470 1.00 89.83 ATOM 1508 CB PRO A 185 54.741 67.491 98.349 1.00 89.83 ATOM 1509 CG PRO A 185 54.728 65.966 98.132 1.00 89.83 ATOM 1510 CD PRO A 185 55.247 65.801 96.693 1.00 89.83 ATOM 1511 N LYS A 186 57.241 69.637 98.574 1.00 83.93 ATOM 1512 CA LYS A 186 58.269 70.021 99.492 1.00 83.93 ATOM 1513 C LYS A 186 57.573 69.955 100.812 1.00 83.93 ATOM 1514 O LYS A 186 56.441 70.421 100.933 1.00 83.93 ATOM 1515 CB LYS A 186 58.810 71.443 99.276 1.00 83.93 ATOM 1516 CG LYS A 186 59.705 71.542 98.040 1.00 83.93 ATOM 1517 CD LYS A 186 59.989 72.974 97.584 1.00 83.93 ATOM 1518 CE LYS A 186 61.054 73.054 96.488 1.00 83.93 ATOM 1519 NZ LYS A 186 60.584 72.364 95.266 1.00 83.93 ATOM 1520 N THR A 187 58.213 69.366 101.842 1.00 55.83 ATOM 1521 CA THR A 187 57.477 69.180 103.060 1.00 55.83 ATOM 1522 C THR A 187 58.242 69.690 104.243 1.00 55.83 ATOM 1523 O THR A 187 59.453 69.895 104.183 1.00 55.83 ATOM 1524 CB THR A 187 57.150 67.738 103.332 1.00 55.83 ATOM 1525 OG1 THR A 187 58.345 66.976 103.426 1.00 55.83 ATOM 1526 CG2 THR A 187 56.267 67.197 102.196 1.00 55.83 ATOM 1527 N HIS A 188 57.511 69.950 105.353 1.00 50.01 ATOM 1528 CA HIS A 188 58.111 70.366 106.591 1.00 50.01 ATOM 1529 C HIS A 188 57.070 70.277 107.670 1.00 50.01 ATOM 1530 O HIS A 188 55.874 70.206 107.388 1.00 50.01 ATOM 1531 CB HIS A 188 58.641 71.810 106.568 1.00 50.01 ATOM 1532 CG HIS A 188 57.563 72.836 106.394 1.00 50.01 ATOM 1533 ND1 HIS A 188 56.947 73.117 105.195 1.00 50.01 ATOM 1534 CD2 HIS A 188 56.994 73.670 107.308 1.00 50.01 ATOM 1535 CE1 HIS A 188 56.043 74.097 105.440 1.00 50.01 ATOM 1536 NE2 HIS A 188 56.036 74.465 106.709 1.00 50.01 ATOM 1537 N VAL A 189 57.504 70.265 108.949 1.00 34.98 ATOM 1538 CA VAL A 189 56.577 70.201 110.044 1.00 34.98 ATOM 1539 C VAL A 189 56.770 71.428 110.885 1.00 34.98 ATOM 1540 O VAL A 189 57.899 71.863 111.118 1.00 34.98 ATOM 1541 CB VAL A 189 56.781 68.998 110.923 1.00 34.98 ATOM 1542 CG1 VAL A 189 55.788 69.069 112.095 1.00 34.98 ATOM 1543 CG2 VAL A 189 56.637 67.733 110.059 1.00 34.98 ATOM 1544 N THR A 190 55.653 72.017 111.362 1.00 37.64 ATOM 1545 CA THR A 190 55.692 73.203 112.176 1.00 37.64 ATOM 1546 C THR A 190 55.106 72.854 113.510 1.00 37.64 ATOM 1547 O THR A 190 54.392 71.861 113.646 1.00 37.64 ATOM 1548 CB THR A 190 54.869 74.332 111.627 1.00 37.64 ATOM 1549 OG1 THR A 190 53.503 73.953 111.547 1.00 37.64 ATOM 1550 CG2 THR A 190 55.399 74.710 110.233 1.00 37.64 ATOM 1551 N HIS A 191 55.416 73.672 114.540 1.00 57.89 ATOM 1552 CA HIS A 191 54.962 73.419 115.878 1.00 57.89 ATOM 1553 C HIS A 191 54.364 74.689 116.414 1.00 57.89 ATOM 1554 O HIS A 191 54.963 75.757 116.291 1.00 57.89 ATOM 1555 CB HIS A 191 56.136 73.028 116.794 1.00 57.89 ATOM 1556 CG HIS A 191 55.770 72.608 118.185 1.00 57.89 ATOM 1557 ND1 HIS A 191 55.649 73.475 119.249 1.00 57.89 ATOM 1558 CD2 HIS A 191 55.524 71.367 118.688 1.00 57.89 ATOM 1559 CE1 HIS A 191 55.340 72.721 120.334 1.00 57.89 ATOM 1560 NE2 HIS A 191 55.254 71.435 120.043 1.00 57.89 ATOM 1561 N HIS A 192 53.151 74.606 117.012 1.00 66.07 ATOM 1562 CA HIS A 192 52.521 75.771 117.581 1.00 66.07 ATOM 1563 C HIS A 192 51.925 75.379 118.903 1.00 66.07 ATOM 1564 O HIS A 192 51.011 74.559 118.951 1.00 66.07 ATOM 1565 CB HIS A 192 51.338 76.301 116.749 1.00 66.07 ATOM 1566 CG HIS A 192 51.697 76.719 115.355 1.00 66.07 ATOM 1567 ND1 HIS A 192 51.592 75.899 114.254 1.00 66.07 ATOM 1568 CD2 HIS A 192 52.155 77.913 114.886 1.00 66.07 ATOM 1569 CE1 HIS A 192 51.985 76.630 113.181 1.00 66.07 ATOM 1570 NE2 HIS A 192 52.336 77.859 113.516 1.00 66.07 ATOM 1571 N PRO A 193 52.392 75.936 119.988 1.00 86.12 ATOM 1572 CA PRO A 193 51.822 75.559 121.257 1.00 86.12 ATOM 1573 C PRO A 193 50.438 76.092 121.433 1.00 86.12 ATOM 1574 O PRO A 193 50.219 77.270 121.160 1.00 86.12 ATOM 1575 CB PRO A 193 52.813 76.033 122.317 1.00 86.12 ATOM 1576 CG PRO A 193 54.166 76.007 121.582 1.00 86.12 ATOM 1577 CD PRO A 193 53.806 76.257 120.107 1.00 86.12 ATOM 1578 N VAL A 194 49.480 75.220 121.802 1.00133.75 ATOM 1579 CA VAL A 194 48.133 75.604 122.107 1.00133.75 ATOM 1580 C VAL A 194 48.094 76.149 123.503 1.00133.75 ATOM 1581 O VAL A 194 47.516 77.202 123.772 1.00133.75 ATOM 1582 CB VAL A 194 47.223 74.420 122.073 1.00133.75 ATOM 1583 CG1 VAL A 194 45.811 74.900 122.397 1.00133.75 ATOM 1584 CG2 VAL A 194 47.370 73.696 120.729 1.00133.75 ATOM 1585 N SER A 195 48.747 75.420 124.433 1.00 49.05 ATOM 1586 CA SER A 195 48.737 75.742 125.830 1.00 49.05 ATOM 1587 C SER A 195 49.982 75.154 126.416 1.00 49.05 ATOM 1588 O SER A 195 50.877 74.723 125.693 1.00 49.05 ATOM 1589 CB SER A 195 47.559 75.120 126.598 1.00 49.05 ATOM 1590 OG SER A 195 47.683 73.705 126.614 1.00 49.05 ATOM 1591 N ASP A 196 50.081 75.156 127.758 1.00 44.18 ATOM 1592 CA ASP A 196 51.242 74.618 128.402 1.00 44.18 ATOM 1593 C ASP A 196 51.315 73.143 128.135 1.00 44.18 ATOM 1594 O ASP A 196 52.406 72.598 127.975 1.00 44.18 ATOM 1595 CB ASP A 196 51.218 74.818 129.925 1.00 44.18 ATOM 1596 CG ASP A 196 51.441 76.298 130.204 1.00 44.18 ATOM 1597 OD1 ASP A 196 52.497 76.832 129.770 1.00 44.18 ATOM 1598 OD2 ASP A 196 50.561 76.914 130.862 1.00 44.18 ATOM 1599 N HIS A 197 50.149 72.463 128.156 1.00100.45 ATOM 1600 CA HIS A 197 49.992 71.041 127.973 1.00100.45 ATOM 1601 C HIS A 197 50.133 70.563 126.555 1.00100.45 ATOM 1602 O HIS A 197 50.724 69.509 126.328 1.00100.45 ATOM 1603 CB HIS A 197 48.626 70.541 128.472 1.00100.45 ATOM 1604 CG HIS A 197 48.499 69.046 128.449 1.00100.45 ATOM 1605 ND1 HIS A 197 48.001 68.320 127.389 1.00100.45 ATOM 1606 CD2 HIS A 197 48.823 68.134 129.404 1.00100.45 ATOM 1607 CE1 HIS A 197 48.047 67.015 127.754 1.00100.45 ATOM 1608 NE2 HIS A 197 48.539 66.852 128.969 1.00100.45 ATOM 1609 N GLU A 198 49.589 71.294 125.557 1.00 59.71 ATOM 1610 CA GLU A 198 49.535 70.719 124.236 1.00 59.71 ATOM 1611 C GLU A 198 50.065 71.660 123.195 1.00 59.71 ATOM 1612 O GLU A 198 50.223 72.857 123.433 1.00 59.71 ATOM 1613 CB GLU A 198 48.101 70.365 123.811 1.00 59.71 ATOM 1614 CG GLU A 198 47.460 69.281 124.680 1.00 59.71 ATOM 1615 CD GLU A 198 46.012 69.119 124.237 1.00 59.71 ATOM 1616 OE1 GLU A 198 45.333 70.162 124.038 1.00 59.71 ATOM 1617 OE2 GLU A 198 45.565 67.949 124.090 1.00 59.71 ATOM 1618 N ALA A 199 50.368 71.105 121.996 1.00 35.46 ATOM 1619 CA ALA A 199 50.867 71.875 120.889 1.00 35.46 ATOM 1620 C ALA A 199 50.324 71.273 119.629 1.00 35.46 ATOM 1621 O ALA A 199 49.950 70.102 119.594 1.00 35.46 ATOM 1622 CB ALA A 199 52.400 71.853 120.769 1.00 35.46 ATOM 1623 N THR A 200 50.273 72.076 118.544 1.00 47.96 ATOM 1624 CA THR A 200 49.755 71.594 117.299 1.00 47.96 ATOM 1625 C THR A 200 50.910 71.325 116.390 1.00 47.96 ATOM 1626 O THR A 200 51.807 72.153 116.235 1.00 47.96 ATOM 1627 CB THR A 200 48.859 72.587 116.612 1.00 47.96 ATOM 1628 OG1 THR A 200 47.758 72.919 117.446 1.00 47.96 ATOM 1629 CG2 THR A 200 48.364 71.975 115.290 1.00 47.96 ATOM 1630 N LEU A 201 50.927 70.115 115.792 1.00 52.98 ATOM 1631 CA LEU A 201 51.941 69.761 114.839 1.00 52.98 ATOM 1632 C LEU A 201 51.280 69.844 113.498 1.00 52.98 ATOM 1633 O LEU A 201 50.232 69.240 113.278 1.00 52.98 ATOM 1634 CB LEU A 201 52.456 68.319 114.991 1.00 52.98 ATOM 1635 CG LEU A 201 53.221 68.051 116.300 1.00 52.98 ATOM 1636 CD1 LEU A 201 53.698 66.593 116.377 1.00 52.98 ATOM 1637 CD2 LEU A 201 54.369 69.054 116.487 1.00 52.98 ATOM 1638 N ARG A 202 51.878 70.609 112.563 1.00135.08 ATOM 1639 CA ARG A 202 51.296 70.785 111.261 1.00135.08 ATOM 1640 C ARG A 202 52.270 70.253 110.251 1.00135.08 ATOM 1641 O ARG A 202 53.437 70.639 110.239 1.00135.08 ATOM 1642 CB ARG A 202 51.084 72.274 110.929 1.00135.08 ATOM 1643 CG ARG A 202 50.451 72.555 109.565 1.00135.08 ATOM 1644 CD ARG A 202 48.924 72.534 109.569 1.00135.08 ATOM 1645 NE ARG A 202 48.472 73.920 109.882 1.00135.08 ATOM 1646 CZ ARG A 202 48.273 74.308 111.175 1.00135.08 ATOM 1647 NH1 ARG A 202 48.402 73.405 112.189 1.00135.08 ATOM 1648 NH2 ARG A 202 47.951 75.605 111.456 1.00135.08 ATOM 1649 N CYS A 203 51.800 69.352 109.365 1.00 46.45 ATOM 1650 CA CYS A 203 52.645 68.781 108.352 1.00 46.45 ATOM 1651 C CYS A 203 52.233 69.420 107.058 1.00 46.45 ATOM 1652 O CYS A 203 51.058 69.396 106.693 1.00 46.45 ATOM 1653 CB CYS A 203 52.462 67.251 108.259 1.00 46.45 ATOM 1654 SG CYS A 203 53.521 66.411 107.046 1.00 46.45 ATOM 1655 N TRP A 204 53.204 70.012 106.327 1.00 71.25 ATOM 1656 CA TRP A 204 52.871 70.757 105.143 1.00 71.25 ATOM 1657 C TRP A 204 53.438 70.100 103.926 1.00 71.25 ATOM 1658 O TRP A 204 54.526 69.526 103.956 1.00 71.25 ATOM 1659 CB TRP A 204 53.433 72.190 105.144 1.00 71.25 ATOM 1660 CG TRP A 204 52.800 73.129 106.143 1.00 71.25 ATOM 1661 CD1 TRP A 204 53.041 73.264 107.479 1.00 71.25 ATOM 1662 CD2 TRP A 204 51.808 74.111 105.806 1.00 71.25 ATOM 1663 NE1 TRP A 204 52.256 74.268 107.996 1.00 71.25 ATOM 1664 CE2 TRP A 204 51.494 74.798 106.977 1.00 71.25 ATOM 1665 CE3 TRP A 204 51.213 74.420 104.617 1.00 71.25 ATOM 1666 CZ2 TRP A 204 50.575 75.807 106.976 1.00 71.25 ATOM 1667 CZ3 TRP A 204 50.281 75.434 104.619 1.00 71.25 ATOM 1668 CH2 TRP A 204 49.968 76.114 105.778 1.00 71.25 ATOM 1669 N ALA A 205 52.669 70.156 102.819 1.00 47.80 ATOM 1670 CA ALA A 205 53.129 69.691 101.540 1.00 47.80 ATOM 1671 C ALA A 205 52.898 70.830 100.588 1.00 47.80 ATOM 1672 O ALA A 205 51.783 71.341 100.493 1.00 47.80 ATOM 1673 CB ALA A 205 52.343 68.481 101.003 1.00 47.80 ATOM 1674 N LEU A 206 53.946 71.256 99.852 1.00 56.52 ATOM 1675 CA LEU A 206 53.790 72.385 98.972 1.00 56.52 ATOM 1676 C LEU A 206 54.436 72.100 97.648 1.00 56.52 ATOM 1677 O LEU A 206 55.416 71.360 97.562 1.00 56.52 ATOM 1678 CB LEU A 206 54.460 73.663 99.509 1.00 56.52 ATOM 1679 CG LEU A 206 53.889 74.158 100.851 1.00 56.52 ATOM 1680 CD1 LEU A 206 54.604 75.435 101.321 1.00 56.52 ATOM 1681 CD2 LEU A 206 52.364 74.319 100.791 1.00 56.52 ATOM 1682 N GLY A 207 53.876 72.686 96.567 1.00 44.53 ATOM 1683 CA GLY A 207 54.475 72.629 95.262 1.00 44.53 ATOM 1684 C GLY A 207 54.329 71.287 94.600 1.00 44.53 ATOM 1685 O GLY A 207 55.152 70.953 93.751 1.00 44.53 ATOM 1686 N PHE A 208 53.257 70.516 94.883 1.00 76.31 ATOM 1687 CA PHE A 208 53.148 69.232 94.238 1.00 76.31 ATOM 1688 C PHE A 208 52.084 69.222 93.172 1.00 76.31 ATOM 1689 O PHE A 208 51.130 69.999 93.197 1.00 76.31 ATOM 1690 CB PHE A 208 52.876 68.065 95.213 1.00 76.31 ATOM 1691 CG PHE A 208 51.620 68.305 95.987 1.00 76.31 ATOM 1692 CD1 PHE A 208 51.645 69.051 97.143 1.00 76.31 ATOM 1693 CD2 PHE A 208 50.421 67.772 95.572 1.00 76.31 ATOM 1694 CE1 PHE A 208 50.495 69.267 97.866 1.00 76.31 ATOM 1695 CE2 PHE A 208 49.268 67.985 96.291 1.00 76.31 ATOM 1696 CZ PHE A 208 49.303 68.735 97.440 1.00 76.31 ATOM 1697 N TYR A 209 52.292 68.365 92.147 1.00 87.67 ATOM 1698 CA TYR A 209 51.360 68.137 91.069 1.00 87.67 ATOM 1699 C TYR A 209 51.454 66.677 90.747 1.00 87.67 ATOM 1700 O TYR A 209 52.573 66.170 90.685 1.00 87.67 ATOM 1701 CB TYR A 209 51.729 68.941 89.809 1.00 87.67 ATOM 1702 CG TYR A 209 50.741 68.673 88.727 1.00 87.67 ATOM 1703 CD1 TYR A 209 50.863 67.566 87.917 1.00 87.67 ATOM 1704 CD2 TYR A 209 49.696 69.541 88.511 1.00 87.67 ATOM 1705 CE1 TYR A 209 49.951 67.330 86.916 1.00 87.67 ATOM 1706 CE2 TYR A 209 48.781 69.310 87.511 1.00 87.67 ATOM 1707 CZ TYR A 209 48.907 68.199 86.711 1.00 87.67 ATOM 1708 OH TYR A 209 47.973 67.951 85.682 1.00 87.67 ATOM 1709 N PRO A 210 50.394 65.931 90.527 1.00 91.54 ATOM 1710 CA PRO A 210 49.020 66.357 90.557 1.00 91.54 ATOM 1711 C PRO A 210 48.551 66.515 91.970 1.00 91.54 ATOM 1712 O PRO A 210 49.321 66.266 92.893 1.00 91.54 ATOM 1713 CB PRO A 210 48.229 65.287 89.802 1.00 91.54 ATOM 1714 CG PRO A 210 49.136 64.050 89.830 1.00 91.54 ATOM 1715 CD PRO A 210 50.550 64.649 89.860 1.00 91.54 ATOM 1716 N ALA A 211 47.279 66.921 92.143 1.00 57.39 ATOM 1717 CA ALA A 211 46.669 67.211 93.410 1.00 57.39 ATOM 1718 C ALA A 211 46.619 66.013 94.319 1.00 57.39 ATOM 1719 O ALA A 211 46.725 66.165 95.535 1.00 57.39 ATOM 1720 CB ALA A 211 45.225 67.727 93.268 1.00 57.39 ATOM 1721 N GLU A 212 46.420 64.793 93.780 1.00 87.65 ATOM 1722 CA GLU A 212 46.262 63.633 94.623 1.00 87.65 ATOM 1723 C GLU A 212 47.452 63.477 95.523 1.00 87.65 ATOM 1724 O GLU A 212 48.595 63.444 95.070 1.00 87.65 ATOM 1725 CB GLU A 212 46.067 62.336 93.812 1.00 87.65 ATOM 1726 CG GLU A 212 45.768 61.100 94.661 1.00 87.65 ATOM 1727 CD GLU A 212 47.095 60.480 95.068 1.00 87.65 ATOM 1728 OE1 GLU A 212 48.112 60.752 94.376 1.00 87.65 ATOM 1729 OE2 GLU A 212 47.108 59.722 96.074 1.00 87.65 ATOM 1730 N ILE A 213 47.192 63.393 96.847 1.00117.54 ATOM 1731 CA ILE A 213 48.237 63.276 97.830 1.00117.54 ATOM 1732 C ILE A 213 47.658 62.597 99.036 1.00117.54 ATOM 1733 O ILE A 213 46.450 62.646 99.263 1.00117.54 ATOM 1734 CB ILE A 213 48.715 64.630 98.292 1.00117.54 ATOM 1735 CG1 ILE A 213 49.984 64.554 99.159 1.00117.54 ATOM 1736 CG2 ILE A 213 47.530 65.319 98.990 1.00117.54 ATOM 1737 CD1 ILE A 213 51.275 64.362 98.368 1.00117.54 ATOM 1738 N THR A 214 48.514 61.928 99.838 1.00 54.59 ATOM 1739 CA THR A 214 48.059 61.326 101.060 1.00 54.59 ATOM 1740 C THR A 214 48.917 61.870 102.164 1.00 54.59 ATOM 1741 O THR A 214 50.134 61.698 102.146 1.00 54.59 ATOM 1742 CB THR A 214 48.222 59.834 101.073 1.00 54.59 ATOM 1743 OG1 THR A 214 47.492 59.247 100.004 1.00 54.59 ATOM 1744 CG2 THR A 214 47.724 59.292 102.422 1.00 54.59 ATOM 1745 N LEU A 215 48.307 62.563 103.151 1.00106.55 ATOM 1746 CA LEU A 215 49.074 63.055 104.262 1.00106.55 ATOM 1747 C LEU A 215 48.434 62.530 105.503 1.00106.55 ATOM 1748 O LEU A 215 47.242 62.733 105.729 1.00106.55 ATOM 1749 CB LEU A 215 49.124 64.587 104.369 1.00106.55 ATOM 1750 CG LEU A 215 49.794 65.236 103.145 1.00106.55 ATOM 1751 CD1 LEU A 215 48.879 65.178 101.912 1.00106.55 ATOM 1752 CD2 LEU A 215 50.328 66.636 103.459 1.00106.55 ATOM 1753 N THR A 216 49.219 61.829 106.346 1.00 46.96 ATOM 1754 CA THR A 216 48.646 61.262 107.530 1.00 46.96 ATOM 1755 C THR A 216 49.581 61.470 108.679 1.00 46.96 ATOM 1756 O THR A 216 50.783 61.658 108.496 1.00 46.96 ATOM 1757 CB THR A 216 48.404 59.784 107.418 1.00 46.96 ATOM 1758 OG1 THR A 216 49.629 59.101 107.199 1.00 46.96 ATOM 1759 CG2 THR A 216 47.437 59.526 106.250 1.00 46.96 ATOM 1760 N TRP A 217 49.019 61.473 109.906 1.00 74.12 ATOM 1761 CA TRP A 217 49.806 61.542 111.103 1.00 74.12 ATOM 1762 C TRP A 217 49.614 60.254 111.840 1.00 74.12 ATOM 1763 O TRP A 217 48.511 59.710 111.898 1.00 74.12 ATOM 1764 CB TRP A 217 49.417 62.664 112.080 1.00 74.12 ATOM 1765 CG TRP A 217 49.933 64.033 111.717 1.00 74.12 ATOM 1766 CD1 TRP A 217 49.330 65.068 111.066 1.00 74.12 ATOM 1767 CD2 TRP A 217 51.259 64.475 112.045 1.00 74.12 ATOM 1768 NE1 TRP A 217 50.197 66.131 110.972 1.00 74.12 ATOM 1769 CE2 TRP A 217 51.390 65.778 111.571 1.00 74.12 ATOM 1770 CE3 TRP A 217 52.284 63.845 112.692 1.00 74.12 ATOM 1771 CZ2 TRP A 217 52.554 66.475 111.734 1.00 74.12 ATOM 1772 CZ3 TRP A 217 53.457 64.548 112.855 1.00 74.12 ATOM 1773 CH2 TRP A 217 53.587 65.839 112.385 1.00 74.12 ATOM 1774 N GLN A 218 50.710 59.718 112.410 1.00 55.49 ATOM 1775 CA GLN A 218 50.607 58.500 113.161 1.00 55.49 ATOM 1776 C GLN A 218 51.256 58.732 114.485 1.00 55.49 ATOM 1777 O GLN A 218 52.179 59.538 114.601 1.00 55.49 ATOM 1778 CB GLN A 218 51.332 57.307 112.511 1.00 55.49 ATOM 1779 CG GLN A 218 50.715 56.873 111.179 1.00 55.49 ATOM 1780 CD GLN A 218 51.526 55.698 110.642 1.00 55.49 ATOM 1781 OE1 GLN A 218 52.622 55.413 111.120 1.00 55.49 ATOM 1782 NE2 GLN A 218 50.980 54.992 109.616 1.00 55.49 ATOM 1783 N ARG A 219 50.745 58.068 115.545 1.00114.13 ATOM 1784 CA ARG A 219 51.456 58.154 116.785 1.00114.13 ATOM 1785 C ARG A 219 51.796 56.749 117.149 1.00114.13 ATOM 1786 O ARG A 219 50.926 55.880 117.204 1.00114.13 ATOM 1787 CB ARG A 219 50.702 58.750 117.982 1.00114.13 ATOM 1788 CG ARG A 219 49.552 57.903 118.514 1.00114.13 ATOM 1789 CD ARG A 219 49.069 58.376 119.886 1.00114.13 ATOM 1790 NE ARG A 219 48.038 57.414 120.361 1.00114.13 ATOM 1791 CZ ARG A 219 46.718 57.651 120.112 1.00114.13 ATOM 1792 NH1 ARG A 219 46.342 58.767 119.424 1.00114.13 ATOM 1793 NH2 ARG A 219 45.771 56.773 120.555 1.00114.13 ATOM 1794 N ASP A 220 53.089 56.498 117.414 1.00 49.75 ATOM 1795 CA ASP A 220 53.550 55.182 117.739 1.00 49.75 ATOM 1796 C ASP A 220 53.188 54.260 116.620 1.00 49.75 ATOM 1797 O ASP A 220 52.889 53.088 116.843 1.00 49.75 ATOM 1798 CB ASP A 220 52.961 54.644 119.049 1.00 49.75 ATOM 1799 CG ASP A 220 53.566 55.466 120.176 1.00 49.75 ATOM 1800 OD1 ASP A 220 54.464 56.301 119.883 1.00 49.75 ATOM 1801 OD2 ASP A 220 53.139 55.273 121.343 1.00 49.75 ATOM 1802 N GLY A 221 53.220 54.781 115.378 1.00 27.75 ATOM 1803 CA GLY A 221 52.987 53.983 114.209 1.00 27.75 ATOM 1804 C GLY A 221 51.523 53.700 114.041 1.00 27.75 ATOM 1805 O GLY A 221 51.159 52.784 113.306 1.00 27.75 ATOM 1806 N GLU A 222 50.638 54.473 114.700 1.00 59.14 ATOM 1807 CA GLU A 222 49.231 54.197 114.586 1.00 59.14 ATOM 1808 C GLU A 222 48.576 55.371 113.916 1.00 59.14 ATOM 1809 O GLU A 222 48.810 56.514 114.304 1.00 59.14 ATOM 1810 CB GLU A 222 48.553 54.060 115.958 1.00 59.14 ATOM 1811 CG GLU A 222 49.118 52.926 116.815 1.00 59.14 ATOM 1812 CD GLU A 222 48.647 53.159 118.244 1.00 59.14 ATOM 1813 OE1 GLU A 222 47.506 52.738 118.571 1.00 59.14 ATOM 1814 OE2 GLU A 222 49.422 53.771 119.026 1.00 59.14 ATOM 1815 N ASP A 223 47.716 55.116 112.903 1.00 83.77 ATOM 1816 CA ASP A 223 47.052 56.166 112.174 1.00 83.77 ATOM 1817 C ASP A 223 46.117 56.901 113.094 1.00 83.77 ATOM 1818 O ASP A 223 45.309 56.319 113.815 1.00 83.77 ATOM 1819 CB ASP A 223 46.210 55.665 110.983 1.00 83.77 ATOM 1820 CG ASP A 223 47.147 55.154 109.901 1.00 83.77 ATOM 1821 OD1 ASP A 223 48.381 55.346 110.056 1.00 83.77 ATOM 1822 OD2 ASP A 223 46.646 54.564 108.907 1.00 83.77 ATOM 1823 N GLN A 224 46.282 58.232 113.074 1.00152.86 ATOM 1824 CA GLN A 224 45.659 59.328 113.762 1.00152.86 ATOM 1825 C GLN A 224 44.377 59.803 113.150 1.00152.86 ATOM 1826 O GLN A 224 43.905 60.871 113.531 1.00152.86 ATOM 1827 CB GLN A 224 46.591 60.538 113.916 1.00152.86 ATOM 1828 CG GLN A 224 47.784 60.202 114.809 1.00152.86 ATOM 1829 CD GLN A 224 47.214 59.676 116.118 1.00152.86 ATOM 1830 OE1 GLN A 224 46.619 60.419 116.896 1.00152.86 ATOM 1831 NE2 GLN A 224 47.391 58.349 116.361 1.00152.86 ATOM 1832 N THR A 225 43.828 59.102 112.144 1.00143.84 ATOM 1833 CA THR A 225 42.796 59.595 111.269 1.00143.84 ATOM 1834 C THR A 225 41.711 60.379 111.965 1.00143.84 ATOM 1835 O THR A 225 41.373 61.468 111.502 1.00143.84 ATOM 1836 CB THR A 225 42.142 58.467 110.535 1.00143.84 ATOM 1837 OG1 THR A 225 43.113 57.727 109.811 1.00143.84 ATOM 1838 CG2 THR A 225 41.121 59.056 109.562 1.00143.84 ATOM 1839 N GLN A 226 41.121 59.903 113.072 1.00 51.13 ATOM 1840 CA GLN A 226 40.045 60.672 113.644 1.00 51.13 ATOM 1841 C GLN A 226 40.539 62.009 114.143 1.00 51.13 ATOM 1842 O GLN A 226 39.864 63.025 113.981 1.00 51.13 ATOM 1843 CB GLN A 226 39.368 59.947 114.820 1.00 51.13 ATOM 1844 CG GLN A 226 38.734 58.613 114.416 1.00 51.13 ATOM 1845 CD GLN A 226 37.585 58.894 113.456 1.00 51.13 ATOM 1846 OE1 GLN A 226 36.614 59.563 113.808 1.00 51.13 ATOM 1847 NE2 GLN A 226 37.697 58.370 112.206 1.00 51.13 ATOM 1848 N ASP A 227 41.730 62.022 114.770 1.00 83.04 ATOM 1849 CA ASP A 227 42.380 63.132 115.420 1.00 83.04 ATOM 1850 C ASP A 227 42.922 64.164 114.469 1.00 83.04 ATOM 1851 O ASP A 227 43.193 65.293 114.883 1.00 83.04 ATOM 1852 CB ASP A 227 43.555 62.666 116.293 1.00 83.04 ATOM 1853 CG ASP A 227 42.982 61.835 117.433 1.00 83.04 ATOM 1854 OD1 ASP A 227 42.030 62.321 118.098 1.00 83.04 ATOM 1855 OD2 ASP A 227 43.480 60.698 117.645 1.00 83.04 ATOM 1856 N THR A 228 43.158 63.823 113.187 1.00131.62 ATOM 1857 CA THR A 228 43.863 64.777 112.377 1.00131.62 ATOM 1858 C THR A 228 42.939 65.629 111.568 1.00131.62 ATOM 1859 O THR A 228 41.898 65.194 111.080 1.00131.62 ATOM 1860 CB THR A 228 44.857 64.144 111.450 1.00131.62 ATOM 1861 OG1 THR A 228 45.753 65.124 110.953 1.00131.62 ATOM 1862 CG2 THR A 228 44.107 63.485 110.286 1.00131.62 ATOM 1863 N GLU A 229 43.324 66.915 111.432 1.00 49.21 ATOM 1864 CA GLU A 229 42.575 67.872 110.675 1.00 49.21 ATOM 1865 C GLU A 229 43.265 68.027 109.358 1.00 49.21 ATOM 1866 O GLU A 229 44.443 68.374 109.304 1.00 49.21 ATOM 1867 CB GLU A 229 42.549 69.262 111.333 1.00 49.21 ATOM 1868 CG GLU A 229 41.754 70.312 110.556 1.00 49.21 ATOM 1869 CD GLU A 229 41.841 71.626 111.322 1.00 49.21 ATOM 1870 OE1 GLU A 229 42.982 72.012 111.699 1.00 49.21 ATOM 1871 OE2 GLU A 229 40.776 72.258 111.544 1.00 49.21 ATOM 1872 N LEU A 230 42.548 67.745 108.250 1.00 95.61 ATOM 1873 CA LEU A 230 43.156 67.918 106.965 1.00 95.61 ATOM 1874 C LEU A 230 42.408 68.979 106.229 1.00 95.61 ATOM 1875 O LEU A 230 41.186 68.937 106.108 1.00 95.61 ATOM 1876 CB LEU A 230 43.157 66.676 106.056 1.00 95.61 ATOM 1877 CG LEU A 230 44.040 65.521 106.554 1.00 95.61 ATOM 1878 CD1 LEU A 230 43.392 64.784 107.736 1.00 95.61 ATOM 1879 CD2 LEU A 230 44.462 64.603 105.397 1.00 95.61 ATOM 1880 N VAL A 231 43.150 69.974 105.717 1.00109.08 ATOM 1881 CA VAL A 231 42.588 71.056 104.965 1.00109.08 ATOM 1882 C VAL A 231 42.432 70.580 103.556 1.00109.08 ATOM 1883 O VAL A 231 43.150 69.686 103.113 1.00109.08 ATOM 1884 CB VAL A 231 43.487 72.257 104.964 1.00109.08 ATOM 1885 CG1 VAL A 231 44.830 71.850 104.336 1.00109.08 ATOM 1886 CG2 VAL A 231 42.795 73.419 104.242 1.00109.08 ATOM 1887 N GLU A 232 41.456 71.145 102.815 1.00 71.85 ATOM 1888 CA GLU A 232 41.276 70.731 101.454 1.00 71.85 ATOM 1889 C GLU A 232 42.459 71.216 100.680 1.00 71.85 ATOM 1890 O GLU A 232 43.011 72.281 100.957 1.00 71.85 ATOM 1891 CB GLU A 232 40.007 71.288 100.782 1.00 71.85 ATOM 1892 CG GLU A 232 39.725 70.659 99.414 1.00 71.85 ATOM 1893 CD GLU A 232 39.251 69.228 99.647 1.00 71.85 ATOM 1894 OE1 GLU A 232 38.330 69.043 100.485 1.00 71.85 ATOM 1895 OE2 GLU A 232 39.807 68.303 98.997 1.00 71.85 ATOM 1896 N THR A 233 42.883 70.427 99.675 1.00 43.36 ATOM 1897 CA THR A 233 44.022 70.793 98.886 1.00 43.36 ATOM 1898 C THR A 233 43.654 72.040 98.143 1.00 43.36 ATOM 1899 O THR A 233 42.515 72.184 97.699 1.00 43.36 ATOM 1900 CB THR A 233 44.400 69.733 97.892 1.00 43.36 ATOM 1901 OG1 THR A 233 44.647 68.505 98.563 1.00 43.36 ATOM 1902 CG2 THR A 233 45.665 70.183 97.139 1.00 43.36 ATOM 1903 N ARG A 234 44.607 72.992 98.005 1.00 56.27 ATOM 1904 CA ARG A 234 44.287 74.236 97.352 1.00 56.27 ATOM 1905 C ARG A 234 45.335 74.557 96.322 1.00 56.27 ATOM 1906 O ARG A 234 46.504 74.206 96.467 1.00 56.27 ATOM 1907 CB ARG A 234 44.227 75.445 98.302 1.00 56.27 ATOM 1908 CG ARG A 234 45.554 75.757 98.999 1.00 56.27 ATOM 1909 CD ARG A 234 45.566 77.136 99.663 1.00 56.27 ATOM 1910 NE ARG A 234 46.926 77.362 100.233 1.00 56.27 ATOM 1911 CZ ARG A 234 47.176 77.079 101.544 1.00 56.27 ATOM 1912 NH1 ARG A 234 46.172 76.617 102.345 1.00 56.27 ATOM 1913 NH2 ARG A 234 48.430 77.259 102.054 1.00 56.27 ATOM 1914 N PRO A 235 44.911 75.207 95.264 1.00159.72 ATOM 1915 CA PRO A 235 45.826 75.563 94.205 1.00159.72 ATOM 1916 C PRO A 235 46.744 76.710 94.508 1.00159.72 ATOM 1917 O PRO A 235 46.290 77.721 95.044 1.00159.72 ATOM 1918 CB PRO A 235 44.968 75.802 92.964 1.00159.72 ATOM 1919 CG PRO A 235 43.710 74.958 93.220 1.00159.72 ATOM 1920 CD PRO A 235 43.577 74.936 94.750 1.00159.72 ATOM 1921 N ALA A 236 48.044 76.559 94.175 1.00 48.16 ATOM 1922 CA ALA A 236 49.045 77.584 94.309 1.00 48.16 ATOM 1923 C ALA A 236 48.810 78.660 93.284 1.00 48.16 ATOM 1924 O ALA A 236 48.962 79.844 93.575 1.00 48.16 ATOM 1925 CB ALA A 236 50.474 77.047 94.109 1.00 48.16 ATOM 1926 N GLY A 237 48.414 78.270 92.051 1.00 38.85 ATOM 1927 CA GLY A 237 48.217 79.208 90.973 1.00 38.85 ATOM 1928 C GLY A 237 49.244 78.947 89.900 1.00 38.85 ATOM 1929 O GLY A 237 49.065 79.344 88.748 1.00 38.85 ATOM 1930 N ASP A 238 50.372 78.318 90.283 1.00121.42 ATOM 1931 CA ASP A 238 51.472 77.910 89.444 1.00121.42 ATOM 1932 C ASP A 238 51.208 76.584 88.771 1.00121.42 ATOM 1933 O ASP A 238 52.081 76.089 88.064 1.00121.42 ATOM 1934 CB ASP A 238 52.838 77.896 90.159 1.00121.42 ATOM 1935 CG ASP A 238 52.790 76.944 91.333 1.00121.42 ATOM 1936 OD1 ASP A 238 51.709 76.338 91.550 1.00121.42 ATOM 1937 OD2 ASP A 238 53.828 76.820 92.037 1.00121.42 ATOM 1938 N ARG A 239 50.018 75.979 89.001 1.00168.86 ATOM 1939 CA ARG A 239 49.525 74.678 88.586 1.00168.86 ATOM 1940 C ARG A 239 49.857 73.689 89.657 1.00168.86 ATOM 1941 O ARG A 239 49.484 72.522 89.568 1.00168.86 ATOM 1942 CB ARG A 239 50.134 74.053 87.310 1.00168.86 ATOM 1943 CG ARG A 239 51.552 73.485 87.458 1.00168.86 ATOM 1944 CD ARG A 239 52.015 72.683 86.239 1.00168.86 ATOM 1945 NE ARG A 239 53.178 71.846 86.654 1.00168.86 ATOM 1946 CZ ARG A 239 53.205 70.524 86.312 1.00168.86 ATOM 1947 NH1 ARG A 239 52.169 69.984 85.604 1.00168.86 ATOM 1948 NH2 ARG A 239 54.258 69.740 86.683 1.00168.86 ATOM 1949 N THR A 240 50.503 74.149 90.739 1.00153.75 ATOM 1950 CA THR A 240 50.918 73.264 91.779 1.00153.75 ATOM 1951 C THR A 240 49.879 73.332 92.873 1.00153.75 ATOM 1952 O THR A 240 48.993 74.185 92.830 1.00153.75 ATOM 1953 CB THR A 240 52.219 73.729 92.309 1.00153.75 ATOM 1954 OG1 THR A 240 53.021 72.611 92.592 1.00153.75 ATOM 1955 CG2 THR A 240 51.969 74.528 93.596 1.00153.75 ATOM 1956 N PHE A 241 49.964 72.439 93.889 1.00 55.29 ATOM 1957 CA PHE A 241 48.967 72.405 94.933 1.00 55.29 ATOM 1958 C PHE A 241 49.624 72.441 96.284 1.00 55.29 ATOM 1959 O PHE A 241 50.833 72.248 96.412 1.00 55.29 ATOM 1960 CB PHE A 241 48.101 71.135 94.908 1.00 55.29 ATOM 1961 CG PHE A 241 47.330 71.146 93.636 1.00 55.29 ATOM 1962 CD1 PHE A 241 47.882 70.638 92.483 1.00 55.29 ATOM 1963 CD2 PHE A 241 46.057 71.664 93.593 1.00 55.29 ATOM 1964 CE1 PHE A 241 47.175 70.648 91.305 1.00 55.29 ATOM 1965 CE2 PHE A 241 45.345 71.676 92.417 1.00 55.29 ATOM 1966 CZ PHE A 241 45.904 71.166 91.270 1.00 55.29 ATOM 1967 N GLN A 242 48.815 72.715 97.336 1.00 49.86 ATOM 1968 CA GLN A 242 49.310 72.800 98.687 1.00 49.86 ATOM 1969 C GLN A 242 48.327 72.119 99.604 1.00 49.86 ATOM 1970 O GLN A 242 47.128 72.103 99.335 1.00 49.86 ATOM 1971 CB GLN A 242 49.448 74.256 99.160 1.00 49.86 ATOM 1972 CG GLN A 242 50.423 75.064 98.298 1.00 49.86 ATOM 1973 CD GLN A 242 50.471 76.494 98.816 1.00 49.86 ATOM 1974 OE1 GLN A 242 49.746 76.859 99.740 1.00 49.86 ATOM 1975 NE2 GLN A 242 51.350 77.330 98.202 1.00 49.86 ATOM 1976 N LYS A 243 48.816 71.509 100.711 1.00 66.00 ATOM 1977 CA LYS A 243 47.928 70.873 101.654 1.00 66.00 ATOM 1978 C LYS A 243 48.650 70.715 102.963 1.00 66.00 ATOM 1979 O LYS A 243 49.880 70.748 103.009 1.00 66.00 ATOM 1980 CB LYS A 243 47.453 69.475 101.213 1.00 66.00 ATOM 1981 CG LYS A 243 46.309 68.915 102.066 1.00 66.00 ATOM 1982 CD LYS A 243 45.599 67.722 101.423 1.00 66.00 ATOM 1983 CE LYS A 243 44.364 67.243 102.191 1.00 66.00 ATOM 1984 NZ LYS A 243 43.641 66.224 101.399 1.00 66.00 ATOM 1985 N TRP A 244 47.886 70.578 104.074 1.00 94.45 ATOM 1986 CA TRP A 244 48.478 70.361 105.367 1.00 94.45 ATOM 1987 C TRP A 244 47.559 69.525 106.214 1.00 94.45 ATOM 1988 O TRP A 244 46.348 69.493 106.002 1.00 94.45 ATOM 1989 CB TRP A 244 48.797 71.661 106.127 1.00 94.45 ATOM 1990 CG TRP A 244 47.661 72.650 106.257 1.00 94.45 ATOM 1991 CD1 TRP A 244 47.399 73.751 105.496 1.00 94.45 ATOM 1992 CD2 TRP A 244 46.636 72.597 107.260 1.00 94.45 ATOM 1993 NE1 TRP A 244 46.283 74.396 105.969 1.00 94.45 ATOM 1994 CE2 TRP A 244 45.802 73.694 107.055 1.00 94.45 ATOM 1995 CE3 TRP A 244 46.408 71.707 108.272 1.00 94.45 ATOM 1996 CZ2 TRP A 244 44.724 73.920 107.862 1.00 94.45 ATOM 1997 CZ3 TRP A 244 45.321 71.939 109.084 1.00 94.45 ATOM 1998 CH2 TRP A 244 44.496 73.026 108.883 1.00 94.45 ATOM 1999 N ALA A 245 48.144 68.790 107.190 1.00 42.43 ATOM 2000 CA ALA A 245 47.403 67.985 108.125 1.00 42.43 ATOM 2001 C ALA A 245 47.937 68.329 109.484 1.00 42.43 ATOM 2002 O ALA A 245 49.142 68.522 109.641 1.00 42.43 ATOM 2003 CB ALA A 245 47.597 66.472 107.915 1.00 42.43 ATOM 2004 N ALA A 246 47.056 68.414 110.509 1.00 42.66 ATOM 2005 CA ALA A 246 47.527 68.815 111.809 1.00 42.66 ATOM 2006 C ALA A 246 46.920 67.959 112.878 1.00 42.66 ATOM 2007 O ALA A 246 45.812 67.444 112.734 1.00 42.66 ATOM 2008 CB ALA A 246 47.185 70.273 112.160 1.00 42.66 ATOM 2009 N VAL A 247 47.675 67.776 113.984 1.00 46.92 ATOM 2010 CA VAL A 247 47.220 67.037 115.127 1.00 46.92 ATOM 2011 C VAL A 247 47.648 67.780 116.353 1.00 46.92 ATOM 2012 O VAL A 247 48.694 68.427 116.366 1.00 46.92 ATOM 2013 CB VAL A 247 47.794 65.650 115.215 1.00 46.92 ATOM 2014 CG1 VAL A 247 47.212 64.804 114.070 1.00 46.92 ATOM 2015 CG2 VAL A 247 49.329 65.755 115.172 1.00 46.92 ATOM 2016 N VAL A 248 46.828 67.714 117.424 1.00 41.51 ATOM 2017 CA VAL A 248 47.181 68.357 118.658 1.00 41.51 ATOM 2018 C VAL A 248 47.747 67.279 119.524 1.00 41.51 ATOM 2019 O VAL A 248 47.114 66.244 119.726 1.00 41.51 ATOM 2020 CB VAL A 248 46.008 68.947 119.384 1.00 41.51 ATOM 2021 CG1 VAL A 248 46.496 69.521 120.724 1.00 41.51 ATOM 2022 CG2 VAL A 248 45.338 69.984 118.469 1.00 41.51 ATOM 2023 N VAL A 249 48.966 67.496 120.060 1.00 50.38 ATOM 2024 CA VAL A 249 49.600 66.459 120.825 1.00 50.38 ATOM 2025 C VAL A 249 50.027 66.999 122.153 1.00 50.38 ATOM 2026 O VAL A 249 50.150 68.206 122.358 1.00 50.38 ATOM 2027 CB VAL A 249 50.819 65.896 120.158 1.00 50.38 ATOM 2028 CG1 VAL A 249 50.393 65.285 118.811 1.00 50.38 ATOM 2029 CG2 VAL A 249 51.877 67.005 120.038 1.00 50.38 ATOM 2030 N PRO A 250 50.219 66.094 123.079 1.00 68.90 ATOM 2031 CA PRO A 250 50.665 66.495 124.384 1.00 68.90 ATOM 2032 C PRO A 250 52.088 66.942 124.303 1.00 68.90 ATOM 2033 O PRO A 250 52.871 66.323 123.584 1.00 68.90 ATOM 2034 CB PRO A 250 50.429 65.294 125.295 1.00 68.90 ATOM 2035 CG PRO A 250 49.245 64.567 124.628 1.00 68.90 ATOM 2036 CD PRO A 250 49.380 64.906 123.134 1.00 68.90 ATOM 2037 N SER A 251 52.449 67.998 125.052 1.00 34.66 ATOM 2038 CA SER A 251 53.782 68.518 124.983 1.00 34.66 ATOM 2039 C SER A 251 54.711 67.496 125.550 1.00 34.66 ATOM 2040 O SER A 251 54.431 66.903 126.591 1.00 34.66 ATOM 2041 CB SER A 251 53.968 69.813 125.792 1.00 34.66 ATOM 2042 OG SER A 251 53.127 70.835 125.275 1.00 34.66 ATOM 2043 N GLY A 252 55.855 67.279 124.863 1.00 33.38 ATOM 2044 CA GLY A 252 56.864 66.351 125.288 1.00 33.38 ATOM 2045 C GLY A 252 56.721 65.081 124.500 1.00 33.38 ATOM 2046 O GLY A 252 57.680 64.329 124.343 1.00 33.38 ATOM 2047 N GLU A 253 55.495 64.817 124.013 1.00 93.26 ATOM 2048 CA GLU A 253 55.088 63.666 123.250 1.00 93.26 ATOM 2049 C GLU A 253 55.436 63.746 121.785 1.00 93.26 ATOM 2050 O GLU A 253 55.248 62.770 121.064 1.00 93.26 ATOM 2051 CB GLU A 253 53.596 63.325 123.393 1.00 93.26 ATOM 2052 CG GLU A 253 53.269 62.827 124.803 1.00 93.26 ATOM 2053 CD GLU A 253 51.904 62.161 124.790 1.00 93.26 ATOM 2054 OE1 GLU A 253 51.334 61.994 123.678 1.00 93.26 ATOM 2055 OE2 GLU A 253 51.419 61.797 125.894 1.00 93.26 ATOM 2056 N GLU A 254 55.925 64.897 121.286 1.00102.82 ATOM 2057 CA GLU A 254 56.055 65.149 119.869 1.00102.82 ATOM 2058 C GLU A 254 56.772 64.055 119.118 1.00102.82 ATOM 2059 O GLU A 254 56.414 63.766 117.977 1.00102.82 ATOM 2060 CB GLU A 254 56.808 66.452 119.543 1.00102.82 ATOM 2061 CG GLU A 254 56.043 67.734 119.880 1.00102.82 ATOM 2062 CD GLU A 254 56.326 68.094 121.329 1.00102.82 ATOM 2063 OE1 GLU A 254 56.897 67.233 122.051 1.00102.82 ATOM 2064 OE2 GLU A 254 55.978 69.235 121.733 1.00102.82 ATOM 2065 N GLN A 255 57.796 63.418 119.710 1.00 74.38 ATOM 2066 CA GLN A 255 58.588 62.422 119.032 1.00 74.38 ATOM 2067 C GLN A 255 57.777 61.215 118.658 1.00 74.38 ATOM 2068 O GLN A 255 58.140 60.483 117.740 1.00 74.38 ATOM 2069 CB GLN A 255 59.808 61.967 119.845 1.00 74.38 ATOM 2070 CG GLN A 255 60.824 63.096 120.013 1.00 74.38 ATOM 2071 CD GLN A 255 61.143 63.622 118.620 1.00 74.38 ATOM 2072 OE1 GLN A 255 61.489 62.859 117.720 1.00 74.38 ATOM 2073 NE2 GLN A 255 61.008 64.962 118.431 1.00 74.38 ATOM 2074 N ARG A 256 56.690 60.938 119.392 1.00128.23 ATOM 2075 CA ARG A 256 55.837 59.808 119.153 1.00128.23 ATOM 2076 C ARG A 256 55.149 59.946 117.821 1.00128.23 ATOM 2077 O ARG A 256 54.689 58.950 117.265 1.00128.23 ATOM 2078 CB ARG A 256 54.743 59.651 120.222 1.00128.23 ATOM 2079 CG ARG A 256 55.305 59.297 121.599 1.00128.23 ATOM 2080 CD ARG A 256 54.226 59.142 122.669 1.00128.23 ATOM 2081 NE ARG A 256 53.273 58.101 122.195 1.00128.23 ATOM 2082 CZ ARG A 256 52.204 57.762 122.972 1.00128.23 ATOM 2083 NH1 ARG A 256 52.016 58.374 124.177 1.00128.23 ATOM 2084 NH2 ARG A 256 51.325 56.809 122.546 1.00128.23 ATOM 2085 N TYR A 257 55.031 61.179 117.282 1.00 78.27 ATOM 2086 CA TYR A 257 54.238 61.380 116.097 1.00 78.27 ATOM 2087 C TYR A 257 55.081 61.546 114.867 1.00 78.27 ATOM 2088 O TYR A 257 56.129 62.190 114.878 1.00 78.27 ATOM 2089 CB TYR A 257 53.345 62.630 116.187 1.00 78.27 ATOM 2090 CG TYR A 257 52.361 62.407 117.284 1.00 78.27 ATOM 2091 CD1 TYR A 257 52.738 62.541 118.600 1.00 78.27 ATOM 2092 CD2 TYR A 257 51.058 62.076 116.996 1.00 78.27 ATOM 2093 CE1 TYR A 257 51.830 62.339 119.614 1.00 78.27 ATOM 2094 CE2 TYR A 257 50.147 61.873 118.004 1.00 78.27 ATOM 2095 CZ TYR A 257 50.532 62.002 119.316 1.00 78.27 ATOM 2096 OH TYR A 257 49.598 61.793 120.353 1.00 78.27 ATOM 2097 N THR A 258 54.626 60.918 113.756 1.00 54.90 ATOM 2098 CA THR A 258 55.307 61.022 112.497 1.00 54.90 ATOM 2099 C THR A 258 54.298 61.355 111.432 1.00 54.90 ATOM 2100 O THR A 258 53.168 60.867 111.453 1.00 54.90 ATOM 2101 CB THR A 258 56.006 59.752 112.100 1.00 54.90 ATOM 2102 OG1 THR A 258 55.070 58.689 112.009 1.00 54.90 ATOM 2103 CG2 THR A 258 57.087 59.424 113.146 1.00 54.90 ATOM 2104 N CYS A 259 54.692 62.226 110.476 1.00 48.60 ATOM 2105 CA CYS A 259 53.852 62.590 109.365 1.00 48.60 ATOM 2106 C CYS A 259 54.307 61.775 108.198 1.00 48.60 ATOM 2107 O CYS A 259 55.504 61.664 107.941 1.00 48.60 ATOM 2108 CB CYS A 259 53.967 64.073 108.952 1.00 48.60 ATOM 2109 SG CYS A 259 53.122 64.443 107.381 1.00 48.60 ATOM 2110 N HIS A 260 53.352 61.175 107.458 1.00 53.45 ATOM 2111 CA HIS A 260 53.725 60.350 106.347 1.00 53.45 ATOM 2112 C HIS A 260 53.109 60.926 105.115 1.00 53.45 ATOM 2113 O HIS A 260 51.920 61.244 105.096 1.00 53.45 ATOM 2114 CB HIS A 260 53.226 58.905 106.493 1.00 53.45 ATOM 2115 CG HIS A 260 53.836 58.225 107.682 1.00 53.45 ATOM 2116 ND1 HIS A 260 54.986 57.469 107.631 1.00 53.45 ATOM 2117 CD2 HIS A 260 53.443 58.216 108.985 1.00 53.45 ATOM 2118 CE1 HIS A 260 55.230 57.042 108.896 1.00 53.45 ATOM 2119 NE2 HIS A 260 54.320 57.470 109.753 1.00 53.45 ATOM 2120 N VAL A 261 53.917 61.088 104.048 1.00120.08 ATOM 2121 CA VAL A 261 53.395 61.631 102.828 1.00120.08 ATOM 2122 C VAL A 261 53.621 60.678 101.705 1.00120.08 ATOM 2123 O VAL A 261 54.670 60.046 101.594 1.00120.08 ATOM 2124 CB VAL A 261 53.990 62.951 102.419 1.00120.08 ATOM 2125 CG1 VAL A 261 53.411 64.068 103.295 1.00120.08 ATOM 2126 CG2 VAL A 261 55.515 62.839 102.552 1.00120.08 ATOM 2127 N GLN A 262 52.593 60.550 100.842 1.00 54.87 ATOM 2128 CA GLN A 262 52.686 59.712 99.689 1.00 54.87 ATOM 2129 C GLN A 262 52.243 60.534 98.525 1.00 54.87 ATOM 2130 O GLN A 262 51.171 61.140 98.554 1.00 54.87 ATOM 2131 CB GLN A 262 51.761 58.490 99.761 1.00 54.87 ATOM 2132 CG GLN A 262 52.102 57.557 100.921 1.00 54.87 ATOM 2133 CD GLN A 262 51.090 56.426 100.908 1.00 54.87 ATOM 2134 OE1 GLN A 262 50.965 55.700 99.924 1.00 54.87 ATOM 2135 NE2 GLN A 262 50.333 56.282 102.030 1.00 54.87 ATOM 2136 N HIS A 263 53.082 60.580 97.473 1.00 53.19 ATOM 2137 CA HIS A 263 52.772 61.316 96.283 1.00 53.19 ATOM 2138 C HIS A 263 53.481 60.621 95.164 1.00 53.19 ATOM 2139 O HIS A 263 54.494 59.958 95.373 1.00 53.19 ATOM 2140 CB HIS A 263 53.276 62.770 96.318 1.00 53.19 ATOM 2141 CG HIS A 263 52.841 63.583 95.134 1.00 53.19 ATOM 2142 ND1 HIS A 263 51.599 64.162 95.010 1.00 53.19 ATOM 2143 CD2 HIS A 263 53.522 63.920 94.005 1.00 53.19 ATOM 2144 CE1 HIS A 263 51.588 64.818 93.822 1.00 53.19 ATOM 2145 NE2 HIS A 263 52.734 64.698 93.175 1.00 53.19 ATOM 2146 N GLU A 264 52.962 60.770 93.936 1.00 46.36 ATOM 2147 CA GLU A 264 53.492 60.116 92.771 1.00 46.36 ATOM 2148 C GLU A 264 54.888 60.599 92.477 1.00 46.36 ATOM 2149 O GLU A 264 55.725 59.837 91.997 1.00 46.36 ATOM 2150 CB GLU A 264 52.631 60.378 91.525 1.00 46.36 ATOM 2151 CG GLU A 264 53.117 59.654 90.271 1.00 46.36 ATOM 2152 CD GLU A 264 52.167 60.015 89.138 1.00 46.36 ATOM 2153 OE1 GLU A 264 51.508 61.085 89.234 1.00 46.36 ATOM 2154 OE2 GLU A 264 52.085 59.223 88.161 1.00 46.36 ATOM 2155 N GLY A 265 55.162 61.888 92.735 1.00 50.37 ATOM 2156 CA GLY A 265 56.410 62.531 92.420 1.00 50.37 ATOM 2157 C GLY A 265 57.566 61.996 93.211 1.00 50.37 ATOM 2158 O GLY A 265 58.696 62.040 92.734 1.00 50.37 ATOM 2159 N LEU A 266 57.336 61.546 94.463 1.00 66.22 ATOM 2160 CA LEU A 266 58.403 61.130 95.342 1.00 66.22 ATOM 2161 C LEU A 266 58.922 59.771 94.961 1.00 66.22 ATOM 2162 O LEU A 266 58.173 58.893 94.535 1.00 66.22 ATOM 2163 CB LEU A 266 57.947 61.034 96.811 1.00 66.22 ATOM 2164 CG LEU A 266 57.499 62.377 97.428 1.00 66.22 ATOM 2165 CD1 LEU A 266 57.057 62.201 98.890 1.00 66.22 ATOM 2166 CD2 LEU A 266 58.587 63.452 97.275 1.00 66.22 ATOM 2167 N PRO A 267 60.219 59.592 95.082 1.00 72.54 ATOM 2168 CA PRO A 267 60.802 58.301 94.826 1.00 72.54 ATOM 2169 C PRO A 267 60.327 57.308 95.836 1.00 72.54 ATOM 2170 O PRO A 267 60.142 56.143 95.485 1.00 72.54 ATOM 2171 CB PRO A 267 62.311 58.521 94.812 1.00 72.54 ATOM 2172 CG PRO A 267 62.451 59.984 94.348 1.00 72.54 ATOM 2173 CD PRO A 267 61.162 60.671 94.837 1.00 72.54 ATOM 2174 N LYS A 268 60.138 57.747 97.096 1.00132.90 ATOM 2175 CA LYS A 268 59.645 56.882 98.125 1.00132.90 ATOM 2176 C LYS A 268 58.871 57.748 99.066 1.00132.90 ATOM 2177 O LYS A 268 59.064 58.962 99.103 1.00132.90 ATOM 2178 CB LYS A 268 60.748 56.171 98.929 1.00132.90 ATOM 2179 CG LYS A 268 61.632 57.107 99.753 1.00132.90 ATOM 2180 CD LYS A 268 62.370 58.153 98.922 1.00132.90 ATOM 2181 CE LYS A 268 63.318 59.030 99.741 1.00132.90 ATOM 2182 NZ LYS A 268 64.067 59.936 98.842 1.00132.90 ATOM 2183 N PRO A 269 58.003 57.160 99.838 1.00 65.38 ATOM 2184 CA PRO A 269 57.213 57.947 100.742 1.00 65.38 ATOM 2185 C PRO A 269 58.084 58.547 101.795 1.00 65.38 ATOM 2186 O PRO A 269 59.142 57.992 102.088 1.00 65.38 ATOM 2187 CB PRO A 269 56.128 57.009 101.265 1.00 65.38 ATOM 2188 CG PRO A 269 55.930 56.014 100.105 1.00 65.38 ATOM 2189 CD PRO A 269 57.297 55.966 99.400 1.00 65.38 ATOM 2190 N LEU A 270 57.666 59.694 102.361 1.00 62.94 ATOM 2191 CA LEU A 270 58.470 60.375 103.335 1.00 62.94 ATOM 2192 C LEU A 270 57.875 60.174 104.688 1.00 62.94 ATOM 2193 O LEU A 270 56.661 60.039 104.841 1.00 62.94 ATOM 2194 CB LEU A 270 58.498 61.900 103.129 1.00 62.94 ATOM 2195 CG LEU A 270 59.138 62.374 101.812 1.00 62.94 ATOM 2196 CD1 LEU A 270 59.111 63.909 101.713 1.00 62.94 ATOM 2197 CD2 LEU A 270 60.555 61.802 101.632 1.00 62.94 ATOM 2198 N THR A 271 58.750 60.106 105.709 1.00 50.03 ATOM 2199 CA THR A 271 58.320 60.065 107.073 1.00 50.03 ATOM 2200 C THR A 271 58.973 61.254 107.699 1.00 50.03 ATOM 2201 O THR A 271 60.197 61.378 107.668 1.00 50.03 ATOM 2202 CB THR A 271 58.793 58.855 107.826 1.00 50.03 ATOM 2203 OG1 THR A 271 58.315 57.670 107.209 1.00 50.03 ATOM 2204 CG2 THR A 271 58.280 58.947 109.272 1.00 50.03 ATOM 2205 N LEU A 272 58.178 62.178 108.273 1.00109.35 ATOM 2206 CA LEU A 272 58.802 63.348 108.816 1.00109.35 ATOM 2207 C LEU A 272 58.384 63.524 110.238 1.00109.35 ATOM 2208 O LEU A 272 57.342 63.029 110.663 1.00109.35 ATOM 2209 CB LEU A 272 58.451 64.635 108.060 1.00109.35 ATOM 2210 CG LEU A 272 58.709 64.496 106.550 1.00109.35 ATOM 2211 CD1 LEU A 272 57.580 63.706 105.872 1.00109.35 ATOM 2212 CD2 LEU A 272 58.994 65.843 105.884 1.00109.35 ATOM 2213 N ARG A 273 59.231 64.229 111.018 1.00 73.47 ATOM 2214 CA ARG A 273 58.951 64.506 112.397 1.00 73.47 ATOM 2215 C ARG A 273 59.280 65.945 112.628 1.00 73.47 ATOM 2216 O ARG A 273 59.964 66.573 111.822 1.00 73.47 ATOM 2217 CB ARG A 273 59.821 63.715 113.386 1.00 73.47 ATOM 2218 CG ARG A 273 59.542 62.214 113.384 1.00 73.47 ATOM 2219 CD ARG A 273 60.416 61.447 114.374 1.00 73.47 ATOM 2220 NE ARG A 273 60.010 60.017 114.309 1.00 73.47 ATOM 2221 CZ ARG A 273 60.783 59.070 114.910 1.00 73.47 ATOM 2222 NH1 ARG A 273 61.932 59.436 115.548 1.00 73.47 ATOM 2223 NH2 ARG A 273 60.402 57.761 114.885 1.00 73.47 ATOM 2224 N TRP A 274 58.766 66.513 113.735 1.00 76.12 ATOM 2225 CA TRP A 274 59.074 67.873 114.049 1.00 76.12 ATOM 2226 C TRP A 274 60.488 67.904 114.527 1.00 76.12 ATOM 2227 O TRP A 274 60.895 67.096 115.361 1.00 76.12 ATOM 2228 CB TRP A 274 58.161 68.456 115.145 1.00 76.12 ATOM 2229 CG TRP A 274 58.450 69.889 115.530 1.00 76.12 ATOM 2230 CD1 TRP A 274 58.444 71.009 114.752 1.00 76.12 ATOM 2231 CD2 TRP A 274 58.735 70.325 116.869 1.00 76.12 ATOM 2232 NE1 TRP A 274 58.717 72.117 115.521 1.00 76.12 ATOM 2233 CE2 TRP A 274 58.893 71.710 116.827 1.00 76.12 ATOM 2234 CE3 TRP A 274 58.843 69.629 118.040 1.00 76.12 ATOM 2235 CZ2 TRP A 274 59.169 72.424 117.958 1.00 76.12 ATOM 2236 CZ3 TRP A 274 59.128 70.353 119.178 1.00 76.12 ATOM 2237 CH2 TRP A 274 59.289 71.722 119.137 1.00 76.12 ATOM 2238 N GLU A 275 61.298 68.828 113.978 1.00 99.18 ATOM 2239 CA GLU A 275 62.650 68.910 114.432 1.00 99.18 ATOM 2240 C GLU A 275 62.865 70.295 114.930 1.00 99.18 ATOM 2241 O GLU A 275 62.806 71.278 114.192 1.00 99.18 ATOM 2242 CB GLU A 275 63.678 68.558 113.345 1.00 99.18 ATOM 2243 CG GLU A 275 63.534 69.359 112.055 1.00 99.18 ATOM 2244 CD GLU A 275 64.230 68.545 110.974 1.00 99.18 ATOM 2245 OE1 GLU A 275 64.538 67.356 111.252 1.00 99.18 ATOM 2246 OE2 GLU A 275 64.452 69.090 109.860 1.00 99.18 ATOM 2247 N PRO A 276 63.099 70.361 116.207 1.00 78.56 ATOM 2248 CA PRO A 276 63.304 71.642 116.816 1.00 78.56 ATOM 2249 C PRO A 276 64.687 72.122 116.527 1.00 78.56 ATOM 2250 O PRO A 276 64.829 73.149 115.810 1.00 78.56 ATOM 2251 CB PRO A 276 63.027 71.453 118.305 1.00 78.56 ATOM 2252 CG PRO A 276 62.042 70.275 118.342 1.00 78.56 ATOM 2253 CD PRO A 276 62.400 69.447 117.098 1.00 78.56 TER 2254 PRO A 276 ATOM 2255 N ILE B 1 19.618 74.552 100.179 1.00 28.94 ATOM 2256 CA ILE B 1 19.846 74.652 98.700 1.00 27.59 ATOM 2257 C ILE B 1 21.115 75.417 98.354 1.00 26.73 ATOM 2258 O ILE B 1 21.603 75.286 97.234 1.00 28.40 ATOM 2259 CB ILE B 1 18.653 75.337 97.963 1.00 28.34 ATOM 2260 CG1 ILE B 1 17.908 76.279 98.917 1.00 28.64 ATOM 2261 CG2 ILE B 1 17.729 74.287 97.375 1.00 28.65 ATOM 2262 CD1 ILE B 1 17.159 77.407 98.239 1.00 29.26 ATOM 2263 N GLN B 2 21.638 76.218 99.291 1.00 24.86 ATOM 2264 CA GLN B 2 22.826 77.041 99.029 1.00 23.18 ATOM 2265 C GLN B 2 23.972 76.644 99.954 1.00 21.53 ATOM 2266 O GLN B 2 23.738 76.170 101.079 1.00 21.51 ATOM 2267 CB GLN B 2 22.480 78.530 99.151 1.00 23.48 ATOM 2268 CG GLN B 2 21.285 78.910 98.262 1.00 23.73 ATOM 2269 CD GLN B 2 20.974 80.397 98.233 1.00 23.75 ATOM 2270 OE1 GLN B 2 21.005 81.068 99.256 1.00 25.79 ATOM 2271 NE2 GLN B 2 20.634 80.905 97.051 1.00 24.82 ATOM 2272 N ARG B 3 25.209 76.825 99.486 1.00 19.71 ATOM 2273 CA ARG B 3 26.393 76.425 100.253 1.00 19.20 ATOM 2274 C ARG B 3 27.337 77.594 100.386 1.00 17.85 ATOM 2275 O ARG B 3 27.606 78.289 99.409 1.00 16.70 ATOM 2276 CB ARG B 3 27.113 75.252 99.574 1.00 18.74 ATOM 2277 CG ARG B 3 26.358 73.933 99.698 1.00 20.17 ATOM 2278 CD ARG B 3 27.025 72.794 98.956 1.00 20.73 ATOM 2279 NE ARG B 3 26.295 72.480 97.739 1.00 22.22 ATOM 2280 CZ ARG B 3 26.648 71.554 96.846 1.00 22.83 ATOM 2281 NH1 ARG B 3 27.745 70.830 97.010 1.00 22.73 ATOM 2282 NH2 ARG B 3 25.881 71.360 95.777 1.00 24.50 ATOM 2283 N THR B 4 27.832 77.828 101.598 1.00 17.80 ATOM 2284 CA THR B 4 28.648 79.001 101.865 1.00 17.35 ATOM 2285 C THR B 4 30.094 78.683 101.493 1.00 16.57 ATOM 2286 O THR B 4 30.513 77.529 101.611 1.00 16.10 ATOM 2287 CB THR B 4 28.555 79.442 103.360 1.00 17.90 ATOM 2288 OG1 THR B 4 28.844 80.836 103.465 1.00 19.53 ATOM 2289 CG2 THR B 4 29.496 78.639 104.230 1.00 18.39 ATOM 2290 N PRO B 5 30.838 79.685 100.999 1.00 16.31 ATOM 2291 CA PRO B 5 32.225 79.422 100.620 1.00 16.31 ATOM 2292 C PRO B 5 33.163 79.127 101.772 1.00 16.60 ATOM 2293 O PRO B 5 33.039 79.736 102.869 1.00 16.05 ATOM 2294 CB PRO B 5 32.660 80.720 99.925 1.00 16.36 ATOM 2295 CG PRO B 5 31.722 81.752 100.419 1.00 17.62 ATOM 2296 CD PRO B 5 30.440 81.068 100.675 1.00 16.28 ATOM 2297 N LYS B 6 34.051 78.163 101.526 1.00 15.66 ATOM 2298 CA LYS B 6 35.296 78.010 102.291 1.00 16.43 ATOM 2299 C LYS B 6 36.309 78.997 101.723 1.00 15.28 ATOM 2300 O LYS B 6 36.295 79.285 100.511 1.00 15.08 ATOM 2301 CB LYS B 6 35.839 76.594 102.149 1.00 16.69 ATOM 2302 CG LYS B 6 34.923 75.540 102.732 1.00 18.85 ATOM 2303 CD LYS B 6 35.426 74.133 102.451 1.00 19.61 ATOM 2304 CE LYS B 6 35.204 73.738 100.987 1.00 23.44 ATOM 2305 NZ LYS B 6 35.339 72.280 100.750 1.00 24.92 ATOM 2306 N ILE B 7 37.193 79.508 102.586 1.00 14.75 ATOM 2307 CA ILE B 7 38.131 80.558 102.212 1.00 15.09 ATOM 2308 C ILE B 7 39.518 80.246 102.771 1.00 15.06 ATOM 2309 O ILE B 7 39.642 80.021 103.985 1.00 15.24 ATOM 2310 CB ILE B 7 37.696 81.962 102.767 1.00 15.09 ATOM 2311 CG1 ILE B 7 36.266 82.307 102.347 1.00 16.42 ATOM 2312 CG2 ILE B 7 38.659 83.052 102.280 1.00 14.96 ATOM 2313 CD1 ILE B 7 35.708 83.538 103.065 1.00 16.35 ATOM 2314 N GLN B 8 40.532 80.210 101.901 1.00 14.35 ATOM 2315 CA GLN B 8 41.947 80.139 102.313 1.00 14.54 ATOM 2316 C GLN B 8 42.745 81.283 101.709 1.00 15.20 ATOM 2317 O GLN B 8 42.613 81.609 100.523 1.00 15.32 ATOM 2318 CB GLN B 8 42.615 78.798 101.950 1.00 13.91 ATOM 2319 CG GLN B 8 42.012 77.594 102.633 1.00 13.91 ATOM 2320 CD GLN B 8 42.878 76.368 102.518 1.00 13.48 ATOM 2321 OE1 GLN B 8 43.982 76.333 103.069 1.00 14.71 ATOM 2322 NE2 GLN B 8 42.367 75.324 101.842 1.00 12.61 ATOM 2323 N VAL B 9 43.585 81.902 102.536 1.00 14.41 ATOM 2324 CA VAL B 9 44.416 83.004 102.102 1.00 15.07 ATOM 2325 C VAL B 9 45.860 82.646 102.403 1.00 14.79 ATOM 2326 O VAL B 9 46.185 82.276 103.521 1.00 15.40 ATOM 2327 CB VAL B 9 44.035 84.329 102.818 1.00 15.55 ATOM 2328 CG1 VAL B 9 44.751 85.496 102.169 1.00 15.59 ATOM 2329 CG2 VAL B 9 42.507 84.522 102.796 1.00 17.50 ATOM 2330 N TYR B 10 46.695 82.709 101.387 1.00 15.20 ATOM 2331 CA TYR B 10 48.046 82.151 101.461 1.00 15.55 ATOM 2332 C TYR B 10 48.880 82.660 100.307 1.00 16.23 ATOM 2333 O TYR B 10 48.359 83.276 99.377 1.00 17.51 ATOM 2334 CB TYR B 10 47.979 80.610 101.450 1.00 15.11 ATOM 2335 CG TYR B 10 47.245 80.026 100.238 1.00 13.67 ATOM 2336 CD1 TYR B 10 45.848 80.030 100.176 1.00 13.98 ATOM 2337 CD2 TYR B 10 47.946 79.484 99.168 1.00 14.72 ATOM 2338 CE1 TYR B 10 45.160 79.512 99.068 1.00 13.48 ATOM 2339 CE2 TYR B 10 47.267 78.958 98.040 1.00 13.08 ATOM 2340 CZ TYR B 10 45.878 78.979 98.003 1.00 13.21 ATOM 2341 OH TYR B 10 45.180 78.483 96.914 1.00 14.01 ATOM 2342 N SER B 11 50.184 82.404 100.362 1.00 16.91 ATOM 2343 CA SER B 11 51.081 82.831 99.305 1.00 16.57 ATOM 2344 C SER B 11 51.490 81.638 98.441 1.00 16.31 ATOM 2345 O SER B 11 51.488 80.503 98.897 1.00 15.48 ATOM 2346 CB SER B 11 52.307 83.538 99.882 1.00 17.35 ATOM 2347 OG SER B 11 52.946 82.724 100.843 1.00 16.66 ATOM 2348 N ARG B 12 51.836 81.906 97.191 1.00 16.61 ATOM 2349 CA ARG B 12 52.324 80.853 96.302 1.00 17.37 ATOM 2350 C ARG B 12 53.611 80.205 96.818 1.00 18.42 ATOM 2351 O ARG B 12 53.739 78.987 96.820 1.00 17.72 ATOM 2352 CB ARG B 12 52.582 81.418 94.902 1.00 16.80 ATOM 2353 CG ARG B 12 53.089 80.369 93.893 1.00 16.86 ATOM 2354 CD ARG B 12 53.302 80.999 92.524 1.00 16.58 ATOM 2355 NE ARG B 12 52.059 81.500 91.935 1.00 17.11 ATOM 2356 CZ ARG B 12 51.970 82.064 90.735 1.00 18.15 ATOM 2357 NH1 ARG B 12 53.045 82.186 89.968 1.00 19.07 ATOM 2358 NH2 ARG B 12 50.804 82.501 90.284 1.00 18.11 ATOM 2359 N HIS B 13 54.569 81.053 97.191 1.00 19.88 ATOM 2360 CA HIS B 13 55.885 80.641 97.665 1.00 21.12 ATOM 2361 C HIS B 13 55.985 80.964 99.162 1.00 22.56 ATOM 2362 O HIS B 13 55.233 81.791 99.667 1.00 22.03 ATOM 2363 CB HIS B 13 56.969 81.389 96.880 1.00 21.63 ATOM 2364 CG HIS B 13 56.922 81.146 95.404 1.00 22.30 ATOM 2365 ND1 HIS B 13 57.151 79.904 94.851 1.00 24.01 ATOM 2366 CD2 HIS B 13 56.692 81.983 94.364 1.00 23.49 ATOM 2367 CE1 HIS B 13 57.054 79.984 93.537 1.00 22.96 ATOM 2368 NE2 HIS B 13 56.769 81.233 93.214 1.00 23.84 ATOM 2369 N PRO B 14 56.903 80.301 99.890 1.00 23.79 ATOM 2370 CA PRO B 14 57.090 80.684 101.288 1.00 24.93 ATOM 2371 C PRO B 14 57.377 82.175 101.399 1.00 25.62 ATOM 2372 O PRO B 14 58.147 82.704 100.610 1.00 25.94 ATOM 2373 CB PRO B 14 58.315 79.865 101.712 1.00 25.29 ATOM 2374 CG PRO B 14 58.313 78.709 100.823 1.00 24.46 ATOM 2375 CD PRO B 14 57.795 79.192 99.508 1.00 24.31 ATOM 2376 N ALA B 15 56.739 82.837 102.357 1.00 27.42 ATOM 2377 CA ALA B 15 56.836 84.286 102.485 1.00 28.39 ATOM 2378 C ALA B 15 58.219 84.706 103.004 1.00 29.64 ATOM 2379 O ALA B 15 58.700 84.186 104.013 1.00 30.02 ATOM 2380 CB ALA B 15 55.726 84.812 103.408 1.00 28.44 ATOM 2381 N GLU B 16 58.847 85.620 102.274 1.00 30.70 ATOM 2382 CA GLU B 16 60.099 86.258 102.682 1.00 32.08 ATOM 2383 C GLU B 16 59.940 87.763 102.476 1.00 31.98 ATOM 2384 O GLU B 16 59.733 88.222 101.355 1.00 32.55 ATOM 2385 CB GLU B 16 61.276 85.722 101.852 1.00 32.13 ATOM 2386 CG GLU B 16 61.574 84.230 102.079 1.00 34.72 ATOM 2387 CD GLU B 16 62.563 83.636 101.060 1.00 35.47 ATOM 2388 OE1 GLU B 16 62.516 82.398 100.845 1.00 40.42 ATOM 2389 OE2 GLU B 16 63.383 84.394 100.479 1.00 40.64 ATOM 2390 N ASN B 17 60.019 88.524 103.565 1.00 32.48 ATOM 2391 CA ASN B 17 59.901 89.987 103.518 1.00 32.51 ATOM 2392 C ASN B 17 60.803 90.593 102.460 1.00 32.41 ATOM 2393 O ASN B 17 61.961 90.194 102.325 1.00 32.62 ATOM 2394 CB ASN B 17 60.209 90.604 104.889 1.00 32.86 ATOM 2395 CG ASN B 17 59.168 90.262 105.917 1.00 33.95 ATOM 2396 OD1 ASN B 17 57.991 90.138 105.590 1.00 36.50 ATOM 2397 ND2 ASN B 17 59.588 90.087 107.167 1.00 35.12 ATOM 2398 N GLY B 18 60.258 91.529 101.690 1.00 31.91 ATOM 2399 CA GLY B 18 60.991 92.174 100.616 1.00 31.70 ATOM 2400 C GLY B 18 61.172 91.391 99.331 1.00 31.90 ATOM 2401 O GLY B 18 61.751 91.910 98.369 1.00 31.99 ATOM 2402 N LYS B 19 60.679 90.150 99.294 1.00 31.66 ATOM 2403 CA LYS B 19 60.754 89.314 98.105 1.00 30.67 ATOM 2404 C LYS B 19 59.352 89.212 97.496 1.00 29.92 ATOM 2405 O LYS B 19 58.391 88.867 98.186 1.00 29.66 ATOM 2406 CB LYS B 19 61.266 87.923 98.474 1.00 31.36 ATOM 2407 CG LYS B 19 61.306 86.927 97.314 1.00 32.47 ATOM 2408 CD LYS B 19 62.708 86.421 96.999 1.00 34.54 ATOM 2409 CE LYS B 19 62.657 85.229 96.042 1.00 35.27 ATOM 2410 NZ LYS B 19 62.465 83.921 96.731 1.00 37.48 ATOM 2411 N SER B 20 59.248 89.521 96.206 1.00 28.67 ATOM 2412 CA SER B 20 57.995 89.442 95.487 1.00 27.67 ATOM 2413 C SER B 20 57.489 87.997 95.508 1.00 26.70 ATOM 2414 O SER B 20 58.267 87.038 95.577 1.00 25.91 ATOM 2415 CB SER B 20 58.165 89.935 94.045 1.00 28.10 ATOM 2416 OG SER B 20 56.923 89.957 93.330 1.00 29.75 ATOM 2417 N ASN B 21 56.175 87.867 95.431 1.00 25.01 ATOM 2418 CA ASN B 21 55.498 86.594 95.631 1.00 24.06 ATOM 2419 C ASN B 21 54.119 86.777 94.982 1.00 23.15 ATOM 2420 O ASN B 21 53.884 87.782 94.293 1.00 23.03 ATOM 2421 CB ASN B 21 55.403 86.342 97.136 1.00 23.82 ATOM 2422 CG ASN B 21 55.230 84.881 97.513 1.00 24.15 ATOM 2423 OD1 ASN B 21 54.656 84.078 96.763 1.00 23.70 ATOM 2424 ND2 ASN B 21 55.707 84.537 98.707 1.00 22.31 ATOM 2425 N PHE B 22 53.230 85.808 95.161 1.00 21.97 ATOM 2426 CA PHE B 22 51.822 85.946 94.775 1.00 21.28 ATOM 2427 C PHE B 22 50.933 85.692 95.974 1.00 19.81 ATOM 2428 O PHE B 22 51.146 84.734 96.718 1.00 19.61 ATOM 2429 CB PHE B 22 51.460 84.963 93.673 1.00 22.39 ATOM 2430 CG PHE B 22 51.867 85.417 92.320 1.00 23.75 ATOM 2431 CD1 PHE B 22 53.145 85.177 91.855 1.00 23.66 ATOM 2432 CD2 PHE B 22 50.967 86.089 91.502 1.00 24.88 ATOM 2433 CE1 PHE B 22 53.524 85.608 90.584 1.00 24.18 ATOM 2434 CE2 PHE B 22 51.329 86.506 90.243 1.00 25.65 ATOM 2435 CZ PHE B 22 52.616 86.269 89.778 1.00 24.82 ATOM 2436 N LEU B 23 49.963 86.581 96.170 1.00 18.44 ATOM 2437 CA LEU B 23 48.957 86.450 97.193 1.00 18.23 ATOM 2438 C LEU B 23 47.726 85.776 96.571 1.00 17.25 ATOM 2439 O LEU B 23 47.213 86.253 95.547 1.00 16.27 ATOM 2440 CB LEU B 23 48.578 87.824 97.751 1.00 17.96 ATOM 2441 CG LEU B 23 47.489 87.854 98.834 1.00 18.83 ATOM 2442 CD1 LEU B 23 47.849 87.055 100.078 1.00 20.84 ATOM 2443 CD2 LEU B 23 47.127 89.319 99.176 1.00 19.15 ATOM 2444 N ASN B 24 47.302 84.671 97.196 1.00 16.26 ATOM 2445 CA ASN B 24 46.169 83.837 96.770 1.00 15.75 ATOM 2446 C ASN B 24 44.995 83.862 97.750 1.00 14.89 ATOM 2447 O ASN B 24 45.171 83.803 98.964 1.00 13.60 ATOM 2448 CB ASN B 24 46.623 82.364 96.630 1.00 15.14 ATOM 2449 CG ASN B 24 47.597 82.157 95.502 1.00 16.40 ATOM 2450 OD1 ASN B 24 47.582 82.878 94.501 1.00 17.27 ATOM 2451 ND2 ASN B 24 48.462 81.159 95.654 1.00 16.60 ATOM 2452 N CYS B 25 43.780 83.918 97.216 1.00 14.48 ATOM 2453 CA CYS B 25 42.585 83.669 97.994 1.00 14.17 ATOM 2454 C CYS B 25 41.795 82.621 97.229 1.00 13.87 ATOM 2455 O CYS B 25 41.324 82.906 96.132 1.00 13.41 ATOM 2456 CB CYS B 25 41.729 84.923 98.149 1.00 14.69 ATOM 2457 SG CYS B 25 40.313 84.686 99.267 1.00 15.79 ATOM 2458 N TYR B 26 41.728 81.422 97.792 1.00 13.28 ATOM 2459 CA TYR B 26 40.979 80.307 97.235 1.00 12.80 ATOM 2460 C TYR B 26 39.611 80.198 97.901 1.00 12.81 ATOM 2461 O TYR B 26 39.499 79.954 99.113 1.00 12.85 ATOM 2462 CB TYR B 26 41.770 79.016 97.447 1.00 14.01 ATOM 2463 CG TYR B 26 41.198 77.783 96.780 1.00 12.96 ATOM 2464 CD1 TYR B 26 40.993 77.748 95.408 1.00 13.46 ATOM 2465 CD2 TYR B 26 40.918 76.629 97.514 1.00 14.29 ATOM 2466 CE1 TYR B 26 40.511 76.614 94.790 1.00 14.42 ATOM 2467 CE2 TYR B 26 40.420 75.491 96.898 1.00 14.69 ATOM 2468 CZ TYR B 26 40.231 75.500 95.525 1.00 15.33 ATOM 2469 OH TYR B 26 39.749 74.375 94.887 1.00 17.40 ATOM 2470 N VAL B 27 38.565 80.395 97.103 1.00 12.65 ATOM 2471 CA VAL B 27 37.191 80.204 97.557 1.00 12.38 ATOM 2472 C VAL B 27 36.625 78.916 96.903 1.00 12.37 ATOM 2473 O VAL B 27 36.804 78.673 95.693 1.00 12.19 ATOM 2474 CB VAL B 27 36.289 81.437 97.272 1.00 12.75 ATOM 2475 CG1 VAL B 27 36.679 82.645 98.169 1.00 12.96 ATOM 2476 CG2 VAL B 27 36.353 81.812 95.831 1.00 12.25 ATOM 2477 N SER B 28 35.976 78.093 97.717 1.00 12.51 ATOM 2478 CA SER B 28 35.524 76.766 97.297 1.00 12.20 ATOM 2479 C SER B 28 34.287 76.287 98.067 1.00 12.41 ATOM 2480 O SER B 28 33.924 76.844 99.124 1.00 12.60 ATOM 2481 CB SER B 28 36.678 75.756 97.447 1.00 12.31 ATOM 2482 OG SER B 28 37.049 75.614 98.811 1.00 11.10 ATOM 2483 N GLY B 29 33.637 75.246 97.544 1.00 12.64 ATOM 2484 CA GLY B 29 32.495 74.629 98.235 1.00 12.81 ATOM 2485 C GLY B 29 31.223 75.455 98.300 1.00 13.21 ATOM 2486 O GLY B 29 30.352 75.167 99.134 1.00 14.66 ATOM 2487 N PHE B 30 31.103 76.451 97.414 1.00 12.58 ATOM 2488 CA PHE B 30 29.945 77.360 97.369 1.00 12.37 ATOM 2489 C PHE B 30 28.975 77.091 96.231 1.00 12.53 ATOM 2490 O PHE B 30 29.314 76.485 95.215 1.00 12.29 ATOM 2491 CB PHE B 30 30.390 78.844 97.390 1.00 12.01 ATOM 2492 CG PHE B 30 31.253 79.278 96.233 1.00 12.64 ATOM 2493 CD1 PHE B 30 30.699 79.883 95.116 1.00 12.53 ATOM 2494 CD2 PHE B 30 32.632 79.126 96.277 1.00 11.49 ATOM 2495 CE1 PHE B 30 31.495 80.291 94.058 1.00 12.80 ATOM 2496 CE2 PHE B 30 33.425 79.543 95.235 1.00 12.69 ATOM 2497 CZ PHE B 30 32.860 80.132 94.112 1.00 13.17 ATOM 2498 N HIS B 31 27.738 77.532 96.437 1.00 12.89 ATOM 2499 CA HIS B 31 26.675 77.370 95.474 1.00 12.87 ATOM 2500 C HIS B 31 25.566 78.310 95.958 1.00 13.81 ATOM 2501 O HIS B 31 25.243 78.297 97.165 1.00 13.92 ATOM 2502 CB HIS B 31 26.181 75.931 95.449 1.00 13.22 ATOM 2503 CG HIS B 31 25.684 75.491 94.112 1.00 13.01 ATOM 2504 ND1 HIS B 31 24.516 75.967 93.547 1.00 12.68 ATOM 2505 CD2 HIS B 31 26.204 74.613 93.226 1.00 12.87 ATOM 2506 CE1 HIS B 31 24.361 75.416 92.354 1.00 12.78 ATOM 2507 NE2 HIS B 31 25.368 74.590 92.138 1.00 11.24 ATOM 2508 N PRO B 32 25.023 79.149 95.062 1.00 14.18 ATOM 2509 CA PRO B 32 25.322 79.289 93.634 1.00 14.30 ATOM 2510 C PRO B 32 26.672 79.973 93.325 1.00 14.04 ATOM 2511 O PRO B 32 27.429 80.305 94.237 1.00 12.70 ATOM 2512 CB PRO B 32 24.136 80.107 93.125 1.00 14.56 ATOM 2513 CG PRO B 32 23.795 80.964 94.267 1.00 15.64 ATOM 2514 CD PRO B 32 23.951 80.080 95.464 1.00 14.49 ATOM 2515 N SER B 33 26.980 80.153 92.045 1.00 14.29 ATOM 2516 CA SER B 33 28.328 80.538 91.613 1.00 14.62 ATOM 2517 C SER B 33 28.680 82.034 91.769 1.00 15.56 ATOM 2518 O SER B 33 29.851 82.395 91.761 1.00 14.85 ATOM 2519 CB SER B 33 28.549 80.140 90.139 1.00 15.61 ATOM 2520 OG SER B 33 27.505 80.635 89.335 1.00 16.17 ATOM 2521 N ASP B 34 27.682 82.900 91.845 1.00 16.02 ATOM 2522 CA ASP B 34 27.974 84.329 91.975 1.00 17.43 ATOM 2523 C ASP B 34 28.688 84.556 93.303 1.00 17.11 ATOM 2524 O ASP B 34 28.236 84.099 94.347 1.00 16.28 ATOM 2525 CB ASP B 34 26.709 85.170 91.899 1.00 17.90 ATOM 2526 CG ASP B 34 26.260 85.447 90.456 1.00 21.67 ATOM 2527 OD1 ASP B 34 26.891 84.959 89.502 1.00 24.95 ATOM 2528 OD2 ASP B 34 25.260 86.169 90.282 1.00 26.48 ATOM 2529 N ILE B 35 29.802 85.274 93.237 1.00 18.05 ATOM 2530 CA ILE B 35 30.620 85.544 94.407 1.00 18.59 ATOM 2531 C ILE B 35 31.469 86.785 94.152 1.00 19.25 ATOM 2532 O ILE B 35 31.899 87.020 93.028 1.00 19.95 ATOM 2533 CB ILE B 35 31.540 84.310 94.712 1.00 18.51 ATOM 2534 CG1 ILE B 35 32.177 84.406 96.094 1.00 18.59 ATOM 2535 CG2 ILE B 35 32.576 84.129 93.600 1.00 19.19 ATOM 2536 CD1 ILE B 35 32.554 83.036 96.694 1.00 17.50 ATOM 2537 N GLU B 36 31.708 87.566 95.207 1.00 20.53 ATOM 2538 CA GLU B 36 32.588 88.733 95.113 1.00 21.15 ATOM 2539 C GLU B 36 33.801 88.491 95.979 1.00 20.13 ATOM 2540 O GLU B 36 33.657 88.162 97.150 1.00 20.08 ATOM 2541 CB GLU B 36 31.902 90.009 95.617 1.00 21.68 ATOM 2542 CG GLU B 36 30.396 90.070 95.478 1.00 24.23 ATOM 2543 CD GLU B 36 29.810 91.368 96.014 1.00 26.20 ATOM 2544 OE1 GLU B 36 28.650 91.322 96.476 1.00 31.62 ATOM 2545 OE2 GLU B 36 30.513 92.420 95.979 1.00 31.45 ATOM 2546 N VAL B 37 34.976 88.685 95.403 1.00 20.10 ATOM 2547 CA VAL B 37 36.235 88.482 96.124 1.00 20.07 ATOM 2548 C VAL B 37 37.214 89.601 95.792 1.00 20.17 ATOM 2549 O VAL B 37 37.493 89.884 94.608 1.00 21.01 ATOM 2550 CB VAL B 37 36.900 87.128 95.796 1.00 19.67 ATOM 2551 CG1 VAL B 37 38.183 86.947 96.617 1.00 18.25 ATOM 2552 CG2 VAL B 37 35.944 85.970 96.076 1.00 18.84 ATOM 2553 N ASP B 38 37.727 90.233 96.841 1.00 20.72 ATOM 2554 CA ASP B 38 38.770 91.241 96.705 1.00 20.84 ATOM 2555 C ASP B 38 39.916 90.908 97.633 1.00 20.49 ATOM 2556 O ASP B 38 39.702 90.372 98.718 1.00 20.18 ATOM 2557 CB ASP B 38 38.254 92.609 97.113 1.00 21.28 ATOM 2558 CG ASP B 38 37.164 93.109 96.213 1.00 21.63 ATOM 2559 OD1 ASP B 38 37.412 93.274 95.007 1.00 27.30 ATOM 2560 OD2 ASP B 38 36.075 93.353 96.737 1.00 25.15 ATOM 2561 N LEU B 39 41.115 91.276 97.212 1.00 20.64 ATOM 2562 CA LEU B 39 42.298 91.216 98.068 1.00 21.30 ATOM 2563 C LEU B 39 42.529 92.632 98.596 1.00 21.93 ATOM 2564 O LEU B 39 42.394 93.608 97.853 1.00 21.35 ATOM 2565 CB LEU B 39 43.500 90.722 97.271 1.00 21.09 ATOM 2566 CG LEU B 39 43.327 89.330 96.628 1.00 20.60 ATOM 2567 CD1 LEU B 39 44.567 88.903 95.902 1.00 18.54 ATOM 2568 CD2 LEU B 39 42.936 88.287 97.655 1.00 21.12 ATOM 2569 N LEU B 40 42.841 92.716 99.887 1.00 22.32 ATOM 2570 CA LEU B 40 43.041 93.985 100.575 1.00 23.46 ATOM 2571 C LEU B 40 44.503 94.112 101.025 1.00 23.88 ATOM 2572 O LEU B 40 45.090 93.136 101.500 1.00 23.46 ATOM 2573 CB LEU B 40 42.134 94.033 101.801 1.00 23.02 ATOM 2574 CG LEU B 40 40.650 93.704 101.616 1.00 23.39 ATOM 2575 CD1 LEU B 40 39.928 93.838 102.945 1.00 24.19 ATOM 2576 CD2 LEU B 40 40.015 94.598 100.541 1.00 21.55 ATOM 2577 N LYS B 41 45.086 95.298 100.853 1.00 25.49 ATOM 2578 CA LYS B 41 46.368 95.655 101.482 1.00 26.22 ATOM 2579 C LYS B 41 46.055 96.763 102.490 1.00 26.89 ATOM 2580 O LYS B 41 45.570 97.836 102.101 1.00 27.53 ATOM 2581 CB LYS B 41 47.379 96.137 100.444 1.00 26.73 ATOM 2582 CG LYS B 41 48.751 96.548 101.009 1.00 26.74 ATOM 2583 CD LYS B 41 49.576 97.248 99.937 1.00 27.57 ATOM 2584 CE LYS B 41 50.873 97.847 100.480 1.00 30.06 ATOM 2585 NZ LYS B 41 51.754 96.806 101.050 1.00 32.82 ATOM 2586 N ASN B 42 46.278 96.478 103.774 1.00 27.15 ATOM 2587 CA ASN B 42 45.960 97.411 104.854 1.00 27.38 ATOM 2588 C ASN B 42 44.520 97.939 104.743 1.00 27.82 ATOM 2589 O ASN B 42 44.263 99.142 104.847 1.00 27.98 ATOM 2590 CB ASN B 42 46.999 98.539 104.877 1.00 27.67 ATOM 2591 CG ASN B 42 48.418 98.019 105.104 1.00 27.16 ATOM 2592 OD1 ASN B 42 48.649 97.190 105.980 1.00 27.76 ATOM 2593 ND2 ASN B 42 49.362 98.485 104.299 1.00 26.54 ATOM 2594 N GLY B 43 43.588 97.017 104.505 1.00 27.79 ATOM 2595 CA GLY B 43 42.152 97.318 104.446 1.00 27.58 ATOM 2596 C GLY B 43 41.666 97.867 103.116 1.00 27.60 ATOM 2597 O GLY B 43 40.461 98.012 102.916 1.00 28.15 ATOM 2598 N GLU B 44 42.583 98.146 102.198 1.00 27.48 ATOM 2599 CA GLU B 44 42.246 98.781 100.925 1.00 27.82 ATOM 2600 C GLU B 44 42.323 97.799 99.750 1.00 26.92 ATOM 2601 O GLU B 44 43.324 97.097 99.568 1.00 26.39 ATOM 2602 CB GLU B 44 43.181 99.958 100.667 1.00 28.21 ATOM 2603 CG GLU B 44 43.362 100.866 101.878 1.00 30.78 ATOM 2604 CD GLU B 44 43.945 102.228 101.525 1.00 31.92 ATOM 2605 OE1 GLU B 44 43.574 103.222 102.202 1.00 38.02 ATOM 2606 OE2 GLU B 44 44.779 102.306 100.584 1.00 38.88 ATOM 2607 N ARG B 45 41.272 97.788 98.934 1.00 25.91 ATOM 2608 CA ARG B 45 41.182 96.904 97.770 1.00 25.33 ATOM 2609 C ARG B 45 42.333 97.104 96.784 1.00 24.79 ATOM 2610 O ARG B 45 42.590 98.219 96.319 1.00 23.67 ATOM 2611 CB ARG B 45 39.843 97.124 97.055 1.00 24.95 ATOM 2612 CG ARG B 45 39.675 96.388 95.740 1.00 25.21 ATOM 2613 CD ARG B 45 38.313 96.691 95.158 1.00 24.17 ATOM 2614 NE ARG B 45 38.200 96.203 93.789 1.00 23.23 ATOM 2615 CZ ARG B 45 38.653 96.823 92.705 1.00 22.09 ATOM 2616 NH1 ARG B 45 39.283 97.990 92.782 1.00 22.58 ATOM 2617 NH2 ARG B 45 38.465 96.259 91.519 1.00 22.24 ATOM 2618 N ILE B 46 43.012 96.004 96.470 1.00 23.73 ATOM 2619 CA ILE B 46 44.067 95.963 95.466 1.00 23.97 ATOM 2620 C ILE B 46 43.446 95.875 94.069 1.00 23.84 ATOM 2621 O ILE B 46 42.498 95.119 93.854 1.00 23.45 ATOM 2622 CB ILE B 46 44.985 94.710 95.689 1.00 23.22 ATOM 2623 CG1 ILE B 46 45.685 94.788 97.051 1.00 24.61 ATOM 2624 CG2 ILE B 46 46.012 94.554 94.560 1.00 22.92 ATOM 2625 CD1 ILE B 46 46.119 93.453 97.629 1.00 23.44 ATOM 2626 N GLU B 47 43.995 96.630 93.124 1.00 24.36 ATOM 2627 CA GLU B 47 43.589 96.551 91.720 1.00 24.51 ATOM 2628 C GLU B 47 44.343 95.450 90.965 1.00 24.92 ATOM 2629 O GLU B 47 45.337 94.926 91.444 1.00 24.97 ATOM 2630 CB GLU B 47 43.861 97.890 91.013 1.00 25.00 ATOM 2631 CG GLU B 47 43.200 99.097 91.666 1.00 24.08 ATOM 2632 CD GLU B 47 43.306 100.351 90.795 1.00 25.11 ATOM 2633 OE1 GLU B 47 42.294 101.064 90.653 1.00 24.08 ATOM 2634 OE2 GLU B 47 44.397 100.600 90.228 1.00 25.52 ATOM 2635 N LYS B 48 43.869 95.140 89.762 1.00 24.60 ATOM 2636 CA LYS B 48 44.509 94.167 88.873 1.00 25.15 ATOM 2637 C LYS B 48 44.624 92.765 89.489 1.00 24.56 ATOM 2638 O LYS B 48 45.543 91.997 89.156 1.00 25.47 ATOM 2639 CB LYS B 48 45.871 94.687 88.399 1.00 25.79 ATOM 2640 CG LYS B 48 45.806 96.134 87.939 1.00 27.26 ATOM 2641 CD LYS B 48 47.043 96.576 87.165 1.00 27.53 ATOM 2642 CE LYS B 48 46.805 97.966 86.537 1.00 29.64 ATOM 2643 NZ LYS B 48 45.918 98.867 87.369 1.00 32.43 ATOM 2644 N VAL B 49 43.688 92.441 90.378 1.00 23.53 ATOM 2645 CA VAL B 49 43.561 91.088 90.929 1.00 22.81 ATOM 2646 C VAL B 49 42.875 90.264 89.849 1.00 22.39 ATOM 2647 O VAL B 49 41.869 90.698 89.276 1.00 21.66 ATOM 2648 CB VAL B 49 42.745 91.061 92.241 1.00 22.66 ATOM 2649 CG1 VAL B 49 42.413 89.630 92.665 1.00 21.74 ATOM 2650 CG2 VAL B 49 43.492 91.786 93.394 1.00 21.47 ATOM 2651 N GLU B 50 43.427 89.087 89.573 1.00 21.48 ATOM 2652 CA GLU B 50 42.891 88.180 88.564 1.00 21.53 ATOM 2653 C GLU B 50 42.267 86.961 89.247 1.00 20.21 ATOM 2654 O GLU B 50 42.427 86.762 90.460 1.00 19.00 ATOM 2655 CB GLU B 50 44.009 87.727 87.627 1.00 21.63 ATOM 2656 CG GLU B 50 44.746 88.883 86.920 1.00 24.23 ATOM 2657 CD GLU B 50 46.040 88.429 86.284 1.00 25.70 ATOM 2658 OE1 GLU B 50 45.992 87.769 85.216 1.00 32.90 ATOM 2659 OE2 GLU B 50 47.117 88.713 86.847 1.00 34.72 ATOM 2660 N HIS B 51 41.548 86.156 88.462 1.00 19.03 ATOM 2661 CA HIS B 51 40.989 84.913 88.973 1.00 18.67 ATOM 2662 C HIS B 51 40.937 83.847 87.887 1.00 17.56 ATOM 2663 O HIS B 51 40.926 84.152 86.697 1.00 16.84 ATOM 2664 CB HIS B 51 39.592 85.130 89.569 1.00 19.15 ATOM 2665 CG HIS B 51 38.586 85.655 88.594 1.00 21.25 ATOM 2666 ND1 HIS B 51 37.999 84.863 87.630 1.00 22.97 ATOM 2667 CD2 HIS B 51 38.070 86.899 88.424 1.00 24.09 ATOM 2668 CE1 HIS B 51 37.163 85.592 86.909 1.00 24.38 ATOM 2669 NE2 HIS B 51 37.185 86.829 87.371 1.00 24.70 ATOM 2670 N SER B 52 40.902 82.597 88.334 1.00 16.63 ATOM 2671 CA SER B 52 40.751 81.434 87.480 1.00 16.11 ATOM 2672 C SER B 52 39.351 81.350 86.865 1.00 15.23 ATOM 2673 O SER B 52 38.418 82.068 87.258 1.00 15.92 ATOM 2674 CB SER B 52 41.026 80.160 88.306 1.00 16.39 ATOM 2675 OG SER B 52 40.128 80.077 89.407 1.00 15.35 ATOM 2676 N ASP B 53 39.217 80.480 85.867 1.00 14.30 ATOM 2677 CA ASP B 53 37.937 80.246 85.231 1.00 14.07 ATOM 2678 C ASP B 53 37.038 79.377 86.116 1.00 14.21 ATOM 2679 O ASP B 53 37.498 78.406 86.751 1.00 14.15 ATOM 2680 CB ASP B 53 38.112 79.578 83.861 1.00 12.94 ATOM 2681 CG ASP B 53 39.071 80.324 82.965 1.00 12.96 ATOM 2682 OD1 ASP B 53 39.013 81.583 82.963 1.00 13.98 ATOM 2683 OD2 ASP B 53 39.895 79.640 82.298 1.00 12.24 ATOM 2684 N LEU B 54 35.750 79.722 86.135 1.00 14.70 ATOM 2685 CA LEU B 54 34.773 79.017 86.966 1.00 14.27 ATOM 2686 C LEU B 54 34.743 77.531 86.644 1.00 13.75 ATOM 2687 O LEU B 54 34.530 77.135 85.487 1.00 13.35 ATOM 2688 CB LEU B 54 33.369 79.587 86.765 1.00 14.71 ATOM 2689 CG LEU B 54 32.314 78.993 87.698 1.00 14.88 ATOM 2690 CD1 LEU B 54 32.637 79.476 89.147 1.00 13.08 ATOM 2691 CD2 LEU B 54 30.905 79.349 87.257 1.00 15.71 ATOM 2692 N SER B 55 34.963 76.713 87.674 1.00 12.38 ATOM 2693 CA SER B 55 34.791 75.271 87.568 1.00 12.79 ATOM 2694 C SER B 55 34.133 74.764 88.842 1.00 11.27 ATOM 2695 O SER B 55 33.837 75.554 89.747 1.00 10.80 ATOM 2696 CB SER B 55 36.116 74.562 87.325 1.00 13.46 ATOM 2697 OG SER B 55 35.899 73.211 86.876 1.00 18.50 ATOM 2698 N PHE B 56 33.897 73.455 88.886 1.00 11.02 ATOM 2699 CA PHE B 56 33.237 72.841 90.034 1.00 11.29 ATOM 2700 C PHE B 56 33.769 71.455 90.340 1.00 11.23 ATOM 2701 O PHE B 56 34.387 70.761 89.497 1.00 11.47 ATOM 2702 CB PHE B 56 31.703 72.850 89.906 1.00 11.31 ATOM 2703 CG PHE B 56 31.162 72.229 88.640 1.00 11.05 ATOM 2704 CD1 PHE B 56 30.861 73.003 87.520 1.00 11.53 ATOM 2705 CD2 PHE B 56 30.887 70.876 88.592 1.00 12.26 ATOM 2706 CE1 PHE B 56 30.332 72.421 86.369 1.00 11.24 ATOM 2707 CE2 PHE B 56 30.364 70.298 87.439 1.00 12.10 ATOM 2708 CZ PHE B 56 30.091 71.072 86.329 1.00 10.69 ATOM 2709 N SER B 57 33.574 71.095 91.600 1.00 12.05 ATOM 2710 CA SER B 57 34.018 69.823 92.182 1.00 13.04 ATOM 2711 C SER B 57 32.980 68.715 91.960 1.00 13.49 ATOM 2712 O SER B 57 31.864 68.971 91.453 1.00 13.26 ATOM 2713 CB SER B 57 34.256 70.035 93.692 1.00 12.90 ATOM 2714 OG SER B 57 35.187 71.094 93.917 1.00 13.00 ATOM 2715 N LYS B 58 33.326 67.478 92.357 1.00 14.24 ATOM 2716 CA LYS B 58 32.425 66.329 92.152 1.00 14.95 ATOM 2717 C LYS B 58 31.063 66.503 92.862 1.00 14.35 ATOM 2718 O LYS B 58 30.030 65.997 92.393 1.00 15.72 ATOM 2719 CB LYS B 58 33.101 65.020 92.585 1.00 15.43 ATOM 2720 CG LYS B 58 34.231 64.589 91.685 1.00 18.21 ATOM 2721 CD LYS B 58 34.960 63.328 92.173 1.00 19.38 ATOM 2722 CE LYS B 58 36.253 63.138 91.390 1.00 23.45 ATOM 2723 NZ LYS B 58 37.069 61.949 91.834 1.00 26.46 ATOM 2724 N ASP B 59 31.048 67.240 93.968 1.00 13.46 ATOM 2725 CA ASP B 59 29.801 67.526 94.688 1.00 12.99 ATOM 2726 C ASP B 59 29.001 68.715 94.145 1.00 12.35 ATOM 2727 O ASP B 59 28.082 69.192 94.799 1.00 11.69 ATOM 2728 CB ASP B 59 30.072 67.692 96.175 1.00 13.98 ATOM 2729 CG ASP B 59 30.846 68.948 96.512 1.00 14.68 ATOM 2730 OD1 ASP B 59 31.161 69.751 95.612 1.00 13.53 ATOM 2731 OD2 ASP B 59 31.141 69.132 97.720 1.00 15.69 ATOM 2732 N TRP B 60 29.379 69.181 92.957 1.00 11.68 ATOM 2733 CA TRP B 60 28.761 70.319 92.254 1.00 11.25 ATOM 2734 C TRP B 60 29.100 71.711 92.795 1.00 11.55 ATOM 2735 O TRP B 60 28.712 72.719 92.192 1.00 10.06 ATOM 2736 CB TRP B 60 27.234 70.159 92.133 1.00 10.81 ATOM 2737 CG TRP B 60 26.825 68.851 91.554 1.00 9.50 ATOM 2738 CD1 TRP B 60 26.269 67.789 92.222 1.00 10.94 ATOM 2739 CD2 TRP B 60 26.966 68.440 90.188 1.00 9.89 ATOM 2740 NE1 TRP B 60 26.049 66.759 91.347 1.00 10.77 ATOM 2741 CE2 TRP B 60 26.475 67.123 90.094 1.00 11.36 ATOM 2742 CE3 TRP B 60 27.481 69.056 89.037 1.00 7.63 ATOM 2743 CZ2 TRP B 60 26.432 66.425 88.889 1.00 10.30 ATOM 2744 CZ3 TRP B 60 27.433 68.379 87.843 1.00 10.71 ATOM 2745 CH2 TRP B 60 26.933 67.061 87.773 1.00 10.87 ATOM 2746 N SER B 61 29.828 71.806 93.905 1.00 11.59 ATOM 2747 CA SER B 61 30.164 73.125 94.430 1.00 11.44 ATOM 2748 C SER B 61 31.270 73.770 93.606 1.00 10.96 ATOM 2749 O SER B 61 32.136 73.095 93.036 1.00 10.15 ATOM 2750 CB SER B 61 30.527 73.064 95.926 1.00 12.09 ATOM 2751 OG SER B 61 31.678 72.287 96.159 1.00 13.45 ATOM 2752 N PHE B 62 31.226 75.096 93.553 1.00 10.35 ATOM 2753 CA PHE B 62 32.147 75.871 92.715 1.00 10.21 ATOM 2754 C PHE B 62 33.446 76.181 93.449 1.00 10.53 ATOM 2755 O PHE B 62 33.477 76.202 94.687 1.00 10.18 ATOM 2756 CB PHE B 62 31.457 77.152 92.264 1.00 10.09 ATOM 2757 CG PHE B 62 30.282 76.901 91.355 1.00 8.79 ATOM 2758 CD1 PHE B 62 30.479 76.569 90.039 1.00 8.44 ATOM 2759 CD2 PHE B 62 28.993 76.896 91.860 1.00 9.02 ATOM 2760 CE1 PHE B 62 29.412 76.313 89.199 1.00 9.70 ATOM 2761 CE2 PHE B 62 27.914 76.646 91.049 1.00 10.83 ATOM 2762 CZ PHE B 62 28.116 76.368 89.702 1.00 10.68 ATOM 2763 N TYR B 63 34.496 76.459 92.675 1.00 10.89 ATOM 2764 CA TYR B 63 35.751 76.954 93.225 1.00 11.34 ATOM 2765 C TYR B 63 36.437 77.922 92.253 1.00 11.75 ATOM 2766 O TYR B 63 36.269 77.812 91.017 1.00 11.25 ATOM 2767 CB TYR B 63 36.669 75.789 93.626 1.00 11.25 ATOM 2768 CG TYR B 63 37.156 74.934 92.469 1.00 12.50 ATOM 2769 CD1 TYR B 63 38.238 75.339 91.690 1.00 12.89 ATOM 2770 CD2 TYR B 63 36.541 73.730 92.146 1.00 12.59 ATOM 2771 CE1 TYR B 63 38.668 74.576 90.598 1.00 13.12 ATOM 2772 CE2 TYR B 63 36.991 72.949 91.089 1.00 12.68 ATOM 2773 CZ TYR B 63 38.061 73.379 90.312 1.00 12.60 ATOM 2774 OH TYR B 63 38.510 72.591 89.253 1.00 14.35 ATOM 2775 N LEU B 64 37.138 78.896 92.832 1.00 11.84 ATOM 2776 CA LEU B 64 37.865 79.939 92.102 1.00 12.17 ATOM 2777 C LEU B 64 39.095 80.335 92.923 1.00 12.16 ATOM 2778 O LEU B 64 39.036 80.378 94.167 1.00 11.84 ATOM 2779 CB LEU B 64 36.990 81.202 91.902 1.00 13.09 ATOM 2780 CG LEU B 64 35.768 81.195 90.987 1.00 14.61 ATOM 2781 CD1 LEU B 64 34.933 82.455 91.195 1.00 15.39 ATOM 2782 CD2 LEU B 64 36.227 81.137 89.503 1.00 14.90 ATOM 2783 N LEU B 65 40.186 80.593 92.217 1.00 12.87 ATOM 2784 CA LEU B 65 41.396 81.191 92.782 1.00 13.24 ATOM 2785 C LEU B 65 41.503 82.663 92.367 1.00 13.16 ATOM 2786 O LEU B 65 41.547 82.975 91.166 1.00 13.54 ATOM 2787 CB LEU B 65 42.637 80.438 92.291 1.00 13.67 ATOM 2788 CG LEU B 65 43.979 80.926 92.861 1.00 13.41 ATOM 2789 CD1 LEU B 65 44.035 80.774 94.367 1.00 14.14 ATOM 2790 CD2 LEU B 65 45.185 80.227 92.184 1.00 13.82 ATOM 2791 N TYR B 66 41.550 83.552 93.353 1.00 14.76 ATOM 2792 CA TYR B 66 41.880 84.965 93.130 1.00 15.45 ATOM 2793 C TYR B 66 43.339 85.190 93.523 1.00 16.60 ATOM 2794 O TYR B 66 43.781 84.661 94.554 1.00 15.99 ATOM 2795 CB TYR B 66 40.944 85.855 93.952 1.00 16.15 ATOM 2796 CG TYR B 66 39.545 85.905 93.356 1.00 15.93 ATOM 2797 CD1 TYR B 66 38.668 84.818 93.467 1.00 16.79 ATOM 2798 CD2 TYR B 66 39.120 87.019 92.644 1.00 17.60 ATOM 2799 CE1 TYR B 66 37.387 84.858 92.887 1.00 17.97 ATOM 2800 CE2 TYR B 66 37.851 87.073 92.087 1.00 18.70 ATOM 2801 CZ TYR B 66 36.996 86.003 92.209 1.00 17.93 ATOM 2802 OH TYR B 66 35.743 86.093 91.628 1.00 18.95 ATOM 2803 N TYR B 67 44.080 85.959 92.719 1.00 17.63 ATOM 2804 CA TYR B 67 45.515 86.139 92.950 1.00 18.84 ATOM 2805 C TYR B 67 46.075 87.464 92.415 1.00 20.24 ATOM 2806 O TYR B 67 45.606 88.021 91.404 1.00 19.79 ATOM 2807 CB TYR B 67 46.321 84.970 92.356 1.00 19.16 ATOM 2808 CG TYR B 67 46.109 84.814 90.870 1.00 19.41 ATOM 2809 CD1 TYR B 67 44.999 84.138 90.386 1.00 18.91 ATOM 2810 CD2 TYR B 67 46.988 85.379 89.948 1.00 21.21 ATOM 2811 CE1 TYR B 67 44.766 84.015 89.050 1.00 19.69 ATOM 2812 CE2 TYR B 67 46.760 85.249 88.589 1.00 21.69 ATOM 2813 CZ TYR B 67 45.642 84.569 88.146 1.00 21.36 ATOM 2814 OH TYR B 67 45.380 84.425 86.801 1.00 22.08 ATOM 2815 N THR B 68 47.122 87.921 93.092 1.00 21.39 ATOM 2816 CA THR B 68 47.868 89.080 92.654 1.00 22.78 ATOM 2817 C THR B 68 49.322 88.935 93.106 1.00 23.49 ATOM 2818 O THR B 68 49.587 88.373 94.150 1.00 23.18 ATOM 2819 CB THR B 68 47.235 90.369 93.205 1.00 22.94 ATOM 2820 OG1 THR B 68 47.844 91.498 92.566 1.00 25.79 ATOM 2821 CG2 THR B 68 47.381 90.483 94.731 1.00 23.50 ATOM 2822 N GLU B 69 50.248 89.425 92.292 1.00 25.71 ATOM 2823 CA GLU B 69 51.638 89.607 92.722 1.00 26.70 ATOM 2824 C GLU B 69 51.670 90.534 93.933 1.00 26.85 ATOM 2825 O GLU B 69 50.885 91.484 94.002 1.00 27.34 ATOM 2826 CB GLU B 69 52.437 90.207 91.584 1.00 26.87 ATOM 2827 CG GLU B 69 53.918 90.175 91.775 1.00 28.17 ATOM 2828 CD GLU B 69 54.636 90.345 90.453 1.00 30.77 ATOM 2829 OE1 GLU B 69 54.430 91.410 89.815 1.00 36.99 ATOM 2830 OE2 GLU B 69 55.377 89.408 90.042 1.00 35.60 ATOM 2831 N PHE B 70 52.541 90.244 94.900 1.00 27.36 ATOM 2832 CA PHE B 70 52.735 91.129 96.050 1.00 27.71 ATOM 2833 C PHE B 70 54.102 90.926 96.694 1.00 28.37 ATOM 2834 O PHE B 70 54.762 89.917 96.442 1.00 28.60 ATOM 2835 CB PHE B 70 51.605 90.976 97.087 1.00 27.02 ATOM 2836 CG PHE B 70 51.800 89.857 98.093 1.00 26.20 ATOM 2837 CD1 PHE B 70 52.148 88.570 97.695 1.00 24.64 ATOM 2838 CD2 PHE B 70 51.561 90.078 99.435 1.00 25.40 ATOM 2839 CE1 PHE B 70 52.290 87.552 98.633 1.00 25.38 ATOM 2840 CE2 PHE B 70 51.707 89.081 100.365 1.00 25.85 ATOM 2841 CZ PHE B 70 52.070 87.807 99.966 1.00 26.22 ATOM 2842 N THR B 71 54.519 91.910 97.493 1.00 29.21 ATOM 2843 CA THR B 71 55.756 91.820 98.276 1.00 29.34 ATOM 2844 C THR B 71 55.426 91.971 99.742 1.00 30.11 ATOM 2845 O THR B 71 55.149 93.086 100.219 1.00 30.06 ATOM 2846 CB THR B 71 56.785 92.882 97.869 1.00 29.40 ATOM 2847 OG1 THR B 71 57.200 92.641 96.523 1.00 30.51 ATOM 2848 CG2 THR B 71 58.010 92.826 98.774 1.00 29.90 ATOM 2849 N PRO B 72 55.450 90.849 100.476 1.00 30.96 ATOM 2850 CA PRO B 72 55.119 90.942 101.871 1.00 32.01 ATOM 2851 C PRO B 72 56.197 91.741 102.600 1.00 32.84 ATOM 2852 O PRO B 72 57.341 91.789 102.149 1.00 32.89 ATOM 2853 CB PRO B 72 55.097 89.479 102.335 1.00 31.81 ATOM 2854 CG PRO B 72 55.874 88.731 101.348 1.00 31.29 ATOM 2855 CD PRO B 72 55.796 89.472 100.069 1.00 30.81 ATOM 2856 N THR B 73 55.796 92.391 103.684 1.00 33.69 ATOM 2857 CA THR B 73 56.709 93.086 104.570 1.00 34.32 ATOM 2858 C THR B 73 56.361 92.698 106.001 1.00 35.08 ATOM 2859 O THR B 73 55.387 91.982 106.252 1.00 34.70 ATOM 2860 CB THR B 73 56.584 94.592 104.413 1.00 34.08 ATOM 2861 OG1 THR B 73 55.232 94.981 104.688 1.00 35.14 ATOM 2862 CG2 THR B 73 56.967 95.011 103.004 1.00 34.08 ATOM 2863 N GLU B 74 57.164 93.169 106.946 1.00 36.13 ATOM 2864 CA GLU B 74 56.900 92.903 108.345 1.00 36.36 ATOM 2865 C GLU B 74 55.561 93.507 108.764 1.00 36.55 ATOM 2866 O GLU B 74 54.793 92.877 109.492 1.00 37.08 ATOM 2867 CB GLU B 74 58.037 93.458 109.214 1.00 36.62 ATOM 2868 CG GLU B 74 57.749 93.421 110.711 1.00 37.25 ATOM 2869 CD GLU B 74 58.950 93.798 111.561 1.00 38.17 ATOM 2870 OE1 GLU B 74 60.096 93.721 111.062 1.00 41.15 ATOM 2871 OE2 GLU B 74 58.740 94.157 112.741 1.00 41.04 ATOM 2872 N LYS B 75 55.282 94.708 108.267 1.00 36.59 ATOM 2873 CA LYS B 75 54.199 95.548 108.783 1.00 36.43 ATOM 2874 C LYS B 75 52.862 95.428 108.041 1.00 35.94 ATOM 2875 O LYS B 75 51.802 95.463 108.673 1.00 36.40 ATOM 2876 CB LYS B 75 54.637 97.019 108.767 1.00 36.89 ATOM 2877 CG LYS B 75 54.862 97.587 107.366 1.00 37.47 ATOM 2878 CD LYS B 75 55.290 99.035 107.374 1.00 37.72 ATOM 2879 CE LYS B 75 55.271 99.600 105.951 1.00 38.68 ATOM 2880 NZ LYS B 75 55.795 98.624 104.949 1.00 38.91 ATOM 2881 N ASP B 76 52.916 95.320 106.714 1.00 35.02 ATOM 2882 CA ASP B 76 51.710 95.343 105.870 1.00 34.19 ATOM 2883 C ASP B 76 50.796 94.156 106.149 1.00 33.31 ATOM 2884 O ASP B 76 51.258 93.017 106.207 1.00 33.54 ATOM 2885 CB ASP B 76 52.087 95.342 104.390 1.00 34.25 ATOM 2886 CG ASP B 76 52.706 96.651 103.936 1.00 35.62 ATOM 2887 OD1 ASP B 76 52.203 97.725 104.337 1.00 37.30 ATOM 2888 OD2 ASP B 76 53.679 96.610 103.151 1.00 35.71 ATOM 2889 N GLU B 77 49.504 94.423 106.326 1.00 31.92 ATOM 2890 CA GLU B 77 48.539 93.359 106.551 1.00 30.84 ATOM 2891 C GLU B 77 47.788 93.092 105.248 1.00 29.04 ATOM 2892 O GLU B 77 47.360 94.029 104.570 1.00 28.41 ATOM 2893 CB GLU B 77 47.575 93.725 107.681 1.00 31.09 ATOM 2894 CG GLU B 77 48.281 93.933 109.026 1.00 32.82 ATOM 2895 CD GLU B 77 47.323 94.062 110.198 1.00 33.77 ATOM 2896 OE1 GLU B 77 46.090 93.964 109.994 1.00 38.58 ATOM 2897 OE2 GLU B 77 47.805 94.262 111.334 1.00 38.16 ATOM 2898 N TYR B 78 47.659 91.810 104.896 1.00 27.06 ATOM 2899 CA TYR B 78 46.876 91.399 103.729 1.00 25.38 ATOM 2900 C TYR B 78 45.672 90.594 104.168 1.00 23.59 ATOM 2901 O TYR B 78 45.655 89.996 105.247 1.00 22.53 ATOM 2902 CB TYR B 78 47.741 90.623 102.745 1.00 24.43 ATOM 2903 CG TYR B 78 48.744 91.526 102.076 1.00 24.86 ATOM 2904 CD1 TYR B 78 48.419 92.222 100.922 1.00 23.06 ATOM 2905 CD2 TYR B 78 50.005 91.717 102.623 1.00 23.81 ATOM 2906 CE1 TYR B 78 49.332 93.069 100.316 1.00 24.07 ATOM 2907 CE2 TYR B 78 50.924 92.559 102.029 1.00 24.21 ATOM 2908 CZ TYR B 78 50.583 93.233 100.882 1.00 24.27 ATOM 2909 OH TYR B 78 51.493 94.058 100.294 1.00 25.52 ATOM 2910 N ALA B 79 44.635 90.606 103.338 1.00 22.07 ATOM 2911 CA ALA B 79 43.414 89.888 103.669 1.00 21.44 ATOM 2912 C ALA B 79 42.597 89.662 102.411 1.00 19.73 ATOM 2913 O ALA B 79 42.890 90.238 101.358 1.00 18.81 ATOM 2914 CB ALA B 79 42.586 90.659 104.679 1.00 21.37 ATOM 2915 N CYS B 80 41.581 88.828 102.550 1.00 19.22 ATOM 2916 CA CYS B 80 40.650 88.540 101.462 1.00 19.80 ATOM 2917 C CYS B 80 39.230 88.806 101.935 1.00 19.90 ATOM 2918 O CYS B 80 38.805 88.283 102.961 1.00 20.83 ATOM 2919 CB CYS B 80 40.811 87.091 101.004 1.00 18.88 ATOM 2920 SG CYS B 80 39.727 86.625 99.624 1.00 19.04 ATOM 2921 N ARG B 81 38.516 89.641 101.177 1.00 20.61 ATOM 2922 CA ARG B 81 37.126 90.041 101.479 1.00 20.40 ATOM 2923 C ARG B 81 36.192 89.296 100.542 1.00 19.21 ATOM 2924 O ARG B 81 36.248 89.511 99.323 1.00 18.91 ATOM 2925 CB ARG B 81 36.963 91.549 101.233 1.00 20.83 ATOM 2926 CG ARG B 81 35.565 92.148 101.475 1.00 21.85 ATOM 2927 CD ARG B 81 35.450 93.495 100.707 1.00 22.98 ATOM 2928 NE ARG B 81 34.193 94.226 100.911 1.00 25.67 ATOM 2929 CZ ARG B 81 33.091 94.160 100.152 1.00 26.74 ATOM 2930 NH1 ARG B 81 33.002 93.346 99.103 1.00 27.28 ATOM 2931 NH2 ARG B 81 32.039 94.909 100.476 1.00 27.42 ATOM 2932 N VAL B 82 35.339 88.455 101.114 1.00 19.59 ATOM 2933 CA VAL B 82 34.407 87.632 100.333 1.00 19.76 ATOM 2934 C VAL B 82 32.937 87.937 100.650 1.00 19.93 ATOM 2935 O VAL B 82 32.533 87.921 101.814 1.00 20.10 ATOM 2936 CB VAL B 82 34.647 86.110 100.546 1.00 19.47 ATOM 2937 CG1 VAL B 82 33.675 85.287 99.663 1.00 19.51 ATOM 2938 CG2 VAL B 82 36.085 85.719 100.235 1.00 20.27 ATOM 2939 N ASN B 83 32.149 88.152 99.592 1.00 20.69 ATOM 2940 CA ASN B 83 30.698 88.237 99.710 1.00 20.74 ATOM 2941 C ASN B 83 29.987 87.199 98.838 1.00 20.48 ATOM 2942 O ASN B 83 30.387 86.957 97.692 1.00 20.04 ATOM 2943 CB ASN B 83 30.227 89.648 99.334 1.00 21.76 ATOM 2944 CG ASN B 83 28.907 90.026 99.975 1.00 22.18 ATOM 2945 OD1 ASN B 83 28.396 91.124 99.716 1.00 30.46 ATOM 2946 ND2 ASN B 83 28.366 89.168 100.839 1.00 22.60 ATOM 2947 N HIS B 84 28.948 86.594 99.411 1.00 20.02 ATOM 2948 CA HIS B 84 28.128 85.569 98.755 1.00 20.44 ATOM 2949 C HIS B 84 26.690 85.697 99.285 1.00 21.08 ATOM 2950 O HIS B 84 26.472 86.262 100.365 1.00 20.74 ATOM 2951 CB HIS B 84 28.718 84.190 99.087 1.00 19.48 ATOM 2952 CG HIS B 84 28.147 83.056 98.292 1.00 19.02 ATOM 2953 ND1 HIS B 84 27.319 82.106 98.842 1.00 15.99 ATOM 2954 CD2 HIS B 84 28.310 82.707 96.994 1.00 16.59 ATOM 2955 CE1 HIS B 84 26.984 81.224 97.915 1.00 14.96 ATOM 2956 NE2 HIS B 84 27.573 81.569 96.780 1.00 14.42 ATOM 2957 N VAL B 85 25.716 85.160 98.554 1.00 21.78 ATOM 2958 CA VAL B 85 24.306 85.213 98.990 1.00 22.33 ATOM 2959 C VAL B 85 24.050 84.562 100.376 1.00 22.98 ATOM 2960 O VAL B 85 23.138 84.968 101.127 1.00 23.20 ATOM 2961 CB VAL B 85 23.366 84.595 97.914 1.00 22.37 ATOM 2962 CG1 VAL B 85 23.572 83.080 97.795 1.00 22.32 ATOM 2963 CG2 VAL B 85 21.901 84.899 98.244 1.00 22.22 ATOM 2964 N THR B 86 24.861 83.568 100.726 1.00 22.73 ATOM 2965 CA THR B 86 24.779 82.914 102.028 1.00 23.57 ATOM 2966 C THR B 86 25.330 83.754 103.183 1.00 24.17 ATOM 2967 O THR B 86 25.192 83.364 104.340 1.00 24.78 ATOM 2968 CB THR B 86 25.543 81.579 102.008 1.00 23.19 ATOM 2969 OG1 THR B 86 26.897 81.821 101.594 1.00 21.09 ATOM 2970 CG2 THR B 86 24.881 80.614 101.061 1.00 23.87 ATOM 2971 N LEU B 87 25.977 84.877 102.887 1.00 25.31 ATOM 2972 CA LEU B 87 26.625 85.697 103.932 1.00 26.22 ATOM 2973 C LEU B 87 25.832 86.972 104.240 1.00 26.92 ATOM 2974 O LEU B 87 25.453 87.695 103.325 1.00 27.21 ATOM 2975 CB LEU B 87 28.055 86.056 103.507 1.00 26.30 ATOM 2976 CG LEU B 87 29.027 84.871 103.390 1.00 26.14 ATOM 2977 CD1 LEU B 87 30.375 85.346 102.900 1.00 26.41 ATOM 2978 CD2 LEU B 87 29.174 84.145 104.704 1.00 26.05 ATOM 2979 N SER B 88 25.597 87.242 105.527 1.00 28.23 ATOM 2980 CA SER B 88 24.907 88.476 105.972 1.00 28.92 ATOM 2981 C SER B 88 25.693 89.751 105.667 1.00 29.39 ATOM 2982 O SER B 88 25.119 90.777 105.283 1.00 29.49 ATOM 2983 CB SER B 88 24.650 88.427 107.483 1.00 29.36 ATOM 2984 OG SER B 88 23.978 87.233 107.855 1.00 32.20 ATOM 2985 N GLN B 89 27.002 89.687 105.887 1.00 29.64 ATOM 2986 CA GLN B 89 27.911 90.776 105.562 1.00 30.02 ATOM 2987 C GLN B 89 29.188 90.155 105.010 1.00 29.66 ATOM 2988 O GLN B 89 29.441 88.971 105.259 1.00 28.91 ATOM 2989 CB GLN B 89 28.229 91.605 106.811 1.00 30.24 ATOM 2990 CG GLN B 89 28.797 90.808 107.980 1.00 31.73 ATOM 2991 CD GLN B 89 28.966 91.647 109.251 1.00 33.07 ATOM 2992 OE1 GLN B 89 28.626 91.202 110.357 1.00 37.86 ATOM 2993 NE2 GLN B 89 29.492 92.862 109.099 1.00 36.58 ATOM 2994 N PRO B 90 29.992 90.941 104.266 1.00 29.54 ATOM 2995 CA PRO B 90 31.250 90.417 103.738 1.00 29.69 ATOM 2996 C PRO B 90 32.095 89.757 104.829 1.00 29.84 ATOM 2997 O PRO B 90 32.089 90.201 105.977 1.00 29.34 ATOM 2998 CB PRO B 90 31.944 91.661 103.183 1.00 29.70 ATOM 2999 CG PRO B 90 30.846 92.583 102.846 1.00 29.70 ATOM 3000 CD PRO B 90 29.768 92.335 103.855 1.00 29.52 ATOM 3001 N LYS B 91 32.768 88.670 104.465 1.00 29.74 ATOM 3002 CA LYS B 91 33.665 87.961 105.354 1.00 29.75 ATOM 3003 C LYS B 91 35.089 88.342 104.989 1.00 29.33 ATOM 3004 O LYS B 91 35.473 88.253 103.831 1.00 28.71 ATOM 3005 CB LYS B 91 33.471 86.459 105.187 1.00 29.87 ATOM 3006 CG LYS B 91 34.143 85.624 106.260 1.00 30.49 ATOM 3007 CD LYS B 91 33.781 84.157 106.115 1.00 30.82 ATOM 3008 CE LYS B 91 32.396 83.856 106.674 1.00 31.35 ATOM 3009 NZ LYS B 91 32.022 82.407 106.571 1.00 30.97 ATOM 3010 N ILE B 92 35.864 88.768 105.981 1.00 29.19 ATOM 3011 CA ILE B 92 37.247 89.167 105.763 1.00 28.99 ATOM 3012 C ILE B 92 38.158 88.161 106.474 1.00 28.67 ATOM 3013 O ILE B 92 38.041 87.940 107.684 1.00 28.13 ATOM 3014 CB ILE B 92 37.505 90.607 106.272 1.00 29.18 ATOM 3015 CG1 ILE B 92 36.674 91.607 105.461 1.00 29.61 ATOM 3016 CG2 ILE B 92 39.002 90.957 106.185 1.00 29.36 ATOM 3017 CD1 ILE B 92 36.491 92.961 106.133 1.00 29.31 ATOM 3018 N VAL B 93 39.030 87.511 105.703 1.00 27.72 ATOM 3019 CA VAL B 93 39.964 86.526 106.247 1.00 27.43 ATOM 3020 C VAL B 93 41.369 87.073 106.065 1.00 26.54 ATOM 3021 O VAL B 93 41.784 87.397 104.953 1.00 25.61 ATOM 3022 CB VAL B 93 39.834 85.158 105.556 1.00 27.30 ATOM 3023 CG1 VAL B 93 40.846 84.167 106.115 1.00 27.26 ATOM 3024 CG2 VAL B 93 38.432 84.630 105.735 1.00 28.02 ATOM 3025 N LYS B 94 42.084 87.206 107.175 1.00 26.67 ATOM 3026 CA LYS B 94 43.427 87.759 107.159 1.00 26.92 ATOM 3027 C LYS B 94 44.446 86.727 106.685 1.00 26.43 ATOM 3028 O LYS B 94 44.287 85.528 106.913 1.00 26.32 ATOM 3029 CB LYS B 94 43.804 88.255 108.560 1.00 27.22 ATOM 3030 CG LYS B 94 42.895 89.362 109.070 1.00 28.52 ATOM 3031 CD LYS B 94 43.174 89.732 110.536 1.00 29.17 ATOM 3032 CE LYS B 94 42.605 88.701 111.533 1.00 32.48 ATOM 3033 NZ LYS B 94 41.107 88.494 111.391 1.00 34.44 ATOM 3034 N TRP B 95 45.489 87.196 106.019 1.00 25.97 ATOM 3035 CA TRP B 95 46.608 86.335 105.673 1.00 26.72 ATOM 3036 C TRP B 95 47.429 86.031 106.924 1.00 27.38 ATOM 3037 O TRP B 95 47.862 86.953 107.616 1.00 27.22 ATOM 3038 CB TRP B 95 47.482 87.011 104.632 1.00 25.66 ATOM 3039 CG TRP B 95 48.664 86.229 104.248 1.00 25.24 ATOM 3040 CD1 TRP B 95 48.700 84.912 103.914 1.00 24.60 ATOM 3041 CD2 TRP B 95 49.997 86.718 104.107 1.00 24.20 ATOM 3042 NE1 TRP B 95 49.986 84.538 103.592 1.00 24.21 ATOM 3043 CE2 TRP B 95 50.801 85.631 103.697 1.00 24.71 ATOM 3044 CE3 TRP B 95 50.594 87.965 104.299 1.00 24.63 ATOM 3045 CZ2 TRP B 95 52.171 85.751 103.489 1.00 25.37 ATOM 3046 CZ3 TRP B 95 51.963 88.090 104.079 1.00 25.01 ATOM 3047 CH2 TRP B 95 52.733 86.990 103.674 1.00 25.00 ATOM 3048 N ASP B 96 47.605 84.745 107.214 1.00 28.35 ATOM 3049 CA ASP B 96 48.492 84.271 108.272 1.00 29.37 ATOM 3050 C ASP B 96 49.601 83.448 107.621 1.00 30.28 ATOM 3051 O ASP B 96 49.334 82.394 107.042 1.00 29.66 ATOM 3052 CB ASP B 96 47.707 83.415 109.265 1.00 29.68 ATOM 3053 CG ASP B 96 48.542 82.960 110.457 1.00 29.61 ATOM 3054 OD1 ASP B 96 49.782 82.915 110.355 1.00 31.50 ATOM 3055 OD2 ASP B 96 47.938 82.638 111.498 1.00 32.25 ATOM 3056 N ARG B 97 50.833 83.937 107.733 1.00 31.42 ATOM 3057 CA ARG B 97 52.041 83.263 107.227 1.00 32.93 ATOM 3058 C ARG B 97 52.165 81.760 107.477 1.00 33.58 ATOM 3059 O ARG B 97 52.838 81.070 106.709 1.00 33.97 ATOM 3060 CB ARG B 97 53.285 83.910 107.848 1.00 33.34 ATOM 3061 CG ARG B 97 53.862 85.043 107.042 1.00 34.77 ATOM 3062 CD ARG B 97 54.852 85.859 107.858 1.00 34.56 ATOM 3063 NE ARG B 97 54.786 87.258 107.448 1.00 36.01 ATOM 3064 CZ ARG B 97 55.623 87.873 106.614 1.00 36.40 ATOM 3065 NH1 ARG B 97 56.674 87.250 106.074 1.00 36.50 ATOM 3066 NH2 ARG B 97 55.402 89.149 106.330 1.00 36.77 ATOM 3067 N ASP B 98 51.578 81.272 108.571 1.00 34.31 ATOM 3068 CA ASP B 98 51.721 79.866 108.992 1.00 34.48 ATOM 3069 C ASP B 98 50.456 79.050 108.751 1.00 34.62 ATOM 3070 O ASP B 98 50.173 78.093 109.490 1.00 34.97 ATOM 3071 CB ASP B 98 52.075 79.812 110.479 1.00 35.00 ATOM 3072 CG ASP B 98 53.245 80.693 110.825 1.00 36.76 ATOM 3073 OD1 ASP B 98 54.198 80.780 110.009 1.00 38.86 ATOM 3074 OD2 ASP B 98 53.202 81.315 111.909 1.00 40.73 ATOM 3075 N MET B 99 49.689 79.443 107.734 1.00 34.47 ATOM 3076 CA MET B 99 48.438 78.777 107.399 1.00 34.33 ATOM 3077 C MET B 99 48.274 78.633 105.893 1.00 33.60 ATOM 3078 O MET B 99 49.044 79.164 105.096 1.00 32.33 ATOM 3079 CB MET B 99 47.247 79.554 107.970 1.00 34.77 ATOM 3080 CG MET B 99 47.221 79.634 109.488 1.00 37.18 ATOM 3081 SD MET B 99 47.096 78.011 110.255 1.00 42.73 ATOM 3082 CE MET B 99 45.331 77.725 110.063 1.00 42.38 ATOM 3083 OXT MET B 99 47.335 77.965 105.466 1.00 32.86 TER 3084 MET B 99 ATOM 3085 N LYS C 1 38.924 67.270 73.053 1.00 15.26 ATOM 3086 CA LYS C 1 37.891 67.940 72.196 1.00 15.70 ATOM 3087 C LYS C 1 36.500 67.599 72.720 1.00 14.11 ATOM 3088 O LYS C 1 36.245 66.444 73.006 1.00 13.88 ATOM 3089 CB LYS C 1 38.016 67.448 70.752 1.00 16.54 ATOM 3090 CG LYS C 1 37.055 68.152 69.758 1.00 17.90 ATOM 3091 CD LYS C 1 37.477 67.915 68.308 1.00 19.55 ATOM 3092 CE LYS C 1 36.414 68.391 67.316 1.00 22.18 ATOM 3093 NZ LYS C 1 36.755 67.975 65.903 1.00 23.95 ATOM 3094 N PRO C 2 35.596 68.595 72.848 1.00 14.25 ATOM 3095 CA PRO C 2 34.256 68.302 73.360 1.00 14.04 ATOM 3096 C PRO C 2 33.412 67.478 72.396 1.00 14.24 ATOM 3097 O PRO C 2 33.692 67.415 71.190 1.00 13.66 ATOM 3098 CB PRO C 2 33.630 69.694 73.553 1.00 14.42 ATOM 3099 CG PRO C 2 34.348 70.567 72.608 1.00 14.40 ATOM 3100 CD PRO C 2 35.756 70.031 72.565 1.00 13.66 ATOM 3101 N ILE C 3 32.407 66.825 72.950 1.00 13.82 ATOM 3102 CA ILE C 3 31.410 66.152 72.125 1.00 14.17 ATOM 3103 C ILE C 3 30.563 67.193 71.401 1.00 13.90 ATOM 3104 O ILE C 3 30.436 68.342 71.827 1.00 13.46 ATOM 3105 CB ILE C 3 30.513 65.239 73.002 1.00 13.63 ATOM 3106 CG1 ILE C 3 29.688 64.247 72.174 1.00 15.35 ATOM 3107 CG2 ILE C 3 29.627 66.081 73.949 1.00 13.37 ATOM 3108 CD1 ILE C 3 29.026 63.199 73.059 1.00 14.88 ATOM 3109 N VAL C 4 29.974 66.780 70.285 1.00 14.54 ATOM 3110 CA VAL C 4 29.038 67.654 69.585 1.00 15.95 ATOM 3111 C VAL C 4 27.866 68.017 70.469 1.00 15.70 ATOM 3112 O VAL C 4 27.567 67.327 71.451 1.00 16.02 ATOM 3113 CB VAL C 4 28.489 66.989 68.314 1.00 16.61 ATOM 3114 CG1 VAL C 4 29.581 66.904 67.268 1.00 19.26 ATOM 3115 CG2 VAL C 4 27.876 65.634 68.652 1.00 18.01 ATOM 3116 N VAL C 5 27.191 69.107 70.129 1.00 16.52 ATOM 3117 CA VAL C 5 26.024 69.528 70.886 1.00 16.10 ATOM 3118 C VAL C 5 24.980 68.399 70.916 1.00 16.58 ATOM 3119 O VAL C 5 24.583 67.864 69.877 1.00 16.43 ATOM 3120 CB VAL C 5 25.399 70.850 70.320 1.00 17.04 ATOM 3121 CG1 VAL C 5 24.103 71.217 71.063 1.00 17.05 ATOM 3122 CG2 VAL C 5 26.424 71.996 70.357 1.00 16.85 ATOM 3123 N LEU C 6 24.565 68.050 72.128 1.00 16.00 ATOM 3124 CA LEU C 6 23.563 67.017 72.406 1.00 15.99 ATOM 3125 C LEU C 6 22.213 67.671 72.650 1.00 15.83 ATOM 3126 O LEU C 6 22.125 68.879 72.914 1.00 16.45 ATOM 3127 CB LEU C 6 23.972 66.203 73.652 1.00 16.30 ATOM 3128 CG LEU C 6 25.247 65.359 73.529 1.00 16.06 ATOM 3129 CD1 LEU C 6 25.610 64.783 74.889 1.00 16.11 ATOM 3130 CD2 LEU C 6 25.097 64.244 72.489 1.00 15.63 ATOM 3131 N HIS C 7 21.159 66.869 72.571 1.00 15.55 ATOM 3132 CA HIS C 7 19.796 67.373 72.796 1.00 15.33 ATOM 3133 C HIS C 7 19.676 68.137 74.114 1.00 14.86 ATOM 3134 O HIS C 7 20.341 67.801 75.102 1.00 14.03 ATOM 3135 CB HIS C 7 18.794 66.213 72.784 1.00 16.14 ATOM 3136 CG HIS C 7 17.392 66.636 72.485 1.00 16.01 ATOM 3137 ND1 HIS C 7 16.861 66.586 71.211 1.00 19.24 ATOM 3138 CD2 HIS C 7 16.410 67.101 73.286 1.00 17.86 ATOM 3139 CE1 HIS C 7 15.616 67.018 71.246 1.00 17.48 ATOM 3140 NE2 HIS C 7 15.317 67.338 72.490 1.00 18.99 ATOM 3141 N GLY C 8 18.834 69.170 74.122 1.00 13.49 ATOM 3142 CA GLY C 8 18.526 69.905 75.343 1.00 13.73 ATOM 3143 C GLY C 8 17.749 69.119 76.382 1.00 13.21 ATOM 3144 O GLY C 8 17.332 67.975 76.150 1.00 13.39 ATOM 3145 N TYR C 9 17.570 69.720 77.548 1.00 13.18 ATOM 3146 CA TYR C 9 16.944 69.058 78.695 1.00 12.70 ATOM 3147 C TYR C 9 15.423 69.093 78.585 1.00 13.44 ATOM 3148 O TYR C 9 14.880 69.875 77.785 1.00 12.98 ATOM 3149 CB TYR C 9 17.389 69.691 80.027 1.00 12.89 ATOM 3150 CG TYR C 9 18.832 69.397 80.416 1.00 11.42 ATOM 3151 CD1 TYR C 9 19.146 68.536 81.471 1.00 12.52 ATOM 3152 CD2 TYR C 9 19.889 69.984 79.722 1.00 12.47 ATOM 3153 CE1 TYR C 9 20.475 68.252 81.782 1.00 12.31 ATOM 3154 CE2 TYR C 9 21.202 69.734 80.053 1.00 11.35 ATOM 3155 CZ TYR C 9 21.498 68.869 81.080 1.00 12.10 ATOM 3156 OH TYR C 9 22.830 68.653 81.362 1.00 11.02 ATOM 3157 OXT TYR C 9 14.747 68.356 79.316 1.00 13.24 END