REMARK File generated by pHLA3D REMARK http://www.phla3d.com.br HEADER GLYCOPROTEIN/PEPTIDE 01-JUL-05 2BVP TITLE STRUCTURES OF THREE HIV-1 HLA-B5703-PEPTIDE COMPLEXES AND TITLE 2 IDENTIFICATION OF RELATED HLAS POTENTIALLY ASSOCIATED WITH TITLE 3 LONG-TERM NON-PROGRESSION COMPND MOL_ID: 1; COMPND 2 MOLECULE: HLA CLASS I HISTOCOMPATIBILITY ANTIGEN, B-57 COMPND 3 ALPHA CHAIN; COMPND 4 CHAIN: A; COMPND 5 SYNONYM: HLA-B5703, MHC CLASS I ANTIGEN B*57, BW-57; COMPND 6 ENGINEERED: YES; COMPND 7 MOL_ID: 2; COMPND 8 MOLECULE: BETA-2-MICROGLOBULIN; COMPND 9 CHAIN: B; COMPND 10 ENGINEERED: YES; COMPND 11 MOL_ID: 3; COMPND 12 MOLECULE: HIV-P24; COMPND 13 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: 511693; SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21; SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PGM-T7; SOURCE 9 MOL_ID: 2; SOURCE 10 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 11 ORGANISM_COMMON: HUMAN; SOURCE 12 ORGANISM_TAXID: 9606; SOURCE 13 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 14 EXPRESSION_SYSTEM_TAXID: 511693; SOURCE 15 EXPRESSION_SYSTEM_STRAIN: BL21; SOURCE 16 EXPRESSION_SYSTEM_PLASMID: PGM-T7; SOURCE 17 MOL_ID: 3; SOURCE 18 SYNTHETIC: YES; SOURCE 19 ORGANISM_SCIENTIFIC: HUMAN IMMUNODEFICIENCY VIRUS; SOURCE 20 ORGANISM_TAXID: 12721 KEYWDS GLYCOPROTEIN/PEPTIDE, MHC, HLA-B57, LTNP, HIV-1, KEYWDS 2 GLYCOPROTEIN, MHC I, POLYMORPHISM, TRANSMEMBRANE, KEYWDS 3 IMMUNOGLOBULIN DOMAIN, PYRROLIDONE CARBOXYLIC ACID, KEYWDS 4 GLYCOPROTEIN/PEPTIDE COMPLEX, IMMUNE RESPONSE EXPDTA X-RAY DIFFRACTION AUTHOR G.B.STEWART-JONES,G.GILLESPIE,I.M.OVERTON,R.KAUL,P.ROCHE, AUTHOR 2 A.J.MCMICHAEL,S.ROWLAND-JONES,E.Y.JONES REVDAT 2 24-FEB-09 2BVP 1 VERSN REVDAT 1 07-SEP-05 2BVP 0 REMARK 2 REMARK 2 RESOLUTION. 1.35 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC 5.2.0005 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) : 1.35 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 65.23 REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL REMARK 3 COMPLETENESS FOR RANGE (%) : 98.0 REMARK 3 NUMBER OF REFLECTIONS : 91216 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 : 0.215 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000 REMARK 3 FREE R VALUE TEST SET COUNT : 4806 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) : 1.35 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.39 REMARK 3 REFLECTION IN BIN (WORKING SET) : 6084 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 89.09 REMARK 3 BIN R VALUE (WORKING SET) : 0.3000 REMARK 3 BIN FREE R VALUE SET COUNT : 308 REMARK 3 BIN FREE R VALUE : 0.3290 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 3128 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 0 REMARK 3 SOLVENT ATOMS : 769 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 22.59 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 0.05000 REMARK 3 B22 (A**2) : -0.31000 REMARK 3 B33 (A**2) : 0.27000 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): 0.062 REMARK 3 ESU BASED ON FREE R VALUE (A): 0.061 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.042 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.038 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.966 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.960 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3218 ; 0.010 ; 0.021 REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4373 ; 1.321 ; 1.931 REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 379 ; 5.739 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 173 ;31.666 ;23.121 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 519 ;12.692 ;15.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 31 ;15.658 ;15.000 REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 447 ; 0.080 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2538 ; 0.005 ; 0.020 REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1862 ; 0.199 ; 0.200 REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 2246 ; 0.317 ; 0.200 REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 725 ; 0.108 ; 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): 55 ; 0.146 ; 0.200 REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 74 ; 0.134 ; 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): 1939 ; 0.737 ; 1.500 REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3074 ; 1.270 ; 2.000 REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1471 ; 1.831 ; 3.000 REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1299 ; 2.823 ; 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 2BVP COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 01-JUL-05. REMARK 100 THE PDBE ID CODE IS EBI-24680. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : NULL REMARK 200 TEMPERATURE (KELVIN) : 100.0 REMARK 200 PH : NULL REMARK 200 NUMBER OF CRYSTALS USED : NULL REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : SRS REMARK 200 BEAMLINE : PX14.2 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.973 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : NULL REMARK 200 DETECTOR MANUFACTURER : NULL REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL REMARK 200 DATA SCALING SOFTWARE : NULL REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 98052 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.350 REMARK 200 RESOLUTION RANGE LOW (A) : 30.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.900 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 98.1 REMARK 200 DATA REDUNDANCY : 9.500 REMARK 200 R MERGE (I) : 0.06000 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : NULL REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL REMARK 200 COMPLETENESS FOR SHELL (%) : NULL REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : NULL REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: OTHER REMARK 200 SOFTWARE USED: NULL REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 33.88 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.87 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: NULL 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 24.95600 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 54.07700 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 40.94350 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 54.07700 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 24.95600 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 40.94350 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 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 GLU A 275 REMARK 465 PRO A 276 REMARK 465 MET B 0 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT REMARK 500 REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT. REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE REMARK 500 OD1 ASN A 66 - O HOH A 2212 2.16 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 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 66.99 -158.49 REMARK 500 ASP A 29 -124.91 49.74 REMARK 500 SER A 131 -30.80 -136.20 REMARK 500 GLN A 224 44.56 -99.29 REMARK 500 ARG A 239 -22.38 92.45 REMARK 500 TRP B 60 -1.61 77.47 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 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 PEPTIDE TYPDINQML 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 REMARK 900 (75-82) 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 REMARK 900 CORECEPTOR 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 REMARK 900 2-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 REMARK 900 GAMMA/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 VIRUS NUCLEOPROTEIN PEPTIDE REMARK 900 RELATED ID: 1CG9 RELATED DB: PDB REMARK 900 COMPLEX RECOGNITION OF THE SUPERTYPIC BW6- REMARK 900 DETERMINANT ON HLA-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 TRANSFERRIN RECEPTOR 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 REMARK 900 (HLA-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 TO PEPTIDE 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 RELATED ID: 1HHH RELATED DB: PDB REMARK 900 RELATED ID: 1HHI RELATED DB: PDB REMARK 900 RELATED ID: 1HHJ RELATED DB: PDB REMARK 900 HUMAN CLASS I HISTOCOMPATIBILITY ANTIGEN REMARK 900 (HLA-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 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 REMARK 900 HLA-B*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 PEPTIDE P1058 REMARK 900 RELATED ID: 1I7T RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF CLASS I MHC A2 IN REMARK 900 COMPLEX WITH PEPTIDE P1049-5V 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 US2 BOUND 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 CELL INHIBITORY 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 A DECAMERIC 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 REMARK 900 BETA2-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 REMARK 900 BETA-2-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-EBV PEPTIDE 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 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 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-1, REMARK 900 A HOST ANDVIRAL MHC RECEPTOR REMARK 900 RELATED ID: 1PY4 RELATED DB: PDB REMARK 900 BETA2 MICROGLOBULIN MUTANT H31Y DISPLAYS HINTS REMARK 900 FOR AMYLOID FORMATIONS REMARK 900 RELATED ID: 1Q94 RELATED DB: PDB REMARK 900 STRUCTURES OF HLA-A*1101 IN COMPLEX WITH REMARK 900 IMMUNODOMINANT NONAMER AND DECAMER HIV-1 REMARK 900 EPITOPES CLEARLY REVEAL THE PRESENCE OF A REMARK 900 MIDDLE ANCHOR RESIDUE REMARK 900 RELATED ID: 1QEW RELATED DB: PDB REMARK 900 HUMAN CLASS I HISTOCOMPATIBILITY ANTIGEN REMARK 900 (HLA-A 0201)COMPLEX WITH A NONAMERIC PEPTIDE REMARK 900 FROM MELANOMA-ASSOCIATED ANTIGEN 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-A2 REMARK 900 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 REMARK 900 PEPTIDE Y8A REMARK 900 RELATED ID: 1QVO RELATED DB: PDB REMARK 900 STRUCTURES OF HLA-A*1101 IN COMPLEX WITH REMARK 900 IMMUNODOMINANT NONAMER 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-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: 1W0V RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF HLA-B*2705 COMPLEXED REMARK 900 WITH THE SELF-PEPTIDE TIS FROM REMARK 900 EGF-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 REMARK 900 EGF-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 NUCLEOCAPSID PEPTIDE REMARK 900 RELATED ID: 1XH3 RELATED DB: PDB REMARK 900 CONFORMATIONAL RESTRAINTS AND FLEXIBILITY OF REMARK 900 14-MERICPEPTIDES IN COMPLEX WITH HLA-B*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 SYNTHETIC MYCOBACTIN 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 EBV ANTIGEN 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: 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: 2BVO 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 REMARK 900 LONG-TERM NON-PROGRESSION 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 REMARK 900 LONG-TERM NON-PROGRESSION REMARK 900 RELATED ID: 2CLR RELATED DB: PDB REMARK 900 HUMAN CLASS I HISTOCOMPATIBILITY ANTIGEN REMARK 900 (HLA-A 0201) COMPLEXED WITH A DECAMERIC PEPTIDE REMARK 900 FROM CALRETICULIN 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 ANTIGEN) REMARK 900 RELATED ID: 3HLA RELATED DB: PDB REMARK 900 HUMAN CLASS I HISTOCOMPATIBILITY ANTIGEN A2.1 REMARK 900 (HLA-A2.1 HUMAN LEUCOCYTE ANTIGEN) DBREF 2BVP A 1 276 UNP P18465 1B57_HUMAN 25 300 DBREF 2BVP B 0 0 PDB 2BVP 2BVP 0 0 DBREF 2BVP B 1 99 UNP P61769 B2MG_HUMAN 21 119 DBREF 2BVP C 1 9 PDB 2BVP 2BVP 1 9 CRYST1 49.912 81.887 108.154 90.00 90.00 90.00 P 21 21 21 4 ATOM 1 N GLY A 1 0.851 57.275 24.460 1.00 12.63 ATOM 2 CA GLY A 1 1.883 56.274 24.120 1.00 12.63 ATOM 3 C GLY A 1 3.163 56.607 24.807 1.00 12.63 ATOM 4 O GLY A 1 3.183 56.873 26.009 1.00 12.63 ATOM 5 N SER A 2 4.274 56.595 24.047 1.00 26.89 ATOM 6 CA SER A 2 5.549 56.893 24.625 1.00 26.89 ATOM 7 C SER A 2 5.663 58.370 24.786 1.00 26.89 ATOM 8 O SER A 2 4.944 59.143 24.151 1.00 26.89 ATOM 9 CB SER A 2 6.751 56.439 23.778 1.00 26.89 ATOM 10 OG SER A 2 6.757 55.027 23.642 1.00 26.89 ATOM 11 N HIS A 3 6.583 58.792 25.676 1.00 43.89 ATOM 12 CA HIS A 3 6.778 60.187 25.920 1.00 43.89 ATOM 13 C HIS A 3 8.225 60.397 26.214 1.00 43.89 ATOM 14 O HIS A 3 8.956 59.455 26.518 1.00 43.89 ATOM 15 CB HIS A 3 5.965 60.709 27.114 1.00 43.89 ATOM 16 CG HIS A 3 4.484 60.619 26.885 1.00 43.89 ATOM 17 ND1 HIS A 3 3.756 61.553 26.181 1.00 43.89 ATOM 18 CD2 HIS A 3 3.588 59.672 27.280 1.00 43.89 ATOM 19 CE1 HIS A 3 2.467 61.130 26.186 1.00 43.89 ATOM 20 NE2 HIS A 3 2.316 59.993 26.841 1.00 43.89 ATOM 21 N SER A 4 8.680 61.661 26.108 1.00 37.89 ATOM 22 CA SER A 4 10.060 61.951 26.352 1.00 37.89 ATOM 23 C SER A 4 10.150 63.260 27.060 1.00 37.89 ATOM 24 O SER A 4 9.236 64.082 27.010 1.00 37.89 ATOM 25 CB SER A 4 10.892 62.077 25.063 1.00 37.89 ATOM 26 OG SER A 4 10.397 63.141 24.263 1.00 37.89 ATOM 27 N MET A 5 11.268 63.454 27.781 1.00 67.06 ATOM 28 CA MET A 5 11.534 64.700 28.426 1.00 67.06 ATOM 29 C MET A 5 12.901 65.087 27.960 1.00 67.06 ATOM 30 O MET A 5 13.788 64.240 27.864 1.00 67.06 ATOM 31 CB MET A 5 11.534 64.583 29.962 1.00 67.06 ATOM 32 CG MET A 5 11.683 65.919 30.689 1.00 67.06 ATOM 33 SD MET A 5 11.267 65.862 32.459 1.00 67.06 ATOM 34 CE MET A 5 12.568 64.670 32.886 1.00 67.06 ATOM 35 N ARG A 6 13.098 66.372 27.609 1.00 94.09 ATOM 36 CA ARG A 6 14.393 66.767 27.139 1.00 94.09 ATOM 37 C ARG A 6 14.740 68.090 27.739 1.00 94.09 ATOM 38 O ARG A 6 13.883 68.951 27.936 1.00 94.09 ATOM 39 CB ARG A 6 14.479 66.943 25.611 1.00 94.09 ATOM 40 CG ARG A 6 14.328 65.649 24.802 1.00 94.09 ATOM 41 CD ARG A 6 15.616 64.829 24.689 1.00 94.09 ATOM 42 NE ARG A 6 15.385 63.746 23.689 1.00 94.09 ATOM 43 CZ ARG A 6 14.838 62.551 24.061 1.00 94.09 ATOM 44 NH1 ARG A 6 14.427 62.350 25.347 1.00 94.09 ATOM 45 NH2 ARG A 6 14.697 61.552 23.140 1.00 94.09 ATOM 46 N TYR A 7 16.034 68.256 28.073 1.00143.22 ATOM 47 CA TYR A 7 16.554 69.510 28.537 1.00143.22 ATOM 48 C TYR A 7 17.650 69.870 27.596 1.00143.22 ATOM 49 O TYR A 7 18.553 69.064 27.369 1.00143.22 ATOM 50 CB TYR A 7 17.173 69.452 29.945 1.00143.22 ATOM 51 CG TYR A 7 16.069 69.420 30.943 1.00143.22 ATOM 52 CD1 TYR A 7 15.517 68.236 31.375 1.00143.22 ATOM 53 CD2 TYR A 7 15.581 70.605 31.448 1.00143.22 ATOM 54 CE1 TYR A 7 14.496 68.240 32.298 1.00143.22 ATOM 55 CE2 TYR A 7 14.565 70.616 32.370 1.00143.22 ATOM 56 CZ TYR A 7 14.020 69.430 32.797 1.00143.22 ATOM 57 OH TYR A 7 12.975 69.444 33.744 1.00143.22 ATOM 58 N PHE A 8 17.586 71.086 27.009 1.00139.05 ATOM 59 CA PHE A 8 18.604 71.498 26.087 1.00139.05 ATOM 60 C PHE A 8 19.253 72.727 26.637 1.00139.05 ATOM 61 O PHE A 8 18.579 73.674 27.039 1.00139.05 ATOM 62 CB PHE A 8 18.083 71.885 24.688 1.00139.05 ATOM 63 CG PHE A 8 17.396 70.698 24.106 1.00139.05 ATOM 64 CD1 PHE A 8 18.103 69.723 23.444 1.00139.05 ATOM 65 CD2 PHE A 8 16.033 70.557 24.233 1.00139.05 ATOM 66 CE1 PHE A 8 17.460 68.628 22.914 1.00139.05 ATOM 67 CE2 PHE A 8 15.385 69.465 23.705 1.00139.05 ATOM 68 CZ PHE A 8 16.099 68.496 23.041 1.00139.05 ATOM 69 N TYR A 9 20.600 72.740 26.664 1.00150.93 ATOM 70 CA TYR A 9 21.264 73.908 27.154 1.00150.93 ATOM 71 C TYR A 9 22.143 74.398 26.063 1.00150.93 ATOM 72 O TYR A 9 22.758 73.606 25.350 1.00150.93 ATOM 73 CB TYR A 9 22.246 73.699 28.325 1.00150.93 ATOM 74 CG TYR A 9 21.571 73.083 29.500 1.00150.93 ATOM 75 CD1 TYR A 9 20.532 73.725 30.128 1.00150.93 ATOM 76 CD2 TYR A 9 21.954 71.842 29.949 1.00150.93 ATOM 77 CE1 TYR A 9 19.908 73.152 31.210 1.00150.93 ATOM 78 CE2 TYR A 9 21.335 71.264 31.033 1.00150.93 ATOM 79 CZ TYR A 9 20.313 71.925 31.669 1.00150.93 ATOM 80 OH TYR A 9 19.670 71.345 32.784 1.00150.93 ATOM 81 N THR A 10 22.195 75.729 25.879 1.00126.90 ATOM 82 CA THR A 10 23.130 76.242 24.931 1.00126.90 ATOM 83 C THR A 10 23.895 77.323 25.633 1.00126.90 ATOM 84 O THR A 10 23.316 78.205 26.269 1.00126.90 ATOM 85 CB THR A 10 22.504 76.779 23.671 1.00126.90 ATOM 86 OG1 THR A 10 23.483 76.850 22.648 1.00126.90 ATOM 87 CG2 THR A 10 21.913 78.174 23.922 1.00126.90 ATOM 88 N ALA A 11 25.238 77.243 25.582 1.00 42.77 ATOM 89 CA ALA A 11 26.050 78.258 26.187 1.00 42.77 ATOM 90 C ALA A 11 26.815 78.871 25.065 1.00 42.77 ATOM 91 O ALA A 11 27.462 78.165 24.293 1.00 42.77 ATOM 92 CB ALA A 11 27.069 77.724 27.210 1.00 42.77 ATOM 93 N MET A 12 26.761 80.212 24.950 1.00 65.95 ATOM 94 CA MET A 12 27.385 80.839 23.823 1.00 65.95 ATOM 95 C MET A 12 28.292 81.921 24.317 1.00 65.95 ATOM 96 O MET A 12 27.852 82.885 24.939 1.00 65.95 ATOM 97 CB MET A 12 26.339 81.463 22.886 1.00 65.95 ATOM 98 CG MET A 12 25.415 80.409 22.271 1.00 65.95 ATOM 99 SD MET A 12 23.827 81.042 21.657 1.00 65.95 ATOM 100 CE MET A 12 23.075 81.106 23.310 1.00 65.95 ATOM 101 N SER A 13 29.602 81.791 24.037 1.00 40.98 ATOM 102 CA SER A 13 30.537 82.786 24.471 1.00 40.98 ATOM 103 C SER A 13 30.469 83.940 23.526 1.00 40.98 ATOM 104 O SER A 13 30.099 83.783 22.365 1.00 40.98 ATOM 105 CB SER A 13 31.994 82.287 24.522 1.00 40.98 ATOM 106 OG SER A 13 32.443 81.954 23.217 1.00 40.98 ATOM 107 N ARG A 14 30.777 85.153 24.027 1.00206.76 ATOM 108 CA ARG A 14 30.816 86.326 23.205 1.00206.76 ATOM 109 C ARG A 14 31.901 87.143 23.813 1.00206.76 ATOM 110 O ARG A 14 31.667 87.876 24.772 1.00206.76 ATOM 111 CB ARG A 14 29.532 87.166 23.325 1.00206.76 ATOM 112 CG ARG A 14 28.252 86.412 22.958 1.00206.76 ATOM 113 CD ARG A 14 26.973 87.191 23.289 1.00206.76 ATOM 114 NE ARG A 14 26.873 87.293 24.774 1.00206.76 ATOM 115 CZ ARG A 14 25.661 87.519 25.365 1.00206.76 ATOM 116 NH1 ARG A 14 24.546 87.683 24.596 1.00206.76 ATOM 117 NH2 ARG A 14 25.559 87.575 26.724 1.00206.76 ATOM 118 N PRO A 15 33.082 87.070 23.290 1.00145.63 ATOM 119 CA PRO A 15 34.132 87.792 23.939 1.00145.63 ATOM 120 C PRO A 15 33.985 89.271 23.815 1.00145.63 ATOM 121 O PRO A 15 33.729 89.759 22.714 1.00145.63 ATOM 122 CB PRO A 15 35.447 87.198 23.426 1.00145.63 ATOM 123 CG PRO A 15 35.026 86.191 22.334 1.00145.63 ATOM 124 CD PRO A 15 33.573 85.843 22.692 1.00145.63 ATOM 125 N GLY A 16 34.150 89.988 24.947 1.00 30.62 ATOM 126 CA GLY A 16 34.084 91.418 25.003 1.00 30.62 ATOM 127 C GLY A 16 32.694 91.820 25.396 1.00 30.62 ATOM 128 O GLY A 16 32.481 92.882 25.978 1.00 30.62 ATOM 129 N ARG A 17 31.715 90.974 25.036 1.00114.45 ATOM 130 CA ARG A 17 30.315 91.139 25.300 1.00114.45 ATOM 131 C ARG A 17 29.966 90.791 26.716 1.00114.45 ATOM 132 O ARG A 17 28.872 91.101 27.182 1.00114.45 ATOM 133 CB ARG A 17 29.442 90.321 24.347 1.00114.45 ATOM 134 CG ARG A 17 29.479 90.895 22.931 1.00114.45 ATOM 135 CD ARG A 17 28.430 91.982 22.702 1.00114.45 ATOM 136 NE ARG A 17 27.113 91.335 22.948 1.00114.45 ATOM 137 CZ ARG A 17 26.582 90.512 21.999 1.00114.45 ATOM 138 NH1 ARG A 17 27.248 90.314 20.824 1.00114.45 ATOM 139 NH2 ARG A 17 25.397 89.877 22.233 1.00114.45 ATOM 140 N GLY A 18 30.821 90.032 27.418 1.00 41.41 ATOM 141 CA GLY A 18 30.463 89.698 28.764 1.00 41.41 ATOM 142 C GLY A 18 30.602 88.217 28.893 1.00 41.41 ATOM 143 O GLY A 18 31.336 87.581 28.138 1.00 41.41 ATOM 144 N GLU A 19 29.889 87.634 29.873 1.00 89.51 ATOM 145 CA GLU A 19 29.942 86.223 30.106 1.00 89.51 ATOM 146 C GLU A 19 29.145 85.556 29.035 1.00 89.51 ATOM 147 O GLU A 19 28.299 86.172 28.392 1.00 89.51 ATOM 148 CB GLU A 19 29.301 85.799 31.440 1.00 89.51 ATOM 149 CG GLU A 19 30.008 86.372 32.665 1.00 89.51 ATOM 150 CD GLU A 19 31.420 85.816 32.659 1.00 89.51 ATOM 151 OE1 GLU A 19 31.558 84.564 32.654 1.00 89.51 ATOM 152 OE2 GLU A 19 32.379 86.633 32.647 1.00 89.51 ATOM 153 N PRO A 20 29.405 84.293 28.830 1.00 68.18 ATOM 154 CA PRO A 20 28.696 83.564 27.821 1.00 68.18 ATOM 155 C PRO A 20 27.257 83.461 28.199 1.00 68.18 ATOM 156 O PRO A 20 26.955 83.271 29.376 1.00 68.18 ATOM 157 CB PRO A 20 29.410 82.220 27.702 1.00 68.18 ATOM 158 CG PRO A 20 30.855 82.541 28.128 1.00 68.18 ATOM 159 CD PRO A 20 30.714 83.725 29.101 1.00 68.18 ATOM 160 N ARG A 21 26.360 83.587 27.206 1.00 80.92 ATOM 161 CA ARG A 21 24.951 83.507 27.433 1.00 80.92 ATOM 162 C ARG A 21 24.619 82.068 27.654 1.00 80.92 ATOM 163 O ARG A 21 25.125 81.188 26.961 1.00 80.92 ATOM 164 CB ARG A 21 24.165 84.002 26.208 1.00 80.92 ATOM 165 CG ARG A 21 22.656 84.146 26.384 1.00 80.92 ATOM 166 CD ARG A 21 22.011 84.660 25.094 1.00 80.92 ATOM 167 NE ARG A 21 20.544 84.792 25.306 1.00 80.92 ATOM 168 CZ ARG A 21 19.819 85.553 24.435 1.00 80.92 ATOM 169 NH1 ARG A 21 20.447 86.178 23.395 1.00 80.92 ATOM 170 NH2 ARG A 21 18.473 85.703 24.609 1.00 80.92 ATOM 171 N PHE A 22 23.760 81.794 28.653 1.00 64.14 ATOM 172 CA PHE A 22 23.377 80.443 28.946 1.00 64.14 ATOM 173 C PHE A 22 21.885 80.387 28.815 1.00 64.14 ATOM 174 O PHE A 22 21.168 81.113 29.502 1.00 64.14 ATOM 175 CB PHE A 22 23.747 80.078 30.396 1.00 64.14 ATOM 176 CG PHE A 22 23.380 78.667 30.692 1.00 64.14 ATOM 177 CD1 PHE A 22 24.231 77.650 30.335 1.00 64.14 ATOM 178 CD2 PHE A 22 22.204 78.360 31.336 1.00 64.14 ATOM 179 CE1 PHE A 22 23.907 76.343 30.612 1.00 64.14 ATOM 180 CE2 PHE A 22 21.874 77.055 31.615 1.00 64.14 ATOM 181 CZ PHE A 22 22.727 76.041 31.250 1.00 64.14 ATOM 182 N ILE A 23 21.377 79.526 27.912 1.00 42.65 ATOM 183 CA ILE A 23 19.957 79.426 27.732 1.00 42.65 ATOM 184 C ILE A 23 19.587 77.992 27.873 1.00 42.65 ATOM 185 O ILE A 23 20.191 77.119 27.251 1.00 42.65 ATOM 186 CB ILE A 23 19.509 79.832 26.365 1.00 42.65 ATOM 187 CG1 ILE A 23 19.889 81.294 26.102 1.00 42.65 ATOM 188 CG2 ILE A 23 18.001 79.550 26.253 1.00 42.65 ATOM 189 CD1 ILE A 23 19.766 81.693 24.634 1.00 42.65 ATOM 190 N ALA A 24 18.568 77.708 28.699 1.00 33.53 ATOM 191 CA ALA A 24 18.168 76.344 28.854 1.00 33.53 ATOM 192 C ALA A 24 16.698 76.276 28.623 1.00 33.53 ATOM 193 O ALA A 24 15.959 77.199 28.962 1.00 33.53 ATOM 194 CB ALA A 24 18.426 75.793 30.264 1.00 33.53 ATOM 195 N VAL A 25 16.240 75.179 27.995 1.00 38.46 ATOM 196 CA VAL A 25 14.834 74.999 27.802 1.00 38.46 ATOM 197 C VAL A 25 14.537 73.565 28.071 1.00 38.46 ATOM 198 O VAL A 25 15.379 72.693 27.861 1.00 38.46 ATOM 199 CB VAL A 25 14.343 75.344 26.425 1.00 38.46 ATOM 200 CG1 VAL A 25 14.513 76.860 26.222 1.00 38.46 ATOM 201 CG2 VAL A 25 15.096 74.492 25.389 1.00 38.46 ATOM 202 N GLY A 26 13.318 73.292 28.572 1.00 24.20 ATOM 203 CA GLY A 26 12.948 71.940 28.862 1.00 24.20 ATOM 204 C GLY A 26 11.703 71.647 28.093 1.00 24.20 ATOM 205 O GLY A 26 10.826 72.501 27.963 1.00 24.20 ATOM 206 N TYR A 27 11.607 70.410 27.563 1.00 84.63 ATOM 207 CA TYR A 27 10.478 70.003 26.779 1.00 84.63 ATOM 208 C TYR A 27 9.974 68.685 27.269 1.00 84.63 ATOM 209 O TYR A 27 10.739 67.814 27.683 1.00 84.63 ATOM 210 CB TYR A 27 10.793 69.712 25.297 1.00 84.63 ATOM 211 CG TYR A 27 11.076 70.935 24.491 1.00 84.63 ATOM 212 CD1 TYR A 27 12.325 71.512 24.472 1.00 84.63 ATOM 213 CD2 TYR A 27 10.079 71.489 23.718 1.00 84.63 ATOM 214 CE1 TYR A 27 12.567 72.630 23.705 1.00 84.63 ATOM 215 CE2 TYR A 27 10.313 72.606 22.953 1.00 84.63 ATOM 216 CZ TYR A 27 11.562 73.178 22.946 1.00 84.63 ATOM 217 OH TYR A 27 11.811 74.324 22.159 1.00 84.63 ATOM 218 N VAL A 28 8.639 68.533 27.259 1.00 76.50 ATOM 219 CA VAL A 28 8.058 67.241 27.433 1.00 76.50 ATOM 220 C VAL A 28 7.437 67.024 26.104 1.00 76.50 ATOM 221 O VAL A 28 6.560 67.786 25.700 1.00 76.50 ATOM 222 CB VAL A 28 6.970 67.188 28.461 1.00 76.50 ATOM 223 CG1 VAL A 28 6.319 65.796 28.407 1.00 76.50 ATOM 224 CG2 VAL A 28 7.583 67.530 29.829 1.00 76.50 ATOM 225 N ASP A 29 7.883 65.981 25.384 1.00132.02 ATOM 226 CA ASP A 29 7.379 65.810 24.059 1.00132.02 ATOM 227 C ASP A 29 7.680 67.083 23.318 1.00132.02 ATOM 228 O ASP A 29 8.783 67.617 23.381 1.00132.02 ATOM 229 CB ASP A 29 5.853 65.590 24.036 1.00132.02 ATOM 230 CG ASP A 29 5.533 64.305 24.791 1.00132.02 ATOM 231 OD1 ASP A 29 6.457 63.466 24.967 1.00132.02 ATOM 232 OD2 ASP A 29 4.353 64.148 25.208 1.00132.02 ATOM 233 N ASP A 30 6.683 67.567 22.562 1.00129.35 ATOM 234 CA ASP A 30 6.716 68.739 21.732 1.00129.35 ATOM 235 C ASP A 30 6.503 70.027 22.484 1.00129.35 ATOM 236 O ASP A 30 6.558 71.092 21.866 1.00129.35 ATOM 237 CB ASP A 30 5.663 68.687 20.615 1.00129.35 ATOM 238 CG ASP A 30 5.906 67.412 19.815 1.00129.35 ATOM 239 OD1 ASP A 30 5.841 66.312 20.424 1.00129.35 ATOM 240 OD2 ASP A 30 6.167 67.517 18.589 1.00129.35 ATOM 241 N THR A 31 6.125 69.974 23.782 1.00147.44 ATOM 242 CA THR A 31 5.813 71.187 24.497 1.00147.44 ATOM 243 C THR A 31 6.936 71.622 25.382 1.00147.44 ATOM 244 O THR A 31 7.440 70.855 26.201 1.00147.44 ATOM 245 CB THR A 31 4.618 71.075 25.400 1.00147.44 ATOM 246 OG1 THR A 31 4.759 69.945 26.246 1.00147.44 ATOM 247 CG2 THR A 31 3.333 70.983 24.578 1.00147.44 ATOM 248 N GLN A 32 7.341 72.904 25.243 1.00 96.24 ATOM 249 CA GLN A 32 8.378 73.419 26.087 1.00 96.24 ATOM 250 C GLN A 32 7.727 73.908 27.343 1.00 96.24 ATOM 251 O GLN A 32 6.753 74.657 27.286 1.00 96.24 ATOM 252 CB GLN A 32 9.171 74.598 25.497 1.00 96.24 ATOM 253 CG GLN A 32 10.312 75.039 26.415 1.00 96.24 ATOM 254 CD GLN A 32 10.955 76.289 25.836 1.00 96.24 ATOM 255 OE1 GLN A 32 11.172 77.273 26.541 1.00 96.24 ATOM 256 NE2 GLN A 32 11.279 76.254 24.516 1.00 96.24 ATOM 257 N PHE A 33 8.154 73.355 28.499 1.00135.38 ATOM 258 CA PHE A 33 7.693 73.736 29.803 1.00135.38 ATOM 259 C PHE A 33 8.491 74.777 30.546 1.00135.38 ATOM 260 O PHE A 33 7.929 75.473 31.387 1.00135.38 ATOM 261 CB PHE A 33 7.370 72.536 30.717 1.00135.38 ATOM 262 CG PHE A 33 8.561 71.690 30.998 1.00135.38 ATOM 263 CD1 PHE A 33 9.091 70.859 30.036 1.00135.38 ATOM 264 CD2 PHE A 33 9.116 71.696 32.255 1.00135.38 ATOM 265 CE1 PHE A 33 10.181 70.071 30.326 1.00135.38 ATOM 266 CE2 PHE A 33 10.205 70.910 32.549 1.00135.38 ATOM 267 CZ PHE A 33 10.741 70.097 31.581 1.00135.38 ATOM 268 N VAL A 34 9.823 74.878 30.338 1.00 59.98 ATOM 269 CA VAL A 34 10.574 75.809 31.146 1.00 59.98 ATOM 270 C VAL A 34 11.655 76.437 30.329 1.00 59.98 ATOM 271 O VAL A 34 12.028 75.940 29.268 1.00 59.98 ATOM 272 CB VAL A 34 11.231 75.160 32.331 1.00 59.98 ATOM 273 CG1 VAL A 34 10.132 74.613 33.259 1.00 59.98 ATOM 274 CG2 VAL A 34 12.206 74.083 31.825 1.00 59.98 ATOM 275 N ARG A 35 12.167 77.587 30.816 1.00189.91 ATOM 276 CA ARG A 35 13.217 78.279 30.131 1.00189.91 ATOM 277 C ARG A 35 14.045 79.007 31.140 1.00189.91 ATOM 278 O ARG A 35 13.573 79.359 32.220 1.00189.91 ATOM 279 CB ARG A 35 12.673 79.313 29.133 1.00189.91 ATOM 280 CG ARG A 35 13.748 80.115 28.408 1.00189.91 ATOM 281 CD ARG A 35 13.179 81.084 27.373 1.00189.91 ATOM 282 NE ARG A 35 12.190 81.960 28.062 1.00189.91 ATOM 283 CZ ARG A 35 11.475 82.857 27.322 1.00189.91 ATOM 284 NH1 ARG A 35 11.728 82.991 25.988 1.00189.91 ATOM 285 NH2 ARG A 35 10.511 83.622 27.912 1.00189.91 ATOM 286 N PHE A 36 15.333 79.207 30.806 1.00 66.06 ATOM 287 CA PHE A 36 16.245 79.949 31.627 1.00 66.06 ATOM 288 C PHE A 36 17.106 80.731 30.682 1.00 66.06 ATOM 289 O PHE A 36 17.610 80.182 29.704 1.00 66.06 ATOM 290 CB PHE A 36 17.180 79.027 32.430 1.00 66.06 ATOM 291 CG PHE A 36 18.121 79.853 33.236 1.00 66.06 ATOM 292 CD1 PHE A 36 17.770 80.297 34.488 1.00 66.06 ATOM 293 CD2 PHE A 36 19.360 80.176 32.729 1.00 66.06 ATOM 294 CE1 PHE A 36 18.645 81.057 35.227 1.00 66.06 ATOM 295 CE2 PHE A 36 20.239 80.933 33.463 1.00 66.06 ATOM 296 CZ PHE A 36 19.880 81.375 34.714 1.00 66.06 ATOM 297 N ASP A 37 17.282 82.042 30.940 1.00 52.45 ATOM 298 CA ASP A 37 18.125 82.845 30.098 1.00 52.45 ATOM 299 C ASP A 37 18.972 83.698 30.996 1.00 52.45 ATOM 300 O ASP A 37 18.465 84.487 31.793 1.00 52.45 ATOM 301 CB ASP A 37 17.345 83.776 29.155 1.00 52.45 ATOM 302 CG ASP A 37 18.327 84.377 28.159 1.00 52.45 ATOM 303 OD1 ASP A 37 19.552 84.125 28.310 1.00 52.45 ATOM 304 OD2 ASP A 37 17.865 85.098 27.235 1.00 52.45 ATOM 305 N SER A 38 20.302 83.557 30.878 1.00 95.53 ATOM 306 CA SER A 38 21.226 84.278 31.711 1.00 95.53 ATOM 307 C SER A 38 21.148 85.747 31.413 1.00 95.53 ATOM 308 O SER A 38 21.494 86.573 32.256 1.00 95.53 ATOM 309 CB SER A 38 22.685 83.890 31.435 1.00 95.53 ATOM 310 OG SER A 38 22.863 82.496 31.618 1.00 95.53 ATOM 311 N ASP A 39 20.747 86.108 30.183 1.00 67.90 ATOM 312 CA ASP A 39 20.666 87.481 29.758 1.00 67.90 ATOM 313 C ASP A 39 19.537 88.223 30.411 1.00 67.90 ATOM 314 O ASP A 39 19.613 89.441 30.557 1.00 67.90 ATOM 315 CB ASP A 39 20.567 87.649 28.229 1.00 67.90 ATOM 316 CG ASP A 39 21.973 87.509 27.640 1.00 67.90 ATOM 317 OD1 ASP A 39 22.944 87.378 28.434 1.00 67.90 ATOM 318 OD2 ASP A 39 22.097 87.549 26.386 1.00 67.90 ATOM 319 N ALA A 40 18.460 87.524 30.820 1.00 35.48 ATOM 320 CA ALA A 40 17.308 88.189 31.372 1.00 35.48 ATOM 321 C ALA A 40 17.728 89.073 32.507 1.00 35.48 ATOM 322 O ALA A 40 18.748 88.843 33.154 1.00 35.48 ATOM 323 CB ALA A 40 16.240 87.218 31.893 1.00 35.48 ATOM 324 N ALA A 41 16.937 90.137 32.766 1.00 28.75 ATOM 325 CA ALA A 41 17.300 91.080 33.783 1.00 28.75 ATOM 326 C ALA A 41 17.414 90.326 35.063 1.00 28.75 ATOM 327 O ALA A 41 18.375 90.507 35.812 1.00 28.75 ATOM 328 CB ALA A 41 16.244 92.178 33.985 1.00 28.75 ATOM 329 N SER A 42 16.433 89.453 35.353 1.00 50.57 ATOM 330 CA SER A 42 16.559 88.640 36.524 1.00 50.57 ATOM 331 C SER A 42 16.422 87.234 36.038 1.00 50.57 ATOM 332 O SER A 42 15.324 86.769 35.734 1.00 50.57 ATOM 333 CB SER A 42 15.458 88.907 37.561 1.00 50.57 ATOM 334 OG SER A 42 15.537 90.255 38.000 1.00 50.57 ATOM 335 N PRO A 43 17.520 86.536 35.965 1.00 74.61 ATOM 336 CA PRO A 43 17.462 85.203 35.435 1.00 74.61 ATOM 337 C PRO A 43 16.762 84.256 36.351 1.00 74.61 ATOM 338 O PRO A 43 17.077 84.240 37.539 1.00 74.61 ATOM 339 CB PRO A 43 18.909 84.812 35.141 1.00 74.61 ATOM 340 CG PRO A 43 19.599 86.159 34.857 1.00 74.61 ATOM 341 CD PRO A 43 18.792 87.182 35.677 1.00 74.61 ATOM 342 N ARG A 44 15.834 83.441 35.816 1.00182.35 ATOM 343 CA ARG A 44 15.143 82.481 36.625 1.00182.35 ATOM 344 C ARG A 44 14.686 81.390 35.724 1.00182.35 ATOM 345 O ARG A 44 14.501 81.597 34.526 1.00182.35 ATOM 346 CB ARG A 44 13.833 83.012 37.232 1.00182.35 ATOM 347 CG ARG A 44 13.994 84.005 38.376 1.00182.35 ATOM 348 CD ARG A 44 12.702 84.752 38.717 1.00182.35 ATOM 349 NE ARG A 44 12.904 85.443 40.024 1.00182.35 ATOM 350 CZ ARG A 44 12.738 86.795 40.137 1.00182.35 ATOM 351 NH1 ARG A 44 12.513 87.559 39.030 1.00182.35 ATOM 352 NH2 ARG A 44 12.806 87.386 41.367 1.00182.35 ATOM 353 N MET A 45 14.515 80.177 36.279 1.00 84.45 ATOM 354 CA MET A 45 13.864 79.194 35.476 1.00 84.45 ATOM 355 C MET A 45 12.453 79.681 35.476 1.00 84.45 ATOM 356 O MET A 45 11.898 79.969 36.535 1.00 84.45 ATOM 357 CB MET A 45 13.869 77.778 36.077 1.00 84.45 ATOM 358 CG MET A 45 13.162 76.745 35.196 1.00 84.45 ATOM 359 SD MET A 45 14.061 76.285 33.687 1.00 84.45 ATOM 360 CE MET A 45 15.234 75.201 34.553 1.00 84.45 ATOM 361 N ALA A 46 11.839 79.800 34.283 1.00 51.04 ATOM 362 CA ALA A 46 10.517 80.353 34.207 1.00 51.04 ATOM 363 C ALA A 46 9.637 79.386 33.474 1.00 51.04 ATOM 364 O ALA A 46 10.092 78.631 32.617 1.00 51.04 ATOM 365 CB ALA A 46 10.476 81.686 33.443 1.00 51.04 ATOM 366 N PRO A 47 8.376 79.373 33.837 1.00103.40 ATOM 367 CA PRO A 47 7.397 78.495 33.253 1.00103.40 ATOM 368 C PRO A 47 7.024 78.869 31.852 1.00103.40 ATOM 369 O PRO A 47 6.737 80.035 31.590 1.00103.40 ATOM 370 CB PRO A 47 6.200 78.511 34.206 1.00103.40 ATOM 371 CG PRO A 47 6.382 79.807 35.017 1.00103.40 ATOM 372 CD PRO A 47 7.907 80.002 35.057 1.00103.40 ATOM 373 N ARG A 48 7.153 77.915 30.917 1.00160.76 ATOM 374 CA ARG A 48 6.707 77.996 29.559 1.00160.76 ATOM 375 C ARG A 48 5.336 77.414 29.340 1.00160.76 ATOM 376 O ARG A 48 4.708 77.713 28.327 1.00160.76 ATOM 377 CB ARG A 48 7.721 77.410 28.567 1.00160.76 ATOM 378 CG ARG A 48 9.002 78.254 28.521 1.00160.76 ATOM 379 CD ARG A 48 8.759 79.748 28.271 1.00160.76 ATOM 380 NE ARG A 48 8.186 79.903 26.904 1.00160.76 ATOM 381 CZ ARG A 48 9.013 80.098 25.838 1.00160.76 ATOM 382 NH1 ARG A 48 10.363 80.154 26.031 1.00160.76 ATOM 383 NH2 ARG A 48 8.493 80.232 24.583 1.00160.76 ATOM 384 N ALA A 49 4.870 76.491 30.214 1.00 47.40 ATOM 385 CA ALA A 49 3.590 75.862 29.992 1.00 47.40 ATOM 386 C ALA A 49 2.799 75.944 31.263 1.00 47.40 ATOM 387 O ALA A 49 3.348 75.944 32.363 1.00 47.40 ATOM 388 CB ALA A 49 3.698 74.377 29.614 1.00 47.40 ATOM 389 N PRO A 50 1.502 76.021 31.123 1.00 74.72 ATOM 390 CA PRO A 50 0.602 76.187 32.233 1.00 74.72 ATOM 391 C PRO A 50 0.713 75.134 33.300 1.00 74.72 ATOM 392 O PRO A 50 0.598 75.475 34.477 1.00 74.72 ATOM 393 CB PRO A 50 -0.794 76.181 31.616 1.00 74.72 ATOM 394 CG PRO A 50 -0.625 75.280 30.378 1.00 74.72 ATOM 395 CD PRO A 50 0.827 75.527 29.934 1.00 74.72 ATOM 396 N TRP A 51 0.929 73.862 32.923 1.00102.84 ATOM 397 CA TRP A 51 0.931 72.759 33.848 1.00102.84 ATOM 398 C TRP A 51 2.065 72.812 34.827 1.00102.84 ATOM 399 O TRP A 51 1.938 72.291 35.934 1.00102.84 ATOM 400 CB TRP A 51 0.887 71.380 33.157 1.00102.84 ATOM 401 CG TRP A 51 1.783 71.203 31.950 1.00102.84 ATOM 402 CD1 TRP A 51 1.452 71.366 30.636 1.00102.84 ATOM 403 CD2 TRP A 51 3.162 70.796 31.972 1.00102.84 ATOM 404 NE1 TRP A 51 2.532 71.080 29.837 1.00102.84 ATOM 405 CE2 TRP A 51 3.591 70.729 30.645 1.00102.84 ATOM 406 CE3 TRP A 51 4.000 70.498 33.007 1.00102.84 ATOM 407 CZ2 TRP A 51 4.869 70.360 30.334 1.00102.84 ATOM 408 CZ3 TRP A 51 5.291 70.133 32.688 1.00102.84 ATOM 409 CH2 TRP A 51 5.717 70.065 31.377 1.00102.84 ATOM 410 N ILE A 52 3.221 73.360 34.415 1.00117.02 ATOM 411 CA ILE A 52 4.389 73.504 35.241 1.00117.02 ATOM 412 C ILE A 52 4.181 74.542 36.307 1.00117.02 ATOM 413 O ILE A 52 4.789 74.474 37.373 1.00117.02 ATOM 414 CB ILE A 52 5.646 73.844 34.482 1.00117.02 ATOM 415 CG1 ILE A 52 6.884 73.601 35.367 1.00117.02 ATOM 416 CG2 ILE A 52 5.528 75.290 33.971 1.00117.02 ATOM 417 CD1 ILE A 52 7.126 72.129 35.707 1.00117.02 ATOM 418 N GLU A 53 3.329 75.546 36.037 1.00 99.09 ATOM 419 CA GLU A 53 3.182 76.693 36.891 1.00 99.09 ATOM 420 C GLU A 53 2.835 76.295 38.295 1.00 99.09 ATOM 421 O GLU A 53 3.276 76.936 39.245 1.00 99.09 ATOM 422 CB GLU A 53 2.095 77.660 36.403 1.00 99.09 ATOM 423 CG GLU A 53 2.079 78.979 37.173 1.00 99.09 ATOM 424 CD GLU A 53 0.965 79.838 36.594 1.00 99.09 ATOM 425 OE1 GLU A 53 0.944 80.013 35.347 1.00 99.09 ATOM 426 OE2 GLU A 53 0.118 80.328 37.389 1.00 99.09 ATOM 427 N GLN A 54 2.053 75.220 38.474 1.00 72.05 ATOM 428 CA GLN A 54 1.615 74.829 39.782 1.00 72.05 ATOM 429 C GLN A 54 2.778 74.486 40.674 1.00 72.05 ATOM 430 O GLN A 54 2.647 74.599 41.891 1.00 72.05 ATOM 431 CB GLN A 54 0.582 73.690 39.766 1.00 72.05 ATOM 432 CG GLN A 54 1.074 72.386 39.151 1.00 72.05 ATOM 433 CD GLN A 54 -0.124 71.449 39.125 1.00 72.05 ATOM 434 OE1 GLN A 54 -1.201 71.813 38.656 1.00 72.05 ATOM 435 NE2 GLN A 54 0.059 70.213 39.655 1.00 72.05 ATOM 436 N GLU A 55 3.930 74.046 40.117 1.00105.83 ATOM 437 CA GLU A 55 5.069 73.692 40.934 1.00105.83 ATOM 438 C GLU A 55 5.373 74.834 41.862 1.00105.83 ATOM 439 O GLU A 55 5.267 76.004 41.496 1.00105.83 ATOM 440 CB GLU A 55 6.352 73.378 40.133 1.00105.83 ATOM 441 CG GLU A 55 6.234 72.165 39.202 1.00105.83 ATOM 442 CD GLU A 55 6.195 70.886 40.031 1.00105.83 ATOM 443 OE1 GLU A 55 6.373 70.964 41.275 1.00105.83 ATOM 444 OE2 GLU A 55 5.986 69.805 39.418 1.00105.83 ATOM 445 N GLY A 56 5.769 74.500 43.110 1.00 27.02 ATOM 446 CA GLY A 56 5.952 75.468 44.157 1.00 27.02 ATOM 447 C GLY A 56 7.248 76.195 43.997 1.00 27.02 ATOM 448 O GLY A 56 8.036 75.950 43.085 1.00 27.02 ATOM 449 N PRO A 57 7.451 77.108 44.909 1.00 54.99 ATOM 450 CA PRO A 57 8.627 77.927 44.892 1.00 54.99 ATOM 451 C PRO A 57 9.876 77.135 45.069 1.00 54.99 ATOM 452 O PRO A 57 10.918 77.560 44.571 1.00 54.99 ATOM 453 CB PRO A 57 8.406 78.990 45.965 1.00 54.99 ATOM 454 CG PRO A 57 6.875 79.147 46.002 1.00 54.99 ATOM 455 CD PRO A 57 6.338 77.770 45.573 1.00 54.99 ATOM 456 N GLU A 58 9.806 75.991 45.770 1.00105.66 ATOM 457 CA GLU A 58 10.992 75.220 45.995 1.00105.66 ATOM 458 C GLU A 58 11.479 74.785 44.660 1.00105.66 ATOM 459 O GLU A 58 12.675 74.818 44.373 1.00105.66 ATOM 460 CB GLU A 58 10.714 73.939 46.794 1.00105.66 ATOM 461 CG GLU A 58 10.120 74.214 48.174 1.00105.66 ATOM 462 CD GLU A 58 8.648 74.554 47.984 1.00105.66 ATOM 463 OE1 GLU A 58 7.953 73.768 47.288 1.00105.66 ATOM 464 OE2 GLU A 58 8.199 75.597 48.530 1.00105.66 ATOM 465 N TYR A 59 10.533 74.375 43.800 1.00 59.69 ATOM 466 CA TYR A 59 10.850 73.880 42.498 1.00 59.69 ATOM 467 C TYR A 59 11.496 74.965 41.691 1.00 59.69 ATOM 468 O TYR A 59 12.552 74.757 41.095 1.00 59.69 ATOM 469 CB TYR A 59 9.572 73.422 41.769 1.00 59.69 ATOM 470 CG TYR A 59 9.896 72.956 40.392 1.00 59.69 ATOM 471 CD1 TYR A 59 9.960 73.856 39.355 1.00 59.69 ATOM 472 CD2 TYR A 59 10.123 71.623 40.134 1.00 59.69 ATOM 473 CE1 TYR A 59 10.250 73.437 38.078 1.00 59.69 ATOM 474 CE2 TYR A 59 10.413 71.197 38.859 1.00 59.69 ATOM 475 CZ TYR A 59 10.478 72.105 37.829 1.00 59.69 ATOM 476 OH TYR A 59 10.775 71.671 36.520 1.00 59.69 ATOM 477 N TRP A 60 10.896 76.169 41.671 1.00 62.25 ATOM 478 CA TRP A 60 11.422 77.208 40.837 1.00 62.25 ATOM 479 C TRP A 60 12.765 77.643 41.322 1.00 62.25 ATOM 480 O TRP A 60 13.693 77.803 40.532 1.00 62.25 ATOM 481 CB TRP A 60 10.514 78.443 40.766 1.00 62.25 ATOM 482 CG TRP A 60 9.168 78.119 40.170 1.00 62.25 ATOM 483 CD1 TRP A 60 7.928 78.270 40.712 1.00 62.25 ATOM 484 CD2 TRP A 60 8.983 77.500 38.888 1.00 62.25 ATOM 485 NE1 TRP A 60 6.975 77.804 39.839 1.00 62.25 ATOM 486 CE2 TRP A 60 7.610 77.320 38.715 1.00 62.25 ATOM 487 CE3 TRP A 60 9.879 77.105 37.937 1.00 62.25 ATOM 488 CZ2 TRP A 60 7.112 76.742 37.580 1.00 62.25 ATOM 489 CZ3 TRP A 60 9.374 76.529 36.793 1.00 62.25 ATOM 490 CH2 TRP A 60 8.018 76.351 36.618 1.00 62.25 ATOM 491 N ASP A 61 12.901 77.844 42.645 1.00 28.55 ATOM 492 CA ASP A 61 14.144 78.311 43.187 1.00 28.55 ATOM 493 C ASP A 61 15.195 77.281 42.927 1.00 28.55 ATOM 494 O ASP A 61 16.315 77.612 42.547 1.00 28.55 ATOM 495 CB ASP A 61 14.095 78.528 44.711 1.00 28.55 ATOM 496 CG ASP A 61 13.214 79.734 45.013 1.00 28.55 ATOM 497 OD1 ASP A 61 12.966 80.544 44.081 1.00 28.55 ATOM 498 OD2 ASP A 61 12.782 79.862 46.189 1.00 28.55 ATOM 499 N GLY A 62 14.853 75.996 43.121 1.00 16.97 ATOM 500 CA GLY A 62 15.831 74.965 42.944 1.00 16.97 ATOM 501 C GLY A 62 16.279 74.938 41.518 1.00 16.97 ATOM 502 O GLY A 62 17.470 74.814 41.236 1.00 16.97 ATOM 503 N GLU A 63 15.326 75.044 40.573 1.00 85.27 ATOM 504 CA GLU A 63 15.665 74.959 39.183 1.00 85.27 ATOM 505 C GLU A 63 16.487 76.147 38.801 1.00 85.27 ATOM 506 O GLU A 63 17.434 76.032 38.024 1.00 85.27 ATOM 507 CB GLU A 63 14.432 74.877 38.271 1.00 85.27 ATOM 508 CG GLU A 63 13.603 73.621 38.550 1.00 85.27 ATOM 509 CD GLU A 63 14.550 72.428 38.573 1.00 85.27 ATOM 510 OE1 GLU A 63 15.037 72.025 37.483 1.00 85.27 ATOM 511 OE2 GLU A 63 14.801 71.905 39.692 1.00 85.27 ATOM 512 N THR A 64 16.140 77.329 39.343 1.00 23.30 ATOM 513 CA THR A 64 16.862 78.524 39.026 1.00 23.30 ATOM 514 C THR A 64 18.267 78.360 39.512 1.00 23.30 ATOM 515 O THR A 64 19.220 78.702 38.814 1.00 23.30 ATOM 516 CB THR A 64 16.289 79.743 39.685 1.00 23.30 ATOM 517 OG1 THR A 64 14.938 79.925 39.288 1.00 23.30 ATOM 518 CG2 THR A 64 17.131 80.962 39.272 1.00 23.30 ATOM 519 N ARG A 65 18.425 77.808 40.728 1.00 65.81 ATOM 520 CA ARG A 65 19.730 77.636 41.300 1.00 65.81 ATOM 521 C ARG A 65 20.509 76.726 40.407 1.00 65.81 ATOM 522 O ARG A 65 21.667 76.994 40.092 1.00 65.81 ATOM 523 CB ARG A 65 19.697 76.935 42.669 1.00 65.81 ATOM 524 CG ARG A 65 18.960 77.697 43.771 1.00 65.81 ATOM 525 CD ARG A 65 18.948 76.949 45.107 1.00 65.81 ATOM 526 NE ARG A 65 18.262 77.821 46.100 1.00 65.81 ATOM 527 CZ ARG A 65 18.966 78.809 46.725 1.00 65.81 ATOM 528 NH1 ARG A 65 20.286 78.995 46.429 1.00 65.81 ATOM 529 NH2 ARG A 65 18.344 79.633 47.618 1.00 65.81 ATOM 530 N ASN A 66 19.872 75.626 39.963 1.00 35.85 ATOM 531 CA ASN A 66 20.551 74.655 39.154 1.00 35.85 ATOM 532 C ASN A 66 20.956 75.295 37.865 1.00 35.85 ATOM 533 O ASN A 66 22.060 75.070 37.373 1.00 35.85 ATOM 534 CB ASN A 66 19.684 73.424 38.816 1.00 35.85 ATOM 535 CG ASN A 66 20.598 72.328 38.274 1.00 35.85 ATOM 536 OD1 ASN A 66 21.801 72.325 38.530 1.00 35.85 ATOM 537 ND2 ASN A 66 20.016 71.372 37.501 1.00 35.85 ATOM 538 N MET A 67 20.072 76.123 37.282 1.00 81.71 ATOM 539 CA MET A 67 20.380 76.722 36.017 1.00 81.71 ATOM 540 C MET A 67 21.556 77.633 36.152 1.00 81.71 ATOM 541 O MET A 67 22.434 77.650 35.291 1.00 81.71 ATOM 542 CB MET A 67 19.220 77.543 35.433 1.00 81.71 ATOM 543 CG MET A 67 17.981 76.699 35.137 1.00 81.71 ATOM 544 SD MET A 67 18.317 75.165 34.220 1.00 81.71 ATOM 545 CE MET A 67 19.511 75.908 33.076 1.00 81.71 ATOM 546 N LYS A 68 21.612 78.428 37.236 1.00 42.11 ATOM 547 CA LYS A 68 22.704 79.344 37.379 1.00 42.11 ATOM 548 C LYS A 68 23.981 78.579 37.545 1.00 42.11 ATOM 549 O LYS A 68 25.012 78.957 36.989 1.00 42.11 ATOM 550 CB LYS A 68 22.486 80.350 38.523 1.00 42.11 ATOM 551 CG LYS A 68 21.410 81.379 38.149 1.00 42.11 ATOM 552 CD LYS A 68 20.896 82.251 39.297 1.00 42.11 ATOM 553 CE LYS A 68 19.828 83.253 38.847 1.00 42.11 ATOM 554 NZ LYS A 68 19.345 84.045 40.000 1.00 42.11 ATOM 555 N ALA A 69 23.945 77.475 38.314 1.00 19.69 ATOM 556 CA ALA A 69 25.116 76.667 38.510 1.00 19.69 ATOM 557 C ALA A 69 25.514 76.071 37.193 1.00 19.69 ATOM 558 O ALA A 69 26.697 76.004 36.865 1.00 19.69 ATOM 559 CB ALA A 69 24.881 75.501 39.485 1.00 19.69 ATOM 560 N SER A 70 24.520 75.622 36.403 1.00 26.43 ATOM 561 CA SER A 70 24.793 75.007 35.136 1.00 26.43 ATOM 562 C SER A 70 25.434 76.020 34.243 1.00 26.43 ATOM 563 O SER A 70 26.358 75.705 33.495 1.00 26.43 ATOM 564 CB SER A 70 23.525 74.498 34.424 1.00 26.43 ATOM 565 OG SER A 70 22.945 73.430 35.159 1.00 26.43 ATOM 566 N ALA A 71 24.972 77.281 34.310 1.00 29.29 ATOM 567 CA ALA A 71 25.529 78.296 33.467 1.00 29.29 ATOM 568 C ALA A 71 26.975 78.415 33.809 1.00 29.29 ATOM 569 O ALA A 71 27.830 78.528 32.932 1.00 29.29 ATOM 570 CB ALA A 71 24.887 79.674 33.698 1.00 29.29 ATOM 571 N GLN A 72 27.282 78.368 35.111 1.00115.57 ATOM 572 CA GLN A 72 28.631 78.520 35.552 1.00115.57 ATOM 573 C GLN A 72 29.453 77.390 35.008 1.00115.57 ATOM 574 O GLN A 72 30.561 77.606 34.518 1.00115.57 ATOM 575 CB GLN A 72 28.729 78.468 37.081 1.00115.57 ATOM 576 CG GLN A 72 30.119 78.825 37.586 1.00115.57 ATOM 577 CD GLN A 72 30.299 80.311 37.321 1.00115.57 ATOM 578 OE1 GLN A 72 29.397 80.981 36.822 1.00115.57 ATOM 579 NE2 GLN A 72 31.501 80.842 37.667 1.00115.57 ATOM 580 N THR A 73 28.922 76.152 35.057 1.00111.60 ATOM 581 CA THR A 73 29.686 75.018 34.617 1.00111.60 ATOM 582 C THR A 73 29.976 75.152 33.159 1.00111.60 ATOM 583 O THR A 73 31.089 74.885 32.712 1.00111.60 ATOM 584 CB THR A 73 28.983 73.697 34.764 1.00111.60 ATOM 585 OG1 THR A 73 27.836 73.640 33.930 1.00111.60 ATOM 586 CG2 THR A 73 28.584 73.504 36.230 1.00111.60 ATOM 587 N TYR A 74 28.962 75.558 32.380 1.00 89.34 ATOM 588 CA TYR A 74 29.102 75.675 30.959 1.00 89.34 ATOM 589 C TYR A 74 30.035 76.780 30.583 1.00 89.34 ATOM 590 O TYR A 74 30.732 76.679 29.574 1.00 89.34 ATOM 591 CB TYR A 74 27.762 75.795 30.216 1.00 89.34 ATOM 592 CG TYR A 74 27.199 74.415 30.288 1.00 89.34 ATOM 593 CD1 TYR A 74 27.694 73.433 29.461 1.00 89.34 ATOM 594 CD2 TYR A 74 26.193 74.091 31.169 1.00 89.34 ATOM 595 CE1 TYR A 74 27.202 72.151 29.509 1.00 89.34 ATOM 596 CE2 TYR A 74 25.695 72.811 31.224 1.00 89.34 ATOM 597 CZ TYR A 74 26.200 71.839 30.395 1.00 89.34 ATOM 598 OH TYR A 74 25.687 70.526 30.456 1.00 89.34 ATOM 599 N ARG A 75 30.045 77.895 31.339 1.00148.83 ATOM 600 CA ARG A 75 31.003 78.911 31.005 1.00148.83 ATOM 601 C ARG A 75 32.369 78.342 31.192 1.00148.83 ATOM 602 O ARG A 75 33.261 78.580 30.379 1.00148.83 ATOM 603 CB ARG A 75 30.937 80.194 31.855 1.00148.83 ATOM 604 CG ARG A 75 29.915 81.217 31.366 1.00148.83 ATOM 605 CD ARG A 75 28.488 80.993 31.853 1.00148.83 ATOM 606 NE ARG A 75 28.268 81.941 32.978 1.00148.83 ATOM 607 CZ ARG A 75 27.131 82.695 33.028 1.00148.83 ATOM 608 NH1 ARG A 75 26.238 82.662 31.996 1.00148.83 ATOM 609 NH2 ARG A 75 26.890 83.483 34.116 1.00148.83 ATOM 610 N GLU A 76 32.571 77.569 32.275 1.00 93.66 ATOM 611 CA GLU A 76 33.852 76.977 32.520 1.00 93.66 ATOM 612 C GLU A 76 34.166 76.041 31.398 1.00 93.66 ATOM 613 O GLU A 76 35.287 76.012 30.894 1.00 93.66 ATOM 614 CB GLU A 76 33.895 76.157 33.822 1.00 93.66 ATOM 615 CG GLU A 76 34.141 76.989 35.080 1.00 93.66 ATOM 616 CD GLU A 76 35.649 77.162 35.171 1.00 93.66 ATOM 617 OE1 GLU A 76 36.268 77.453 34.113 1.00 93.66 ATOM 618 OE2 GLU A 76 36.205 76.990 36.289 1.00 93.66 ATOM 619 N ASN A 77 33.158 75.266 30.957 1.00 46.80 ATOM 620 CA ASN A 77 33.364 74.279 29.939 1.00 46.80 ATOM 621 C ASN A 77 33.785 74.957 28.675 1.00 46.80 ATOM 622 O ASN A 77 34.611 74.429 27.932 1.00 46.80 ATOM 623 CB ASN A 77 32.102 73.451 29.651 1.00 46.80 ATOM 624 CG ASN A 77 31.851 72.599 30.887 1.00 46.80 ATOM 625 OD1 ASN A 77 32.737 72.423 31.722 1.00 46.80 ATOM 626 ND2 ASN A 77 30.612 72.050 31.006 1.00 46.80 ATOM 627 N LEU A 78 33.227 76.146 28.385 1.00 46.51 ATOM 628 CA LEU A 78 33.582 76.842 27.183 1.00 46.51 ATOM 629 C LEU A 78 35.040 77.185 27.226 1.00 46.51 ATOM 630 O LEU A 78 35.734 77.080 26.217 1.00 46.51 ATOM 631 CB LEU A 78 32.792 78.150 26.989 1.00 46.51 ATOM 632 CG LEU A 78 31.303 77.947 26.640 1.00 46.51 ATOM 633 CD1 LEU A 78 30.588 79.300 26.478 1.00 46.51 ATOM 634 CD2 LEU A 78 31.140 77.054 25.398 1.00 46.51 ATOM 635 N ARG A 79 35.538 77.624 28.399 1.00 42.43 ATOM 636 CA ARG A 79 36.921 77.978 28.560 1.00 42.43 ATOM 637 C ARG A 79 37.760 76.750 28.394 1.00 42.43 ATOM 638 O ARG A 79 38.817 76.782 27.765 1.00 42.43 ATOM 639 CB ARG A 79 37.213 78.565 29.955 1.00 42.43 ATOM 640 CG ARG A 79 36.543 79.923 30.188 1.00 42.43 ATOM 641 CD ARG A 79 36.982 80.638 31.472 1.00 42.43 ATOM 642 NE ARG A 79 36.281 80.015 32.633 1.00 42.43 ATOM 643 CZ ARG A 79 35.120 80.557 33.107 1.00 42.43 ATOM 644 NH1 ARG A 79 34.584 81.661 32.508 1.00 42.43 ATOM 645 NH2 ARG A 79 34.496 80.002 34.186 1.00 42.43 ATOM 646 N ILE A 80 37.289 75.626 28.960 1.00106.39 ATOM 647 CA ILE A 80 37.991 74.378 28.951 1.00106.39 ATOM 648 C ILE A 80 38.129 73.937 27.524 1.00106.39 ATOM 649 O ILE A 80 39.199 73.510 27.089 1.00106.39 ATOM 650 CB ILE A 80 37.210 73.332 29.696 1.00106.39 ATOM 651 CG1 ILE A 80 36.897 73.787 31.136 1.00106.39 ATOM 652 CG2 ILE A 80 38.000 72.019 29.638 1.00106.39 ATOM 653 CD1 ILE A 80 38.119 73.979 32.031 1.00106.39 ATOM 654 N ALA A 81 37.038 74.068 26.748 1.00 33.76 ATOM 655 CA ALA A 81 36.995 73.630 25.383 1.00 33.76 ATOM 656 C ALA A 81 38.013 74.376 24.582 1.00 33.76 ATOM 657 O ALA A 81 38.665 73.797 23.716 1.00 33.76 ATOM 658 CB ALA A 81 35.624 73.871 24.725 1.00 33.76 ATOM 659 N LEU A 82 38.187 75.684 24.847 1.00 42.25 ATOM 660 CA LEU A 82 39.115 76.453 24.069 1.00 42.25 ATOM 661 C LEU A 82 40.476 75.869 24.256 1.00 42.25 ATOM 662 O LEU A 82 41.256 75.775 23.311 1.00 42.25 ATOM 663 CB LEU A 82 39.172 77.936 24.471 1.00 42.25 ATOM 664 CG LEU A 82 37.880 78.706 24.147 1.00 42.25 ATOM 665 CD1 LEU A 82 38.004 80.193 24.520 1.00 42.25 ATOM 666 CD2 LEU A 82 37.459 78.492 22.684 1.00 42.25 ATOM 667 N ARG A 83 40.795 75.470 25.497 1.00132.14 ATOM 668 CA ARG A 83 42.081 74.920 25.801 1.00132.14 ATOM 669 C ARG A 83 42.276 73.605 25.093 1.00132.14 ATOM 670 O ARG A 83 43.322 73.372 24.490 1.00132.14 ATOM 671 CB ARG A 83 42.266 74.764 27.324 1.00132.14 ATOM 672 CG ARG A 83 43.622 74.205 27.744 1.00132.14 ATOM 673 CD ARG A 83 44.120 74.741 29.094 1.00132.14 ATOM 674 NE ARG A 83 43.200 74.299 30.184 1.00132.14 ATOM 675 CZ ARG A 83 42.193 75.110 30.628 1.00132.14 ATOM 676 NH1 ARG A 83 41.934 76.295 30.007 1.00132.14 ATOM 677 NH2 ARG A 83 41.441 74.739 31.707 1.00132.14 ATOM 678 N TYR A 84 41.247 72.731 25.099 1.00 90.77 ATOM 679 CA TYR A 84 41.323 71.410 24.523 1.00 90.77 ATOM 680 C TYR A 84 41.600 71.514 23.057 1.00 90.77 ATOM 681 O TYR A 84 42.348 70.711 22.498 1.00 90.77 ATOM 682 CB TYR A 84 40.013 70.623 24.725 1.00 90.77 ATOM 683 CG TYR A 84 39.990 70.118 26.132 1.00 90.77 ATOM 684 CD1 TYR A 84 40.259 70.959 27.186 1.00 90.77 ATOM 685 CD2 TYR A 84 39.653 68.811 26.404 1.00 90.77 ATOM 686 CE1 TYR A 84 40.231 70.491 28.480 1.00 90.77 ATOM 687 CE2 TYR A 84 39.621 68.339 27.697 1.00 90.77 ATOM 688 CZ TYR A 84 39.916 69.180 28.741 1.00 90.77 ATOM 689 OH TYR A 84 39.885 68.695 30.067 1.00 90.77 ATOM 690 N TYR A 85 40.916 72.463 22.404 1.00112.88 ATOM 691 CA TYR A 85 41.017 72.817 21.019 1.00112.88 ATOM 692 C TYR A 85 42.234 73.651 20.718 1.00112.88 ATOM 693 O TYR A 85 42.692 73.693 19.578 1.00112.88 ATOM 694 CB TYR A 85 39.730 73.469 20.493 1.00112.88 ATOM 695 CG TYR A 85 38.744 72.348 20.500 1.00112.88 ATOM 696 CD1 TYR A 85 38.841 71.360 19.548 1.00112.88 ATOM 697 CD2 TYR A 85 37.738 72.270 21.437 1.00112.88 ATOM 698 CE1 TYR A 85 37.955 70.308 19.525 1.00112.88 ATOM 699 CE2 TYR A 85 36.847 71.219 21.418 1.00112.88 ATOM 700 CZ TYR A 85 36.955 70.235 20.462 1.00112.88 ATOM 701 OH TYR A 85 36.047 69.154 20.438 1.00112.88 ATOM 702 N ASN A 86 42.784 74.381 21.708 1.00 74.75 ATOM 703 CA ASN A 86 43.863 75.279 21.405 1.00 74.75 ATOM 704 C ASN A 86 43.308 76.346 20.517 1.00 74.75 ATOM 705 O ASN A 86 43.932 76.759 19.541 1.00 74.75 ATOM 706 CB ASN A 86 45.044 74.601 20.686 1.00 74.75 ATOM 707 CG ASN A 86 45.847 73.824 21.722 1.00 74.75 ATOM 708 OD1 ASN A 86 47.030 74.082 21.930 1.00 74.75 ATOM 709 ND2 ASN A 86 45.188 72.858 22.413 1.00 74.75 ATOM 710 N GLN A 87 42.095 76.825 20.863 1.00 58.71 ATOM 711 CA GLN A 87 41.426 77.844 20.105 1.00 58.71 ATOM 712 C GLN A 87 41.576 79.151 20.818 1.00 58.71 ATOM 713 O GLN A 87 41.867 79.190 22.013 1.00 58.71 ATOM 714 CB GLN A 87 39.934 77.537 19.903 1.00 58.71 ATOM 715 CG GLN A 87 39.732 76.264 19.075 1.00 58.71 ATOM 716 CD GLN A 87 38.250 75.935 19.009 1.00 58.71 ATOM 717 OE1 GLN A 87 37.484 76.276 19.908 1.00 58.71 ATOM 718 NE2 GLN A 87 37.833 75.244 17.914 1.00 58.71 ATOM 719 N SER A 88 41.403 80.264 20.072 1.00 83.23 ATOM 720 CA SER A 88 41.603 81.593 20.584 1.00 83.23 ATOM 721 C SER A 88 40.447 82.018 21.432 1.00 83.23 ATOM 722 O SER A 88 39.327 81.528 21.302 1.00 83.23 ATOM 723 CB SER A 88 41.743 82.662 19.488 1.00 83.23 ATOM 724 OG SER A 88 40.502 82.837 18.821 1.00 83.23 ATOM 725 N GLU A 89 40.737 82.965 22.344 1.00 53.68 ATOM 726 CA GLU A 89 39.812 83.582 23.252 1.00 53.68 ATOM 727 C GLU A 89 38.904 84.504 22.496 1.00 53.68 ATOM 728 O GLU A 89 37.796 84.803 22.934 1.00 53.68 ATOM 729 CB GLU A 89 40.527 84.407 24.329 1.00 53.68 ATOM 730 CG GLU A 89 41.359 83.542 25.275 1.00 53.68 ATOM 731 CD GLU A 89 42.094 84.469 26.228 1.00 53.68 ATOM 732 OE1 GLU A 89 41.966 85.711 26.060 1.00 53.68 ATOM 733 OE2 GLU A 89 42.799 83.949 27.134 1.00 53.68 ATOM 734 N ALA A 90 39.390 85.019 21.357 1.00 42.36 ATOM 735 CA ALA A 90 38.697 85.997 20.566 1.00 42.36 ATOM 736 C ALA A 90 37.402 85.475 20.015 1.00 42.36 ATOM 737 O ALA A 90 36.443 86.232 19.882 1.00 42.36 ATOM 738 CB ALA A 90 39.543 86.483 19.377 1.00 42.36 ATOM 739 N GLY A 91 37.336 84.180 19.651 1.00 34.79 ATOM 740 CA GLY A 91 36.175 83.674 18.970 1.00 34.79 ATOM 741 C GLY A 91 35.023 83.385 19.885 1.00 34.79 ATOM 742 O GLY A 91 35.156 83.247 21.100 1.00 34.79 ATOM 743 N SER A 92 33.836 83.257 19.257 1.00 44.48 ATOM 744 CA SER A 92 32.606 82.950 19.920 1.00 44.48 ATOM 745 C SER A 92 32.377 81.490 19.698 1.00 44.48 ATOM 746 O SER A 92 32.521 80.997 18.580 1.00 44.48 ATOM 747 CB SER A 92 31.414 83.703 19.304 1.00 44.48 ATOM 748 OG SER A 92 30.191 83.240 19.852 1.00 44.48 ATOM 749 N HIS A 93 32.022 80.748 20.766 1.00 55.74 ATOM 750 CA HIS A 93 31.844 79.335 20.606 1.00 55.74 ATOM 751 C HIS A 93 30.613 78.927 21.347 1.00 55.74 ATOM 752 O HIS A 93 30.121 79.655 22.208 1.00 55.74 ATOM 753 CB HIS A 93 33.041 78.518 21.111 1.00 55.74 ATOM 754 CG HIS A 93 34.273 78.783 20.291 1.00 55.74 ATOM 755 ND1 HIS A 93 34.566 78.131 19.113 1.00 55.74 ATOM 756 CD2 HIS A 93 35.292 79.663 20.491 1.00 55.74 ATOM 757 CE1 HIS A 93 35.740 78.643 18.663 1.00 55.74 ATOM 758 NE2 HIS A 93 36.219 79.575 19.467 1.00 55.74 ATOM 759 N ILE A 94 30.068 77.743 21.000 1.00 56.76 ATOM 760 CA ILE A 94 28.834 77.326 21.594 1.00 56.76 ATOM 761 C ILE A 94 28.961 75.928 22.099 1.00 56.76 ATOM 762 O ILE A 94 29.512 75.050 21.438 1.00 56.76 ATOM 763 CB ILE A 94 27.702 77.290 20.606 1.00 56.76 ATOM 764 CG1 ILE A 94 27.498 78.673 19.971 1.00 56.76 ATOM 765 CG2 ILE A 94 26.451 76.743 21.315 1.00 56.76 ATOM 766 CD1 ILE A 94 26.592 78.644 18.742 1.00 56.76 ATOM 767 N ILE A 95 28.433 75.690 23.311 1.00109.94 ATOM 768 CA ILE A 95 28.413 74.355 23.812 1.00109.94 ATOM 769 C ILE A 95 26.956 74.041 23.955 1.00109.94 ATOM 770 O ILE A 95 26.168 74.880 24.391 1.00109.94 ATOM 771 CB ILE A 95 29.111 74.224 25.134 1.00109.94 ATOM 772 CG1 ILE A 95 29.644 72.803 25.320 1.00109.94 ATOM 773 CG2 ILE A 95 28.152 74.656 26.255 1.00109.94 ATOM 774 CD1 ILE A 95 30.667 72.714 26.449 1.00109.94 ATOM 775 N GLN A 96 26.543 72.838 23.514 1.00 56.24 ATOM 776 CA GLN A 96 25.156 72.491 23.603 1.00 56.24 ATOM 777 C GLN A 96 25.070 71.179 24.301 1.00 56.24 ATOM 778 O GLN A 96 25.917 70.307 24.113 1.00 56.24 ATOM 779 CB GLN A 96 24.495 72.358 22.224 1.00 56.24 ATOM 780 CG GLN A 96 24.469 73.691 21.478 1.00 56.24 ATOM 781 CD GLN A 96 24.103 73.420 20.032 1.00 56.24 ATOM 782 OE1 GLN A 96 24.628 74.059 19.122 1.00 56.24 ATOM 783 NE2 GLN A 96 23.182 72.446 19.812 1.00 56.24 ATOM 784 N VAL A 97 24.042 71.014 25.155 1.00 47.11 ATOM 785 CA VAL A 97 23.899 69.787 25.879 1.00 47.11 ATOM 786 C VAL A 97 22.473 69.364 25.796 1.00 47.11 ATOM 787 O VAL A 97 21.562 70.191 25.739 1.00 47.11 ATOM 788 CB VAL A 97 24.224 69.926 27.337 1.00 47.11 ATOM 789 CG1 VAL A 97 24.005 68.570 28.029 1.00 47.11 ATOM 790 CG2 VAL A 97 25.651 70.481 27.468 1.00 47.11 ATOM 791 N MET A 98 22.251 68.040 25.767 1.00 53.30 ATOM 792 CA MET A 98 20.923 67.511 25.730 1.00 53.30 ATOM 793 C MET A 98 20.869 66.391 26.711 1.00 53.30 ATOM 794 O MET A 98 21.780 65.570 26.782 1.00 53.30 ATOM 795 CB MET A 98 20.535 66.945 24.350 1.00 53.30 ATOM 796 CG MET A 98 19.196 66.200 24.302 1.00 53.30 ATOM 797 SD MET A 98 19.246 64.491 24.926 1.00 53.30 ATOM 798 CE MET A 98 20.147 63.804 23.503 1.00 53.30 ATOM 799 N TYR A 99 19.794 66.368 27.518 1.00 69.50 ATOM 800 CA TYR A 99 19.534 65.307 28.444 1.00 69.50 ATOM 801 C TYR A 99 18.156 64.855 28.121 1.00 69.50 ATOM 802 O TYR A 99 17.312 65.671 27.756 1.00 69.50 ATOM 803 CB TYR A 99 19.431 65.729 29.921 1.00 69.50 ATOM 804 CG TYR A 99 20.761 66.037 30.515 1.00 69.50 ATOM 805 CD1 TYR A 99 21.347 67.270 30.351 1.00 69.50 ATOM 806 CD2 TYR A 99 21.409 65.082 31.265 1.00 69.50 ATOM 807 CE1 TYR A 99 22.567 67.543 30.922 1.00 69.50 ATOM 808 CE2 TYR A 99 22.629 65.348 31.837 1.00 69.50 ATOM 809 CZ TYR A 99 23.210 66.580 31.664 1.00 69.50 ATOM 810 OH TYR A 99 24.463 66.854 32.254 1.00 69.50 ATOM 811 N GLY A 100 17.880 63.544 28.230 1.00 37.30 ATOM 812 CA GLY A 100 16.532 63.179 27.940 1.00 37.30 ATOM 813 C GLY A 100 16.285 61.763 28.319 1.00 37.30 ATOM 814 O GLY A 100 17.189 60.932 28.364 1.00 37.30 ATOM 815 N CYS A 101 15.016 61.466 28.642 1.00 72.88 ATOM 816 CA CYS A 101 14.661 60.102 28.844 1.00 72.88 ATOM 817 C CYS A 101 13.380 59.861 28.144 1.00 72.88 ATOM 818 O CYS A 101 12.531 60.744 28.028 1.00 72.88 ATOM 819 CB CYS A 101 14.562 59.622 30.294 1.00 72.88 ATOM 820 SG CYS A 101 13.782 60.811 31.400 1.00 72.88 ATOM 821 N ASP A 102 13.257 58.636 27.612 1.00 55.37 ATOM 822 CA ASP A 102 12.102 58.222 26.885 1.00 55.37 ATOM 823 C ASP A 102 11.433 57.200 27.737 1.00 55.37 ATOM 824 O ASP A 102 12.101 56.368 28.354 1.00 55.37 ATOM 825 CB ASP A 102 12.457 57.514 25.568 1.00 55.37 ATOM 826 CG ASP A 102 13.175 58.518 24.683 1.00 55.37 ATOM 827 OD1 ASP A 102 13.081 59.737 24.986 1.00 55.37 ATOM 828 OD2 ASP A 102 13.833 58.084 23.699 1.00 55.37 ATOM 829 N VAL A 103 10.089 57.245 27.802 1.00 31.08 ATOM 830 CA VAL A 103 9.378 56.292 28.600 1.00 31.08 ATOM 831 C VAL A 103 8.291 55.711 27.750 1.00 31.08 ATOM 832 O VAL A 103 7.843 56.334 26.787 1.00 31.08 ATOM 833 CB VAL A 103 8.731 56.908 29.806 1.00 31.08 ATOM 834 CG1 VAL A 103 9.837 57.498 30.701 1.00 31.08 ATOM 835 CG2 VAL A 103 7.701 57.948 29.333 1.00 31.08 ATOM 836 N GLY A 104 7.863 54.472 28.078 1.00 29.26 ATOM 837 CA GLY A 104 6.816 53.817 27.346 1.00 29.26 ATOM 838 C GLY A 104 5.510 54.227 27.954 1.00 29.26 ATOM 839 O GLY A 104 5.476 55.011 28.901 1.00 29.26 ATOM 840 N PRO A 105 4.427 53.701 27.439 1.00 68.54 ATOM 841 CA PRO A 105 3.121 54.032 27.945 1.00 68.54 ATOM 842 C PRO A 105 3.021 53.596 29.366 1.00 68.54 ATOM 843 O PRO A 105 2.230 54.157 30.123 1.00 68.54 ATOM 844 CB PRO A 105 2.132 53.366 26.993 1.00 68.54 ATOM 845 CG PRO A 105 2.896 53.332 25.655 1.00 68.54 ATOM 846 CD PRO A 105 4.380 53.251 26.057 1.00 68.54 ATOM 847 N ASP A 106 3.811 52.575 29.715 1.00139.92 ATOM 848 CA ASP A 106 3.928 52.013 31.023 1.00139.92 ATOM 849 C ASP A 106 4.573 53.037 31.915 1.00139.92 ATOM 850 O ASP A 106 4.368 53.029 33.128 1.00139.92 ATOM 851 CB ASP A 106 4.786 50.734 30.954 1.00139.92 ATOM 852 CG ASP A 106 5.081 50.216 32.343 1.00139.92 ATOM 853 OD1 ASP A 106 5.824 50.916 33.079 1.00139.92 ATOM 854 OD2 ASP A 106 4.583 49.111 32.684 1.00139.92 ATOM 855 N GLY A 107 5.407 53.929 31.347 1.00 24.90 ATOM 856 CA GLY A 107 6.063 54.922 32.155 1.00 24.90 ATOM 857 C GLY A 107 7.439 54.427 32.472 1.00 24.90 ATOM 858 O GLY A 107 8.234 55.128 33.098 1.00 24.90 ATOM 859 N ARG A 108 7.754 53.189 32.045 1.00 86.79 ATOM 860 CA ARG A 108 9.054 52.641 32.309 1.00 86.79 ATOM 861 C ARG A 108 10.032 53.227 31.345 1.00 86.79 ATOM 862 O ARG A 108 9.691 53.546 30.208 1.00 86.79 ATOM 863 CB ARG A 108 9.111 51.111 32.202 1.00 86.79 ATOM 864 CG ARG A 108 8.502 50.428 33.425 1.00 86.79 ATOM 865 CD ARG A 108 8.571 48.905 33.398 1.00 86.79 ATOM 866 NE ARG A 108 8.276 48.457 34.786 1.00 86.79 ATOM 867 CZ ARG A 108 7.387 47.449 35.004 1.00 86.79 ATOM 868 NH1 ARG A 108 6.748 46.876 33.945 1.00 86.79 ATOM 869 NH2 ARG A 108 7.136 47.022 36.276 1.00 86.79 ATOM 870 N LEU A 109 11.293 53.384 31.792 1.00 71.57 ATOM 871 CA LEU A 109 12.281 54.028 30.978 1.00 71.57 ATOM 872 C LEU A 109 12.627 53.163 29.810 1.00 71.57 ATOM 873 O LEU A 109 13.029 52.010 29.965 1.00 71.57 ATOM 874 CB LEU A 109 13.565 54.370 31.757 1.00 71.57 ATOM 875 CG LEU A 109 14.612 55.139 30.932 1.00 71.57 ATOM 876 CD1 LEU A 109 14.037 56.474 30.433 1.00 71.57 ATOM 877 CD2 LEU A 109 15.920 55.327 31.719 1.00 71.57 ATOM 878 N LEU A 110 12.388 53.694 28.594 1.00 60.82 ATOM 879 CA LEU A 110 12.778 53.027 27.388 1.00 60.82 ATOM 880 C LEU A 110 14.257 53.169 27.242 1.00 60.82 ATOM 881 O LEU A 110 14.977 52.201 27.002 1.00 60.82 ATOM 882 CB LEU A 110 12.140 53.648 26.134 1.00 60.82 ATOM 883 CG LEU A 110 10.601 53.591 26.108 1.00 60.82 ATOM 884 CD1 LEU A 110 10.057 54.152 24.785 1.00 60.82 ATOM 885 CD2 LEU A 110 10.079 52.178 26.411 1.00 60.82 ATOM 886 N ARG A 111 14.744 54.418 27.407 1.00216.09 ATOM 887 CA ARG A 111 16.139 54.678 27.229 1.00216.09 ATOM 888 C ARG A 111 16.435 56.071 27.702 1.00216.09 ATOM 889 O ARG A 111 15.536 56.906 27.806 1.00216.09 ATOM 890 CB ARG A 111 16.557 54.588 25.759 1.00216.09 ATOM 891 CG ARG A 111 18.020 54.937 25.570 1.00216.09 ATOM 892 CD ARG A 111 18.434 55.166 24.125 1.00216.09 ATOM 893 NE ARG A 111 19.737 55.875 24.212 1.00216.09 ATOM 894 CZ ARG A 111 20.406 56.240 23.084 1.00216.09 ATOM 895 NH1 ARG A 111 19.931 55.877 21.857 1.00216.09 ATOM 896 NH2 ARG A 111 21.545 56.981 23.197 1.00216.09 ATOM 897 N GLY A 112 17.726 56.356 27.988 1.00 38.45 ATOM 898 CA GLY A 112 18.149 57.648 28.456 1.00 38.45 ATOM 899 C GLY A 112 19.084 58.240 27.444 1.00 38.45 ATOM 900 O GLY A 112 19.659 57.530 26.618 1.00 38.45 ATOM 901 N HIS A 113 19.259 59.579 27.490 1.00 68.38 ATOM 902 CA HIS A 113 20.093 60.235 26.527 1.00 68.38 ATOM 903 C HIS A 113 20.842 61.334 27.212 1.00 68.38 ATOM 904 O HIS A 113 20.319 62.012 28.094 1.00 68.38 ATOM 905 CB HIS A 113 19.286 60.912 25.405 1.00 68.38 ATOM 906 CG HIS A 113 18.343 59.969 24.716 1.00 68.38 ATOM 907 ND1 HIS A 113 18.645 59.248 23.584 1.00 68.38 ATOM 908 CD2 HIS A 113 17.066 59.629 25.044 1.00 68.38 ATOM 909 CE1 HIS A 113 17.543 58.512 23.283 1.00 68.38 ATOM 910 NE2 HIS A 113 16.561 58.711 24.142 1.00 68.38 ATOM 911 N ASN A 114 22.123 61.500 26.841 1.00 77.23 ATOM 912 CA ASN A 114 22.890 62.604 27.331 1.00 77.23 ATOM 913 C ASN A 114 23.948 62.838 26.307 1.00 77.23 ATOM 914 O ASN A 114 24.843 62.008 26.138 1.00 77.23 ATOM 915 CB ASN A 114 23.600 62.303 28.660 1.00 77.23 ATOM 916 CG ASN A 114 24.318 63.565 29.106 1.00 77.23 ATOM 917 OD1 ASN A 114 25.271 63.506 29.881 1.00 77.23 ATOM 918 ND2 ASN A 114 23.853 64.742 28.606 1.00 77.23 ATOM 919 N GLN A 115 23.882 63.981 25.597 1.00 49.36 ATOM 920 CA GLN A 115 24.869 64.226 24.588 1.00 49.36 ATOM 921 C GLN A 115 25.340 65.639 24.697 1.00 49.36 ATOM 922 O GLN A 115 24.622 66.518 25.171 1.00 49.36 ATOM 923 CB GLN A 115 24.362 64.013 23.152 1.00 49.36 ATOM 924 CG GLN A 115 23.963 62.566 22.853 1.00 49.36 ATOM 925 CD GLN A 115 23.549 62.485 21.391 1.00 49.36 ATOM 926 OE1 GLN A 115 22.541 61.869 21.046 1.00 49.36 ATOM 927 NE2 GLN A 115 24.358 63.121 20.502 1.00 49.36 ATOM 928 N TYR A 116 26.590 65.882 24.254 1.00 55.47 ATOM 929 CA TYR A 116 27.164 67.194 24.326 1.00 55.47 ATOM 930 C TYR A 116 27.703 67.523 22.969 1.00 55.47 ATOM 931 O TYR A 116 28.096 66.637 22.211 1.00 55.47 ATOM 932 CB TYR A 116 28.352 67.271 25.302 1.00 55.47 ATOM 933 CG TYR A 116 27.866 66.872 26.656 1.00 55.47 ATOM 934 CD1 TYR A 116 27.658 65.544 26.948 1.00 55.47 ATOM 935 CD2 TYR A 116 27.633 67.812 27.634 1.00 55.47 ATOM 936 CE1 TYR A 116 27.216 65.153 28.189 1.00 55.47 ATOM 937 CE2 TYR A 116 27.190 67.428 28.879 1.00 55.47 ATOM 938 CZ TYR A 116 26.977 66.099 29.155 1.00 55.47 ATOM 939 OH TYR A 116 26.521 65.703 30.430 1.00 55.47 ATOM 940 N ALA A 117 27.711 68.826 22.624 1.00 29.78 ATOM 941 CA ALA A 117 28.229 69.240 21.354 1.00 29.78 ATOM 942 C ALA A 117 29.017 70.491 21.572 1.00 29.78 ATOM 943 O ALA A 117 28.761 71.250 22.505 1.00 29.78 ATOM 944 CB ALA A 117 27.134 69.561 20.324 1.00 29.78 ATOM 945 N TYR A 118 30.043 70.699 20.721 1.00 67.98 ATOM 946 CA TYR A 118 30.833 71.892 20.784 1.00 67.98 ATOM 947 C TYR A 118 30.825 72.453 19.393 1.00 67.98 ATOM 948 O TYR A 118 31.180 71.770 18.435 1.00 67.98 ATOM 949 CB TYR A 118 32.288 71.607 21.202 1.00 67.98 ATOM 950 CG TYR A 118 33.053 72.884 21.309 1.00 67.98 ATOM 951 CD1 TYR A 118 32.840 73.742 22.363 1.00 67.98 ATOM 952 CD2 TYR A 118 34.013 73.206 20.376 1.00 67.98 ATOM 953 CE1 TYR A 118 33.550 74.916 22.469 1.00 67.98 ATOM 954 CE2 TYR A 118 34.727 74.377 20.475 1.00 67.98 ATOM 955 CZ TYR A 118 34.496 75.234 21.524 1.00 67.98 ATOM 956 OH TYR A 118 35.228 76.436 21.628 1.00 67.98 ATOM 957 N ASP A 119 30.403 73.723 19.256 1.00 56.81 ATOM 958 CA ASP A 119 30.331 74.385 17.985 1.00 56.81 ATOM 959 C ASP A 119 29.483 73.592 17.040 1.00 56.81 ATOM 960 O ASP A 119 29.717 73.588 15.831 1.00 56.81 ATOM 961 CB ASP A 119 31.700 74.647 17.329 1.00 56.81 ATOM 962 CG ASP A 119 32.374 75.795 18.070 1.00 56.81 ATOM 963 OD1 ASP A 119 31.949 76.098 19.218 1.00 56.81 ATOM 964 OD2 ASP A 119 33.321 76.393 17.491 1.00 56.81 ATOM 965 N GLY A 120 28.456 72.906 17.568 1.00 19.92 ATOM 966 CA GLY A 120 27.530 72.228 16.708 1.00 19.92 ATOM 967 C GLY A 120 28.057 70.888 16.289 1.00 19.92 ATOM 968 O GLY A 120 27.463 70.240 15.430 1.00 19.92 ATOM 969 N LYS A 121 29.184 70.429 16.869 1.00 64.26 ATOM 970 CA LYS A 121 29.711 69.136 16.524 1.00 64.26 ATOM 971 C LYS A 121 29.573 68.281 17.744 1.00 64.26 ATOM 972 O LYS A 121 29.736 68.764 18.862 1.00 64.26 ATOM 973 CB LYS A 121 31.212 69.158 16.176 1.00 64.26 ATOM 974 CG LYS A 121 31.784 67.785 15.808 1.00 64.26 ATOM 975 CD LYS A 121 33.203 67.839 15.239 1.00 64.26 ATOM 976 CE LYS A 121 33.797 66.461 14.933 1.00 64.26 ATOM 977 NZ LYS A 121 34.074 65.735 16.193 1.00 64.26 ATOM 978 N ASP A 122 29.264 66.980 17.567 1.00 67.55 ATOM 979 CA ASP A 122 29.076 66.116 18.699 1.00 67.55 ATOM 980 C ASP A 122 30.384 65.970 19.415 1.00 67.55 ATOM 981 O ASP A 122 31.388 65.625 18.796 1.00 67.55 ATOM 982 CB ASP A 122 28.577 64.722 18.298 1.00 67.55 ATOM 983 CG ASP A 122 27.198 64.914 17.685 1.00 67.55 ATOM 984 OD1 ASP A 122 26.678 66.062 17.731 1.00 67.55 ATOM 985 OD2 ASP A 122 26.644 63.915 17.156 1.00 67.55 ATOM 986 N TYR A 123 30.434 66.376 20.704 1.00102.19 ATOM 987 CA TYR A 123 31.605 66.245 21.531 1.00102.19 ATOM 988 C TYR A 123 31.722 64.885 22.164 1.00102.19 ATOM 989 O TYR A 123 32.705 64.166 21.985 1.00102.19 ATOM 990 CB TYR A 123 31.575 67.297 22.656 1.00102.19 ATOM 991 CG TYR A 123 32.883 67.336 23.370 1.00102.19 ATOM 992 CD1 TYR A 123 33.935 68.055 22.849 1.00102.19 ATOM 993 CD2 TYR A 123 33.057 66.676 24.563 1.00102.19 ATOM 994 CE1 TYR A 123 35.145 68.105 23.500 1.00102.19 ATOM 995 CE2 TYR A 123 34.267 66.721 25.220 1.00102.19 ATOM 996 CZ TYR A 123 35.313 67.438 24.690 1.00102.19 ATOM 997 OH TYR A 123 36.554 67.485 25.363 1.00102.19 ATOM 998 N ILE A 124 30.679 64.495 22.928 1.00 62.71 ATOM 999 CA ILE A 124 30.695 63.243 23.631 1.00 62.71 ATOM 1000 C ILE A 124 29.276 62.849 23.864 1.00 62.71 ATOM 1001 O ILE A 124 28.395 63.703 23.958 1.00 62.71 ATOM 1002 CB ILE A 124 31.365 63.308 24.974 1.00 62.71 ATOM 1003 CG1 ILE A 124 31.595 61.896 25.536 1.00 62.71 ATOM 1004 CG2 ILE A 124 30.521 64.211 25.891 1.00 62.71 ATOM 1005 CD1 ILE A 124 32.532 61.869 26.741 1.00 62.71 ATOM 1006 N ALA A 125 29.006 61.533 23.963 1.00 41.03 ATOM 1007 CA ALA A 125 27.657 61.128 24.218 1.00 41.03 ATOM 1008 C ALA A 125 27.683 59.955 25.138 1.00 41.03 ATOM 1009 O ALA A 125 28.583 59.118 25.082 1.00 41.03 ATOM 1010 CB ALA A 125 26.903 60.688 22.951 1.00 41.03 ATOM 1011 N LEU A 126 26.692 59.888 26.045 1.00 53.13 ATOM 1012 CA LEU A 126 26.596 58.751 26.907 1.00 53.13 ATOM 1013 C LEU A 126 25.977 57.673 26.080 1.00 53.13 ATOM 1014 O LEU A 126 25.047 57.920 25.317 1.00 53.13 ATOM 1015 CB LEU A 126 25.730 58.999 28.157 1.00 53.13 ATOM 1016 CG LEU A 126 25.618 57.786 29.100 1.00 53.13 ATOM 1017 CD1 LEU A 126 26.988 57.392 29.671 1.00 53.13 ATOM 1018 CD2 LEU A 126 24.577 58.042 30.201 1.00 53.13 ATOM 1019 N ASN A 127 26.490 56.436 26.204 1.00 57.35 ATOM 1020 CA ASN A 127 25.962 55.354 25.427 1.00 57.35 ATOM 1021 C ASN A 127 24.647 54.947 26.006 1.00 57.35 ATOM 1022 O ASN A 127 24.276 55.352 27.105 1.00 57.35 ATOM 1023 CB ASN A 127 26.869 54.113 25.381 1.00 57.35 ATOM 1024 CG ASN A 127 28.029 54.410 24.439 1.00 57.35 ATOM 1025 OD1 ASN A 127 28.679 55.451 24.528 1.00 57.35 ATOM 1026 ND2 ASN A 127 28.294 53.468 23.496 1.00 57.35 ATOM 1027 N GLU A 128 23.912 54.115 25.246 1.00 58.50 ATOM 1028 CA GLU A 128 22.592 53.668 25.584 1.00 58.50 ATOM 1029 C GLU A 128 22.653 52.895 26.862 1.00 58.50 ATOM 1030 O GLU A 128 21.702 52.894 27.643 1.00 58.50 ATOM 1031 CB GLU A 128 21.991 52.785 24.480 1.00 58.50 ATOM 1032 CG GLU A 128 20.509 52.467 24.671 1.00 58.50 ATOM 1033 CD GLU A 128 19.991 51.934 23.343 1.00 58.50 ATOM 1034 OE1 GLU A 128 20.627 52.240 22.298 1.00 58.50 ATOM 1035 OE2 GLU A 128 18.952 51.223 23.350 1.00 58.50 ATOM 1036 N ASP A 129 23.787 52.218 27.110 1.00 66.61 ATOM 1037 CA ASP A 129 23.966 51.434 28.299 1.00 66.61 ATOM 1038 C ASP A 129 23.900 52.332 29.502 1.00 66.61 ATOM 1039 O ASP A 129 23.636 51.865 30.608 1.00 66.61 ATOM 1040 CB ASP A 129 25.286 50.626 28.310 1.00 66.61 ATOM 1041 CG ASP A 129 26.496 51.544 28.188 1.00 66.61 ATOM 1042 OD1 ASP A 129 26.305 52.784 28.083 1.00 66.61 ATOM 1043 OD2 ASP A 129 27.637 51.008 28.183 1.00 66.61 ATOM 1044 N LEU A 130 24.160 53.645 29.314 1.00 93.16 ATOM 1045 CA LEU A 130 24.166 54.636 30.360 1.00 93.16 ATOM 1046 C LEU A 130 25.376 54.410 31.208 1.00 93.16 ATOM 1047 O LEU A 130 25.529 55.033 32.259 1.00 93.16 ATOM 1048 CB LEU A 130 22.932 54.607 31.282 1.00 93.16 ATOM 1049 CG LEU A 130 21.625 55.007 30.575 1.00 93.16 ATOM 1050 CD1 LEU A 130 20.465 55.104 31.578 1.00 93.16 ATOM 1051 CD2 LEU A 130 21.801 56.282 29.732 1.00 93.16 ATOM 1052 N SER A 131 26.211 53.427 30.815 1.00 90.05 ATOM 1053 CA SER A 131 27.449 53.115 31.473 1.00 90.05 ATOM 1054 C SER A 131 28.670 53.724 30.830 1.00 90.05 ATOM 1055 O SER A 131 29.598 54.134 31.526 1.00 90.05 ATOM 1056 CB SER A 131 27.698 51.597 31.536 1.00 90.05 ATOM 1057 OG SER A 131 26.672 50.965 32.289 1.00 90.05 ATOM 1058 N SER A 132 28.710 53.798 29.480 1.00 53.08 ATOM 1059 CA SER A 132 29.945 54.138 28.819 1.00 53.08 ATOM 1060 C SER A 132 29.767 55.323 27.927 1.00 53.08 ATOM 1061 O SER A 132 28.654 55.805 27.723 1.00 53.08 ATOM 1062 CB SER A 132 30.511 52.980 27.979 1.00 53.08 ATOM 1063 OG SER A 132 29.589 52.614 26.963 1.00 53.08 ATOM 1064 N TRP A 133 30.894 55.823 27.368 1.00 85.20 ATOM 1065 CA TRP A 133 30.849 57.052 26.634 1.00 85.20 ATOM 1066 C TRP A 133 31.405 56.856 25.261 1.00 85.20 ATOM 1067 O TRP A 133 32.203 55.956 25.009 1.00 85.20 ATOM 1068 CB TRP A 133 31.728 58.131 27.283 1.00 85.20 ATOM 1069 CG TRP A 133 31.409 58.358 28.738 1.00 85.20 ATOM 1070 CD1 TRP A 133 32.002 57.795 29.831 1.00 85.20 ATOM 1071 CD2 TRP A 133 30.374 59.222 29.237 1.00 85.20 ATOM 1072 NE1 TRP A 133 31.403 58.250 30.979 1.00 85.20 ATOM 1073 CE2 TRP A 133 30.401 59.129 30.630 1.00 85.20 ATOM 1074 CE3 TRP A 133 29.478 60.017 28.587 1.00 85.20 ATOM 1075 CZ2 TRP A 133 29.522 59.837 31.397 1.00 85.20 ATOM 1076 CZ3 TRP A 133 28.599 60.736 29.369 1.00 85.20 ATOM 1077 CH2 TRP A 133 28.621 60.648 30.747 1.00 85.20 ATOM 1078 N THR A 134 30.945 57.710 24.325 1.00 41.54 ATOM 1079 CA THR A 134 31.474 57.742 22.995 1.00 41.54 ATOM 1080 C THR A 134 32.009 59.127 22.828 1.00 41.54 ATOM 1081 O THR A 134 31.264 60.100 22.938 1.00 41.54 ATOM 1082 CB THR A 134 30.437 57.556 21.928 1.00 41.54 ATOM 1083 OG1 THR A 134 29.786 56.305 22.093 1.00 41.54 ATOM 1084 CG2 THR A 134 31.117 57.632 20.550 1.00 41.54 ATOM 1085 N ALA A 135 33.323 59.252 22.557 1.00 32.99 ATOM 1086 CA ALA A 135 33.907 60.556 22.420 1.00 32.99 ATOM 1087 C ALA A 135 34.200 60.781 20.971 1.00 32.99 ATOM 1088 O ALA A 135 34.726 59.907 20.285 1.00 32.99 ATOM 1089 CB ALA A 135 35.227 60.716 23.190 1.00 32.99 ATOM 1090 N ALA A 136 33.825 61.975 20.473 1.00 47.70 ATOM 1091 CA ALA A 136 34.002 62.351 19.098 1.00 47.70 ATOM 1092 C ALA A 136 35.451 62.485 18.746 1.00 47.70 ATOM 1093 O ALA A 136 35.872 62.034 17.683 1.00 47.70 ATOM 1094 CB ALA A 136 33.344 63.701 18.767 1.00 47.70 ATOM 1095 N ASP A 137 36.259 63.127 19.613 1.00 72.79 ATOM 1096 CA ASP A 137 37.628 63.326 19.238 1.00 72.79 ATOM 1097 C ASP A 137 38.506 63.215 20.440 1.00 72.79 ATOM 1098 O ASP A 137 38.076 62.805 21.515 1.00 72.79 ATOM 1099 CB ASP A 137 37.894 64.676 18.544 1.00 72.79 ATOM 1100 CG ASP A 137 37.535 65.823 19.480 1.00 72.79 ATOM 1101 OD1 ASP A 137 37.074 65.553 20.621 1.00 72.79 ATOM 1102 OD2 ASP A 137 37.714 66.996 19.054 1.00 72.79 ATOM 1103 N THR A 138 39.791 63.575 20.260 1.00101.12 ATOM 1104 CA THR A 138 40.785 63.476 21.287 1.00101.12 ATOM 1105 C THR A 138 40.449 64.384 22.429 1.00101.12 ATOM 1106 O THR A 138 40.715 64.050 23.581 1.00101.12 ATOM 1107 CB THR A 138 42.152 63.846 20.800 1.00101.12 ATOM 1108 OG1 THR A 138 43.104 63.650 21.834 1.00101.12 ATOM 1109 CG2 THR A 138 42.137 65.317 20.357 1.00101.12 ATOM 1110 N ALA A 139 39.904 65.582 22.148 1.00 36.81 ATOM 1111 CA ALA A 139 39.581 66.487 23.215 1.00 36.81 ATOM 1112 C ALA A 139 38.509 65.875 24.063 1.00 36.81 ATOM 1113 O ALA A 139 38.594 65.875 25.290 1.00 36.81 ATOM 1114 CB ALA A 139 39.070 67.851 22.713 1.00 36.81 ATOM 1115 N ALA A 140 37.485 65.299 23.411 1.00 36.40 ATOM 1116 CA ALA A 140 36.368 64.701 24.082 1.00 36.40 ATOM 1117 C ALA A 140 36.860 63.559 24.907 1.00 36.40 ATOM 1118 O ALA A 140 36.319 63.275 25.974 1.00 36.40 ATOM 1119 CB ALA A 140 35.316 64.138 23.111 1.00 36.40 ATOM 1120 N GLN A 141 37.894 62.857 24.413 1.00 42.26 ATOM 1121 CA GLN A 141 38.423 61.722 25.108 1.00 42.26 ATOM 1122 C GLN A 141 38.953 62.171 26.429 1.00 42.26 ATOM 1123 O GLN A 141 38.889 61.432 27.409 1.00 42.26 ATOM 1124 CB GLN A 141 39.551 61.016 24.344 1.00 42.26 ATOM 1125 CG GLN A 141 39.049 60.376 23.051 1.00 42.26 ATOM 1126 CD GLN A 141 40.226 59.701 22.369 1.00 42.26 ATOM 1127 OE1 GLN A 141 41.321 59.623 22.925 1.00 42.26 ATOM 1128 NE2 GLN A 141 39.991 59.188 21.133 1.00 42.26 ATOM 1129 N ILE A 142 39.514 63.391 26.495 1.00 87.60 ATOM 1130 CA ILE A 142 40.024 63.854 27.748 1.00 87.60 ATOM 1131 C ILE A 142 38.879 63.944 28.701 1.00 87.60 ATOM 1132 O ILE A 142 38.987 63.536 29.856 1.00 87.60 ATOM 1133 CB ILE A 142 40.678 65.196 27.656 1.00 87.60 ATOM 1134 CG1 ILE A 142 41.911 65.086 26.745 1.00 87.60 ATOM 1135 CG2 ILE A 142 41.003 65.668 29.080 1.00 87.60 ATOM 1136 CD1 ILE A 142 42.907 64.029 27.220 1.00 87.60 ATOM 1137 N THR A 143 37.740 64.476 28.228 1.00 34.87 ATOM 1138 CA THR A 143 36.569 64.598 29.043 1.00 34.87 ATOM 1139 C THR A 143 36.117 63.224 29.428 1.00 34.87 ATOM 1140 O THR A 143 35.737 62.979 30.573 1.00 34.87 ATOM 1141 CB THR A 143 35.448 65.265 28.307 1.00 34.87 ATOM 1142 OG1 THR A 143 35.844 66.572 27.916 1.00 34.87 ATOM 1143 CG2 THR A 143 34.209 65.322 29.215 1.00 34.87 ATOM 1144 N GLN A 144 36.170 62.276 28.476 1.00 41.38 ATOM 1145 CA GLN A 144 35.702 60.944 28.725 1.00 41.38 ATOM 1146 C GLN A 144 36.503 60.336 29.832 1.00 41.38 ATOM 1147 O GLN A 144 35.955 59.717 30.742 1.00 41.38 ATOM 1148 CB GLN A 144 35.876 60.031 27.499 1.00 41.38 ATOM 1149 CG GLN A 144 35.393 58.598 27.721 1.00 41.38 ATOM 1150 CD GLN A 144 35.731 57.803 26.467 1.00 41.38 ATOM 1151 OE1 GLN A 144 36.378 58.307 25.552 1.00 41.38 ATOM 1152 NE2 GLN A 144 35.285 56.519 26.426 1.00 41.38 ATOM 1153 N ARG A 145 37.831 60.527 29.790 1.00109.26 ATOM 1154 CA ARG A 145 38.722 59.923 30.734 1.00109.26 ATOM 1155 C ARG A 145 38.390 60.464 32.089 1.00109.26 ATOM 1156 O ARG A 145 38.340 59.726 33.073 1.00109.26 ATOM 1157 CB ARG A 145 40.179 60.272 30.384 1.00109.26 ATOM 1158 CG ARG A 145 41.206 59.213 30.782 1.00109.26 ATOM 1159 CD ARG A 145 42.626 59.562 30.323 1.00109.26 ATOM 1160 NE ARG A 145 42.539 60.084 28.927 1.00109.26 ATOM 1161 CZ ARG A 145 42.488 59.246 27.850 1.00109.26 ATOM 1162 NH1 ARG A 145 42.474 57.892 28.024 1.00109.26 ATOM 1163 NH2 ARG A 145 42.436 59.768 26.590 1.00109.26 ATOM 1164 N LYS A 146 38.137 61.783 32.166 1.00 61.90 ATOM 1165 CA LYS A 146 37.826 62.412 33.413 1.00 61.90 ATOM 1166 C LYS A 146 36.532 61.864 33.931 1.00 61.90 ATOM 1167 O LYS A 146 36.408 61.548 35.113 1.00 61.90 ATOM 1168 CB LYS A 146 37.655 63.934 33.285 1.00 61.90 ATOM 1169 CG LYS A 146 38.916 64.665 32.822 1.00 61.90 ATOM 1170 CD LYS A 146 38.677 66.144 32.507 1.00 61.90 ATOM 1171 CE LYS A 146 38.405 66.979 33.761 1.00 61.90 ATOM 1172 NZ LYS A 146 38.352 68.418 33.420 1.00 61.90 ATOM 1173 N TRP A 147 35.531 61.732 33.040 1.00 73.75 ATOM 1174 CA TRP A 147 34.216 61.283 33.400 1.00 73.75 ATOM 1175 C TRP A 147 34.241 59.858 33.846 1.00 73.75 ATOM 1176 O TRP A 147 33.496 59.473 34.746 1.00 73.75 ATOM 1177 CB TRP A 147 33.211 61.458 32.254 1.00 73.75 ATOM 1178 CG TRP A 147 32.883 62.916 32.058 1.00 73.75 ATOM 1179 CD1 TRP A 147 33.474 63.993 32.648 1.00 73.75 ATOM 1180 CD2 TRP A 147 31.845 63.432 31.212 1.00 73.75 ATOM 1181 NE1 TRP A 147 32.871 65.151 32.224 1.00 73.75 ATOM 1182 CE2 TRP A 147 31.867 64.823 31.340 1.00 73.75 ATOM 1183 CE3 TRP A 147 30.949 62.805 30.397 1.00 73.75 ATOM 1184 CZ2 TRP A 147 30.989 65.607 30.651 1.00 73.75 ATOM 1185 CZ3 TRP A 147 30.063 63.601 29.705 1.00 73.75 ATOM 1186 CH2 TRP A 147 30.083 64.974 29.829 1.00 73.75 ATOM 1187 N GLU A 148 35.067 59.022 33.198 1.00 42.95 ATOM 1188 CA GLU A 148 35.145 57.648 33.596 1.00 42.95 ATOM 1189 C GLU A 148 35.745 57.569 34.965 1.00 42.95 ATOM 1190 O GLU A 148 35.282 56.806 35.812 1.00 42.95 ATOM 1191 CB GLU A 148 35.989 56.806 32.632 1.00 42.95 ATOM 1192 CG GLU A 148 35.269 56.587 31.301 1.00 42.95 ATOM 1193 CD GLU A 148 36.228 55.913 30.336 1.00 42.95 ATOM 1194 OE1 GLU A 148 37.234 56.567 29.951 1.00 42.95 ATOM 1195 OE2 GLU A 148 35.965 54.739 29.965 1.00 42.95 ATOM 1196 N ALA A 149 36.794 58.374 35.226 1.00 25.01 ATOM 1197 CA ALA A 149 37.448 58.346 36.504 1.00 25.01 ATOM 1198 C ALA A 149 36.458 58.764 37.549 1.00 25.01 ATOM 1199 O ALA A 149 36.385 58.178 38.629 1.00 25.01 ATOM 1200 CB ALA A 149 38.634 59.323 36.573 1.00 25.01 ATOM 1201 N ALA A 150 35.681 59.814 37.227 1.00 54.68 ATOM 1202 CA ALA A 150 34.662 60.411 38.044 1.00 54.68 ATOM 1203 C ALA A 150 33.524 59.453 38.221 1.00 54.68 ATOM 1204 O ALA A 150 32.832 59.487 39.235 1.00 54.68 ATOM 1205 CB ALA A 150 34.079 61.698 37.431 1.00 54.68 ATOM 1206 N ARG A 151 33.280 58.578 37.232 1.00120.60 ATOM 1207 CA ARG A 151 32.130 57.725 37.321 1.00120.60 ATOM 1208 C ARG A 151 30.910 58.585 37.221 1.00120.60 ATOM 1209 O ARG A 151 29.919 58.384 37.922 1.00120.60 ATOM 1210 CB ARG A 151 32.061 56.921 38.631 1.00120.60 ATOM 1211 CG ARG A 151 33.028 55.739 38.667 1.00120.60 ATOM 1212 CD ARG A 151 32.616 54.634 37.696 1.00120.60 ATOM 1213 NE ARG A 151 33.469 53.443 37.957 1.00120.60 ATOM 1214 CZ ARG A 151 33.178 52.274 37.318 1.00120.60 ATOM 1215 NH1 ARG A 151 32.160 52.236 36.410 1.00120.60 ATOM 1216 NH2 ARG A 151 33.896 51.146 37.587 1.00120.60 ATOM 1217 N VAL A 152 30.972 59.578 36.313 1.00130.51 ATOM 1218 CA VAL A 152 29.883 60.473 36.043 1.00130.51 ATOM 1219 C VAL A 152 28.737 59.711 35.451 1.00130.51 ATOM 1220 O VAL A 152 27.579 60.058 35.675 1.00130.51 ATOM 1221 CB VAL A 152 30.223 61.570 35.081 1.00130.51 ATOM 1222 CG1 VAL A 152 31.202 62.554 35.726 1.00130.51 ATOM 1223 CG2 VAL A 152 30.791 60.900 33.832 1.00130.51 ATOM 1224 N ALA A 153 29.022 58.648 34.680 1.00 41.74 ATOM 1225 CA ALA A 153 27.989 57.921 33.992 1.00 41.74 ATOM 1226 C ALA A 153 27.002 57.403 34.992 1.00 41.74 ATOM 1227 O ALA A 153 25.799 57.427 34.738 1.00 41.74 ATOM 1228 CB ALA A 153 28.542 56.711 33.218 1.00 41.74 ATOM 1229 N GLU A 154 27.474 56.924 36.158 1.00 75.47 ATOM 1230 CA GLU A 154 26.552 56.400 37.123 1.00 75.47 ATOM 1231 C GLU A 154 25.616 57.484 37.564 1.00 75.47 ATOM 1232 O GLU A 154 24.427 57.233 37.750 1.00 75.47 ATOM 1233 CB GLU A 154 27.208 55.815 38.389 1.00 75.47 ATOM 1234 CG GLU A 154 27.739 54.387 38.227 1.00 75.47 ATOM 1235 CD GLU A 154 29.170 54.428 37.718 1.00 75.47 ATOM 1236 OE1 GLU A 154 29.389 54.972 36.603 1.00 75.47 ATOM 1237 OE2 GLU A 154 30.065 53.913 38.440 1.00 75.47 ATOM 1238 N GLN A 155 26.122 58.719 37.743 1.00 58.44 ATOM 1239 CA GLN A 155 25.291 59.804 38.192 1.00 58.44 ATOM 1240 C GLN A 155 24.233 60.037 37.166 1.00 58.44 ATOM 1241 O GLN A 155 23.056 60.197 37.488 1.00 58.44 ATOM 1242 CB GLN A 155 26.037 61.146 38.235 1.00 58.44 ATOM 1243 CG GLN A 155 27.255 61.216 39.152 1.00 58.44 ATOM 1244 CD GLN A 155 27.853 62.607 38.956 1.00 58.44 ATOM 1245 OE1 GLN A 155 28.655 63.075 39.760 1.00 58.44 ATOM 1246 NE2 GLN A 155 27.451 63.291 37.850 1.00 58.44 ATOM 1247 N LEU A 156 24.647 60.072 35.889 1.00 53.70 ATOM 1248 CA LEU A 156 23.748 60.353 34.811 1.00 53.70 ATOM 1249 C LEU A 156 22.742 59.256 34.707 1.00 53.70 ATOM 1250 O LEU A 156 21.561 59.515 34.493 1.00 53.70 ATOM 1251 CB LEU A 156 24.471 60.488 33.460 1.00 53.70 ATOM 1252 CG LEU A 156 25.380 61.733 33.384 1.00 53.70 ATOM 1253 CD1 LEU A 156 26.147 61.785 32.054 1.00 53.70 ATOM 1254 CD2 LEU A 156 24.584 63.026 33.641 1.00 53.70 ATOM 1255 N ARG A 157 23.172 57.992 34.869 1.00144.29 ATOM 1256 CA ARG A 157 22.220 56.930 34.734 1.00144.29 ATOM 1257 C ARG A 157 21.202 57.082 35.819 1.00144.29 ATOM 1258 O ARG A 157 20.014 56.861 35.600 1.00144.29 ATOM 1259 CB ARG A 157 22.809 55.505 34.826 1.00144.29 ATOM 1260 CG ARG A 157 23.417 55.126 36.176 1.00144.29 ATOM 1261 CD ARG A 157 23.979 53.699 36.222 1.00144.29 ATOM 1262 NE ARG A 157 22.853 52.739 36.038 1.00144.29 ATOM 1263 CZ ARG A 157 23.027 51.419 36.347 1.00144.29 ATOM 1264 NH1 ARG A 157 24.207 50.989 36.882 1.00144.29 ATOM 1265 NH2 ARG A 157 22.024 50.523 36.116 1.00144.29 ATOM 1266 N ALA A 158 21.645 57.484 37.025 1.00 28.26 ATOM 1267 CA ALA A 158 20.749 57.615 38.137 1.00 28.26 ATOM 1268 C ALA A 158 19.706 58.644 37.814 1.00 28.26 ATOM 1269 O ALA A 158 18.526 58.445 38.098 1.00 28.26 ATOM 1270 CB ALA A 158 21.461 58.075 39.418 1.00 28.26 ATOM 1271 N TYR A 159 20.120 59.778 37.218 1.00 60.42 ATOM 1272 CA TYR A 159 19.219 60.847 36.874 1.00 60.42 ATOM 1273 C TYR A 159 18.250 60.392 35.827 1.00 60.42 ATOM 1274 O TYR A 159 17.039 60.560 35.970 1.00 60.42 ATOM 1275 CB TYR A 159 19.988 62.052 36.296 1.00 60.42 ATOM 1276 CG TYR A 159 19.036 63.018 35.679 1.00 60.42 ATOM 1277 CD1 TYR A 159 18.373 63.950 36.443 1.00 60.42 ATOM 1278 CD2 TYR A 159 18.818 62.997 34.319 1.00 60.42 ATOM 1279 CE1 TYR A 159 17.505 64.843 35.859 1.00 60.42 ATOM 1280 CE2 TYR A 159 17.952 63.885 33.727 1.00 60.42 ATOM 1281 CZ TYR A 159 17.291 64.806 34.502 1.00 60.42 ATOM 1282 OH TYR A 159 16.402 65.719 33.898 1.00 60.42 ATOM 1283 N LEU A 160 18.766 59.774 34.751 1.00 53.01 ATOM 1284 CA LEU A 160 17.932 59.383 33.653 1.00 53.01 ATOM 1285 C LEU A 160 16.982 58.322 34.102 1.00 53.01 ATOM 1286 O LEU A 160 15.824 58.296 33.691 1.00 53.01 ATOM 1287 CB LEU A 160 18.718 58.839 32.443 1.00 53.01 ATOM 1288 CG LEU A 160 19.622 59.877 31.741 1.00 53.01 ATOM 1289 CD1 LEU A 160 20.359 59.243 30.548 1.00 53.01 ATOM 1290 CD2 LEU A 160 18.847 61.146 31.348 1.00 53.01 ATOM 1291 N GLU A 161 17.469 57.372 34.913 1.00 93.01 ATOM 1292 CA GLU A 161 16.607 56.330 35.375 1.00 93.01 ATOM 1293 C GLU A 161 15.627 56.872 36.375 1.00 93.01 ATOM 1294 O GLU A 161 14.436 56.576 36.303 1.00 93.01 ATOM 1295 CB GLU A 161 17.396 55.237 36.118 1.00 93.01 ATOM 1296 CG GLU A 161 18.462 54.535 35.275 1.00 93.01 ATOM 1297 CD GLU A 161 19.318 53.711 36.229 1.00 93.01 ATOM 1298 OE1 GLU A 161 19.552 54.185 37.373 1.00 93.01 ATOM 1299 OE2 GLU A 161 19.747 52.596 35.830 1.00 93.01 ATOM 1300 N GLY A 162 16.123 57.575 37.418 1.00 92.37 ATOM 1301 CA GLY A 162 15.214 58.004 38.448 1.00 92.37 ATOM 1302 C GLY A 162 14.429 59.271 38.247 1.00 92.37 ATOM 1303 O GLY A 162 13.249 59.246 37.899 1.00 92.37 ATOM 1304 N LEU A 163 15.120 60.426 38.374 1.00 69.74 ATOM 1305 CA LEU A 163 14.442 61.695 38.449 1.00 69.74 ATOM 1306 C LEU A 163 13.805 62.049 37.163 1.00 69.74 ATOM 1307 O LEU A 163 12.659 62.492 37.132 1.00 69.74 ATOM 1308 CB LEU A 163 15.350 62.879 38.826 1.00 69.74 ATOM 1309 CG LEU A 163 15.766 62.909 40.306 1.00 69.74 ATOM 1310 CD1 LEU A 163 16.667 64.119 40.604 1.00 69.74 ATOM 1311 CD2 LEU A 163 14.533 62.864 41.222 1.00 69.74 ATOM 1312 N CYS A 164 14.527 61.865 36.050 1.00113.97 ATOM 1313 CA CYS A 164 13.926 62.352 34.856 1.00113.97 ATOM 1314 C CYS A 164 12.686 61.574 34.541 1.00113.97 ATOM 1315 O CYS A 164 11.693 62.152 34.107 1.00113.97 ATOM 1316 CB CYS A 164 14.865 62.460 33.645 1.00113.97 ATOM 1317 SG CYS A 164 15.222 60.907 32.817 1.00113.97 ATOM 1318 N VAL A 165 12.701 60.247 34.757 1.00 41.49 ATOM 1319 CA VAL A 165 11.548 59.429 34.490 1.00 41.49 ATOM 1320 C VAL A 165 10.451 59.806 35.438 1.00 41.49 ATOM 1321 O VAL A 165 9.290 59.922 35.052 1.00 41.49 ATOM 1322 CB VAL A 165 11.820 57.967 34.686 1.00 41.49 ATOM 1323 CG1 VAL A 165 10.516 57.187 34.448 1.00 41.49 ATOM 1324 CG2 VAL A 165 12.976 57.552 33.762 1.00 41.49 ATOM 1325 N GLU A 166 10.813 60.003 36.716 1.00100.57 ATOM 1326 CA GLU A 166 9.895 60.295 37.775 1.00100.57 ATOM 1327 C GLU A 166 9.196 61.588 37.503 1.00100.57 ATOM 1328 O GLU A 166 7.969 61.660 37.546 1.00100.57 ATOM 1329 CB GLU A 166 10.678 60.461 39.086 1.00100.57 ATOM 1330 CG GLU A 166 9.852 60.862 40.300 1.00100.57 ATOM 1331 CD GLU A 166 10.852 61.185 41.402 1.00100.57 ATOM 1332 OE1 GLU A 166 11.636 60.273 41.780 1.00100.57 ATOM 1333 OE2 GLU A 166 10.858 62.355 41.873 1.00100.57 ATOM 1334 N TRP A 167 9.967 62.644 37.201 1.00 67.13 ATOM 1335 CA TRP A 167 9.393 63.933 36.971 1.00 67.13 ATOM 1336 C TRP A 167 8.607 63.917 35.702 1.00 67.13 ATOM 1337 O TRP A 167 7.553 64.543 35.610 1.00 67.13 ATOM 1338 CB TRP A 167 10.436 65.059 36.940 1.00 67.13 ATOM 1339 CG TRP A 167 10.978 65.333 38.323 1.00 67.13 ATOM 1340 CD1 TRP A 167 12.046 64.777 38.966 1.00 67.13 ATOM 1341 CD2 TRP A 167 10.386 66.260 39.247 1.00 67.13 ATOM 1342 NE1 TRP A 167 12.150 65.292 40.237 1.00 67.13 ATOM 1343 CE2 TRP A 167 11.136 66.208 40.421 1.00 67.13 ATOM 1344 CE3 TRP A 167 9.300 67.081 39.129 1.00 67.13 ATOM 1345 CZ2 TRP A 167 10.811 66.981 41.501 1.00 67.13 ATOM 1346 CZ3 TRP A 167 8.980 67.864 40.216 1.00 67.13 ATOM 1347 CH2 TRP A 167 9.721 67.815 41.379 1.00 67.13 ATOM 1348 N LEU A 168 9.093 63.191 34.682 1.00 49.65 ATOM 1349 CA LEU A 168 8.383 63.152 33.438 1.00 49.65 ATOM 1350 C LEU A 168 7.022 62.590 33.689 1.00 49.65 ATOM 1351 O LEU A 168 6.036 63.080 33.142 1.00 49.65 ATOM 1352 CB LEU A 168 9.061 62.279 32.371 1.00 49.65 ATOM 1353 CG LEU A 168 8.206 62.137 31.099 1.00 49.65 ATOM 1354 CD1 LEU A 168 7.889 63.507 30.480 1.00 49.65 ATOM 1355 CD2 LEU A 168 8.857 61.168 30.100 1.00 49.65 ATOM 1356 N ARG A 169 6.933 61.553 34.539 1.00 40.11 ATOM 1357 CA ARG A 169 5.667 60.951 34.830 1.00 40.11 ATOM 1358 C ARG A 169 4.806 61.998 35.467 1.00 40.11 ATOM 1359 O ARG A 169 3.620 62.103 35.156 1.00 40.11 ATOM 1360 CB ARG A 169 5.763 59.775 35.821 1.00 40.11 ATOM 1361 CG ARG A 169 6.618 58.604 35.326 1.00 40.11 ATOM 1362 CD ARG A 169 6.468 57.329 36.165 1.00 40.11 ATOM 1363 NE ARG A 169 6.813 57.666 37.575 1.00 40.11 ATOM 1364 CZ ARG A 169 8.104 57.595 38.017 1.00 40.11 ATOM 1365 NH1 ARG A 169 9.097 57.194 37.171 1.00 40.11 ATOM 1366 NH2 ARG A 169 8.402 57.929 39.307 1.00 40.11 ATOM 1367 N ARG A 170 5.384 62.810 36.374 1.00162.85 ATOM 1368 CA ARG A 170 4.621 63.814 37.060 1.00162.85 ATOM 1369 C ARG A 170 4.083 64.796 36.074 1.00162.85 ATOM 1370 O ARG A 170 2.902 65.141 36.108 1.00162.85 ATOM 1371 CB ARG A 170 5.451 64.684 38.014 1.00162.85 ATOM 1372 CG ARG A 170 5.779 64.053 39.359 1.00162.85 ATOM 1373 CD ARG A 170 6.536 65.014 40.280 1.00162.85 ATOM 1374 NE ARG A 170 5.700 66.241 40.453 1.00162.85 ATOM 1375 CZ ARG A 170 5.689 66.901 41.648 1.00162.85 ATOM 1376 NH1 ARG A 170 6.440 66.437 42.688 1.00162.85 ATOM 1377 NH2 ARG A 170 4.928 68.025 41.803 1.00162.85 ATOM 1378 N TYR A 171 4.944 65.265 35.154 1.00 78.05 ATOM 1379 CA TYR A 171 4.537 66.288 34.244 1.00 78.05 ATOM 1380 C TYR A 171 3.437 65.751 33.388 1.00 78.05 ATOM 1381 O TYR A 171 2.463 66.446 33.106 1.00 78.05 ATOM 1382 CB TYR A 171 5.658 66.790 33.310 1.00 78.05 ATOM 1383 CG TYR A 171 6.763 67.359 34.142 1.00 78.05 ATOM 1384 CD1 TYR A 171 6.515 68.341 35.074 1.00 78.05 ATOM 1385 CD2 TYR A 171 8.062 66.942 33.957 1.00 78.05 ATOM 1386 CE1 TYR A 171 7.531 68.876 35.832 1.00 78.05 ATOM 1387 CE2 TYR A 171 9.085 67.473 34.710 1.00 78.05 ATOM 1388 CZ TYR A 171 8.820 68.435 35.654 1.00 78.05 ATOM 1389 OH TYR A 171 9.866 68.980 36.429 1.00 78.05 ATOM 1390 N LEU A 172 3.556 64.482 32.961 1.00 51.64 ATOM 1391 CA LEU A 172 2.560 63.910 32.104 1.00 51.64 ATOM 1392 C LEU A 172 1.243 63.939 32.811 1.00 51.64 ATOM 1393 O LEU A 172 0.217 64.235 32.202 1.00 51.64 ATOM 1394 CB LEU A 172 2.857 62.450 31.728 1.00 51.64 ATOM 1395 CG LEU A 172 4.017 62.298 30.728 1.00 51.64 ATOM 1396 CD1 LEU A 172 4.269 60.822 30.391 1.00 51.64 ATOM 1397 CD2 LEU A 172 3.764 63.132 29.459 1.00 51.64 ATOM 1398 N GLU A 173 1.226 63.611 34.115 1.00 79.65 ATOM 1399 CA GLU A 173 -0.011 63.605 34.841 1.00 79.65 ATOM 1400 C GLU A 173 -0.566 65.000 34.974 1.00 79.65 ATOM 1401 O GLU A 173 -1.750 65.229 34.731 1.00 79.65 ATOM 1402 CB GLU A 173 0.137 63.021 36.257 1.00 79.65 ATOM 1403 CG GLU A 173 -1.132 63.144 37.107 1.00 79.65 ATOM 1404 CD GLU A 173 -2.220 62.256 36.519 1.00 79.65 ATOM 1405 OE1 GLU A 173 -1.900 61.383 35.669 1.00 79.65 ATOM 1406 OE2 GLU A 173 -3.397 62.444 36.925 1.00 79.65 ATOM 1407 N ASN A 174 0.275 65.983 35.349 1.00 79.13 ATOM 1408 CA ASN A 174 -0.211 67.319 35.582 1.00 79.13 ATOM 1409 C ASN A 174 -0.703 67.908 34.290 1.00 79.13 ATOM 1410 O ASN A 174 -1.712 68.610 34.242 1.00 79.13 ATOM 1411 CB ASN A 174 0.888 68.256 36.116 1.00 79.13 ATOM 1412 CG ASN A 174 1.344 67.754 37.483 1.00 79.13 ATOM 1413 OD1 ASN A 174 2.333 68.231 38.036 1.00 79.13 ATOM 1414 ND2 ASN A 174 0.608 66.754 38.039 1.00 79.13 ATOM 1415 N GLY A 175 0.080 67.664 33.231 1.00 82.48 ATOM 1416 CA GLY A 175 -0.037 68.052 31.854 1.00 82.48 ATOM 1417 C GLY A 175 -1.055 67.271 31.076 1.00 82.48 ATOM 1418 O GLY A 175 -1.302 67.598 29.917 1.00 82.48 ATOM 1419 N LYS A 176 -1.629 66.197 31.654 1.00139.34 ATOM 1420 CA LYS A 176 -2.337 65.182 30.918 1.00139.34 ATOM 1421 C LYS A 176 -3.303 65.728 29.918 1.00139.34 ATOM 1422 O LYS A 176 -3.425 65.146 28.841 1.00139.34 ATOM 1423 CB LYS A 176 -3.116 64.190 31.808 1.00139.34 ATOM 1424 CG LYS A 176 -4.325 64.776 32.543 1.00139.34 ATOM 1425 CD LYS A 176 -5.275 63.704 33.087 1.00139.34 ATOM 1426 CE LYS A 176 -4.643 62.808 34.154 1.00139.34 ATOM 1427 NZ LYS A 176 -5.622 61.802 34.626 1.00139.34 ATOM 1428 N GLU A 177 -4.010 66.834 30.206 1.00 65.06 ATOM 1429 CA GLU A 177 -4.970 67.277 29.236 1.00 65.06 ATOM 1430 C GLU A 177 -4.275 67.569 27.934 1.00 65.06 ATOM 1431 O GLU A 177 -4.726 67.111 26.886 1.00 65.06 ATOM 1432 CB GLU A 177 -5.711 68.555 29.666 1.00 65.06 ATOM 1433 CG GLU A 177 -4.806 69.778 29.818 1.00 65.06 ATOM 1434 CD GLU A 177 -5.687 70.951 30.223 1.00 65.06 ATOM 1435 OE1 GLU A 177 -6.317 71.556 29.316 1.00 65.06 ATOM 1436 OE2 GLU A 177 -5.751 71.251 31.445 1.00 65.06 ATOM 1437 N THR A 178 -3.195 68.379 27.954 1.00 72.14 ATOM 1438 CA THR A 178 -2.445 68.685 26.760 1.00 72.14 ATOM 1439 C THR A 178 -1.431 67.640 26.362 1.00 72.14 ATOM 1440 O THR A 178 -1.388 67.207 25.211 1.00 72.14 ATOM 1441 CB THR A 178 -1.728 70.002 26.853 1.00 72.14 ATOM 1442 OG1 THR A 178 -0.792 69.992 27.923 1.00 72.14 ATOM 1443 CG2 THR A 178 -2.773 71.108 27.068 1.00 72.14 ATOM 1444 N LEU A 179 -0.592 67.184 27.315 1.00 68.60 ATOM 1445 CA LEU A 179 0.522 66.319 27.006 1.00 68.60 ATOM 1446 C LEU A 179 0.039 65.006 26.487 1.00 68.60 ATOM 1447 O LEU A 179 0.643 64.413 25.596 1.00 68.60 ATOM 1448 CB LEU A 179 1.381 66.029 28.249 1.00 68.60 ATOM 1449 CG LEU A 179 2.004 67.294 28.872 1.00 68.60 ATOM 1450 CD1 LEU A 179 2.850 66.950 30.108 1.00 68.60 ATOM 1451 CD2 LEU A 179 2.781 68.112 27.825 1.00 68.60 ATOM 1452 N GLN A 180 -1.028 64.490 27.107 1.00101.67 ATOM 1453 CA GLN A 180 -1.661 63.241 26.811 1.00101.67 ATOM 1454 C GLN A 180 -2.553 63.296 25.609 1.00101.67 ATOM 1455 O GLN A 180 -2.995 62.252 25.139 1.00101.67 ATOM 1456 CB GLN A 180 -2.401 62.650 28.019 1.00101.67 ATOM 1457 CG GLN A 180 -1.395 62.209 29.090 1.00101.67 ATOM 1458 CD GLN A 180 -2.146 61.583 30.252 1.00101.67 ATOM 1459 OE1 GLN A 180 -3.372 61.644 30.325 1.00101.67 ATOM 1460 NE2 GLN A 180 -1.388 60.959 31.194 1.00101.67 ATOM 1461 N ARG A 181 -2.937 64.497 25.142 1.00158.24 ATOM 1462 CA ARG A 181 -3.877 64.604 24.060 1.00158.24 ATOM 1463 C ARG A 181 -3.185 64.832 22.754 1.00158.24 ATOM 1464 O ARG A 181 -2.342 65.718 22.618 1.00158.24 ATOM 1465 CB ARG A 181 -4.843 65.783 24.260 1.00158.24 ATOM 1466 CG ARG A 181 -5.659 66.142 23.021 1.00158.24 ATOM 1467 CD ARG A 181 -6.355 67.501 23.135 1.00158.24 ATOM 1468 NE ARG A 181 -5.367 68.449 23.724 1.00158.24 ATOM 1469 CZ ARG A 181 -5.319 69.756 23.331 1.00158.24 ATOM 1470 NH1 ARG A 181 -6.118 70.203 22.319 1.00158.24 ATOM 1471 NH2 ARG A 181 -4.464 70.618 23.952 1.00158.24 ATOM 1472 N ALA A 182 -3.554 64.020 21.742 1.00 38.21 ATOM 1473 CA ALA A 182 -3.033 64.197 20.423 1.00 38.21 ATOM 1474 C ALA A 182 -4.103 64.916 19.672 1.00 38.21 ATOM 1475 O ALA A 182 -5.284 64.587 19.786 1.00 38.21 ATOM 1476 CB ALA A 182 -2.765 62.874 19.682 1.00 38.21 ATOM 1477 N ASP A 183 -3.710 65.958 18.916 1.00 61.75 ATOM 1478 CA ASP A 183 -4.647 66.694 18.122 1.00 61.75 ATOM 1479 C ASP A 183 -4.379 66.263 16.713 1.00 61.75 ATOM 1480 O ASP A 183 -3.301 66.517 16.181 1.00 61.75 ATOM 1481 CB ASP A 183 -4.408 68.214 18.174 1.00 61.75 ATOM 1482 CG ASP A 183 -4.608 68.675 19.610 1.00 61.75 ATOM 1483 OD1 ASP A 183 -5.345 67.973 20.352 1.00 61.75 ATOM 1484 OD2 ASP A 183 -4.021 69.724 19.989 1.00 61.75 ATOM 1485 N PRO A 184 -5.312 65.598 16.092 1.00 73.67 ATOM 1486 CA PRO A 184 -5.161 65.111 14.749 1.00 73.67 ATOM 1487 C PRO A 184 -4.998 66.260 13.809 1.00 73.67 ATOM 1488 O PRO A 184 -5.456 67.361 14.114 1.00 73.67 ATOM 1489 CB PRO A 184 -6.444 64.331 14.464 1.00 73.67 ATOM 1490 CG PRO A 184 -7.490 65.006 15.372 1.00 73.67 ATOM 1491 CD PRO A 184 -6.672 65.469 16.589 1.00 73.67 ATOM 1492 N PRO A 185 -4.345 66.038 12.703 1.00 82.84 ATOM 1493 CA PRO A 185 -4.161 67.080 11.740 1.00 82.84 ATOM 1494 C PRO A 185 -5.435 67.319 11.006 1.00 82.84 ATOM 1495 O PRO A 185 -6.194 66.375 10.797 1.00 82.84 ATOM 1496 CB PRO A 185 -3.009 66.626 10.839 1.00 82.84 ATOM 1497 CG PRO A 185 -2.884 65.114 11.107 1.00 82.84 ATOM 1498 CD PRO A 185 -3.381 64.963 12.553 1.00 82.84 ATOM 1499 N LYS A 186 -5.700 68.581 10.633 1.00 87.82 ATOM 1500 CA LYS A 186 -6.816 68.845 9.782 1.00 87.82 ATOM 1501 C LYS A 186 -6.183 68.839 8.435 1.00 87.82 ATOM 1502 O LYS A 186 -5.204 69.550 8.214 1.00 87.82 ATOM 1503 CB LYS A 186 -7.467 70.218 10.006 1.00 87.82 ATOM 1504 CG LYS A 186 -8.089 70.362 11.395 1.00 87.82 ATOM 1505 CD LYS A 186 -8.536 71.790 11.710 1.00 87.82 ATOM 1506 CE LYS A 186 -7.462 72.842 11.437 1.00 87.82 ATOM 1507 NZ LYS A 186 -8.025 74.197 11.632 1.00 87.82 ATOM 1508 N THR A 187 -6.698 68.022 7.497 1.00 49.94 ATOM 1509 CA THR A 187 -5.987 67.916 6.257 1.00 49.94 ATOM 1510 C THR A 187 -6.866 68.267 5.101 1.00 49.94 ATOM 1511 O THR A 187 -8.089 68.157 5.158 1.00 49.94 ATOM 1512 CB THR A 187 -5.452 66.536 6.007 1.00 49.94 ATOM 1513 OG1 THR A 187 -6.520 65.599 5.989 1.00 49.94 ATOM 1514 CG2 THR A 187 -4.451 66.177 7.118 1.00 49.94 ATOM 1515 N HIS A 188 -6.226 68.749 4.016 1.00 61.62 ATOM 1516 CA HIS A 188 -6.923 69.040 2.801 1.00 61.62 ATOM 1517 C HIS A 188 -5.900 69.106 1.718 1.00 61.62 ATOM 1518 O HIS A 188 -4.710 69.282 1.983 1.00 61.62 ATOM 1519 CB HIS A 188 -7.696 70.373 2.813 1.00 61.62 ATOM 1520 CG HIS A 188 -6.822 71.586 2.912 1.00 61.62 ATOM 1521 ND1 HIS A 188 -6.350 72.102 4.097 1.00 61.62 ATOM 1522 CD2 HIS A 188 -6.346 72.404 1.933 1.00 61.62 ATOM 1523 CE1 HIS A 188 -5.620 73.202 3.779 1.00 61.62 ATOM 1524 NE2 HIS A 188 -5.590 73.424 2.480 1.00 61.62 ATOM 1525 N VAL A 189 -6.338 68.929 0.456 1.00107.43 ATOM 1526 CA VAL A 189 -5.390 69.016 -0.610 1.00107.43 ATOM 1527 C VAL A 189 -5.794 70.193 -1.432 1.00107.43 ATOM 1528 O VAL A 189 -6.976 70.432 -1.679 1.00107.43 ATOM 1529 CB VAL A 189 -5.335 67.799 -1.490 1.00107.43 ATOM 1530 CG1 VAL A 189 -6.412 67.900 -2.581 1.00107.43 ATOM 1531 CG2 VAL A 189 -3.896 67.636 -1.995 1.00107.43 ATOM 1532 N THR A 190 -4.794 70.978 -1.856 1.00125.68 ATOM 1533 CA THR A 190 -5.011 72.170 -2.611 1.00125.68 ATOM 1534 C THR A 190 -4.395 71.953 -3.955 1.00125.68 ATOM 1535 O THR A 190 -3.458 71.169 -4.095 1.00125.68 ATOM 1536 CB THR A 190 -4.384 73.341 -1.914 1.00125.68 ATOM 1537 OG1 THR A 190 -4.561 74.541 -2.645 1.00125.68 ATOM 1538 CG2 THR A 190 -2.906 73.035 -1.650 1.00125.68 ATOM 1539 N HIS A 191 -4.948 72.619 -4.988 1.00 64.32 ATOM 1540 CA HIS A 191 -4.507 72.432 -6.340 1.00 64.32 ATOM 1541 C HIS A 191 -4.080 73.777 -6.838 1.00 64.32 ATOM 1542 O HIS A 191 -4.808 74.757 -6.684 1.00 64.32 ATOM 1543 CB HIS A 191 -5.668 71.928 -7.221 1.00 64.32 ATOM 1544 CG HIS A 191 -5.294 71.444 -8.589 1.00 64.32 ATOM 1545 ND1 HIS A 191 -5.260 72.234 -9.716 1.00 64.32 ATOM 1546 CD2 HIS A 191 -4.951 70.193 -9.001 1.00 64.32 ATOM 1547 CE1 HIS A 191 -4.902 71.428 -10.747 1.00 64.32 ATOM 1548 NE2 HIS A 191 -4.702 70.180 -10.362 1.00 64.32 ATOM 1549 N HIS A 192 -2.871 73.866 -7.427 1.00 75.31 ATOM 1550 CA HIS A 192 -2.417 75.139 -7.909 1.00 75.31 ATOM 1551 C HIS A 192 -1.832 74.928 -9.270 1.00 75.31 ATOM 1552 O HIS A 192 -0.746 74.365 -9.388 1.00 75.31 ATOM 1553 CB HIS A 192 -1.285 75.726 -7.055 1.00 75.31 ATOM 1554 CG HIS A 192 -1.646 75.817 -5.605 1.00 75.31 ATOM 1555 ND1 HIS A 192 -1.491 74.778 -4.716 1.00 75.31 ATOM 1556 CD2 HIS A 192 -2.159 76.850 -4.882 1.00 75.31 ATOM 1557 CE1 HIS A 192 -1.912 75.229 -3.508 1.00 75.31 ATOM 1558 NE2 HIS A 192 -2.326 76.482 -3.560 1.00 75.31 ATOM 1559 N PRO A 193 -2.496 75.352 -10.312 1.00 90.83 ATOM 1560 CA PRO A 193 -1.888 75.150 -11.598 1.00 90.83 ATOM 1561 C PRO A 193 -0.705 76.033 -11.823 1.00 90.83 ATOM 1562 O PRO A 193 -0.812 77.234 -11.594 1.00 90.83 ATOM 1563 CB PRO A 193 -3.005 75.298 -12.628 1.00 90.83 ATOM 1564 CG PRO A 193 -4.257 74.857 -11.850 1.00 90.83 ATOM 1565 CD PRO A 193 -3.942 75.205 -10.382 1.00 90.83 ATOM 1566 N ILE A 194 0.450 75.439 -12.181 1.00 67.76 ATOM 1567 CA ILE A 194 1.622 76.169 -12.559 1.00 67.76 ATOM 1568 C ILE A 194 1.510 76.613 -13.986 1.00 67.76 ATOM 1569 O ILE A 194 1.797 77.761 -14.324 1.00 67.76 ATOM 1570 CB ILE A 194 2.873 75.363 -12.389 1.00 67.76 ATOM 1571 CG1 ILE A 194 2.891 74.140 -13.319 1.00 67.76 ATOM 1572 CG2 ILE A 194 2.963 75.003 -10.896 1.00 67.76 ATOM 1573 CD1 ILE A 194 4.255 73.453 -13.377 1.00 67.76 ATOM 1574 N SER A 195 1.067 75.684 -14.859 1.00 98.77 ATOM 1575 CA SER A 195 1.012 75.897 -16.276 1.00 98.77 ATOM 1576 C SER A 195 -0.144 75.094 -16.794 1.00 98.77 ATOM 1577 O SER A 195 -0.855 74.442 -16.032 1.00 98.77 ATOM 1578 CB SER A 195 2.295 75.396 -16.961 1.00 98.77 ATOM 1579 OG SER A 195 2.229 75.601 -18.361 1.00 98.77 ATOM 1580 N ASP A 196 -0.375 75.128 -18.119 1.00 86.31 ATOM 1581 CA ASP A 196 -1.495 74.430 -18.674 1.00 86.31 ATOM 1582 C ASP A 196 -1.345 72.961 -18.412 1.00 86.31 ATOM 1583 O ASP A 196 -2.326 72.276 -18.130 1.00 86.31 ATOM 1584 CB ASP A 196 -1.598 74.606 -20.195 1.00 86.31 ATOM 1585 CG ASP A 196 -2.960 74.083 -20.615 1.00 86.31 ATOM 1586 OD1 ASP A 196 -3.819 73.878 -19.715 1.00 86.31 ATOM 1587 OD2 ASP A 196 -3.157 73.874 -21.840 1.00 86.31 ATOM 1588 N HIS A 197 -0.114 72.441 -18.586 1.00 96.39 ATOM 1589 CA HIS A 197 0.243 71.060 -18.406 1.00 96.39 ATOM 1590 C HIS A 197 0.461 70.616 -16.990 1.00 96.39 ATOM 1591 O HIS A 197 0.221 69.450 -16.695 1.00 96.39 ATOM 1592 CB HIS A 197 1.461 70.658 -19.250 1.00 96.39 ATOM 1593 CG HIS A 197 2.466 71.759 -19.375 1.00 96.39 ATOM 1594 ND1 HIS A 197 3.493 72.003 -18.490 1.00 96.39 ATOM 1595 CD2 HIS A 197 2.571 72.716 -20.338 1.00 96.39 ATOM 1596 CE1 HIS A 197 4.163 73.085 -18.960 1.00 96.39 ATOM 1597 NE2 HIS A 197 3.640 73.551 -20.079 1.00 96.39 ATOM 1598 N GLU A 198 0.952 71.470 -16.069 1.00 59.52 ATOM 1599 CA GLU A 198 1.282 70.933 -14.772 1.00 59.52 ATOM 1600 C GLU A 198 0.590 71.696 -13.685 1.00 59.52 ATOM 1601 O GLU A 198 0.184 72.841 -13.868 1.00 59.52 ATOM 1602 CB GLU A 198 2.792 70.977 -14.501 1.00 59.52 ATOM 1603 CG GLU A 198 3.570 70.052 -15.437 1.00 59.52 ATOM 1604 CD GLU A 198 5.054 70.226 -15.162 1.00 59.52 ATOM 1605 OE1 GLU A 198 5.435 71.304 -14.633 1.00 59.52 ATOM 1606 OE2 GLU A 198 5.829 69.288 -15.490 1.00 59.52 ATOM 1607 N ALA A 199 0.420 71.045 -12.510 1.00 34.47 ATOM 1608 CA ALA A 199 -0.218 71.680 -11.393 1.00 34.47 ATOM 1609 C ALA A 199 0.423 71.161 -10.148 1.00 34.47 ATOM 1610 O ALA A 199 1.020 70.085 -10.143 1.00 34.47 ATOM 1611 CB ALA A 199 -1.719 71.362 -11.280 1.00 34.47 ATOM 1612 N THR A 200 0.320 71.930 -9.046 1.00 45.13 ATOM 1613 CA THR A 200 0.891 71.489 -7.814 1.00 45.13 ATOM 1614 C THR A 200 -0.229 71.047 -6.942 1.00 45.13 ATOM 1615 O THR A 200 -1.250 71.723 -6.826 1.00 45.13 ATOM 1616 CB THR A 200 1.624 72.559 -7.060 1.00 45.13 ATOM 1617 OG1 THR A 200 2.701 73.066 -7.835 1.00 45.13 ATOM 1618 CG2 THR A 200 2.143 71.957 -5.743 1.00 45.13 ATOM 1619 N LEU A 201 -0.069 69.851 -6.350 1.00 60.98 ATOM 1620 CA LEU A 201 -1.017 69.364 -5.394 1.00 60.98 ATOM 1621 C LEU A 201 -0.331 69.538 -4.084 1.00 60.98 ATOM 1622 O LEU A 201 0.774 69.032 -3.889 1.00 60.98 ATOM 1623 CB LEU A 201 -1.328 67.862 -5.528 1.00 60.98 ATOM 1624 CG LEU A 201 -2.126 67.475 -6.786 1.00 60.98 ATOM 1625 CD1 LEU A 201 -2.382 65.960 -6.826 1.00 60.98 ATOM 1626 CD2 LEU A 201 -3.429 68.286 -6.893 1.00 60.98 ATOM 1627 N ARG A 202 -0.956 70.285 -3.157 1.00102.76 ATOM 1628 CA ARG A 202 -0.318 70.488 -1.891 1.00102.76 ATOM 1629 C ARG A 202 -1.190 69.853 -0.858 1.00102.76 ATOM 1630 O ARG A 202 -2.379 70.152 -0.758 1.00102.76 ATOM 1631 CB ARG A 202 -0.161 71.978 -1.524 1.00102.76 ATOM 1632 CG ARG A 202 0.925 72.255 -0.480 1.00102.76 ATOM 1633 CD ARG A 202 0.998 73.710 -0.003 1.00102.76 ATOM 1634 NE ARG A 202 0.831 74.605 -1.185 1.00102.76 ATOM 1635 CZ ARG A 202 1.865 74.953 -2.005 1.00102.76 ATOM 1636 NH1 ARG A 202 3.115 74.443 -1.815 1.00102.76 ATOM 1637 NH2 ARG A 202 1.636 75.826 -3.030 1.00102.76 ATOM 1638 N CYS A 203 -0.609 68.943 -0.057 1.00 45.98 ATOM 1639 CA CYS A 203 -1.348 68.257 0.960 1.00 45.98 ATOM 1640 C CYS A 203 -1.052 68.975 2.240 1.00 45.98 ATOM 1641 O CYS A 203 0.109 69.111 2.621 1.00 45.98 ATOM 1642 CB CYS A 203 -0.891 66.790 1.082 1.00 45.98 ATOM 1643 SG CYS A 203 -1.760 65.817 2.342 1.00 45.98 ATOM 1644 N TRP A 204 -2.101 69.450 2.944 1.00 86.17 ATOM 1645 CA TRP A 204 -1.883 70.247 4.123 1.00 86.17 ATOM 1646 C TRP A 204 -2.292 69.495 5.351 1.00 86.17 ATOM 1647 O TRP A 204 -3.280 68.762 5.355 1.00 86.17 ATOM 1648 CB TRP A 204 -2.719 71.540 4.135 1.00 86.17 ATOM 1649 CG TRP A 204 -2.332 72.568 3.099 1.00 86.17 ATOM 1650 CD1 TRP A 204 -2.500 72.538 1.746 1.00 86.17 ATOM 1651 CD2 TRP A 204 -1.726 73.835 3.405 1.00 86.17 ATOM 1652 NE1 TRP A 204 -2.034 73.704 1.188 1.00 86.17 ATOM 1653 CE2 TRP A 204 -1.555 74.510 2.199 1.00 86.17 ATOM 1654 CE3 TRP A 204 -1.350 74.392 4.596 1.00 86.17 ATOM 1655 CZ2 TRP A 204 -1.000 75.759 2.164 1.00 86.17 ATOM 1656 CZ3 TRP A 204 -0.784 75.648 4.558 1.00 86.17 ATOM 1657 CH2 TRP A 204 -0.611 76.317 3.363 1.00 86.17 ATOM 1658 N ALA A 205 -1.493 69.658 6.428 1.00 47.38 ATOM 1659 CA ALA A 205 -1.813 69.126 7.722 1.00 47.38 ATOM 1660 C ALA A 205 -1.699 70.295 8.652 1.00 47.38 ATOM 1661 O ALA A 205 -0.654 70.942 8.721 1.00 47.38 ATOM 1662 CB ALA A 205 -0.822 68.052 8.204 1.00 47.38 ATOM 1663 N LEU A 206 -2.777 70.597 9.403 1.00 62.62 ATOM 1664 CA LEU A 206 -2.751 71.761 10.249 1.00 62.62 ATOM 1665 C LEU A 206 -3.293 71.420 11.602 1.00 62.62 ATOM 1666 O LEU A 206 -4.087 70.494 11.755 1.00 62.62 ATOM 1667 CB LEU A 206 -3.642 72.912 9.739 1.00 62.62 ATOM 1668 CG LEU A 206 -3.193 73.561 8.417 1.00 62.62 ATOM 1669 CD1 LEU A 206 -4.146 74.697 8.002 1.00 62.62 ATOM 1670 CD2 LEU A 206 -1.727 74.021 8.490 1.00 62.62 ATOM 1671 N GLY A 207 -2.835 72.167 12.631 1.00 35.81 ATOM 1672 CA GLY A 207 -3.392 72.097 13.954 1.00 35.81 ATOM 1673 C GLY A 207 -3.138 70.776 14.612 1.00 35.81 ATOM 1674 O GLY A 207 -3.942 70.349 15.439 1.00 35.81 ATOM 1675 N PHE A 208 -2.018 70.097 14.301 1.00 69.42 ATOM 1676 CA PHE A 208 -1.825 68.805 14.900 1.00 69.42 ATOM 1677 C PHE A 208 -0.767 68.858 15.961 1.00 69.42 ATOM 1678 O PHE A 208 0.131 69.696 15.940 1.00 69.42 ATOM 1679 CB PHE A 208 -1.441 67.703 13.891 1.00 69.42 ATOM 1680 CG PHE A 208 -0.142 68.054 13.241 1.00 69.42 ATOM 1681 CD1 PHE A 208 -0.104 68.909 12.163 1.00 69.42 ATOM 1682 CD2 PHE A 208 1.037 67.515 13.702 1.00 69.42 ATOM 1683 CE1 PHE A 208 1.092 69.228 11.562 1.00 69.42 ATOM 1684 CE2 PHE A 208 2.235 67.829 13.107 1.00 69.42 ATOM 1685 CZ PHE A 208 2.264 68.687 12.034 1.00 69.42 ATOM 1686 N TYR A 209 -0.917 67.980 16.974 1.00 95.04 ATOM 1687 CA TYR A 209 0.039 67.831 18.039 1.00 95.04 ATOM 1688 C TYR A 209 0.044 66.363 18.335 1.00 95.04 ATOM 1689 O TYR A 209 -1.041 65.784 18.388 1.00 95.04 ATOM 1690 CB TYR A 209 -0.402 68.586 19.311 1.00 95.04 ATOM 1691 CG TYR A 209 0.652 68.510 20.366 1.00 95.04 ATOM 1692 CD1 TYR A 209 0.725 67.424 21.206 1.00 95.04 ATOM 1693 CD2 TYR A 209 1.562 69.532 20.525 1.00 95.04 ATOM 1694 CE1 TYR A 209 1.694 67.357 22.181 1.00 95.04 ATOM 1695 CE2 TYR A 209 2.534 69.470 21.497 1.00 95.04 ATOM 1696 CZ TYR A 209 2.603 68.378 22.328 1.00 95.04 ATOM 1697 OH TYR A 209 3.597 68.312 23.327 1.00 95.04 ATOM 1698 N PRO A 210 1.142 65.675 18.540 1.00181.61 ATOM 1699 CA PRO A 210 2.483 66.206 18.516 1.00181.61 ATOM 1700 C PRO A 210 2.931 66.487 17.119 1.00181.61 ATOM 1701 O PRO A 210 2.172 66.268 16.178 1.00181.61 ATOM 1702 CB PRO A 210 3.367 65.153 19.176 1.00181.61 ATOM 1703 CG PRO A 210 2.409 64.367 20.077 1.00181.61 ATOM 1704 CD PRO A 210 1.053 64.484 19.370 1.00181.61 ATOM 1705 N ALA A 211 4.172 66.990 16.977 1.00 49.60 ATOM 1706 CA ALA A 211 4.759 67.373 15.726 1.00 49.60 ATOM 1707 C ALA A 211 4.925 66.208 14.798 1.00 49.60 ATOM 1708 O ALA A 211 4.754 66.361 13.589 1.00 49.60 ATOM 1709 CB ALA A 211 6.153 68.007 15.891 1.00 49.60 ATOM 1710 N GLU A 212 5.278 65.020 15.325 1.00 91.93 ATOM 1711 CA GLU A 212 5.574 63.910 14.463 1.00 91.93 ATOM 1712 C GLU A 212 4.412 63.638 13.567 1.00 91.93 ATOM 1713 O GLU A 212 3.286 63.419 14.014 1.00 91.93 ATOM 1714 CB GLU A 212 5.915 62.625 15.242 1.00 91.93 ATOM 1715 CG GLU A 212 6.527 61.511 14.388 1.00 91.93 ATOM 1716 CD GLU A 212 5.407 60.776 13.667 1.00 91.93 ATOM 1717 OE1 GLU A 212 4.459 60.314 14.354 1.00 91.93 ATOM 1718 OE2 GLU A 212 5.486 60.668 12.414 1.00 91.93 ATOM 1719 N ILE A 213 4.672 63.676 12.246 1.00 62.04 ATOM 1720 CA ILE A 213 3.638 63.423 11.291 1.00 62.04 ATOM 1721 C ILE A 213 4.303 62.910 10.059 1.00 62.04 ATOM 1722 O ILE A 213 5.471 63.200 9.807 1.00 62.04 ATOM 1723 CB ILE A 213 2.878 64.670 10.934 1.00 62.04 ATOM 1724 CG1 ILE A 213 1.594 64.343 10.158 1.00 62.04 ATOM 1725 CG2 ILE A 213 3.840 65.611 10.190 1.00 62.04 ATOM 1726 CD1 ILE A 213 0.624 65.522 10.087 1.00 62.04 ATOM 1727 N THR A 214 3.577 62.097 9.272 1.00 55.32 ATOM 1728 CA THR A 214 4.127 61.618 8.046 1.00 55.32 ATOM 1729 C THR A 214 3.170 62.018 6.972 1.00 55.32 ATOM 1730 O THR A 214 2.011 61.607 6.987 1.00 55.32 ATOM 1731 CB THR A 214 4.237 60.123 8.003 1.00 55.32 ATOM 1732 OG1 THR A 214 5.071 59.669 9.059 1.00 55.32 ATOM 1733 CG2 THR A 214 4.813 59.697 6.641 1.00 55.32 ATOM 1734 N LEU A 215 3.636 62.867 6.035 1.00112.78 ATOM 1735 CA LEU A 215 2.859 63.273 4.902 1.00112.78 ATOM 1736 C LEU A 215 3.591 62.711 3.736 1.00112.78 ATOM 1737 O LEU A 215 4.774 62.993 3.549 1.00112.78 ATOM 1738 CB LEU A 215 2.845 64.799 4.670 1.00112.78 ATOM 1739 CG LEU A 215 1.976 65.635 5.631 1.00112.78 ATOM 1740 CD1 LEU A 215 0.497 65.587 5.232 1.00112.78 ATOM 1741 CD2 LEU A 215 2.186 65.217 7.090 1.00112.78 ATOM 1742 N THR A 216 2.921 61.878 2.927 1.00 46.01 ATOM 1743 CA THR A 216 3.608 61.334 1.803 1.00 46.01 ATOM 1744 C THR A 216 2.681 61.410 0.641 1.00 46.01 ATOM 1745 O THR A 216 1.464 61.323 0.800 1.00 46.01 ATOM 1746 CB THR A 216 4.011 59.893 1.986 1.00 46.01 ATOM 1747 OG1 THR A 216 2.866 59.077 2.180 1.00 46.01 ATOM 1748 CG2 THR A 216 4.948 59.793 3.205 1.00 46.01 ATOM 1749 N TRP A 217 3.241 61.630 -0.562 1.00 73.52 ATOM 1750 CA TRP A 217 2.421 61.594 -1.730 1.00 73.52 ATOM 1751 C TRP A 217 2.800 60.361 -2.469 1.00 73.52 ATOM 1752 O TRP A 217 3.975 60.018 -2.593 1.00 73.52 ATOM 1753 CB TRP A 217 2.596 62.773 -2.707 1.00 73.52 ATOM 1754 CG TRP A 217 1.890 64.055 -2.327 1.00 73.52 ATOM 1755 CD1 TRP A 217 2.344 65.142 -1.642 1.00 73.52 ATOM 1756 CD2 TRP A 217 0.529 64.335 -2.684 1.00 73.52 ATOM 1757 NE1 TRP A 217 1.350 66.090 -1.560 1.00 73.52 ATOM 1758 CE2 TRP A 217 0.226 65.602 -2.194 1.00 73.52 ATOM 1759 CE3 TRP A 217 -0.394 63.593 -3.366 1.00 73.52 ATOM 1760 CZ2 TRP A 217 -1.013 66.151 -2.377 1.00 73.52 ATOM 1761 CZ3 TRP A 217 -1.641 64.147 -3.550 1.00 73.52 ATOM 1762 CH2 TRP A 217 -1.945 65.403 -3.065 1.00 73.52 ATOM 1763 N GLN A 218 1.781 59.638 -2.954 1.00 52.67 ATOM 1764 CA GLN A 218 2.026 58.442 -3.690 1.00 52.67 ATOM 1765 C GLN A 218 1.491 58.678 -5.057 1.00 52.67 ATOM 1766 O GLN A 218 0.509 59.396 -5.245 1.00 52.67 ATOM 1767 CB GLN A 218 1.299 57.212 -3.123 1.00 52.67 ATOM 1768 CG GLN A 218 1.781 56.805 -1.731 1.00 52.67 ATOM 1769 CD GLN A 218 0.970 55.594 -1.301 1.00 52.67 ATOM 1770 OE1 GLN A 218 -0.093 55.318 -1.854 1.00 52.67 ATOM 1771 NE2 GLN A 218 1.480 54.853 -0.281 1.00 52.67 ATOM 1772 N ARG A 219 2.188 58.112 -6.053 1.00119.23 ATOM 1773 CA ARG A 219 1.768 58.145 -7.417 1.00119.23 ATOM 1774 C ARG A 219 1.599 56.702 -7.752 1.00119.23 ATOM 1775 O ARG A 219 2.554 55.932 -7.667 1.00119.23 ATOM 1776 CB ARG A 219 2.854 58.755 -8.325 1.00119.23 ATOM 1777 CG ARG A 219 2.619 58.678 -9.835 1.00119.23 ATOM 1778 CD ARG A 219 3.648 59.504 -10.617 1.00119.23 ATOM 1779 NE ARG A 219 3.566 59.122 -12.054 1.00119.23 ATOM 1780 CZ ARG A 219 3.541 60.085 -13.023 1.00119.23 ATOM 1781 NH1 ARG A 219 3.471 61.405 -12.688 1.00119.23 ATOM 1782 NH2 ARG A 219 3.583 59.733 -14.340 1.00119.23 ATOM 1783 N ASP A 220 0.363 56.303 -8.107 1.00137.98 ATOM 1784 CA ASP A 220 0.022 54.940 -8.404 1.00137.98 ATOM 1785 C ASP A 220 0.603 54.030 -7.369 1.00137.98 ATOM 1786 O ASP A 220 1.186 52.992 -7.680 1.00137.98 ATOM 1787 CB ASP A 220 0.283 54.465 -9.856 1.00137.98 ATOM 1788 CG ASP A 220 1.738 54.587 -10.284 1.00137.98 ATOM 1789 OD1 ASP A 220 2.297 55.712 -10.206 1.00137.98 ATOM 1790 OD2 ASP A 220 2.307 53.551 -10.720 1.00137.98 ATOM 1791 N GLY A 221 0.454 54.436 -6.091 1.00 27.10 ATOM 1792 CA GLY A 221 0.823 53.639 -4.957 1.00 27.10 ATOM 1793 C GLY A 221 2.308 53.633 -4.747 1.00 27.10 ATOM 1794 O GLY A 221 2.809 52.838 -3.952 1.00 27.10 ATOM 1795 N GLU A 222 3.061 54.511 -5.435 1.00 38.39 ATOM 1796 CA GLU A 222 4.486 54.518 -5.252 1.00 38.39 ATOM 1797 C GLU A 222 4.844 55.786 -4.542 1.00 38.39 ATOM 1798 O GLU A 222 4.366 56.858 -4.905 1.00 38.39 ATOM 1799 CB GLU A 222 5.259 54.503 -6.585 1.00 38.39 ATOM 1800 CG GLU A 222 6.783 54.510 -6.459 1.00 38.39 ATOM 1801 CD GLU A 222 7.335 54.480 -7.879 1.00 38.39 ATOM 1802 OE1 GLU A 222 6.537 54.189 -8.811 1.00 38.39 ATOM 1803 OE2 GLU A 222 8.554 54.749 -8.056 1.00 38.39 ATOM 1804 N ASP A 223 5.697 55.694 -3.500 1.00 72.08 ATOM 1805 CA ASP A 223 6.068 56.869 -2.767 1.00 72.08 ATOM 1806 C ASP A 223 6.874 57.765 -3.656 1.00 72.08 ATOM 1807 O ASP A 223 7.763 57.348 -4.397 1.00 72.08 ATOM 1808 CB ASP A 223 6.866 56.589 -1.478 1.00 72.08 ATOM 1809 CG ASP A 223 5.893 56.037 -0.441 1.00 72.08 ATOM 1810 OD1 ASP A 223 4.666 56.279 -0.590 1.00 72.08 ATOM 1811 OD2 ASP A 223 6.365 55.366 0.515 1.00 72.08 ATOM 1812 N GLN A 224 6.490 59.045 -3.597 1.00139.12 ATOM 1813 CA GLN A 224 6.918 60.233 -4.266 1.00139.12 ATOM 1814 C GLN A 224 8.146 60.860 -3.690 1.00139.12 ATOM 1815 O GLN A 224 8.454 61.986 -4.077 1.00139.12 ATOM 1816 CB GLN A 224 5.813 61.294 -4.343 1.00139.12 ATOM 1817 CG GLN A 224 4.669 60.803 -5.224 1.00139.12 ATOM 1818 CD GLN A 224 5.322 60.316 -6.507 1.00139.12 ATOM 1819 OE1 GLN A 224 5.915 61.093 -7.254 1.00139.12 ATOM 1820 NE2 GLN A 224 5.240 58.982 -6.755 1.00139.12 ATOM 1821 N THR A 225 8.817 60.217 -2.714 1.00 75.17 ATOM 1822 CA THR A 225 9.825 60.829 -1.882 1.00 75.17 ATOM 1823 C THR A 225 10.754 61.739 -2.639 1.00 75.17 ATOM 1824 O THR A 225 10.937 62.883 -2.228 1.00 75.17 ATOM 1825 CB THR A 225 10.679 59.812 -1.184 1.00 75.17 ATOM 1826 OG1 THR A 225 9.873 58.974 -0.369 1.00 75.17 ATOM 1827 CG2 THR A 225 11.720 60.548 -0.324 1.00 75.17 ATOM 1828 N GLN A 226 11.343 61.311 -3.766 1.00121.38 ATOM 1829 CA GLN A 226 12.262 62.185 -4.446 1.00121.38 ATOM 1830 C GLN A 226 11.548 63.427 -4.920 1.00121.38 ATOM 1831 O GLN A 226 12.072 64.535 -4.820 1.00121.38 ATOM 1832 CB GLN A 226 12.865 61.513 -5.692 1.00121.38 ATOM 1833 CG GLN A 226 14.031 62.275 -6.323 1.00121.38 ATOM 1834 CD GLN A 226 15.316 61.794 -5.665 1.00121.38 ATOM 1835 OE1 GLN A 226 15.505 60.597 -5.451 1.00121.38 ATOM 1836 NE2 GLN A 226 16.227 62.748 -5.338 1.00121.38 ATOM 1837 N ASP A 227 10.332 63.244 -5.468 1.00 85.87 ATOM 1838 CA ASP A 227 9.481 64.220 -6.107 1.00 85.87 ATOM 1839 C ASP A 227 8.764 65.162 -5.172 1.00 85.87 ATOM 1840 O ASP A 227 8.222 66.169 -5.625 1.00 85.87 ATOM 1841 CB ASP A 227 8.410 63.549 -6.977 1.00 85.87 ATOM 1842 CG ASP A 227 9.131 62.777 -8.075 1.00 85.87 ATOM 1843 OD1 ASP A 227 10.057 63.353 -8.706 1.00 85.87 ATOM 1844 OD2 ASP A 227 8.774 61.588 -8.280 1.00 85.87 ATOM 1845 N THR A 228 8.662 64.862 -3.864 1.00 53.99 ATOM 1846 CA THR A 228 7.810 65.686 -3.048 1.00 53.99 ATOM 1847 C THR A 228 8.569 66.767 -2.347 1.00 53.99 ATOM 1848 O THR A 228 9.669 66.557 -1.838 1.00 53.99 ATOM 1849 CB THR A 228 7.112 64.895 -1.985 1.00 53.99 ATOM 1850 OG1 THR A 228 6.349 63.853 -2.577 1.00 53.99 ATOM 1851 CG2 THR A 228 6.195 65.832 -1.182 1.00 53.99 ATOM 1852 N GLU A 229 7.977 67.982 -2.321 1.00 53.32 ATOM 1853 CA GLU A 229 8.560 69.053 -1.572 1.00 53.32 ATOM 1854 C GLU A 229 7.877 69.016 -0.249 1.00 53.32 ATOM 1855 O GLU A 229 6.657 69.164 -0.157 1.00 53.32 ATOM 1856 CB GLU A 229 8.340 70.461 -2.156 1.00 53.32 ATOM 1857 CG GLU A 229 9.010 71.551 -1.310 1.00 53.32 ATOM 1858 CD GLU A 229 8.537 72.919 -1.783 1.00 53.32 ATOM 1859 OE1 GLU A 229 8.042 73.009 -2.937 1.00 53.32 ATOM 1860 OE2 GLU A 229 8.659 73.892 -0.990 1.00 53.32 ATOM 1861 N LEU A 230 8.661 68.791 0.820 1.00 57.25 ATOM 1862 CA LEU A 230 8.105 68.676 2.131 1.00 57.25 ATOM 1863 C LEU A 230 8.670 69.794 2.950 1.00 57.25 ATOM 1864 O LEU A 230 9.878 69.880 3.157 1.00 57.25 ATOM 1865 CB LEU A 230 8.510 67.345 2.796 1.00 57.25 ATOM 1866 CG LEU A 230 7.943 67.127 4.211 1.00 57.25 ATOM 1867 CD1 LEU A 230 6.416 66.954 4.176 1.00 57.25 ATOM 1868 CD2 LEU A 230 8.659 65.974 4.934 1.00 57.25 ATOM 1869 N VAL A 231 7.793 70.691 3.433 1.00111.66 ATOM 1870 CA VAL A 231 8.194 71.798 4.252 1.00111.66 ATOM 1871 C VAL A 231 8.413 71.264 5.635 1.00111.66 ATOM 1872 O VAL A 231 7.754 70.312 6.047 1.00111.66 ATOM 1873 CB VAL A 231 7.126 72.855 4.285 1.00111.66 ATOM 1874 CG1 VAL A 231 5.826 72.203 4.776 1.00111.66 ATOM 1875 CG2 VAL A 231 7.575 74.035 5.151 1.00111.66 ATOM 1876 N GLU A 232 9.371 71.846 6.391 1.00 39.30 ATOM 1877 CA GLU A 232 9.610 71.349 7.716 1.00 39.30 ATOM 1878 C GLU A 232 8.388 71.626 8.522 1.00 39.30 ATOM 1879 O GLU A 232 7.703 72.627 8.316 1.00 39.30 ATOM 1880 CB GLU A 232 10.785 72.006 8.468 1.00 39.30 ATOM 1881 CG GLU A 232 10.984 71.405 9.867 1.00 39.30 ATOM 1882 CD GLU A 232 12.036 72.208 10.622 1.00 39.30 ATOM 1883 OE1 GLU A 232 13.082 72.543 10.004 1.00 39.30 ATOM 1884 OE2 GLU A 232 11.807 72.502 11.826 1.00 39.30 ATOM 1885 N THR A 233 8.080 70.718 9.466 1.00 40.53 ATOM 1886 CA THR A 233 6.936 70.922 10.299 1.00 40.53 ATOM 1887 C THR A 233 7.197 72.205 11.012 1.00 40.53 ATOM 1888 O THR A 233 8.317 72.451 11.457 1.00 40.53 ATOM 1889 CB THR A 233 6.763 69.848 11.338 1.00 40.53 ATOM 1890 OG1 THR A 233 6.643 68.577 10.716 1.00 40.53 ATOM 1891 CG2 THR A 233 5.503 70.148 12.167 1.00 40.53 ATOM 1892 N ARG A 234 6.174 73.075 11.124 1.00 50.53 ATOM 1893 CA ARG A 234 6.414 74.343 11.751 1.00 50.53 ATOM 1894 C ARG A 234 5.359 74.584 12.781 1.00 50.53 ATOM 1895 O ARG A 234 4.213 74.160 12.641 1.00 50.53 ATOM 1896 CB ARG A 234 6.367 75.524 10.771 1.00 50.53 ATOM 1897 CG ARG A 234 5.025 75.682 10.057 1.00 50.53 ATOM 1898 CD ARG A 234 4.998 76.899 9.132 1.00 50.53 ATOM 1899 NE ARG A 234 3.657 76.973 8.485 1.00 50.53 ATOM 1900 CZ ARG A 234 3.457 76.470 7.232 1.00 50.53 ATOM 1901 NH1 ARG A 234 4.465 75.837 6.568 1.00 50.53 ATOM 1902 NH2 ARG A 234 2.239 76.601 6.631 1.00 50.53 ATOM 1903 N PRO A 235 5.754 75.237 13.843 1.00 83.27 ATOM 1904 CA PRO A 235 4.820 75.542 14.893 1.00 83.27 ATOM 1905 C PRO A 235 3.903 76.676 14.575 1.00 83.27 ATOM 1906 O PRO A 235 4.361 77.701 14.071 1.00 83.27 ATOM 1907 CB PRO A 235 5.646 75.739 16.166 1.00 83.27 ATOM 1908 CG PRO A 235 7.097 75.873 15.670 1.00 83.27 ATOM 1909 CD PRO A 235 7.105 75.086 14.352 1.00 83.27 ATOM 1910 N ALA A 236 2.596 76.495 14.853 1.00 45.50 ATOM 1911 CA ALA A 236 1.592 77.506 14.671 1.00 45.50 ATOM 1912 C ALA A 236 1.765 78.580 15.706 1.00 45.50 ATOM 1913 O ALA A 236 1.571 79.759 15.418 1.00 45.50 ATOM 1914 CB ALA A 236 0.158 76.959 14.769 1.00 45.50 ATOM 1915 N GLY A 237 2.143 78.192 16.947 1.00 36.94 ATOM 1916 CA GLY A 237 2.271 79.126 18.038 1.00 36.94 ATOM 1917 C GLY A 237 1.226 78.792 19.066 1.00 36.94 ATOM 1918 O GLY A 237 1.346 79.163 20.235 1.00 36.94 ATOM 1919 N ASP A 238 0.156 78.112 18.620 1.00109.04 ATOM 1920 CA ASP A 238 -0.942 77.624 19.412 1.00109.04 ATOM 1921 C ASP A 238 -0.578 76.334 20.101 1.00109.04 ATOM 1922 O ASP A 238 -1.415 75.770 20.799 1.00109.04 ATOM 1923 CB ASP A 238 -2.276 77.513 18.640 1.00109.04 ATOM 1924 CG ASP A 238 -2.081 76.617 17.439 1.00109.04 ATOM 1925 OD1 ASP A 238 -0.951 76.083 17.291 1.00109.04 ATOM 1926 OD2 ASP A 238 -3.048 76.471 16.645 1.00109.04 ATOM 1927 N ARG A 239 0.666 75.838 19.902 1.00170.66 ATOM 1928 CA ARG A 239 1.263 74.610 20.383 1.00170.66 ATOM 1929 C ARG A 239 1.057 73.550 19.346 1.00170.66 ATOM 1930 O ARG A 239 1.648 72.475 19.443 1.00170.66 ATOM 1931 CB ARG A 239 0.646 73.985 21.655 1.00170.66 ATOM 1932 CG ARG A 239 -0.665 73.224 21.419 1.00170.66 ATOM 1933 CD ARG A 239 -1.333 72.717 22.698 1.00170.66 ATOM 1934 NE ARG A 239 -2.147 71.522 22.343 1.00170.66 ATOM 1935 CZ ARG A 239 -1.630 70.285 22.592 1.00170.66 ATOM 1936 NH1 ARG A 239 -0.427 70.176 23.227 1.00170.66 ATOM 1937 NH2 ARG A 239 -2.324 69.164 22.236 1.00170.66 ATOM 1938 N THR A 240 0.266 73.830 18.289 1.00 49.10 ATOM 1939 CA THR A 240 0.089 72.834 17.270 1.00 49.10 ATOM 1940 C THR A 240 1.102 73.075 16.197 1.00 49.10 ATOM 1941 O THR A 240 1.849 74.054 16.232 1.00 49.10 ATOM 1942 CB THR A 240 -1.269 72.814 16.624 1.00 49.10 ATOM 1943 OG1 THR A 240 -1.487 74.000 15.877 1.00 49.10 ATOM 1944 CG2 THR A 240 -2.335 72.668 17.725 1.00 49.10 ATOM 1945 N PHE A 241 1.148 72.161 15.207 1.00 52.95 ATOM 1946 CA PHE A 241 2.111 72.252 14.152 1.00 52.95 ATOM 1947 C PHE A 241 1.395 72.221 12.842 1.00 52.95 ATOM 1948 O PHE A 241 0.217 71.874 12.763 1.00 52.95 ATOM 1949 CB PHE A 241 3.114 71.086 14.163 1.00 52.95 ATOM 1950 CG PHE A 241 3.873 71.208 15.438 1.00 52.95 ATOM 1951 CD1 PHE A 241 3.364 70.693 16.608 1.00 52.95 ATOM 1952 CD2 PHE A 241 5.090 71.847 15.464 1.00 52.95 ATOM 1953 CE1 PHE A 241 4.062 70.808 17.786 1.00 52.95 ATOM 1954 CE2 PHE A 241 5.792 71.966 16.640 1.00 52.95 ATOM 1955 CZ PHE A 241 5.278 71.447 17.804 1.00 52.95 ATOM 1956 N GLN A 242 2.107 72.634 11.776 1.00 47.83 ATOM 1957 CA GLN A 242 1.552 72.642 10.455 1.00 47.83 ATOM 1958 C GLN A 242 2.585 72.050 9.557 1.00 47.83 ATOM 1959 O GLN A 242 3.781 72.137 9.829 1.00 47.83 ATOM 1960 CB GLN A 242 1.273 74.061 9.933 1.00 47.83 ATOM 1961 CG GLN A 242 0.276 74.831 10.800 1.00 47.83 ATOM 1962 CD GLN A 242 0.163 76.240 10.239 1.00 47.83 ATOM 1963 OE1 GLN A 242 0.550 76.501 9.101 1.00 47.83 ATOM 1964 NE2 GLN A 242 -0.380 77.179 11.061 1.00 47.83 ATOM 1965 N LYS A 243 2.143 71.395 8.469 1.00 71.21 ATOM 1966 CA LYS A 243 3.093 70.834 7.560 1.00 71.21 ATOM 1967 C LYS A 243 2.388 70.659 6.260 1.00 71.21 ATOM 1968 O LYS A 243 1.168 70.502 6.221 1.00 71.21 ATOM 1969 CB LYS A 243 3.577 69.446 8.007 1.00 71.21 ATOM 1970 CG LYS A 243 4.813 68.927 7.274 1.00 71.21 ATOM 1971 CD LYS A 243 5.439 67.735 7.999 1.00 71.21 ATOM 1972 CE LYS A 243 6.808 67.309 7.474 1.00 71.21 ATOM 1973 NZ LYS A 243 7.437 66.385 8.444 1.00 71.21 ATOM 1974 N TRP A 244 3.134 70.731 5.144 1.00112.71 ATOM 1975 CA TRP A 244 2.512 70.449 3.890 1.00112.71 ATOM 1976 C TRP A 244 3.511 69.765 3.018 1.00112.71 ATOM 1977 O TRP A 244 4.720 69.917 3.192 1.00112.71 ATOM 1978 CB TRP A 244 1.884 71.669 3.174 1.00112.71 ATOM 1979 CG TRP A 244 2.733 72.905 2.977 1.00112.71 ATOM 1980 CD1 TRP A 244 2.744 74.073 3.686 1.00112.71 ATOM 1981 CD2 TRP A 244 3.695 73.058 1.925 1.00112.71 ATOM 1982 NE1 TRP A 244 3.641 74.953 3.126 1.00112.71 ATOM 1983 CE2 TRP A 244 4.235 74.336 2.043 1.00112.71 ATOM 1984 CE3 TRP A 244 4.090 72.203 0.935 1.00112.71 ATOM 1985 CZ2 TRP A 244 5.182 74.782 1.166 1.00112.71 ATOM 1986 CZ3 TRP A 244 5.050 72.651 0.056 1.00112.71 ATOM 1987 CH2 TRP A 244 5.583 73.918 0.171 1.00112.71 ATOM 1988 N ALA A 245 3.000 68.929 2.091 1.00 36.92 ATOM 1989 CA ALA A 245 3.817 68.226 1.150 1.00 36.92 ATOM 1990 C ALA A 245 3.237 68.543 -0.186 1.00 36.92 ATOM 1991 O ALA A 245 2.018 68.562 -0.346 1.00 36.92 ATOM 1992 CB ALA A 245 3.776 66.698 1.325 1.00 36.92 ATOM 1993 N ALA A 246 4.092 68.805 -1.193 1.00 37.41 ATOM 1994 CA ALA A 246 3.542 69.181 -2.461 1.00 37.41 ATOM 1995 C ALA A 246 4.210 68.391 -3.536 1.00 37.41 ATOM 1996 O ALA A 246 5.375 68.013 -3.423 1.00 37.41 ATOM 1997 CB ALA A 246 3.757 70.668 -2.791 1.00 37.41 ATOM 1998 N VAL A 247 3.448 68.097 -4.606 1.00 43.72 ATOM 1999 CA VAL A 247 3.984 67.409 -5.741 1.00 43.72 ATOM 2000 C VAL A 247 3.518 68.129 -6.963 1.00 43.72 ATOM 2001 O VAL A 247 2.443 68.727 -6.979 1.00 43.72 ATOM 2002 CB VAL A 247 3.524 65.984 -5.868 1.00 43.72 ATOM 2003 CG1 VAL A 247 4.127 65.176 -4.709 1.00 43.72 ATOM 2004 CG2 VAL A 247 1.986 65.955 -5.894 1.00 43.72 ATOM 2005 N VAL A 248 4.346 68.106 -8.024 1.00 44.91 ATOM 2006 CA VAL A 248 3.956 68.708 -9.263 1.00 44.91 ATOM 2007 C VAL A 248 3.451 67.575 -10.092 1.00 44.91 ATOM 2008 O VAL A 248 4.158 66.590 -10.301 1.00 44.91 ATOM 2009 CB VAL A 248 5.099 69.344 -9.999 1.00 44.91 ATOM 2010 CG1 VAL A 248 4.608 69.820 -11.378 1.00 44.91 ATOM 2011 CG2 VAL A 248 5.674 70.463 -9.113 1.00 44.91 ATOM 2012 N VAL A 249 2.202 67.683 -10.584 1.00 53.21 ATOM 2013 CA VAL A 249 1.634 66.576 -11.295 1.00 53.21 ATOM 2014 C VAL A 249 1.205 67.023 -12.659 1.00 53.21 ATOM 2015 O VAL A 249 0.934 68.201 -12.898 1.00 53.21 ATOM 2016 CB VAL A 249 0.429 65.998 -10.603 1.00 53.21 ATOM 2017 CG1 VAL A 249 0.867 65.505 -9.213 1.00 53.21 ATOM 2018 CG2 VAL A 249 -0.686 67.056 -10.557 1.00 53.21 ATOM 2019 N PRO A 250 1.169 66.085 -13.573 1.00 71.29 ATOM 2020 CA PRO A 250 0.717 66.397 -14.902 1.00 71.29 ATOM 2021 C PRO A 250 -0.752 66.653 -14.846 1.00 71.29 ATOM 2022 O PRO A 250 -1.437 66.027 -14.040 1.00 71.29 ATOM 2023 CB PRO A 250 1.101 65.200 -15.767 1.00 71.29 ATOM 2024 CG PRO A 250 2.341 64.628 -15.054 1.00 71.29 ATOM 2025 CD PRO A 250 2.145 65.007 -13.574 1.00 71.29 ATOM 2026 N SER A 251 -1.263 67.555 -15.698 1.00 78.90 ATOM 2027 CA SER A 251 -2.650 67.899 -15.659 1.00 78.90 ATOM 2028 C SER A 251 -3.451 66.692 -16.038 1.00 78.90 ATOM 2029 O SER A 251 -3.147 66.017 -17.019 1.00 78.90 ATOM 2030 CB SER A 251 -3.013 69.040 -16.623 1.00 78.90 ATOM 2031 OG SER A 251 -4.398 69.332 -16.536 1.00 78.90 ATOM 2032 N GLY A 252 -4.501 66.391 -15.243 1.00 36.52 ATOM 2033 CA GLY A 252 -5.397 65.304 -15.526 1.00 36.52 ATOM 2034 C GLY A 252 -4.963 64.068 -14.787 1.00 36.52 ATOM 2035 O GLY A 252 -5.734 63.122 -14.643 1.00 36.52 ATOM 2036 N GLU A 253 -3.695 64.052 -14.339 1.00121.75 ATOM 2037 CA GLU A 253 -3.013 63.007 -13.620 1.00121.75 ATOM 2038 C GLU A 253 -3.391 62.981 -12.162 1.00121.75 ATOM 2039 O GLU A 253 -3.071 62.026 -11.459 1.00121.75 ATOM 2040 CB GLU A 253 -1.483 63.157 -13.680 1.00121.75 ATOM 2041 CG GLU A 253 -0.902 62.987 -15.084 1.00121.75 ATOM 2042 CD GLU A 253 -0.540 61.526 -15.290 1.00121.75 ATOM 2043 OE1 GLU A 253 0.340 61.023 -14.542 1.00121.75 ATOM 2044 OE2 GLU A 253 -1.136 60.898 -16.203 1.00121.75 ATOM 2045 N GLU A 254 -4.065 64.031 -11.655 1.00117.23 ATOM 2046 CA GLU A 254 -4.237 64.242 -10.239 1.00117.23 ATOM 2047 C GLU A 254 -4.763 63.036 -9.512 1.00117.23 ATOM 2048 O GLU A 254 -4.372 62.801 -8.370 1.00117.23 ATOM 2049 CB GLU A 254 -5.170 65.424 -9.917 1.00117.23 ATOM 2050 CG GLU A 254 -4.522 66.799 -10.116 1.00117.23 ATOM 2051 CD GLU A 254 -4.531 67.175 -11.592 1.00117.23 ATOM 2052 OE1 GLU A 254 -3.790 66.533 -12.383 1.00117.23 ATOM 2053 OE2 GLU A 254 -5.279 68.125 -11.945 1.00117.23 ATOM 2054 N GLN A 255 -5.650 62.238 -10.123 1.00 74.30 ATOM 2055 CA GLN A 255 -6.239 61.113 -9.446 1.00 74.30 ATOM 2056 C GLN A 255 -5.213 60.075 -9.087 1.00 74.30 ATOM 2057 O GLN A 255 -5.417 59.306 -8.150 1.00 74.30 ATOM 2058 CB GLN A 255 -7.362 60.446 -10.251 1.00 74.30 ATOM 2059 CG GLN A 255 -8.555 61.387 -10.410 1.00 74.30 ATOM 2060 CD GLN A 255 -8.875 61.914 -9.017 1.00 74.30 ATOM 2061 OE1 GLN A 255 -9.050 61.145 -8.074 1.00 74.30 ATOM 2062 NE2 GLN A 255 -8.926 63.267 -8.877 1.00 74.30 ATOM 2063 N ARG A 256 -4.107 59.991 -9.845 1.00142.45 ATOM 2064 CA ARG A 256 -3.066 59.025 -9.604 1.00142.45 ATOM 2065 C ARG A 256 -2.429 59.273 -8.274 1.00142.45 ATOM 2066 O ARG A 256 -1.850 58.359 -7.689 1.00142.45 ATOM 2067 CB ARG A 256 -1.912 59.071 -10.622 1.00142.45 ATOM 2068 CG ARG A 256 -2.230 58.426 -11.969 1.00142.45 ATOM 2069 CD ARG A 256 -1.039 58.405 -12.933 1.00142.45 ATOM 2070 NE ARG A 256 -0.093 57.337 -12.497 1.00142.45 ATOM 2071 CZ ARG A 256 1.068 57.142 -13.189 1.00142.45 ATOM 2072 NH1 ARG A 256 1.361 57.927 -14.267 1.00142.45 ATOM 2073 NH2 ARG A 256 1.942 56.169 -12.803 1.00142.45 ATOM 2074 N TYR A 257 -2.490 60.521 -7.771 1.00 85.05 ATOM 2075 CA TYR A 257 -1.766 60.857 -6.578 1.00 85.05 ATOM 2076 C TYR A 257 -2.650 60.825 -5.378 1.00 85.05 ATOM 2077 O TYR A 257 -3.786 61.299 -5.391 1.00 85.05 ATOM 2078 CB TYR A 257 -1.179 62.275 -6.605 1.00 85.05 ATOM 2079 CG TYR A 257 -0.090 62.371 -7.618 1.00 85.05 ATOM 2080 CD1 TYR A 257 -0.363 62.441 -8.966 1.00 85.05 ATOM 2081 CD2 TYR A 257 1.219 62.417 -7.202 1.00 85.05 ATOM 2082 CE1 TYR A 257 0.656 62.545 -9.885 1.00 85.05 ATOM 2083 CE2 TYR A 257 2.240 62.522 -8.113 1.00 85.05 ATOM 2084 CZ TYR A 257 1.960 62.588 -9.454 1.00 85.05 ATOM 2085 OH TYR A 257 3.021 62.702 -10.374 1.00 85.05 ATOM 2086 N THR A 258 -2.131 60.213 -4.296 1.00 51.94 ATOM 2087 CA THR A 258 -2.845 60.207 -3.060 1.00 51.94 ATOM 2088 C THR A 258 -1.900 60.679 -2.001 1.00 51.94 ATOM 2089 O THR A 258 -0.715 60.346 -2.009 1.00 51.94 ATOM 2090 CB THR A 258 -3.377 58.859 -2.678 1.00 51.94 ATOM 2091 OG1 THR A 258 -2.312 57.927 -2.583 1.00 51.94 ATOM 2092 CG2 THR A 258 -4.380 58.410 -3.754 1.00 51.94 ATOM 2093 N CYS A 259 -2.411 61.515 -1.077 1.00 47.43 ATOM 2094 CA CYS A 259 -1.619 61.992 0.018 1.00 47.43 ATOM 2095 C CYS A 259 -1.935 61.098 1.165 1.00 47.43 ATOM 2096 O CYS A 259 -3.095 60.769 1.402 1.00 47.43 ATOM 2097 CB CYS A 259 -1.950 63.435 0.451 1.00 47.43 ATOM 2098 SG CYS A 259 -1.106 63.922 1.989 1.00 47.43 ATOM 2099 N HIS A 260 -0.901 60.652 1.897 1.00 61.06 ATOM 2100 CA HIS A 260 -1.174 59.785 2.999 1.00 61.06 ATOM 2101 C HIS A 260 -0.684 60.466 4.222 1.00 61.06 ATOM 2102 O HIS A 260 0.438 60.971 4.263 1.00 61.06 ATOM 2103 CB HIS A 260 -0.506 58.410 2.861 1.00 61.06 ATOM 2104 CG HIS A 260 -1.139 57.617 1.756 1.00 61.06 ATOM 2105 ND1 HIS A 260 -2.084 56.637 1.953 1.00 61.06 ATOM 2106 CD2 HIS A 260 -0.969 57.704 0.409 1.00 61.06 ATOM 2107 CE1 HIS A 260 -2.436 56.178 0.725 1.00 61.06 ATOM 2108 NE2 HIS A 260 -1.785 56.797 -0.242 1.00 61.06 ATOM 2109 N VAL A 261 -1.546 60.516 5.253 1.00 43.15 ATOM 2110 CA VAL A 261 -1.177 61.200 6.450 1.00 43.15 ATOM 2111 C VAL A 261 -1.187 60.209 7.555 1.00 43.15 ATOM 2112 O VAL A 261 -2.156 59.475 7.746 1.00 43.15 ATOM 2113 CB VAL A 261 -2.135 62.296 6.808 1.00 43.15 ATOM 2114 CG1 VAL A 261 -1.708 62.929 8.144 1.00 43.15 ATOM 2115 CG2 VAL A 261 -2.184 63.283 5.632 1.00 43.15 ATOM 2116 N GLN A 262 -0.075 60.163 8.308 1.00 53.39 ATOM 2117 CA GLN A 262 0.018 59.272 9.419 1.00 53.39 ATOM 2118 C GLN A 262 0.291 60.142 10.599 1.00 53.39 ATOM 2119 O GLN A 262 1.237 60.928 10.600 1.00 53.39 ATOM 2120 CB GLN A 262 1.176 58.268 9.264 1.00 53.39 ATOM 2121 CG GLN A 262 1.030 57.374 8.027 1.00 53.39 ATOM 2122 CD GLN A 262 2.313 56.577 7.838 1.00 53.39 ATOM 2123 OE1 GLN A 262 2.491 55.508 8.422 1.00 53.39 ATOM 2124 NE2 GLN A 262 3.239 57.108 6.995 1.00 53.39 ATOM 2125 N HIS A 263 -0.573 60.046 11.624 1.00 51.88 ATOM 2126 CA HIS A 263 -0.394 60.828 12.810 1.00 51.88 ATOM 2127 C HIS A 263 -0.927 60.011 13.940 1.00 51.88 ATOM 2128 O HIS A 263 -1.826 59.192 13.765 1.00 51.88 ATOM 2129 CB HIS A 263 -1.173 62.154 12.798 1.00 51.88 ATOM 2130 CG HIS A 263 -0.865 63.041 13.971 1.00 51.88 ATOM 2131 ND1 HIS A 263 0.304 63.756 14.105 1.00 51.88 ATOM 2132 CD2 HIS A 263 -1.609 63.338 15.073 1.00 51.88 ATOM 2133 CE1 HIS A 263 0.211 64.446 15.270 1.00 51.88 ATOM 2134 NE2 HIS A 263 -0.932 64.224 15.892 1.00 51.88 ATOM 2135 N GLU A 264 -0.389 60.245 15.146 1.00 52.54 ATOM 2136 CA GLU A 264 -0.748 59.536 16.340 1.00 52.54 ATOM 2137 C GLU A 264 -2.201 59.763 16.616 1.00 52.54 ATOM 2138 O GLU A 264 -2.907 58.874 17.090 1.00 52.54 ATOM 2139 CB GLU A 264 0.019 60.099 17.546 1.00 52.54 ATOM 2140 CG GLU A 264 -0.334 59.473 18.892 1.00 52.54 ATOM 2141 CD GLU A 264 0.342 60.335 19.949 1.00 52.54 ATOM 2142 OE1 GLU A 264 1.384 60.957 19.612 1.00 52.54 ATOM 2143 OE2 GLU A 264 -0.176 60.394 21.096 1.00 52.54 ATOM 2144 N GLY A 265 -2.668 60.985 16.327 1.00 51.43 ATOM 2145 CA GLY A 265 -4.001 61.445 16.584 1.00 51.43 ATOM 2146 C GLY A 265 -5.013 60.691 15.784 1.00 51.43 ATOM 2147 O GLY A 265 -6.178 60.649 16.171 1.00 51.43 ATOM 2148 N LEU A 266 -4.638 60.150 14.607 1.00 61.74 ATOM 2149 CA LEU A 266 -5.626 59.506 13.782 1.00 61.74 ATOM 2150 C LEU A 266 -5.658 58.029 14.045 1.00 61.74 ATOM 2151 O LEU A 266 -4.626 57.377 14.195 1.00 61.74 ATOM 2152 CB LEU A 266 -5.374 59.730 12.284 1.00 61.74 ATOM 2153 CG LEU A 266 -5.523 61.210 11.890 1.00 61.74 ATOM 2154 CD1 LEU A 266 -5.274 61.424 10.391 1.00 61.74 ATOM 2155 CD2 LEU A 266 -6.882 61.770 12.346 1.00 61.74 ATOM 2156 N PRO A 267 -6.855 57.495 14.136 1.00 67.46 ATOM 2157 CA PRO A 267 -7.020 56.086 14.358 1.00 67.46 ATOM 2158 C PRO A 267 -6.514 55.299 13.194 1.00 67.46 ATOM 2159 O PRO A 267 -6.004 54.199 13.403 1.00 67.46 ATOM 2160 CB PRO A 267 -8.499 55.883 14.684 1.00 67.46 ATOM 2161 CG PRO A 267 -8.908 57.227 15.317 1.00 67.46 ATOM 2162 CD PRO A 267 -7.974 58.259 14.660 1.00 67.46 ATOM 2163 N LYS A 268 -6.655 55.827 11.962 1.00104.44 ATOM 2164 CA LYS A 268 -6.124 55.143 10.819 1.00104.44 ATOM 2165 C LYS A 268 -5.500 56.189 9.957 1.00104.44 ATOM 2166 O LYS A 268 -5.886 57.356 9.997 1.00104.44 ATOM 2167 CB LYS A 268 -7.171 54.398 9.962 1.00104.44 ATOM 2168 CG LYS A 268 -7.756 53.155 10.642 1.00104.44 ATOM 2169 CD LYS A 268 -8.942 52.521 9.902 1.00104.44 ATOM 2170 CE LYS A 268 -10.315 52.882 10.479 1.00104.44 ATOM 2171 NZ LYS A 268 -11.125 53.597 9.467 1.00104.44 ATOM 2172 N PRO A 269 -4.538 55.800 9.170 1.00 60.45 ATOM 2173 CA PRO A 269 -3.903 56.766 8.323 1.00 60.45 ATOM 2174 C PRO A 269 -4.895 57.267 7.331 1.00 60.45 ATOM 2175 O PRO A 269 -5.759 56.502 6.905 1.00 60.45 ATOM 2176 CB PRO A 269 -2.683 56.060 7.740 1.00 60.45 ATOM 2177 CG PRO A 269 -2.300 55.052 8.843 1.00 60.45 ATOM 2178 CD PRO A 269 -3.628 54.731 9.551 1.00 60.45 ATOM 2179 N LEU A 270 -4.794 58.556 6.956 1.00 51.71 ATOM 2180 CA LEU A 270 -5.749 59.111 6.049 1.00 51.71 ATOM 2181 C LEU A 270 -5.169 59.083 4.676 1.00 51.71 ATOM 2182 O LEU A 270 -3.959 59.196 4.487 1.00 51.71 ATOM 2183 CB LEU A 270 -6.109 60.583 6.332 1.00 51.71 ATOM 2184 CG LEU A 270 -6.845 60.837 7.661 1.00 51.71 ATOM 2185 CD1 LEU A 270 -7.164 62.331 7.837 1.00 51.71 ATOM 2186 CD2 LEU A 270 -8.095 59.952 7.795 1.00 51.71 ATOM 2187 N THR A 271 -6.049 58.879 3.681 1.00 41.25 ATOM 2188 CA THR A 271 -5.651 58.931 2.311 1.00 41.25 ATOM 2189 C THR A 271 -6.418 60.081 1.746 1.00 41.25 ATOM 2190 O THR A 271 -7.646 60.119 1.837 1.00 41.25 ATOM 2191 CB THR A 271 -6.053 57.709 1.534 1.00 41.25 ATOM 2192 OG1 THR A 271 -5.486 56.546 2.119 1.00 41.25 ATOM 2193 CG2 THR A 271 -5.571 57.858 0.082 1.00 41.25 ATOM 2194 N LEU A 272 -5.712 61.073 1.176 1.00 97.12 ATOM 2195 CA LEU A 272 -6.408 62.187 0.608 1.00 97.12 ATOM 2196 C LEU A 272 -6.119 62.226 -0.849 1.00 97.12 ATOM 2197 O LEU A 272 -5.099 61.722 -1.320 1.00 97.12 ATOM 2198 CB LEU A 272 -5.988 63.577 1.118 1.00 97.12 ATOM 2199 CG LEU A 272 -6.316 63.886 2.587 1.00 97.12 ATOM 2200 CD1 LEU A 272 -5.411 63.107 3.555 1.00 97.12 ATOM 2201 CD2 LEU A 272 -6.305 65.404 2.825 1.00 97.12 ATOM 2202 N ARG A 273 -7.053 62.827 -1.603 1.00177.06 ATOM 2203 CA ARG A 273 -6.887 63.014 -3.009 1.00177.06 ATOM 2204 C ARG A 273 -7.404 64.384 -3.279 1.00177.06 ATOM 2205 O ARG A 273 -8.164 64.932 -2.482 1.00177.06 ATOM 2206 CB ARG A 273 -7.780 62.108 -3.878 1.00177.06 ATOM 2207 CG ARG A 273 -7.429 60.621 -3.921 1.00177.06 ATOM 2208 CD ARG A 273 -8.505 59.811 -4.654 1.00177.06 ATOM 2209 NE ARG A 273 -7.962 58.451 -4.933 1.00177.06 ATOM 2210 CZ ARG A 273 -8.058 57.458 -4.002 1.00177.06 ATOM 2211 NH1 ARG A 273 -8.628 57.710 -2.788 1.00177.06 ATOM 2212 NH2 ARG A 273 -7.584 56.212 -4.294 1.00177.06 ATOM 2213 N TRP A 274 -6.981 64.989 -4.403 1.00 59.86 ATOM 2214 CA TRP A 274 -7.549 66.246 -4.776 1.00 59.86 ATOM 2215 C TRP A 274 -9.015 65.963 -5.069 1.00 59.86 ATOM 2216 O TRP A 274 -9.295 65.062 -5.905 1.00 59.86 ATOM 2217 CB TRP A 274 -6.916 66.868 -6.037 1.00 59.86 ATOM 2218 CG TRP A 274 -7.691 68.041 -6.592 1.00 59.86 ATOM 2219 CD1 TRP A 274 -8.467 68.108 -7.716 1.00 59.86 ATOM 2220 CD2 TRP A 274 -7.799 69.321 -5.950 1.00 59.86 ATOM 2221 NE1 TRP A 274 -9.043 69.351 -7.814 1.00 59.86 ATOM 2222 CE2 TRP A 274 -8.646 70.107 -6.732 1.00 59.86 ATOM 2223 CE3 TRP A 274 -7.249 69.799 -4.794 1.00 59.86 ATOM 2224 CZ2 TRP A 274 -8.955 71.385 -6.365 1.00 59.86 ATOM 2225 CZ3 TRP A 274 -7.550 71.091 -4.434 1.00 59.86 ATOM 2226 CH2 TRP A 274 -8.390 71.871 -5.205 1.00 59.86 TER 2227 TRP A 274 ATOM 2228 N ILE B 1 32.605 75.712 10.645 1.00 30.47 ATOM 2229 CA ILE B 1 31.400 75.075 10.026 1.00 30.02 ATOM 2230 C ILE B 1 30.114 75.718 10.558 1.00 28.79 ATOM 2231 O ILE B 1 29.746 75.550 11.727 1.00 29.40 ATOM 2232 CB ILE B 1 31.365 73.541 10.258 1.00 30.56 ATOM 2233 CG1 ILE B 1 32.663 72.883 9.771 1.00 31.53 ATOM 2234 CG2 ILE B 1 30.159 72.917 9.557 1.00 31.27 ATOM 2235 CD1 ILE B 1 32.979 71.547 10.438 1.00 33.28 ATOM 2236 N GLN B 2 29.434 76.454 9.686 1.00 26.70 ATOM 2237 CA GLN B 2 28.213 77.165 10.057 1.00 24.85 ATOM 2238 C GLN B 2 27.050 76.671 9.217 1.00 22.85 ATOM 2239 O GLN B 2 27.247 76.052 8.170 1.00 22.92 ATOM 2240 CB GLN B 2 28.407 78.678 9.909 1.00 24.79 ATOM 2241 CG GLN B 2 29.445 79.225 10.896 1.00 25.80 ATOM 2242 CD GLN B 2 29.739 80.708 10.734 1.00 26.20 ATOM 2243 OE1 GLN B 2 29.768 81.238 9.618 1.00 28.58 ATOM 2244 NE2 GLN B 2 29.984 81.383 11.853 1.00 27.82 ATOM 2245 N ARG B 3 25.835 76.921 9.691 1.00 20.37 ATOM 2246 CA ARG B 3 24.649 76.465 8.996 1.00 18.72 ATOM 2247 C ARG B 3 23.672 77.611 8.829 1.00 18.06 ATOM 2248 O ARG B 3 23.384 78.347 9.768 1.00 17.36 ATOM 2249 CB ARG B 3 24.018 75.275 9.728 1.00 18.15 ATOM 2250 CG ARG B 3 24.809 73.985 9.523 1.00 18.90 ATOM 2251 CD ARG B 3 24.227 72.822 10.315 1.00 20.31 ATOM 2252 NE ARG B 3 24.764 72.808 11.665 1.00 20.21 ATOM 2253 CZ ARG B 3 24.434 71.925 12.600 1.00 20.05 ATOM 2254 NH1 ARG B 3 23.558 70.967 12.344 1.00 19.22 ATOM 2255 NH2 ARG B 3 24.984 72.016 13.801 1.00 20.59 ATOM 2256 N THR B 4 23.190 77.785 7.606 1.00 18.01 ATOM 2257 CA THR B 4 22.365 78.931 7.300 1.00 18.03 ATOM 2258 C THR B 4 20.904 78.644 7.653 1.00 17.77 ATOM 2259 O THR B 4 20.462 77.501 7.539 1.00 17.52 ATOM 2260 CB THR B 4 22.525 79.372 5.823 1.00 18.87 ATOM 2261 OG1 THR B 4 22.176 80.755 5.713 1.00 19.90 ATOM 2262 CG2 THR B 4 21.676 78.536 4.908 1.00 19.37 ATOM 2263 N PRO B 5 20.164 79.670 8.113 1.00 17.35 ATOM 2264 CA PRO B 5 18.785 79.363 8.481 1.00 17.67 ATOM 2265 C PRO B 5 17.900 78.987 7.313 1.00 18.02 ATOM 2266 O PRO B 5 17.994 79.577 6.231 1.00 18.54 ATOM 2267 CB PRO B 5 18.281 80.666 9.101 1.00 17.88 ATOM 2268 CG PRO B 5 19.195 81.728 8.571 1.00 19.13 ATOM 2269 CD PRO B 5 20.517 81.070 8.418 1.00 17.82 ATOM 2270 N LYS B 6 17.067 77.980 7.543 1.00 17.44 ATOM 2271 CA LYS B 6 15.844 77.790 6.781 1.00 17.57 ATOM 2272 C LYS B 6 14.857 78.807 7.317 1.00 16.75 ATOM 2273 O LYS B 6 14.911 79.177 8.486 1.00 15.93 ATOM 2274 CB LYS B 6 15.286 76.373 6.944 1.00 18.45 ATOM 2275 CG LYS B 6 16.252 75.259 6.575 1.00 21.10 ATOM 2276 CD LYS B 6 15.716 73.909 7.016 1.00 25.07 ATOM 2277 CE LYS B 6 16.849 72.905 7.218 1.00 28.00 ATOM 2278 NZ LYS B 6 16.503 71.859 8.231 1.00 31.09 ATOM 2279 N ILE B 7 13.967 79.274 6.454 1.00 16.79 ATOM 2280 CA ILE B 7 13.019 80.305 6.812 1.00 16.97 ATOM 2281 C ILE B 7 11.670 79.925 6.252 1.00 17.01 ATOM 2282 O ILE B 7 11.534 79.666 5.056 1.00 17.99 ATOM 2283 CB ILE B 7 13.423 81.692 6.251 1.00 16.91 ATOM 2284 CG1 ILE B 7 14.844 82.067 6.689 1.00 17.34 ATOM 2285 CG2 ILE B 7 12.404 82.742 6.655 1.00 18.04 ATOM 2286 CD1 ILE B 7 15.510 83.131 5.803 1.00 17.84 ATOM 2287 N GLN B 8 10.676 79.869 7.124 1.00 16.13 ATOM 2288 CA GLN B 8 9.303 79.753 6.670 1.00 16.18 ATOM 2289 C GLN B 8 8.528 80.888 7.252 1.00 16.39 ATOM 2290 O GLN B 8 8.664 81.188 8.432 1.00 15.89 ATOM 2291 CB GLN B 8 8.671 78.439 7.093 1.00 15.99 ATOM 2292 CG GLN B 8 9.312 77.229 6.503 1.00 15.94 ATOM 2293 CD GLN B 8 8.452 76.008 6.676 1.00 15.54 ATOM 2294 OE1 GLN B 8 7.350 75.935 6.133 1.00 16.39 ATOM 2295 NE2 GLN B 8 8.952 75.026 7.426 1.00 15.70 ATOM 2296 N VAL B 9 7.737 81.545 6.403 1.00 16.33 ATOM 2297 CA VAL B 9 6.876 82.626 6.837 1.00 17.19 ATOM 2298 C VAL B 9 5.465 82.170 6.548 1.00 17.00 ATOM 2299 O VAL B 9 5.164 81.706 5.441 1.00 17.63 ATOM 2300 CB VAL B 9 7.182 83.950 6.096 1.00 17.53 ATOM 2301 CG1 VAL B 9 6.377 85.097 6.692 1.00 18.08 ATOM 2302 CG2 VAL B 9 8.665 84.270 6.168 1.00 18.03 ATOM 2303 N TYR B 10 4.611 82.270 7.556 1.00 16.96 ATOM 2304 CA TYR B 10 3.287 81.684 7.444 1.00 17.02 ATOM 2305 C TYR B 10 2.424 82.194 8.566 1.00 17.76 ATOM 2306 O TYR B 10 2.893 82.844 9.492 1.00 18.90 ATOM 2307 CB TYR B 10 3.376 80.148 7.478 1.00 16.79 ATOM 2308 CG TYR B 10 4.095 79.626 8.701 1.00 15.62 ATOM 2309 CD1 TYR B 10 5.485 79.675 8.790 1.00 14.98 ATOM 2310 CD2 TYR B 10 3.384 79.117 9.772 1.00 14.66 ATOM 2311 CE1 TYR B 10 6.139 79.221 9.915 1.00 14.33 ATOM 2312 CE2 TYR B 10 4.034 78.646 10.897 1.00 13.35 ATOM 2313 CZ TYR B 10 5.408 78.709 10.956 1.00 14.33 ATOM 2314 OH TYR B 10 6.078 78.277 12.070 1.00 14.23 ATOM 2315 N SER B 11 1.139 81.891 8.502 1.00 18.09 ATOM 2316 CA SER B 11 0.266 82.333 9.549 1.00 18.23 ATOM 2317 C SER B 11 -0.130 81.154 10.430 1.00 18.26 ATOM 2318 O SER B 11 -0.061 79.986 10.015 1.00 18.26 ATOM 2319 CB SER B 11 -0.963 83.018 8.958 1.00 18.45 ATOM 2320 OG SER B 11 -1.593 82.147 8.040 1.00 20.06 ATOM 2321 N ARG B 12 -0.511 81.463 11.657 1.00 18.45 ATOM 2322 CA ARG B 12 -0.953 80.437 12.578 1.00 19.42 ATOM 2323 C ARG B 12 -2.194 79.735 12.045 1.00 20.48 ATOM 2324 O ARG B 12 -2.317 78.506 12.134 1.00 20.31 ATOM 2325 CB ARG B 12 -1.250 81.069 13.922 1.00 19.16 ATOM 2326 CG ARG B 12 -1.826 80.097 14.933 1.00 19.22 ATOM 2327 CD ARG B 12 -2.002 80.754 16.264 1.00 18.31 ATOM 2328 NE ARG B 12 -0.748 81.268 16.795 1.00 19.16 ATOM 2329 CZ ARG B 12 -0.644 81.915 17.953 1.00 19.79 ATOM 2330 NH1 ARG B 12 -1.722 82.102 18.705 1.00 22.66 ATOM 2331 NH2 ARG B 12 0.537 82.370 18.358 1.00 21.11 ATOM 2332 N HIS B 13 -3.111 80.530 11.506 1.00 21.88 ATOM 2333 CA HIS B 13 -4.353 80.017 10.953 1.00 23.80 ATOM 2334 C HIS B 13 -4.439 80.371 9.485 1.00 24.43 ATOM 2335 O HIS B 13 -3.772 81.311 9.047 1.00 24.15 ATOM 2336 CB HIS B 13 -5.535 80.604 11.715 1.00 23.90 ATOM 2337 CG HIS B 13 -5.581 80.172 13.141 1.00 26.77 ATOM 2338 ND1 HIS B 13 -5.820 78.866 13.507 1.00 28.77 ATOM 2339 CD2 HIS B 13 -5.383 80.860 14.290 1.00 28.10 ATOM 2340 CE1 HIS B 13 -5.785 78.771 14.824 1.00 28.81 ATOM 2341 NE2 HIS B 13 -5.519 79.966 15.322 1.00 29.05 ATOM 2342 N PRO B 14 -5.235 79.610 8.707 1.00 25.62 ATOM 2343 CA PRO B 14 -5.468 79.988 7.320 1.00 26.38 ATOM 2344 C PRO B 14 -5.804 81.470 7.241 1.00 26.88 ATOM 2345 O PRO B 14 -6.605 81.963 8.036 1.00 26.68 ATOM 2346 CB PRO B 14 -6.675 79.136 6.938 1.00 26.13 ATOM 2347 CG PRO B 14 -6.491 77.896 7.741 1.00 26.95 ATOM 2348 CD PRO B 14 -5.937 78.357 9.053 1.00 25.87 ATOM 2349 N ALA B 15 -5.151 82.178 6.325 1.00 27.97 ATOM 2350 CA ALA B 15 -5.332 83.616 6.203 1.00 29.20 ATOM 2351 C ALA B 15 -6.740 83.943 5.729 1.00 30.16 ATOM 2352 O ALA B 15 -7.247 83.332 4.788 1.00 30.24 ATOM 2353 CB ALA B 15 -4.305 84.203 5.256 1.00 29.50 ATOM 2354 N GLU B 16 -7.360 84.893 6.416 1.00 31.30 ATOM 2355 CA GLU B 16 -8.662 85.417 6.044 1.00 32.88 ATOM 2356 C GLU B 16 -8.586 86.929 6.193 1.00 32.90 ATOM 2357 O GLU B 16 -8.418 87.442 7.304 1.00 32.96 ATOM 2358 CB GLU B 16 -9.734 84.832 6.957 1.00 32.81 ATOM 2359 CG GLU B 16 -11.156 84.993 6.458 1.00 34.57 ATOM 2360 CD GLU B 16 -12.173 84.422 7.426 1.00 34.70 ATOM 2361 OE1 GLU B 16 -11.982 83.275 7.888 1.00 38.05 ATOM 2362 OE2 GLU B 16 -13.173 85.116 7.718 1.00 38.33 ATOM 2363 N ASN B 17 -8.682 87.641 5.070 1.00 33.46 ATOM 2364 CA ASN B 17 -8.540 89.101 5.068 1.00 33.90 ATOM 2365 C ASN B 17 -9.478 89.776 6.061 1.00 33.84 ATOM 2366 O ASN B 17 -10.666 89.445 6.134 1.00 33.78 ATOM 2367 CB ASN B 17 -8.721 89.680 3.659 1.00 34.27 ATOM 2368 CG ASN B 17 -7.620 89.250 2.700 1.00 35.28 ATOM 2369 OD1 ASN B 17 -6.541 88.818 3.118 1.00 36.46 ATOM 2370 ND2 ASN B 17 -7.887 89.370 1.403 1.00 36.33 ATOM 2371 N GLY B 18 -8.924 90.699 6.842 1.00 33.64 ATOM 2372 CA GLY B 18 -9.678 91.409 7.868 1.00 33.63 ATOM 2373 C GLY B 18 -9.861 90.640 9.165 1.00 33.38 ATOM 2374 O GLY B 18 -10.451 91.158 10.117 1.00 33.83 ATOM 2375 N LYS B 19 -9.352 89.410 9.215 1.00 33.14 ATOM 2376 CA LYS B 19 -9.444 88.596 10.427 1.00 32.71 ATOM 2377 C LYS B 19 -8.088 88.472 11.111 1.00 31.96 ATOM 2378 O LYS B 19 -7.100 88.094 10.477 1.00 31.88 ATOM 2379 CB LYS B 19 -10.020 87.207 10.123 1.00 33.20 ATOM 2380 CG LYS B 19 -11.479 87.209 9.646 1.00 33.88 ATOM 2381 CD LYS B 19 -12.433 87.762 10.710 1.00 35.84 ATOM 2382 CE LYS B 19 -13.865 87.870 10.188 1.00 35.78 ATOM 2383 NZ LYS B 19 -14.520 86.537 10.061 1.00 37.45 ATOM 2384 N SER B 20 -8.061 88.799 12.400 1.00 31.07 ATOM 2385 CA SER B 20 -6.838 88.760 13.198 1.00 30.01 ATOM 2386 C SER B 20 -6.226 87.370 13.198 1.00 28.62 ATOM 2387 O SER B 20 -6.928 86.362 13.273 1.00 28.97 ATOM 2388 CB SER B 20 -7.101 89.216 14.631 1.00 30.09 ATOM 2389 OG SER B 20 -5.878 89.413 15.317 1.00 31.36 ATOM 2390 N ASN B 21 -4.903 87.336 13.125 1.00 26.87 ATOM 2391 CA ASN B 21 -4.161 86.108 12.919 1.00 24.72 ATOM 2392 C ASN B 21 -2.785 86.340 13.524 1.00 23.69 ATOM 2393 O ASN B 21 -2.538 87.381 14.136 1.00 23.21 ATOM 2394 CB ASN B 21 -4.066 85.825 11.412 1.00 24.41 ATOM 2395 CG ASN B 21 -3.833 84.358 11.082 1.00 23.73 ATOM 2396 OD1 ASN B 21 -3.169 83.620 11.820 1.00 22.41 ATOM 2397 ND2 ASN B 21 -4.342 83.937 9.937 1.00 22.66 ATOM 2398 N PHE B 22 -1.899 85.365 13.377 1.00 22.38 ATOM 2399 CA PHE B 22 -0.518 85.538 13.780 1.00 21.57 ATOM 2400 C PHE B 22 0.351 85.265 12.602 1.00 20.02 ATOM 2401 O PHE B 22 0.154 84.283 11.887 1.00 19.53 ATOM 2402 CB PHE B 22 -0.148 84.597 14.922 1.00 21.98 ATOM 2403 CG PHE B 22 -0.518 85.121 16.263 1.00 23.37 ATOM 2404 CD1 PHE B 22 0.429 85.768 17.050 1.00 25.17 ATOM 2405 CD2 PHE B 22 -1.812 84.967 16.751 1.00 24.23 ATOM 2406 CE1 PHE B 22 0.094 86.263 18.306 1.00 26.02 ATOM 2407 CE2 PHE B 22 -2.166 85.466 18.009 1.00 24.90 ATOM 2408 CZ PHE B 22 -1.210 86.115 18.786 1.00 24.62 ATOM 2409 N LEU B 23 1.299 86.168 12.394 1.00 18.99 ATOM 2410 CA LEU B 23 2.285 86.042 11.360 1.00 18.36 ATOM 2411 C LEU B 23 3.504 85.433 12.012 1.00 17.23 ATOM 2412 O LEU B 23 4.007 85.968 12.990 1.00 16.96 ATOM 2413 CB LEU B 23 2.639 87.412 10.781 1.00 18.79 ATOM 2414 CG LEU B 23 3.749 87.411 9.734 1.00 19.24 ATOM 2415 CD1 LEU B 23 3.353 86.640 8.496 1.00 19.44 ATOM 2416 CD2 LEU B 23 4.160 88.840 9.378 1.00 19.88 ATOM 2417 N ASN B 24 3.950 84.321 11.449 1.00 16.42 ATOM 2418 CA ASN B 24 5.052 83.565 11.994 1.00 15.68 ATOM 2419 C ASN B 24 6.188 83.593 11.043 1.00 15.38 ATOM 2420 O ASN B 24 5.998 83.474 9.835 1.00 15.38 ATOM 2421 CB ASN B 24 4.658 82.107 12.164 1.00 15.74 ATOM 2422 CG ASN B 24 3.696 81.899 13.288 1.00 15.67 ATOM 2423 OD1 ASN B 24 3.716 82.627 14.273 1.00 17.97 ATOM 2424 ND2 ASN B 24 2.822 80.909 13.142 1.00 16.64 ATOM 2425 N CYS B 25 7.385 83.718 11.592 1.00 15.39 ATOM 2426 CA CYS B 25 8.559 83.447 10.829 1.00 15.26 ATOM 2427 C CYS B 25 9.382 82.437 11.598 1.00 14.53 ATOM 2428 O CYS B 25 9.847 82.730 12.699 1.00 14.78 ATOM 2429 CB CYS B 25 9.337 84.725 10.600 1.00 15.93 ATOM 2430 SG CYS B 25 10.796 84.442 9.634 1.00 17.47 ATOM 2431 N TYR B 26 9.516 81.250 11.024 1.00 13.57 ATOM 2432 CA TYR B 26 10.183 80.144 11.687 1.00 13.68 ATOM 2433 C TYR B 26 11.533 80.005 11.055 1.00 14.11 ATOM 2434 O TYR B 26 11.638 79.741 9.869 1.00 14.10 ATOM 2435 CB TYR B 26 9.376 78.860 11.521 1.00 14.17 ATOM 2436 CG TYR B 26 9.980 77.643 12.173 1.00 13.50 ATOM 2437 CD1 TYR B 26 10.261 77.631 13.537 1.00 13.18 ATOM 2438 CD2 TYR B 26 10.262 76.496 11.431 1.00 14.12 ATOM 2439 CE1 TYR B 26 10.823 76.508 14.139 1.00 14.52 ATOM 2440 CE2 TYR B 26 10.818 75.369 12.028 1.00 15.02 ATOM 2441 CZ TYR B 26 11.085 75.388 13.375 1.00 15.41 ATOM 2442 OH TYR B 26 11.634 74.264 13.977 1.00 18.12 ATOM 2443 N VAL B 27 12.567 80.233 11.851 1.00 13.55 ATOM 2444 CA VAL B 27 13.927 80.078 11.378 1.00 13.99 ATOM 2445 C VAL B 27 14.503 78.854 12.051 1.00 13.77 ATOM 2446 O VAL B 27 14.327 78.659 13.245 1.00 13.28 ATOM 2447 CB VAL B 27 14.794 81.344 11.610 1.00 15.14 ATOM 2448 CG1 VAL B 27 14.330 82.475 10.701 1.00 16.71 ATOM 2449 CG2 VAL B 27 14.762 81.786 13.050 1.00 15.61 ATOM 2450 N SER B 28 15.136 78.001 11.276 1.00 13.00 ATOM 2451 CA SER B 28 15.608 76.738 11.802 1.00 13.73 ATOM 2452 C SER B 28 16.825 76.281 11.061 1.00 13.99 ATOM 2453 O SER B 28 17.185 76.847 10.044 1.00 14.20 ATOM 2454 CB SER B 28 14.523 75.668 11.703 1.00 13.65 ATOM 2455 OG SER B 28 14.201 75.423 10.347 1.00 15.45 ATOM 2456 N GLY B 29 17.464 75.247 11.569 1.00 13.96 ATOM 2457 CA GLY B 29 18.588 74.657 10.893 1.00 13.85 ATOM 2458 C GLY B 29 19.838 75.490 10.890 1.00 13.90 ATOM 2459 O GLY B 29 20.765 75.154 10.184 1.00 14.95 ATOM 2460 N PHE B 30 19.890 76.544 11.699 1.00 14.09 ATOM 2461 CA PHE B 30 21.024 77.447 11.679 1.00 14.06 ATOM 2462 C PHE B 30 21.991 77.223 12.810 1.00 13.88 ATOM 2463 O PHE B 30 21.658 76.683 13.857 1.00 13.56 ATOM 2464 CB PHE B 30 20.595 78.926 11.610 1.00 13.75 ATOM 2465 CG PHE B 30 19.743 79.390 12.759 1.00 13.10 ATOM 2466 CD1 PHE B 30 18.372 79.190 12.746 1.00 14.64 ATOM 2467 CD2 PHE B 30 20.316 80.067 13.836 1.00 12.07 ATOM 2468 CE1 PHE B 30 17.585 79.618 13.808 1.00 14.08 ATOM 2469 CE2 PHE B 30 19.536 80.527 14.893 1.00 12.25 ATOM 2470 CZ PHE B 30 18.158 80.304 14.879 1.00 13.69 ATOM 2471 N HIS B 31 23.218 77.640 12.577 1.00 14.40 ATOM 2472 CA HIS B 31 24.240 77.579 13.576 1.00 14.73 ATOM 2473 C HIS B 31 25.329 78.538 13.103 1.00 15.30 ATOM 2474 O HIS B 31 25.701 78.484 11.949 1.00 15.86 ATOM 2475 CB HIS B 31 24.774 76.154 13.684 1.00 13.98 ATOM 2476 CG HIS B 31 25.242 75.817 15.051 1.00 13.98 ATOM 2477 ND1 HIS B 31 26.393 76.345 15.600 1.00 13.84 ATOM 2478 CD2 HIS B 31 24.691 75.031 16.001 1.00 12.76 ATOM 2479 CE1 HIS B 31 26.531 75.890 16.830 1.00 14.39 ATOM 2480 NE2 HIS B 31 25.512 75.093 17.099 1.00 13.02 ATOM 2481 N PRO B 32 25.825 79.428 13.971 1.00 15.25 ATOM 2482 CA PRO B 32 25.514 79.624 15.375 1.00 15.31 ATOM 2483 C PRO B 32 24.159 80.284 15.615 1.00 15.39 ATOM 2484 O PRO B 32 23.375 80.505 14.690 1.00 14.74 ATOM 2485 CB PRO B 32 26.648 80.543 15.844 1.00 15.51 ATOM 2486 CG PRO B 32 26.950 81.365 14.624 1.00 16.55 ATOM 2487 CD PRO B 32 26.864 80.377 13.508 1.00 15.82 ATOM 2488 N SER B 33 23.900 80.603 16.866 1.00 15.89 ATOM 2489 CA SER B 33 22.567 80.942 17.295 1.00 16.32 ATOM 2490 C SER B 33 22.158 82.387 17.094 1.00 16.70 ATOM 2491 O SER B 33 20.974 82.665 17.087 1.00 16.14 ATOM 2492 CB SER B 33 22.405 80.585 18.767 1.00 17.18 ATOM 2493 OG SER B 33 23.459 81.177 19.484 1.00 19.14 ATOM 2494 N ASP B 34 23.120 83.301 16.979 1.00 17.88 ATOM 2495 CA ASP B 34 22.751 84.702 16.825 1.00 18.90 ATOM 2496 C ASP B 34 22.105 84.858 15.475 1.00 18.31 ATOM 2497 O ASP B 34 22.586 84.338 14.480 1.00 18.73 ATOM 2498 CB ASP B 34 23.944 85.640 16.972 1.00 19.77 ATOM 2499 CG ASP B 34 24.269 85.968 18.433 1.00 21.97 ATOM 2500 OD1 ASP B 34 23.572 85.516 19.371 1.00 24.21 ATOM 2501 OD2 ASP B 34 25.248 86.712 18.642 1.00 27.25 ATOM 2502 N ILE B 35 20.995 85.573 15.468 1.00 18.41 ATOM 2503 CA ILE B 35 20.216 85.741 14.275 1.00 18.83 ATOM 2504 C ILE B 35 19.368 86.985 14.491 1.00 19.57 ATOM 2505 O ILE B 35 18.930 87.263 15.608 1.00 20.19 ATOM 2506 CB ILE B 35 19.371 84.459 14.001 1.00 18.55 ATOM 2507 CG1 ILE B 35 18.801 84.458 12.583 1.00 17.98 ATOM 2508 CG2 ILE B 35 18.296 84.260 15.056 1.00 19.55 ATOM 2509 CD1 ILE B 35 18.360 83.075 12.114 1.00 17.31 ATOM 2510 N GLU B 36 19.207 87.763 13.425 1.00 20.78 ATOM 2511 CA GLU B 36 18.375 88.955 13.455 1.00 22.35 ATOM 2512 C GLU B 36 17.163 88.629 12.608 1.00 21.33 ATOM 2513 O GLU B 36 17.295 88.236 11.452 1.00 21.75 ATOM 2514 CB GLU B 36 19.125 90.173 12.892 1.00 22.45 ATOM 2515 CG GLU B 36 18.273 91.454 12.840 1.00 25.78 ATOM 2516 CD GLU B 36 18.968 92.655 12.197 1.00 26.29 ATOM 2517 OE1 GLU B 36 20.102 92.996 12.603 1.00 31.49 ATOM 2518 OE2 GLU B 36 18.358 93.274 11.295 1.00 31.36 ATOM 2519 N VAL B 37 15.986 88.736 13.205 1.00 21.29 ATOM 2520 CA VAL B 37 14.763 88.463 12.471 1.00 21.40 ATOM 2521 C VAL B 37 13.812 89.626 12.687 1.00 21.75 ATOM 2522 O VAL B 37 13.551 90.020 13.819 1.00 22.24 ATOM 2523 CB VAL B 37 14.111 87.128 12.903 1.00 21.02 ATOM 2524 CG1 VAL B 37 12.806 86.897 12.153 1.00 21.60 ATOM 2525 CG2 VAL B 37 15.064 85.963 12.672 1.00 20.46 ATOM 2526 N ASP B 38 13.344 90.192 11.579 1.00 22.34 ATOM 2527 CA ASP B 38 12.339 91.239 11.600 1.00 22.77 ATOM 2528 C ASP B 38 11.138 90.748 10.845 1.00 22.29 ATOM 2529 O ASP B 38 11.274 90.078 9.832 1.00 22.00 ATOM 2530 CB ASP B 38 12.852 92.504 10.902 1.00 23.21 ATOM 2531 CG ASP B 38 13.990 93.149 11.643 1.00 26.29 ATOM 2532 OD1 ASP B 38 13.808 93.469 12.840 1.00 28.28 ATOM 2533 OD2 ASP B 38 15.059 93.332 11.022 1.00 29.77 ATOM 2534 N LEU B 39 9.960 91.100 11.342 1.00 22.39 ATOM 2535 CA LEU B 39 8.755 90.955 10.553 1.00 22.86 ATOM 2536 C LEU B 39 8.450 92.318 9.947 1.00 23.07 ATOM 2537 O LEU B 39 8.493 93.343 10.636 1.00 23.22 ATOM 2538 CB LEU B 39 7.595 90.417 11.395 1.00 22.56 ATOM 2539 CG LEU B 39 7.824 89.010 11.983 1.00 22.87 ATOM 2540 CD1 LEU B 39 6.647 88.566 12.838 1.00 22.80 ATOM 2541 CD2 LEU B 39 8.075 87.997 10.885 1.00 23.60 ATOM 2542 N LEU B 40 8.160 92.312 8.653 1.00 24.09 ATOM 2543 CA LEU B 40 7.947 93.548 7.912 1.00 25.04 ATOM 2544 C LEU B 40 6.510 93.638 7.446 1.00 25.83 ATOM 2545 O LEU B 40 5.931 92.647 6.996 1.00 25.58 ATOM 2546 CB LEU B 40 8.886 93.621 6.710 1.00 25.18 ATOM 2547 CG LEU B 40 10.378 93.376 6.966 1.00 24.56 ATOM 2548 CD1 LEU B 40 11.149 93.456 5.660 1.00 24.19 ATOM 2549 CD2 LEU B 40 10.955 94.330 8.020 1.00 23.75 ATOM 2550 N LYS B 41 5.940 94.831 7.593 1.00 26.21 ATOM 2551 CA LYS B 41 4.645 95.158 7.034 1.00 27.01 ATOM 2552 C LYS B 41 4.894 96.267 6.030 1.00 27.61 ATOM 2553 O LYS B 41 5.307 97.367 6.408 1.00 27.71 ATOM 2554 CB LYS B 41 3.687 95.640 8.121 1.00 26.85 ATOM 2555 CG LYS B 41 2.327 96.077 7.579 1.00 27.42 ATOM 2556 CD LYS B 41 1.480 96.689 8.668 1.00 28.71 ATOM 2557 CE LYS B 41 0.095 97.028 8.158 1.00 29.77 ATOM 2558 NZ LYS B 41 -0.775 97.442 9.289 1.00 31.18 ATOM 2559 N ASN B 42 4.657 95.958 4.758 1.00 28.58 ATOM 2560 CA ASN B 42 4.925 96.883 3.653 1.00 29.16 ATOM 2561 C ASN B 42 6.334 97.479 3.754 1.00 29.61 ATOM 2562 O ASN B 42 6.514 98.697 3.692 1.00 29.94 ATOM 2563 CB ASN B 42 3.849 97.982 3.594 1.00 29.21 ATOM 2564 CG ASN B 42 2.445 97.419 3.449 1.00 28.21 ATOM 2565 OD1 ASN B 42 2.191 96.569 2.600 1.00 27.52 ATOM 2566 ND2 ASN B 42 1.527 97.891 4.283 1.00 29.24 ATOM 2567 N GLY B 43 7.321 96.600 3.938 1.00 29.96 ATOM 2568 CA GLY B 43 8.730 96.989 4.025 1.00 30.41 ATOM 2569 C GLY B 43 9.175 97.573 5.357 1.00 30.57 ATOM 2570 O GLY B 43 10.375 97.730 5.599 1.00 31.01 ATOM 2571 N GLU B 44 8.219 97.888 6.223 1.00 30.72 ATOM 2572 CA GLU B 44 8.508 98.550 7.491 1.00 30.96 ATOM 2573 C GLU B 44 8.542 97.546 8.640 1.00 30.59 ATOM 2574 O GLU B 44 7.722 96.630 8.701 1.00 30.20 ATOM 2575 CB GLU B 44 7.479 99.657 7.765 1.00 31.48 ATOM 2576 CG GLU B 44 7.476 100.772 6.709 1.00 34.38 ATOM 2577 CD GLU B 44 6.143 101.507 6.596 1.00 37.66 ATOM 2578 OE1 GLU B 44 5.623 101.989 7.629 1.00 39.33 ATOM 2579 OE2 GLU B 44 5.623 101.614 5.460 1.00 40.02 ATOM 2580 N ARG B 45 9.497 97.731 9.544 1.00 30.06 ATOM 2581 CA ARG B 45 9.680 96.829 10.676 1.00 30.08 ATOM 2582 C ARG B 45 8.481 96.913 11.616 1.00 29.37 ATOM 2583 O ARG B 45 8.093 97.992 12.045 1.00 29.36 ATOM 2584 CB ARG B 45 10.973 97.188 11.414 1.00 30.55 ATOM 2585 CG ARG B 45 11.412 96.201 12.470 1.00 32.80 ATOM 2586 CD ARG B 45 12.680 96.698 13.145 1.00 35.60 ATOM 2587 NE ARG B 45 13.107 95.840 14.250 1.00 39.36 ATOM 2588 CZ ARG B 45 12.600 95.879 15.481 1.00 40.52 ATOM 2589 NH1 ARG B 45 11.616 96.721 15.781 1.00 41.63 ATOM 2590 NH2 ARG B 45 13.066 95.062 16.414 1.00 41.84 ATOM 2591 N ILE B 46 7.876 95.763 11.903 1.00 28.47 ATOM 2592 CA ILE B 46 6.816 95.682 12.895 1.00 28.07 ATOM 2593 C ILE B 46 7.462 95.756 14.273 1.00 28.28 ATOM 2594 O ILE B 46 8.450 95.064 14.540 1.00 28.30 ATOM 2595 CB ILE B 46 5.981 94.382 12.734 1.00 27.48 ATOM 2596 CG1 ILE B 46 5.304 94.362 11.357 1.00 27.34 ATOM 2597 CG2 ILE B 46 4.960 94.253 13.861 1.00 27.30 ATOM 2598 CD1 ILE B 46 4.811 92.995 10.903 1.00 25.19 ATOM 2599 N GLU B 47 6.922 96.609 15.137 1.00 28.43 ATOM 2600 CA GLU B 47 7.502 96.821 16.460 1.00 29.14 ATOM 2601 C GLU B 47 7.200 95.683 17.419 1.00 29.09 ATOM 2602 O GLU B 47 8.073 95.262 18.188 1.00 29.45 ATOM 2603 CB GLU B 47 7.031 98.144 17.060 1.00 29.49 ATOM 2604 CG GLU B 47 7.751 99.346 16.497 1.00 30.80 ATOM 2605 CD GLU B 47 7.419 100.638 17.218 1.00 32.28 ATOM 2606 OE1 GLU B 47 6.618 100.620 18.185 1.00 32.33 ATOM 2607 OE2 GLU B 47 7.975 101.678 16.806 1.00 33.42 ATOM 2608 N LYS B 48 5.969 95.184 17.369 1.00 28.83 ATOM 2609 CA LYS B 48 5.506 94.202 18.339 1.00 29.06 ATOM 2610 C LYS B 48 5.794 92.785 17.858 1.00 28.23 ATOM 2611 O LYS B 48 4.866 92.065 17.491 1.00 28.91 ATOM 2612 CB LYS B 48 3.998 94.349 18.607 1.00 29.59 ATOM 2613 CG LYS B 48 3.494 95.768 18.860 1.00 31.81 ATOM 2614 CD LYS B 48 3.037 96.452 17.567 1.00 35.22 ATOM 2615 CE LYS B 48 2.412 97.815 17.857 1.00 36.69 ATOM 2616 NZ LYS B 48 3.390 98.768 18.459 1.00 38.43 ATOM 2617 N VAL B 49 7.069 92.385 17.873 1.00 26.27 ATOM 2618 CA VAL B 49 7.442 91.015 17.488 1.00 24.09 ATOM 2619 C VAL B 49 8.038 90.245 18.665 1.00 23.37 ATOM 2620 O VAL B 49 8.951 90.713 19.350 1.00 23.26 ATOM 2621 CB VAL B 49 8.391 90.976 16.263 1.00 23.85 ATOM 2622 CG1 VAL B 49 8.745 89.523 15.884 1.00 22.82 ATOM 2623 CG2 VAL B 49 7.745 91.676 15.072 1.00 22.15 ATOM 2624 N GLU B 50 7.508 89.050 18.885 1.00 22.12 ATOM 2625 CA GLU B 50 8.029 88.189 19.926 1.00 20.96 ATOM 2626 C GLU B 50 8.695 86.983 19.304 1.00 19.17 ATOM 2627 O GLU B 50 8.514 86.688 18.130 1.00 17.58 ATOM 2628 CB GLU B 50 6.908 87.765 20.857 1.00 21.60 ATOM 2629 CG GLU B 50 6.323 88.924 21.653 1.00 25.29 ATOM 2630 CD GLU B 50 5.130 88.504 22.473 1.00 28.84 ATOM 2631 OE1 GLU B 50 5.338 87.907 23.551 1.00 31.83 ATOM 2632 OE2 GLU B 50 3.987 88.771 22.044 1.00 32.73 ATOM 2633 N HIS B 51 9.499 86.288 20.090 1.00 18.10 ATOM 2634 CA HIS B 51 10.056 85.041 19.606 1.00 17.29 ATOM 2635 C HIS B 51 10.130 83.999 20.688 1.00 16.37 ATOM 2636 O HIS B 51 10.103 84.300 21.880 1.00 16.70 ATOM 2637 CB HIS B 51 11.431 85.254 18.985 1.00 18.09 ATOM 2638 CG HIS B 51 12.436 85.808 19.939 1.00 19.35 ATOM 2639 ND1 HIS B 51 13.168 85.013 20.795 1.00 22.58 ATOM 2640 CD2 HIS B 51 12.825 87.082 20.179 1.00 22.61 ATOM 2641 CE1 HIS B 51 13.971 85.774 21.517 1.00 23.31 ATOM 2642 NE2 HIS B 51 13.782 87.032 21.163 1.00 23.32 ATOM 2643 N SER B 52 10.221 82.758 20.230 1.00 15.06 ATOM 2644 CA SER B 52 10.357 81.625 21.117 1.00 14.31 ATOM 2645 C SER B 52 11.744 81.583 21.764 1.00 14.33 ATOM 2646 O SER B 52 12.673 82.305 21.371 1.00 14.38 ATOM 2647 CB SER B 52 10.108 80.343 20.334 1.00 14.21 ATOM 2648 OG SER B 52 11.095 80.203 19.328 1.00 14.98 ATOM 2649 N ASP B 53 11.867 80.728 22.770 1.00 13.15 ATOM 2650 CA ASP B 53 13.130 80.543 23.441 1.00 13.33 ATOM 2651 C ASP B 53 14.020 79.648 22.617 1.00 12.81 ATOM 2652 O ASP B 53 13.583 78.640 22.073 1.00 13.29 ATOM 2653 CB ASP B 53 12.913 79.900 24.785 1.00 12.88 ATOM 2654 CG ASP B 53 11.954 80.678 25.639 1.00 13.53 ATOM 2655 OD1 ASP B 53 12.026 81.932 25.640 1.00 15.41 ATOM 2656 OD2 ASP B 53 11.125 80.054 26.324 1.00 13.52 ATOM 2657 N LEU B 54 15.283 80.008 22.546 1.00 12.99 ATOM 2658 CA LEU B 54 16.239 79.270 21.755 1.00 13.22 ATOM 2659 C LEU B 54 16.262 77.792 22.095 1.00 13.44 ATOM 2660 O LEU B 54 16.482 77.391 23.230 1.00 13.37 ATOM 2661 CB LEU B 54 17.623 79.866 21.936 1.00 13.32 ATOM 2662 CG LEU B 54 18.685 79.248 21.039 1.00 13.04 ATOM 2663 CD1 LEU B 54 18.426 79.652 19.614 1.00 13.85 ATOM 2664 CD2 LEU B 54 20.052 79.747 21.493 1.00 14.76 ATOM 2665 N SER B 55 16.065 76.984 21.067 1.00 12.91 ATOM 2666 CA SER B 55 16.148 75.553 21.209 1.00 13.11 ATOM 2667 C SER B 55 16.839 75.028 19.982 1.00 11.81 ATOM 2668 O SER B 55 17.188 75.779 19.075 1.00 12.18 ATOM 2669 CB SER B 55 14.761 74.947 21.328 1.00 13.86 ATOM 2670 OG SER B 55 14.860 73.592 21.727 1.00 18.01 ATOM 2671 N PHE B 56 17.078 73.726 19.964 1.00 11.41 ATOM 2672 CA PHE B 56 17.762 73.150 18.844 1.00 11.85 ATOM 2673 C PHE B 56 17.297 71.734 18.578 1.00 12.19 ATOM 2674 O PHE B 56 16.698 71.068 19.433 1.00 12.22 ATOM 2675 CB PHE B 56 19.278 73.208 19.052 1.00 11.23 ATOM 2676 CG PHE B 56 19.743 72.590 20.331 1.00 11.08 ATOM 2677 CD1 PHE B 56 19.883 71.200 20.449 1.00 11.19 ATOM 2678 CD2 PHE B 56 20.068 73.400 21.418 1.00 11.47 ATOM 2679 CE1 PHE B 56 20.333 70.649 21.632 1.00 11.63 ATOM 2680 CE2 PHE B 56 20.511 72.854 22.586 1.00 10.10 ATOM 2681 CZ PHE B 56 20.644 71.481 22.700 1.00 10.60 ATOM 2682 N SER B 57 17.602 71.303 17.365 1.00 12.68 ATOM 2683 CA SER B 57 17.201 70.010 16.853 1.00 13.12 ATOM 2684 C SER B 57 18.253 68.968 17.140 1.00 13.01 ATOM 2685 O SER B 57 19.308 69.261 17.685 1.00 12.42 ATOM 2686 CB SER B 57 16.985 70.147 15.350 1.00 13.10 ATOM 2687 OG SER B 57 15.991 71.121 15.127 1.00 14.95 ATOM 2688 N LYS B 58 17.966 67.726 16.768 1.00 14.48 ATOM 2689 CA LYS B 58 18.844 66.623 17.098 1.00 15.08 ATOM 2690 C LYS B 58 20.205 66.781 16.446 1.00 14.54 ATOM 2691 O LYS B 58 21.191 66.284 16.965 1.00 15.62 ATOM 2692 CB LYS B 58 18.216 65.292 16.685 1.00 15.89 ATOM 2693 CG LYS B 58 17.072 64.918 17.585 1.00 18.01 ATOM 2694 CD LYS B 58 16.526 63.522 17.314 1.00 22.53 ATOM 2695 CE LYS B 58 15.149 63.378 17.935 1.00 27.45 ATOM 2696 NZ LYS B 58 14.638 61.979 17.924 1.00 30.97 ATOM 2697 N ASP B 59 20.264 67.510 15.334 1.00 13.52 ATOM 2698 CA ASP B 59 21.545 67.785 14.688 1.00 13.34 ATOM 2699 C ASP B 59 22.236 69.035 15.236 1.00 12.94 ATOM 2700 O ASP B 59 23.212 69.507 14.685 1.00 13.21 ATOM 2701 CB ASP B 59 21.380 67.884 13.171 1.00 13.21 ATOM 2702 CG ASP B 59 20.559 69.066 12.742 1.00 15.55 ATOM 2703 OD1 ASP B 59 20.188 69.900 13.586 1.00 14.45 ATOM 2704 OD2 ASP B 59 20.281 69.152 11.529 1.00 17.54 ATOM 2705 N TRP B 60 21.704 69.556 16.341 1.00 12.40 ATOM 2706 CA TRP B 60 22.267 70.710 17.045 1.00 11.88 ATOM 2707 C TRP B 60 21.977 72.040 16.396 1.00 12.21 ATOM 2708 O TRP B 60 22.395 73.066 16.912 1.00 12.50 ATOM 2709 CB TRP B 60 23.762 70.566 17.275 1.00 11.74 ATOM 2710 CG TRP B 60 24.154 69.267 17.909 1.00 11.94 ATOM 2711 CD1 TRP B 60 24.787 68.212 17.303 1.00 13.01 ATOM 2712 CD2 TRP B 60 23.929 68.870 19.262 1.00 11.03 ATOM 2713 NE1 TRP B 60 24.978 67.200 18.201 1.00 12.58 ATOM 2714 CE2 TRP B 60 24.470 67.577 19.413 1.00 11.73 ATOM 2715 CE3 TRP B 60 23.333 69.489 20.369 1.00 11.49 ATOM 2716 CZ2 TRP B 60 24.440 66.894 20.614 1.00 11.82 ATOM 2717 CZ3 TRP B 60 23.309 68.807 21.564 1.00 11.46 ATOM 2718 CH2 TRP B 60 23.866 67.520 21.680 1.00 11.99 ATOM 2719 N SER B 61 21.291 72.050 15.267 1.00 11.96 ATOM 2720 CA SER B 61 20.968 73.317 14.664 1.00 12.28 ATOM 2721 C SER B 61 19.823 73.957 15.431 1.00 11.93 ATOM 2722 O SER B 61 18.955 73.286 15.981 1.00 11.70 ATOM 2723 CB SER B 61 20.639 73.138 13.187 1.00 13.51 ATOM 2724 OG SER B 61 19.456 72.373 13.021 1.00 13.89 ATOM 2725 N PHE B 62 19.838 75.281 15.456 1.00 11.47 ATOM 2726 CA PHE B 62 18.887 76.036 16.247 1.00 11.94 ATOM 2727 C PHE B 62 17.616 76.301 15.509 1.00 11.53 ATOM 2728 O PHE B 62 17.582 76.293 14.282 1.00 12.23 ATOM 2729 CB PHE B 62 19.509 77.359 16.644 1.00 12.18 ATOM 2730 CG PHE B 62 20.663 77.201 17.561 1.00 11.43 ATOM 2731 CD1 PHE B 62 20.455 76.889 18.889 1.00 10.93 ATOM 2732 CD2 PHE B 62 21.949 77.306 17.084 1.00 12.70 ATOM 2733 CE1 PHE B 62 21.512 76.710 19.744 1.00 11.68 ATOM 2734 CE2 PHE B 62 23.023 77.141 17.927 1.00 11.65 ATOM 2735 CZ PHE B 62 22.811 76.835 19.261 1.00 11.03 ATOM 2736 N TYR B 63 16.567 76.572 16.266 1.00 11.98 ATOM 2737 CA TYR B 63 15.336 77.046 15.681 1.00 12.26 ATOM 2738 C TYR B 63 14.686 78.054 16.600 1.00 11.93 ATOM 2739 O TYR B 63 14.823 77.990 17.823 1.00 11.48 ATOM 2740 CB TYR B 63 14.383 75.891 15.322 1.00 13.20 ATOM 2741 CG TYR B 63 13.950 75.058 16.479 1.00 12.13 ATOM 2742 CD1 TYR B 63 12.867 75.434 17.258 1.00 13.85 ATOM 2743 CD2 TYR B 63 14.589 73.858 16.758 1.00 12.14 ATOM 2744 CE1 TYR B 63 12.456 74.654 18.309 1.00 12.33 ATOM 2745 CE2 TYR B 63 14.194 73.078 17.822 1.00 13.35 ATOM 2746 CZ TYR B 63 13.125 73.478 18.592 1.00 14.54 ATOM 2747 OH TYR B 63 12.715 72.708 19.663 1.00 16.82 ATOM 2748 N LEU B 64 13.994 79.002 15.984 1.00 12.78 ATOM 2749 CA LEU B 64 13.251 80.040 16.660 1.00 12.70 ATOM 2750 C LEU B 64 12.032 80.370 15.860 1.00 12.78 ATOM 2751 O LEU B 64 12.066 80.365 14.635 1.00 12.78 ATOM 2752 CB LEU B 64 14.064 81.333 16.752 1.00 13.00 ATOM 2753 CG LEU B 64 15.282 81.334 17.661 1.00 14.23 ATOM 2754 CD1 LEU B 64 16.108 82.568 17.390 1.00 15.48 ATOM 2755 CD2 LEU B 64 14.821 81.340 19.088 1.00 14.92 ATOM 2756 N LEU B 65 10.966 80.672 16.576 1.00 13.37 ATOM 2757 CA LEU B 65 9.776 81.204 15.967 1.00 13.56 ATOM 2758 C LEU B 65 9.621 82.670 16.352 1.00 14.34 ATOM 2759 O LEU B 65 9.610 83.005 17.520 1.00 14.41 ATOM 2760 CB LEU B 65 8.564 80.397 16.444 1.00 13.03 ATOM 2761 CG LEU B 65 7.221 80.858 15.900 1.00 14.60 ATOM 2762 CD1 LEU B 65 7.130 80.595 14.422 1.00 15.75 ATOM 2763 CD2 LEU B 65 6.116 80.127 16.636 1.00 15.18 ATOM 2764 N TYR B 66 9.514 83.535 15.349 1.00 15.34 ATOM 2765 CA TYR B 66 9.191 84.937 15.577 1.00 16.26 ATOM 2766 C TYR B 66 7.772 85.134 15.146 1.00 16.32 ATOM 2767 O TYR B 66 7.339 84.540 14.173 1.00 15.83 ATOM 2768 CB TYR B 66 10.096 85.847 14.756 1.00 16.46 ATOM 2769 CG TYR B 66 11.490 85.934 15.310 1.00 16.49 ATOM 2770 CD1 TYR B 66 12.373 84.858 15.198 1.00 15.60 ATOM 2771 CD2 TYR B 66 11.922 87.085 15.964 1.00 17.58 ATOM 2772 CE1 TYR B 66 13.643 84.929 15.720 1.00 17.20 ATOM 2773 CE2 TYR B 66 13.206 87.169 16.483 1.00 16.92 ATOM 2774 CZ TYR B 66 14.054 86.085 16.348 1.00 17.89 ATOM 2775 OH TYR B 66 15.330 86.135 16.843 1.00 19.40 ATOM 2776 N TYR B 67 7.025 85.932 15.880 1.00 17.11 ATOM 2777 CA TYR B 67 5.605 86.010 15.592 1.00 18.16 ATOM 2778 C TYR B 67 5.031 87.322 16.057 1.00 19.34 ATOM 2779 O TYR B 67 5.498 87.918 17.018 1.00 18.68 ATOM 2780 CB TYR B 67 4.861 84.831 16.249 1.00 18.64 ATOM 2781 CG TYR B 67 5.097 84.710 17.737 1.00 18.84 ATOM 2782 CD1 TYR B 67 6.238 84.078 18.238 1.00 19.17 ATOM 2783 CD2 TYR B 67 4.184 85.240 18.644 1.00 19.74 ATOM 2784 CE1 TYR B 67 6.455 83.980 19.601 1.00 19.34 ATOM 2785 CE2 TYR B 67 4.393 85.148 20.001 1.00 20.12 ATOM 2786 CZ TYR B 67 5.528 84.515 20.480 1.00 20.05 ATOM 2787 OH TYR B 67 5.727 84.435 21.837 1.00 22.36 ATOM 2788 N THR B 68 3.991 87.753 15.359 1.00 19.95 ATOM 2789 CA THR B 68 3.286 88.957 15.733 1.00 21.72 ATOM 2790 C THR B 68 1.836 88.778 15.349 1.00 22.57 ATOM 2791 O THR B 68 1.524 88.094 14.382 1.00 21.64 ATOM 2792 CB THR B 68 3.897 90.228 15.080 1.00 22.04 ATOM 2793 OG1 THR B 68 3.276 91.393 15.638 1.00 23.98 ATOM 2794 CG2 THR B 68 3.723 90.238 13.567 1.00 22.92 ATOM 2795 N GLU B 69 0.958 89.379 16.143 1.00 24.10 ATOM 2796 CA GLU B 69 -0.449 89.465 15.813 1.00 26.15 ATOM 2797 C GLU B 69 -0.540 90.335 14.566 1.00 26.47 ATOM 2798 O GLU B 69 0.145 91.361 14.471 1.00 26.79 ATOM 2799 CB GLU B 69 -1.176 90.125 16.979 1.00 26.65 ATOM 2800 CG GLU B 69 -2.658 89.861 17.091 1.00 30.51 ATOM 2801 CD GLU B 69 -3.154 90.115 18.505 1.00 34.15 ATOM 2802 OE1 GLU B 69 -2.738 89.368 19.418 1.00 36.11 ATOM 2803 OE2 GLU B 69 -3.948 91.065 18.712 1.00 37.50 ATOM 2804 N PHE B 70 -1.337 89.907 13.594 1.00 26.88 ATOM 2805 CA PHE B 70 -1.568 90.708 12.394 1.00 27.10 ATOM 2806 C PHE B 70 -2.951 90.454 11.813 1.00 28.13 ATOM 2807 O PHE B 70 -3.536 89.386 12.000 1.00 28.00 ATOM 2808 CB PHE B 70 -0.446 90.515 11.348 1.00 26.36 ATOM 2809 CG PHE B 70 -0.632 89.341 10.416 1.00 25.43 ATOM 2810 CD1 PHE B 70 -0.903 88.058 10.893 1.00 23.54 ATOM 2811 CD2 PHE B 70 -0.470 89.516 9.045 1.00 23.71 ATOM 2812 CE1 PHE B 70 -1.045 86.992 10.019 1.00 23.84 ATOM 2813 CE2 PHE B 70 -0.609 88.453 8.168 1.00 23.43 ATOM 2814 CZ PHE B 70 -0.894 87.184 8.658 1.00 24.85 ATOM 2815 N THR B 71 -3.483 91.459 11.134 1.00 29.22 ATOM 2816 CA THR B 71 -4.734 91.288 10.430 1.00 30.23 ATOM 2817 C THR B 71 -4.428 91.404 8.948 1.00 30.78 ATOM 2818 O THR B 71 -4.255 92.512 8.438 1.00 30.98 ATOM 2819 CB THR B 71 -5.789 92.293 10.912 1.00 30.23 ATOM 2820 OG1 THR B 71 -6.027 92.077 12.307 1.00 30.79 ATOM 2821 CG2 THR B 71 -7.092 92.105 10.161 1.00 30.98 ATOM 2822 N PRO B 72 -4.308 90.251 8.259 1.00 31.32 ATOM 2823 CA PRO B 72 -3.994 90.243 6.839 1.00 31.98 ATOM 2824 C PRO B 72 -5.079 90.943 6.034 1.00 32.80 ATOM 2825 O PRO B 72 -6.261 90.850 6.364 1.00 32.78 ATOM 2826 CB PRO B 72 -3.949 88.750 6.490 1.00 31.98 ATOM 2827 CG PRO B 72 -4.695 88.073 7.570 1.00 31.36 ATOM 2828 CD PRO B 72 -4.454 88.884 8.790 1.00 31.41 ATOM 2829 N THR B 73 -4.660 91.669 5.008 1.00 33.66 ATOM 2830 CA THR B 73 -5.586 92.278 4.066 1.00 34.62 ATOM 2831 C THR B 73 -5.161 91.850 2.667 1.00 35.22 ATOM 2832 O THR B 73 -4.204 91.088 2.514 1.00 35.32 ATOM 2833 CB THR B 73 -5.591 93.815 4.184 1.00 34.46 ATOM 2834 OG1 THR B 73 -4.257 94.307 4.034 1.00 34.92 ATOM 2835 CG2 THR B 73 -6.143 94.264 5.533 1.00 34.73 ATOM 2836 N GLU B 74 -5.875 92.318 1.646 1.00 35.97 ATOM 2837 CA GLU B 74 -5.537 91.965 0.273 1.00 36.65 ATOM 2838 C GLU B 74 -4.242 92.648 -0.169 1.00 36.59 ATOM 2839 O GLU B 74 -3.424 92.045 -0.869 1.00 36.89 ATOM 2840 CB GLU B 74 -6.682 92.328 -0.682 1.00 36.83 ATOM 2841 CG GLU B 74 -6.586 91.656 -2.051 1.00 38.22 ATOM 2842 CD GLU B 74 -7.243 92.461 -3.165 1.00 40.30 ATOM 2843 OE1 GLU B 74 -7.520 93.666 -2.964 1.00 41.33 ATOM 2844 OE2 GLU B 74 -7.471 91.885 -4.250 1.00 41.41 ATOM 2845 N LYS B 75 -4.064 93.896 0.259 1.00 36.64 ATOM 2846 CA LYS B 75 -2.980 94.750 -0.235 1.00 36.64 ATOM 2847 C LYS B 75 -1.693 94.657 0.588 1.00 36.00 ATOM 2848 O LYS B 75 -0.597 94.682 0.025 1.00 35.99 ATOM 2849 CB LYS B 75 -3.442 96.215 -0.356 1.00 36.72 ATOM 2850 CG LYS B 75 -3.973 96.851 0.941 1.00 37.33 ATOM 2851 CD LYS B 75 -4.544 98.257 0.719 1.00 37.78 ATOM 2852 CE LYS B 75 -5.948 98.221 0.096 1.00 39.82 ATOM 2853 NZ LYS B 75 -6.630 99.554 0.141 1.00 40.84 ATOM 2854 N ASP B 76 -1.835 94.552 1.909 1.00 35.23 ATOM 2855 CA ASP B 76 -0.685 94.556 2.809 1.00 34.36 ATOM 2856 C ASP B 76 0.254 93.391 2.547 1.00 33.60 ATOM 2857 O ASP B 76 -0.162 92.232 2.484 1.00 33.39 ATOM 2858 CB ASP B 76 -1.127 94.569 4.272 1.00 34.69 ATOM 2859 CG ASP B 76 -1.702 95.908 4.698 1.00 35.30 ATOM 2860 OD1 ASP B 76 -1.176 96.956 4.263 1.00 36.85 ATOM 2861 OD2 ASP B 76 -2.674 95.911 5.480 1.00 36.28 ATOM 2862 N GLU B 77 1.524 93.725 2.363 1.00 32.42 ATOM 2863 CA GLU B 77 2.554 92.733 2.139 1.00 31.50 ATOM 2864 C GLU B 77 3.290 92.491 3.441 1.00 29.77 ATOM 2865 O GLU B 77 3.649 93.431 4.154 1.00 29.30 ATOM 2866 CB GLU B 77 3.529 93.197 1.056 1.00 31.63 ATOM 2867 CG GLU B 77 2.926 93.236 -0.345 1.00 33.16 ATOM 2868 CD GLU B 77 3.911 93.719 -1.395 1.00 33.47 ATOM 2869 OE1 GLU B 77 4.709 94.641 -1.098 1.00 37.18 ATOM 2870 OE2 GLU B 77 3.885 93.182 -2.524 1.00 37.01 ATOM 2871 N TYR B 78 3.493 91.219 3.758 1.00 28.04 ATOM 2872 CA TYR B 78 4.248 90.866 4.941 1.00 26.59 ATOM 2873 C TYR B 78 5.465 90.077 4.546 1.00 25.22 ATOM 2874 O TYR B 78 5.472 89.373 3.533 1.00 24.69 ATOM 2875 CB TYR B 78 3.377 90.110 5.945 1.00 26.61 ATOM 2876 CG TYR B 78 2.348 91.001 6.584 1.00 26.57 ATOM 2877 CD1 TYR B 78 2.668 91.770 7.698 1.00 26.62 ATOM 2878 CD2 TYR B 78 1.061 91.106 6.057 1.00 26.08 ATOM 2879 CE1 TYR B 78 1.734 92.602 8.291 1.00 27.31 ATOM 2880 CE2 TYR B 78 0.117 91.946 6.639 1.00 26.82 ATOM 2881 CZ TYR B 78 0.461 92.691 7.757 1.00 27.22 ATOM 2882 OH TYR B 78 -0.455 93.530 8.364 1.00 27.83 ATOM 2883 N ALA B 79 6.513 90.221 5.347 1.00 23.88 ATOM 2884 CA ALA B 79 7.760 89.558 5.056 1.00 22.40 ATOM 2885 C ALA B 79 8.510 89.326 6.336 1.00 21.23 ATOM 2886 O ALA B 79 8.256 89.968 7.350 1.00 20.70 ATOM 2887 CB ALA B 79 8.601 90.390 4.101 1.00 23.10 ATOM 2888 N CYS B 80 9.447 88.399 6.253 1.00 20.43 ATOM 2889 CA CYS B 80 10.366 88.164 7.329 1.00 20.19 ATOM 2890 C CYS B 80 11.760 88.455 6.812 1.00 20.04 ATOM 2891 O CYS B 80 12.150 87.933 5.771 1.00 20.88 ATOM 2892 CB CYS B 80 10.245 86.718 7.768 1.00 19.99 ATOM 2893 SG CYS B 80 11.342 86.307 9.100 1.00 18.87 ATOM 2894 N ARG B 81 12.491 89.293 7.539 1.00 20.49 ATOM 2895 CA ARG B 81 13.836 89.666 7.153 1.00 20.69 ATOM 2896 C ARG B 81 14.787 89.010 8.136 1.00 20.11 ATOM 2897 O ARG B 81 14.701 89.247 9.336 1.00 21.33 ATOM 2898 CB ARG B 81 14.002 91.186 7.179 1.00 21.37 ATOM 2899 CG ARG B 81 15.402 91.658 6.829 1.00 22.39 ATOM 2900 CD ARG B 81 15.448 93.174 6.677 1.00 23.87 ATOM 2901 NE ARG B 81 15.099 93.880 7.908 1.00 27.26 ATOM 2902 CZ ARG B 81 14.583 95.106 7.949 1.00 27.54 ATOM 2903 NH1 ARG B 81 14.351 95.771 6.822 1.00 28.85 ATOM 2904 NH2 ARG B 81 14.295 95.669 9.115 1.00 29.35 ATOM 2905 N VAL B 82 15.686 88.193 7.604 1.00 20.20 ATOM 2906 CA VAL B 82 16.585 87.422 8.449 1.00 19.90 ATOM 2907 C VAL B 82 18.022 87.760 8.130 1.00 20.23 ATOM 2908 O VAL B 82 18.440 87.726 6.966 1.00 20.58 ATOM 2909 CB VAL B 82 16.350 85.903 8.280 1.00 19.62 ATOM 2910 CG1 VAL B 82 17.363 85.073 9.101 1.00 19.79 ATOM 2911 CG2 VAL B 82 14.930 85.548 8.677 1.00 18.65 ATOM 2912 N ASN B 83 18.771 88.090 9.172 1.00 20.54 ATOM 2913 CA ASN B 83 20.207 88.175 9.040 1.00 20.68 ATOM 2914 C ASN B 83 20.892 87.199 9.974 1.00 20.40 ATOM 2915 O ASN B 83 20.466 86.984 11.117 1.00 19.83 ATOM 2916 CB ASN B 83 20.729 89.595 9.247 1.00 21.60 ATOM 2917 CG ASN B 83 21.996 89.866 8.441 1.00 23.04 ATOM 2918 OD1 ASN B 83 22.534 88.975 7.767 1.00 22.36 ATOM 2919 ND2 ASN B 83 22.467 91.109 8.489 1.00 24.84 ATOM 2920 N HIS B 84 21.966 86.625 9.464 1.00 20.14 ATOM 2921 CA HIS B 84 22.722 85.621 10.168 1.00 19.75 ATOM 2922 C HIS B 84 24.133 85.713 9.609 1.00 20.53 ATOM 2923 O HIS B 84 24.331 86.189 8.483 1.00 20.79 ATOM 2924 CB HIS B 84 22.098 84.260 9.879 1.00 19.53 ATOM 2925 CG HIS B 84 22.715 83.134 10.644 1.00 16.90 ATOM 2926 ND1 HIS B 84 23.587 82.239 10.066 1.00 16.71 ATOM 2927 CD2 HIS B 84 22.596 82.763 11.941 1.00 16.44 ATOM 2928 CE1 HIS B 84 23.970 81.353 10.971 1.00 17.46 ATOM 2929 NE2 HIS B 84 23.384 81.651 12.117 1.00 16.36 ATOM 2930 N VAL B 85 25.108 85.255 10.383 1.00 20.63 ATOM 2931 CA VAL B 85 26.512 85.331 9.975 1.00 21.34 ATOM 2932 C VAL B 85 26.752 84.658 8.615 1.00 22.07 ATOM 2933 O VAL B 85 27.606 85.097 7.838 1.00 22.49 ATOM 2934 CB VAL B 85 27.438 84.754 11.076 1.00 21.38 ATOM 2935 CG1 VAL B 85 27.211 83.253 11.247 1.00 21.55 ATOM 2936 CG2 VAL B 85 28.904 85.058 10.776 1.00 22.22 ATOM 2937 N THR B 86 25.975 83.618 8.312 1.00 21.81 ATOM 2938 CA THR B 86 26.074 82.892 7.043 1.00 22.59 ATOM 2939 C THR B 86 25.547 83.688 5.846 1.00 23.75 ATOM 2940 O THR B 86 25.717 83.270 4.699 1.00 24.59 ATOM 2941 CB THR B 86 25.286 81.572 7.082 1.00 22.57 ATOM 2942 OG1 THR B 86 23.926 81.848 7.451 1.00 20.84 ATOM 2943 CG2 THR B 86 25.910 80.587 8.065 1.00 21.53 ATOM 2944 N LEU B 87 24.886 84.809 6.123 1.00 24.86 ATOM 2945 CA LEU B 87 24.275 85.629 5.079 1.00 26.20 ATOM 2946 C LEU B 87 25.050 86.927 4.873 1.00 27.19 ATOM 2947 O LEU B 87 25.265 87.685 5.818 1.00 27.58 ATOM 2948 CB LEU B 87 22.817 85.934 5.431 1.00 25.85 ATOM 2949 CG LEU B 87 21.894 84.719 5.592 1.00 26.02 ATOM 2950 CD1 LEU B 87 20.563 85.142 6.169 1.00 26.28 ATOM 2951 CD2 LEU B 87 21.697 83.981 4.279 1.00 26.13 ATOM 2952 N SER B 88 25.464 87.172 3.631 1.00 28.82 ATOM 2953 CA SER B 88 26.163 88.412 3.271 1.00 30.07 ATOM 2954 C SER B 88 25.240 89.622 3.358 1.00 30.43 ATOM 2955 O SER B 88 25.677 90.732 3.670 1.00 30.83 ATOM 2956 CB SER B 88 26.761 88.303 1.866 1.00 30.21 ATOM 2957 OG SER B 88 25.805 87.823 0.943 1.00 31.85 ATOM 2958 N GLN B 89 23.960 89.387 3.086 1.00 30.69 ATOM 2959 CA GLN B 89 22.929 90.406 3.185 1.00 31.07 ATOM 2960 C GLN B 89 21.669 89.767 3.764 1.00 30.40 ATOM 2961 O GLN B 89 21.481 88.554 3.623 1.00 30.39 ATOM 2962 CB GLN B 89 22.647 91.021 1.806 1.00 31.16 ATOM 2963 CG GLN B 89 22.308 90.012 0.704 1.00 32.25 ATOM 2964 CD GLN B 89 22.197 90.650 -0.678 1.00 32.68 ATOM 2965 OE1 GLN B 89 22.224 89.955 -1.696 1.00 35.19 ATOM 2966 NE2 GLN B 89 22.068 91.974 -0.719 1.00 34.76 ATOM 2967 N PRO B 90 20.814 90.571 4.425 1.00 30.16 ATOM 2968 CA PRO B 90 19.581 90.018 4.978 1.00 29.84 ATOM 2969 C PRO B 90 18.737 89.322 3.915 1.00 29.94 ATOM 2970 O PRO B 90 18.595 89.818 2.794 1.00 29.89 ATOM 2971 CB PRO B 90 18.860 91.252 5.530 1.00 29.93 ATOM 2972 CG PRO B 90 19.960 92.221 5.832 1.00 29.98 ATOM 2973 CD PRO B 90 20.937 92.013 4.714 1.00 30.34 ATOM 2974 N LYS B 91 18.217 88.153 4.262 1.00 29.57 ATOM 2975 CA LYS B 91 17.344 87.411 3.377 1.00 29.87 ATOM 2976 C LYS B 91 15.916 87.804 3.718 1.00 29.36 ATOM 2977 O LYS B 91 15.505 87.743 4.879 1.00 29.35 ATOM 2978 CB LYS B 91 17.554 85.906 3.556 1.00 29.91 ATOM 2979 CG LYS B 91 16.953 85.051 2.445 1.00 30.97 ATOM 2980 CD LYS B 91 17.193 83.561 2.675 1.00 30.79 ATOM 2981 CE LYS B 91 18.609 83.135 2.313 1.00 32.47 ATOM 2982 NZ LYS B 91 18.785 81.660 2.383 1.00 33.56 ATOM 2983 N ILE B 92 15.174 88.247 2.711 1.00 29.15 ATOM 2984 CA ILE B 92 13.775 88.587 2.900 1.00 28.88 ATOM 2985 C ILE B 92 12.920 87.491 2.285 1.00 28.55 ATOM 2986 O ILE B 92 13.035 87.182 1.099 1.00 28.71 ATOM 2987 CB ILE B 92 13.422 89.984 2.328 1.00 28.98 ATOM 2988 CG1 ILE B 92 14.145 91.076 3.125 1.00 28.68 ATOM 2989 CG2 ILE B 92 11.916 90.208 2.387 1.00 28.95 ATOM 2990 CD1 ILE B 92 14.137 92.466 2.488 1.00 29.56 ATOM 2991 N VAL B 93 12.094 86.869 3.117 1.00 27.69 ATOM 2992 CA VAL B 93 11.148 85.885 2.634 1.00 27.10 ATOM 2993 C VAL B 93 9.756 86.476 2.794 1.00 26.51 ATOM 2994 O VAL B 93 9.344 86.864 3.888 1.00 25.53 ATOM 2995 CB VAL B 93 11.293 84.523 3.362 1.00 27.05 ATOM 2996 CG1 VAL B 93 10.298 83.510 2.816 1.00 27.42 ATOM 2997 CG2 VAL B 93 12.708 83.991 3.199 1.00 27.25 ATOM 2998 N LYS B 94 9.062 86.584 1.669 1.00 26.86 ATOM 2999 CA LYS B 94 7.743 87.179 1.639 1.00 27.32 ATOM 3000 C LYS B 94 6.715 86.196 2.145 1.00 26.70 ATOM 3001 O LYS B 94 6.807 84.995 1.878 1.00 27.05 ATOM 3002 CB LYS B 94 7.380 87.593 0.217 1.00 27.60 ATOM 3003 CG LYS B 94 8.192 88.762 -0.315 1.00 29.79 ATOM 3004 CD LYS B 94 7.983 88.950 -1.817 1.00 32.50 ATOM 3005 CE LYS B 94 6.556 89.382 -2.142 1.00 34.69 ATOM 3006 NZ LYS B 94 6.359 89.660 -3.601 1.00 36.26 ATOM 3007 N TRP B 95 5.734 86.707 2.876 1.00 26.22 ATOM 3008 CA TRP B 95 4.634 85.869 3.293 1.00 26.06 ATOM 3009 C TRP B 95 3.774 85.508 2.092 1.00 26.67 ATOM 3010 O TRP B 95 3.224 86.387 1.419 1.00 26.29 ATOM 3011 CB TRP B 95 3.790 86.559 4.352 1.00 25.67 ATOM 3012 CG TRP B 95 2.606 85.753 4.744 1.00 25.32 ATOM 3013 CD1 TRP B 95 2.591 84.435 5.121 1.00 25.33 ATOM 3014 CD2 TRP B 95 1.254 86.205 4.807 1.00 25.19 ATOM 3015 NE1 TRP B 95 1.308 84.043 5.411 1.00 24.38 ATOM 3016 CE2 TRP B 95 0.467 85.110 5.228 1.00 24.69 ATOM 3017 CE3 TRP B 95 0.627 87.431 4.544 1.00 26.18 ATOM 3018 CZ2 TRP B 95 -0.914 85.204 5.401 1.00 25.72 ATOM 3019 CZ3 TRP B 95 -0.747 87.526 4.715 1.00 25.96 ATOM 3020 CH2 TRP B 95 -1.504 86.416 5.138 1.00 26.33 ATOM 3021 N ASP B 96 3.695 84.210 1.824 1.00 27.24 ATOM 3022 CA ASP B 96 2.815 83.659 0.802 1.00 28.16 ATOM 3023 C ASP B 96 1.765 82.836 1.531 1.00 28.70 ATOM 3024 O ASP B 96 2.069 81.791 2.123 1.00 28.62 ATOM 3025 CB ASP B 96 3.605 82.785 -0.178 1.00 28.14 ATOM 3026 CG ASP B 96 2.753 82.256 -1.325 1.00 28.64 ATOM 3027 OD1 ASP B 96 1.514 82.168 -1.193 1.00 30.06 ATOM 3028 OD2 ASP B 96 3.340 81.909 -2.369 1.00 31.10 ATOM 3029 N ARG B 97 0.530 83.316 1.481 1.00 29.24 ATOM 3030 CA ARG B 97 -0.578 82.720 2.225 1.00 30.19 ATOM 3031 C ARG B 97 -0.892 81.259 1.845 1.00 30.14 ATOM 3032 O ARG B 97 -1.601 80.564 2.571 1.00 30.51 ATOM 3033 CB ARG B 97 -1.786 83.672 2.151 1.00 30.38 ATOM 3034 CG ARG B 97 -3.150 83.097 1.804 1.00 32.71 ATOM 3035 CD ARG B 97 -3.963 84.111 0.985 1.00 34.70 ATOM 3036 NE ARG B 97 -3.587 85.505 1.255 1.00 36.00 ATOM 3037 CZ ARG B 97 -4.310 86.371 1.963 1.00 36.16 ATOM 3038 NH1 ARG B 97 -5.477 86.013 2.489 1.00 36.42 ATOM 3039 NH2 ARG B 97 -3.867 87.609 2.138 1.00 36.22 ATOM 3040 N ASP B 98 -0.320 80.782 0.740 1.00 30.34 ATOM 3041 CA ASP B 98 -0.531 79.402 0.293 1.00 30.62 ATOM 3042 C ASP B 98 0.643 78.470 0.596 1.00 30.41 ATOM 3043 O ASP B 98 0.735 77.373 0.039 1.00 29.79 ATOM 3044 CB ASP B 98 -0.855 79.370 -1.206 1.00 30.78 ATOM 3045 CG ASP B 98 -2.180 80.030 -1.526 1.00 32.00 ATOM 3046 OD1 ASP B 98 -3.190 79.688 -0.875 1.00 34.05 ATOM 3047 OD2 ASP B 98 -2.210 80.900 -2.423 1.00 34.15 ATOM 3048 N MET B 99 1.541 78.901 1.475 1.00 30.54 ATOM 3049 CA MET B 99 2.702 78.079 1.823 1.00 31.44 ATOM 3050 C MET B 99 3.001 78.034 3.319 1.00 30.69 ATOM 3051 O MET B 99 4.024 77.477 3.723 1.00 29.54 ATOM 3052 CB MET B 99 3.936 78.542 1.055 1.00 31.37 ATOM 3053 CG MET B 99 4.021 78.011 -0.370 1.00 32.60 ATOM 3054 SD MET B 99 5.402 78.774 -1.215 1.00 34.92 ATOM 3055 CE MET B 99 6.792 77.924 -0.465 1.00 35.50 TER 3056 MET B 99 ATOM 3057 N ILE C 1 12.232 67.917 35.701 1.00 13.28 ATOM 3058 CA ILE C 1 13.219 68.581 36.576 1.00 13.89 ATOM 3059 C ILE C 1 14.584 68.463 35.924 1.00 14.04 ATOM 3060 O ILE C 1 14.902 67.422 35.341 1.00 13.77 ATOM 3061 CB ILE C 1 13.213 67.961 37.983 1.00 14.63 ATOM 3062 CG1 ILE C 1 13.881 68.916 38.962 1.00 16.17 ATOM 3063 CG2 ILE C 1 13.857 66.561 37.985 1.00 16.03 ATOM 3064 CD1 ILE C 1 13.520 68.647 40.407 1.00 19.56 ATOM 3065 N SER C 2 15.381 69.523 36.020 1.00 12.92 ATOM 3066 CA SER C 2 16.656 69.565 35.329 1.00 12.68 ATOM 3067 C SER C 2 17.697 68.765 36.087 1.00 13.65 ATOM 3068 O SER C 2 17.641 68.647 37.306 1.00 13.80 ATOM 3069 CB SER C 2 17.103 71.003 35.087 1.00 12.58 ATOM 3070 OG SER C 2 17.197 71.701 36.319 1.00 12.90 ATOM 3071 N PRO C 3 18.649 68.182 35.359 1.00 12.91 ATOM 3072 CA PRO C 3 19.687 67.404 35.997 1.00 13.63 ATOM 3073 C PRO C 3 20.671 68.294 36.732 1.00 14.72 ATOM 3074 O PRO C 3 20.968 69.404 36.279 1.00 14.10 ATOM 3075 CB PRO C 3 20.367 66.702 34.823 1.00 13.44 ATOM 3076 CG PRO C 3 20.162 67.658 33.704 1.00 12.95 ATOM 3077 CD PRO C 3 18.792 68.192 33.893 1.00 13.16 ATOM 3078 N ARG C 4 21.143 67.798 37.870 1.00 17.07 ATOM 3079 CA ARG C 4 22.099 68.510 38.708 1.00 19.45 ATOM 3080 C ARG C 4 23.496 68.007 38.457 1.00 20.76 ATOM 3081 O ARG C 4 24.429 68.355 39.178 1.00 21.46 ATOM 3082 CB ARG C 4 21.780 68.289 40.182 1.00 20.23 ATOM 3083 CG ARG C 4 21.014 69.399 40.831 1.00 22.44 ATOM 3084 CD ARG C 4 19.634 69.465 40.269 1.00 24.21 ATOM 3085 NE ARG C 4 18.752 70.317 41.056 1.00 23.81 ATOM 3086 CZ ARG C 4 17.557 70.715 40.638 1.00 24.78 ATOM 3087 NH1 ARG C 4 17.114 70.349 39.435 1.00 17.79 ATOM 3088 NH2 ARG C 4 16.806 71.487 41.414 1.00 25.89 ATOM 3089 N THR C 5 23.623 67.162 37.443 1.00 21.40 ATOM 3090 CA THR C 5 24.877 66.537 37.100 1.00 21.69 ATOM 3091 C THR C 5 25.703 67.590 36.391 1.00 21.75 ATOM 3092 O THR C 5 25.495 67.849 35.202 1.00 21.62 ATOM 3093 CB THR C 5 24.616 65.338 36.195 1.00 21.94 ATOM 3094 OG1 THR C 5 23.660 65.713 35.187 1.00 21.99 ATOM 3095 CG2 THR C 5 24.044 64.178 37.019 1.00 22.97 ATOM 3096 N LEU C 6 26.598 68.225 37.146 1.00 22.18 ATOM 3097 CA LEU C 6 27.426 69.301 36.647 1.00 22.67 ATOM 3098 C LEU C 6 28.855 68.815 36.561 1.00 22.78 ATOM 3099 O LEU C 6 29.547 68.637 37.565 1.00 23.52 ATOM 3100 CB LEU C 6 27.324 70.544 37.527 1.00 22.30 ATOM 3101 CG LEU C 6 26.084 71.405 37.287 1.00 24.16 ATOM 3102 CD1 LEU C 6 26.333 72.767 37.896 1.00 25.34 ATOM 3103 CD2 LEU C 6 25.762 71.553 35.802 1.00 25.73 ATOM 3104 N ASP C 7 29.290 68.567 35.338 1.00 22.46 ATOM 3105 CA ASP C 7 30.594 67.975 35.138 1.00 22.15 ATOM 3106 C ASP C 7 31.430 68.837 34.245 1.00 20.87 ATOM 3107 O ASP C 7 31.014 69.194 33.140 1.00 21.20 ATOM 3108 CB ASP C 7 30.451 66.575 34.557 1.00 22.85 ATOM 3109 CG ASP C 7 29.666 65.664 35.469 1.00 24.29 ATOM 3110 OD1 ASP C 7 28.560 65.247 35.066 1.00 27.25 ATOM 3111 OD2 ASP C 7 30.133 65.400 36.603 1.00 26.25 ATOM 3112 N ALA C 8 32.616 69.175 34.728 1.00 18.99 ATOM 3113 CA ALA C 8 33.545 69.943 33.932 1.00 17.98 ATOM 3114 C ALA C 8 33.982 69.048 32.797 1.00 16.78 ATOM 3115 O ALA C 8 34.189 67.854 32.973 1.00 15.93 ATOM 3116 CB ALA C 8 34.749 70.347 34.771 1.00 19.00 ATOM 3117 N TRP C 9 34.158 69.645 31.633 1.00 15.67 ATOM 3118 CA TRP C 9 34.737 68.953 30.509 1.00 15.18 ATOM 3119 C TRP C 9 36.206 68.660 30.727 1.00 15.59 ATOM 3120 O TRP C 9 36.778 67.877 29.984 1.00 15.06 ATOM 3121 CB TRP C 9 34.547 69.802 29.266 1.00 14.54 ATOM 3122 CG TRP C 9 33.170 69.725 28.726 1.00 13.20 ATOM 3123 CD1 TRP C 9 32.040 69.297 29.379 1.00 14.45 ATOM 3124 CD2 TRP C 9 32.769 70.069 27.416 1.00 13.16 ATOM 3125 NE1 TRP C 9 30.953 69.364 28.540 1.00 14.95 ATOM 3126 CE2 TRP C 9 31.371 69.833 27.324 1.00 12.38 ATOM 3127 CE3 TRP C 9 33.447 70.562 26.300 1.00 11.66 ATOM 3128 CZ2 TRP C 9 30.658 70.064 26.161 1.00 13.93 ATOM 3129 CZ3 TRP C 9 32.723 70.787 25.140 1.00 13.18 ATOM 3130 CH2 TRP C 9 31.347 70.530 25.081 1.00 12.38 END