HEADER TRANSPORT PROTEIN 30-JAN-99 1B8E TITLE HIGH RESOLUTION CRYSTAL STRUCTURE OF THE BOVINE BETA- TITLE 2 LACTOGLOBULIN (ISOFORMS A AND B) IN ORTHOROMBIC SPACE GROUP COMPND MOL_ID: 1; COMPND 2 MOLECULE: PROTEIN (BETA-LACTOGLOBULIN); COMPND 3 CHAIN: A SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: BOS TAURUS; SOURCE 3 ORGANISM_COMMON: CATTLE; SOURCE 4 ORGANISM_TAXID: 9913; SOURCE 5 VARIANT: VARIANT B; SOURCE 6 ORGAN: BREAST; SOURCE 7 TISSUE: MAMMARY GLAND; SOURCE 8 SECRETION: MILK; SOURCE 9 OTHER_DETAILS: ALL REAGENTS WERE PURCHASED FROM SIGMA KEYWDS BETA-LACTOGLOBULIN, VARIANTS, LIPOCALIN, TRANSPORT PROTEIN EXPDTA X-RAY DIFFRACTION AUTHOR K.M.G.OLIVEIRA,L.SAWYER,I.POLIKARPOV REVDAT 3 24-FEB-09 1B8E 1 VERSN REVDAT 2 01-APR-03 1B8E 1 JRNL REVDAT 1 02-MAY-01 1B8E 0 JRNL AUTH K.M.OLIVEIRA,V.L.VALENTE-MESQUITA,M.M.BOTELHO, JRNL AUTH 2 L.SAWYER,S.T.FERREIRA,I.POLIKARPOV JRNL TITL CRYSTAL STRUCTURES OF BOVINE BETA-LACTOGLOBULIN IN JRNL TITL 2 THE ORTHORHOMBIC SPACE GROUP C222(1). STRUCTURAL JRNL TITL 3 DIFFERENCES BETWEEN GENETIC VARIANTS A AND B AND JRNL TITL 4 FEATURES OF THE TANFORD TRANSITION. JRNL REF EUR.J.BIOCHEM. V. 268 477 2001 JRNL REFN ISSN 0014-2956 JRNL PMID 11168385 REMARK 1 REMARK 2 REMARK 2 RESOLUTION. 1.95 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.95 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 9.50 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000 REMARK 3 COMPLETENESS FOR RANGE (%) : 85.0 REMARK 3 NUMBER OF REFLECTIONS : 9795 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) : NULL REMARK 3 R VALUE (WORKING SET) : 0.189 REMARK 3 FREE R VALUE : 0.252 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000 REMARK 3 FREE R VALUE TEST SET COUNT : 471 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 1197 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 0 REMARK 3 SOLVENT ATOMS : 104 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 25.18 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 42.46 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : NULL REMARK 3 B22 (A**2) : NULL REMARK 3 B33 (A**2) : NULL REMARK 3 B12 (A**2) : NULL REMARK 3 B13 (A**2) : NULL REMARK 3 B23 (A**2) : NULL REMARK 3 REMARK 3 ESTIMATED OVERALL COORDINATE ERROR. REMARK 3 ESU BASED ON R VALUE (A): 0.150 REMARK 3 ESU BASED ON FREE R VALUE (A): NULL REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): NULL REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. REMARK 3 DISTANCE RESTRAINTS. RMS SIGMA REMARK 3 BOND LENGTH (A) : 0.030 ; NULL REMARK 3 ANGLE DISTANCE (A) : 3.550 ; NULL REMARK 3 INTRAPLANAR 1-4 DISTANCE (A) : NULL ; NULL REMARK 3 H-BOND OR METAL COORDINATION (A) : NULL ; NULL REMARK 3 REMARK 3 PLANE RESTRAINT (A) : NULL ; NULL REMARK 3 CHIRAL-CENTER RESTRAINT (A**3) : NULL ; NULL REMARK 3 REMARK 3 NON-BONDED CONTACT RESTRAINTS. REMARK 3 SINGLE TORSION (A) : NULL ; NULL REMARK 3 MULTIPLE TORSION (A) : NULL ; NULL REMARK 3 H-BOND (X...Y) (A) : NULL ; NULL REMARK 3 H-BOND (X-H...Y) (A) : NULL ; NULL REMARK 3 REMARK 3 CONFORMATIONAL TORSION ANGLE RESTRAINTS. REMARK 3 SPECIFIED (DEGREES) : NULL ; NULL REMARK 3 PLANAR (DEGREES) : NULL ; NULL REMARK 3 STAGGERED (DEGREES) : NULL ; NULL REMARK 3 TRANSVERSE (DEGREES) : NULL ; NULL REMARK 3 REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1B8E COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-FEB-99. REMARK 100 THE RCSB ID CODE IS RCSB000410. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : SEP-97 REMARK 200 TEMPERATURE (KELVIN) : 291 REMARK 200 PH : 7.9 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : LNLS REMARK 200 BEAMLINE : D03B-MX1 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.38 REMARK 200 MONOCHROMATOR : SI REMARK 200 OPTICS : MIRRORS REMARK 200 REMARK 200 DETECTOR TYPE : IMAGE PLATE REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO REMARK 200 DATA SCALING SOFTWARE : SCALEPACK REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 9834 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.950 REMARK 200 RESOLUTION RANGE LOW (A) : 14.980 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 86.4 REMARK 200 DATA REDUNDANCY : 3.000 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : 0.08500 REMARK 200 FOR THE DATA SET : 9.2000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.95 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.00 REMARK 200 COMPLETENESS FOR SHELL (%) : 88.8 REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : 0.44000 REMARK 200 FOR SHELL : NULL REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: AMORE REMARK 200 STARTING MODEL: B-LG LATTICE Y FROM MIXTURE OF GENETIC VARIANTS REMARK 200 A AND B REMARK 200 REMARK 200 REMARK: DATA WERE COLLECTED USING OSCILLATION METHOD REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 41.00 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.10 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: METHOD IN PRESENCE OF AMMONIUM REMARK 280 SULPHATE 2.5 M, 180MM TRIZMA BUFFER AT A PROTEIN CONCENTRATION REMARK 280 OF 20MG/ML, PH 7.9, VAPOR DIFFUSION, HANGING DROP REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,-Y,Z+1/2 REMARK 290 3555 -X,Y,-Z+1/2 REMARK 290 4555 X,-Y,-Z REMARK 290 5555 X+1/2,Y+1/2,Z REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2 REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2 REMARK 290 8555 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 0.00000 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 33.43000 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 33.43000 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 27.82000 REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 40.82500 REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 27.82000 REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 40.82500 REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 33.43000 REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 27.82000 REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 40.82500 REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 33.43000 REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 27.82000 REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 40.82500 REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A 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 350 BIOMT1 2 -1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 33.43000 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 PRO A 153 REMARK 465 THR A 154 REMARK 465 GLN A 155 REMARK 465 LEU A 156 REMARK 465 GLU A 157 REMARK 465 GLU A 158 REMARK 465 GLN A 159 REMARK 465 CYS A 160 REMARK 465 HIS A 161 REMARK 465 ILE A 162 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT REMARK 500 REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT. REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE REMARK 500 O HOH A 166 O HOH A 255 2.08 REMARK 500 O HOH A 164 O HOH A 258 2.14 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND ANGLES REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1) REMARK 500 REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3 REMARK 500 ASP A 11 CB - CG - OD2 ANGL. DEV. = -6.0 DEGREES REMARK 500 ARG A 40 NE - CZ - NH2 ANGL. DEV. = -3.6 DEGREES REMARK 500 ASP A 53 CB - CG - OD2 ANGL. DEV. = -5.8 DEGREES REMARK 500 ARG A 124 NE - CZ - NH2 ANGL. DEV. = 3.3 DEGREES REMARK 500 ARG A 148 CD - NE - CZ ANGL. DEV. = 11.8 DEGREES REMARK 500 ARG A 148 NE - CZ - NH1 ANGL. DEV. = 4.1 DEGREES REMARK 500 ARG A 148 NE - CZ - NH2 ANGL. DEV. = -3.5 DEGREES REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 ASP A 33 -81.76 -46.44 REMARK 500 TYR A 99 -38.08 65.49 REMARK 500 LYS A 101 -49.65 -135.21 REMARK 500 PRO A 113 -89.88 -49.58 REMARK 500 GLU A 114 -82.46 -86.05 REMARK 500 GLN A 115 87.51 -154.69 REMARK 500 PRO A 126 24.43 -71.93 REMARK 500 GLU A 127 157.49 -47.38 REMARK 500 VAL A 128 42.64 -93.00 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 525 REMARK 525 M RES CSSEQI REMARK 525 HOH A 225 DISTANCE = 6.44 ANGSTROMS REMARK 525 HOH A 245 DISTANCE = 5.72 ANGSTROMS REMARK 525 HOH A 263 DISTANCE = 5.73 ANGSTROMS REMARK 999 REMARK 999 SEQUENCE REMARK 999 REMARK 999 THE VARIANT B DIFFERS IN PRIMARY AMINO ACID SEQUENCE FROM REMARK 999 VARIANT A AT THE POSITIONS 64 (GLU-->ASP) AND 118 REMARK 999 (ALA -->VAL) DBREF 1B8E A 1 162 UNP P02754 LACB_BOVIN 17 178 SEQRES 1 A 162 LEU ILE VAL THR GLN THR MET LYS GLY LEU ASP ILE GLN SEQRES 2 A 162 LYS VAL ALA GLY THR TRP TYR SER LEU ALA MET ALA ALA SEQRES 3 A 162 SER ASP ILE SER LEU LEU ASP ALA GLN SER ALA PRO LEU SEQRES 4 A 162 ARG VAL TYR VAL GLU GLU LEU LYS PRO THR PRO GLU GLY SEQRES 5 A 162 ASP LEU GLU ILE LEU LEU GLN LYS TRP GLU ASN GLY GLU SEQRES 6 A 162 CYS ALA GLN LYS LYS ILE ILE ALA GLU LYS THR LYS ILE SEQRES 7 A 162 PRO ALA VAL PHE LYS ILE ASP ALA LEU ASN GLU ASN LYS SEQRES 8 A 162 VAL LEU VAL LEU ASP THR ASP TYR LYS LYS TYR LEU LEU SEQRES 9 A 162 PHE CYS MET GLU ASN SER ALA GLU PRO GLU GLN SER LEU SEQRES 10 A 162 ALA CYS GLN CYS LEU VAL ARG THR PRO GLU VAL ASP ASP SEQRES 11 A 162 GLU ALA LEU GLU LYS PHE ASP LYS ALA LEU LYS ALA LEU SEQRES 12 A 162 PRO MET HIS ILE ARG LEU SER PHE ASN PRO THR GLN LEU SEQRES 13 A 162 GLU GLU GLN CYS HIS ILE FORMUL 2 HOH *104(H2 O) HELIX 1 1 ILE A 2 THR A 6 5 5 HELIX 2 2 ASP A 11 ALA A 16 5 6 HELIX 3 3 ASP A 28 ASP A 33 1 6 HELIX 4 4 ASP A 130 LEU A 140 1 11 HELIX 5 5 LYS A 141 LEU A 143 5 3 SHEET 1 A10 GLY A 17 THR A 18 0 SHEET 2 A10 TYR A 42 PRO A 48 -1 O LEU A 46 N GLY A 17 SHEET 3 A10 LEU A 54 GLU A 62 -1 O GLU A 55 N LYS A 47 SHEET 4 A10 GLU A 65 LYS A 75 -1 O GLU A 65 N GLU A 62 SHEET 5 A10 VAL A 81 ILE A 84 -1 O LYS A 83 N GLU A 74 SHEET 6 A10 ASN A 90 THR A 97 -1 O ASN A 90 N ILE A 84 SHEET 7 A10 TYR A 102 ASN A 109 -1 N LEU A 104 O ASP A 96 SHEET 8 A10 SER A 116 VAL A 123 -1 O SER A 116 N ASN A 109 SHEET 9 A10 TYR A 20 ALA A 26 -1 O TYR A 20 N VAL A 123 SHEET 10 A10 ILE A 147 SER A 150 -1 O ILE A 147 N ALA A 26 SSBOND 1 CYS A 106 CYS A 119 1555 1555 2.06 CRYST1 55.640 81.650 66.860 90.00 90.00 90.00 C 2 2 21 8 ORIGX1 1.000000 0.000000 0.000000 0.00000 ORIGX2 0.000000 1.000000 0.000000 0.00000 ORIGX3 0.000000 0.000000 1.000000 0.00000 SCALE1 0.017973 0.000000 0.000000 0.00000 SCALE2 0.000000 0.012247 0.000000 0.00000 SCALE3 0.000000 0.000000 0.014957 0.00000 ATOM 1 N LEU A 1 6.557 22.146 36.079 1.00 44.36 N ATOM 2 CA LEU A 1 7.098 20.874 35.478 1.00 45.52 C ATOM 3 C LEU A 1 7.719 20.099 36.638 1.00 44.22 C ATOM 4 O LEU A 1 7.981 20.764 37.665 1.00 45.23 O ATOM 5 CB LEU A 1 8.101 21.252 34.409 1.00 46.27 C ATOM 6 CG LEU A 1 8.138 20.624 33.022 1.00 48.05 C ATOM 7 CD1 LEU A 1 7.007 21.055 32.097 1.00 48.81 C ATOM 8 CD2 LEU A 1 9.477 20.920 32.339 1.00 48.31 C ATOM 9 N ILE A 2 8.000 18.808 36.512 1.00 42.60 N ATOM 10 CA ILE A 2 8.625 18.064 37.610 1.00 43.17 C ATOM 11 C ILE A 2 10.078 17.739 37.363 1.00 42.73 C ATOM 12 O ILE A 2 10.569 17.838 36.223 1.00 40.78 O ATOM 13 CB ILE A 2 7.872 16.756 37.939 1.00 44.38 C ATOM 14 CG1 ILE A 2 7.751 15.854 36.704 1.00 45.93 C ATOM 15 CG2 ILE A 2 6.496 17.056 38.500 1.00 45.11 C ATOM 16 CD1 ILE A 2 7.511 14.397 37.071 1.00 46.87 C ATOM 17 N VAL A 3 10.864 17.340 38.375 1.00 43.22 N ATOM 18 CA VAL A 3 12.283 17.088 38.131 1.00 45.31 C ATOM 19 C VAL A 3 12.544 15.977 37.129 1.00 45.89 C ATOM 20 O VAL A 3 13.597 15.908 36.494 1.00 46.08 O ATOM 21 CB VAL A 3 13.084 16.792 39.414 1.00 45.18 C ATOM 22 CG1 VAL A 3 12.710 17.780 40.499 1.00 46.16 C ATOM 23 CG2 VAL A 3 12.921 15.364 39.908 1.00 46.68 C ATOM 24 N THR A 4 11.608 15.042 37.008 1.00 47.17 N ATOM 25 CA THR A 4 11.747 13.939 36.078 1.00 47.83 C ATOM 26 C THR A 4 11.507 14.350 34.633 1.00 46.07 C ATOM 27 O THR A 4 11.744 13.451 33.801 1.00 48.18 O ATOM 28 CB THR A 4 10.808 12.768 36.444 1.00 49.03 C ATOM 29 OG1 THR A 4 9.612 12.834 35.652 1.00 50.89 O ATOM 30 CG2 THR A 4 10.410 12.800 37.914 1.00 50.04 C ATOM 31 N GLN A 5 11.076 15.553 34.266 1.00 42.97 N ATOM 32 CA GLN A 5 10.855 15.826 32.835 1.00 41.00 C ATOM 33 C GLN A 5 12.030 16.577 32.219 1.00 40.23 C ATOM 34 O GLN A 5 12.124 16.820 31.008 1.00 40.02 O ATOM 35 CB GLN A 5 9.534 16.545 32.569 1.00 43.55 C ATOM 36 CG GLN A 5 8.334 15.913 33.227 1.00 45.07 C ATOM 37 CD GLN A 5 7.100 16.706 33.530 1.00 46.80 C ATOM 38 OE1 GLN A 5 7.104 17.675 34.297 1.00 48.04 O ATOM 39 NE2 GLN A 5 5.936 16.301 33.000 1.00 46.43 N ATOM 40 N THR A 6 12.975 16.964 33.075 1.00 36.18 N ATOM 41 CA THR A 6 14.126 17.698 32.630 1.00 34.05 C ATOM 42 C THR A 6 15.310 16.756 32.414 1.00 34.54 C ATOM 43 O THR A 6 15.328 15.576 32.765 1.00 32.90 O ATOM 44 CB THR A 6 14.538 18.806 33.597 1.00 34.89 C ATOM 45 OG1 THR A 6 15.046 18.156 34.772 1.00 35.26 O ATOM 46 CG2 THR A 6 13.357 19.700 33.949 1.00 35.80 C ATOM 47 N MET A 7 16.340 17.342 31.827 1.00 33.85 N ATOM 48 CA MET A 7 17.472 16.500 31.501 1.00 37.42 C ATOM 49 C MET A 7 18.387 16.082 32.643 1.00 40.15 C ATOM 50 O MET A 7 18.924 16.884 33.396 1.00 40.00 O ATOM 51 CB MET A 7 18.353 17.163 30.454 1.00 36.18 C ATOM 52 CG MET A 7 18.862 16.034 29.542 1.00 38.06 C ATOM 53 SD MET A 7 20.089 16.694 28.413 1.00 37.56 S ATOM 54 CE MET A 7 20.666 15.171 27.663 1.00 38.98 C ATOM 55 N LYS A 8 18.684 14.783 32.602 1.00 42.72 N ATOM 56 CA LYS A 8 19.646 14.212 33.527 1.00 45.15 C ATOM 57 C LYS A 8 21.032 14.278 32.880 1.00 43.11 C ATOM 58 O LYS A 8 21.158 14.108 31.666 1.00 43.62 O ATOM 59 CB LYS A 8 19.336 12.745 33.847 1.00 49.44 C ATOM 60 CG LYS A 8 19.963 12.319 35.167 1.00 53.80 C ATOM 61 CD LYS A 8 20.653 10.967 35.075 1.00 57.09 C ATOM 62 CE LYS A 8 22.076 11.043 34.534 1.00 59.36 C ATOM 63 NZ LYS A 8 22.094 10.829 33.005 1.00 60.93 N ATOM 64 N GLY A 9 22.044 14.545 33.684 1.00 40.34 N ATOM 65 CA GLY A 9 23.416 14.573 33.212 1.00 37.55 C ATOM 66 C GLY A 9 23.743 15.694 32.249 1.00 35.89 C ATOM 67 O GLY A 9 24.709 15.539 31.483 1.00 36.82 O ATOM 68 N LEU A 10 22.994 16.789 32.172 1.00 32.92 N ATOM 69 CA LEU A 10 23.367 17.833 31.223 1.00 31.81 C ATOM 70 C LEU A 10 24.755 18.362 31.518 1.00 30.22 C ATOM 71 O LEU A 10 25.093 18.604 32.663 1.00 31.21 O ATOM 72 CB LEU A 10 22.322 18.958 31.331 1.00 29.01 C ATOM 73 CG LEU A 10 22.701 20.260 30.642 1.00 28.99 C ATOM 74 CD1 LEU A 10 22.616 20.108 29.133 1.00 28.15 C ATOM 75 CD2 LEU A 10 21.767 21.357 31.170 1.00 28.72 C ATOM 76 N ASP A 11 25.603 18.573 30.527 1.00 30.39 N ATOM 77 CA ASP A 11 26.905 19.209 30.592 1.00 31.30 C ATOM 78 C ASP A 11 26.650 20.562 29.884 1.00 29.27 C ATOM 79 O ASP A 11 26.753 20.647 28.659 1.00 27.65 O ATOM 80 CB ASP A 11 28.074 18.622 29.826 1.00 31.87 C ATOM 81 CG ASP A 11 29.387 19.355 29.947 1.00 34.66 C ATOM 82 OD1 ASP A 11 29.374 20.529 30.356 1.00 34.87 O ATOM 83 OD2 ASP A 11 30.359 18.639 29.634 1.00 34.51 O ATOM 84 N ILE A 12 26.396 21.582 30.669 1.00 28.97 N ATOM 85 CA ILE A 12 26.077 22.868 30.001 1.00 29.01 C ATOM 86 C ILE A 12 27.168 23.317 29.085 1.00 28.74 C ATOM 87 O ILE A 12 26.803 23.835 28.012 1.00 28.01 O ATOM 88 CB ILE A 12 25.585 23.823 31.110 1.00 30.99 C ATOM 89 CG1 ILE A 12 24.496 24.754 30.542 1.00 34.30 C ATOM 90 CG2 ILE A 12 26.698 24.558 31.826 1.00 30.45 C ATOM 91 CD1 ILE A 12 25.085 25.812 29.626 1.00 36.41 C ATOM 92 N GLN A 13 28.491 23.077 29.272 1.00 26.72 N ATOM 93 CA GLN A 13 29.478 23.568 28.345 1.00 24.62 C ATOM 94 C GLN A 13 29.316 23.019 26.938 1.00 24.49 C ATOM 95 O GLN A 13 29.738 23.736 26.029 1.00 23.96 O ATOM 96 CB GLN A 13 30.927 23.343 28.850 1.00 27.34 C ATOM 97 CG GLN A 13 31.167 23.713 30.307 1.00 27.65 C ATOM 98 CD GLN A 13 31.105 25.198 30.594 1.00 30.38 C ATOM 99 OE1 GLN A 13 30.721 25.701 31.665 1.00 31.81 O ATOM 100 NE2 GLN A 13 31.486 25.950 29.572 1.00 28.60 N ATOM 101 N LYS A 14 28.730 21.861 26.664 1.00 23.75 N ATOM 102 CA LYS A 14 28.569 21.338 25.321 1.00 25.01 C ATOM 103 C LYS A 14 27.440 21.970 24.504 1.00 25.10 C ATOM 104 O LYS A 14 27.381 21.748 23.294 1.00 23.05 O ATOM 105 CB LYS A 14 28.337 19.827 25.459 1.00 29.35 C ATOM 106 CG LYS A 14 29.599 19.096 25.958 1.00 34.00 C ATOM 107 CD LYS A 14 29.583 17.694 25.359 1.00 38.16 C ATOM 108 CE LYS A 14 29.828 16.643 26.420 1.00 40.28 C ATOM 109 NZ LYS A 14 31.297 16.504 26.670 1.00 41.88 N ATOM 110 N VAL A 15 26.559 22.787 25.110 1.00 23.45 N ATOM 111 CA VAL A 15 25.531 23.473 24.320 1.00 24.39 C ATOM 112 C VAL A 15 26.031 24.806 23.762 1.00 22.91 C ATOM 113 O VAL A 15 25.304 25.519 23.060 1.00 22.48 O ATOM 114 CB VAL A 15 24.220 23.801 25.082 1.00 25.25 C ATOM 115 CG1 VAL A 15 23.591 22.552 25.686 1.00 26.16 C ATOM 116 CG2 VAL A 15 24.421 24.877 26.148 1.00 25.06 C ATOM 117 N ALA A 16 27.260 25.232 24.034 1.00 22.05 N ATOM 118 CA ALA A 16 27.782 26.493 23.551 1.00 21.20 C ATOM 119 C ALA A 16 27.696 26.640 22.034 1.00 20.15 C ATOM 120 O ALA A 16 27.904 25.634 21.344 1.00 22.96 O ATOM 121 CB ALA A 16 29.290 26.635 23.857 1.00 21.59 C ATOM 122 N GLY A 17 27.362 27.826 21.575 1.00 20.21 N ATOM 123 CA GLY A 17 27.472 28.107 20.149 1.00 21.71 C ATOM 124 C GLY A 17 26.167 28.595 19.561 1.00 21.90 C ATOM 125 O GLY A 17 25.205 28.740 20.282 1.00 20.22 O ATOM 126 N THR A 18 26.101 28.562 18.225 1.00 22.02 N ATOM 127 CA THR A 18 24.901 29.061 17.558 1.00 23.20 C ATOM 128 C THR A 18 23.812 28.010 17.493 1.00 22.96 C ATOM 129 O THR A 18 24.059 26.790 17.512 1.00 21.24 O ATOM 130 CB THR A 18 25.200 29.655 16.168 1.00 27.53 C ATOM 131 OG1 THR A 18 24.360 29.163 15.100 1.00 31.53 O ATOM 132 CG2 THR A 18 26.630 29.515 15.772 1.00 23.84 C ATOM 133 N TRP A 19 22.586 28.478 17.558 1.00 21.85 N ATOM 134 CA TRP A 19 21.401 27.618 17.448 1.00 20.63 C ATOM 135 C TRP A 19 20.389 28.427 16.648 1.00 21.84 C ATOM 136 O TRP A 19 20.508 29.665 16.527 1.00 22.20 O ATOM 137 CB TRP A 19 20.809 27.367 18.862 1.00 20.47 C ATOM 138 CG TRP A 19 21.636 26.482 19.742 1.00 19.79 C ATOM 139 CD1 TRP A 19 22.606 26.817 20.636 1.00 20.07 C ATOM 140 CD2 TRP A 19 21.597 25.042 19.756 1.00 21.22 C ATOM 141 NE1 TRP A 19 23.167 25.702 21.189 1.00 20.28 N ATOM 142 CE2 TRP A 19 22.555 24.595 20.684 1.00 20.07 C ATOM 143 CE3 TRP A 19 20.844 24.096 19.054 1.00 19.89 C ATOM 144 CZ2 TRP A 19 22.785 23.240 20.956 1.00 21.81 C ATOM 145 CZ3 TRP A 19 21.048 22.763 19.308 1.00 20.07 C ATOM 146 CH2 TRP A 19 22.012 22.348 20.239 1.00 21.04 C ATOM 147 N TYR A 20 19.367 27.779 16.128 1.00 21.56 N ATOM 148 CA TYR A 20 18.260 28.418 15.454 1.00 25.07 C ATOM 149 C TYR A 20 16.940 27.918 16.070 1.00 23.85 C ATOM 150 O TYR A 20 16.860 26.713 16.340 1.00 23.82 O ATOM 151 CB TYR A 20 18.251 28.002 13.971 1.00 28.93 C ATOM 152 CG TYR A 20 19.460 28.505 13.207 1.00 34.09 C ATOM 153 CD1 TYR A 20 19.457 29.750 12.600 1.00 36.78 C ATOM 154 CD2 TYR A 20 20.612 27.732 13.135 1.00 35.66 C ATOM 155 CE1 TYR A 20 20.576 30.211 11.911 1.00 38.40 C ATOM 156 CE2 TYR A 20 21.732 28.175 12.457 1.00 38.20 C ATOM 157 CZ TYR A 20 21.693 29.417 11.846 1.00 39.10 C ATOM 158 OH TYR A 20 22.810 29.843 11.158 1.00 42.90 O ATOM 159 N SER A 21 15.982 28.786 16.303 1.00 24.32 N ATOM 160 CA SER A 21 14.685 28.413 16.865 1.00 24.56 C ATOM 161 C SER A 21 13.837 27.820 15.752 1.00 24.83 C ATOM 162 O SER A 21 13.420 28.604 14.880 1.00 25.48 O ATOM 163 CB SER A 21 14.049 29.689 17.429 1.00 27.22 C ATOM 164 OG SER A 21 14.596 30.064 18.693 1.00 29.19 O ATOM 165 N LEU A 22 13.537 26.532 15.690 1.00 21.02 N ATOM 166 CA LEU A 22 12.785 25.951 14.608 1.00 22.06 C ATOM 167 C LEU A 22 11.276 25.881 14.881 1.00 21.86 C ATOM 168 O LEU A 22 10.460 25.885 13.959 1.00 22.05 O ATOM 169 CB LEU A 22 13.321 24.526 14.400 1.00 25.32 C ATOM 170 CG LEU A 22 12.795 23.714 13.220 1.00 27.70 C ATOM 171 CD1 LEU A 22 13.047 24.390 11.876 1.00 29.60 C ATOM 172 CD2 LEU A 22 13.483 22.348 13.231 1.00 29.22 C ATOM 173 N ALA A 23 10.912 25.768 16.157 1.00 20.22 N ATOM 174 CA ALA A 23 9.478 25.628 16.474 1.00 20.55 C ATOM 175 C ALA A 23 9.253 26.062 17.913 1.00 21.77 C ATOM 176 O ALA A 23 10.178 25.985 18.739 1.00 17.99 O ATOM 177 CB ALA A 23 9.064 24.170 16.331 1.00 20.12 C ATOM 178 N MET A 24 8.028 26.533 18.168 1.00 20.87 N ATOM 179 CA MET A 24 7.711 26.974 19.506 1.00 22.04 C ATOM 180 C MET A 24 6.276 26.527 19.868 1.00 22.02 C ATOM 181 O MET A 24 5.483 26.386 18.931 1.00 20.35 O ATOM 182 CB MET A 24 7.661 28.504 19.559 1.00 23.53 C ATOM 183 CG MET A 24 8.820 29.371 19.238 1.00 31.44 C ATOM 184 SD MET A 24 8.562 31.153 19.171 1.00 35.46 S ATOM 185 CE MET A 24 10.197 31.680 18.661 1.00 36.53 C ATOM 186 N ALA A 25 6.002 26.467 21.169 1.00 20.82 N ATOM 187 CA ALA A 25 4.617 26.177 21.602 1.00 18.65 C ATOM 188 C ALA A 25 4.473 26.753 23.010 1.00 21.77 C ATOM 189 O ALA A 25 5.501 26.878 23.743 1.00 19.89 O ATOM 190 CB ALA A 25 4.346 24.692 21.685 1.00 19.61 C ATOM 191 N ALA A 26 3.210 27.056 23.327 1.00 17.17 N ATOM 192 CA ALA A 26 3.000 27.621 24.665 1.00 20.56 C ATOM 193 C ALA A 26 1.656 27.193 25.228 1.00 20.78 C ATOM 194 O ALA A 26 0.789 26.753 24.484 1.00 21.29 O ATOM 195 CB ALA A 26 3.110 29.138 24.505 1.00 19.18 C ATOM 196 N SER A 27 1.558 27.199 26.554 1.00 22.36 N ATOM 197 CA SER A 27 0.345 26.749 27.229 1.00 26.22 C ATOM 198 C SER A 27 -0.796 27.744 27.090 1.00 29.64 C ATOM 199 O SER A 27 -1.947 27.413 27.344 1.00 30.46 O ATOM 200 CB SER A 27 0.713 26.573 28.735 1.00 24.30 C ATOM 201 OG SER A 27 1.085 27.860 29.190 1.00 26.30 O ATOM 202 N ASP A 28 -0.505 28.993 26.771 1.00 31.57 N ATOM 203 CA ASP A 28 -1.423 30.073 26.605 1.00 35.06 C ATOM 204 C ASP A 28 -1.186 30.827 25.293 1.00 34.41 C ATOM 205 O ASP A 28 -0.075 31.315 25.049 1.00 32.03 O ATOM 206 CB ASP A 28 -1.357 31.102 27.754 1.00 39.83 C ATOM 207 CG ASP A 28 -2.462 32.116 27.457 1.00 43.98 C ATOM 208 OD1 ASP A 28 -3.641 31.705 27.378 1.00 47.05 O ATOM 209 OD2 ASP A 28 -2.177 33.301 27.237 1.00 46.68 O ATOM 210 N ILE A 29 -2.248 31.000 24.504 1.00 32.99 N ATOM 211 CA ILE A 29 -2.185 31.693 23.224 1.00 35.01 C ATOM 212 C ILE A 29 -1.446 33.019 23.325 1.00 34.56 C ATOM 213 O ILE A 29 -0.578 33.359 22.524 1.00 34.55 O ATOM 214 CB ILE A 29 -3.540 32.091 22.584 1.00 35.68 C ATOM 215 CG1 ILE A 29 -4.488 30.963 22.230 1.00 38.46 C ATOM 216 CG2 ILE A 29 -3.350 32.921 21.305 1.00 34.02 C ATOM 217 CD1 ILE A 29 -3.942 29.580 22.243 1.00 39.96 C ATOM 218 N SER A 30 -1.818 33.820 24.304 1.00 36.12 N ATOM 219 CA SER A 30 -1.237 35.134 24.518 1.00 39.00 C ATOM 220 C SER A 30 0.258 35.111 24.796 1.00 38.13 C ATOM 221 O SER A 30 0.874 36.164 24.681 1.00 39.07 O ATOM 222 CB SER A 30 -1.956 35.909 25.629 1.00 40.62 C ATOM 223 OG SER A 30 -1.538 35.470 26.912 1.00 42.69 O ATOM 224 N LEU A 31 0.874 33.999 25.159 1.00 38.13 N ATOM 225 CA LEU A 31 2.322 33.985 25.316 1.00 38.71 C ATOM 226 C LEU A 31 3.059 34.201 23.997 1.00 39.72 C ATOM 227 O LEU A 31 4.134 34.832 24.021 1.00 39.39 O ATOM 228 CB LEU A 31 2.734 32.671 25.990 1.00 38.28 C ATOM 229 CG LEU A 31 2.512 32.686 27.516 1.00 38.66 C ATOM 230 CD1 LEU A 31 2.907 31.342 28.098 1.00 38.81 C ATOM 231 CD2 LEU A 31 3.252 33.846 28.167 1.00 38.54 C ATOM 232 N LEU A 32 2.543 33.732 22.865 1.00 38.93 N ATOM 233 CA LEU A 32 3.219 33.841 21.582 1.00 40.71 C ATOM 234 C LEU A 32 2.437 34.521 20.460 1.00 45.35 C ATOM 235 O LEU A 32 2.867 34.500 19.296 1.00 44.17 O ATOM 236 CB LEU A 32 3.564 32.416 21.082 1.00 38.02 C ATOM 237 CG LEU A 32 4.598 31.617 21.887 1.00 36.75 C ATOM 238 CD1 LEU A 32 4.722 30.182 21.410 1.00 33.30 C ATOM 239 CD2 LEU A 32 5.949 32.334 21.841 1.00 36.08 C ATOM 240 N ASP A 33 1.270 35.099 20.754 1.00 49.44 N ATOM 241 CA ASP A 33 0.409 35.680 19.728 1.00 54.61 C ATOM 242 C ASP A 33 1.047 36.574 18.687 1.00 58.10 C ATOM 243 O ASP A 33 1.251 36.111 17.548 1.00 60.56 O ATOM 244 CB ASP A 33 -0.835 36.300 20.388 1.00 54.02 C ATOM 245 CG ASP A 33 -2.062 36.207 19.497 1.00 54.09 C ATOM 246 OD1 ASP A 33 -1.965 35.611 18.402 1.00 54.63 O ATOM 247 OD2 ASP A 33 -3.136 36.733 19.855 1.00 53.29 O ATOM 248 N ALA A 34 1.298 37.845 18.947 1.00 61.71 N ATOM 249 CA ALA A 34 1.912 38.694 17.925 1.00 64.33 C ATOM 250 C ALA A 34 3.416 38.790 18.147 1.00 66.33 C ATOM 251 O ALA A 34 3.961 38.478 19.212 1.00 65.64 O ATOM 252 CB ALA A 34 1.261 40.065 17.923 1.00 65.05 C ATOM 253 N GLN A 35 4.127 39.328 17.166 1.00 68.57 N ATOM 254 CA GLN A 35 5.558 39.542 17.172 1.00 70.77 C ATOM 255 C GLN A 35 6.139 40.152 18.441 1.00 70.33 C ATOM 256 O GLN A 35 7.316 39.941 18.746 1.00 70.84 O ATOM 257 CB GLN A 35 5.934 40.456 15.991 1.00 73.13 C ATOM 258 CG GLN A 35 5.646 39.866 14.625 1.00 75.76 C ATOM 259 CD GLN A 35 6.019 40.791 13.484 1.00 77.53 C ATOM 260 OE1 GLN A 35 6.503 41.900 13.705 1.00 78.18 O ATOM 261 NE2 GLN A 35 5.802 40.353 12.244 1.00 78.28 N ATOM 262 N SER A 36 5.405 40.935 19.205 1.00 69.00 N ATOM 263 CA SER A 36 5.827 41.591 20.412 1.00 67.32 C ATOM 264 C SER A 36 5.576 40.841 21.710 1.00 65.26 C ATOM 265 O SER A 36 6.003 41.316 22.776 1.00 65.81 O ATOM 266 CB SER A 36 5.080 42.939 20.486 1.00 68.71 C ATOM 267 OG SER A 36 3.717 42.746 20.111 1.00 69.24 O ATOM 268 N ALA A 37 4.935 39.682 21.662 1.00 61.62 N ATOM 269 CA ALA A 37 4.742 38.917 22.905 1.00 57.69 C ATOM 270 C ALA A 37 6.108 38.763 23.552 1.00 54.51 C ATOM 271 O ALA A 37 7.110 38.517 22.866 1.00 53.60 O ATOM 272 CB ALA A 37 4.100 37.589 22.543 1.00 57.97 C ATOM 273 N PRO A 38 6.205 38.913 24.871 1.00 50.98 N ATOM 274 CA PRO A 38 7.447 38.788 25.600 1.00 48.21 C ATOM 275 C PRO A 38 8.152 37.443 25.498 1.00 44.05 C ATOM 276 O PRO A 38 9.392 37.420 25.566 1.00 42.55 O ATOM 277 CB PRO A 38 7.103 39.114 27.045 1.00 49.78 C ATOM 278 CG PRO A 38 5.625 39.109 27.139 1.00 50.28 C ATOM 279 CD PRO A 38 5.070 39.247 25.759 1.00 51.36 C ATOM 280 N LEU A 39 7.428 36.342 25.306 1.00 40.35 N ATOM 281 CA LEU A 39 8.098 35.051 25.133 1.00 38.64 C ATOM 282 C LEU A 39 8.236 34.684 23.661 1.00 35.78 C ATOM 283 O LEU A 39 8.725 33.585 23.389 1.00 35.41 O ATOM 284 CB LEU A 39 7.475 33.919 25.939 1.00 38.96 C ATOM 285 CG LEU A 39 7.423 34.114 27.458 1.00 39.28 C ATOM 286 CD1 LEU A 39 7.075 32.784 28.109 1.00 40.49 C ATOM 287 CD2 LEU A 39 8.716 34.669 28.030 1.00 39.93 C ATOM 288 N ARG A 40 7.872 35.531 22.698 1.00 32.64 N ATOM 289 CA ARG A 40 8.166 35.180 21.310 1.00 31.87 C ATOM 290 C ARG A 40 9.611 35.661 20.995 1.00 32.41 C ATOM 291 O ARG A 40 9.790 36.747 20.433 1.00 31.18 O ATOM 292 CB ARG A 40 7.230 35.856 20.335 1.00 35.52 C ATOM 293 CG ARG A 40 7.497 35.474 18.882 1.00 36.93 C ATOM 294 CD ARG A 40 6.252 34.747 18.367 1.00 40.48 C ATOM 295 NE ARG A 40 6.174 34.765 16.920 1.00 40.31 N ATOM 296 CZ ARG A 40 5.114 35.035 16.171 1.00 41.85 C ATOM 297 NH1 ARG A 40 3.933 35.365 16.675 1.00 40.24 N ATOM 298 NH2 ARG A 40 5.282 34.969 14.850 1.00 42.10 N ATOM 299 N VAL A 41 10.637 34.913 21.376 1.00 29.05 N ATOM 300 CA VAL A 41 12.021 35.346 21.148 1.00 29.41 C ATOM 301 C VAL A 41 12.751 34.263 20.364 1.00 29.15 C ATOM 302 O VAL A 41 12.383 33.093 20.477 1.00 28.50 O ATOM 303 CB VAL A 41 12.755 35.611 22.476 1.00 31.58 C ATOM 304 CG1 VAL A 41 12.168 36.806 23.245 1.00 32.72 C ATOM 305 CG2 VAL A 41 12.678 34.396 23.382 1.00 31.54 C ATOM 306 N TYR A 42 13.730 34.638 19.535 1.00 27.49 N ATOM 307 CA TYR A 42 14.412 33.644 18.701 1.00 28.28 C ATOM 308 C TYR A 42 15.844 33.486 19.243 1.00 27.78 C ATOM 309 O TYR A 42 16.519 34.503 19.331 1.00 26.58 O ATOM 310 CB TYR A 42 14.394 34.054 17.221 1.00 30.66 C ATOM 311 CG TYR A 42 12.984 34.453 16.774 1.00 35.09 C ATOM 312 CD1 TYR A 42 12.103 33.488 16.323 1.00 37.62 C ATOM 313 CD2 TYR A 42 12.534 35.753 16.862 1.00 36.11 C ATOM 314 CE1 TYR A 42 10.812 33.810 15.941 1.00 39.42 C ATOM 315 CE2 TYR A 42 11.241 36.105 16.491 1.00 39.21 C ATOM 316 CZ TYR A 42 10.392 35.126 16.040 1.00 40.06 C ATOM 317 OH TYR A 42 9.100 35.427 15.665 1.00 42.23 O ATOM 318 N VAL A 43 16.238 32.274 19.576 1.00 26.42 N ATOM 319 CA VAL A 43 17.578 32.063 20.115 1.00 27.40 C ATOM 320 C VAL A 43 18.585 32.112 18.963 1.00 27.41 C ATOM 321 O VAL A 43 18.374 31.494 17.933 1.00 27.78 O ATOM 322 CB VAL A 43 17.708 30.757 20.886 1.00 28.77 C ATOM 323 CG1 VAL A 43 19.116 30.520 21.457 1.00 28.42 C ATOM 324 CG2 VAL A 43 16.662 30.764 22.008 1.00 28.84 C ATOM 325 N GLU A 44 19.665 32.813 19.239 1.00 26.43 N ATOM 326 CA GLU A 44 20.759 32.965 18.289 1.00 27.05 C ATOM 327 C GLU A 44 22.009 32.241 18.766 1.00 24.77 C ATOM 328 O GLU A 44 22.698 31.654 17.935 1.00 23.03 O ATOM 329 CB GLU A 44 20.966 34.474 18.165 1.00 31.30 C ATOM 330 CG GLU A 44 22.342 34.979 17.802 1.00 39.87 C ATOM 331 CD GLU A 44 22.252 36.173 16.858 1.00 44.20 C ATOM 332 OE1 GLU A 44 21.421 37.077 17.106 1.00 45.60 O ATOM 333 OE2 GLU A 44 23.013 36.181 15.868 1.00 47.28 O ATOM 334 N GLU A 45 22.306 32.288 20.073 1.00 21.72 N ATOM 335 CA GLU A 45 23.523 31.660 20.563 1.00 23.16 C ATOM 336 C GLU A 45 23.461 31.337 22.043 1.00 20.78 C ATOM 337 O GLU A 45 22.823 32.117 22.731 1.00 20.66 O ATOM 338 CB GLU A 45 24.614 32.755 20.325 1.00 26.46 C ATOM 339 CG GLU A 45 26.034 32.263 20.367 1.00 32.87 C ATOM 340 CD GLU A 45 27.065 33.351 20.089 1.00 35.29 C ATOM 341 OE1 GLU A 45 26.784 34.326 19.365 1.00 37.51 O ATOM 342 OE2 GLU A 45 28.173 33.212 20.606 1.00 36.33 O ATOM 343 N LEU A 46 24.050 30.271 22.548 1.00 19.02 N ATOM 344 CA LEU A 46 24.086 29.956 23.966 1.00 20.48 C ATOM 345 C LEU A 46 25.552 30.080 24.405 1.00 20.63 C ATOM 346 O LEU A 46 26.449 29.666 23.667 1.00 21.66 O ATOM 347 CB LEU A 46 23.487 28.584 24.263 1.00 19.61 C ATOM 348 CG LEU A 46 22.005 28.321 24.003 1.00 24.19 C ATOM 349 CD1 LEU A 46 21.700 26.847 24.346 1.00 26.39 C ATOM 350 CD2 LEU A 46 21.147 29.175 24.925 1.00 25.52 C ATOM 351 N LYS A 47 25.805 30.763 25.531 1.00 24.84 N ATOM 352 CA LYS A 47 27.202 30.906 25.938 1.00 28.41 C ATOM 353 C LYS A 47 27.320 30.614 27.433 1.00 26.83 C ATOM 354 O LYS A 47 27.066 31.478 28.262 1.00 26.86 O ATOM 355 CB LYS A 47 27.849 32.238 25.615 1.00 32.89 C ATOM 356 CG LYS A 47 26.967 33.311 25.024 1.00 38.53 C ATOM 357 CD LYS A 47 27.431 33.657 23.611 1.00 41.22 C ATOM 358 CE LYS A 47 28.368 34.864 23.649 1.00 43.19 C ATOM 359 NZ LYS A 47 29.794 34.458 23.497 1.00 44.11 N ATOM 360 N PRO A 48 27.638 29.369 27.719 1.00 26.59 N ATOM 361 CA PRO A 48 27.825 28.966 29.094 1.00 26.34 C ATOM 362 C PRO A 48 29.009 29.748 29.644 1.00 28.73 C ATOM 363 O PRO A 48 29.906 30.163 28.905 1.00 28.03 O ATOM 364 CB PRO A 48 28.136 27.487 29.037 1.00 27.38 C ATOM 365 CG PRO A 48 27.869 27.062 27.630 1.00 28.56 C ATOM 366 CD PRO A 48 27.937 28.281 26.758 1.00 26.78 C ATOM 367 N THR A 49 28.970 30.013 30.943 1.00 29.91 N ATOM 368 CA THR A 49 30.097 30.734 31.549 1.00 32.24 C ATOM 369 C THR A 49 30.934 29.680 32.264 1.00 35.06 C ATOM 370 O THR A 49 30.480 28.576 32.569 1.00 32.76 O ATOM 371 CB THR A 49 29.605 31.815 32.512 1.00 31.78 C ATOM 372 OG1 THR A 49 29.047 31.218 33.697 1.00 30.39 O ATOM 373 CG2 THR A 49 28.522 32.615 31.761 1.00 31.79 C ATOM 374 N PRO A 50 32.185 30.025 32.571 1.00 37.44 N ATOM 375 CA PRO A 50 33.086 29.144 33.303 1.00 38.62 C ATOM 376 C PRO A 50 32.498 28.800 34.658 1.00 38.21 C ATOM 377 O PRO A 50 32.740 27.696 35.147 1.00 39.06 O ATOM 378 CB PRO A 50 34.391 29.937 33.422 1.00 39.24 C ATOM 379 CG PRO A 50 34.303 30.911 32.287 1.00 39.44 C ATOM 380 CD PRO A 50 32.838 31.325 32.270 1.00 38.15 C ATOM 381 N GLU A 51 31.686 29.685 35.253 1.00 37.84 N ATOM 382 CA GLU A 51 31.025 29.400 36.497 1.00 38.36 C ATOM 383 C GLU A 51 29.769 28.540 36.318 1.00 35.80 C ATOM 384 O GLU A 51 29.170 28.244 37.356 1.00 36.11 O ATOM 385 CB GLU A 51 30.631 30.600 37.344 1.00 42.75 C ATOM 386 CG GLU A 51 30.427 31.952 36.740 1.00 48.27 C ATOM 387 CD GLU A 51 31.695 32.628 36.246 1.00 52.01 C ATOM 388 OE1 GLU A 51 32.784 32.394 36.817 1.00 53.57 O ATOM 389 OE2 GLU A 51 31.583 33.400 35.267 1.00 53.62 O ATOM 390 N GLY A 52 29.385 28.093 35.139 1.00 32.02 N ATOM 391 CA GLY A 52 28.189 27.253 35.069 1.00 30.07 C ATOM 392 C GLY A 52 26.885 27.980 34.882 1.00 26.08 C ATOM 393 O GLY A 52 25.827 27.318 34.893 1.00 27.53 O ATOM 394 N ASP A 53 26.856 29.267 34.622 1.00 23.61 N ATOM 395 CA ASP A 53 25.658 30.015 34.300 1.00 23.68 C ATOM 396 C ASP A 53 25.469 30.016 32.759 1.00 21.29 C ATOM 397 O ASP A 53 26.319 29.536 32.027 1.00 24.22 O ATOM 398 CB ASP A 53 25.645 31.442 34.793 1.00 23.68 C ATOM 399 CG ASP A 53 25.787 31.468 36.311 1.00 27.41 C ATOM 400 OD1 ASP A 53 25.190 30.615 36.999 1.00 26.41 O ATOM 401 OD2 ASP A 53 26.513 32.397 36.706 1.00 29.77 O ATOM 402 N LEU A 54 24.332 30.505 32.313 1.00 23.63 N ATOM 403 CA LEU A 54 24.045 30.425 30.859 1.00 23.46 C ATOM 404 C LEU A 54 23.595 31.761 30.321 1.00 24.87 C ATOM 405 O LEU A 54 22.553 32.322 30.693 1.00 26.11 O ATOM 406 CB LEU A 54 23.006 29.319 30.626 1.00 23.52 C ATOM 407 CG LEU A 54 22.590 29.134 29.166 1.00 26.48 C ATOM 408 CD1 LEU A 54 23.716 28.499 28.367 1.00 25.57 C ATOM 409 CD2 LEU A 54 21.296 28.326 29.103 1.00 29.08 C ATOM 410 N GLU A 55 24.438 32.296 29.428 1.00 23.17 N ATOM 411 CA GLU A 55 24.145 33.558 28.780 1.00 25.85 C ATOM 412 C GLU A 55 23.417 33.235 27.468 1.00 23.84 C ATOM 413 O GLU A 55 23.787 32.318 26.740 1.00 24.53 O ATOM 414 CB GLU A 55 25.435 34.315 28.561 1.00 30.06 C ATOM 415 CG GLU A 55 25.368 35.645 27.837 1.00 35.89 C ATOM 416 CD GLU A 55 26.806 36.173 27.745 1.00 38.46 C ATOM 417 OE1 GLU A 55 27.498 36.198 28.775 1.00 40.71 O ATOM 418 OE2 GLU A 55 27.235 36.508 26.630 1.00 41.79 O ATOM 419 N ILE A 56 22.295 33.903 27.265 1.00 22.07 N ATOM 420 CA ILE A 56 21.412 33.658 26.150 1.00 24.61 C ATOM 421 C ILE A 56 21.314 34.854 25.213 1.00 24.55 C ATOM 422 O ILE A 56 20.826 35.864 25.707 1.00 24.61 O ATOM 423 CB ILE A 56 20.011 33.145 26.583 1.00 24.65 C ATOM 424 CG1 ILE A 56 20.065 31.919 27.481 1.00 25.44 C ATOM 425 CG2 ILE A 56 19.235 32.758 25.321 1.00 27.59 C ATOM 426 CD1 ILE A 56 18.823 31.434 28.198 1.00 25.57 C ATOM 427 N LEU A 57 21.707 34.693 23.956 1.00 23.20 N ATOM 428 CA LEU A 57 21.598 35.747 22.976 1.00 23.80 C ATOM 429 C LEU A 57 20.304 35.442 22.169 1.00 23.83 C ATOM 430 O LEU A 57 20.186 34.337 21.669 1.00 19.55 O ATOM 431 CB LEU A 57 22.714 35.935 21.971 1.00 26.92 C ATOM 432 CG LEU A 57 24.188 35.824 22.340 1.00 32.63 C ATOM 433 CD1 LEU A 57 25.054 36.746 21.460 1.00 33.91 C ATOM 434 CD2 LEU A 57 24.488 36.057 23.805 1.00 32.72 C ATOM 435 N LEU A 58 19.414 36.417 22.213 1.00 23.85 N ATOM 436 CA LEU A 58 18.126 36.242 21.563 1.00 27.16 C ATOM 437 C LEU A 58 17.818 37.409 20.609 1.00 28.57 C ATOM 438 O LEU A 58 18.273 38.539 20.809 1.00 27.66 O ATOM 439 CB LEU A 58 16.998 36.329 22.609 1.00 29.46 C ATOM 440 CG LEU A 58 16.919 35.391 23.792 1.00 30.93 C ATOM 441 CD1 LEU A 58 16.072 35.919 24.924 1.00 29.57 C ATOM 442 CD2 LEU A 58 16.406 34.020 23.348 1.00 32.18 C ATOM 443 N GLN A 59 16.899 37.123 19.700 1.00 29.89 N ATOM 444 CA GLN A 59 16.419 38.161 18.805 1.00 36.07 C ATOM 445 C GLN A 59 14.917 38.283 19.115 1.00 38.04 C ATOM 446 O GLN A 59 14.252 37.275 19.323 1.00 34.88 O ATOM 447 CB GLN A 59 16.634 37.941 17.330 1.00 39.58 C ATOM 448 CG GLN A 59 17.169 36.615 16.842 1.00 43.56 C ATOM 449 CD GLN A 59 17.614 36.709 15.394 1.00 46.51 C ATOM 450 OE1 GLN A 59 18.804 36.848 15.095 1.00 49.21 O ATOM 451 NE2 GLN A 59 16.660 36.626 14.478 1.00 47.69 N ATOM 452 N LYS A 60 14.476 39.512 19.158 1.00 43.62 N ATOM 453 CA LYS A 60 13.074 39.808 19.416 1.00 52.25 C ATOM 454 C LYS A 60 12.661 40.907 18.442 1.00 58.67 C ATOM 455 O LYS A 60 13.491 41.703 17.989 1.00 58.49 O ATOM 456 CB LYS A 60 12.940 40.242 20.862 1.00 52.36 C ATOM 457 CG LYS A 60 11.645 40.034 21.610 1.00 54.39 C ATOM 458 CD LYS A 60 10.424 40.432 20.808 1.00 55.57 C ATOM 459 CE LYS A 60 9.141 40.352 21.612 1.00 55.88 C ATOM 460 NZ LYS A 60 9.267 41.171 22.854 1.00 56.34 N ATOM 461 N TRP A 61 11.391 40.934 18.083 1.00 67.43 N ATOM 462 CA TRP A 61 10.871 41.984 17.207 1.00 75.97 C ATOM 463 C TRP A 61 10.366 43.111 18.107 1.00 79.61 C ATOM 464 O TRP A 61 9.602 42.882 19.042 1.00 80.14 O ATOM 465 CB TRP A 61 9.801 41.429 16.288 1.00 79.29 C ATOM 466 CG TRP A 61 9.393 42.344 15.178 1.00 83.05 C ATOM 467 CD1 TRP A 61 8.490 43.361 15.263 1.00 83.91 C ATOM 468 CD2 TRP A 61 9.866 42.335 13.826 1.00 84.88 C ATOM 469 NE1 TRP A 61 8.363 43.980 14.046 1.00 85.16 N ATOM 470 CE2 TRP A 61 9.198 43.373 13.145 1.00 85.55 C ATOM 471 CE3 TRP A 61 10.789 41.552 13.124 1.00 85.81 C ATOM 472 CZ2 TRP A 61 9.415 43.641 11.792 1.00 86.21 C ATOM 473 CZ3 TRP A 61 11.006 41.827 11.783 1.00 86.40 C ATOM 474 CH2 TRP A 61 10.326 42.865 11.133 1.00 86.54 C ATOM 475 N GLU A 62 10.881 44.306 17.885 1.00 84.27 N ATOM 476 CA GLU A 62 10.509 45.501 18.639 1.00 88.37 C ATOM 477 C GLU A 62 10.417 46.658 17.644 1.00 89.87 C ATOM 478 O GLU A 62 11.384 46.951 16.938 1.00 90.30 O ATOM 479 CB GLU A 62 11.490 45.766 19.766 1.00 90.28 C ATOM 480 CG GLU A 62 11.693 47.203 20.203 1.00 92.27 C ATOM 481 CD GLU A 62 13.145 47.484 20.557 1.00 93.45 C ATOM 482 OE1 GLU A 62 13.921 47.811 19.630 1.00 94.05 O ATOM 483 OE2 GLU A 62 13.512 47.372 21.746 1.00 93.99 O ATOM 484 N ASN A 63 9.240 47.247 17.504 1.00 91.33 N ATOM 485 CA ASN A 63 9.011 48.362 16.613 1.00 92.49 C ATOM 486 C ASN A 63 9.319 48.153 15.145 1.00 92.27 C ATOM 487 O ASN A 63 9.702 49.153 14.512 1.00 93.01 O ATOM 488 CB ASN A 63 9.829 49.584 17.090 1.00 93.65 C ATOM 489 CG ASN A 63 9.269 50.234 18.334 1.00 94.66 C ATOM 490 OD1 ASN A 63 8.159 50.779 18.307 1.00 95.19 O ATOM 491 ND2 ASN A 63 10.021 50.184 19.430 1.00 94.92 N ATOM 492 N GLY A 64 9.176 46.988 14.531 1.00 91.34 N ATOM 493 CA GLY A 64 9.476 46.877 13.102 1.00 89.63 C ATOM 494 C GLY A 64 10.967 46.669 12.857 1.00 88.36 C ATOM 495 O GLY A 64 11.472 46.875 11.753 1.00 88.94 O ATOM 496 N GLU A 65 11.673 46.199 13.873 1.00 86.34 N ATOM 497 CA GLU A 65 13.083 45.881 13.818 1.00 83.65 C ATOM 498 C GLU A 65 13.300 44.492 14.451 1.00 79.48 C ATOM 499 O GLU A 65 12.447 43.927 15.130 1.00 79.30 O ATOM 500 CB GLU A 65 13.989 46.809 14.608 1.00 85.97 C ATOM 501 CG GLU A 65 14.478 48.136 14.148 1.00 88.22 C ATOM 502 CD GLU A 65 14.875 48.343 12.710 1.00 89.33 C ATOM 503 OE1 GLU A 65 13.982 48.592 11.868 1.00 89.87 O ATOM 504 OE2 GLU A 65 16.090 48.283 12.417 1.00 89.98 O ATOM 505 N CYS A 66 14.526 44.030 14.312 1.00 74.21 N ATOM 506 CA CYS A 66 14.953 42.768 14.906 1.00 68.94 C ATOM 507 C CYS A 66 15.962 43.137 15.989 1.00 64.32 C ATOM 508 O CYS A 66 17.102 43.456 15.652 1.00 64.06 O ATOM 509 CB CYS A 66 15.567 41.894 13.825 1.00 69.85 C ATOM 510 SG CYS A 66 15.835 40.182 14.297 1.00 71.55 S ATOM 511 N ALA A 67 15.514 43.207 17.238 1.00 58.15 N ATOM 512 CA ALA A 67 16.445 43.628 18.287 1.00 53.04 C ATOM 513 C ALA A 67 17.129 42.430 18.933 1.00 49.66 C ATOM 514 O ALA A 67 16.664 41.291 18.922 1.00 45.58 O ATOM 515 CB ALA A 67 15.771 44.509 19.319 1.00 52.54 C ATOM 516 N GLN A 68 18.324 42.729 19.437 1.00 47.73 N ATOM 517 CA GLN A 68 19.096 41.702 20.126 1.00 47.54 C ATOM 518 C GLN A 68 19.008 41.983 21.627 1.00 44.49 C ATOM 519 O GLN A 68 18.995 43.131 22.073 1.00 44.81 O ATOM 520 CB GLN A 68 20.557 41.625 19.712 1.00 50.17 C ATOM 521 CG GLN A 68 20.772 41.504 18.218 1.00 54.57 C ATOM 522 CD GLN A 68 20.288 40.214 17.600 1.00 57.11 C ATOM 523 OE1 GLN A 68 20.522 39.109 18.097 1.00 58.99 O ATOM 524 NE2 GLN A 68 19.588 40.328 16.479 1.00 58.48 N ATOM 525 N LYS A 69 18.867 40.903 22.380 1.00 40.18 N ATOM 526 CA LYS A 69 18.857 41.000 23.824 1.00 37.75 C ATOM 527 C LYS A 69 19.699 39.843 24.380 1.00 35.80 C ATOM 528 O LYS A 69 19.686 38.710 23.914 1.00 33.31 O ATOM 529 CB LYS A 69 17.505 40.985 24.495 1.00 39.58 C ATOM 530 CG LYS A 69 16.357 41.733 23.877 1.00 41.07 C ATOM 531 CD LYS A 69 15.032 41.381 24.554 1.00 43.96 C ATOM 532 CE LYS A 69 14.597 42.515 25.480 1.00 45.56 C ATOM 533 NZ LYS A 69 13.134 42.772 25.303 1.00 47.89 N ATOM 534 N LYS A 70 20.398 40.187 25.450 1.00 33.77 N ATOM 535 CA LYS A 70 21.246 39.275 26.166 1.00 35.17 C ATOM 536 C LYS A 70 20.709 39.075 27.583 1.00 34.65 C ATOM 537 O LYS A 70 20.522 40.043 28.344 1.00 32.69 O ATOM 538 CB LYS A 70 22.684 39.802 26.325 1.00 38.49 C ATOM 539 CG LYS A 70 23.622 38.679 26.740 1.00 43.16 C ATOM 540 CD LYS A 70 24.792 39.115 27.608 1.00 46.67 C ATOM 541 CE LYS A 70 25.853 39.880 26.835 1.00 48.83 C ATOM 542 NZ LYS A 70 27.197 39.728 27.496 1.00 50.78 N ATOM 543 N ILE A 71 20.394 37.817 27.898 1.00 31.63 N ATOM 544 CA ILE A 71 19.910 37.572 29.265 1.00 31.36 C ATOM 545 C ILE A 71 20.758 36.489 29.899 1.00 30.19 C ATOM 546 O ILE A 71 21.271 35.571 29.239 1.00 29.57 O ATOM 547 CB ILE A 71 18.414 37.238 29.327 1.00 34.24 C ATOM 548 CG1 ILE A 71 18.103 35.983 28.505 1.00 34.63 C ATOM 549 CG2 ILE A 71 17.535 38.405 28.831 1.00 34.27 C ATOM 550 CD1 ILE A 71 16.671 35.493 28.684 1.00 36.73 C ATOM 551 N ILE A 72 20.915 36.561 31.226 1.00 29.67 N ATOM 552 CA ILE A 72 21.755 35.555 31.896 1.00 29.49 C ATOM 553 C ILE A 72 20.869 34.619 32.709 1.00 27.24 C ATOM 554 O ILE A 72 20.057 35.116 33.485 1.00 27.85 O ATOM 555 CB ILE A 72 22.842 36.167 32.810 1.00 31.80 C ATOM 556 CG1 ILE A 72 23.550 37.344 32.138 1.00 34.50 C ATOM 557 CG2 ILE A 72 23.854 35.124 33.284 1.00 32.51 C ATOM 558 CD1 ILE A 72 24.404 36.951 30.952 1.00 35.17 C ATOM 559 N ALA A 73 20.954 33.326 32.496 1.00 25.14 N ATOM 560 CA ALA A 73 20.187 32.361 33.264 1.00 25.88 C ATOM 561 C ALA A 73 21.205 31.672 34.202 1.00 25.78 C ATOM 562 O ALA A 73 22.194 31.064 33.800 1.00 27.72 O ATOM 563 CB ALA A 73 19.412 31.362 32.434 1.00 24.05 C ATOM 564 N GLU A 74 21.004 31.898 35.502 1.00 27.06 N ATOM 565 CA GLU A 74 21.943 31.424 36.523 1.00 26.64 C ATOM 566 C GLU A 74 21.697 29.993 36.967 1.00 25.39 C ATOM 567 O GLU A 74 20.521 29.632 37.041 1.00 22.88 O ATOM 568 CB GLU A 74 21.803 32.295 37.791 1.00 31.05 C ATOM 569 CG GLU A 74 21.859 33.775 37.500 1.00 39.12 C ATOM 570 CD GLU A 74 21.924 34.622 38.764 1.00 43.77 C ATOM 571 OE1 GLU A 74 21.776 34.107 39.890 1.00 45.72 O ATOM 572 OE2 GLU A 74 22.109 35.845 38.583 1.00 46.48 O ATOM 573 N LYS A 75 22.714 29.193 37.215 1.00 24.14 N ATOM 574 CA LYS A 75 22.508 27.849 37.687 1.00 27.77 C ATOM 575 C LYS A 75 21.767 27.904 39.037 1.00 27.01 C ATOM 576 O LYS A 75 21.572 28.889 39.774 1.00 23.71 O ATOM 577 CB LYS A 75 23.800 27.024 37.805 1.00 33.04 C ATOM 578 CG LYS A 75 25.021 27.817 38.152 1.00 36.81 C ATOM 579 CD LYS A 75 26.294 27.001 38.396 1.00 39.70 C ATOM 580 CE LYS A 75 27.166 27.784 39.365 1.00 41.99 C ATOM 581 NZ LYS A 75 27.056 29.264 39.192 1.00 41.91 N ATOM 582 N THR A 76 21.113 26.784 39.269 1.00 25.45 N ATOM 583 CA THR A 76 20.288 26.625 40.482 1.00 27.20 C ATOM 584 C THR A 76 20.757 25.338 41.133 1.00 29.64 C ATOM 585 O THR A 76 21.628 24.678 40.575 1.00 31.25 O ATOM 586 CB THR A 76 18.768 26.531 40.263 1.00 27.70 C ATOM 587 OG1 THR A 76 18.453 25.353 39.481 1.00 26.95 O ATOM 588 CG2 THR A 76 18.154 27.732 39.557 1.00 28.45 C ATOM 589 N LYS A 77 20.106 24.886 42.205 1.00 33.69 N ATOM 590 CA LYS A 77 20.524 23.598 42.775 1.00 37.94 C ATOM 591 C LYS A 77 20.071 22.405 41.956 1.00 38.58 C ATOM 592 O LYS A 77 20.493 21.266 42.181 1.00 39.04 O ATOM 593 CB LYS A 77 19.921 23.533 44.189 1.00 39.83 C ATOM 594 CG LYS A 77 20.588 24.561 45.087 1.00 43.47 C ATOM 595 CD LYS A 77 21.955 24.042 45.528 1.00 45.67 C ATOM 596 CE LYS A 77 22.073 24.278 47.043 1.00 47.61 C ATOM 597 NZ LYS A 77 21.695 25.683 47.368 1.00 48.56 N ATOM 598 N ILE A 78 19.123 22.644 41.051 1.00 37.81 N ATOM 599 CA ILE A 78 18.616 21.598 40.179 1.00 37.71 C ATOM 600 C ILE A 78 19.343 21.708 38.851 1.00 35.62 C ATOM 601 O ILE A 78 19.476 22.790 38.283 1.00 34.38 O ATOM 602 CB ILE A 78 17.100 21.715 40.026 1.00 39.62 C ATOM 603 CG1 ILE A 78 16.477 21.809 41.430 1.00 42.13 C ATOM 604 CG2 ILE A 78 16.506 20.502 39.324 1.00 39.14 C ATOM 605 CD1 ILE A 78 15.158 22.544 41.432 1.00 43.57 C ATOM 606 N PRO A 79 19.976 20.609 38.448 1.00 35.55 N ATOM 607 CA PRO A 79 20.686 20.585 37.197 1.00 35.94 C ATOM 608 C PRO A 79 19.622 20.704 36.105 1.00 35.04 C ATOM 609 O PRO A 79 18.451 20.331 36.293 1.00 35.47 O ATOM 610 CB PRO A 79 21.430 19.263 37.201 1.00 37.76 C ATOM 611 CG PRO A 79 20.763 18.396 38.203 1.00 37.35 C ATOM 612 CD PRO A 79 19.883 19.265 39.070 1.00 36.70 C ATOM 613 N ALA A 80 19.955 21.387 35.031 1.00 32.27 N ATOM 614 CA ALA A 80 19.103 21.629 33.876 1.00 28.46 C ATOM 615 C ALA A 80 18.050 22.705 34.086 1.00 26.11 C ATOM 616 O ALA A 80 17.211 22.955 33.194 1.00 24.75 O ATOM 617 CB ALA A 80 18.453 20.323 33.420 1.00 29.53 C ATOM 618 N VAL A 81 18.008 23.316 35.251 1.00 22.70 N ATOM 619 CA VAL A 81 17.055 24.360 35.619 1.00 22.65 C ATOM 620 C VAL A 81 17.820 25.649 35.908 1.00 22.84 C ATOM 621 O VAL A 81 18.774 25.624 36.704 1.00 22.55 O ATOM 622 CB VAL A 81 16.166 23.979 36.805 1.00 23.89 C ATOM 623 CG1 VAL A 81 15.146 25.090 37.073 1.00 23.69 C ATOM 624 CG2 VAL A 81 15.376 22.694 36.495 1.00 26.20 C ATOM 625 N PHE A 82 17.568 26.727 35.177 1.00 20.41 N ATOM 626 CA PHE A 82 18.324 27.968 35.278 1.00 20.46 C ATOM 627 C PHE A 82 17.333 29.064 35.620 1.00 23.22 C ATOM 628 O PHE A 82 16.153 28.926 35.257 1.00 24.00 O ATOM 629 CB PHE A 82 19.131 28.377 34.017 1.00 19.76 C ATOM 630 CG PHE A 82 20.194 27.366 33.731 1.00 22.93 C ATOM 631 CD1 PHE A 82 19.876 26.166 33.099 1.00 23.50 C ATOM 632 CD2 PHE A 82 21.516 27.590 34.144 1.00 22.93 C ATOM 633 CE1 PHE A 82 20.824 25.191 32.904 1.00 25.36 C ATOM 634 CE2 PHE A 82 22.475 26.628 33.915 1.00 25.23 C ATOM 635 CZ PHE A 82 22.149 25.430 33.307 1.00 26.49 C ATOM 636 N LYS A 83 17.745 30.083 36.332 1.00 25.56 N ATOM 637 CA LYS A 83 16.826 31.131 36.730 1.00 27.16 C ATOM 638 C LYS A 83 17.258 32.478 36.163 1.00 26.71 C ATOM 639 O LYS A 83 18.405 32.870 36.346 1.00 26.14 O ATOM 640 CB LYS A 83 16.799 31.256 38.260 1.00 32.32 C ATOM 641 CG LYS A 83 15.728 32.230 38.765 1.00 37.84 C ATOM 642 CD LYS A 83 15.916 32.412 40.274 1.00 41.45 C ATOM 643 CE LYS A 83 15.158 31.380 41.081 1.00 43.94 C ATOM 644 NZ LYS A 83 15.017 30.067 40.391 1.00 45.58 N ATOM 645 N ILE A 84 16.298 33.126 35.527 1.00 26.07 N ATOM 646 CA ILE A 84 16.585 34.484 35.054 1.00 28.71 C ATOM 647 C ILE A 84 16.107 35.359 36.218 1.00 30.90 C ATOM 648 O ILE A 84 14.912 35.458 36.439 1.00 30.44 O ATOM 649 CB ILE A 84 15.906 34.822 33.744 1.00 27.20 C ATOM 650 CG1 ILE A 84 16.388 33.827 32.670 1.00 27.48 C ATOM 651 CG2 ILE A 84 16.235 36.236 33.309 1.00 27.36 C ATOM 652 CD1 ILE A 84 15.305 33.544 31.648 1.00 30.02 C ATOM 653 N ASP A 85 17.082 35.898 36.923 1.00 35.72 N ATOM 654 CA ASP A 85 16.834 36.650 38.144 1.00 40.76 C ATOM 655 C ASP A 85 16.530 38.123 37.963 1.00 40.00 C ATOM 656 O ASP A 85 17.039 38.999 38.662 1.00 40.78 O ATOM 657 CB ASP A 85 18.056 36.417 39.060 1.00 44.46 C ATOM 658 CG ASP A 85 17.714 36.792 40.491 1.00 48.88 C ATOM 659 OD1 ASP A 85 16.775 36.247 41.116 1.00 49.57 O ATOM 660 OD2 ASP A 85 18.429 37.704 40.961 1.00 50.64 O ATOM 661 N ALA A 86 15.594 38.421 37.082 1.00 38.68 N ATOM 662 CA ALA A 86 15.104 39.744 36.758 1.00 37.10 C ATOM 663 C ALA A 86 13.986 40.179 37.688 1.00 36.02 C ATOM 664 O ALA A 86 13.481 39.397 38.510 1.00 37.01 O ATOM 665 CB ALA A 86 14.558 39.631 35.318 1.00 36.44 C ATOM 666 N LEU A 87 13.449 41.386 37.513 1.00 34.37 N ATOM 667 CA LEU A 87 12.304 41.831 38.312 1.00 33.76 C ATOM 668 C LEU A 87 11.135 40.850 38.174 1.00 34.63 C ATOM 669 O LEU A 87 10.374 40.625 39.121 1.00 34.00 O ATOM 670 CB LEU A 87 11.886 43.232 37.902 1.00 34.35 C ATOM 671 CG LEU A 87 12.958 44.334 38.077 1.00 34.73 C ATOM 672 CD1 LEU A 87 12.445 45.610 37.416 1.00 35.74 C ATOM 673 CD2 LEU A 87 13.324 44.524 39.534 1.00 33.81 C ATOM 674 N ASN A 88 10.916 40.304 37.001 1.00 34.27 N ATOM 675 CA ASN A 88 9.895 39.290 36.723 1.00 37.30 C ATOM 676 C ASN A 88 10.690 37.994 36.496 1.00 36.62 C ATOM 677 O ASN A 88 11.421 37.858 35.511 1.00 35.92 O ATOM 678 CB ASN A 88 9.045 39.617 35.507 1.00 40.28 C ATOM 679 CG ASN A 88 8.541 41.049 35.505 1.00 43.29 C ATOM 680 OD1 ASN A 88 7.527 41.369 36.124 1.00 44.95 O ATOM 681 ND2 ASN A 88 9.262 41.932 34.828 1.00 45.33 N ATOM 682 N GLU A 89 10.591 37.096 37.453 1.00 35.88 N ATOM 683 CA GLU A 89 11.359 35.862 37.409 1.00 37.85 C ATOM 684 C GLU A 89 10.909 34.844 36.376 1.00 34.45 C ATOM 685 O GLU A 89 9.716 34.641 36.166 1.00 34.09 O ATOM 686 CB GLU A 89 11.316 35.202 38.790 1.00 42.86 C ATOM 687 CG GLU A 89 12.719 34.774 39.201 1.00 49.77 C ATOM 688 CD GLU A 89 13.009 35.309 40.605 1.00 53.71 C ATOM 689 OE1 GLU A 89 12.550 34.667 41.568 1.00 55.30 O ATOM 690 OE2 GLU A 89 13.679 36.368 40.694 1.00 56.59 O ATOM 691 N ASN A 90 11.876 34.198 35.735 1.00 30.39 N ATOM 692 CA ASN A 90 11.556 33.185 34.747 1.00 30.10 C ATOM 693 C ASN A 90 12.552 32.031 34.957 1.00 27.45 C ATOM 694 O ASN A 90 13.673 32.347 35.310 1.00 27.37 O ATOM 695 CB ASN A 90 11.722 33.660 33.318 1.00 30.87 C ATOM 696 CG ASN A 90 10.557 34.400 32.721 1.00 34.01 C ATOM 697 OD1 ASN A 90 10.597 35.618 32.569 1.00 35.28 O ATOM 698 ND2 ASN A 90 9.534 33.644 32.339 1.00 34.75 N ATOM 699 N LYS A 91 12.096 30.817 34.741 1.00 24.09 N ATOM 700 CA LYS A 91 13.036 29.687 34.813 1.00 23.71 C ATOM 701 C LYS A 91 13.210 29.162 33.400 1.00 23.58 C ATOM 702 O LYS A 91 12.305 29.320 32.555 1.00 24.32 O ATOM 703 CB LYS A 91 12.507 28.590 35.727 1.00 28.75 C ATOM 704 CG LYS A 91 12.600 29.060 37.173 1.00 33.63 C ATOM 705 CD LYS A 91 11.964 28.115 38.153 1.00 37.58 C ATOM 706 CE LYS A 91 12.344 28.581 39.571 1.00 39.97 C ATOM 707 NZ LYS A 91 11.214 28.350 40.494 1.00 43.48 N ATOM 708 N VAL A 92 14.394 28.661 33.134 1.00 21.96 N ATOM 709 CA VAL A 92 14.703 28.051 31.837 1.00 23.66 C ATOM 710 C VAL A 92 14.920 26.587 32.179 1.00 24.12 C ATOM 711 O VAL A 92 15.690 26.281 33.135 1.00 22.69 O ATOM 712 CB VAL A 92 15.997 28.634 31.254 1.00 25.93 C ATOM 713 CG1 VAL A 92 16.455 27.928 29.990 1.00 26.11 C ATOM 714 CG2 VAL A 92 15.854 30.126 31.006 1.00 26.11 C ATOM 715 N LEU A 93 14.258 25.688 31.488 1.00 22.77 N ATOM 716 CA LEU A 93 14.364 24.275 31.804 1.00 24.95 C ATOM 717 C LEU A 93 14.859 23.529 30.579 1.00 25.08 C ATOM 718 O LEU A 93 14.219 23.709 29.544 1.00 24.68 O ATOM 719 CB LEU A 93 13.013 23.675 32.189 1.00 28.09 C ATOM 720 CG LEU A 93 12.087 24.372 33.184 1.00 30.85 C ATOM 721 CD1 LEU A 93 12.810 24.663 34.483 1.00 32.72 C ATOM 722 CD2 LEU A 93 11.449 25.635 32.627 1.00 32.87 C ATOM 723 N VAL A 94 15.948 22.780 30.708 1.00 23.02 N ATOM 724 CA VAL A 94 16.418 22.042 29.510 1.00 21.71 C ATOM 725 C VAL A 94 15.761 20.676 29.558 1.00 22.07 C ATOM 726 O VAL A 94 15.995 19.929 30.530 1.00 22.25 O ATOM 727 CB VAL A 94 17.947 21.935 29.471 1.00 22.68 C ATOM 728 CG1 VAL A 94 18.450 21.147 28.267 1.00 21.79 C ATOM 729 CG2 VAL A 94 18.501 23.356 29.420 1.00 23.84 C ATOM 730 N LEU A 95 14.952 20.378 28.569 1.00 21.91 N ATOM 731 CA LEU A 95 14.292 19.068 28.582 1.00 23.72 C ATOM 732 C LEU A 95 15.199 17.981 28.022 1.00 24.35 C ATOM 733 O LEU A 95 15.080 16.847 28.478 1.00 25.62 O ATOM 734 CB LEU A 95 13.004 19.131 27.782 1.00 25.29 C ATOM 735 CG LEU A 95 11.962 20.188 28.080 1.00 28.86 C ATOM 736 CD1 LEU A 95 10.621 19.852 27.418 1.00 29.67 C ATOM 737 CD2 LEU A 95 11.743 20.412 29.562 1.00 29.62 C ATOM 738 N ASP A 96 15.937 18.284 26.957 1.00 23.51 N ATOM 739 CA ASP A 96 16.761 17.247 26.312 1.00 25.86 C ATOM 740 C ASP A 96 17.621 17.898 25.230 1.00 25.47 C ATOM 741 O ASP A 96 17.262 18.961 24.715 1.00 23.38 O ATOM 742 CB ASP A 96 15.829 16.243 25.620 1.00 28.58 C ATOM 743 CG ASP A 96 16.470 15.053 24.965 1.00 30.41 C ATOM 744 OD1 ASP A 96 17.534 14.609 25.411 1.00 31.59 O ATOM 745 OD2 ASP A 96 15.960 14.494 23.971 1.00 33.28 O ATOM 746 N THR A 97 18.753 17.257 24.932 1.00 23.37 N ATOM 747 CA THR A 97 19.644 17.728 23.901 1.00 23.58 C ATOM 748 C THR A 97 20.594 16.588 23.532 1.00 25.69 C ATOM 749 O THR A 97 20.918 15.752 24.393 1.00 26.69 O ATOM 750 CB THR A 97 20.453 18.987 24.248 1.00 20.56 C ATOM 751 OG1 THR A 97 21.307 19.355 23.159 1.00 22.04 O ATOM 752 CG2 THR A 97 21.310 18.849 25.497 1.00 23.25 C ATOM 753 N ASP A 98 21.103 16.616 22.311 1.00 25.39 N ATOM 754 CA ASP A 98 22.149 15.614 21.994 1.00 28.85 C ATOM 755 C ASP A 98 23.403 16.398 21.723 1.00 28.84 C ATOM 756 O ASP A 98 24.405 15.957 21.151 1.00 31.70 O ATOM 757 CB ASP A 98 21.668 14.748 20.836 1.00 30.32 C ATOM 758 CG ASP A 98 21.648 15.477 19.524 1.00 30.84 C ATOM 759 OD1 ASP A 98 21.696 16.724 19.486 1.00 31.82 O ATOM 760 OD2 ASP A 98 21.557 14.811 18.467 1.00 33.67 O ATOM 761 N TYR A 99 23.407 17.701 22.046 1.00 26.24 N ATOM 762 CA TYR A 99 24.459 18.656 21.850 1.00 27.91 C ATOM 763 C TYR A 99 24.829 18.994 20.401 1.00 29.15 C ATOM 764 O TYR A 99 25.074 20.160 20.086 1.00 30.47 O ATOM 765 CB TYR A 99 25.801 18.274 22.546 1.00 26.23 C ATOM 766 CG TYR A 99 25.526 17.985 24.013 1.00 28.13 C ATOM 767 CD1 TYR A 99 25.236 18.988 24.915 1.00 27.38 C ATOM 768 CD2 TYR A 99 25.517 16.658 24.429 1.00 29.03 C ATOM 769 CE1 TYR A 99 24.957 18.699 26.237 1.00 27.29 C ATOM 770 CE2 TYR A 99 25.258 16.346 25.757 1.00 29.27 C ATOM 771 CZ TYR A 99 24.967 17.373 26.621 1.00 29.14 C ATOM 772 OH TYR A 99 24.669 16.996 27.915 1.00 29.49 O ATOM 773 N LYS A 100 24.822 18.023 19.509 1.00 29.67 N ATOM 774 CA LYS A 100 25.255 18.244 18.130 1.00 32.45 C ATOM 775 C LYS A 100 24.152 18.503 17.146 1.00 31.16 C ATOM 776 O LYS A 100 24.473 18.831 15.999 1.00 30.15 O ATOM 777 CB LYS A 100 26.049 16.973 17.721 1.00 36.41 C ATOM 778 CG LYS A 100 25.116 15.771 17.550 1.00 42.27 C ATOM 779 CD LYS A 100 25.868 14.449 17.616 1.00 46.74 C ATOM 780 CE LYS A 100 25.424 13.485 16.527 1.00 49.06 C ATOM 781 NZ LYS A 100 26.318 13.598 15.319 1.00 52.99 N ATOM 782 N LYS A 101 22.877 18.339 17.511 1.00 28.30 N ATOM 783 CA LYS A 101 21.820 18.618 16.527 1.00 27.93 C ATOM 784 C LYS A 101 20.666 19.427 17.100 1.00 25.58 C ATOM 785 O LYS A 101 20.242 20.404 16.480 1.00 23.22 O ATOM 786 CB LYS A 101 21.225 17.278 16.080 1.00 31.44 C ATOM 787 CG LYS A 101 20.500 17.273 14.753 1.00 38.08 C ATOM 788 CD LYS A 101 20.801 15.955 14.010 1.00 41.64 C ATOM 789 CE LYS A 101 19.556 15.084 13.986 1.00 43.79 C ATOM 790 NZ LYS A 101 19.691 13.927 13.053 1.00 43.94 N ATOM 791 N TYR A 102 20.157 18.958 18.267 1.00 22.83 N ATOM 792 CA TYR A 102 18.959 19.643 18.769 1.00 22.49 C ATOM 793 C TYR A 102 19.000 19.932 20.264 1.00 20.99 C ATOM 794 O TYR A 102 19.726 19.294 21.022 1.00 21.20 O ATOM 795 CB TYR A 102 17.717 18.785 18.430 1.00 24.35 C ATOM 796 CG TYR A 102 17.616 17.541 19.279 1.00 25.69 C ATOM 797 CD1 TYR A 102 18.218 16.354 18.912 1.00 26.80 C ATOM 798 CD2 TYR A 102 16.890 17.575 20.488 1.00 27.14 C ATOM 799 CE1 TYR A 102 18.158 15.241 19.727 1.00 29.03 C ATOM 800 CE2 TYR A 102 16.808 16.463 21.285 1.00 27.91 C ATOM 801 CZ TYR A 102 17.440 15.303 20.902 1.00 28.95 C ATOM 802 OH TYR A 102 17.366 14.189 21.682 1.00 31.89 O ATOM 803 N LEU A 103 18.173 20.905 20.686 1.00 20.27 N ATOM 804 CA LEU A 103 18.068 21.180 22.125 1.00 19.35 C ATOM 805 C LEU A 103 16.618 21.591 22.340 1.00 18.23 C ATOM 806 O LEU A 103 16.098 22.405 21.584 1.00 19.27 O ATOM 807 CB LEU A 103 19.049 22.252 22.571 1.00 19.87 C ATOM 808 CG LEU A 103 19.169 22.678 24.025 1.00 23.16 C ATOM 809 CD1 LEU A 103 20.526 23.360 24.231 1.00 24.15 C ATOM 810 CD2 LEU A 103 18.097 23.621 24.510 1.00 24.15 C ATOM 811 N LEU A 104 15.948 21.009 23.308 1.00 18.55 N ATOM 812 CA LEU A 104 14.581 21.346 23.652 1.00 18.62 C ATOM 813 C LEU A 104 14.563 22.092 24.969 1.00 20.53 C ATOM 814 O LEU A 104 15.194 21.600 25.920 1.00 20.14 O ATOM 815 CB LEU A 104 13.733 20.070 23.805 1.00 19.20 C ATOM 816 CG LEU A 104 13.914 19.053 22.678 1.00 21.11 C ATOM 817 CD1 LEU A 104 13.021 17.825 22.891 1.00 21.94 C ATOM 818 CD2 LEU A 104 13.548 19.683 21.314 1.00 19.43 C ATOM 819 N PHE A 105 13.881 23.233 25.038 1.00 21.36 N ATOM 820 CA PHE A 105 13.838 23.872 26.361 1.00 23.73 C ATOM 821 C PHE A 105 12.529 24.642 26.494 1.00 23.21 C ATOM 822 O PHE A 105 11.948 24.961 25.468 1.00 23.39 O ATOM 823 CB PHE A 105 15.010 24.839 26.589 1.00 24.33 C ATOM 824 CG PHE A 105 14.875 26.181 25.924 1.00 27.20 C ATOM 825 CD1 PHE A 105 15.171 26.347 24.577 1.00 25.05 C ATOM 826 CD2 PHE A 105 14.360 27.269 26.624 1.00 27.82 C ATOM 827 CE1 PHE A 105 15.033 27.572 23.968 1.00 26.41 C ATOM 828 CE2 PHE A 105 14.213 28.498 25.997 1.00 28.93 C ATOM 829 CZ PHE A 105 14.564 28.659 24.665 1.00 27.78 C ATOM 830 N CYS A 106 12.214 24.921 27.752 1.00 22.98 N ATOM 831 CA CYS A 106 11.021 25.707 28.056 1.00 23.33 C ATOM 832 C CYS A 106 11.418 26.871 28.979 1.00 25.66 C ATOM 833 O CYS A 106 12.399 26.822 29.729 1.00 22.88 O ATOM 834 CB CYS A 106 9.986 24.850 28.802 1.00 24.28 C ATOM 835 SG CYS A 106 9.446 23.373 27.870 1.00 26.23 S ATOM 836 N MET A 107 10.674 27.943 28.921 1.00 26.46 N ATOM 837 CA MET A 107 10.733 29.125 29.721 1.00 29.66 C ATOM 838 C MET A 107 9.393 29.145 30.485 1.00 31.42 C ATOM 839 O MET A 107 8.316 28.956 29.915 1.00 27.60 O ATOM 840 CB MET A 107 10.915 30.423 28.948 1.00 32.41 C ATOM 841 CG MET A 107 12.373 30.677 28.572 1.00 37.15 C ATOM 842 SD MET A 107 12.487 32.101 27.451 1.00 42.00 S ATOM 843 CE MET A 107 11.975 31.305 25.935 1.00 43.57 C ATOM 844 N GLU A 108 9.534 29.265 31.797 1.00 34.29 N ATOM 845 CA GLU A 108 8.349 29.245 32.641 1.00 38.40 C ATOM 846 C GLU A 108 8.186 30.577 33.352 1.00 42.31 C ATOM 847 O GLU A 108 9.140 31.227 33.776 1.00 37.39 O ATOM 848 CB GLU A 108 8.458 28.092 33.623 1.00 38.82 C ATOM 849 CG GLU A 108 7.394 28.011 34.685 1.00 41.51 C ATOM 850 CD GLU A 108 7.771 27.060 35.813 1.00 43.62 C ATOM 851 OE1 GLU A 108 8.512 27.433 36.738 1.00 44.26 O ATOM 852 OE2 GLU A 108 7.318 25.899 35.774 1.00 45.22 O ATOM 853 N ASN A 109 6.933 30.967 33.504 1.00 50.15 N ATOM 854 CA ASN A 109 6.596 32.154 34.281 1.00 59.91 C ATOM 855 C ASN A 109 5.928 31.712 35.577 1.00 65.14 C ATOM 856 O ASN A 109 4.740 31.385 35.571 1.00 65.65 O ATOM 857 CB ASN A 109 5.720 33.098 33.459 1.00 62.44 C ATOM 858 CG ASN A 109 6.602 33.922 32.536 1.00 65.16 C ATOM 859 OD1 ASN A 109 7.451 34.677 33.022 1.00 67.29 O ATOM 860 ND2 ASN A 109 6.471 33.794 31.231 1.00 66.19 N ATOM 861 N SER A 110 6.672 31.662 36.683 1.00 72.46 N ATOM 862 CA SER A 110 6.042 31.241 37.937 1.00 79.31 C ATOM 863 C SER A 110 5.187 32.345 38.542 1.00 83.23 C ATOM 864 O SER A 110 4.074 32.101 39.021 1.00 84.55 O ATOM 865 CB SER A 110 7.040 30.780 38.995 1.00 79.94 C ATOM 866 OG SER A 110 7.461 31.876 39.788 1.00 81.01 O ATOM 867 N ALA A 111 5.652 33.586 38.467 1.00 87.22 N ATOM 868 CA ALA A 111 4.935 34.741 38.996 1.00 90.60 C ATOM 869 C ALA A 111 3.503 34.846 38.485 1.00 92.72 C ATOM 870 O ALA A 111 2.647 35.434 39.153 1.00 93.46 O ATOM 871 CB ALA A 111 5.721 36.012 38.695 1.00 90.92 C ATOM 872 N GLU A 112 3.213 34.331 37.298 1.00 94.59 N ATOM 873 CA GLU A 112 1.887 34.296 36.720 1.00 95.80 C ATOM 874 C GLU A 112 1.032 33.213 37.364 1.00 96.14 C ATOM 875 O GLU A 112 1.503 32.395 38.156 1.00 96.43 O ATOM 876 CB GLU A 112 1.963 34.150 35.199 1.00 96.49 C ATOM 877 CG GLU A 112 2.133 35.525 34.559 1.00 97.36 C ATOM 878 CD GLU A 112 1.380 35.678 33.256 1.00 97.75 C ATOM 879 OE1 GLU A 112 0.856 34.676 32.728 1.00 97.94 O ATOM 880 OE2 GLU A 112 1.298 36.826 32.764 1.00 98.03 O ATOM 881 N PRO A 113 -0.262 33.230 37.055 1.00 95.97 N ATOM 882 CA PRO A 113 -1.239 32.354 37.652 1.00 95.24 C ATOM 883 C PRO A 113 -0.944 30.870 37.700 1.00 93.89 C ATOM 884 O PRO A 113 -0.415 30.369 38.700 1.00 94.23 O ATOM 885 CB PRO A 113 -2.543 32.642 36.905 1.00 95.76 C ATOM 886 CG PRO A 113 -2.180 33.502 35.750 1.00 96.09 C ATOM 887 CD PRO A 113 -0.915 34.212 36.149 1.00 96.09 C ATOM 888 N GLU A 114 -1.346 30.141 36.662 1.00 91.70 N ATOM 889 CA GLU A 114 -1.226 28.693 36.669 1.00 89.06 C ATOM 890 C GLU A 114 0.100 28.132 36.210 1.00 85.22 C ATOM 891 O GLU A 114 0.927 27.710 37.020 1.00 85.67 O ATOM 892 CB GLU A 114 -2.394 28.096 35.853 1.00 90.71 C ATOM 893 CG GLU A 114 -3.624 27.856 36.729 1.00 92.34 C ATOM 894 CD GLU A 114 -3.388 26.791 37.785 1.00 93.13 C ATOM 895 OE1 GLU A 114 -2.377 26.066 37.697 1.00 93.09 O ATOM 896 OE2 GLU A 114 -4.214 26.667 38.718 1.00 93.83 O ATOM 897 N GLN A 115 0.262 28.023 34.904 1.00 79.97 N ATOM 898 CA GLN A 115 1.517 27.508 34.370 1.00 74.55 C ATOM 899 C GLN A 115 1.698 28.053 32.959 1.00 67.41 C ATOM 900 O GLN A 115 1.205 27.488 31.998 1.00 68.85 O ATOM 901 CB GLN A 115 1.696 26.013 34.512 1.00 77.22 C ATOM 902 CG GLN A 115 2.888 25.620 35.374 1.00 79.61 C ATOM 903 CD GLN A 115 3.881 24.818 34.560 1.00 81.01 C ATOM 904 OE1 GLN A 115 3.457 24.110 33.642 1.00 81.73 O ATOM 905 NE2 GLN A 115 5.166 24.878 34.880 1.00 81.59 N ATOM 906 N SER A 116 2.302 29.229 32.957 1.00 57.02 N ATOM 907 CA SER A 116 2.579 29.921 31.695 1.00 47.84 C ATOM 908 C SER A 116 3.966 29.372 31.325 1.00 40.04 C ATOM 909 O SER A 116 4.909 29.519 32.100 1.00 37.02 O ATOM 910 CB SER A 116 2.441 31.410 31.908 1.00 47.01 C ATOM 911 OG SER A 116 3.153 32.203 30.994 1.00 49.94 O ATOM 912 N LEU A 117 3.955 28.526 30.319 1.00 33.07 N ATOM 913 CA LEU A 117 5.162 27.851 29.824 1.00 28.65 C ATOM 914 C LEU A 117 5.253 28.116 28.316 1.00 27.39 C ATOM 915 O LEU A 117 4.205 28.000 27.671 1.00 24.35 O ATOM 916 CB LEU A 117 4.872 26.378 30.025 1.00 32.43 C ATOM 917 CG LEU A 117 5.877 25.261 30.218 1.00 33.90 C ATOM 918 CD1 LEU A 117 7.036 25.715 31.085 1.00 35.87 C ATOM 919 CD2 LEU A 117 5.157 24.071 30.870 1.00 36.78 C ATOM 920 N ALA A 118 6.435 28.348 27.771 1.00 23.37 N ATOM 921 CA ALA A 118 6.637 28.403 26.337 1.00 22.69 C ATOM 922 C ALA A 118 7.892 27.539 26.081 1.00 22.60 C ATOM 923 O ALA A 118 8.838 27.708 26.880 1.00 22.84 O ATOM 924 CB ALA A 118 6.828 29.809 25.819 1.00 22.33 C ATOM 925 N CYS A 119 7.831 26.637 25.114 1.00 20.54 N ATOM 926 CA CYS A 119 8.962 25.732 24.874 1.00 21.56 C ATOM 927 C CYS A 119 9.424 25.918 23.429 1.00 20.58 C ATOM 928 O CYS A 119 8.683 26.446 22.595 1.00 19.36 O ATOM 929 CB CYS A 119 8.604 24.265 25.138 1.00 20.06 C ATOM 930 SG CYS A 119 7.840 24.083 26.798 1.00 24.29 S ATOM 931 N GLN A 120 10.691 25.570 23.178 1.00 20.08 N ATOM 932 CA GLN A 120 11.209 25.721 21.839 1.00 19.39 C ATOM 933 C GLN A 120 12.035 24.475 21.480 1.00 19.75 C ATOM 934 O GLN A 120 12.593 23.840 22.345 1.00 18.87 O ATOM 935 CB GLN A 120 12.195 26.902 21.667 1.00 20.96 C ATOM 936 CG GLN A 120 11.615 28.244 22.024 1.00 23.44 C ATOM 937 CD GLN A 120 12.348 29.431 21.431 1.00 25.02 C ATOM 938 OE1 GLN A 120 13.283 29.224 20.644 1.00 23.53 O ATOM 939 NE2 GLN A 120 11.847 30.581 21.869 1.00 24.95 N ATOM 940 N CYS A 121 12.084 24.308 20.157 1.00 19.32 N ATOM 941 CA CYS A 121 12.904 23.274 19.575 1.00 19.41 C ATOM 942 C CYS A 121 14.069 24.008 18.862 1.00 20.18 C ATOM 943 O CYS A 121 13.800 24.732 17.901 1.00 18.78 O ATOM 944 CB CYS A 121 12.094 22.430 18.594 1.00 21.15 C ATOM 945 SG CYS A 121 13.136 21.270 17.666 1.00 22.96 S ATOM 946 N LEU A 122 15.272 23.841 19.373 1.00 19.31 N ATOM 947 CA LEU A 122 16.424 24.522 18.734 1.00 18.52 C ATOM 948 C LEU A 122 17.202 23.548 17.875 1.00 17.92 C ATOM 949 O LEU A 122 17.330 22.412 18.299 1.00 18.96 O ATOM 950 CB LEU A 122 17.366 25.110 19.794 1.00 17.68 C ATOM 951 CG LEU A 122 16.859 26.083 20.827 1.00 18.71 C ATOM 952 CD1 LEU A 122 17.942 26.641 21.763 1.00 19.40 C ATOM 953 CD2 LEU A 122 16.141 27.264 20.144 1.00 20.04 C ATOM 954 N VAL A 123 17.794 23.958 16.760 1.00 19.64 N ATOM 955 CA VAL A 123 18.646 23.073 15.982 1.00 19.58 C ATOM 956 C VAL A 123 19.976 23.800 15.685 1.00 20.32 C ATOM 957 O VAL A 123 20.033 25.020 15.642 1.00 19.23 O ATOM 958 CB VAL A 123 18.037 22.582 14.649 1.00 21.85 C ATOM 959 CG1 VAL A 123 17.031 21.443 14.891 1.00 22.03 C ATOM 960 CG2 VAL A 123 17.476 23.778 13.921 1.00 21.03 C ATOM 961 N ARG A 124 21.024 23.032 15.507 1.00 22.48 N ATOM 962 CA ARG A 124 22.362 23.609 15.247 1.00 25.96 C ATOM 963 C ARG A 124 22.483 24.213 13.857 1.00 27.43 C ATOM 964 O ARG A 124 23.154 25.217 13.642 1.00 27.08 O ATOM 965 CB ARG A 124 23.379 22.480 15.392 1.00 25.69 C ATOM 966 CG ARG A 124 23.531 22.069 16.857 1.00 25.66 C ATOM 967 CD ARG A 124 24.441 23.035 17.558 1.00 24.85 C ATOM 968 NE ARG A 124 25.083 22.533 18.757 1.00 25.51 N ATOM 969 CZ ARG A 124 25.846 23.253 19.553 1.00 25.12 C ATOM 970 NH1 ARG A 124 26.027 24.521 19.283 1.00 23.66 N ATOM 971 NH2 ARG A 124 26.432 22.770 20.646 1.00 24.18 N ATOM 972 N THR A 125 21.865 23.504 12.909 1.00 27.50 N ATOM 973 CA THR A 125 21.859 23.928 11.529 1.00 33.03 C ATOM 974 C THR A 125 20.475 23.659 10.938 1.00 35.12 C ATOM 975 O THR A 125 19.771 22.700 11.279 1.00 33.22 O ATOM 976 CB THR A 125 22.858 23.208 10.590 1.00 33.71 C ATOM 977 OG1 THR A 125 22.384 21.870 10.347 1.00 34.58 O ATOM 978 CG2 THR A 125 24.269 23.104 11.135 1.00 34.88 C ATOM 979 N PRO A 126 20.144 24.473 9.949 1.00 40.12 N ATOM 980 CA PRO A 126 18.894 24.319 9.212 1.00 43.24 C ATOM 981 C PRO A 126 18.813 23.135 8.272 1.00 45.20 C ATOM 982 O PRO A 126 17.990 23.109 7.348 1.00 45.38 O ATOM 983 CB PRO A 126 18.734 25.676 8.541 1.00 43.19 C ATOM 984 CG PRO A 126 20.106 26.227 8.384 1.00 42.93 C ATOM 985 CD PRO A 126 20.954 25.620 9.460 1.00 41.78 C ATOM 986 N GLU A 127 19.547 22.054 8.436 1.00 48.92 N ATOM 987 CA GLU A 127 19.479 20.790 7.734 1.00 52.31 C ATOM 988 C GLU A 127 18.044 20.279 7.636 1.00 52.14 C ATOM 989 O GLU A 127 17.245 20.606 8.514 1.00 52.11 O ATOM 990 CB GLU A 127 20.262 19.753 8.562 1.00 56.00 C ATOM 991 CG GLU A 127 20.351 18.387 7.918 1.00 60.11 C ATOM 992 CD GLU A 127 20.778 17.272 8.853 1.00 62.47 C ATOM 993 OE1 GLU A 127 21.359 17.555 9.921 1.00 63.24 O ATOM 994 OE2 GLU A 127 20.519 16.097 8.500 1.00 64.04 O ATOM 995 N VAL A 128 17.715 19.413 6.682 1.00 50.85 N ATOM 996 CA VAL A 128 16.395 18.883 6.419 1.00 50.54 C ATOM 997 C VAL A 128 15.982 17.570 7.061 1.00 50.56 C ATOM 998 O VAL A 128 15.359 16.682 6.434 1.00 51.77 O ATOM 999 CB VAL A 128 16.221 18.743 4.871 1.00 50.34 C ATOM 1000 CG1 VAL A 128 16.759 20.001 4.171 1.00 49.72 C ATOM 1001 CG2 VAL A 128 16.925 17.531 4.281 1.00 49.92 C ATOM 1002 N ASP A 129 16.278 17.333 8.327 1.00 48.59 N ATOM 1003 CA ASP A 129 15.875 16.048 8.951 1.00 46.84 C ATOM 1004 C ASP A 129 14.869 16.440 10.022 1.00 44.57 C ATOM 1005 O ASP A 129 14.965 17.599 10.448 1.00 43.80 O ATOM 1006 CB ASP A 129 17.104 15.258 9.336 1.00 49.33 C ATOM 1007 CG ASP A 129 16.983 14.415 10.589 1.00 52.10 C ATOM 1008 OD1 ASP A 129 16.144 13.484 10.638 1.00 53.59 O ATOM 1009 OD2 ASP A 129 17.735 14.728 11.541 1.00 52.74 O ATOM 1010 N ASP A 130 13.893 15.606 10.371 1.00 42.39 N ATOM 1011 CA ASP A 130 12.884 16.050 11.339 1.00 39.92 C ATOM 1012 C ASP A 130 12.968 15.313 12.672 1.00 38.02 C ATOM 1013 O ASP A 130 12.009 15.214 13.426 1.00 37.16 O ATOM 1014 CB ASP A 130 11.494 15.970 10.710 1.00 41.59 C ATOM 1015 CG ASP A 130 10.966 14.577 10.464 1.00 41.88 C ATOM 1016 OD1 ASP A 130 11.755 13.623 10.610 1.00 42.15 O ATOM 1017 OD2 ASP A 130 9.761 14.435 10.159 1.00 41.39 O ATOM 1018 N GLU A 131 14.148 14.816 13.001 1.00 34.97 N ATOM 1019 CA GLU A 131 14.377 14.142 14.264 1.00 35.21 C ATOM 1020 C GLU A 131 14.081 15.121 15.415 1.00 32.89 C ATOM 1021 O GLU A 131 13.418 14.735 16.378 1.00 32.83 O ATOM 1022 CB GLU A 131 15.811 13.618 14.416 1.00 36.01 C ATOM 1023 CG GLU A 131 16.075 13.212 15.850 1.00 38.70 C ATOM 1024 CD GLU A 131 17.362 12.598 16.291 1.00 41.63 C ATOM 1025 OE1 GLU A 131 18.415 12.688 15.631 1.00 42.25 O ATOM 1026 OE2 GLU A 131 17.318 11.999 17.410 1.00 43.20 O ATOM 1027 N ALA A 132 14.634 16.331 15.333 1.00 29.40 N ATOM 1028 CA ALA A 132 14.370 17.348 16.363 1.00 27.83 C ATOM 1029 C ALA A 132 12.887 17.631 16.533 1.00 25.45 C ATOM 1030 O ALA A 132 12.372 17.732 17.652 1.00 25.02 O ATOM 1031 CB ALA A 132 15.025 18.698 15.974 1.00 25.83 C ATOM 1032 N LEU A 133 12.191 17.808 15.410 1.00 24.53 N ATOM 1033 CA LEU A 133 10.759 18.104 15.445 1.00 25.30 C ATOM 1034 C LEU A 133 9.936 16.958 16.019 1.00 26.33 C ATOM 1035 O LEU A 133 8.957 17.227 16.733 1.00 25.91 O ATOM 1036 CB LEU A 133 10.173 18.555 14.104 1.00 27.02 C ATOM 1037 CG LEU A 133 10.510 19.966 13.611 1.00 29.49 C ATOM 1038 CD1 LEU A 133 10.127 20.141 12.144 1.00 29.95 C ATOM 1039 CD2 LEU A 133 9.832 21.031 14.461 1.00 29.05 C ATOM 1040 N GLU A 134 10.313 15.731 15.780 1.00 27.85 N ATOM 1041 CA GLU A 134 9.603 14.564 16.337 1.00 32.86 C ATOM 1042 C GLU A 134 9.826 14.447 17.840 1.00 31.17 C ATOM 1043 O GLU A 134 8.919 14.243 18.636 1.00 32.00 O ATOM 1044 CB GLU A 134 10.173 13.309 15.637 1.00 37.14 C ATOM 1045 CG GLU A 134 9.631 13.217 14.212 1.00 44.10 C ATOM 1046 CD GLU A 134 8.203 12.690 14.204 1.00 48.38 C ATOM 1047 OE1 GLU A 134 7.828 11.942 15.138 1.00 50.86 O ATOM 1048 OE2 GLU A 134 7.451 13.015 13.256 1.00 51.58 O ATOM 1049 N LYS A 135 11.077 14.688 18.263 1.00 29.25 N ATOM 1050 CA LYS A 135 11.369 14.679 19.698 1.00 30.16 C ATOM 1051 C LYS A 135 10.600 15.819 20.379 1.00 26.94 C ATOM 1052 O LYS A 135 10.219 15.660 21.537 1.00 26.13 O ATOM 1053 CB LYS A 135 12.835 14.845 20.051 1.00 31.36 C ATOM 1054 CG LYS A 135 13.928 13.984 19.459 1.00 36.18 C ATOM 1055 CD LYS A 135 13.946 12.626 20.114 1.00 38.49 C ATOM 1056 CE LYS A 135 14.905 11.622 19.533 1.00 40.87 C ATOM 1057 NZ LYS A 135 16.316 11.898 19.899 1.00 40.51 N ATOM 1058 N PHE A 136 10.493 16.999 19.755 1.00 26.54 N ATOM 1059 CA PHE A 136 9.801 18.144 20.406 1.00 24.13 C ATOM 1060 C PHE A 136 8.331 17.795 20.596 1.00 27.81 C ATOM 1061 O PHE A 136 7.736 17.984 21.649 1.00 26.39 O ATOM 1062 CB PHE A 136 9.967 19.405 19.594 1.00 22.50 C ATOM 1063 CG PHE A 136 9.364 20.704 19.991 1.00 22.82 C ATOM 1064 CD1 PHE A 136 9.681 21.346 21.180 1.00 25.06 C ATOM 1065 CD2 PHE A 136 8.464 21.337 19.169 1.00 23.71 C ATOM 1066 CE1 PHE A 136 9.117 22.569 21.514 1.00 22.63 C ATOM 1067 CE2 PHE A 136 7.886 22.555 19.488 1.00 25.80 C ATOM 1068 CZ PHE A 136 8.256 23.193 20.665 1.00 23.97 C ATOM 1069 N ASP A 137 7.755 17.229 19.542 1.00 30.39 N ATOM 1070 CA ASP A 137 6.400 16.743 19.535 1.00 34.93 C ATOM 1071 C ASP A 137 6.115 15.751 20.648 1.00 34.88 C ATOM 1072 O ASP A 137 5.087 15.854 21.316 1.00 34.41 O ATOM 1073 CB ASP A 137 6.167 15.943 18.225 1.00 38.30 C ATOM 1074 CG ASP A 137 5.001 16.656 17.561 1.00 41.89 C ATOM 1075 OD1 ASP A 137 5.149 17.894 17.509 1.00 41.75 O ATOM 1076 OD2 ASP A 137 4.041 15.963 17.167 1.00 45.80 O ATOM 1077 N LYS A 138 7.026 14.808 20.795 1.00 36.52 N ATOM 1078 CA LYS A 138 6.962 13.790 21.833 1.00 38.70 C ATOM 1079 C LYS A 138 7.185 14.347 23.233 1.00 39.41 C ATOM 1080 O LYS A 138 6.527 13.953 24.209 1.00 38.10 O ATOM 1081 CB LYS A 138 7.990 12.716 21.490 1.00 41.73 C ATOM 1082 CG LYS A 138 8.211 11.660 22.552 1.00 46.20 C ATOM 1083 CD LYS A 138 9.252 10.626 22.119 1.00 48.44 C ATOM 1084 CE LYS A 138 9.623 9.733 23.310 1.00 50.57 C ATOM 1085 NZ LYS A 138 10.831 8.897 23.048 1.00 51.64 N ATOM 1086 N ALA A 139 8.122 15.293 23.393 1.00 36.42 N ATOM 1087 CA ALA A 139 8.311 15.910 24.702 1.00 34.29 C ATOM 1088 C ALA A 139 7.093 16.746 25.079 1.00 34.75 C ATOM 1089 O ALA A 139 6.746 16.744 26.267 1.00 36.54 O ATOM 1090 CB ALA A 139 9.597 16.707 24.734 1.00 34.79 C ATOM 1091 N LEU A 140 6.335 17.374 24.196 1.00 32.63 N ATOM 1092 CA LEU A 140 5.191 18.180 24.485 1.00 33.49 C ATOM 1093 C LEU A 140 3.851 17.418 24.591 1.00 35.31 C ATOM 1094 O LEU A 140 2.822 18.055 24.826 1.00 31.99 O ATOM 1095 CB LEU A 140 4.969 19.231 23.390 1.00 33.49 C ATOM 1096 CG LEU A 140 6.079 20.245 23.092 1.00 34.81 C ATOM 1097 CD1 LEU A 140 5.556 21.268 22.096 1.00 35.78 C ATOM 1098 CD2 LEU A 140 6.603 20.951 24.327 1.00 35.10 C ATOM 1099 N LYS A 141 3.907 16.098 24.443 1.00 36.88 N ATOM 1100 CA LYS A 141 2.668 15.305 24.523 1.00 41.17 C ATOM 1101 C LYS A 141 2.124 15.330 25.936 1.00 39.90 C ATOM 1102 O LYS A 141 0.917 15.325 26.150 1.00 41.38 O ATOM 1103 CB LYS A 141 2.914 13.906 23.974 1.00 44.51 C ATOM 1104 CG LYS A 141 3.522 12.862 24.879 1.00 48.18 C ATOM 1105 CD LYS A 141 4.404 11.856 24.153 1.00 51.75 C ATOM 1106 CE LYS A 141 3.915 11.453 22.766 1.00 53.61 C ATOM 1107 NZ LYS A 141 5.061 11.263 21.819 1.00 54.66 N ATOM 1108 N ALA A 142 2.977 15.500 26.944 1.00 39.43 N ATOM 1109 CA ALA A 142 2.541 15.578 28.325 1.00 38.35 C ATOM 1110 C ALA A 142 2.106 16.951 28.810 1.00 39.38 C ATOM 1111 O ALA A 142 1.692 17.030 29.981 1.00 39.67 O ATOM 1112 CB ALA A 142 3.650 15.077 29.230 1.00 37.93 C ATOM 1113 N LEU A 143 2.230 18.001 28.018 1.00 37.73 N ATOM 1114 CA LEU A 143 1.868 19.348 28.458 1.00 36.57 C ATOM 1115 C LEU A 143 0.690 19.889 27.676 1.00 37.38 C ATOM 1116 O LEU A 143 0.427 19.545 26.519 1.00 38.11 O ATOM 1117 CB LEU A 143 3.106 20.248 28.264 1.00 36.86 C ATOM 1118 CG LEU A 143 4.411 19.718 28.878 1.00 36.56 C ATOM 1119 CD1 LEU A 143 5.597 20.592 28.509 1.00 36.70 C ATOM 1120 CD2 LEU A 143 4.277 19.645 30.397 1.00 37.90 C ATOM 1121 N PRO A 144 -0.038 20.831 28.264 1.00 37.68 N ATOM 1122 CA PRO A 144 -1.174 21.465 27.626 1.00 37.34 C ATOM 1123 C PRO A 144 -0.775 22.699 26.837 1.00 36.66 C ATOM 1124 O PRO A 144 -0.904 23.850 27.244 1.00 37.75 O ATOM 1125 CB PRO A 144 -2.083 21.716 28.830 1.00 37.71 C ATOM 1126 CG PRO A 144 -1.143 22.045 29.943 1.00 36.89 C ATOM 1127 CD PRO A 144 0.147 21.328 29.658 1.00 36.99 C ATOM 1128 N MET A 145 -0.331 22.493 25.596 1.00 34.99 N ATOM 1129 CA MET A 145 0.051 23.568 24.685 1.00 33.49 C ATOM 1130 C MET A 145 -1.136 24.110 23.895 1.00 34.21 C ATOM 1131 O MET A 145 -1.833 23.329 23.226 1.00 35.58 O ATOM 1132 CB MET A 145 1.140 22.944 23.790 1.00 33.54 C ATOM 1133 CG MET A 145 2.373 22.562 24.639 1.00 34.49 C ATOM 1134 SD MET A 145 3.056 24.055 25.413 1.00 34.63 S ATOM 1135 CE MET A 145 3.377 23.475 27.066 1.00 36.34 C ATOM 1136 N HIS A 146 -1.455 25.424 23.904 1.00 31.74 N ATOM 1137 CA HIS A 146 -2.599 25.864 23.107 1.00 33.33 C ATOM 1138 C HIS A 146 -2.205 26.601 21.827 1.00 31.09 C ATOM 1139 O HIS A 146 -3.082 27.064 21.083 1.00 28.16 O ATOM 1140 CB HIS A 146 -3.595 26.730 23.901 1.00 37.47 C ATOM 1141 CG HIS A 146 -4.111 25.910 25.053 1.00 41.82 C ATOM 1142 ND1 HIS A 146 -4.448 24.581 24.842 1.00 45.01 N ATOM 1143 CD2 HIS A 146 -4.362 26.158 26.350 1.00 43.76 C ATOM 1144 CE1 HIS A 146 -4.862 24.035 25.973 1.00 45.55 C ATOM 1145 NE2 HIS A 146 -4.831 24.983 26.895 1.00 45.91 N ATOM 1146 N ILE A 147 -0.898 26.717 21.567 1.00 27.03 N ATOM 1147 CA ILE A 147 -0.488 27.414 20.349 1.00 25.25 C ATOM 1148 C ILE A 147 0.829 26.767 19.956 1.00 26.33 C ATOM 1149 O ILE A 147 1.636 26.505 20.860 1.00 23.19 O ATOM 1150 CB ILE A 147 -0.406 28.937 20.445 1.00 25.63 C ATOM 1151 CG1 ILE A 147 0.225 29.480 19.165 1.00 25.50 C ATOM 1152 CG2 ILE A 147 0.447 29.387 21.634 1.00 26.37 C ATOM 1153 CD1 ILE A 147 0.184 30.962 18.967 1.00 27.97 C ATOM 1154 N ARG A 148 0.936 26.497 18.662 1.00 25.91 N ATOM 1155 CA ARG A 148 2.162 25.767 18.230 1.00 29.06 C ATOM 1156 C ARG A 148 2.565 26.391 16.909 1.00 29.44 C ATOM 1157 O ARG A 148 1.649 26.578 16.095 1.00 27.98 O ATOM 1158 CB ARG A 148 1.703 24.323 18.243 1.00 33.77 C ATOM 1159 CG ARG A 148 2.493 23.283 17.496 1.00 43.18 C ATOM 1160 CD ARG A 148 3.984 23.433 17.700 1.00 49.89 C ATOM 1161 NE ARG A 148 4.746 22.224 17.771 1.00 55.71 N ATOM 1162 CZ ARG A 148 4.472 20.953 17.986 1.00 57.56 C ATOM 1163 NH1 ARG A 148 3.257 20.474 18.185 1.00 59.54 N ATOM 1164 NH2 ARG A 148 5.503 20.109 17.989 1.00 58.76 N ATOM 1165 N LEU A 149 3.821 26.779 16.745 1.00 27.60 N ATOM 1166 CA LEU A 149 4.314 27.491 15.573 1.00 29.89 C ATOM 1167 C LEU A 149 5.560 26.741 15.052 1.00 31.03 C ATOM 1168 O LEU A 149 6.343 26.268 15.887 1.00 26.66 O ATOM 1169 CB LEU A 149 4.901 28.864 15.906 1.00 31.28 C ATOM 1170 CG LEU A 149 4.213 30.196 15.864 1.00 34.73 C ATOM 1171 CD1 LEU A 149 2.753 30.087 16.293 1.00 36.28 C ATOM 1172 CD2 LEU A 149 4.833 31.239 16.802 1.00 36.08 C ATOM 1173 N SER A 150 5.687 26.747 13.737 1.00 31.46 N ATOM 1174 CA SER A 150 6.818 26.066 13.129 1.00 35.51 C ATOM 1175 C SER A 150 7.420 26.966 12.036 1.00 37.88 C ATOM 1176 O SER A 150 6.668 27.472 11.207 1.00 34.66 O ATOM 1177 CB SER A 150 6.381 24.719 12.523 1.00 35.51 C ATOM 1178 OG SER A 150 7.274 24.578 11.413 1.00 42.81 O ATOM 1179 N PHE A 151 8.734 27.140 12.072 1.00 40.07 N ATOM 1180 CA PHE A 151 9.428 28.040 11.186 1.00 46.74 C ATOM 1181 C PHE A 151 10.056 27.420 9.959 1.00 51.93 C ATOM 1182 O PHE A 151 10.373 26.250 9.870 1.00 51.18 O ATOM 1183 CB PHE A 151 10.481 28.899 11.936 1.00 45.55 C ATOM 1184 CG PHE A 151 9.682 29.748 12.906 1.00 46.78 C ATOM 1185 CD1 PHE A 151 8.980 30.849 12.456 1.00 44.93 C ATOM 1186 CD2 PHE A 151 9.603 29.382 14.243 1.00 46.74 C ATOM 1187 CE1 PHE A 151 8.237 31.597 13.339 1.00 45.71 C ATOM 1188 CE2 PHE A 151 8.845 30.138 15.119 1.00 45.89 C ATOM 1189 CZ PHE A 151 8.162 31.243 14.673 1.00 45.41 C ATOM 1190 N ASN A 152 10.119 28.296 8.957 1.00 59.69 N ATOM 1191 CA ASN A 152 10.598 28.046 7.621 1.00 66.47 C ATOM 1192 C ASN A 152 11.782 28.931 7.251 1.00 68.92 C ATOM 1193 O ASN A 152 12.867 28.375 6.941 1.00 71.84 O ATOM 1194 CB ASN A 152 9.491 28.345 6.581 1.00 69.98 C ATOM 1195 CG ASN A 152 8.297 27.478 6.952 1.00 72.70 C ATOM 1196 OD1 ASN A 152 8.288 26.304 6.585 1.00 74.06 O ATOM 1197 ND2 ASN A 152 7.399 28.075 7.732 1.00 73.70 N TER 1198 ASN A 152 HETATM 1199 O HOH A 163 14.595 42.981 35.308 1.00 33.51 O HETATM 1200 O HOH A 164 19.743 38.947 32.404 1.00 35.44 O HETATM 1201 O HOH A 165 11.812 41.905 34.276 1.00 42.01 O HETATM 1202 O HOH A 166 25.976 25.181 14.395 1.00 39.27 O HETATM 1203 O HOH A 167 21.296 24.429 37.301 1.00 35.50 O HETATM 1204 O HOH A 168 19.837 36.136 36.113 1.00 42.82 O HETATM 1205 O HOH A 169 12.801 37.392 33.169 1.00 45.42 O HETATM 1206 O HOH A 170 -3.932 26.574 29.641 1.00 53.80 O HETATM 1207 O HOH A 171 31.662 25.939 26.410 1.00 39.63 O HETATM 1208 O HOH A 172 9.276 31.108 23.254 1.00 45.31 O HETATM 1209 O HOH A 173 21.958 31.475 15.082 1.00 43.48 O HETATM 1210 O HOH A 174 21.262 20.470 13.297 1.00 52.85 O HETATM 1211 O HOH A 175 24.150 17.460 35.090 1.00 60.24 O HETATM 1212 O HOH A 176 26.202 20.908 33.302 1.00 44.34 O HETATM 1213 O HOH A 177 25.528 24.836 34.936 1.00 41.37 O HETATM 1214 O HOH A 178 28.505 33.591 35.289 1.00 56.92 O HETATM 1215 O HOH A 179 14.695 28.743 5.169 1.00 71.11 O HETATM 1216 O HOH A 180 19.995 39.295 40.139 1.00 47.18 O HETATM 1217 O HOH A 181 29.092 20.426 21.318 1.00 41.25 O HETATM 1218 O HOH A 182 16.826 17.380 13.260 1.00 45.30 O HETATM 1219 O HOH A 183 15.509 25.501 40.552 1.00 52.02 O HETATM 1220 O HOH A 184 -4.844 30.276 25.770 1.00 41.43 O HETATM 1221 O HOH A 185 2.716 17.137 20.908 1.00 67.97 O HETATM 1222 O HOH A 186 21.420 20.831 44.697 1.00 61.07 O HETATM 1223 O HOH A 187 32.504 28.626 29.261 1.00 44.74 O HETATM 1224 O HOH A 188 -0.526 25.952 32.996 1.00 57.57 O HETATM 1225 O HOH A 189 13.475 31.069 5.376 1.00 74.00 O HETATM 1226 O HOH A 190 -3.765 35.647 29.279 1.00 54.20 O HETATM 1227 O HOH A 191 23.383 18.479 13.052 1.00 69.25 O HETATM 1228 O HOH A 192 17.198 41.801 34.449 1.00 38.06 O HETATM 1229 O HOH A 193 26.888 20.371 14.886 1.00 56.29 O HETATM 1230 O HOH A 194 8.381 12.098 10.415 1.00 58.38 O HETATM 1231 O HOH A 195 30.589 21.141 32.494 1.00 55.33 O HETATM 1232 O HOH A 196 20.035 33.382 14.196 1.00 63.21 O HETATM 1233 O HOH A 197 8.007 37.539 15.146 1.00 48.12 O HETATM 1234 O HOH A 198 18.619 40.621 14.192 1.00 62.35 O HETATM 1235 O HOH A 199 7.717 41.902 26.101 1.00 58.64 O HETATM 1236 O HOH A 200 9.773 26.600 39.220 1.00 79.49 O HETATM 1237 O HOH A 201 -1.264 36.585 34.130 1.00 83.17 O HETATM 1238 O HOH A 202 9.549 38.710 18.527 1.00 47.64 O HETATM 1239 O HOH A 203 -6.226 25.775 29.774 1.00 59.33 O HETATM 1240 O HOH A 204 23.448 20.408 41.643 1.00 80.15 O HETATM 1241 O HOH A 205 21.928 40.074 34.516 1.00 71.58 O HETATM 1242 O HOH A 206 11.991 31.636 39.605 1.00 60.46 O HETATM 1243 O HOH A 207 32.596 19.633 29.247 1.00 58.17 O HETATM 1244 O HOH A 208 1.697 14.384 18.282 1.00 72.66 O HETATM 1245 O HOH A 209 16.433 31.637 15.520 1.00 40.99 O HETATM 1246 O HOH A 210 27.005 26.576 15.897 1.00 51.04 O HETATM 1247 O HOH A 211 13.613 30.758 9.026 1.00 51.48 O HETATM 1248 O HOH A 212 12.323 25.739 7.695 1.00 54.52 O HETATM 1249 O HOH A 213 9.474 30.322 37.501 1.00 53.04 O HETATM 1250 O HOH A 214 4.958 30.125 41.138 1.00 65.98 O HETATM 1251 O HOH A 215 1.934 40.666 15.070 1.00 61.26 O HETATM 1252 O HOH A 216 4.464 22.052 34.607 1.00 65.27 O HETATM 1253 O HOH A 217 16.899 33.674 13.867 1.00 67.94 O HETATM 1254 O HOH A 218 13.435 30.827 13.502 1.00 53.71 O HETATM 1255 O HOH A 219 28.687 20.882 33.755 1.00 52.15 O HETATM 1256 O HOH A 220 12.022 49.647 14.584 1.00 57.69 O HETATM 1257 O HOH A 221 -2.080 25.477 30.837 1.00 58.85 O HETATM 1258 O HOH A 222 16.545 30.200 13.572 1.00 72.05 O HETATM 1259 O HOH A 223 28.854 30.711 21.943 1.00 60.66 O HETATM 1260 O HOH A 224 1.192 23.200 32.951 1.00 61.84 O HETATM 1261 O HOH A 225 11.010 10.593 41.632 1.00 72.73 O HETATM 1262 O HOH A 226 30.574 34.240 20.983 1.00 67.46 O HETATM 1263 O HOH A 227 13.036 40.183 15.262 1.00 72.35 O HETATM 1264 O HOH A 228 14.616 27.755 9.683 1.00 71.03 O HETATM 1265 O HOH A 229 24.126 29.273 42.136 1.00 62.82 O HETATM 1266 O HOH A 230 13.083 38.257 13.772 1.00 67.92 O HETATM 1267 O HOH A 231 14.802 30.068 11.346 1.00 68.90 O HETATM 1268 O HOH A 232 22.102 31.641 24.940 1.00 80.28 O HETATM 1269 O HOH A 233 13.529 13.587 23.829 1.00 65.83 O HETATM 1270 O HOH A 234 6.943 12.272 18.389 1.00 65.25 O HETATM 1271 O HOH A 235 5.917 21.686 15.499 1.00 67.21 O HETATM 1272 O HOH A 236 12.403 50.543 18.074 1.00 64.87 O HETATM 1273 O HOH A 237 9.560 18.774 34.240 1.00 61.71 O HETATM 1274 O HOH A 238 3.937 28.365 35.235 1.00 61.20 O HETATM 1275 O HOH A 239 11.055 13.299 23.107 1.00 56.48 O HETATM 1276 O HOH A 240 8.060 51.630 12.727 1.00 70.95 O HETATM 1277 O HOH A 241 12.668 43.217 20.673 1.00 80.14 O HETATM 1278 O HOH A 242 18.842 16.408 6.398 1.00 73.55 O HETATM 1279 O HOH A 243 1.840 22.086 20.241 1.00 81.79 O HETATM 1280 O HOH A 244 17.209 17.816 36.234 1.00 68.09 O HETATM 1281 O HOH A 245 15.507 17.592 41.704 1.00 70.53 O HETATM 1282 O HOH A 246 8.429 29.547 41.441 1.00 73.23 O HETATM 1283 O HOH A 247 10.115 41.499 41.625 1.00 70.33 O HETATM 1284 O HOH A 248 13.347 45.366 17.515 1.00 72.03 O HETATM 1285 O HOH A 249 19.981 32.517 40.745 1.00 72.25 O HETATM 1286 O HOH A 250 14.392 21.152 4.393 1.00 72.12 O HETATM 1287 O HOH A 251 6.944 44.661 17.390 1.00 73.64 O HETATM 1288 O HOH A 252 18.838 38.377 35.033 1.00 75.13 O HETATM 1289 O HOH A 253 18.195 41.485 11.490 1.00 77.25 O HETATM 1290 O HOH A 254 -2.598 24.228 19.941 1.00 47.78 O HETATM 1291 O HOH A 255 25.174 25.113 16.308 1.00 79.14 O HETATM 1292 O HOH A 256 5.358 26.480 37.093 1.00 66.19 O HETATM 1293 O HOH A 257 -0.644 33.147 20.073 1.00 69.65 O HETATM 1294 O HOH A 258 20.806 37.608 33.695 1.00 75.73 O HETATM 1295 O HOH A 259 3.054 29.433 39.075 1.00 75.76 O HETATM 1296 O HOH A 260 18.371 46.906 10.942 1.00 76.68 O HETATM 1297 O HOH A 261 30.656 23.775 33.535 1.00 73.56 O HETATM 1298 O HOH A 262 15.000 38.213 22.622 1.00 78.33 O HETATM 1299 O HOH A 263 11.250 46.201 40.135 1.00 80.77 O HETATM 1300 O HOH A 264 3.394 44.835 18.064 1.00 77.95 O HETATM 1301 O HOH A 265 15.033 44.279 22.936 1.00 77.15 O HETATM 1302 O HOH A 266 8.645 24.230 9.008 1.00 77.59 O CONECT 835 930 CONECT 930 835 MASTER 309 0 0 5 10 0 0 6 1301 1 2 13 END