HEADER STRUCTURAL GENOMICS, UNKNOWN FUNCTION 31-MAR-08 3CPK TITLE CRYSTAL STRUCTURE OF THE Q7W7N7_BORPA PROTEIN FROM TITLE 2 BORDETELLA PARAPERTUSSIS. NORTHEAST STRUCTURAL GENOMICS TITLE 3 CONSORTIUM TARGET BER31 COMPND MOL_ID: 1; COMPND 2 MOLECULE: UNCHARACTERIZED PROTEIN Q7W7N7_BORPA; COMPND 3 CHAIN: A; COMPND 4 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: BORDETELLA PARAPERTUSSIS 12822; SOURCE 3 ORGANISM_TAXID: 257311; SOURCE 4 STRAIN: 12822 / NCTC 13253; SOURCE 5 ATCC: BAA-587; SOURCE 6 GENE: BPP2477; SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 8 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 9 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)+MAGIC; SOURCE 10 EXPRESSION_SYSTEM_VECTOR: SUMO KEYWDS Q7W7N7_BORPA, BPP2477, BER31, NESG, STRUCTURAL GENOMICS, KEYWDS 2 PSI-2, PROTEIN STRUCTURE INITIATIVE, NORTHEAST STRUCTURAL KEYWDS 3 GENOMICS CONSORTIUM, UNKNOWN FUNCTION EXPDTA X-RAY DIFFRACTION AUTHOR S.M.VOROBIEV,M.ABASHIDZE,J.SEETHARAMAN,L.ZHAO,H.JANJUA, AUTHOR 2 R.XIAO,T.B.ACTON,G.T.MONTELIONE,L.TONG,J.F.HUNT,NORTHEAST AUTHOR 3 STRUCTURAL GENOMICS CONSORTIUM (NESG) REVDAT 2 24-FEB-09 3CPK 1 VERSN REVDAT 1 15-APR-08 3CPK 0 JRNL AUTH S.M.VOROBIEV,M.ABASHIDZE,J.SEETHARAMAN,L.ZHAO, JRNL AUTH 2 H.JANJUA,T.B.ACTON,G.T.MONTELIONE,L.TONG,J.F.HUNT JRNL TITL CRYSTAL STRUCTURE OF THE Q7W7N7_BORPA PROTEIN FROM JRNL TITL 2 BORDETELLA PARAPERTUSSIS. JRNL REF TO BE PUBLISHED JRNL REFN REMARK 1 REMARK 2 REMARK 2 RESOLUTION. 2.50 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : CNS 1.1 REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE- REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU, REMARK 3 : READ,RICE,SIMONSON,WARREN REMARK 3 REMARK 3 REFINEMENT TARGET : ENGH & HUBER REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 40.83 REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000 REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 372303.380 REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000 REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 85.4 REMARK 3 NUMBER OF REFLECTIONS : 6408 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM REMARK 3 R VALUE (WORKING SET) : 0.209 REMARK 3 FREE R VALUE : 0.253 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.400 REMARK 3 FREE R VALUE TEST SET COUNT : 345 REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.014 REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : 6 REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.50 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.66 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 66.00 REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 775 REMARK 3 BIN R VALUE (WORKING SET) : 0.2610 REMARK 3 BIN FREE R VALUE : 0.2810 REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.40 REMARK 3 BIN FREE R VALUE TEST SET COUNT : 44 REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.042 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 852 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 0 REMARK 3 SOLVENT ATOMS : 44 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 28.10 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 44.30 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 11.08000 REMARK 3 B22 (A**2) : 11.08000 REMARK 3 B33 (A**2) : -22.17000 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : 0.00000 REMARK 3 B23 (A**2) : 0.00000 REMARK 3 REMARK 3 ESTIMATED COORDINATE ERROR. REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.28 REMARK 3 ESD FROM SIGMAA (A) : 0.31 REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00 REMARK 3 REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR. REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.37 REMARK 3 ESD FROM C-V SIGMAA (A) : 0.27 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. REMARK 3 BOND LENGTHS (A) : 0.009 REMARK 3 BOND ANGLES (DEGREES) : 1.70 REMARK 3 DIHEDRAL ANGLES (DEGREES) : 26.30 REMARK 3 IMPROPER ANGLES (DEGREES) : 1.27 REMARK 3 REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED REMARK 3 REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA REMARK 3 MAIN-CHAIN BOND (A**2) : 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 BULK SOLVENT MODELING. REMARK 3 METHOD USED : FLAT MODEL REMARK 3 KSOL : 0.35 REMARK 3 BSOL : 57.27 REMARK 3 REMARK 3 NCS MODEL : NULL REMARK 3 REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL REMARK 3 REMARK 3 PARAMETER FILE 1 : PROTEIN_REP.PARAM REMARK 3 PARAMETER FILE 2 : WATER_REP.PARAM REMARK 3 PARAMETER FILE 3 : ION.PARAM REMARK 3 PARAMETER FILE 4 : NULL REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP REMARK 3 TOPOLOGY FILE 2 : WATER.TOP REMARK 3 TOPOLOGY FILE 3 : ION.TOP REMARK 3 TOPOLOGY FILE 4 : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: THE BIJVOET DIFFERENCES WERE USED IN REMARK 3 PHASING REMARK 4 REMARK 4 3CPK COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-APR-08. REMARK 100 THE RCSB ID CODE IS RCSB047059. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 30-JAN-08 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 7.0 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : NSLS REMARK 200 BEAMLINE : X4A REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.97901, 0.97928, 0.96785 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4 REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO REMARK 200 DATA SCALING SOFTWARE : SCALEPACK REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 15148 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500 REMARK 200 RESOLUTION RANGE LOW (A) : 50.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.6 REMARK 200 DATA REDUNDANCY : 5.600 REMARK 200 R MERGE (I) : 0.12000 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 20.4000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.59 REMARK 200 COMPLETENESS FOR SHELL (%) : 96.6 REMARK 200 DATA REDUNDANCY IN SHELL : 5.10 REMARK 200 R MERGE FOR SHELL (I) : 0.56500 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 2.950 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: MAD REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD REMARK 200 SOFTWARE USED: SOLVE REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: THE STRUCTURE FACTOR FILE CONTAINS FRIEDEL PAIRS REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 29.70 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.75 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 15-20% PEG 8000, 0.1M MANGANESE REMARK 280 CHLORIDE, 0.1M MOPS PH 7.0, VAPOR DIFFUSION, HANGING DROP, REMARK 280 TEMPERATURE 277K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2 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 -Y+1/2,X+1/2,Z+3/4 REMARK 290 4555 Y+1/2,-X+1/2,Z+1/4 REMARK 290 5555 -X+1/2,Y+1/2,-Z+3/4 REMARK 290 6555 X+1/2,-Y+1/2,-Z+1/4 REMARK 290 7555 Y,X,-Z REMARK 290 8555 -Y,-X,-Z+1/2 REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 59.11200 REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 21.75500 REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 21.75500 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 88.66800 REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 21.75500 REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 21.75500 REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 29.55600 REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 21.75500 REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 21.75500 REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 88.66800 REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 21.75500 REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 21.75500 REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 29.55600 REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 59.11200 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 300 REMARK: AUTHORS STATE THAT THE BIOLOGICAL UNIT IS A MONOMER REMARK 300 ACCORDING TO AGGREGATION SCREENING 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: MONOMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC REMARK 350 SOFTWARE USED: PISA 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 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 MSE A 1 REMARK 465 LYS A 2 REMARK 465 LEU A 3 REMARK 465 HIS A 4 REMARK 465 THR A 5 REMARK 465 ASP A 6 REMARK 465 GLU A 65 REMARK 465 VAL A 66 REMARK 465 VAL A 67 REMARK 465 ARG A 68 REMARK 465 ASP A 69 REMARK 465 PRO A 70 REMARK 465 LEU A 71 REMARK 465 ALA A 72 REMARK 465 PHE A 73 REMARK 465 LEU A 74 REMARK 465 ASP A 75 REMARK 465 GLU A 76 REMARK 465 PRO A 77 REMARK 465 GLU A 78 REMARK 465 ALA A 79 REMARK 465 GLY A 80 REMARK 465 ALA A 81 REMARK 465 GLY A 82 REMARK 465 ALA A 83 REMARK 465 ARG A 84 REMARK 465 PRO A 85 REMARK 465 ALA A 86 REMARK 465 ASN A 87 REMARK 465 GLY A 148 REMARK 465 ASP A 149 REMARK 465 SER A 150 REMARK 470 REMARK 470 MISSING ATOM REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS(M=MODEL NUMBER; REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 470 I=INSERTION CODE): REMARK 470 M RES CSSEQI ATOMS REMARK 470 ARG A 48 CG CD NE CZ NH1 NH2 REMARK 470 LEU A 63 CG CD1 CD2 REMARK 470 GLU A 106 CG CD OE1 OE2 REMARK 470 ARG A 139 CG CD NE CZ NH1 NH2 REMARK 470 ASP A 147 CG OD1 OD2 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 ALA A 8 67.87 -105.07 REMARK 500 PRO A 45 65.60 -60.39 REMARK 500 GLN A 47 -23.37 -143.48 REMARK 500 PRO A 49 -17.04 -45.42 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 207 DISTANCE = 5.40 ANGSTROMS REMARK 525 HOH A 219 DISTANCE = 8.56 ANGSTROMS REMARK 525 HOH A 226 DISTANCE = 18.05 ANGSTROMS REMARK 525 HOH A 228 DISTANCE = 5.58 ANGSTROMS REMARK 525 HOH A 229 DISTANCE = 11.33 ANGSTROMS REMARK 525 HOH A 230 DISTANCE = 14.56 ANGSTROMS REMARK 525 HOH A 232 DISTANCE = 6.61 ANGSTROMS REMARK 525 HOH A 235 DISTANCE = 5.95 ANGSTROMS REMARK 525 HOH A 241 DISTANCE = 6.09 ANGSTROMS REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: BER31 RELATED DB: TARGETDB DBREF 3CPK A 1 150 UNP Q7W7N7 Q7W7N7_BORPA 1 150 SEQRES 1 A 150 MSE LYS LEU HIS THR ASP PRO ALA THR ALA LEU ASN THR SEQRES 2 A 150 VAL THR ALA TYR GLY ASP GLY TYR ILE GLU VAL ASN GLN SEQRES 3 A 150 VAL ARG PHE SER HIS ALA ILE ALA PHE ALA PRO GLU GLY SEQRES 4 A 150 PRO VAL ALA SER TRP PRO VAL GLN ARG PRO ALA ASP ILE SEQRES 5 A 150 THR ALA SER LEU LEU GLN GLN ALA ALA GLY LEU ALA GLU SEQRES 6 A 150 VAL VAL ARG ASP PRO LEU ALA PHE LEU ASP GLU PRO GLU SEQRES 7 A 150 ALA GLY ALA GLY ALA ARG PRO ALA ASN ALA PRO GLU VAL SEQRES 8 A 150 LEU LEU VAL GLY THR GLY ARG ARG GLN HIS LEU LEU GLY SEQRES 9 A 150 PRO GLU GLN VAL ARG PRO LEU LEU ALA MSE GLY VAL GLY SEQRES 10 A 150 VAL GLU ALA MSE ASP THR GLN ALA ALA ALA ARG THR TYR SEQRES 11 A 150 ASN ILE LEU MSE ALA GLU GLY ARG ARG VAL VAL VAL ALA SEQRES 12 A 150 LEU LEU PRO ASP GLY ASP SER MODRES 3CPK MSE A 114 MET SELENOMETHIONINE MODRES 3CPK MSE A 121 MET SELENOMETHIONINE MODRES 3CPK MSE A 134 MET SELENOMETHIONINE HET MSE A 114 8 HET MSE A 121 8 HET MSE A 134 8 HETNAM MSE SELENOMETHIONINE FORMUL 1 MSE 3(C5 H11 N O2 SE) FORMUL 2 HOH *44(H2 O) HELIX 1 1 ARG A 48 ILE A 52 5 5 HELIX 2 2 THR A 53 GLY A 62 1 10 HELIX 3 3 GLY A 104 ALA A 113 1 10 HELIX 4 4 ASP A 122 GLU A 136 1 15 SHEET 1 A 3 VAL A 14 GLY A 18 0 SHEET 2 A 3 TYR A 21 VAL A 24 -1 O TYR A 21 N GLY A 18 SHEET 3 A 3 VAL A 27 PHE A 29 -1 O VAL A 27 N VAL A 24 SHEET 1 B 5 ALA A 42 SER A 43 0 SHEET 2 B 5 ILE A 33 PHE A 35 -1 N ALA A 34 O ALA A 42 SHEET 3 B 5 VAL A 140 LEU A 144 -1 O LEU A 144 N ILE A 33 SHEET 4 B 5 VAL A 91 GLY A 95 1 N GLY A 95 O ALA A 143 SHEET 5 B 5 GLY A 117 MSE A 121 1 O GLU A 119 N VAL A 94 LINK C ALA A 113 N MSE A 114 1555 1555 1.33 LINK C MSE A 114 N GLY A 115 1555 1555 1.33 LINK C ALA A 120 N MSE A 121 1555 1555 1.32 LINK C MSE A 121 N ASP A 122 1555 1555 1.33 LINK C LEU A 133 N MSE A 134 1555 1555 1.33 LINK C MSE A 134 N ALA A 135 1555 1555 1.33 CRYST1 43.510 43.510 118.224 90.00 90.00 90.00 P 43 21 2 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 0.022983 0.000000 0.000000 0.00000 SCALE2 0.000000 0.022983 0.000000 0.00000 SCALE3 0.000000 0.000000 0.008459 0.00000 REMARK PdbStat -- REMARK PdbStat -- PDB COORDINATES FOR 3CPK.PDB, MODEL/S 1 3CPK.PDB REMARK PdbStat -- SEQRES 1 A 162 PRO ALA THR ALA LEU ASN THR VAL THR ALA TYR GLY ASP SEQRES 2 A 162 GLY TYR ILE GLU VAL ASN GLN VAL ARG PHE SER HIS ALA SEQRES 3 A 162 ILE ALA PHE ALA PRO GLU GLY PRO VAL ALA SER TRP PRO SEQRES 4 A 162 VAL GLN ARG PRO ALA ASP ILE THR ALA SER LEU LEU GLN SEQRES 5 A 162 GLN ALA ALA GLY LEU ALA ALA PRO GLU VAL LEU LEU VAL SEQRES 6 A 162 GLY THR GLY ARG ARG GLN HIS LEU LEU GLY PRO GLU GLN SEQRES 7 A 162 VAL ARG PRO LEU LEU ALA MSE GLY VAL GLY VAL GLU ALA SEQRES 8 A 162 MSE ASP THR GLN ALA ALA ALA ARG THR TYR ASN ILE LEU SEQRES 9 A 162 MSE ALA GLU GLY ARG ARG VAL VAL VAL ALA LEU LEU PRO SEQRES 10 A 162 ASP HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH SEQRES 11 A 162 HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH SEQRES 12 A 162 HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH SEQRES 13 A 162 HOH HOH HOH HOH HOH HOH REMARK PdbStat -- REMARK PdbStat -- PDB COORDINATES FOR 3CPK.PDB, MODEL/S 1 3CPK.PDB REMARK PdbStat -- SEQRES 1 A 162 PRO ALA THR ALA LEU ASN THR VAL THR ALA TYR GLY ASP SEQRES 2 A 162 GLY TYR ILE GLU VAL ASN GLN VAL ARG PHE SER HIS ALA SEQRES 3 A 162 ILE ALA PHE ALA PRO GLU GLY PRO VAL ALA SER TRP PRO SEQRES 4 A 162 VAL GLN ARG PRO ALA ASP ILE THR ALA SER LEU LEU GLN SEQRES 5 A 162 GLN ALA ALA GLY LEU ALA ALA PRO GLU VAL LEU LEU VAL SEQRES 6 A 162 GLY THR GLY ARG ARG GLN HIS LEU LEU GLY PRO GLU GLN SEQRES 7 A 162 VAL ARG PRO LEU LEU ALA MSE GLY VAL GLY VAL GLU ALA SEQRES 8 A 162 MSE ASP THR GLN ALA ALA ALA ARG THR TYR ASN ILE LEU SEQRES 9 A 162 MSE ALA GLU GLY ARG ARG VAL VAL VAL ALA LEU LEU PRO SEQRES 10 A 162 ASP HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH SEQRES 11 A 162 HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH SEQRES 12 A 162 HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH SEQRES 13 A 162 HOH HOH HOH HOH HOH HOH REMARK PdbStat -- REMARK PdbStat -- PDB COORDINATES FOR 3CPK.PDB, MODEL/S 1 3CPK.PDB REMARK PdbStat -- SEQRES 1 A 162 PRO ALA THR ALA LEU ASN THR VAL THR ALA TYR GLY ASP SEQRES 2 A 162 GLY TYR ILE GLU VAL ASN GLN VAL ARG PHE SER HIS ALA SEQRES 3 A 162 ILE ALA PHE ALA PRO GLU GLY PRO VAL ALA SER TRP PRO SEQRES 4 A 162 VAL GLN ARG PRO ALA ASP ILE THR ALA SER LEU LEU GLN SEQRES 5 A 162 GLN ALA ALA GLY LEU ALA ALA PRO GLU VAL LEU LEU VAL SEQRES 6 A 162 GLY THR GLY ARG ARG GLN HIS LEU LEU GLY PRO GLU GLN SEQRES 7 A 162 VAL ARG PRO LEU LEU ALA MSE GLY VAL GLY VAL GLU ALA SEQRES 8 A 162 MSE ASP THR GLN ALA ALA ALA ARG THR TYR ASN ILE LEU SEQRES 9 A 162 MSE ALA GLU GLY ARG ARG VAL VAL VAL ALA LEU LEU PRO SEQRES 10 A 162 ASP HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH SEQRES 11 A 162 HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH SEQRES 12 A 162 HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH SEQRES 13 A 162 HOH HOH HOH HOH HOH HOH REMARK PdbStat -- REMARK PdbStat -- PDB COORDINATES FOR 3CPK.PDB, MODEL/S 1 3CPK.PDB REMARK PdbStat -- SEQRES 1 A 162 PRO ALA THR ALA LEU ASN THR VAL THR ALA TYR GLY ASP SEQRES 2 A 162 GLY TYR ILE GLU VAL ASN GLN VAL ARG PHE SER HIS ALA SEQRES 3 A 162 ILE ALA PHE ALA PRO GLU GLY PRO VAL ALA SER TRP PRO SEQRES 4 A 162 VAL GLN ARG PRO ALA ASP ILE THR ALA SER LEU LEU GLN SEQRES 5 A 162 GLN ALA ALA GLY LEU ALA ALA PRO GLU VAL LEU LEU VAL SEQRES 6 A 162 GLY THR GLY ARG ARG GLN HIS LEU LEU GLY PRO GLU GLN SEQRES 7 A 162 VAL ARG PRO LEU LEU ALA MSE GLY VAL GLY VAL GLU ALA SEQRES 8 A 162 MSE ASP THR GLN ALA ALA ALA ARG THR TYR ASN ILE LEU SEQRES 9 A 162 MSE ALA GLU GLY ARG ARG VAL VAL VAL ALA LEU LEU PRO SEQRES 10 A 162 ASP HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH SEQRES 11 A 162 HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH SEQRES 12 A 162 HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH SEQRES 13 A 162 HOH HOH HOH HOH HOH HOH REMARK PdbStat -- REMARK PdbStat -- PDB COORDINATES FOR 3CPK.PDB, MODEL/S 1 3CPK.PDB REMARK PdbStat -- SEQRES 1 A 162 PRO ALA THR ALA LEU ASN THR VAL THR ALA TYR GLY ASP SEQRES 2 A 162 GLY TYR ILE GLU VAL ASN GLN VAL ARG PHE SER HIS ALA SEQRES 3 A 162 ILE ALA PHE ALA PRO GLU GLY PRO VAL ALA SER TRP PRO SEQRES 4 A 162 VAL GLN ARG PRO ALA ASP ILE THR ALA SER LEU LEU GLN SEQRES 5 A 162 GLN ALA ALA GLY LEU ALA ALA PRO GLU VAL LEU LEU VAL SEQRES 6 A 162 GLY THR GLY ARG ARG GLN HIS LEU LEU GLY PRO GLU GLN SEQRES 7 A 162 VAL ARG PRO LEU LEU ALA MSE GLY VAL GLY VAL GLU ALA SEQRES 8 A 162 MSE ASP THR GLN ALA ALA ALA ARG THR TYR ASN ILE LEU SEQRES 9 A 162 MSE ALA GLU GLY ARG ARG VAL VAL VAL ALA LEU LEU PRO SEQRES 10 A 162 ASP HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH SEQRES 11 A 162 HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH SEQRES 12 A 162 HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH SEQRES 13 A 162 HOH HOH HOH HOH HOH HOH REMARK PdbStat -- REMARK PdbStat -- PDB COORDINATES FOR 3CPK.PDB, MODEL/S 1 3CPK.PDB REMARK PdbStat -- SEQRES 1 A 162 PRO ALA THR ALA LEU ASN THR VAL THR ALA TYR GLY ASP SEQRES 2 A 162 GLY TYR ILE GLU VAL ASN GLN VAL ARG PHE SER HIS ALA SEQRES 3 A 162 ILE ALA PHE ALA PRO GLU GLY PRO VAL ALA SER TRP PRO SEQRES 4 A 162 VAL GLN ARG PRO ALA ASP ILE THR ALA SER LEU LEU GLN SEQRES 5 A 162 GLN ALA ALA GLY LEU ALA ALA PRO GLU VAL LEU LEU VAL SEQRES 6 A 162 GLY THR GLY ARG ARG GLN HIS LEU LEU GLY PRO GLU GLN SEQRES 7 A 162 VAL ARG PRO LEU LEU ALA MSE GLY VAL GLY VAL GLU ALA SEQRES 8 A 162 MSE ASP THR GLN ALA ALA ALA ARG THR TYR ASN ILE LEU SEQRES 9 A 162 MSE ALA GLU GLY ARG ARG VAL VAL VAL ALA LEU LEU PRO SEQRES 10 A 162 ASP HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH SEQRES 11 A 162 HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH SEQRES 12 A 162 HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH SEQRES 13 A 162 HOH HOH HOH HOH HOH HOH REMARK PdbStat -- REMARK PdbStat -- PDB COORDINATES FOR 3CPK.PDB, MODEL/S 1 3CPK.PDB REMARK PdbStat -- SEQRES 1 A 162 PRO ALA THR ALA LEU ASN THR VAL THR ALA TYR GLY ASP SEQRES 2 A 162 GLY TYR ILE GLU VAL ASN GLN VAL ARG PHE SER HIS ALA SEQRES 3 A 162 ILE ALA PHE ALA PRO GLU GLY PRO VAL ALA SER TRP PRO SEQRES 4 A 162 VAL GLN ARG PRO ALA ASP ILE THR ALA SER LEU LEU GLN SEQRES 5 A 162 GLN ALA ALA GLY LEU ALA ALA PRO GLU VAL LEU LEU VAL SEQRES 6 A 162 GLY THR GLY ARG ARG GLN HIS LEU LEU GLY PRO GLU GLN SEQRES 7 A 162 VAL ARG PRO LEU LEU ALA MSE GLY VAL GLY VAL GLU ALA SEQRES 8 A 162 MSE ASP THR GLN ALA ALA ALA ARG THR TYR ASN ILE LEU SEQRES 9 A 162 MSE ALA GLU GLY ARG ARG VAL VAL VAL ALA LEU LEU PRO SEQRES 10 A 162 ASP HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH SEQRES 11 A 162 HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH SEQRES 12 A 162 HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH SEQRES 13 A 162 HOH HOH HOH HOH HOH HOH REMARK PdbStat -- REMARK PdbStat -- PDB COORDINATES FOR 3CPK.PDB, MODEL/S 1 3CPK.PDB REMARK PdbStat -- SEQRES 1 A 162 PRO ALA THR ALA LEU ASN THR VAL THR ALA TYR GLY ASP SEQRES 2 A 162 GLY TYR ILE GLU VAL ASN GLN VAL ARG PHE SER HIS ALA SEQRES 3 A 162 ILE ALA PHE ALA PRO GLU GLY PRO VAL ALA SER TRP PRO SEQRES 4 A 162 VAL GLN ARG PRO ALA ASP ILE THR ALA SER LEU LEU GLN SEQRES 5 A 162 GLN ALA ALA GLY LEU ALA ALA PRO GLU VAL LEU LEU VAL SEQRES 6 A 162 GLY THR GLY ARG ARG GLN HIS LEU LEU GLY PRO GLU GLN SEQRES 7 A 162 VAL ARG PRO LEU LEU ALA MSE GLY VAL GLY VAL GLU ALA SEQRES 8 A 162 MSE ASP THR GLN ALA ALA ALA ARG THR TYR ASN ILE LEU SEQRES 9 A 162 MSE ALA GLU GLY ARG ARG VAL VAL VAL ALA LEU LEU PRO SEQRES 10 A 162 ASP HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH SEQRES 11 A 162 HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH SEQRES 12 A 162 HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH SEQRES 13 A 162 HOH HOH HOH HOH HOH HOH REMARK PdbStat -- REMARK PdbStat -- PDB COORDINATES FOR 3CPK.PDB, MODEL/S 1 3CPK.PDB REMARK PdbStat -- SEQRES 1 A 162 PRO ALA THR ALA LEU ASN THR VAL THR ALA TYR GLY ASP SEQRES 2 A 162 GLY TYR ILE GLU VAL ASN GLN VAL ARG PHE SER HIS ALA SEQRES 3 A 162 ILE ALA PHE ALA PRO GLU GLY PRO VAL ALA SER TRP PRO SEQRES 4 A 162 VAL GLN ARG PRO ALA ASP ILE THR ALA SER LEU LEU GLN SEQRES 5 A 162 GLN ALA ALA GLY LEU ALA ALA PRO GLU VAL LEU LEU VAL SEQRES 6 A 162 GLY THR GLY ARG ARG GLN HIS LEU LEU GLY PRO GLU GLN SEQRES 7 A 162 VAL ARG PRO LEU LEU ALA MSE GLY VAL GLY VAL GLU ALA SEQRES 8 A 162 MSE ASP THR GLN ALA ALA ALA ARG THR TYR ASN ILE LEU SEQRES 9 A 162 MSE ALA GLU GLY ARG ARG VAL VAL VAL ALA LEU LEU PRO SEQRES 10 A 162 ASP HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH SEQRES 11 A 162 HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH SEQRES 12 A 162 HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH SEQRES 13 A 162 HOH HOH HOH HOH HOH HOH REMARK PdbStat -- REMARK PdbStat -- PDB COORDINATES FOR 3CPK.PDB, MODEL/S 1 3CPK.PDB REMARK PdbStat -- SEQRES 1 A 162 PRO ALA THR ALA LEU ASN THR VAL THR ALA TYR GLY ASP SEQRES 2 A 162 GLY TYR ILE GLU VAL ASN GLN VAL ARG PHE SER HIS ALA SEQRES 3 A 162 ILE ALA PHE ALA PRO GLU GLY PRO VAL ALA SER TRP PRO SEQRES 4 A 162 VAL GLN ARG PRO ALA ASP ILE THR ALA SER LEU LEU GLN SEQRES 5 A 162 GLN ALA ALA GLY LEU ALA ALA PRO GLU VAL LEU LEU VAL SEQRES 6 A 162 GLY THR GLY ARG ARG GLN HIS LEU LEU GLY PRO GLU GLN SEQRES 7 A 162 VAL ARG PRO LEU LEU ALA MSE GLY VAL GLY VAL GLU ALA SEQRES 8 A 162 MSE ASP THR GLN ALA ALA ALA ARG THR TYR ASN ILE LEU SEQRES 9 A 162 MSE ALA GLU GLY ARG ARG VAL VAL VAL ALA LEU LEU PRO SEQRES 10 A 162 ASP HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH SEQRES 11 A 162 HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH SEQRES 12 A 162 HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH SEQRES 13 A 162 HOH HOH HOH HOH HOH HOH REMARK PdbStat -- REMARK PdbStat -- PDB COORDINATES FOR 3CPK.PDB, MODEL/S 1 3CPK.PDB REMARK PdbStat -- SEQRES 1 A 162 PRO ALA THR ALA LEU ASN THR VAL THR ALA TYR GLY ASP SEQRES 2 A 162 GLY TYR ILE GLU VAL ASN GLN VAL ARG PHE SER HIS ALA SEQRES 3 A 162 ILE ALA PHE ALA PRO GLU GLY PRO VAL ALA SER TRP PRO SEQRES 4 A 162 VAL GLN ARG PRO ALA ASP ILE THR ALA SER LEU LEU GLN SEQRES 5 A 162 GLN ALA ALA GLY LEU ALA ALA PRO GLU VAL LEU LEU VAL SEQRES 6 A 162 GLY THR GLY ARG ARG GLN HIS LEU LEU GLY PRO GLU GLN SEQRES 7 A 162 VAL ARG PRO LEU LEU ALA MSE GLY VAL GLY VAL GLU ALA SEQRES 8 A 162 MSE ASP THR GLN ALA ALA ALA ARG THR TYR ASN ILE LEU SEQRES 9 A 162 MSE ALA GLU GLY ARG ARG VAL VAL VAL ALA LEU LEU PRO SEQRES 10 A 162 ASP HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH SEQRES 11 A 162 HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH SEQRES 12 A 162 HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH SEQRES 13 A 162 HOH HOH HOH HOH HOH HOH REMARK PdbStat -- REMARK PdbStat -- PDB COORDINATES FOR 3CPK.PDB, MODEL/S 1 3CPK.PDB REMARK PdbStat -- SEQRES 1 A 162 PRO ALA THR ALA LEU ASN THR VAL THR ALA TYR GLY ASP SEQRES 2 A 162 GLY TYR ILE GLU VAL ASN GLN VAL ARG PHE SER HIS ALA SEQRES 3 A 162 ILE ALA PHE ALA PRO GLU GLY PRO VAL ALA SER TRP PRO SEQRES 4 A 162 VAL GLN ARG PRO ALA ASP ILE THR ALA SER LEU LEU GLN SEQRES 5 A 162 GLN ALA ALA GLY LEU ALA ALA PRO GLU VAL LEU LEU VAL SEQRES 6 A 162 GLY THR GLY ARG ARG GLN HIS LEU LEU GLY PRO GLU GLN SEQRES 7 A 162 VAL ARG PRO LEU LEU ALA MSE GLY VAL GLY VAL GLU ALA SEQRES 8 A 162 MSE ASP THR GLN ALA ALA ALA ARG THR TYR ASN ILE LEU SEQRES 9 A 162 MSE ALA GLU GLY ARG ARG VAL VAL VAL ALA LEU LEU PRO SEQRES 10 A 162 ASP HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH SEQRES 11 A 162 HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH SEQRES 12 A 162 HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH SEQRES 13 A 162 HOH HOH HOH HOH HOH HOH REMARK PdbStat -- REMARK PdbStat -- PDB COORDINATES FOR 3CPK.PDB, MODEL/S 1 3CPK.PDB REMARK PdbStat -- SEQRES 1 A 162 PRO ALA THR ALA LEU ASN THR VAL THR ALA TYR GLY ASP SEQRES 2 A 162 GLY TYR ILE GLU VAL ASN GLN VAL ARG PHE SER HIS ALA SEQRES 3 A 162 ILE ALA PHE ALA PRO GLU GLY PRO VAL ALA SER TRP PRO SEQRES 4 A 162 VAL GLN ARG PRO ALA ASP ILE THR ALA SER LEU LEU GLN SEQRES 5 A 162 GLN ALA ALA GLY LEU ALA ALA PRO GLU VAL LEU LEU VAL SEQRES 6 A 162 GLY THR GLY ARG ARG GLN HIS LEU LEU GLY PRO GLU GLN SEQRES 7 A 162 VAL ARG PRO LEU LEU ALA MSE GLY VAL GLY VAL GLU ALA SEQRES 8 A 162 MSE ASP THR GLN ALA ALA ALA ARG THR TYR ASN ILE LEU SEQRES 9 A 162 MSE ALA GLU GLY ARG ARG VAL VAL VAL ALA LEU LEU PRO SEQRES 10 A 162 ASP HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH SEQRES 11 A 162 HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH SEQRES 12 A 162 HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH SEQRES 13 A 162 HOH HOH HOH HOH HOH HOH REMARK PdbStat -- REMARK PdbStat -- PDB COORDINATES FOR 3CPK.PDB, MODEL/S 1 3CPK.PDB REMARK PdbStat -- SEQRES 1 A 162 PRO ALA THR ALA LEU ASN THR VAL THR ALA TYR GLY ASP SEQRES 2 A 162 GLY TYR ILE GLU VAL ASN GLN VAL ARG PHE SER HIS ALA SEQRES 3 A 162 ILE ALA PHE ALA PRO GLU GLY PRO VAL ALA SER TRP PRO SEQRES 4 A 162 VAL GLN ARG PRO ALA ASP ILE THR ALA SER LEU LEU GLN SEQRES 5 A 162 GLN ALA ALA GLY LEU ALA ALA PRO GLU VAL LEU LEU VAL SEQRES 6 A 162 GLY THR GLY ARG ARG GLN HIS LEU LEU GLY PRO GLU GLN SEQRES 7 A 162 VAL ARG PRO LEU LEU ALA MSE GLY VAL GLY VAL GLU ALA SEQRES 8 A 162 MSE ASP THR GLN ALA ALA ALA ARG THR TYR ASN ILE LEU SEQRES 9 A 162 MSE ALA GLU GLY ARG ARG VAL VAL VAL ALA LEU LEU PRO SEQRES 10 A 162 ASP HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH SEQRES 11 A 162 HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH SEQRES 12 A 162 HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH SEQRES 13 A 162 HOH HOH HOH HOH HOH HOH REMARK PdbStat -- REMARK PdbStat -- PDB COORDINATES FOR 3CPK.PDB, MODEL/S 1 3CPK.PDB REMARK PdbStat -- SEQRES 1 A 162 PRO ALA THR ALA LEU ASN THR VAL THR ALA TYR GLY ASP SEQRES 2 A 162 GLY TYR ILE GLU VAL ASN GLN VAL ARG PHE SER HIS ALA SEQRES 3 A 162 ILE ALA PHE ALA PRO GLU GLY PRO VAL ALA SER TRP PRO SEQRES 4 A 162 VAL GLN ARG PRO ALA ASP ILE THR ALA SER LEU LEU GLN SEQRES 5 A 162 GLN ALA ALA GLY LEU ALA ALA PRO GLU VAL LEU LEU VAL SEQRES 6 A 162 GLY THR GLY ARG ARG GLN HIS LEU LEU GLY PRO GLU GLN SEQRES 7 A 162 VAL ARG PRO LEU LEU ALA MSE GLY VAL GLY VAL GLU ALA SEQRES 8 A 162 MSE ASP THR GLN ALA ALA ALA ARG THR TYR ASN ILE LEU SEQRES 9 A 162 MSE ALA GLU GLY ARG ARG VAL VAL VAL ALA LEU LEU PRO SEQRES 10 A 162 ASP HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH SEQRES 11 A 162 HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH SEQRES 12 A 162 HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH SEQRES 13 A 162 HOH HOH HOH HOH HOH HOH REMARK PdbStat -- REMARK PdbStat -- PDB COORDINATES FOR 3CPK.PDB, MODEL/S 1 3CPK.PDB REMARK PdbStat -- SEQRES 1 A 162 PRO ALA THR ALA LEU ASN THR VAL THR ALA TYR GLY ASP SEQRES 2 A 162 GLY TYR ILE GLU VAL ASN GLN VAL ARG PHE SER HIS ALA SEQRES 3 A 162 ILE ALA PHE ALA PRO GLU GLY PRO VAL ALA SER TRP PRO SEQRES 4 A 162 VAL GLN ARG PRO ALA ASP ILE THR ALA SER LEU LEU GLN SEQRES 5 A 162 GLN ALA ALA GLY LEU ALA ALA PRO GLU VAL LEU LEU VAL SEQRES 6 A 162 GLY THR GLY ARG ARG GLN HIS LEU LEU GLY PRO GLU GLN SEQRES 7 A 162 VAL ARG PRO LEU LEU ALA MSE GLY VAL GLY VAL GLU ALA SEQRES 8 A 162 MSE ASP THR GLN ALA ALA ALA ARG THR TYR ASN ILE LEU SEQRES 9 A 162 MSE ALA GLU GLY ARG ARG VAL VAL VAL ALA LEU LEU PRO SEQRES 10 A 162 ASP HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH SEQRES 11 A 162 HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH SEQRES 12 A 162 HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH SEQRES 13 A 162 HOH HOH HOH HOH HOH HOH REMARK PdbStat -- REMARK PdbStat -- PDB COORDINATES FOR 3CPK.PDB, MODEL/S 1 3CPK.PDB REMARK PdbStat -- SEQRES 1 A 162 PRO ALA THR ALA LEU ASN THR VAL THR ALA TYR GLY ASP SEQRES 2 A 162 GLY TYR ILE GLU VAL ASN GLN VAL ARG PHE SER HIS ALA SEQRES 3 A 162 ILE ALA PHE ALA PRO GLU GLY PRO VAL ALA SER TRP PRO SEQRES 4 A 162 VAL GLN ARG PRO ALA ASP ILE THR ALA SER LEU LEU GLN SEQRES 5 A 162 GLN ALA ALA GLY LEU ALA ALA PRO GLU VAL LEU LEU VAL SEQRES 6 A 162 GLY THR GLY ARG ARG GLN HIS LEU LEU GLY PRO GLU GLN SEQRES 7 A 162 VAL ARG PRO LEU LEU ALA MSE GLY VAL GLY VAL GLU ALA SEQRES 8 A 162 MSE ASP THR GLN ALA ALA ALA ARG THR TYR ASN ILE LEU SEQRES 9 A 162 MSE ALA GLU GLY ARG ARG VAL VAL VAL ALA LEU LEU PRO SEQRES 10 A 162 ASP HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH SEQRES 11 A 162 HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH SEQRES 12 A 162 HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH SEQRES 13 A 162 HOH HOH HOH HOH HOH HOH REMARK PdbStat -- REMARK PdbStat -- PDB COORDINATES FOR 3CPK.PDB, MODEL/S 1 3CPK.PDB REMARK PdbStat -- SEQRES 1 A 162 PRO ALA THR ALA LEU ASN THR VAL THR ALA TYR GLY ASP SEQRES 2 A 162 GLY TYR ILE GLU VAL ASN GLN VAL ARG PHE SER HIS ALA SEQRES 3 A 162 ILE ALA PHE ALA PRO GLU GLY PRO VAL ALA SER TRP PRO SEQRES 4 A 162 VAL GLN ARG PRO ALA ASP ILE THR ALA SER LEU LEU GLN SEQRES 5 A 162 GLN ALA ALA GLY LEU ALA ALA PRO GLU VAL LEU LEU VAL SEQRES 6 A 162 GLY THR GLY ARG ARG GLN HIS LEU LEU GLY PRO GLU GLN SEQRES 7 A 162 VAL ARG PRO LEU LEU ALA MSE GLY VAL GLY VAL GLU ALA SEQRES 8 A 162 MSE ASP THR GLN ALA ALA ALA ARG THR TYR ASN ILE LEU SEQRES 9 A 162 MSE ALA GLU GLY ARG ARG VAL VAL VAL ALA LEU LEU PRO SEQRES 10 A 162 ASP HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH SEQRES 11 A 162 HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH SEQRES 12 A 162 HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH SEQRES 13 A 162 HOH HOH HOH HOH HOH HOH REMARK PdbStat -- REMARK PdbStat -- PDB COORDINATES FOR 3CPK.PDB, MODEL/S 1 3CPK.PDB REMARK PdbStat -- SEQRES 1 A 162 PRO ALA THR ALA LEU ASN THR VAL THR ALA TYR GLY ASP SEQRES 2 A 162 GLY TYR ILE GLU VAL ASN GLN VAL ARG PHE SER HIS ALA SEQRES 3 A 162 ILE ALA PHE ALA PRO GLU GLY PRO VAL ALA SER TRP PRO SEQRES 4 A 162 VAL GLN ARG PRO ALA ASP ILE THR ALA SER LEU LEU GLN SEQRES 5 A 162 GLN ALA ALA GLY LEU ALA ALA PRO GLU VAL LEU LEU VAL SEQRES 6 A 162 GLY THR GLY ARG ARG GLN HIS LEU LEU GLY PRO GLU GLN SEQRES 7 A 162 VAL ARG PRO LEU LEU ALA MSE GLY VAL GLY VAL GLU ALA SEQRES 8 A 162 MSE ASP THR GLN ALA ALA ALA ARG THR TYR ASN ILE LEU SEQRES 9 A 162 MSE ALA GLU GLY ARG ARG VAL VAL VAL ALA LEU LEU PRO SEQRES 10 A 162 ASP HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH SEQRES 11 A 162 HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH SEQRES 12 A 162 HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH SEQRES 13 A 162 HOH HOH HOH HOH HOH HOH REMARK PdbStat -- REMARK PdbStat -- PDB COORDINATES FOR 3CPK.PDB, MODEL/S 1 3CPK.PDB REMARK PdbStat -- SEQRES 1 A 162 PRO ALA THR ALA LEU ASN THR VAL THR ALA TYR GLY ASP SEQRES 2 A 162 GLY TYR ILE GLU VAL ASN GLN VAL ARG PHE SER HIS ALA SEQRES 3 A 162 ILE ALA PHE ALA PRO GLU GLY PRO VAL ALA SER TRP PRO SEQRES 4 A 162 VAL GLN ARG PRO ALA ASP ILE THR ALA SER LEU LEU GLN SEQRES 5 A 162 GLN ALA ALA GLY LEU ALA ALA PRO GLU VAL LEU LEU VAL SEQRES 6 A 162 GLY THR GLY ARG ARG GLN HIS LEU LEU GLY PRO GLU GLN SEQRES 7 A 162 VAL ARG PRO LEU LEU ALA MSE GLY VAL GLY VAL GLU ALA SEQRES 8 A 162 MSE ASP THR GLN ALA ALA ALA ARG THR TYR ASN ILE LEU SEQRES 9 A 162 MSE ALA GLU GLY ARG ARG VAL VAL VAL ALA LEU LEU PRO SEQRES 10 A 162 ASP HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH SEQRES 11 A 162 HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH SEQRES 12 A 162 HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH SEQRES 13 A 162 HOH HOH HOH HOH HOH HOH REMARK PdbStat -- REMARK PdbStat -- PDB COORDINATES FOR 3CPK.PDB, MODEL/S 1 3CPK.PDB REMARK PdbStat -- SEQRES 1 A 162 PRO ALA THR ALA LEU ASN THR VAL THR ALA TYR GLY ASP SEQRES 2 A 162 GLY TYR ILE GLU VAL ASN GLN VAL ARG PHE SER HIS ALA SEQRES 3 A 162 ILE ALA PHE ALA PRO GLU GLY PRO VAL ALA SER TRP PRO SEQRES 4 A 162 VAL GLN ARG PRO ALA ASP ILE THR ALA SER LEU LEU GLN SEQRES 5 A 162 GLN ALA ALA GLY LEU ALA ALA PRO GLU VAL LEU LEU VAL SEQRES 6 A 162 GLY THR GLY ARG ARG GLN HIS LEU LEU GLY PRO GLU GLN SEQRES 7 A 162 VAL ARG PRO LEU LEU ALA MSE GLY VAL GLY VAL GLU ALA SEQRES 8 A 162 MSE ASP THR GLN ALA ALA ALA ARG THR TYR ASN ILE LEU SEQRES 9 A 162 MSE ALA GLU GLY ARG ARG VAL VAL VAL ALA LEU LEU PRO SEQRES 10 A 162 ASP HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH SEQRES 11 A 162 HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH SEQRES 12 A 162 HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH SEQRES 13 A 162 HOH HOH HOH HOH HOH HOH REMARK PdbStat -- REMARK PdbStat -- PDB COORDINATES FOR 3CPK.PDB, MODEL/S 1 3CPK.PDB REMARK PdbStat -- SEQRES 1 A 162 PRO ALA THR ALA LEU ASN THR VAL THR ALA TYR GLY ASP SEQRES 2 A 162 GLY TYR ILE GLU VAL ASN GLN VAL ARG PHE SER HIS ALA SEQRES 3 A 162 ILE ALA PHE ALA PRO GLU GLY PRO VAL ALA SER TRP PRO SEQRES 4 A 162 VAL GLN ARG PRO ALA ASP ILE THR ALA SER LEU LEU GLN SEQRES 5 A 162 GLN ALA ALA GLY LEU ALA ALA PRO GLU VAL LEU LEU VAL SEQRES 6 A 162 GLY THR GLY ARG ARG GLN HIS LEU LEU GLY PRO GLU GLN SEQRES 7 A 162 VAL ARG PRO LEU LEU ALA MSE GLY VAL GLY VAL GLU ALA SEQRES 8 A 162 MSE ASP THR GLN ALA ALA ALA ARG THR TYR ASN ILE LEU SEQRES 9 A 162 MSE ALA GLU GLY ARG ARG VAL VAL VAL ALA LEU LEU PRO SEQRES 10 A 162 ASP HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH SEQRES 11 A 162 HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH SEQRES 12 A 162 HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH SEQRES 13 A 162 HOH HOH HOH HOH HOH HOH MODEL 1 REMARK CONFORMATION 1 ENERGY 0.0000 REMARK FAMILY or FILE: 3CPK.pdb ATOM 1 N PRO A 7 5.634 7.939 23.242 1.00 55.81 N ATOM 2 CA PRO A 7 4.831 7.318 24.314 1.00 57.52 C ATOM 3 C PRO A 7 3.839 6.324 23.690 1.00 58.74 C ATOM 4 O PRO A 7 4.251 5.292 23.147 1.00 59.00 O ATOM 5 CB PRO A 7 4.119 8.451 25.034 1.00 57.88 C ATOM 6 CG PRO A 7 3.946 9.451 23.908 1.00 59.17 C ATOM 7 CD PRO A 7 5.202 9.330 23.023 1.00 57.17 C ATOM 8 N ALA A 8 2.545 6.634 23.758 1.00 55.90 N ATOM 9 CA ALA A 8 1.519 5.761 23.186 1.00 51.96 C ATOM 10 C ALA A 8 0.958 6.328 21.881 1.00 50.20 C ATOM 11 O ALA A 8 -0.208 6.725 21.816 1.00 49.87 O ATOM 12 CB ALA A 8 0.401 5.562 24.180 1.00 52.97 C ATOM 13 N THR A 9 1.808 6.353 20.854 1.00 46.57 N ATOM 14 CA THR A 9 1.485 6.853 19.517 1.00 41.41 C ATOM 15 C THR A 9 0.230 6.217 18.916 1.00 37.58 C ATOM 16 O THR A 9 0.097 4.998 18.919 1.00 35.33 O ATOM 17 CB THR A 9 2.648 6.556 18.533 1.00 42.61 C ATOM 18 OG1 THR A 9 3.898 6.905 19.137 1.00 47.27 O ATOM 19 CG2 THR A 9 2.477 7.344 17.248 1.00 41.19 C ATOM 20 N ALA A 10 -0.680 7.024 18.378 1.00 32.41 N ATOM 21 CA ALA A 10 -1.879 6.454 17.762 1.00 28.95 C ATOM 22 C ALA A 10 -1.487 5.782 16.441 1.00 29.82 C ATOM 23 O ALA A 10 -0.606 6.258 15.723 1.00 30.47 O ATOM 24 CB ALA A 10 -2.911 7.516 17.521 1.00 26.71 C ATOM 25 N LEU A 11 -2.142 4.667 16.127 1.00 28.57 N ATOM 26 CA LEU A 11 -1.851 3.922 14.912 1.00 28.85 C ATOM 27 C LEU A 11 -2.820 4.177 13.761 1.00 29.89 C ATOM 28 O LEU A 11 -4.009 4.428 13.970 1.00 29.93 O ATOM 29 CB LEU A 11 -1.833 2.416 15.213 1.00 29.70 C ATOM 30 CG LEU A 11 -0.697 1.724 15.988 1.00 28.46 C ATOM 31 CD1 LEU A 11 0.477 2.668 16.256 1.00 24.84 C ATOM 32 CD2 LEU A 11 -1.264 1.166 17.274 1.00 31.43 C ATOM 33 N ASN A 12 -2.298 4.097 12.540 1.00 28.93 N ATOM 34 CA ASN A 12 -3.107 4.283 11.352 1.00 29.72 C ATOM 35 C ASN A 12 -4.083 3.118 11.204 1.00 28.39 C ATOM 36 O ASN A 12 -3.709 1.935 11.181 1.00 25.81 O ATOM 37 CB ASN A 12 -2.228 4.411 10.102 1.00 30.79 C ATOM 38 CG ASN A 12 -1.506 5.750 10.035 1.00 29.40 C ATOM 39 OD1 ASN A 12 -2.098 6.802 10.298 1.00 24.62 O ATOM 40 ND2 ASN A 12 -0.226 5.717 9.669 1.00 23.32 N ATOM 41 N THR A 13 -5.347 3.484 11.081 1.00 28.69 N ATOM 42 CA THR A 13 -6.418 2.532 10.994 1.00 29.93 C ATOM 43 C THR A 13 -7.377 2.795 9.843 1.00 29.55 C ATOM 44 O THR A 13 -7.841 3.928 9.653 1.00 29.48 O ATOM 45 CB THR A 13 -7.182 2.558 12.324 1.00 30.05 C ATOM 46 OG1 THR A 13 -6.263 2.260 13.385 1.00 35.05 O ATOM 47 CG2 THR A 13 -8.321 1.554 12.329 1.00 32.46 C ATOM 48 N VAL A 14 -7.655 1.744 9.073 1.00 28.86 N ATOM 49 CA VAL A 14 -8.591 1.832 7.969 1.00 29.57 C ATOM 50 C VAL A 14 -9.964 1.927 8.630 1.00 32.98 C ATOM 51 O VAL A 14 -10.475 0.963 9.203 1.00 33.21 O ATOM 52 CB VAL A 14 -8.526 0.586 7.073 1.00 31.85 C ATOM 53 CG1 VAL A 14 -9.771 0.510 6.205 1.00 30.44 C ATOM 54 CG2 VAL A 14 -7.280 0.641 6.197 1.00 28.17 C ATOM 55 N THR A 15 -10.548 3.113 8.549 1.00 35.77 N ATOM 56 CA THR A 15 -11.832 3.406 9.172 1.00 38.30 C ATOM 57 C THR A 15 -13.082 2.874 8.462 1.00 38.83 C ATOM 58 O THR A 15 -14.003 2.377 9.098 1.00 37.38 O ATOM 59 CB THR A 15 -11.974 4.930 9.360 1.00 37.10 C ATOM 60 OG1 THR A 15 -11.031 5.374 10.339 1.00 41.60 O ATOM 61 CG2 THR A 15 -13.367 5.279 9.828 1.00 45.77 C ATOM 62 N ALA A 16 -13.113 3.011 7.147 1.00 41.20 N ATOM 63 CA ALA A 16 -14.236 2.549 6.356 1.00 41.74 C ATOM 64 C ALA A 16 -13.700 2.278 4.964 1.00 44.27 C ATOM 65 O ALA A 16 -12.594 2.692 4.623 1.00 42.16 O ATOM 66 CB ALA A 16 -15.332 3.610 6.311 1.00 41.09 C ATOM 67 N TYR A 17 -14.483 1.568 4.170 1.00 49.13 N ATOM 68 CA TYR A 17 -14.098 1.225 2.809 1.00 51.91 C ATOM 69 C TYR A 17 -15.309 1.583 1.984 1.00 49.67 C ATOM 70 O TYR A 17 -16.441 1.417 2.433 1.00 48.41 O ATOM 71 CB TYR A 17 -13.834 -0.278 2.683 1.00 56.96 C ATOM 72 CG TYR A 17 -13.549 -0.970 4.000 1.00 67.48 C ATOM 73 CD1 TYR A 17 -14.481 -0.942 5.041 1.00 76.17 C ATOM 74 CD2 TYR A 17 -12.340 -1.625 4.220 1.00 73.19 C ATOM 75 CE1 TYR A 17 -14.214 -1.538 6.266 1.00 74.68 C ATOM 76 CE2 TYR A 17 -12.063 -2.230 5.448 1.00 74.27 C ATOM 77 CZ TYR A 17 -13.004 -2.177 6.464 1.00 69.67 C ATOM 78 OH TYR A 17 -12.735 -2.733 7.690 1.00 70.35 O ATOM 79 N GLY A 18 -15.089 2.080 0.783 1.00 49.25 N ATOM 80 CA GLY A 18 -16.227 2.421 -0.033 1.00 50.55 C ATOM 81 C GLY A 18 -15.963 2.187 -1.492 1.00 49.31 C ATOM 82 O GLY A 18 -14.839 1.909 -1.897 1.00 50.44 O ATOM 83 N ASP A 19 -17.019 2.281 -2.283 1.00 48.68 N ATOM 84 CA ASP A 19 -16.892 2.110 -3.713 1.00 48.30 C ATOM 85 C ASP A 19 -16.130 3.341 -4.185 1.00 44.97 C ATOM 86 O ASP A 19 -16.681 4.442 -4.243 1.00 42.13 O ATOM 87 CB ASP A 19 -18.274 2.057 -4.364 1.00 50.41 C ATOM 88 CG ASP A 19 -18.206 1.785 -5.852 1.00 53.98 C ATOM 89 OD1 ASP A 19 -17.081 1.739 -6.403 1.00 52.48 O ATOM 90 OD2 ASP A 19 -19.280 1.620 -6.472 1.00 57.98 O ATOM 91 N GLY A 20 -14.852 3.154 -4.489 1.00 46.39 N ATOM 92 CA GLY A 20 -14.041 4.263 -4.951 1.00 47.30 C ATOM 93 C GLY A 20 -13.220 4.949 -3.877 1.00 46.11 C ATOM 94 O GLY A 20 -12.579 5.964 -4.146 1.00 45.52 O ATOM 95 N TYR A 21 -13.216 4.409 -2.662 1.00 46.09 N ATOM 96 CA TYR A 21 -12.450 5.051 -1.599 1.00 43.63 C ATOM 97 C TYR A 21 -12.155 4.183 -0.397 1.00 41.45 C ATOM 98 O TYR A 21 -12.885 3.241 -0.087 1.00 40.59 O ATOM 99 CB TYR A 21 -13.189 6.298 -1.097 1.00 42.60 C ATOM 100 CG TYR A 21 -14.386 5.977 -0.219 1.00 39.85 C ATOM 101 CD1 TYR A 21 -14.231 5.694 1.142 1.00 33.58 C ATOM 102 CD2 TYR A 21 -15.670 5.929 -0.757 1.00 37.42 C ATOM 103 CE1 TYR A 21 -15.325 5.370 1.943 1.00 33.13 C ATOM 104 CE2 TYR A 21 -16.770 5.608 0.034 1.00 39.37 C ATOM 105 CZ TYR A 21 -16.592 5.329 1.380 1.00 39.14 C ATOM 106 OH TYR A 21 -17.690 5.003 2.151 1.00 43.50 O ATOM 107 N ILE A 22 -11.070 4.531 0.279 1.00 40.95 N ATOM 108 CA ILE A 22 -10.682 3.876 1.509 1.00 38.36 C ATOM 109 C ILE A 22 -10.677 5.035 2.491 1.00 38.20 C ATOM 110 O ILE A 22 -10.234 6.134 2.162 1.00 36.94 O ATOM 111 CB ILE A 22 -9.270 3.266 1.431 1.00 38.45 C ATOM 112 CG1 ILE A 22 -9.253 2.146 0.391 1.00 39.74 C ATOM 113 CG2 ILE A 22 -8.857 2.719 2.791 1.00 39.60 C ATOM 114 CD1 ILE A 22 -10.280 1.042 0.655 1.00 44.68 C ATOM 115 N GLU A 23 -11.214 4.811 3.678 1.00 37.26 N ATOM 116 CA GLU A 23 -11.222 5.849 4.688 1.00 35.18 C ATOM 117 C GLU A 23 -10.184 5.438 5.717 1.00 35.04 C ATOM 118 O GLU A 23 -10.256 4.351 6.300 1.00 36.37 O ATOM 119 CB GLU A 23 -12.601 5.954 5.337 1.00 33.83 C ATOM 120 CG GLU A 23 -12.720 7.092 6.334 1.00 44.33 C ATOM 121 CD GLU A 23 -14.119 7.231 6.907 1.00 51.11 C ATOM 122 OE1 GLU A 23 -14.321 6.875 8.085 1.00 51.31 O ATOM 123 OE2 GLU A 23 -15.022 7.694 6.173 1.00 46.75 O ATOM 124 N VAL A 24 -9.195 6.292 5.923 1.00 32.88 N ATOM 125 CA VAL A 24 -8.169 5.996 6.897 1.00 30.75 C ATOM 126 C VAL A 24 -8.208 7.077 7.966 1.00 32.52 C ATOM 127 O VAL A 24 -8.204 8.268 7.654 1.00 32.14 O ATOM 128 CB VAL A 24 -6.783 5.952 6.232 1.00 29.32 C ATOM 129 CG1 VAL A 24 -5.730 5.457 7.225 1.00 32.50 C ATOM 130 CG2 VAL A 24 -6.832 5.052 5.021 1.00 29.68 C ATOM 131 N ASN A 25 -8.270 6.655 9.227 1.00 32.23 N ATOM 132 CA ASN A 25 -8.308 7.587 10.346 1.00 32.38 C ATOM 133 C ASN A 25 -9.447 8.588 10.148 1.00 31.57 C ATOM 134 O ASN A 25 -9.337 9.765 10.515 1.00 30.13 O ATOM 135 CB ASN A 25 -6.955 8.311 10.464 1.00 29.45 C ATOM 136 CG ASN A 25 -5.772 7.339 10.625 1.00 30.34 C ATOM 137 OD1 ASN A 25 -4.632 7.675 10.314 1.00 34.78 O ATOM 138 ND2 ASN A 25 -6.048 6.142 11.117 1.00 24.59 N ATOM 139 N GLN A 26 -10.539 8.104 9.556 1.00 31.14 N ATOM 140 CA GLN A 26 -11.729 8.914 9.296 1.00 33.78 C ATOM 141 C GLN A 26 -11.578 9.974 8.203 1.00 32.31 C ATOM 142 O GLN A 26 -12.294 10.975 8.180 1.00 33.41 O ATOM 143 CB GLN A 26 -12.214 9.549 10.603 1.00 32.39 C ATOM 144 CG GLN A 26 -12.805 8.518 11.558 1.00 34.66 C ATOM 145 CD GLN A 26 -13.309 9.111 12.860 1.00 41.14 C ATOM 146 OE1 GLN A 26 -13.741 10.261 12.910 1.00 45.13 O ATOM 147 NE2 GLN A 26 -13.278 8.314 13.918 1.00 33.35 N ATOM 148 N VAL A 27 -10.634 9.743 7.301 1.00 33.21 N ATOM 149 CA VAL A 27 -10.397 10.643 6.186 1.00 31.06 C ATOM 150 C VAL A 27 -10.401 9.803 4.904 1.00 34.53 C ATOM 151 O VAL A 27 -9.717 8.783 4.826 1.00 36.89 O ATOM 152 CB VAL A 27 -9.050 11.365 6.339 1.00 29.52 C ATOM 153 CG1 VAL A 27 -8.836 12.332 5.181 1.00 26.70 C ATOM 154 CG2 VAL A 27 -9.021 12.100 7.663 1.00 29.47 C ATOM 155 N ARG A 28 -11.182 10.226 3.912 1.00 33.90 N ATOM 156 CA ARG A 28 -11.279 9.499 2.645 1.00 37.03 C ATOM 157 C ARG A 28 -10.159 9.748 1.644 1.00 35.78 C ATOM 158 O ARG A 28 -9.723 10.878 1.437 1.00 32.78 O ATOM 159 CB ARG A 28 -12.591 9.818 1.925 1.00 35.30 C ATOM 160 CG ARG A 28 -13.825 9.171 2.484 1.00 40.81 C ATOM 161 CD ARG A 28 -14.962 9.308 1.484 1.00 39.53 C ATOM 162 NE ARG A 28 -16.237 8.936 2.085 1.00 46.14 N ATOM 163 CZ ARG A 28 -17.384 8.857 1.424 1.00 47.19 C ATOM 164 NH1 ARG A 28 -17.428 9.119 0.124 1.00 48.91 N ATOM 165 NH2 ARG A 28 -18.491 8.527 2.069 1.00 48.20 N ATOM 166 N PHE A 29 -9.723 8.670 1.007 1.00 36.66 N ATOM 167 CA PHE A 29 -8.696 8.748 -0.012 1.00 38.26 C ATOM 168 C PHE A 29 -9.224 8.098 -1.282 1.00 41.17 C ATOM 169 O PHE A 29 -9.780 6.996 -1.246 1.00 44.99 O ATOM 170 CB PHE A 29 -7.424 8.047 0.449 1.00 37.74 C ATOM 171 CG PHE A 29 -6.761 8.721 1.603 1.00 38.46 C ATOM 172 CD1 PHE A 29 -7.219 8.515 2.901 1.00 40.98 C ATOM 173 CD2 PHE A 29 -5.691 9.588 1.395 1.00 39.82 C ATOM 174 CE1 PHE A 29 -6.633 9.170 3.979 1.00 43.58 C ATOM 175 CE2 PHE A 29 -5.091 10.254 2.466 1.00 37.27 C ATOM 176 CZ PHE A 29 -5.561 10.040 3.763 1.00 42.63 C ATOM 177 N SER A 30 -9.076 8.797 -2.402 1.00 42.65 N ATOM 178 CA SER A 30 -9.533 8.268 -3.676 1.00 41.49 C ATOM 179 C SER A 30 -8.374 8.064 -4.643 1.00 39.98 C ATOM 180 O SER A 30 -8.570 7.717 -5.804 1.00 44.15 O ATOM 181 CB SER A 30 -10.614 9.167 -4.279 1.00 39.54 C ATOM 182 OG SER A 30 -10.299 10.532 -4.124 1.00 47.67 O ATOM 183 N HIS A 31 -7.163 8.291 -4.154 1.00 36.97 N ATOM 184 CA HIS A 31 -5.971 8.054 -4.949 1.00 37.16 C ATOM 185 C HIS A 31 -5.214 6.994 -4.154 1.00 37.00 C ATOM 186 O HIS A 31 -5.476 6.807 -2.964 1.00 37.20 O ATOM 187 CB HIS A 31 -5.134 9.329 -5.120 1.00 39.74 C ATOM 188 CG HIS A 31 -4.540 9.859 -3.852 1.00 46.87 C ATOM 189 ND1 HIS A 31 -5.249 10.638 -2.959 1.00 50.31 N ATOM 190 CD2 HIS A 31 -3.289 9.755 -3.345 1.00 49.44 C ATOM 191 CE1 HIS A 31 -4.459 10.992 -1.963 1.00 54.56 C ATOM 192 NE2 HIS A 31 -3.262 10.469 -2.173 1.00 55.45 N ATOM 193 N ALA A 32 -4.295 6.286 -4.799 1.00 35.62 N ATOM 194 CA ALA A 32 -3.555 5.233 -4.117 1.00 34.86 C ATOM 195 C ALA A 32 -2.704 5.774 -2.980 1.00 35.14 C ATOM 196 O ALA A 32 -2.137 6.860 -3.073 1.00 37.02 O ATOM 197 CB ALA A 32 -2.692 4.468 -5.107 1.00 35.91 C ATOM 198 N ILE A 33 -2.631 5.002 -1.904 1.00 30.80 N ATOM 199 CA ILE A 33 -1.864 5.373 -0.727 1.00 28.41 C ATOM 200 C ILE A 33 -1.078 4.180 -0.185 1.00 29.83 C ATOM 201 O ILE A 33 -1.273 3.037 -0.597 1.00 30.98 O ATOM 202 CB ILE A 33 -2.791 5.909 0.398 1.00 24.02 C ATOM 203 CG1 ILE A 33 -3.860 4.863 0.729 1.00 23.44 C ATOM 204 CG2 ILE A 33 -3.442 7.216 -0.045 1.00 20.94 C ATOM 205 CD1 ILE A 33 -4.816 5.272 1.829 1.00 19.51 C ATOM 206 N ALA A 34 -0.174 4.467 0.738 1.00 29.76 N ATOM 207 CA ALA A 34 0.639 3.438 1.366 1.00 31.10 C ATOM 208 C ALA A 34 0.908 3.936 2.775 1.00 30.57 C ATOM 209 O ALA A 34 0.959 5.143 3.013 1.00 32.01 O ATOM 210 CB ALA A 34 1.944 3.241 0.601 1.00 30.43 C ATOM 211 N PHE A 35 1.051 3.017 3.720 1.00 31.04 N ATOM 212 CA PHE A 35 1.302 3.424 5.088 1.00 30.35 C ATOM 213 C PHE A 35 1.514 2.242 5.996 1.00 28.96 C ATOM 214 O PHE A 35 1.145 1.113 5.681 1.00 28.88 O ATOM 215 CB PHE A 35 0.142 4.297 5.619 1.00 29.63 C ATOM 216 CG PHE A 35 -1.197 3.602 5.636 1.00 29.89 C ATOM 217 CD1 PHE A 35 -1.623 2.911 6.768 1.00 27.22 C ATOM 218 CD2 PHE A 35 -2.023 3.624 4.509 1.00 30.95 C ATOM 219 CE1 PHE A 35 -2.846 2.255 6.791 1.00 24.48 C ATOM 220 CE2 PHE A 35 -3.255 2.970 4.514 1.00 32.19 C ATOM 221 CZ PHE A 35 -3.670 2.280 5.659 1.00 24.44 C ATOM 222 N ALA A 36 2.133 2.538 7.129 1.00 31.05 N ATOM 223 CA ALA A 36 2.431 1.568 8.162 1.00 31.74 C ATOM 224 C ALA A 36 1.577 1.988 9.348 1.00 31.46 C ATOM 225 O ALA A 36 0.863 2.988 9.277 1.00 32.32 O ATOM 226 CB ALA A 36 3.903 1.633 8.518 1.00 32.51 C ATOM 227 N PRO A 37 1.611 1.221 10.445 1.00 31.52 N ATOM 228 CA PRO A 37 0.807 1.589 11.615 1.00 31.30 C ATOM 229 C PRO A 37 1.226 2.963 12.137 1.00 32.76 C ATOM 230 O PRO A 37 0.393 3.798 12.511 1.00 35.55 O ATOM 231 CB PRO A 37 1.118 0.468 12.601 1.00 30.57 C ATOM 232 CG PRO A 37 1.311 -0.699 11.692 1.00 30.13 C ATOM 233 CD PRO A 37 2.175 -0.128 10.602 1.00 31.24 C ATOM 234 N GLU A 38 2.535 3.180 12.153 1.00 31.76 N ATOM 235 CA GLU A 38 3.091 4.437 12.597 1.00 36.67 C ATOM 236 C GLU A 38 3.506 5.232 11.368 1.00 33.49 C ATOM 237 O GLU A 38 3.773 4.650 10.321 1.00 33.49 O ATOM 238 CB GLU A 38 4.288 4.170 13.503 1.00 38.14 C ATOM 239 CG GLU A 38 3.927 3.353 14.736 1.00 47.25 C ATOM 240 CD GLU A 38 5.049 3.293 15.752 1.00 47.73 C ATOM 241 OE1 GLU A 38 5.609 4.365 16.069 1.00 55.39 O ATOM 242 OE2 GLU A 38 5.360 2.181 16.240 1.00 61.70 O ATOM 243 N GLY A 39 3.531 6.559 11.491 1.00 33.91 N ATOM 244 CA GLY A 39 3.929 7.408 10.381 1.00 32.01 C ATOM 245 C GLY A 39 2.756 8.025 9.644 1.00 33.17 C ATOM 246 O GLY A 39 1.612 7.871 10.062 1.00 32.76 O ATOM 247 N PRO A 40 3.012 8.741 8.538 1.00 33.14 N ATOM 248 CA PRO A 40 1.945 9.373 7.763 1.00 32.97 C ATOM 249 C PRO A 40 1.357 8.402 6.751 1.00 34.70 C ATOM 250 O PRO A 40 1.950 7.353 6.456 1.00 31.70 O ATOM 251 CB PRO A 40 2.659 10.532 7.046 1.00 32.66 C ATOM 252 CG PRO A 40 3.983 10.681 7.780 1.00 34.44 C ATOM 253 CD PRO A 40 4.325 9.258 8.119 1.00 35.32 C ATOM 254 N VAL A 41 0.187 8.765 6.230 1.00 33.78 N ATOM 255 CA VAL A 41 -0.470 7.985 5.201 1.00 35.77 C ATOM 256 C VAL A 41 0.075 8.630 3.946 1.00 38.21 C ATOM 257 O VAL A 41 -0.358 9.716 3.569 1.00 40.66 O ATOM 258 CB VAL A 41 -1.977 8.180 5.210 1.00 33.03 C ATOM 259 CG1 VAL A 41 -2.589 7.420 4.052 1.00 30.77 C ATOM 260 CG2 VAL A 41 -2.546 7.726 6.541 1.00 34.60 C ATOM 261 N ALA A 42 1.033 7.978 3.301 1.00 38.78 N ATOM 262 CA ALA A 42 1.637 8.556 2.111 1.00 39.87 C ATOM 263 C ALA A 42 0.910 8.231 0.819 1.00 40.59 C ATOM 264 O ALA A 42 0.209 7.222 0.729 1.00 38.27 O ATOM 265 CB ALA A 42 3.091 8.108 2.004 1.00 41.53 C ATOM 266 N SER A 43 1.081 9.100 -0.180 1.00 40.59 N ATOM 267 CA SER A 43 0.494 8.878 -1.492 1.00 43.17 C ATOM 268 C SER A 43 1.431 7.964 -2.235 1.00 42.61 C ATOM 269 O SER A 43 2.664 8.056 -2.197 1.00 43.18 O ATOM 270 CB SER A 43 0.317 10.202 -2.251 1.00 42.56 C ATOM 271 OG SER A 43 1.535 10.921 -2.316 1.00 46.16 O ATOM 272 N TRP A 44 0.817 7.064 -3.009 1.00 40.25 N ATOM 273 CA TRP A 44 1.579 6.093 -3.720 1.00 39.72 C ATOM 274 C TRP A 44 1.284 6.294 -5.202 1.00 43.21 C ATOM 275 O TRP A 44 0.147 6.106 -5.630 1.00 44.01 O ATOM 276 CB TRP A 44 1.134 4.730 -3.206 1.00 37.90 C ATOM 277 CG TRP A 44 1.961 3.589 -3.611 1.00 35.34 C ATOM 278 CD1 TRP A 44 3.321 3.522 -3.627 1.00 35.62 C ATOM 279 CD2 TRP A 44 1.487 2.308 -4.035 1.00 35.46 C ATOM 280 NE1 TRP A 44 3.727 2.274 -4.047 1.00 36.76 N ATOM 281 CE2 TRP A 44 2.619 1.513 -4.314 1.00 31.84 C ATOM 282 CE3 TRP A 44 0.206 1.760 -4.227 1.00 30.57 C ATOM 283 CZ2 TRP A 44 2.518 0.193 -4.753 1.00 28.06 C ATOM 284 CZ3 TRP A 44 0.105 0.443 -4.665 1.00 29.03 C ATOM 285 CH2 TRP A 44 1.255 -0.320 -4.933 1.00 32.52 C ATOM 286 N PRO A 45 2.305 6.680 -6.003 1.00 44.49 N ATOM 287 CA PRO A 45 2.232 6.937 -7.451 1.00 44.38 C ATOM 288 C PRO A 45 1.804 5.777 -8.346 1.00 45.87 C ATOM 289 O PRO A 45 2.587 5.310 -9.170 1.00 47.65 O ATOM 290 CB PRO A 45 3.650 7.407 -7.799 1.00 43.64 C ATOM 291 CG PRO A 45 4.243 7.818 -6.497 1.00 42.50 C ATOM 292 CD PRO A 45 3.701 6.787 -5.552 1.00 45.12 C ATOM 293 N VAL A 46 0.562 5.329 -8.203 1.00 46.30 N ATOM 294 CA VAL A 46 0.054 4.212 -8.979 1.00 47.91 C ATOM 295 C VAL A 46 -1.384 4.390 -9.189 1.00 52.18 C ATOM 296 O VAL A 46 -2.084 5.171 -8.458 1.00 55.84 O ATOM 297 CB VAL A 46 0.323 2.857 -8.311 1.00 46.99 C ATOM 298 CG1 VAL A 46 -0.162 1.705 -9.189 1.00 48.62 C ATOM 299 CG2 VAL A 46 1.796 2.705 -8.031 1.00 45.88 C ATOM 300 N GLN A 47 -1.799 3.770 -10.276 1.00 55.46 N ATOM 301 CA GLN A 47 -3.124 3.922 -10.747 1.00 57.29 C ATOM 302 C GLN A 47 -3.772 2.703 -11.353 1.00 55.71 C ATOM 303 O GLN A 47 -5.004 2.614 -11.463 1.00 57.30 O ATOM 304 CB GLN A 47 -3.074 5.103 -11.707 1.00 59.88 C ATOM 305 CG GLN A 47 -4.395 5.713 -12.061 1.00 65.59 C ATOM 306 CD GLN A 47 -4.267 7.118 -12.621 1.00 73.18 C ATOM 307 OE1 GLN A 47 -3.162 7.627 -12.818 1.00 74.00 O ATOM 308 NE2 GLN A 47 -5.410 7.755 -12.881 1.00 72.92 N ATOM 309 N ARG A 48 -2.926 1.795 -11.818 1.00 52.47 N ATOM 310 CA ARG A 48 -3.406 0.526 -12.315 1.00 49.14 C ATOM 311 C ARG A 48 -2.454 -0.561 -11.897 1.00 48.39 C ATOM 312 O ARG A 48 -1.248 -0.465 -12.055 1.00 47.29 O ATOM 313 CB ARG A 48 -3.591 0.495 -13.824 1.00 49.63 C ATOM 314 N PRO A 49 -3.010 -1.627 -11.348 1.00 50.03 N ATOM 315 CA PRO A 49 -2.266 -2.802 -10.881 1.00 50.13 C ATOM 316 C PRO A 49 -1.259 -3.140 -11.988 1.00 50.97 C ATOM 317 O PRO A 49 -0.313 -3.892 -11.789 1.00 52.77 O ATOM 318 CB PRO A 49 -3.350 -3.876 -10.787 1.00 49.75 C ATOM 319 CG PRO A 49 -4.430 -3.359 -11.750 1.00 50.41 C ATOM 320 CD PRO A 49 -4.442 -1.906 -11.507 1.00 49.57 C ATOM 321 N ALA A 50 -1.500 -2.597 -13.178 1.00 51.35 N ATOM 322 CA ALA A 50 -0.639 -2.845 -14.332 1.00 51.70 C ATOM 323 C ALA A 50 0.681 -2.080 -14.270 1.00 52.87 C ATOM 324 O ALA A 50 1.704 -2.563 -14.759 1.00 54.90 O ATOM 325 CB ALA A 50 -1.383 -2.504 -15.620 1.00 50.93 C ATOM 326 N ASP A 51 0.655 -0.889 -13.677 1.00 51.77 N ATOM 327 CA ASP A 51 1.868 -0.100 -13.555 1.00 54.86 C ATOM 328 C ASP A 51 2.532 -0.233 -12.186 1.00 54.79 C ATOM 329 O ASP A 51 3.198 0.689 -11.715 1.00 56.35 O ATOM 330 CB ASP A 51 1.643 1.401 -13.866 1.00 58.17 C ATOM 331 CG ASP A 51 0.188 1.774 -14.112 1.00 61.38 C ATOM 332 OD1 ASP A 51 -0.396 2.480 -13.254 1.00 62.62 O ATOM 333 OD2 ASP A 51 -0.361 1.391 -15.170 1.00 62.59 O ATOM 334 N ILE A 52 2.351 -1.387 -11.552 1.00 53.55 N ATOM 335 CA ILE A 52 2.958 -1.656 -10.254 1.00 51.77 C ATOM 336 C ILE A 52 4.312 -2.300 -10.509 1.00 53.75 C ATOM 337 O ILE A 52 4.401 -3.325 -11.190 1.00 54.49 O ATOM 338 CB ILE A 52 2.089 -2.619 -9.412 1.00 51.64 C ATOM 339 CG1 ILE A 52 0.884 -1.862 -8.842 1.00 50.68 C ATOM 340 CG2 ILE A 52 2.923 -3.237 -8.296 1.00 48.66 C ATOM 341 CD1 ILE A 52 -0.173 -2.747 -8.220 1.00 38.59 C ATOM 342 N THR A 53 5.364 -1.703 -9.959 1.00 54.92 N ATOM 343 CA THR A 53 6.721 -2.207 -10.156 1.00 55.92 C ATOM 344 C THR A 53 7.436 -2.449 -8.830 1.00 56.16 C ATOM 345 O THR A 53 7.125 -1.812 -7.825 1.00 57.04 O ATOM 346 CB THR A 53 7.560 -1.204 -10.965 1.00 55.82 C ATOM 347 OG1 THR A 53 8.120 -0.230 -10.077 1.00 56.39 O ATOM 348 CG2 THR A 53 6.686 -0.484 -11.983 1.00 59.88 C ATOM 349 N ALA A 54 8.397 -3.367 -8.837 1.00 56.59 N ATOM 350 CA ALA A 54 9.168 -3.688 -7.640 1.00 54.96 C ATOM 351 C ALA A 54 9.715 -2.408 -7.034 1.00 53.53 C ATOM 352 O ALA A 54 9.826 -2.283 -5.816 1.00 55.14 O ATOM 353 CB ALA A 54 10.313 -4.619 -7.992 1.00 57.70 C ATOM 354 N SER A 55 10.058 -1.459 -7.897 1.00 51.63 N ATOM 355 CA SER A 55 10.591 -0.179 -7.455 1.00 52.00 C ATOM 356 C SER A 55 9.537 0.557 -6.631 1.00 51.10 C ATOM 357 O SER A 55 9.841 1.215 -5.640 1.00 52.27 O ATOM 358 CB SER A 55 10.991 0.661 -8.669 1.00 52.24 C ATOM 359 OG SER A 55 11.625 1.859 -8.268 1.00 52.45 O ATOM 360 N LEU A 56 8.288 0.432 -7.053 1.00 50.97 N ATOM 361 CA LEU A 56 7.177 1.063 -6.365 1.00 49.11 C ATOM 362 C LEU A 56 6.826 0.314 -5.085 1.00 49.91 C ATOM 363 O LEU A 56 6.507 0.924 -4.067 1.00 53.89 O ATOM 364 CB LEU A 56 5.966 1.116 -7.293 1.00 46.64 C ATOM 365 CG LEU A 56 5.905 2.355 -8.179 1.00 48.05 C ATOM 366 CD1 LEU A 56 4.818 2.194 -9.219 1.00 48.42 C ATOM 367 CD2 LEU A 56 5.648 3.574 -7.305 1.00 45.47 C ATOM 368 N LEU A 57 6.891 -1.010 -5.142 1.00 47.70 N ATOM 369 CA LEU A 57 6.581 -1.847 -3.994 1.00 46.78 C ATOM 370 C LEU A 57 7.566 -1.618 -2.861 1.00 47.93 C ATOM 371 O LEU A 57 7.195 -1.637 -1.687 1.00 46.19 O ATOM 372 CB LEU A 57 6.605 -3.319 -4.406 1.00 47.33 C ATOM 373 CG LEU A 57 5.283 -4.068 -4.605 1.00 49.97 C ATOM 374 CD1 LEU A 57 4.087 -3.109 -4.683 1.00 48.05 C ATOM 375 CD2 LEU A 57 5.408 -4.909 -5.867 1.00 50.60 C ATOM 376 N GLN A 58 8.825 -1.403 -3.218 1.00 49.73 N ATOM 377 CA GLN A 58 9.861 -1.176 -2.221 1.00 52.10 C ATOM 378 C GLN A 58 9.784 0.199 -1.585 1.00 50.05 C ATOM 379 O GLN A 58 10.144 0.373 -0.427 1.00 51.15 O ATOM 380 CB GLN A 58 11.234 -1.404 -2.842 1.00 55.15 C ATOM 381 CG GLN A 58 11.525 -2.881 -3.050 1.00 63.10 C ATOM 382 CD GLN A 58 12.535 -3.134 -4.145 1.00 68.98 C ATOM 383 OE1 GLN A 58 12.305 -3.964 -5.028 1.00 70.68 O ATOM 384 NE2 GLN A 58 13.662 -2.424 -4.099 1.00 63.16 N ATOM 385 N GLN A 59 9.313 1.184 -2.330 1.00 50.61 N ATOM 386 CA GLN A 59 9.192 2.513 -1.757 1.00 53.37 C ATOM 387 C GLN A 59 8.031 2.510 -0.762 1.00 52.09 C ATOM 388 O GLN A 59 8.079 3.184 0.263 1.00 51.39 O ATOM 389 CB GLN A 59 8.986 3.537 -2.874 1.00 53.41 C ATOM 390 CG GLN A 59 7.806 4.467 -2.727 1.00 58.10 C ATOM 391 CD GLN A 59 7.773 5.493 -3.840 1.00 63.19 C ATOM 392 OE1 GLN A 59 8.434 5.323 -4.866 1.00 65.62 O ATOM 393 NE2 GLN A 59 6.999 6.558 -3.651 1.00 61.94 N ATOM 394 N ALA A 60 6.999 1.727 -1.062 1.00 52.68 N ATOM 395 CA ALA A 60 5.832 1.616 -0.191 1.00 54.43 C ATOM 396 C ALA A 60 6.213 0.879 1.096 1.00 55.12 C ATOM 397 O ALA A 60 5.852 1.291 2.204 1.00 55.25 O ATOM 398 CB ALA A 60 4.712 0.868 -0.910 1.00 54.41 C ATOM 399 N ALA A 61 6.938 -0.220 0.929 1.00 53.61 N ATOM 400 CA ALA A 61 7.401 -1.019 2.046 1.00 53.64 C ATOM 401 C ALA A 61 8.497 -0.236 2.773 1.00 56.37 C ATOM 402 O ALA A 61 8.615 -0.302 3.995 1.00 57.39 O ATOM 403 CB ALA A 61 7.955 -2.348 1.529 1.00 49.92 C ATOM 404 N GLY A 62 9.275 0.520 1.999 1.00 59.55 N ATOM 405 CA GLY A 62 10.387 1.299 2.522 1.00 63.12 C ATOM 406 C GLY A 62 10.147 2.239 3.683 1.00 67.58 C ATOM 407 O GLY A 62 11.081 2.890 4.149 1.00 69.41 O ATOM 408 N LEU A 63 8.907 2.351 4.137 1.00 71.13 N ATOM 409 CA LEU A 63 8.622 3.207 5.277 1.00 75.59 C ATOM 410 C LEU A 63 8.549 2.266 6.464 1.00 78.68 C ATOM 411 O LEU A 63 7.478 1.761 6.799 1.00 78.36 O ATOM 412 CB LEU A 63 7.303 3.924 5.097 1.00 76.31 C ATOM 413 N ALA A 64 9.703 2.017 7.076 1.00 82.06 N ATOM 414 CA ALA A 64 9.803 1.122 8.223 1.00 82.97 C ATOM 415 C ALA A 64 9.800 -0.329 7.756 1.00 83.99 C ATOM 416 O ALA A 64 10.845 -0.876 7.400 1.00 85.62 O ATOM 417 CB ALA A 64 8.652 1.367 9.187 1.00 83.16 C ATOM 418 N ALA A 88 12.518 -4.601 6.616 1.00 57.10 N ATOM 419 CA ALA A 88 12.206 -4.461 8.034 1.00 57.42 C ATOM 420 C ALA A 88 10.739 -4.714 8.418 1.00 56.75 C ATOM 421 O ALA A 88 10.408 -4.710 9.607 1.00 58.31 O ATOM 422 CB ALA A 88 12.638 -3.081 8.522 1.00 57.06 C ATOM 423 N PRO A 89 9.839 -4.900 7.429 1.00 54.02 N ATOM 424 CA PRO A 89 8.431 -5.155 7.744 1.00 51.69 C ATOM 425 C PRO A 89 8.156 -6.641 7.527 1.00 49.58 C ATOM 426 O PRO A 89 8.791 -7.272 6.686 1.00 49.75 O ATOM 427 CB PRO A 89 7.674 -4.292 6.721 1.00 50.83 C ATOM 428 CG PRO A 89 8.771 -3.547 5.935 1.00 49.35 C ATOM 429 CD PRO A 89 9.941 -4.463 6.030 1.00 54.48 C ATOM 430 N GLU A 90 7.216 -7.195 8.276 1.00 48.62 N ATOM 431 CA GLU A 90 6.870 -8.607 8.150 1.00 51.50 C ATOM 432 C GLU A 90 6.197 -8.877 6.802 1.00 49.26 C ATOM 433 O GLU A 90 6.670 -9.681 6.007 1.00 48.94 O ATOM 434 CB GLU A 90 5.910 -8.993 9.277 1.00 51.45 C ATOM 435 CG GLU A 90 6.312 -10.182 10.129 1.00 56.01 C ATOM 436 CD GLU A 90 5.345 -10.399 11.288 1.00 57.46 C ATOM 437 OE1 GLU A 90 5.385 -9.613 12.264 1.00 62.63 O ATOM 438 OE2 GLU A 90 4.534 -11.346 11.217 1.00 63.53 O ATOM 439 N VAL A 91 5.101 -8.169 6.552 1.00 47.74 N ATOM 440 CA VAL A 91 4.312 -8.337 5.341 1.00 43.65 C ATOM 441 C VAL A 91 3.969 -7.027 4.636 1.00 40.37 C ATOM 442 O VAL A 91 3.667 -6.025 5.287 1.00 39.84 O ATOM 443 CB VAL A 91 2.953 -9.009 5.679 1.00 44.20 C ATOM 444 CG1 VAL A 91 2.314 -9.587 4.426 1.00 42.85 C ATOM 445 CG2 VAL A 91 3.144 -10.069 6.746 1.00 48.11 C ATOM 446 N LEU A 92 4.026 -7.036 3.308 1.00 36.24 N ATOM 447 CA LEU A 92 3.617 -5.875 2.538 1.00 34.33 C ATOM 448 C LEU A 92 2.346 -6.307 1.828 1.00 36.20 C ATOM 449 O LEU A 92 2.370 -7.150 0.929 1.00 37.66 O ATOM 450 CB LEU A 92 4.642 -5.443 1.489 1.00 32.56 C ATOM 451 CG LEU A 92 4.029 -4.434 0.490 1.00 36.23 C ATOM 452 CD1 LEU A 92 3.394 -3.262 1.241 1.00 31.21 C ATOM 453 CD2 LEU A 92 5.084 -3.931 -0.478 1.00 34.89 C ATOM 454 N LEU A 93 1.232 -5.745 2.269 1.00 35.59 N ATOM 455 CA LEU A 93 -0.064 -6.031 1.685 1.00 32.90 C ATOM 456 C LEU A 93 -0.241 -5.101 0.502 1.00 32.78 C ATOM 457 O LEU A 93 0.064 -3.912 0.591 1.00 33.44 O ATOM 458 CB LEU A 93 -1.170 -5.756 2.705 1.00 35.69 C ATOM 459 CG LEU A 93 -1.663 -6.833 3.671 1.00 31.26 C ATOM 460 CD1 LEU A 93 -0.582 -7.855 3.960 1.00 34.83 C ATOM 461 CD2 LEU A 93 -2.143 -6.153 4.935 1.00 31.31 C ATOM 462 N VAL A 94 -0.724 -5.639 -0.607 1.00 32.18 N ATOM 463 CA VAL A 94 -0.954 -4.819 -1.780 1.00 31.10 C ATOM 464 C VAL A 94 -2.397 -4.964 -2.274 1.00 32.83 C ATOM 465 O VAL A 94 -2.831 -6.053 -2.676 1.00 31.97 O ATOM 466 CB VAL A 94 0.024 -5.180 -2.909 1.00 30.97 C ATOM 467 CG1 VAL A 94 -0.174 -4.227 -4.099 1.00 27.07 C ATOM 468 CG2 VAL A 94 1.447 -5.098 -2.389 1.00 27.62 C ATOM 469 N GLY A 95 -3.137 -3.856 -2.201 1.00 33.43 N ATOM 470 CA GLY A 95 -4.520 -3.827 -2.650 1.00 31.59 C ATOM 471 C GLY A 95 -4.540 -3.422 -4.105 1.00 33.47 C ATOM 472 O GLY A 95 -4.304 -2.270 -4.442 1.00 35.24 O ATOM 473 N THR A 96 -4.814 -4.384 -4.973 1.00 35.58 N ATOM 474 CA THR A 96 -4.828 -4.153 -6.408 1.00 33.79 C ATOM 475 C THR A 96 -6.178 -3.699 -6.928 1.00 34.36 C ATOM 476 O THR A 96 -6.540 -3.953 -8.080 1.00 37.94 O ATOM 477 CB THR A 96 -4.373 -5.425 -7.155 1.00 33.87 C ATOM 478 OG1 THR A 96 -5.251 -6.524 -6.851 1.00 27.43 O ATOM 479 CG2 THR A 96 -2.963 -5.784 -6.718 1.00 30.14 C ATOM 480 N GLY A 97 -6.922 -3.013 -6.072 1.00 32.37 N ATOM 481 CA GLY A 97 -8.220 -2.527 -6.487 1.00 29.41 C ATOM 482 C GLY A 97 -9.387 -3.474 -6.282 1.00 29.55 C ATOM 483 O GLY A 97 -9.442 -4.262 -5.337 1.00 31.10 O ATOM 484 N ARG A 98 -10.325 -3.395 -7.209 1.00 30.09 N ATOM 485 CA ARG A 98 -11.558 -4.168 -7.159 1.00 30.54 C ATOM 486 C ARG A 98 -11.423 -5.680 -7.125 1.00 29.86 C ATOM 487 O ARG A 98 -12.260 -6.369 -6.542 1.00 28.63 O ATOM 488 CB ARG A 98 -12.407 -3.739 -8.327 1.00 31.81 C ATOM 489 CG ARG A 98 -13.803 -4.285 -8.418 1.00 38.31 C ATOM 490 CD ARG A 98 -14.221 -3.929 -9.821 1.00 53.41 C ATOM 491 NE ARG A 98 -12.986 -3.686 -10.572 1.00 54.04 N ATOM 492 CZ ARG A 98 -12.917 -3.155 -11.785 1.00 49.02 C ATOM 493 NH1 ARG A 98 -14.029 -2.805 -12.421 1.00 46.88 N ATOM 494 NH2 ARG A 98 -11.730 -2.945 -12.347 1.00 51.23 N ATOM 495 N ARG A 99 -10.385 -6.201 -7.760 1.00 27.65 N ATOM 496 CA ARG A 99 -10.164 -7.632 -7.753 1.00 29.96 C ATOM 497 C ARG A 99 -8.689 -7.889 -7.576 1.00 33.12 C ATOM 498 O ARG A 99 -7.868 -6.978 -7.700 1.00 31.11 O ATOM 499 CB ARG A 99 -10.653 -8.271 -9.057 1.00 30.97 C ATOM 500 CG ARG A 99 -12.026 -8.891 -8.946 1.00 39.17 C ATOM 501 CD ARG A 99 -12.495 -9.487 -10.253 1.00 48.36 C ATOM 502 NE ARG A 99 -12.638 -8.464 -11.280 1.00 51.28 N ATOM 503 CZ ARG A 99 -11.809 -8.322 -12.309 1.00 60.33 C ATOM 504 NH1 ARG A 99 -10.774 -9.147 -12.448 1.00 57.49 N ATOM 505 NH2 ARG A 99 -12.013 -7.353 -13.196 1.00 56.55 N ATOM 506 N GLN A 100 -8.356 -9.135 -7.264 1.00 35.02 N ATOM 507 CA GLN A 100 -6.974 -9.508 -7.087 1.00 36.40 C ATOM 508 C GLN A 100 -6.282 -9.476 -8.443 1.00 37.11 C ATOM 509 O GLN A 100 -6.905 -9.669 -9.484 1.00 37.65 O ATOM 510 CB GLN A 100 -6.892 -10.896 -6.464 1.00 37.20 C ATOM 511 CG GLN A 100 -5.566 -11.587 -6.669 1.00 47.11 C ATOM 512 CD GLN A 100 -5.652 -12.650 -7.737 1.00 52.24 C ATOM 513 OE1 GLN A 100 -6.093 -12.392 -8.858 1.00 53.18 O ATOM 514 NE2 GLN A 100 -5.233 -13.862 -7.393 1.00 63.48 N ATOM 515 N HIS A 101 -4.988 -9.200 -8.413 1.00 37.31 N ATOM 516 CA HIS A 101 -4.162 -9.124 -9.604 1.00 39.72 C ATOM 517 C HIS A 101 -2.853 -9.760 -9.179 1.00 42.51 C ATOM 518 O HIS A 101 -2.230 -9.319 -8.215 1.00 43.53 O ATOM 519 CB HIS A 101 -3.926 -7.664 -9.983 1.00 40.90 C ATOM 520 CG HIS A 101 -2.937 -7.472 -11.090 1.00 48.24 C ATOM 521 ND1 HIS A 101 -3.312 -7.312 -12.409 1.00 49.86 N ATOM 522 CD2 HIS A 101 -1.584 -7.422 -11.077 1.00 49.96 C ATOM 523 CE1 HIS A 101 -2.233 -7.171 -13.156 1.00 50.89 C ATOM 524 NE2 HIS A 101 -1.171 -7.236 -12.373 1.00 51.27 N ATOM 525 N LEU A 102 -2.443 -10.803 -9.887 1.00 45.06 N ATOM 526 CA LEU A 102 -1.209 -11.488 -9.552 1.00 46.81 C ATOM 527 C LEU A 102 0.018 -10.639 -9.836 1.00 46.64 C ATOM 528 O LEU A 102 0.154 -10.060 -10.913 1.00 47.83 O ATOM 529 CB LEU A 102 -1.120 -12.804 -10.323 1.00 47.28 C ATOM 530 CG LEU A 102 0.275 -13.379 -10.602 1.00 52.58 C ATOM 531 CD1 LEU A 102 1.058 -13.551 -9.313 1.00 54.15 C ATOM 532 CD2 LEU A 102 0.119 -14.710 -11.321 1.00 50.11 C ATOM 533 N LEU A 103 0.906 -10.566 -8.848 1.00 47.83 N ATOM 534 CA LEU A 103 2.155 -9.822 -8.969 1.00 48.20 C ATOM 535 C LEU A 103 3.238 -10.819 -9.378 1.00 48.85 C ATOM 536 O LEU A 103 3.354 -11.890 -8.782 1.00 50.31 O ATOM 537 CB LEU A 103 2.537 -9.196 -7.629 1.00 46.04 C ATOM 538 CG LEU A 103 1.618 -8.161 -6.990 1.00 43.93 C ATOM 539 CD1 LEU A 103 2.029 -7.971 -5.548 1.00 45.10 C ATOM 540 CD2 LEU A 103 1.693 -6.858 -7.738 1.00 38.11 C ATOM 541 N GLY A 104 4.037 -10.464 -10.375 1.00 49.41 N ATOM 542 CA GLY A 104 5.070 -11.373 -10.832 1.00 51.09 C ATOM 543 C GLY A 104 6.394 -11.318 -10.095 1.00 53.47 C ATOM 544 O GLY A 104 6.649 -10.397 -9.323 1.00 53.50 O ATOM 545 N PRO A 105 7.259 -12.319 -10.319 1.00 55.34 N ATOM 546 CA PRO A 105 8.597 -12.487 -9.735 1.00 56.04 C ATOM 547 C PRO A 105 9.479 -11.233 -9.797 1.00 55.56 C ATOM 548 O PRO A 105 10.191 -10.919 -8.845 1.00 56.96 O ATOM 549 CB PRO A 105 9.180 -13.667 -10.532 1.00 56.85 C ATOM 550 CG PRO A 105 8.271 -13.777 -11.770 1.00 57.67 C ATOM 551 CD PRO A 105 6.931 -13.457 -11.192 1.00 55.64 C ATOM 552 N GLU A 106 9.431 -10.514 -10.910 1.00 56.32 N ATOM 553 CA GLU A 106 10.222 -9.296 -11.060 1.00 56.68 C ATOM 554 C GLU A 106 9.644 -8.133 -10.246 1.00 57.83 C ATOM 555 O GLU A 106 10.256 -7.068 -10.150 1.00 58.94 O ATOM 556 CB GLU A 106 10.304 -8.906 -12.526 1.00 56.34 C ATOM 557 N GLN A 107 8.465 -8.337 -9.666 1.00 59.07 N ATOM 558 CA GLN A 107 7.807 -7.309 -8.858 1.00 59.77 C ATOM 559 C GLN A 107 8.161 -7.545 -7.407 1.00 58.67 C ATOM 560 O GLN A 107 8.593 -6.658 -6.673 1.00 57.87 O ATOM 561 CB GLN A 107 6.283 -7.447 -8.937 1.00 60.02 C ATOM 562 CG GLN A 107 5.717 -7.817 -10.283 1.00 64.59 C ATOM 563 CD GLN A 107 4.999 -6.658 -10.918 1.00 70.82 C ATOM 564 OE1 GLN A 107 5.582 -5.591 -11.103 1.00 78.48 O ATOM 565 NE2 GLN A 107 3.724 -6.851 -11.251 1.00 63.04 N ATOM 566 N VAL A 108 7.941 -8.794 -7.032 1.00 59.51 N ATOM 567 CA VAL A 108 8.100 -9.300 -5.688 1.00 60.14 C ATOM 568 C VAL A 108 9.437 -9.876 -5.214 1.00 60.98 C ATOM 569 O VAL A 108 9.638 -10.007 -4.011 1.00 60.87 O ATOM 570 CB VAL A 108 6.957 -10.322 -5.446 1.00 59.51 C ATOM 571 CG1 VAL A 108 7.225 -11.188 -4.227 1.00 64.43 C ATOM 572 CG2 VAL A 108 5.647 -9.563 -5.283 1.00 56.42 C ATOM 573 N ARG A 109 10.363 -10.210 -6.106 1.00 62.61 N ATOM 574 CA ARG A 109 11.624 -10.773 -5.617 1.00 62.87 C ATOM 575 C ARG A 109 12.512 -9.865 -4.765 1.00 62.35 C ATOM 576 O ARG A 109 12.934 -10.261 -3.677 1.00 63.34 O ATOM 577 CB ARG A 109 12.441 -11.362 -6.761 1.00 62.95 C ATOM 578 CG ARG A 109 12.149 -12.822 -6.930 1.00 64.87 C ATOM 579 CD ARG A 109 12.837 -13.396 -8.122 1.00 68.07 C ATOM 580 NE ARG A 109 12.423 -14.777 -8.319 1.00 67.19 N ATOM 581 CZ ARG A 109 12.697 -15.479 -9.409 1.00 65.82 C ATOM 582 NH1 ARG A 109 13.384 -14.917 -10.394 1.00 63.96 N ATOM 583 NH2 ARG A 109 12.284 -16.734 -9.514 1.00 60.90 N ATOM 584 N PRO A 110 12.813 -8.647 -5.238 1.00 59.15 N ATOM 585 CA PRO A 110 13.661 -7.781 -4.417 1.00 58.71 C ATOM 586 C PRO A 110 13.239 -7.811 -2.944 1.00 60.60 C ATOM 587 O PRO A 110 14.066 -7.982 -2.048 1.00 61.86 O ATOM 588 CB PRO A 110 13.453 -6.415 -5.047 1.00 56.56 C ATOM 589 CG PRO A 110 13.290 -6.756 -6.493 1.00 58.41 C ATOM 590 CD PRO A 110 12.357 -7.946 -6.449 1.00 57.49 C ATOM 591 N LEU A 111 11.941 -7.657 -2.705 1.00 58.49 N ATOM 592 CA LEU A 111 11.410 -7.668 -1.352 1.00 55.79 C ATOM 593 C LEU A 111 11.708 -8.959 -0.602 1.00 56.87 C ATOM 594 O LEU A 111 12.115 -8.927 0.560 1.00 54.83 O ATOM 595 CB LEU A 111 9.903 -7.429 -1.378 1.00 55.29 C ATOM 596 CG LEU A 111 9.499 -5.979 -1.621 1.00 52.28 C ATOM 597 CD1 LEU A 111 7.990 -5.846 -1.586 1.00 50.50 C ATOM 598 CD2 LEU A 111 10.133 -5.114 -0.549 1.00 50.71 C ATOM 599 N LEU A 112 11.485 -10.097 -1.252 1.00 58.16 N ATOM 600 CA LEU A 112 11.757 -11.379 -0.612 1.00 62.03 C ATOM 601 C LEU A 112 13.256 -11.408 -0.331 1.00 62.27 C ATOM 602 O LEU A 112 13.708 -11.979 0.659 1.00 65.46 O ATOM 603 CB LEU A 112 11.386 -12.540 -1.537 1.00 63.30 C ATOM 604 CG LEU A 112 10.006 -12.510 -2.200 1.00 70.64 C ATOM 605 CD1 LEU A 112 9.839 -13.754 -3.058 1.00 77.18 C ATOM 606 CD2 LEU A 112 8.907 -12.436 -1.148 1.00 75.94 C ATOM 607 N ALA A 113 14.019 -10.774 -1.213 1.00 61.00 N ATOM 608 CA ALA A 113 15.463 -10.706 -1.065 1.00 60.57 C ATOM 609 C ALA A 113 15.768 -10.056 0.279 1.00 61.87 C ATOM 610 O ALA A 113 16.887 -10.136 0.789 1.00 61.83 O ATOM 611 CB ALA A 113 16.066 -9.882 -2.200 1.00 60.78 C HETATM 612 N MSE A 114 14.751 -9.412 0.842 1.00 61.09 N HETATM 613 CA MSE A 114 14.862 -8.743 2.129 1.00 65.41 C HETATM 614 C MSE A 114 14.039 -9.443 3.193 1.00 59.66 C HETATM 615 O MSE A 114 13.834 -8.904 4.277 1.00 60.10 O HETATM 616 CB MSE A 114 14.382 -7.309 2.008 1.00 62.53 C HETATM 617 CG MSE A 114 15.404 -6.389 1.438 1.00 68.71 C HETATM 618 SE MSE A 114 14.509 -4.902 0.658 1.00 92.94 HETATM 619 CE MSE A 114 14.828 -5.333 -1.198 1.00 89.87 C ATOM 620 N GLY A 115 13.565 -10.641 2.881 1.00 57.51 N ATOM 621 CA GLY A 115 12.757 -11.375 3.833 1.00 53.81 C ATOM 622 C GLY A 115 11.372 -10.773 3.999 1.00 53.84 C ATOM 623 O GLY A 115 10.642 -11.138 4.917 1.00 55.38 O ATOM 624 N VAL A 116 11.006 -9.840 3.126 1.00 52.07 N ATOM 625 CA VAL A 116 9.687 -9.223 3.205 1.00 48.69 C ATOM 626 C VAL A 116 8.742 -9.995 2.309 1.00 47.07 C ATOM 627 O VAL A 116 9.005 -10.163 1.122 1.00 47.83 O ATOM 628 CB VAL A 116 9.682 -7.758 2.721 1.00 48.44 C ATOM 629 CG1 VAL A 116 8.274 -7.196 2.847 1.00 47.89 C ATOM 630 CG2 VAL A 116 10.669 -6.925 3.522 1.00 45.83 C ATOM 631 N GLY A 117 7.645 -10.470 2.882 1.00 45.75 N ATOM 632 CA GLY A 117 6.677 -11.219 2.103 1.00 45.95 C ATOM 633 C GLY A 117 5.544 -10.318 1.664 1.00 45.55 C ATOM 634 O GLY A 117 5.050 -9.515 2.454 1.00 48.29 O ATOM 635 N VAL A 118 5.128 -10.441 0.409 1.00 43.30 N ATOM 636 CA VAL A 118 4.052 -9.605 -0.099 1.00 40.70 C ATOM 637 C VAL A 118 2.813 -10.388 -0.503 1.00 40.53 C ATOM 638 O VAL A 118 2.890 -11.523 -0.954 1.00 42.37 O ATOM 639 CB VAL A 118 4.544 -8.713 -1.281 1.00 40.92 C ATOM 640 CG1 VAL A 118 5.985 -9.013 -1.589 1.00 39.81 C ATOM 641 CG2 VAL A 118 3.671 -8.906 -2.511 1.00 37.38 C ATOM 642 N GLU A 119 1.664 -9.755 -0.334 1.00 39.43 N ATOM 643 CA GLU A 119 0.394 -10.372 -0.653 1.00 42.27 C ATOM 644 C GLU A 119 -0.507 -9.387 -1.376 1.00 38.76 C ATOM 645 O GLU A 119 -0.841 -8.334 -0.836 1.00 37.52 O ATOM 646 CB GLU A 119 -0.280 -10.825 0.636 1.00 43.68 C ATOM 647 CG GLU A 119 0.636 -11.637 1.527 1.00 53.70 C ATOM 648 CD GLU A 119 -0.062 -12.151 2.770 1.00 53.31 C ATOM 649 OE1 GLU A 119 -1.290 -12.381 2.704 1.00 66.88 O ATOM 650 OE2 GLU A 119 0.619 -12.341 3.801 1.00 57.88 O ATOM 651 N ALA A 120 -0.896 -9.730 -2.599 1.00 35.94 N ATOM 652 CA ALA A 120 -1.774 -8.875 -3.381 1.00 32.21 C ATOM 653 C ALA A 120 -3.181 -9.429 -3.257 1.00 30.93 C ATOM 654 O ALA A 120 -3.367 -10.631 -3.187 1.00 30.86 O ATOM 655 CB ALA A 120 -1.339 -8.869 -4.824 1.00 33.32 C HETATM 656 N MSE A 121 -4.168 -8.549 -3.193 1.00 29.33 N HETATM 657 CA MSE A 121 -5.557 -8.969 -3.086 1.00 28.54 C HETATM 658 C MSE A 121 -6.382 -7.748 -3.404 1.00 26.32 C HETATM 659 O MSE A 121 -5.841 -6.646 -3.472 1.00 27.92 O HETATM 660 CB MSE A 121 -5.860 -9.470 -1.670 1.00 28.76 C HETATM 661 CG MSE A 121 -5.465 -8.499 -0.557 1.00 36.29 C HETATM 662 SE MSE A 121 -5.632 -9.244 1.232 1.00 39.40 HETATM 663 CE MSE A 121 -3.940 -10.223 1.275 1.00 32.90 C ATOM 664 N ASP A 122 -7.681 -7.927 -3.618 1.00 24.58 N ATOM 665 CA ASP A 122 -8.528 -6.784 -3.909 1.00 25.70 C ATOM 666 C ASP A 122 -8.365 -5.821 -2.741 1.00 28.62 C ATOM 667 O ASP A 122 -8.084 -6.235 -1.617 1.00 29.62 O ATOM 668 CB ASP A 122 -9.991 -7.214 -4.062 1.00 25.31 C ATOM 669 CG ASP A 122 -10.525 -7.907 -2.844 1.00 25.72 C ATOM 670 OD1 ASP A 122 -10.147 -9.076 -2.612 1.00 31.30 O ATOM 671 OD2 ASP A 122 -11.315 -7.278 -2.108 1.00 34.58 O ATOM 672 N THR A 123 -8.550 -4.538 -3.017 1.00 30.86 N ATOM 673 CA THR A 123 -8.394 -3.486 -2.028 1.00 30.94 C ATOM 674 C THR A 123 -9.208 -3.541 -0.736 1.00 32.86 C ATOM 675 O THR A 123 -8.655 -3.277 0.332 1.00 35.25 O ATOM 676 CB THR A 123 -8.580 -2.113 -2.698 1.00 28.87 C ATOM 677 OG1 THR A 123 -7.495 -1.894 -3.604 1.00 29.74 O ATOM 678 CG2 THR A 123 -8.590 -1.001 -1.670 1.00 30.76 C ATOM 679 N GLN A 124 -10.497 -3.875 -0.796 1.00 32.81 N ATOM 680 CA GLN A 124 -11.274 -3.920 0.448 1.00 35.24 C ATOM 681 C GLN A 124 -10.718 -4.984 1.407 1.00 32.93 C ATOM 682 O GLN A 124 -10.795 -4.841 2.627 1.00 34.52 O ATOM 683 CB GLN A 124 -12.762 -4.186 0.182 1.00 34.88 C ATOM 684 CG GLN A 124 -13.388 -3.418 -0.997 1.00 51.66 C ATOM 685 CD GLN A 124 -13.318 -1.896 -0.884 1.00 61.82 C ATOM 686 OE1 GLN A 124 -13.828 -1.297 0.064 1.00 68.17 O ATOM 687 NE2 GLN A 124 -12.695 -1.264 -1.871 1.00 67.14 N ATOM 688 N ALA A 125 -10.146 -6.045 0.853 1.00 33.09 N ATOM 689 CA ALA A 125 -9.566 -7.112 1.666 1.00 33.71 C ATOM 690 C ALA A 125 -8.198 -6.697 2.203 1.00 34.97 C ATOM 691 O ALA A 125 -7.863 -6.972 3.358 1.00 37.31 O ATOM 692 CB ALA A 125 -9.442 -8.391 0.847 1.00 32.80 C ATOM 693 N ALA A 126 -7.408 -6.036 1.365 1.00 32.41 N ATOM 694 CA ALA A 126 -6.092 -5.566 1.787 1.00 32.38 C ATOM 695 C ALA A 126 -6.253 -4.676 3.024 1.00 30.69 C ATOM 696 O ALA A 126 -5.593 -4.873 4.040 1.00 28.69 O ATOM 697 CB ALA A 126 -5.428 -4.789 0.656 1.00 27.05 C ATOM 698 N ALA A 127 -7.165 -3.716 2.920 1.00 32.04 N ATOM 699 CA ALA A 127 -7.457 -2.770 3.989 1.00 33.62 C ATOM 700 C ALA A 127 -7.856 -3.481 5.276 1.00 34.38 C ATOM 701 O ALA A 127 -7.365 -3.179 6.363 1.00 32.81 O ATOM 702 CB ALA A 127 -8.575 -1.824 3.541 1.00 31.00 C ATOM 703 N ARG A 128 -8.766 -4.429 5.127 1.00 34.90 N ATOM 704 CA ARG A 128 -9.275 -5.228 6.223 1.00 31.82 C ATOM 705 C ARG A 128 -8.192 -6.163 6.774 1.00 31.21 C ATOM 706 O ARG A 128 -8.115 -6.409 7.980 1.00 32.38 O ATOM 707 CB ARG A 128 -10.465 -6.011 5.703 1.00 31.24 C ATOM 708 CG ARG A 128 -10.988 -7.108 6.586 1.00 41.92 C ATOM 709 CD ARG A 128 -11.939 -7.933 5.745 1.00 51.99 C ATOM 710 NE ARG A 128 -12.789 -7.046 4.952 1.00 61.81 N ATOM 711 CZ ARG A 128 -13.081 -7.223 3.665 1.00 63.39 C ATOM 712 NH1 ARG A 128 -12.594 -8.267 3.003 1.00 53.63 N ATOM 713 NH2 ARG A 128 -13.851 -6.340 3.037 1.00 56.60 N ATOM 714 N THR A 129 -7.349 -6.690 5.899 1.00 31.13 N ATOM 715 CA THR A 129 -6.288 -7.571 6.373 1.00 30.64 C ATOM 716 C THR A 129 -5.226 -6.745 7.106 1.00 31.21 C ATOM 717 O THR A 129 -4.539 -7.241 7.997 1.00 29.97 O ATOM 718 CB THR A 129 -5.634 -8.362 5.211 1.00 29.74 C ATOM 719 OG1 THR A 129 -6.615 -9.190 4.578 1.00 27.83 O ATOM 720 CG2 THR A 129 -4.546 -9.250 5.731 1.00 27.67 C ATOM 721 N TYR A 130 -5.107 -5.479 6.728 1.00 32.49 N ATOM 722 CA TYR A 130 -4.151 -4.580 7.363 1.00 31.90 C ATOM 723 C TYR A 130 -4.568 -4.296 8.802 1.00 32.61 C ATOM 724 O TYR A 130 -3.743 -4.344 9.715 1.00 32.07 O ATOM 725 CB TYR A 130 -4.066 -3.250 6.607 1.00 28.64 C ATOM 726 CG TYR A 130 -3.457 -2.154 7.442 1.00 25.85 C ATOM 727 CD1 TYR A 130 -2.080 -1.967 7.490 1.00 29.98 C ATOM 728 CD2 TYR A 130 -4.259 -1.358 8.260 1.00 25.19 C ATOM 729 CE1 TYR A 130 -1.515 -1.011 8.346 1.00 30.02 C ATOM 730 CE2 TYR A 130 -3.709 -0.418 9.111 1.00 25.11 C ATOM 731 CZ TYR A 130 -2.338 -0.248 9.152 1.00 25.01 C ATOM 732 OH TYR A 130 -1.796 0.661 10.021 1.00 25.36 O ATOM 733 N ASN A 131 -5.844 -3.967 8.994 1.00 31.59 N ATOM 734 CA ASN A 131 -6.353 -3.677 10.325 1.00 31.67 C ATOM 735 C ASN A 131 -6.054 -4.845 11.253 1.00 34.62 C ATOM 736 O ASN A 131 -5.642 -4.653 12.397 1.00 37.36 O ATOM 737 CB ASN A 131 -7.870 -3.438 10.297 1.00 30.62 C ATOM 738 CG ASN A 131 -8.252 -2.020 9.868 1.00 30.49 C ATOM 739 OD1 ASN A 131 -9.428 -1.745 9.612 1.00 33.04 O ATOM 740 ND2 ASN A 131 -7.270 -1.117 9.797 1.00 25.60 N ATOM 741 N ILE A 132 -6.257 -6.059 10.751 1.00 36.90 N ATOM 742 CA ILE A 132 -6.026 -7.255 11.551 1.00 35.36 C ATOM 743 C ILE A 132 -4.564 -7.474 11.898 1.00 32.80 C ATOM 744 O ILE A 132 -4.225 -7.619 13.064 1.00 34.57 O ATOM 745 CB ILE A 132 -6.602 -8.513 10.850 1.00 34.25 C ATOM 746 CG1 ILE A 132 -8.126 -8.413 10.823 1.00 34.59 C ATOM 747 CG2 ILE A 132 -6.185 -9.782 11.596 1.00 31.71 C ATOM 748 CD1 ILE A 132 -8.802 -9.498 10.024 1.00 39.02 C ATOM 749 N LEU A 133 -3.699 -7.497 10.896 1.00 33.16 N ATOM 750 CA LEU A 133 -2.278 -7.686 11.156 1.00 34.35 C ATOM 751 C LEU A 133 -1.768 -6.598 12.093 1.00 35.27 C ATOM 752 O LEU A 133 -0.841 -6.804 12.869 1.00 34.98 O ATOM 753 CB LEU A 133 -1.484 -7.639 9.853 1.00 35.20 C ATOM 754 CG LEU A 133 -1.756 -8.755 8.852 1.00 39.80 C ATOM 755 CD1 LEU A 133 -0.683 -8.733 7.784 1.00 41.14 C ATOM 756 CD2 LEU A 133 -1.755 -10.091 9.556 1.00 41.85 C HETATM 757 N MSE A 134 -2.396 -5.435 12.005 1.00 34.11 N HETATM 758 CA MSE A 134 -2.036 -4.307 12.828 1.00 35.37 C HETATM 759 C MSE A 134 -2.553 -4.530 14.239 1.00 34.36 C HETATM 760 O MSE A 134 -1.827 -4.339 15.208 1.00 35.75 O HETATM 761 CB MSE A 134 -2.616 -3.029 12.205 1.00 34.13 C HETATM 762 CG MSE A 134 -2.232 -1.742 12.894 1.00 31.45 C HETATM 763 SE MSE A 134 -3.465 -1.372 14.319 1.00 46.90 HETATM 764 CE MSE A 134 -4.921 -0.613 13.246 1.00 39.46 C ATOM 765 N ALA A 135 -3.804 -4.958 14.362 1.00 34.66 N ATOM 766 CA ALA A 135 -4.382 -5.204 15.683 1.00 32.81 C ATOM 767 C ALA A 135 -3.598 -6.232 16.507 1.00 33.43 C ATOM 768 O ALA A 135 -3.534 -6.127 17.726 1.00 35.33 O ATOM 769 CB ALA A 135 -5.831 -5.639 15.548 1.00 28.18 C ATOM 770 N GLU A 136 -3.015 -7.233 15.859 1.00 34.91 N ATOM 771 CA GLU A 136 -2.245 -8.220 16.604 1.00 37.33 C ATOM 772 C GLU A 136 -0.770 -7.833 16.659 1.00 36.31 C ATOM 773 O GLU A 136 0.109 -8.668 16.902 1.00 35.38 O ATOM 774 CB GLU A 136 -2.439 -9.637 16.026 1.00 35.74 C ATOM 775 CG GLU A 136 -2.368 -9.780 14.530 1.00 40.25 C ATOM 776 CD GLU A 136 -3.005 -11.084 14.059 1.00 42.13 C ATOM 777 OE1 GLU A 136 -4.157 -11.374 14.475 1.00 37.73 O ATOM 778 OE2 GLU A 136 -2.359 -11.813 13.276 1.00 46.24 O ATOM 779 N GLY A 137 -0.528 -6.543 16.435 1.00 35.50 N ATOM 780 CA GLY A 137 0.807 -5.979 16.488 1.00 36.44 C ATOM 781 C GLY A 137 1.911 -6.520 15.602 1.00 38.61 C ATOM 782 O GLY A 137 3.046 -6.650 16.052 1.00 41.63 O ATOM 783 N ARG A 138 1.608 -6.836 14.350 1.00 40.13 N ATOM 784 CA ARG A 138 2.638 -7.326 13.440 1.00 40.63 C ATOM 785 C ARG A 138 3.243 -6.126 12.714 1.00 40.71 C ATOM 786 O ARG A 138 2.610 -5.075 12.621 1.00 42.15 O ATOM 787 CB ARG A 138 2.034 -8.288 12.417 1.00 41.78 C ATOM 788 CG ARG A 138 1.706 -9.682 12.944 1.00 46.33 C ATOM 789 CD ARG A 138 0.730 -10.386 11.998 1.00 60.56 C ATOM 790 NE ARG A 138 1.085 -11.780 11.723 1.00 70.18 N ATOM 791 CZ ARG A 138 1.774 -12.191 10.660 1.00 68.88 C ATOM 792 NH1 ARG A 138 2.194 -11.321 9.754 1.00 68.53 N ATOM 793 NH2 ARG A 138 2.040 -13.482 10.497 1.00 78.68 N ATOM 794 N ARG A 139 4.467 -6.270 12.213 1.00 40.39 N ATOM 795 CA ARG A 139 5.113 -5.180 11.479 1.00 40.39 C ATOM 796 C ARG A 139 4.603 -5.236 10.034 1.00 41.71 C ATOM 797 O ARG A 139 5.169 -5.919 9.180 1.00 41.11 O ATOM 798 CB ARG A 139 6.638 -5.333 11.523 1.00 39.66 C ATOM 799 N VAL A 140 3.543 -4.482 9.764 1.00 41.42 N ATOM 800 CA VAL A 140 2.908 -4.501 8.458 1.00 40.43 C ATOM 801 C VAL A 140 2.789 -3.160 7.726 1.00 40.98 C ATOM 802 O VAL A 140 2.580 -2.124 8.346 1.00 42.91 O ATOM 803 CB VAL A 140 1.487 -5.086 8.616 1.00 40.78 C ATOM 804 CG1 VAL A 140 0.644 -4.145 9.480 1.00 36.77 C ATOM 805 CG2 VAL A 140 0.842 -5.311 7.250 1.00 41.30 C ATOM 806 N VAL A 141 2.935 -3.192 6.404 1.00 39.58 N ATOM 807 CA VAL A 141 2.768 -1.996 5.574 1.00 35.34 C ATOM 808 C VAL A 141 1.690 -2.373 4.568 1.00 32.75 C ATOM 809 O VAL A 141 1.567 -3.539 4.194 1.00 31.18 O ATOM 810 CB VAL A 141 4.031 -1.616 4.741 1.00 33.61 C ATOM 811 CG1 VAL A 141 3.724 -0.399 3.888 1.00 32.39 C ATOM 812 CG2 VAL A 141 5.204 -1.319 5.637 1.00 37.20 C ATOM 813 N VAL A 142 0.904 -1.401 4.138 1.00 30.87 N ATOM 814 CA VAL A 142 -0.116 -1.676 3.148 1.00 30.04 C ATOM 815 C VAL A 142 -0.116 -0.612 2.050 1.00 32.29 C ATOM 816 O VAL A 142 0.049 0.575 2.310 1.00 32.15 O ATOM 817 CB VAL A 142 -1.528 -1.761 3.780 1.00 30.45 C ATOM 818 CG1 VAL A 142 -1.950 -0.398 4.321 1.00 31.10 C ATOM 819 CG2 VAL A 142 -2.531 -2.265 2.745 1.00 26.35 C ATOM 820 N ALA A 143 -0.280 -1.079 0.817 1.00 35.15 N ATOM 821 CA ALA A 143 -0.343 -0.237 -0.372 1.00 33.29 C ATOM 822 C ALA A 143 -1.703 -0.558 -0.988 1.00 33.36 C ATOM 823 O ALA A 143 -2.015 -1.727 -1.213 1.00 33.14 O ATOM 824 CB ALA A 143 0.774 -0.604 -1.331 1.00 32.52 C ATOM 825 N LEU A 144 -2.499 0.475 -1.263 1.00 34.13 N ATOM 826 CA LEU A 144 -3.847 0.302 -1.807 1.00 33.37 C ATOM 827 C LEU A 144 -4.224 1.195 -2.986 1.00 35.19 C ATOM 828 O LEU A 144 -4.043 2.417 -2.937 1.00 34.88 O ATOM 829 CB LEU A 144 -4.882 0.568 -0.716 1.00 30.74 C ATOM 830 CG LEU A 144 -4.735 -0.057 0.670 1.00 34.10 C ATOM 831 CD1 LEU A 144 -5.349 0.894 1.695 1.00 34.46 C ATOM 832 CD2 LEU A 144 -5.394 -1.429 0.720 1.00 34.42 C ATOM 833 N LEU A 145 -4.778 0.572 -4.025 1.00 38.35 N ATOM 834 CA LEU A 145 -5.275 1.268 -5.210 1.00 40.25 C ATOM 835 C LEU A 145 -6.778 1.268 -4.934 1.00 40.79 C ATOM 836 O LEU A 145 -7.381 0.215 -4.808 1.00 38.98 O ATOM 837 CB LEU A 145 -4.984 0.454 -6.477 1.00 43.07 C ATOM 838 CG LEU A 145 -3.519 0.164 -6.836 1.00 45.93 C ATOM 839 CD1 LEU A 145 -3.448 -1.082 -7.711 1.00 41.56 C ATOM 840 CD2 LEU A 145 -2.892 1.372 -7.542 1.00 48.91 C ATOM 841 N PRO A 146 -7.405 2.446 -4.856 1.00 45.45 N ATOM 842 CA PRO A 146 -8.843 2.503 -4.574 1.00 49.01 C ATOM 843 C PRO A 146 -9.742 2.091 -5.729 1.00 52.81 C ATOM 844 O PRO A 146 -9.259 1.711 -6.797 1.00 51.57 O ATOM 845 CB PRO A 146 -9.045 3.953 -4.166 1.00 49.08 C ATOM 846 CG PRO A 146 -8.114 4.677 -5.128 1.00 51.83 C ATOM 847 CD PRO A 146 -6.897 3.760 -5.299 1.00 47.47 C ATOM 848 N ASP A 147 -11.054 2.172 -5.508 1.00 58.26 N ATOM 849 CA ASP A 147 -12.016 1.798 -6.537 1.00 60.85 C ATOM 850 C ASP A 147 -11.638 0.402 -7.009 1.00 61.12 C ATOM 851 O ASP A 147 -11.144 -0.372 -6.162 1.00 60.50 O ATOM 852 CB ASP A 147 -11.961 2.784 -7.699 1.00 59.37 C HETATM 853 O HOH A 201 -4.332 3.555 17.575 1.00 38.47 O HETATM 854 O HOH A 202 1.179 -6.519 -13.073 1.00 35.71 O HETATM 855 O HOH A 203 12.040 2.806 8.274 1.00 42.33 O HETATM 856 O HOH A 204 3.177 5.202 7.457 1.00 32.40 O HETATM 857 O HOH A 205 4.665 1.335 12.567 1.00 40.14 O HETATM 858 O HOH A 206 -1.284 9.232 10.409 1.00 44.38 O HETATM 859 O HOH A 207 16.697 -6.331 9.575 1.00 60.76 O HETATM 860 O HOH A 208 -18.722 -1.932 4.689 1.00 54.36 O HETATM 861 O HOH A 209 -6.956 9.118 -8.357 1.00 65.84 O HETATM 862 O HOH A 210 -7.642 11.218 -2.642 1.00 42.18 O HETATM 863 O HOH A 211 -8.712 -10.917 -3.782 1.00 38.78 O HETATM 864 O HOH A 212 1.190 2.961 20.036 1.00 37.79 O HETATM 865 O HOH A 213 -4.980 -12.486 -3.606 1.00 47.01 O HETATM 866 O HOH A 214 -19.021 1.903 -9.781 1.00 53.16 O HETATM 867 O HOH A 215 -19.684 3.785 0.257 1.00 63.12 O HETATM 868 O HOH A 216 -15.677 -0.879 13.585 1.00 55.07 O HETATM 869 O HOH A 217 -4.184 -2.846 -14.834 1.00 40.00 O HETATM 870 O HOH A 218 0.722 6.957 13.363 1.00 40.18 O HETATM 871 O HOH A 219 -22.460 -4.476 0.938 1.00 59.13 O HETATM 872 O HOH A 220 3.138 10.920 11.123 1.00 50.43 O HETATM 873 O HOH A 221 -8.670 -4.959 -9.931 1.00 46.23 O HETATM 874 O HOH A 222 -17.513 0.689 5.900 1.00 50.15 O HETATM 875 O HOH A 223 9.340 -10.380 9.923 1.00 50.01 O HETATM 876 O HOH A 224 -13.716 -2.562 11.961 1.00 54.52 O HETATM 877 O HOH A 225 -12.873 -1.362 -4.422 1.00 53.75 O HETATM 878 O HOH A 226 27.041 -5.502 17.296 1.00 58.24 O HETATM 879 O HOH A 227 13.378 -1.881 11.230 1.00 53.90 O HETATM 880 O HOH A 228 9.811 10.556 25.858 1.00 57.49 O HETATM 881 O HOH A 229 18.321 -11.517 -20.009 1.00 46.95 O HETATM 882 O HOH A 230 24.594 -7.472 14.220 1.00 55.51 O HETATM 883 O HOH A 231 7.736 -10.453 -13.722 1.00 45.18 O HETATM 884 O HOH A 232 -0.988 13.751 -7.734 1.00 54.55 O HETATM 885 O HOH A 233 -10.348 -1.951 -9.850 1.00 43.40 O HETATM 886 O HOH A 234 1.789 9.967 -5.979 1.00 68.92 O HETATM 887 O HOH A 235 14.120 1.549 11.739 1.00 65.18 O HETATM 888 O HOH A 236 -2.608 13.924 -2.049 1.00 46.69 O HETATM 889 O HOH A 237 -4.870 13.634 -0.568 1.00 51.40 O HETATM 890 O HOH A 238 5.782 6.476 -10.586 1.00 46.46 O HETATM 891 O HOH A 239 4.763 4.364 3.631 1.00 45.68 O HETATM 892 O HOH A 240 -10.081 7.542 -11.392 1.00 56.97 O HETATM 893 O HOH A 241 18.088 0.833 -6.731 1.00 63.57 O HETATM 894 O HOH A 242 -20.697 2.004 -0.912 1.00 63.68 O HETATM 895 O HOH A 243 -20.592 -2.301 -4.074 1.00 76.44 O HETATM 896 O HOH A 244 -18.884 -1.295 -5.323 1.00 51.56 O TER 897 HOH A 244 ENDMDL MASTER END