HEADER HYDROLASE 17-SEP-08 3EIY TITLE CRYSTAL STRUCTURE OF INORGANIC PYROPHOSPHATASE FROM BURKHOLDERIA TITLE 2 PSEUDOMALLEI WITH BOUND PYROPHOSPHATE COMPND MOL_ID: 1; COMPND 2 MOLECULE: INORGANIC PYROPHOSPHATASE; COMPND 3 CHAIN: A; COMPND 4 EC: 3.6.1.1; COMPND 5 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: BURKHOLDERIA PSEUDOMALLEI 1710B; SOURCE 3 ORGANISM_TAXID: 320372; SOURCE 4 GENE: PPA, BURPS1710B_1237; SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3); SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 9 EXPRESSION_SYSTEM_PLASMID: AVA0421 KEYWDS STRUCTURAL GENOMICS, SSGCID, PYROPHOSPHATASE, HYDROLASE, KEYWDS 2 BUPSA.00023.A, SEATTLE STRUCTURAL GENOMICS CENTER FOR INFECTIOUS KEYWDS 3 DISEASE' EXPDTA X-RAY DIFFRACTION AUTHOR SEATTLE STRUCTURAL GENOMICS CENTER FOR INFECTIOUS DISEASE (SSGCID) REVDAT 4 23-OCT-13 3EIY 1 REMARK REVDAT 3 05-OCT-11 3EIY 1 JRNL VERSN REVDAT 2 24-FEB-09 3EIY 1 VERSN REVDAT 1 30-SEP-08 3EIY 0 JRNL AUTH W.C.VAN VOORHIS,W.G.HOL,P.J.MYLER,L.J.STEWART JRNL TITL THE ROLE OF MEDICAL STRUCTURAL GENOMICS IN DISCOVERING NEW JRNL TITL 2 DRUGS FOR INFECTIOUS DISEASES. JRNL REF PLOS COMPUT BIOL V. 5 00530 2009 JRNL REFN JRNL PMID 19855826 JRNL DOI 10.1371/JOURNAL.PCBI.1000530 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH L.BAUGH,L.A.GALLAGHER,R.PATRAPUVICH,M.C.CLIFTON, REMARK 1 AUTH 2 A.S.GARDBERG,T.E.EDWARDS,B.ARMOUR,D.W.BEGLEY,S.H.DIETERICH, REMARK 1 AUTH 3 D.M.DRANOW,J.ABENDROTH,J.W.FAIRMAN,D.FOX,B.L.STAKER,I.PHAN, REMARK 1 AUTH 4 A.GILLESPIE,R.CHOI,S.NAKAZAWA-HEWITT,M.T.NGUYEN,A.NAPULI, REMARK 1 AUTH 5 L.BARRETT,G.W.BUCHKO,R.STACY,P.J.MYLER,L.J.STEWART,C.MANOIL, REMARK 1 AUTH 6 W.C.VAN VOORHIS REMARK 1 TITL COMBINING FUNCTIONAL AND STRUCTURAL GENOMICS TO SAMPLE THE REMARK 1 TITL 2 ESSENTIAL BURKHOLDERIA STRUCTOME. REMARK 1 REF PLOS ONE V. 8 53851 2013 REMARK 1 REFN ESSN 1932-6203 REMARK 1 PMID 23382856 REMARK 1 DOI 10.1371/JOURNAL.PONE.0053851 REMARK 2 REMARK 2 RESOLUTION. 2.10 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC 5.4.0067 REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON REMARK 3 REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000 REMARK 3 COMPLETENESS FOR RANGE (%) : NULL REMARK 3 NUMBER OF REFLECTIONS : 19547 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM REMARK 3 R VALUE (WORKING + TEST SET) : 0.213 REMARK 3 R VALUE (WORKING SET) : 0.211 REMARK 3 FREE R VALUE : 0.249 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100 REMARK 3 FREE R VALUE TEST SET COUNT : 991 REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : 20 REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.10 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.15 REMARK 3 REFLECTION IN BIN (WORKING SET) : 1250 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 90.60 REMARK 3 BIN R VALUE (WORKING SET) : 0.3090 REMARK 3 BIN FREE R VALUE SET COUNT : 71 REMARK 3 BIN FREE R VALUE : 0.4070 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 1330 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 39 REMARK 3 SOLVENT ATOMS : 112 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 30.12 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 0.80000 REMARK 3 B22 (A**2) : 0.80000 REMARK 3 B33 (A**2) : -1.21000 REMARK 3 B12 (A**2) : 0.40000 REMARK 3 B13 (A**2) : 0.00000 REMARK 3 B23 (A**2) : 0.00000 REMARK 3 REMARK 3 ESTIMATED OVERALL COORDINATE ERROR. REMARK 3 ESU BASED ON R VALUE (A): 0.156 REMARK 3 ESU BASED ON FREE R VALUE (A): 0.152 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.110 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.164 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.948 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.929 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1393 ; 0.015 ; 0.022 REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 1886 ; 1.460 ; 1.994 REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 173 ; 5.857 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 56 ;32.570 ;25.357 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 222 ;15.203 ;15.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 4 ;18.890 ;15.000 REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 209 ; 0.092 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1034 ; 0.007 ; 0.021 REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL REMARK 3 REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 870 ; 0.890 ; 1.500 REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1408 ; 1.604 ; 2.000 REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 523 ; 2.198 ; 3.000 REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 478 ; 3.551 ; 4.500 REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 REMARK 3 NCS RESTRAINTS STATISTICS REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : NULL REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : MASK REMARK 3 PARAMETERS FOR MASK CALCULATION REMARK 3 VDW PROBE RADIUS : 1.20 REMARK 3 ION PROBE RADIUS : 0.80 REMARK 3 SHRINKAGE RADIUS : 0.80 REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING REMARK 3 POSITIONS REMARK 4 REMARK 4 3EIY COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 18-SEP-08. REMARK 100 THE RCSB ID CODE IS RCSB049380. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 04-SEP-08 REMARK 200 TEMPERATURE (KELVIN) : 100.0 REMARK 200 PH : 6.30 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : N REMARK 200 RADIATION SOURCE : ROTATING ANODE REMARK 200 BEAMLINE : NULL REMARK 200 X-RAY GENERATOR MODEL : RIGAKU MICROMAX-007 HF REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : RIGAKU SATURN 944 REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000 REMARK 200 DATA SCALING SOFTWARE : HKL-2000 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 19792 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100 REMARK 200 RESOLUTION RANGE LOW (A) : 50.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 98.7 REMARK 200 DATA REDUNDANCY : 3.600 REMARK 200 R MERGE (I) : 0.10300 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 8.9000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.18 REMARK 200 COMPLETENESS FOR SHELL (%) : 98.5 REMARK 200 DATA REDUNDANCY IN SHELL : 2.70 REMARK 200 R MERGE FOR SHELL (I) : 0.66900 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : NULL REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: MOLREP REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 67.71 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.81 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM NA/K PHOSPHATE, PH 6.3, 49.5% REMARK 280 PEG 200. CRYSTAL 3 MONTHS OLD., PH 6.30, VAPOR DIFFUSION, SITTING REMARK 280 DROP, TEMPERATURE 289K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 63 2 2 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -Y,X-Y,Z REMARK 290 3555 -X+Y,-X,Z REMARK 290 4555 -X,-Y,Z+1/2 REMARK 290 5555 Y,-X+Y,Z+1/2 REMARK 290 6555 X-Y,X,Z+1/2 REMARK 290 7555 Y,X,-Z REMARK 290 8555 X-Y,-Y,-Z REMARK 290 9555 -X,-X+Y,-Z REMARK 290 10555 -Y,-X,-Z+1/2 REMARK 290 11555 -X+Y,Y,-Z+1/2 REMARK 290 12555 X,X-Y,-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 -0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000 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 55.61650 REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000 REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 55.61650 REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000 REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 55.61650 REMARK 290 SMTRY1 7 -0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 7 0.866025 0.500000 0.000000 0.00000 REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 9 -0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 9 -0.866025 0.500000 0.000000 0.00000 REMARK 290 SMTRY3 9 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 10 0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 10 -0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 55.61650 REMARK 290 SMTRY1 11 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 11 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 55.61650 REMARK 290 SMTRY1 12 0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 12 0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 55.61650 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1, 2, 3 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 20130 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 37680 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -208.0 KCAL/MOL 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 -0.500000 -0.866025 0.000000 50.47600 REMARK 350 BIOMT2 2 0.866025 -0.500000 0.000000 87.42700 REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000 REMARK 350 BIOMT1 3 -0.500000 0.866025 0.000000 -50.47600 REMARK 350 BIOMT2 3 -0.866025 -0.500000 0.000000 87.42700 REMARK 350 BIOMT3 3 0.000000 0.000000 1.000000 0.00000 REMARK 350 BIOMT1 4 0.500000 -0.866025 0.000000 50.47600 REMARK 350 BIOMT2 4 -0.866025 -0.500000 0.000000 87.42700 REMARK 350 BIOMT3 4 0.000000 0.000000 -1.000000 55.61650 REMARK 350 BIOMT1 5 -1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 5 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 5 0.000000 0.000000 -1.000000 55.61650 REMARK 350 BIOMT1 6 0.500000 0.866025 0.000000 -50.47600 REMARK 350 BIOMT2 6 0.866025 -0.500000 0.000000 87.42700 REMARK 350 BIOMT3 6 0.000000 0.000000 -1.000000 55.61650 REMARK 350 REMARK 350 BIOMOLECULE: 2 REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 7740 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 21160 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -92.0 KCAL/MOL 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 -0.500000 -0.866025 0.000000 50.47600 REMARK 350 BIOMT2 2 0.866025 -0.500000 0.000000 87.42700 REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000 REMARK 350 BIOMT1 3 -0.500000 0.866025 0.000000 -50.47600 REMARK 350 BIOMT2 3 -0.866025 -0.500000 0.000000 87.42700 REMARK 350 BIOMT3 3 0.000000 0.000000 1.000000 0.00000 REMARK 350 REMARK 350 BIOMOLECULE: 3 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC 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 375 REMARK 375 SPECIAL POSITION REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL REMARK 375 POSITIONS. REMARK 375 REMARK 375 ATOM RES CSSEQI REMARK 375 K K A 176 LIES ON A SPECIAL POSITION. 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 MET A -20 REMARK 465 ALA A -19 REMARK 465 HIS A -18 REMARK 465 HIS A -17 REMARK 465 HIS A -16 REMARK 465 HIS A -15 REMARK 465 HIS A -14 REMARK 465 HIS A -13 REMARK 465 MET A -12 REMARK 465 GLY A -11 REMARK 465 THR A -10 REMARK 465 LEU A -9 REMARK 465 GLU A -8 REMARK 465 ALA A -7 REMARK 465 GLN A -6 REMARK 465 THR A -5 REMARK 465 GLN A -4 REMARK 465 GLY A -3 REMARK 465 PRO A -2 REMARK 465 GLY A -1 REMARK 465 SER A 0 REMARK 465 MET A 1 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 LYS A 113 CG CD CE NZ REMARK 470 LYS A 147 CG CD CE NZ REMARK 470 LYS A 152 CG CD CE NZ 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 238 O HOH A 281 2.06 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 11 81.33 -159.79 REMARK 500 ASP A 98 -168.63 -122.40 REMARK 500 REMARK 500 REMARK: NULL REMARK 620 REMARK 620 METAL COORDINATION REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE): REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 K A 176 K REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ASP A 11 OD1 REMARK 620 2 LEU A 12 O 92.8 REMARK 620 3 GLN A 14 OE1 100.9 87.2 REMARK 620 N 1 2 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 NA A 178 NA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ASP A 71 OD2 REMARK 620 2 ASP A 103 OD1 94.9 REMARK 620 3 ALA A 104 O 102.5 85.4 REMARK 620 4 HOH A 247 O 169.6 95.4 79.9 REMARK 620 5 HOH A 245 O 72.2 146.6 127.0 98.2 REMARK 620 6 HOH A 263 O 85.2 155.0 70.3 86.0 56.8 REMARK 620 N 1 2 3 4 5 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 NA A 177 NA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ASP A 98 OD2 REMARK 620 2 ASP A 103 OD2 91.4 REMARK 620 3 POP A 179 O6 93.1 172.2 REMARK 620 4 HOH A 257 O 78.3 74.9 112.2 REMARK 620 5 POP A 179 O3 165.9 100.0 76.6 96.5 REMARK 620 6 HOH A 201 O 89.4 88.0 85.7 158.6 99.2 REMARK 620 N 1 2 3 4 5 REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K A 176 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 177 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 178 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE POP A 179 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PG4 A 180 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A 181 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A 182 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: BUPSA.00023.A RELATED DB: TARGETDB REMARK 900 RELATED ID: 3D63 RELATED DB: PDB REMARK 900 THE SAME PROTEIN, "OPEN" CONFORMATION, APO FORM, IN SPACE REMARK 900 GROUP P21212 REMARK 900 RELATED ID: 3EIZ RELATED DB: PDB REMARK 900 RELATED ID: 3EJ0 RELATED DB: PDB REMARK 900 RELATED ID: 3EJ2 RELATED DB: PDB DBREF 3EIY A 1 175 UNP Q3JUV5 Q3JUV5_BURP1 1 175 SEQADV 3EIY MET A -20 UNP Q3JUV5 EXPRESSION TAG SEQADV 3EIY ALA A -19 UNP Q3JUV5 EXPRESSION TAG SEQADV 3EIY HIS A -18 UNP Q3JUV5 EXPRESSION TAG SEQADV 3EIY HIS A -17 UNP Q3JUV5 EXPRESSION TAG SEQADV 3EIY HIS A -16 UNP Q3JUV5 EXPRESSION TAG SEQADV 3EIY HIS A -15 UNP Q3JUV5 EXPRESSION TAG SEQADV 3EIY HIS A -14 UNP Q3JUV5 EXPRESSION TAG SEQADV 3EIY HIS A -13 UNP Q3JUV5 EXPRESSION TAG SEQADV 3EIY MET A -12 UNP Q3JUV5 EXPRESSION TAG SEQADV 3EIY GLY A -11 UNP Q3JUV5 EXPRESSION TAG SEQADV 3EIY THR A -10 UNP Q3JUV5 EXPRESSION TAG SEQADV 3EIY LEU A -9 UNP Q3JUV5 EXPRESSION TAG SEQADV 3EIY GLU A -8 UNP Q3JUV5 EXPRESSION TAG SEQADV 3EIY ALA A -7 UNP Q3JUV5 EXPRESSION TAG SEQADV 3EIY GLN A -6 UNP Q3JUV5 EXPRESSION TAG SEQADV 3EIY THR A -5 UNP Q3JUV5 EXPRESSION TAG SEQADV 3EIY GLN A -4 UNP Q3JUV5 EXPRESSION TAG SEQADV 3EIY GLY A -3 UNP Q3JUV5 EXPRESSION TAG SEQADV 3EIY PRO A -2 UNP Q3JUV5 EXPRESSION TAG SEQADV 3EIY GLY A -1 UNP Q3JUV5 EXPRESSION TAG SEQADV 3EIY SER A 0 UNP Q3JUV5 EXPRESSION TAG SEQRES 1 A 196 MET ALA HIS HIS HIS HIS HIS HIS MET GLY THR LEU GLU SEQRES 2 A 196 ALA GLN THR GLN GLY PRO GLY SER MET SER PHE SER ASN SEQRES 3 A 196 VAL PRO ALA GLY LYS ASP LEU PRO GLN ASP PHE ASN VAL SEQRES 4 A 196 ILE ILE GLU ILE PRO ALA GLN SER GLU PRO VAL LYS TYR SEQRES 5 A 196 GLU ALA ASP LYS ALA LEU GLY LEU LEU VAL VAL ASP ARG SEQRES 6 A 196 PHE ILE GLY THR GLY MET ARG TYR PRO VAL ASN TYR GLY SEQRES 7 A 196 PHE ILE PRO GLN THR LEU SER GLY ASP GLY ASP PRO VAL SEQRES 8 A 196 ASP VAL LEU VAL ILE THR PRO PHE PRO LEU LEU ALA GLY SEQRES 9 A 196 SER VAL VAL ARG ALA ARG ALA LEU GLY MET LEU LYS MET SEQRES 10 A 196 THR ASP GLU SER GLY VAL ASP ALA LYS LEU VAL ALA VAL SEQRES 11 A 196 PRO HIS ASP LYS VAL CYS PRO MET THR ALA ASN LEU LYS SEQRES 12 A 196 SER ILE ASP ASP VAL PRO ALA TYR LEU LYS ASP GLN ILE SEQRES 13 A 196 LYS HIS PHE PHE GLU GLN TYR LYS ALA LEU GLU LYS GLY SEQRES 14 A 196 LYS TRP VAL LYS VAL GLU GLY TRP ASP GLY ILE ASP ALA SEQRES 15 A 196 ALA HIS LYS GLU ILE THR ASP GLY VAL ALA ASN PHE LYS SEQRES 16 A 196 LYS HET K A 176 1 HET NA A 177 1 HET NA A 178 1 HET POP A 179 9 HET PG4 A 180 13 HET PEG A 181 7 HET PEG A 182 7 HETNAM K POTASSIUM ION HETNAM NA SODIUM ION HETNAM POP PYROPHOSPHATE 2- HETNAM PG4 TETRAETHYLENE GLYCOL HETNAM PEG DI(HYDROXYETHYL)ETHER FORMUL 2 K K 1+ FORMUL 3 NA 2(NA 1+) FORMUL 5 POP H2 O7 P2 2- FORMUL 6 PG4 C8 H18 O5 FORMUL 7 PEG 2(C4 H10 O3) FORMUL 9 HOH *112(H2 O) HELIX 1 1 SER A 2 VAL A 6 5 5 HELIX 2 2 CYS A 115 ALA A 119 5 5 HELIX 3 3 SER A 123 VAL A 127 5 5 HELIX 4 4 PRO A 128 TYR A 142 1 15 HELIX 5 5 GLY A 158 LYS A 175 1 18 SHEET 1 A 7 VAL A 151 ASP A 157 0 SHEET 2 A 7 VAL A 85 ASP A 98 -1 N LYS A 95 O GLY A 155 SHEET 3 A 7 GLY A 101 PRO A 110 -1 O LYS A 105 N LEU A 94 SHEET 4 A 7 VAL A 70 VAL A 74 1 N LEU A 73 O ALA A 108 SHEET 5 A 7 ASN A 55 ILE A 59 -1 N GLY A 57 O VAL A 72 SHEET 6 A 7 PHE A 16 ILE A 22 -1 N ILE A 19 O PHE A 58 SHEET 7 A 7 VAL A 85 ASP A 98 -1 O ALA A 88 N PHE A 16 SHEET 1 B 2 VAL A 29 ASP A 34 0 SHEET 2 B 2 LEU A 39 PHE A 45 -1 O LEU A 39 N ASP A 34 LINK OD1 ASP A 11 K K A 176 1555 1555 2.73 LINK O LEU A 12 K K A 176 1555 1555 2.65 LINK OE1 GLN A 14 K K A 176 1555 1555 2.92 LINK OD2 ASP A 71 NA NA A 178 1555 1555 2.81 LINK OD2 ASP A 98 NA NA A 177 1555 1555 2.65 LINK OD1 ASP A 103 NA NA A 178 1555 1555 2.53 LINK OD2 ASP A 103 NA NA A 177 1555 1555 2.58 LINK O ALA A 104 NA NA A 178 1555 1555 2.92 LINK NA NA A 177 O6 POP A 179 1555 1555 2.56 LINK NA NA A 177 O HOH A 257 1555 1555 2.65 LINK NA NA A 177 O3 POP A 179 1555 1555 2.20 LINK NA NA A 177 O HOH A 201 1555 1555 2.50 LINK NA NA A 178 O HOH A 247 1555 1555 2.86 LINK NA NA A 178 O HOH A 245 1555 1555 2.66 LINK NA NA A 178 O HOH A 263 1555 1555 2.50 CISPEP 1 LEU A 12 PRO A 13 0 -0.44 SITE 1 AC1 3 ASP A 11 LEU A 12 GLN A 14 SITE 1 AC2 6 ASP A 98 ASP A 103 LYS A 143 POP A 179 SITE 2 AC2 6 HOH A 201 HOH A 257 SITE 1 AC3 7 ASP A 66 ASP A 71 ASP A 103 ALA A 104 SITE 2 AC3 7 HOH A 245 HOH A 247 HOH A 263 SITE 1 AC4 14 LYS A 30 ARG A 44 TYR A 56 ASP A 103 SITE 2 AC4 14 LYS A 105 TYR A 142 LYS A 143 NA A 177 SITE 3 AC4 14 HOH A 200 HOH A 221 HOH A 238 HOH A 239 SITE 4 AC4 14 HOH A 260 HOH A 267 SITE 1 AC5 7 GLY A 9 LYS A 10 ASP A 11 LEU A 12 SITE 2 AC5 7 GLN A 14 ASP A 160 HIS A 163 SITE 1 AC6 4 LYS A 136 VAL A 153 GLU A 154 TRP A 156 SITE 1 AC7 3 ARG A 87 LYS A 113 VAL A 114 CRYST1 100.952 100.952 111.233 90.00 90.00 120.00 P 63 2 2 12 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 0.009906 0.005719 0.000000 0.00000 SCALE2 0.000000 0.011438 0.000000 0.00000 SCALE3 0.000000 0.000000 0.008990 0.00000 ATOM 1 N SER A 2 2.527 54.656 -1.667 1.00 52.73 N ATOM 2 CA SER A 2 3.259 54.783 -0.368 1.00 52.54 C ATOM 3 C SER A 2 4.127 53.553 -0.105 1.00 52.03 C ATOM 4 O SER A 2 5.274 53.451 -0.594 1.00 52.45 O ATOM 5 CB SER A 2 2.273 54.944 0.792 1.00 52.69 C ATOM 6 OG SER A 2 2.066 56.306 1.121 1.00 54.37 O ATOM 7 N PHE A 3 3.563 52.626 0.674 1.00 50.61 N ATOM 8 CA PHE A 3 4.261 51.413 1.102 1.00 48.73 C ATOM 9 C PHE A 3 4.881 50.670 -0.064 1.00 48.17 C ATOM 10 O PHE A 3 6.035 50.257 0.019 1.00 47.56 O ATOM 11 CB PHE A 3 3.342 50.479 1.896 1.00 47.95 C ATOM 12 CG PHE A 3 2.747 51.112 3.120 1.00 46.23 C ATOM 13 CD1 PHE A 3 3.425 52.100 3.804 1.00 43.75 C ATOM 14 CD2 PHE A 3 1.509 50.701 3.594 1.00 45.77 C ATOM 15 CE1 PHE A 3 2.893 52.679 4.942 1.00 44.62 C ATOM 16 CE2 PHE A 3 0.955 51.280 4.728 1.00 45.65 C ATOM 17 CZ PHE A 3 1.655 52.273 5.409 1.00 45.91 C ATOM 18 N SER A 4 4.122 50.518 -1.151 1.00 47.69 N ATOM 19 CA SER A 4 4.593 49.745 -2.323 1.00 47.00 C ATOM 20 C SER A 4 5.896 50.254 -2.977 1.00 45.29 C ATOM 21 O SER A 4 6.627 49.479 -3.592 1.00 45.34 O ATOM 22 CB SER A 4 3.489 49.633 -3.387 1.00 47.47 C ATOM 23 OG SER A 4 3.169 50.916 -3.908 1.00 49.92 O ATOM 24 N ASN A 5 6.184 51.544 -2.832 1.00 43.32 N ATOM 25 CA ASN A 5 7.351 52.145 -3.480 1.00 41.42 C ATOM 26 C ASN A 5 8.584 52.307 -2.574 1.00 39.00 C ATOM 27 O ASN A 5 9.629 52.802 -3.000 1.00 38.69 O ATOM 28 CB ASN A 5 6.958 53.491 -4.094 1.00 42.02 C ATOM 29 CG ASN A 5 6.108 53.321 -5.366 1.00 45.67 C ATOM 30 OD1 ASN A 5 4.862 53.286 -5.312 1.00 48.48 O ATOM 31 ND2 ASN A 5 6.784 53.176 -6.513 1.00 47.35 N ATOM 32 N VAL A 6 8.466 51.922 -1.312 1.00 35.70 N ATOM 33 CA VAL A 6 9.636 51.959 -0.457 1.00 32.41 C ATOM 34 C VAL A 6 10.595 50.807 -0.862 1.00 30.30 C ATOM 35 O VAL A 6 10.176 49.658 -0.964 1.00 29.28 O ATOM 36 CB VAL A 6 9.242 51.846 1.038 1.00 32.26 C ATOM 37 CG1 VAL A 6 10.476 51.902 1.905 1.00 30.72 C ATOM 38 CG2 VAL A 6 8.257 52.934 1.415 1.00 30.80 C ATOM 39 N PRO A 7 11.890 51.109 -1.064 1.00 28.73 N ATOM 40 CA PRO A 7 12.827 50.031 -1.447 1.00 27.85 C ATOM 41 C PRO A 7 12.952 49.030 -0.321 1.00 26.92 C ATOM 42 O PRO A 7 12.827 49.397 0.859 1.00 26.32 O ATOM 43 CB PRO A 7 14.159 50.763 -1.644 1.00 27.56 C ATOM 44 CG PRO A 7 13.784 52.193 -1.869 1.00 28.99 C ATOM 45 CD PRO A 7 12.550 52.421 -1.016 1.00 28.59 C ATOM 46 N ALA A 8 13.208 47.777 -0.660 1.00 26.04 N ATOM 47 CA ALA A 8 13.463 46.785 0.378 1.00 25.67 C ATOM 48 C ALA A 8 14.702 47.145 1.205 1.00 25.55 C ATOM 49 O ALA A 8 14.786 46.804 2.395 1.00 25.75 O ATOM 50 CB ALA A 8 13.588 45.395 -0.224 1.00 25.25 C ATOM 51 N GLY A 9 15.668 47.834 0.598 1.00 25.34 N ATOM 52 CA GLY A 9 16.864 48.237 1.344 1.00 25.46 C ATOM 53 C GLY A 9 17.905 48.951 0.506 1.00 26.30 C ATOM 54 O GLY A 9 17.865 48.854 -0.717 1.00 26.99 O ATOM 55 N LYS A 10 18.834 49.654 1.159 1.00 26.15 N ATOM 56 CA LYS A 10 19.941 50.322 0.477 1.00 27.63 C ATOM 57 C LYS A 10 21.104 49.348 0.102 1.00 27.17 C ATOM 58 O LYS A 10 21.920 49.640 -0.769 1.00 28.04 O ATOM 59 CB LYS A 10 20.522 51.442 1.352 1.00 27.27 C ATOM 60 CG LYS A 10 19.619 52.654 1.569 1.00 32.65 C ATOM 61 CD LYS A 10 20.334 53.690 2.451 1.00 38.46 C ATOM 62 CE LYS A 10 19.720 55.094 2.319 1.00 42.10 C ATOM 63 NZ LYS A 10 18.235 55.016 2.421 1.00 42.82 N ATOM 64 N ASP A 11 21.204 48.221 0.782 1.00 26.40 N ATOM 65 CA ASP A 11 22.265 47.261 0.452 1.00 25.76 C ATOM 66 C ASP A 11 21.901 45.893 0.979 1.00 24.71 C ATOM 67 O ASP A 11 22.369 45.488 2.037 1.00 25.14 O ATOM 68 CB ASP A 11 23.639 47.723 0.995 1.00 25.24 C ATOM 69 CG ASP A 11 24.809 47.007 0.321 1.00 26.43 C ATOM 70 OD1 ASP A 11 24.583 45.956 -0.326 1.00 25.79 O ATOM 71 OD2 ASP A 11 25.973 47.447 0.460 1.00 27.48 O ATOM 72 N LEU A 12 21.065 45.188 0.225 1.00 24.00 N ATOM 73 CA LEU A 12 20.522 43.892 0.629 1.00 24.17 C ATOM 74 C LEU A 12 21.527 42.731 0.574 1.00 24.26 C ATOM 75 O LEU A 12 22.415 42.717 -0.279 1.00 23.90 O ATOM 76 CB LEU A 12 19.327 43.549 -0.255 1.00 23.47 C ATOM 77 CG LEU A 12 18.183 44.559 -0.124 1.00 24.51 C ATOM 78 CD1 LEU A 12 17.245 44.405 -1.303 1.00 24.49 C ATOM 79 CD2 LEU A 12 17.457 44.315 1.204 1.00 21.79 C ATOM 80 N PRO A 13 21.386 41.743 1.476 1.00 24.36 N ATOM 81 CA PRO A 13 20.351 41.670 2.533 1.00 24.17 C ATOM 82 C PRO A 13 20.685 42.375 3.838 1.00 24.39 C ATOM 83 O PRO A 13 19.834 42.426 4.711 1.00 25.43 O ATOM 84 CB PRO A 13 20.288 40.158 2.827 1.00 23.15 C ATOM 85 CG PRO A 13 21.729 39.721 2.577 1.00 24.50 C ATOM 86 CD PRO A 13 22.089 40.451 1.320 1.00 23.40 C ATOM 87 N GLN A 14 21.914 42.858 4.024 1.00 24.55 N ATOM 88 CA GLN A 14 22.326 43.248 5.367 1.00 24.52 C ATOM 89 C GLN A 14 21.819 44.648 5.828 1.00 24.75 C ATOM 90 O GLN A 14 21.677 44.894 7.030 1.00 24.93 O ATOM 91 CB GLN A 14 23.855 43.075 5.569 1.00 24.43 C ATOM 92 CG GLN A 14 24.713 44.188 5.026 1.00 23.98 C ATOM 93 CD GLN A 14 25.043 43.985 3.535 1.00 28.20 C ATOM 94 OE1 GLN A 14 24.581 43.009 2.886 1.00 24.90 O ATOM 95 NE2 GLN A 14 25.852 44.905 2.978 1.00 26.11 N ATOM 96 N ASP A 15 21.564 45.534 4.870 1.00 23.84 N ATOM 97 CA ASP A 15 21.118 46.909 5.116 1.00 24.38 C ATOM 98 C ASP A 15 19.713 47.043 4.478 1.00 23.69 C ATOM 99 O ASP A 15 19.595 47.207 3.252 1.00 24.21 O ATOM 100 CB ASP A 15 22.139 47.858 4.480 1.00 23.38 C ATOM 101 CG ASP A 15 21.822 49.319 4.698 1.00 26.33 C ATOM 102 OD1 ASP A 15 20.881 49.684 5.451 1.00 27.50 O ATOM 103 OD2 ASP A 15 22.525 50.140 4.100 1.00 26.80 O ATOM 104 N PHE A 16 18.663 46.860 5.294 1.00 23.31 N ATOM 105 CA PHE A 16 17.273 46.837 4.816 1.00 23.19 C ATOM 106 C PHE A 16 16.304 47.845 5.526 1.00 23.35 C ATOM 107 O PHE A 16 16.611 48.396 6.589 1.00 23.52 O ATOM 108 CB PHE A 16 16.708 45.420 4.913 1.00 22.15 C ATOM 109 CG PHE A 16 16.755 44.850 6.304 1.00 23.52 C ATOM 110 CD1 PHE A 16 15.651 44.981 7.178 1.00 21.74 C ATOM 111 CD2 PHE A 16 17.894 44.177 6.749 1.00 21.69 C ATOM 112 CE1 PHE A 16 15.692 44.448 8.458 1.00 23.07 C ATOM 113 CE2 PHE A 16 17.962 43.648 8.041 1.00 21.56 C ATOM 114 CZ PHE A 16 16.870 43.770 8.903 1.00 22.24 C ATOM 115 N ASN A 17 15.127 48.049 4.936 1.00 23.34 N ATOM 116 CA ASN A 17 14.124 48.961 5.479 1.00 22.99 C ATOM 117 C ASN A 17 12.974 48.168 6.088 1.00 22.52 C ATOM 118 O ASN A 17 12.615 47.109 5.587 1.00 21.94 O ATOM 119 CB ASN A 17 13.567 49.872 4.354 1.00 24.37 C ATOM 120 CG ASN A 17 14.635 50.818 3.792 1.00 24.52 C ATOM 121 OD1 ASN A 17 15.483 51.296 4.541 1.00 26.24 O ATOM 122 ND2 ASN A 17 14.609 51.063 2.469 1.00 22.96 N ATOM 123 N VAL A 18 12.406 48.688 7.175 1.00 22.23 N ATOM 124 CA VAL A 18 11.233 48.079 7.822 1.00 20.84 C ATOM 125 C VAL A 18 10.145 49.150 7.953 1.00 20.77 C ATOM 126 O VAL A 18 10.375 50.259 8.466 1.00 20.23 O ATOM 127 CB VAL A 18 11.556 47.505 9.264 1.00 21.36 C ATOM 128 CG1 VAL A 18 10.350 46.768 9.827 1.00 19.07 C ATOM 129 CG2 VAL A 18 12.803 46.559 9.236 1.00 19.34 C ATOM 130 N ILE A 19 8.968 48.830 7.446 1.00 20.63 N ATOM 131 CA ILE A 19 7.808 49.672 7.712 1.00 21.06 C ATOM 132 C ILE A 19 7.109 49.163 8.967 1.00 20.14 C ATOM 133 O ILE A 19 6.763 47.954 9.057 1.00 19.42 O ATOM 134 CB ILE A 19 6.841 49.673 6.498 1.00 22.11 C ATOM 135 CG1 ILE A 19 7.500 50.469 5.349 1.00 22.28 C ATOM 136 CG2 ILE A 19 5.467 50.272 6.876 1.00 19.98 C ATOM 137 CD1 ILE A 19 6.887 50.180 3.973 1.00 24.13 C ATOM 138 N ILE A 20 6.914 50.062 9.937 1.00 19.07 N ATOM 139 CA ILE A 20 6.335 49.641 11.228 1.00 18.73 C ATOM 140 C ILE A 20 4.808 49.541 11.151 1.00 19.01 C ATOM 141 O ILE A 20 4.148 50.500 10.726 1.00 20.15 O ATOM 142 CB ILE A 20 6.767 50.609 12.367 1.00 18.68 C ATOM 143 CG1 ILE A 20 8.310 50.664 12.407 1.00 18.52 C ATOM 144 CG2 ILE A 20 6.131 50.202 13.761 1.00 17.94 C ATOM 145 CD1 ILE A 20 8.972 49.240 12.614 1.00 16.95 C ATOM 146 N GLU A 21 4.251 48.404 11.563 1.00 18.77 N ATOM 147 CA GLU A 21 2.788 48.243 11.677 1.00 19.87 C ATOM 148 C GLU A 21 2.290 48.373 13.130 1.00 19.89 C ATOM 149 O GLU A 21 1.226 48.954 13.377 1.00 20.64 O ATOM 150 CB GLU A 21 2.343 46.896 11.092 1.00 19.24 C ATOM 151 CG GLU A 21 2.620 46.756 9.582 1.00 21.01 C ATOM 152 CD GLU A 21 2.500 45.327 9.118 1.00 22.65 C ATOM 153 OE1 GLU A 21 3.120 44.447 9.729 1.00 26.58 O ATOM 154 OE2 GLU A 21 1.771 45.072 8.153 1.00 23.20 O ATOM 155 N ILE A 22 3.076 47.870 14.079 1.00 19.73 N ATOM 156 CA ILE A 22 2.667 47.809 15.505 1.00 19.94 C ATOM 157 C ILE A 22 3.788 48.237 16.456 1.00 19.81 C ATOM 158 O ILE A 22 4.767 47.517 16.605 1.00 21.37 O ATOM 159 CB ILE A 22 2.182 46.370 15.899 1.00 20.44 C ATOM 160 CG1 ILE A 22 1.021 45.935 15.009 1.00 19.03 C ATOM 161 CG2 ILE A 22 1.789 46.307 17.367 1.00 19.40 C ATOM 162 CD1 ILE A 22 0.659 44.455 15.118 1.00 19.72 C ATOM 163 N PRO A 23 3.672 49.434 17.073 1.00 19.24 N ATOM 164 CA PRO A 23 4.714 49.919 18.016 1.00 18.94 C ATOM 165 C PRO A 23 4.816 48.987 19.246 1.00 19.28 C ATOM 166 O PRO A 23 3.819 48.398 19.666 1.00 19.56 O ATOM 167 CB PRO A 23 4.201 51.308 18.436 1.00 18.92 C ATOM 168 CG PRO A 23 3.286 51.728 17.295 1.00 17.76 C ATOM 169 CD PRO A 23 2.608 50.421 16.861 1.00 17.40 C ATOM 170 N ALA A 24 6.026 48.803 19.761 1.00 18.68 N ATOM 171 CA ALA A 24 6.227 48.079 21.006 1.00 18.54 C ATOM 172 C ALA A 24 5.270 48.569 22.090 1.00 18.10 C ATOM 173 O ALA A 24 5.137 49.785 22.277 1.00 18.29 O ATOM 174 CB ALA A 24 7.660 48.250 21.486 1.00 17.41 C ATOM 175 N GLN A 25 4.623 47.639 22.805 1.00 17.44 N ATOM 176 CA GLN A 25 3.743 48.001 23.972 1.00 18.87 C ATOM 177 C GLN A 25 2.476 48.811 23.642 1.00 18.88 C ATOM 178 O GLN A 25 1.787 49.325 24.541 1.00 19.08 O ATOM 179 CB GLN A 25 4.570 48.733 25.062 1.00 18.70 C ATOM 180 CG GLN A 25 5.715 47.839 25.644 1.00 19.85 C ATOM 181 CD GLN A 25 5.192 46.588 26.346 1.00 22.15 C ATOM 182 OE1 GLN A 25 4.040 46.540 26.806 1.00 25.01 O ATOM 183 NE2 GLN A 25 6.035 45.573 26.446 1.00 22.42 N ATOM 184 N SER A 26 2.145 48.938 22.364 1.00 19.33 N ATOM 185 CA SER A 26 0.912 49.648 21.988 1.00 19.59 C ATOM 186 C SER A 26 -0.320 48.844 22.464 1.00 20.50 C ATOM 187 O SER A 26 -0.237 47.623 22.727 1.00 20.29 O ATOM 188 CB SER A 26 0.884 49.925 20.458 1.00 19.67 C ATOM 189 OG SER A 26 1.003 48.706 19.704 1.00 19.08 O ATOM 190 N GLU A 27 -1.464 49.514 22.603 1.00 20.38 N ATOM 191 CA GLU A 27 -2.696 48.815 22.968 1.00 21.73 C ATOM 192 C GLU A 27 -2.899 47.630 22.013 1.00 21.32 C ATOM 193 O GLU A 27 -2.468 47.677 20.875 1.00 21.54 O ATOM 194 CB GLU A 27 -3.896 49.808 23.027 1.00 21.74 C ATOM 195 CG GLU A 27 -3.758 50.649 24.300 1.00 23.24 C ATOM 196 CD GLU A 27 -4.826 51.710 24.535 1.00 25.87 C ATOM 197 OE1 GLU A 27 -5.477 52.149 23.596 1.00 25.51 O ATOM 198 OE2 GLU A 27 -5.000 52.130 25.698 1.00 25.72 O ATOM 199 N PRO A 28 -3.555 46.560 22.480 1.00 21.62 N ATOM 200 CA PRO A 28 -3.561 45.259 21.771 1.00 21.72 C ATOM 201 C PRO A 28 -4.457 45.171 20.496 1.00 22.43 C ATOM 202 O PRO A 28 -5.421 44.391 20.437 1.00 22.00 O ATOM 203 CB PRO A 28 -4.038 44.271 22.855 1.00 21.26 C ATOM 204 CG PRO A 28 -4.768 45.110 23.839 1.00 21.70 C ATOM 205 CD PRO A 28 -4.153 46.479 23.829 1.00 21.25 C ATOM 206 N VAL A 29 -4.098 45.952 19.485 1.00 23.11 N ATOM 207 CA VAL A 29 -4.811 46.024 18.207 1.00 23.26 C ATOM 208 C VAL A 29 -3.804 45.704 17.111 1.00 23.88 C ATOM 209 O VAL A 29 -2.754 46.345 17.004 1.00 23.18 O ATOM 210 CB VAL A 29 -5.430 47.448 17.974 1.00 23.27 C ATOM 211 CG1 VAL A 29 -6.368 47.470 16.769 1.00 21.69 C ATOM 212 CG2 VAL A 29 -6.114 47.970 19.256 1.00 22.25 C ATOM 213 N LYS A 30 -4.115 44.681 16.315 1.00 24.89 N ATOM 214 CA LYS A 30 -3.209 44.200 15.259 1.00 26.06 C ATOM 215 C LYS A 30 -3.450 44.954 13.937 1.00 26.00 C ATOM 216 O LYS A 30 -4.425 44.686 13.244 1.00 26.59 O ATOM 217 CB LYS A 30 -3.467 42.692 15.077 1.00 26.61 C ATOM 218 CG LYS A 30 -2.248 41.822 14.884 1.00 28.45 C ATOM 219 CD LYS A 30 -1.999 41.562 13.421 1.00 28.74 C ATOM 220 CE LYS A 30 -0.999 40.442 13.240 1.00 30.16 C ATOM 221 NZ LYS A 30 -0.274 40.696 11.977 1.00 28.79 N ATOM 222 N TYR A 31 -2.613 45.936 13.595 1.00 25.80 N ATOM 223 CA TYR A 31 -2.729 46.580 12.294 1.00 25.22 C ATOM 224 C TYR A 31 -1.864 45.867 11.261 1.00 27.00 C ATOM 225 O TYR A 31 -0.798 45.336 11.598 1.00 26.61 O ATOM 226 CB TYR A 31 -2.308 48.046 12.361 1.00 25.12 C ATOM 227 CG TYR A 31 -3.212 48.892 13.226 1.00 23.08 C ATOM 228 CD1 TYR A 31 -4.287 49.571 12.673 1.00 19.20 C ATOM 229 CD2 TYR A 31 -3.015 48.958 14.603 1.00 18.39 C ATOM 230 CE1 TYR A 31 -5.114 50.341 13.448 1.00 19.06 C ATOM 231 CE2 TYR A 31 -3.845 49.730 15.405 1.00 20.45 C ATOM 232 CZ TYR A 31 -4.898 50.419 14.815 1.00 18.45 C ATOM 233 OH TYR A 31 -5.738 51.188 15.591 1.00 21.38 O ATOM 234 N GLU A 32 -2.333 45.871 10.016 1.00 27.55 N ATOM 235 CA GLU A 32 -1.576 45.372 8.868 1.00 30.56 C ATOM 236 C GLU A 32 -1.594 46.427 7.779 1.00 30.42 C ATOM 237 O GLU A 32 -2.638 46.991 7.484 1.00 30.34 O ATOM 238 CB GLU A 32 -2.173 44.050 8.322 1.00 31.34 C ATOM 239 CG GLU A 32 -2.005 42.866 9.281 1.00 36.06 C ATOM 240 CD GLU A 32 -2.344 41.526 8.649 1.00 43.47 C ATOM 241 OE1 GLU A 32 -2.926 41.513 7.531 1.00 44.52 O ATOM 242 OE2 GLU A 32 -2.042 40.483 9.294 1.00 47.61 O ATOM 243 N ALA A 33 -0.434 46.703 7.200 1.00 31.88 N ATOM 244 CA ALA A 33 -0.345 47.623 6.073 1.00 33.76 C ATOM 245 C ALA A 33 -1.055 47.022 4.860 1.00 35.50 C ATOM 246 O ALA A 33 -0.894 45.835 4.550 1.00 36.09 O ATOM 247 CB ALA A 33 1.091 47.937 5.747 1.00 33.39 C ATOM 248 N ASP A 34 -1.890 47.820 4.207 1.00 36.96 N ATOM 249 CA ASP A 34 -2.438 47.426 2.914 1.00 38.49 C ATOM 250 C ASP A 34 -1.577 48.087 1.835 1.00 39.63 C ATOM 251 O ASP A 34 -1.554 49.309 1.686 1.00 38.98 O ATOM 252 CB ASP A 34 -3.896 47.845 2.800 1.00 38.53 C ATOM 253 CG ASP A 34 -4.540 47.355 1.528 1.00 39.38 C ATOM 254 OD1 ASP A 34 -4.180 47.841 0.442 1.00 37.36 O ATOM 255 OD2 ASP A 34 -5.405 46.469 1.619 1.00 42.57 O ATOM 256 N LYS A 35 -0.810 47.282 1.120 1.00 41.54 N ATOM 257 CA LYS A 35 0.108 47.856 0.134 1.00 44.05 C ATOM 258 C LYS A 35 -0.633 48.369 -1.124 1.00 44.94 C ATOM 259 O LYS A 35 -0.100 49.187 -1.886 1.00 45.87 O ATOM 260 CB LYS A 35 1.242 46.868 -0.197 1.00 44.78 C ATOM 261 CG LYS A 35 2.517 47.072 0.672 1.00 44.98 C ATOM 262 CD LYS A 35 2.936 45.792 1.403 1.00 45.99 C ATOM 263 CE LYS A 35 1.747 45.213 2.158 1.00 47.71 C ATOM 264 NZ LYS A 35 2.070 44.230 3.257 1.00 48.24 N ATOM 265 N ALA A 36 -1.873 47.914 -1.313 1.00 44.65 N ATOM 266 CA ALA A 36 -2.707 48.405 -2.391 1.00 44.81 C ATOM 267 C ALA A 36 -3.519 49.652 -2.006 1.00 44.91 C ATOM 268 O ALA A 36 -4.046 50.317 -2.886 1.00 45.28 O ATOM 269 CB ALA A 36 -3.656 47.309 -2.864 1.00 44.78 C ATOM 270 N LEU A 37 -3.680 49.937 -0.708 1.00 43.77 N ATOM 271 CA LEU A 37 -4.397 51.142 -0.298 1.00 42.57 C ATOM 272 C LEU A 37 -3.404 52.197 0.145 1.00 41.06 C ATOM 273 O LEU A 37 -3.735 53.383 0.193 1.00 41.20 O ATOM 274 CB LEU A 37 -5.379 50.861 0.844 1.00 42.92 C ATOM 275 CG LEU A 37 -6.450 49.797 0.612 1.00 43.81 C ATOM 276 CD1 LEU A 37 -7.367 49.636 1.818 1.00 44.72 C ATOM 277 CD2 LEU A 37 -7.258 50.154 -0.608 1.00 45.97 C ATOM 278 N GLY A 38 -2.183 51.759 0.469 1.00 39.85 N ATOM 279 CA GLY A 38 -1.176 52.617 1.131 1.00 37.63 C ATOM 280 C GLY A 38 -1.501 53.016 2.583 1.00 36.28 C ATOM 281 O GLY A 38 -1.003 54.034 3.081 1.00 36.55 O ATOM 282 N LEU A 39 -2.339 52.234 3.265 1.00 33.68 N ATOM 283 CA LEU A 39 -2.850 52.621 4.595 1.00 31.37 C ATOM 284 C LEU A 39 -2.765 51.448 5.548 1.00 29.37 C ATOM 285 O LEU A 39 -2.761 50.301 5.099 1.00 28.58 O ATOM 286 CB LEU A 39 -4.311 53.094 4.516 1.00 30.92 C ATOM 287 CG LEU A 39 -4.593 54.380 3.727 1.00 31.84 C ATOM 288 CD1 LEU A 39 -6.088 54.592 3.563 1.00 31.37 C ATOM 289 CD2 LEU A 39 -3.950 55.577 4.413 1.00 30.83 C ATOM 290 N LEU A 40 -2.685 51.738 6.854 1.00 27.18 N ATOM 291 CA LEU A 40 -2.802 50.690 7.873 1.00 26.07 C ATOM 292 C LEU A 40 -4.260 50.295 8.039 1.00 24.63 C ATOM 293 O LEU A 40 -5.140 51.150 8.125 1.00 23.26 O ATOM 294 CB LEU A 40 -2.218 51.115 9.238 1.00 25.71 C ATOM 295 CG LEU A 40 -0.687 51.351 9.263 1.00 25.93 C ATOM 296 CD1 LEU A 40 -0.250 52.020 10.547 1.00 24.92 C ATOM 297 CD2 LEU A 40 0.064 50.039 9.032 1.00 24.73 C ATOM 298 N VAL A 41 -4.486 48.988 8.093 1.00 24.43 N ATOM 299 CA VAL A 41 -5.822 48.433 8.262 1.00 25.12 C ATOM 300 C VAL A 41 -5.926 47.622 9.556 1.00 25.36 C ATOM 301 O VAL A 41 -4.999 46.846 9.885 1.00 24.93 O ATOM 302 CB VAL A 41 -6.155 47.533 7.039 1.00 25.41 C ATOM 303 CG1 VAL A 41 -7.438 46.711 7.244 1.00 26.79 C ATOM 304 CG2 VAL A 41 -6.270 48.406 5.797 1.00 24.02 C ATOM 305 N VAL A 42 -7.038 47.774 10.285 1.00 24.79 N ATOM 306 CA VAL A 42 -7.232 46.981 11.515 1.00 25.06 C ATOM 307 C VAL A 42 -7.535 45.513 11.174 1.00 25.94 C ATOM 308 O VAL A 42 -8.638 45.197 10.731 1.00 26.93 O ATOM 309 CB VAL A 42 -8.420 47.451 12.370 1.00 24.99 C ATOM 310 CG1 VAL A 42 -8.436 46.718 13.688 1.00 24.48 C ATOM 311 CG2 VAL A 42 -8.400 48.939 12.607 1.00 24.84 C ATOM 312 N ASP A 43 -6.578 44.619 11.376 1.00 25.33 N ATOM 313 CA ASP A 43 -6.825 43.221 11.140 1.00 26.20 C ATOM 314 C ASP A 43 -7.737 42.626 12.210 1.00 25.70 C ATOM 315 O ASP A 43 -8.787 42.081 11.879 1.00 25.64 O ATOM 316 CB ASP A 43 -5.524 42.401 11.040 1.00 27.86 C ATOM 317 CG ASP A 43 -5.814 40.952 10.725 1.00 30.64 C ATOM 318 OD1 ASP A 43 -6.372 40.686 9.642 1.00 37.20 O ATOM 319 OD2 ASP A 43 -5.576 40.084 11.564 1.00 33.64 O ATOM 320 N ARG A 44 -7.345 42.729 13.482 1.00 23.76 N ATOM 321 CA ARG A 44 -8.190 42.297 14.561 1.00 24.05 C ATOM 322 C ARG A 44 -7.761 42.917 15.906 1.00 24.08 C ATOM 323 O ARG A 44 -6.608 43.338 16.065 1.00 24.67 O ATOM 324 CB ARG A 44 -8.171 40.764 14.678 1.00 24.30 C ATOM 325 CG ARG A 44 -6.835 40.203 15.246 1.00 24.56 C ATOM 326 CD ARG A 44 -6.770 38.712 15.056 1.00 28.25 C ATOM 327 NE ARG A 44 -5.527 38.105 15.527 1.00 30.15 N ATOM 328 CZ ARG A 44 -4.436 37.938 14.774 1.00 30.95 C ATOM 329 NH1 ARG A 44 -4.413 38.364 13.500 1.00 29.56 N ATOM 330 NH2 ARG A 44 -3.363 37.358 15.299 1.00 27.85 N ATOM 331 N PHE A 45 -8.708 42.999 16.839 1.00 23.14 N ATOM 332 CA PHE A 45 -8.408 43.175 18.265 1.00 23.01 C ATOM 333 C PHE A 45 -7.891 41.854 18.809 1.00 23.22 C ATOM 334 O PHE A 45 -8.571 40.821 18.730 1.00 22.43 O ATOM 335 CB PHE A 45 -9.621 43.696 19.024 1.00 23.17 C ATOM 336 CG PHE A 45 -9.904 45.174 18.756 1.00 23.12 C ATOM 337 CD1 PHE A 45 -9.587 46.141 19.696 1.00 22.31 C ATOM 338 CD2 PHE A 45 -10.456 45.591 17.546 1.00 22.00 C ATOM 339 CE1 PHE A 45 -9.815 47.525 19.445 1.00 19.37 C ATOM 340 CE2 PHE A 45 -10.689 46.946 17.299 1.00 24.14 C ATOM 341 CZ PHE A 45 -10.363 47.920 18.257 1.00 20.26 C ATOM 342 N ILE A 46 -6.653 41.870 19.303 1.00 22.58 N ATOM 343 CA ILE A 46 -6.049 40.660 19.811 1.00 22.68 C ATOM 344 C ILE A 46 -6.900 40.042 20.937 1.00 22.39 C ATOM 345 O ILE A 46 -7.174 40.697 21.955 1.00 22.85 O ATOM 346 CB ILE A 46 -4.573 40.901 20.294 1.00 22.60 C ATOM 347 CG1 ILE A 46 -3.715 41.434 19.130 1.00 21.33 C ATOM 348 CG2 ILE A 46 -4.021 39.618 20.954 1.00 19.70 C ATOM 349 CD1 ILE A 46 -2.327 41.989 19.546 1.00 21.68 C ATOM 350 N GLY A 47 -7.299 38.783 20.761 1.00 21.82 N ATOM 351 CA GLY A 47 -8.248 38.135 21.701 1.00 20.72 C ATOM 352 C GLY A 47 -7.794 38.069 23.156 1.00 20.43 C ATOM 353 O GLY A 47 -8.593 38.229 24.093 1.00 19.67 O ATOM 354 N THR A 48 -6.499 37.840 23.355 1.00 19.77 N ATOM 355 CA THR A 48 -5.932 37.739 24.683 1.00 19.66 C ATOM 356 C THR A 48 -5.613 39.106 25.314 1.00 20.30 C ATOM 357 O THR A 48 -5.329 39.200 26.512 1.00 20.72 O ATOM 358 CB THR A 48 -4.619 36.917 24.634 1.00 20.30 C ATOM 359 OG1 THR A 48 -3.768 37.491 23.644 1.00 20.44 O ATOM 360 CG2 THR A 48 -4.860 35.453 24.277 1.00 17.40 C ATOM 361 N GLY A 49 -5.651 40.181 24.535 1.00 20.99 N ATOM 362 CA GLY A 49 -5.269 41.493 25.078 1.00 20.69 C ATOM 363 C GLY A 49 -3.758 41.638 25.240 1.00 20.94 C ATOM 364 O GLY A 49 -3.299 42.624 25.806 1.00 21.56 O ATOM 365 N MET A 50 -2.983 40.667 24.749 1.00 19.51 N ATOM 366 CA MET A 50 -1.499 40.721 24.822 1.00 18.69 C ATOM 367 C MET A 50 -0.883 41.715 23.837 1.00 18.94 C ATOM 368 O MET A 50 -1.429 41.916 22.738 1.00 19.06 O ATOM 369 CB MET A 50 -0.898 39.311 24.595 1.00 18.46 C ATOM 370 CG MET A 50 -1.205 38.359 25.743 1.00 16.28 C ATOM 371 SD MET A 50 -0.534 36.732 25.499 1.00 20.35 S ATOM 372 CE MET A 50 1.161 36.996 26.020 1.00 15.70 C ATOM 373 N ARG A 51 0.266 42.306 24.221 1.00 18.83 N ATOM 374 CA ARG A 51 0.901 43.405 23.476 1.00 18.83 C ATOM 375 C ARG A 51 2.255 42.953 22.927 1.00 19.23 C ATOM 376 O ARG A 51 3.000 42.203 23.600 1.00 18.63 O ATOM 377 CB ARG A 51 1.111 44.671 24.362 1.00 18.43 C ATOM 378 CG ARG A 51 -0.162 45.289 24.984 1.00 17.94 C ATOM 379 CD ARG A 51 0.141 46.584 25.739 1.00 17.07 C ATOM 380 NE ARG A 51 -1.057 47.096 26.434 1.00 17.53 N ATOM 381 CZ ARG A 51 -1.381 48.382 26.591 1.00 17.75 C ATOM 382 NH1 ARG A 51 -0.616 49.350 26.093 1.00 15.93 N ATOM 383 NH2 ARG A 51 -2.498 48.705 27.248 1.00 17.88 N ATOM 384 N TYR A 52 2.587 43.425 21.724 1.00 18.81 N ATOM 385 CA TYR A 52 3.925 43.167 21.179 1.00 20.17 C ATOM 386 C TYR A 52 4.969 43.754 22.104 1.00 19.88 C ATOM 387 O TYR A 52 4.909 44.924 22.419 1.00 19.46 O ATOM 388 CB TYR A 52 4.063 43.715 19.744 1.00 19.61 C ATOM 389 CG TYR A 52 3.327 42.878 18.720 1.00 21.97 C ATOM 390 CD1 TYR A 52 4.031 42.070 17.818 1.00 22.85 C ATOM 391 CD2 TYR A 52 1.918 42.863 18.667 1.00 21.92 C ATOM 392 CE1 TYR A 52 3.370 41.301 16.883 1.00 21.48 C ATOM 393 CE2 TYR A 52 1.241 42.079 17.734 1.00 22.65 C ATOM 394 CZ TYR A 52 1.964 41.293 16.853 1.00 23.39 C ATOM 395 OH TYR A 52 1.315 40.519 15.914 1.00 21.36 O ATOM 396 N PRO A 53 5.919 42.920 22.572 1.00 21.29 N ATOM 397 CA PRO A 53 7.017 43.398 23.428 1.00 21.87 C ATOM 398 C PRO A 53 8.071 44.269 22.717 1.00 21.70 C ATOM 399 O PRO A 53 8.819 44.986 23.394 1.00 21.93 O ATOM 400 CB PRO A 53 7.642 42.106 23.998 1.00 21.72 C ATOM 401 CG PRO A 53 7.174 40.998 23.100 1.00 22.80 C ATOM 402 CD PRO A 53 5.885 41.443 22.446 1.00 22.07 C ATOM 403 N VAL A 54 8.100 44.236 21.382 1.00 20.85 N ATOM 404 CA VAL A 54 9.007 45.057 20.582 1.00 21.55 C ATOM 405 C VAL A 54 8.232 45.490 19.356 1.00 20.83 C ATOM 406 O VAL A 54 7.140 44.972 19.117 1.00 20.05 O ATOM 407 CB VAL A 54 10.281 44.275 20.107 1.00 22.98 C ATOM 408 CG1 VAL A 54 11.079 43.719 21.297 1.00 23.11 C ATOM 409 CG2 VAL A 54 9.884 43.163 19.151 1.00 24.55 C ATOM 410 N ASN A 55 8.770 46.452 18.602 1.00 19.90 N ATOM 411 CA ASN A 55 8.127 46.907 17.367 1.00 21.21 C ATOM 412 C ASN A 55 7.999 45.819 16.329 1.00 20.69 C ATOM 413 O ASN A 55 8.869 44.984 16.187 1.00 21.68 O ATOM 414 CB ASN A 55 8.838 48.129 16.748 1.00 20.69 C ATOM 415 CG ASN A 55 9.109 49.224 17.771 1.00 20.45 C ATOM 416 OD1 ASN A 55 8.221 50.008 18.123 1.00 17.26 O ATOM 417 ND2 ASN A 55 10.351 49.292 18.238 1.00 18.77 N ATOM 418 N TYR A 56 6.903 45.849 15.596 1.00 20.79 N ATOM 419 CA TYR A 56 6.622 44.831 14.583 1.00 20.61 C ATOM 420 C TYR A 56 6.243 45.465 13.238 1.00 20.45 C ATOM 421 O TYR A 56 5.457 46.410 13.177 1.00 19.77 O ATOM 422 CB TYR A 56 5.479 43.957 15.068 1.00 20.53 C ATOM 423 CG TYR A 56 5.162 42.754 14.189 1.00 22.99 C ATOM 424 CD1 TYR A 56 6.112 41.762 13.982 1.00 23.35 C ATOM 425 CD2 TYR A 56 3.898 42.608 13.593 1.00 22.26 C ATOM 426 CE1 TYR A 56 5.834 40.653 13.201 1.00 24.86 C ATOM 427 CE2 TYR A 56 3.606 41.493 12.825 1.00 25.04 C ATOM 428 CZ TYR A 56 4.585 40.513 12.637 1.00 26.22 C ATOM 429 OH TYR A 56 4.338 39.402 11.853 1.00 26.67 O ATOM 430 N GLY A 57 6.814 44.934 12.167 1.00 20.57 N ATOM 431 CA GLY A 57 6.543 45.425 10.820 1.00 20.64 C ATOM 432 C GLY A 57 7.020 44.440 9.773 1.00 20.42 C ATOM 433 O GLY A 57 7.108 43.230 10.030 1.00 20.25 O ATOM 434 N PHE A 58 7.317 44.956 8.590 1.00 21.49 N ATOM 435 CA PHE A 58 7.723 44.098 7.462 1.00 22.42 C ATOM 436 C PHE A 58 8.739 44.803 6.557 1.00 21.95 C ATOM 437 O PHE A 58 8.846 46.035 6.548 1.00 21.27 O ATOM 438 CB PHE A 58 6.473 43.668 6.628 1.00 22.41 C ATOM 439 CG PHE A 58 5.792 44.818 5.923 1.00 25.13 C ATOM 440 CD1 PHE A 58 6.084 45.105 4.587 1.00 25.77 C ATOM 441 CD2 PHE A 58 4.881 45.626 6.598 1.00 22.93 C ATOM 442 CE1 PHE A 58 5.476 46.166 3.936 1.00 24.40 C ATOM 443 CE2 PHE A 58 4.289 46.717 5.972 1.00 23.86 C ATOM 444 CZ PHE A 58 4.575 46.987 4.632 1.00 26.77 C ATOM 445 N ILE A 59 9.456 44.013 5.766 1.00 22.61 N ATOM 446 CA ILE A 59 10.300 44.571 4.683 1.00 23.33 C ATOM 447 C ILE A 59 9.523 44.749 3.371 1.00 23.32 C ATOM 448 O ILE A 59 9.003 43.779 2.827 1.00 24.29 O ATOM 449 CB ILE A 59 11.557 43.690 4.429 1.00 22.84 C ATOM 450 CG1 ILE A 59 12.281 43.398 5.748 1.00 22.43 C ATOM 451 CG2 ILE A 59 12.476 44.360 3.354 1.00 22.00 C ATOM 452 CD1 ILE A 59 13.474 42.443 5.622 1.00 19.09 C ATOM 453 N PRO A 60 9.420 45.985 2.872 1.00 24.84 N ATOM 454 CA PRO A 60 8.675 46.182 1.622 1.00 26.36 C ATOM 455 C PRO A 60 9.384 45.522 0.421 1.00 27.39 C ATOM 456 O PRO A 60 10.605 45.317 0.441 1.00 27.93 O ATOM 457 CB PRO A 60 8.639 47.712 1.456 1.00 25.61 C ATOM 458 CG PRO A 60 9.839 48.222 2.254 1.00 25.88 C ATOM 459 CD PRO A 60 9.955 47.257 3.418 1.00 25.38 C ATOM 460 N GLN A 61 8.609 45.181 -0.600 1.00 28.29 N ATOM 461 CA GLN A 61 9.159 44.570 -1.809 1.00 29.22 C ATOM 462 C GLN A 61 9.810 43.208 -1.540 1.00 29.01 C ATOM 463 O GLN A 61 10.828 42.854 -2.136 1.00 28.95 O ATOM 464 CB GLN A 61 10.069 45.568 -2.526 1.00 29.21 C ATOM 465 CG GLN A 61 9.202 46.671 -3.102 1.00 34.78 C ATOM 466 CD GLN A 61 9.957 47.810 -3.699 1.00 43.57 C ATOM 467 OE1 GLN A 61 9.386 48.866 -3.940 1.00 47.87 O ATOM 468 NE2 GLN A 61 11.245 47.619 -3.948 1.00 46.49 N ATOM 469 N THR A 62 9.218 42.458 -0.616 1.00 28.00 N ATOM 470 CA THR A 62 9.631 41.093 -0.365 1.00 28.25 C ATOM 471 C THR A 62 8.383 40.230 -0.370 1.00 29.87 C ATOM 472 O THR A 62 7.269 40.730 -0.203 1.00 29.15 O ATOM 473 CB THR A 62 10.397 40.905 0.989 1.00 28.15 C ATOM 474 OG1 THR A 62 9.545 41.234 2.104 1.00 27.37 O ATOM 475 CG2 THR A 62 11.679 41.753 1.027 1.00 26.31 C ATOM 476 N LEU A 63 8.566 38.932 -0.548 1.00 31.16 N ATOM 477 CA LEU A 63 7.455 38.007 -0.575 1.00 33.88 C ATOM 478 C LEU A 63 7.944 36.718 0.039 1.00 35.46 C ATOM 479 O LEU A 63 8.786 36.019 -0.523 1.00 35.30 O ATOM 480 CB LEU A 63 6.945 37.808 -2.016 1.00 33.87 C ATOM 481 CG LEU A 63 5.795 36.841 -2.280 1.00 34.60 C ATOM 482 CD1 LEU A 63 4.662 37.180 -1.363 1.00 36.93 C ATOM 483 CD2 LEU A 63 5.340 36.969 -3.724 1.00 36.15 C ATOM 484 N SER A 64 7.437 36.436 1.230 1.00 38.38 N ATOM 485 CA SER A 64 7.886 35.307 2.023 1.00 41.11 C ATOM 486 C SER A 64 7.191 34.036 1.577 1.00 43.10 C ATOM 487 O SER A 64 6.349 34.064 0.671 1.00 42.92 O ATOM 488 CB SER A 64 7.564 35.543 3.500 1.00 41.35 C ATOM 489 OG SER A 64 8.363 34.696 4.315 1.00 42.71 O ATOM 490 N GLY A 65 7.537 32.927 2.229 1.00 45.14 N ATOM 491 CA GLY A 65 6.892 31.638 1.968 1.00 47.76 C ATOM 492 C GLY A 65 5.362 31.636 2.005 1.00 49.24 C ATOM 493 O GLY A 65 4.723 30.859 1.293 1.00 50.21 O ATOM 494 N ASP A 66 4.753 32.482 2.832 1.00 50.27 N ATOM 495 CA ASP A 66 3.284 32.510 2.911 1.00 50.78 C ATOM 496 C ASP A 66 2.609 33.496 1.940 1.00 50.21 C ATOM 497 O ASP A 66 1.385 33.600 1.897 1.00 50.77 O ATOM 498 CB ASP A 66 2.820 32.798 4.342 1.00 51.29 C ATOM 499 CG ASP A 66 3.509 34.005 4.947 1.00 54.17 C ATOM 500 OD1 ASP A 66 3.722 35.014 4.219 1.00 55.27 O ATOM 501 OD2 ASP A 66 3.843 33.936 6.161 1.00 57.76 O ATOM 502 N GLY A 67 3.379 34.233 1.160 1.00 48.96 N ATOM 503 CA GLY A 67 2.739 35.181 0.272 1.00 47.16 C ATOM 504 C GLY A 67 2.604 36.550 0.903 1.00 45.61 C ATOM 505 O GLY A 67 2.093 37.467 0.266 1.00 46.42 O ATOM 506 N ASP A 68 3.068 36.690 2.147 1.00 44.01 N ATOM 507 CA ASP A 68 3.176 37.990 2.828 1.00 41.68 C ATOM 508 C ASP A 68 4.634 38.442 2.804 1.00 38.69 C ATOM 509 O ASP A 68 5.530 37.609 2.702 1.00 38.18 O ATOM 510 CB ASP A 68 2.772 37.862 4.299 1.00 43.06 C ATOM 511 CG ASP A 68 1.260 37.693 4.501 1.00 47.11 C ATOM 512 OD1 ASP A 68 0.458 38.106 3.618 1.00 50.50 O ATOM 513 OD2 ASP A 68 0.885 37.144 5.569 1.00 51.66 O ATOM 514 N PRO A 69 4.880 39.755 2.945 1.00 35.51 N ATOM 515 CA PRO A 69 6.253 40.252 3.039 1.00 33.20 C ATOM 516 C PRO A 69 7.007 39.648 4.217 1.00 31.00 C ATOM 517 O PRO A 69 6.388 39.081 5.103 1.00 30.18 O ATOM 518 CB PRO A 69 6.082 41.767 3.260 1.00 33.04 C ATOM 519 CG PRO A 69 4.739 42.103 2.734 1.00 35.64 C ATOM 520 CD PRO A 69 3.880 40.839 2.971 1.00 35.76 C ATOM 521 N VAL A 70 8.336 39.778 4.232 1.00 29.44 N ATOM 522 CA VAL A 70 9.151 39.250 5.348 1.00 27.95 C ATOM 523 C VAL A 70 8.837 40.047 6.625 1.00 26.77 C ATOM 524 O VAL A 70 8.915 41.270 6.619 1.00 26.46 O ATOM 525 CB VAL A 70 10.703 39.275 5.026 1.00 27.88 C ATOM 526 CG1 VAL A 70 11.514 38.958 6.258 1.00 27.39 C ATOM 527 CG2 VAL A 70 11.056 38.280 3.898 1.00 27.44 C ATOM 528 N ASP A 71 8.452 39.351 7.693 1.00 26.51 N ATOM 529 CA ASP A 71 8.153 39.968 9.014 1.00 26.25 C ATOM 530 C ASP A 71 9.381 40.260 9.866 1.00 25.56 C ATOM 531 O ASP A 71 10.322 39.450 9.926 1.00 25.69 O ATOM 532 CB ASP A 71 7.284 39.034 9.838 1.00 26.37 C ATOM 533 CG ASP A 71 5.942 38.790 9.227 1.00 28.24 C ATOM 534 OD1 ASP A 71 5.331 39.745 8.677 1.00 30.97 O ATOM 535 OD2 ASP A 71 5.496 37.624 9.306 1.00 28.38 O ATOM 536 N VAL A 72 9.362 41.410 10.542 1.00 24.69 N ATOM 537 CA VAL A 72 10.480 41.870 11.382 1.00 22.19 C ATOM 538 C VAL A 72 10.034 42.475 12.735 1.00 22.12 C ATOM 539 O VAL A 72 9.148 43.330 12.811 1.00 21.39 O ATOM 540 CB VAL A 72 11.395 42.879 10.629 1.00 22.97 C ATOM 541 CG1 VAL A 72 12.704 43.137 11.390 1.00 20.10 C ATOM 542 CG2 VAL A 72 11.667 42.402 9.171 1.00 21.68 C ATOM 543 N LEU A 73 10.666 41.984 13.798 1.00 21.86 N ATOM 544 CA LEU A 73 10.673 42.593 15.127 1.00 21.24 C ATOM 545 C LEU A 73 11.900 43.511 15.274 1.00 21.59 C ATOM 546 O LEU A 73 13.030 43.037 15.180 1.00 22.50 O ATOM 547 CB LEU A 73 10.739 41.468 16.172 1.00 21.37 C ATOM 548 CG LEU A 73 9.561 40.490 16.014 1.00 21.82 C ATOM 549 CD1 LEU A 73 9.902 39.045 16.446 1.00 23.52 C ATOM 550 CD2 LEU A 73 8.331 41.011 16.770 1.00 20.84 C ATOM 551 N VAL A 74 11.681 44.815 15.494 1.00 20.95 N ATOM 552 CA VAL A 74 12.752 45.796 15.684 1.00 19.54 C ATOM 553 C VAL A 74 12.771 46.277 17.140 1.00 20.67 C ATOM 554 O VAL A 74 11.768 46.843 17.646 1.00 19.81 O ATOM 555 CB VAL A 74 12.558 47.027 14.796 1.00 19.11 C ATOM 556 CG1 VAL A 74 13.790 47.916 14.808 1.00 16.39 C ATOM 557 CG2 VAL A 74 12.228 46.592 13.359 1.00 19.06 C ATOM 558 N ILE A 75 13.897 46.030 17.812 1.00 20.76 N ATOM 559 CA ILE A 75 14.131 46.466 19.213 1.00 21.77 C ATOM 560 C ILE A 75 14.639 47.928 19.210 1.00 22.17 C ATOM 561 O ILE A 75 15.604 48.245 18.487 1.00 22.78 O ATOM 562 CB ILE A 75 15.171 45.535 19.898 1.00 21.89 C ATOM 563 CG1 ILE A 75 14.703 44.087 19.786 1.00 21.31 C ATOM 564 CG2 ILE A 75 15.461 45.946 21.348 1.00 21.98 C ATOM 565 CD1 ILE A 75 15.763 43.077 20.206 1.00 21.97 C ATOM 566 N THR A 76 13.967 48.806 19.964 1.00 21.05 N ATOM 567 CA THR A 76 14.385 50.220 20.093 1.00 20.95 C ATOM 568 C THR A 76 14.241 50.718 21.543 1.00 20.55 C ATOM 569 O THR A 76 13.450 50.161 22.299 1.00 19.88 O ATOM 570 CB THR A 76 13.551 51.151 19.153 1.00 20.86 C ATOM 571 OG1 THR A 76 12.167 51.040 19.496 1.00 19.99 O ATOM 572 CG2 THR A 76 13.745 50.762 17.658 1.00 18.48 C ATOM 573 N PRO A 77 14.992 51.770 21.934 1.00 20.91 N ATOM 574 CA PRO A 77 14.763 52.260 23.309 1.00 21.70 C ATOM 575 C PRO A 77 13.382 52.961 23.583 1.00 21.66 C ATOM 576 O PRO A 77 12.953 53.016 24.743 1.00 21.57 O ATOM 577 CB PRO A 77 15.953 53.209 23.563 1.00 21.31 C ATOM 578 CG PRO A 77 16.481 53.561 22.213 1.00 21.76 C ATOM 579 CD PRO A 77 16.165 52.408 21.295 1.00 20.66 C ATOM 580 N PHE A 78 12.709 53.456 22.545 1.00 20.64 N ATOM 581 CA PHE A 78 11.360 54.051 22.662 1.00 21.02 C ATOM 582 C PHE A 78 10.529 53.502 21.508 1.00 20.26 C ATOM 583 O PHE A 78 11.074 53.303 20.404 1.00 20.09 O ATOM 584 CB PHE A 78 11.409 55.603 22.539 1.00 20.99 C ATOM 585 CG PHE A 78 12.129 56.296 23.695 1.00 22.97 C ATOM 586 CD1 PHE A 78 11.482 56.496 24.931 1.00 22.93 C ATOM 587 CD2 PHE A 78 13.446 56.731 23.549 1.00 20.66 C ATOM 588 CE1 PHE A 78 12.148 57.089 25.992 1.00 23.48 C ATOM 589 CE2 PHE A 78 14.113 57.329 24.597 1.00 21.65 C ATOM 590 CZ PHE A 78 13.472 57.507 25.823 1.00 23.50 C ATOM 591 N PRO A 79 9.201 53.295 21.718 1.00 20.67 N ATOM 592 CA PRO A 79 8.431 52.730 20.586 1.00 19.72 C ATOM 593 C PRO A 79 8.502 53.606 19.329 1.00 19.61 C ATOM 594 O PRO A 79 8.687 54.817 19.437 1.00 18.61 O ATOM 595 CB PRO A 79 6.993 52.618 21.137 1.00 20.21 C ATOM 596 CG PRO A 79 7.184 52.577 22.674 1.00 21.91 C ATOM 597 CD PRO A 79 8.355 53.522 22.918 1.00 19.80 C ATOM 598 N LEU A 80 8.406 52.986 18.147 1.00 19.41 N ATOM 599 CA LEU A 80 8.376 53.710 16.869 1.00 19.62 C ATOM 600 C LEU A 80 6.920 53.965 16.446 1.00 20.50 C ATOM 601 O LEU A 80 5.997 53.210 16.777 1.00 19.42 O ATOM 602 CB LEU A 80 9.054 52.878 15.740 1.00 19.52 C ATOM 603 CG LEU A 80 10.550 52.569 15.948 1.00 19.77 C ATOM 604 CD1 LEU A 80 11.033 51.619 14.875 1.00 18.38 C ATOM 605 CD2 LEU A 80 11.365 53.875 15.950 1.00 18.69 C ATOM 606 N LEU A 81 6.753 55.018 15.663 1.00 21.45 N ATOM 607 CA LEU A 81 5.481 55.415 15.076 1.00 21.99 C ATOM 608 C LEU A 81 4.960 54.399 14.062 1.00 21.60 C ATOM 609 O LEU A 81 5.681 54.045 13.128 1.00 21.18 O ATOM 610 CB LEU A 81 5.765 56.717 14.338 1.00 22.29 C ATOM 611 CG LEU A 81 4.838 57.896 14.175 1.00 28.01 C ATOM 612 CD1 LEU A 81 3.889 58.076 15.398 1.00 30.54 C ATOM 613 CD2 LEU A 81 5.729 59.117 13.976 1.00 30.14 C ATOM 614 N ALA A 82 3.701 53.961 14.200 1.00 20.50 N ATOM 615 CA ALA A 82 3.095 53.083 13.205 1.00 20.23 C ATOM 616 C ALA A 82 3.032 53.805 11.851 1.00 20.71 C ATOM 617 O ALA A 82 2.606 54.969 11.775 1.00 19.92 O ATOM 618 CB ALA A 82 1.685 52.621 13.648 1.00 19.13 C ATOM 619 N GLY A 83 3.473 53.115 10.797 1.00 21.09 N ATOM 620 CA GLY A 83 3.454 53.652 9.450 1.00 21.60 C ATOM 621 C GLY A 83 4.756 54.354 9.070 1.00 22.41 C ATOM 622 O GLY A 83 4.908 54.785 7.922 1.00 22.78 O ATOM 623 N SER A 84 5.675 54.500 10.026 1.00 21.49 N ATOM 624 CA SER A 84 7.003 55.049 9.743 1.00 22.62 C ATOM 625 C SER A 84 7.955 53.963 9.176 1.00 23.06 C ATOM 626 O SER A 84 7.665 52.766 9.271 1.00 23.25 O ATOM 627 CB SER A 84 7.612 55.745 10.986 1.00 21.55 C ATOM 628 OG SER A 84 7.949 54.826 12.039 1.00 21.85 O ATOM 629 N VAL A 85 9.091 54.414 8.626 1.00 23.53 N ATOM 630 CA VAL A 85 10.136 53.570 8.060 1.00 22.93 C ATOM 631 C VAL A 85 11.427 53.725 8.856 1.00 22.89 C ATOM 632 O VAL A 85 11.826 54.860 9.204 1.00 23.40 O ATOM 633 CB VAL A 85 10.436 53.956 6.572 1.00 23.72 C ATOM 634 CG1 VAL A 85 11.236 52.843 5.886 1.00 23.82 C ATOM 635 CG2 VAL A 85 9.154 54.114 5.810 1.00 23.40 C ATOM 636 N VAL A 86 12.073 52.594 9.143 1.00 21.59 N ATOM 637 CA VAL A 86 13.346 52.564 9.868 1.00 21.61 C ATOM 638 C VAL A 86 14.397 51.698 9.102 1.00 22.02 C ATOM 639 O VAL A 86 14.128 50.570 8.703 1.00 21.87 O ATOM 640 CB VAL A 86 13.192 52.095 11.360 1.00 21.44 C ATOM 641 CG1 VAL A 86 12.660 50.635 11.465 1.00 20.11 C ATOM 642 CG2 VAL A 86 14.521 52.237 12.127 1.00 19.16 C ATOM 643 N ARG A 87 15.561 52.278 8.859 1.00 21.94 N ATOM 644 CA ARG A 87 16.701 51.555 8.303 1.00 22.74 C ATOM 645 C ARG A 87 17.227 50.629 9.390 1.00 22.19 C ATOM 646 O ARG A 87 17.477 51.113 10.489 1.00 22.02 O ATOM 647 CB ARG A 87 17.783 52.582 7.935 1.00 23.60 C ATOM 648 CG ARG A 87 18.974 51.991 7.197 1.00 23.36 C ATOM 649 CD ARG A 87 19.981 53.075 6.916 1.00 25.35 C ATOM 650 NE ARG A 87 21.014 52.623 5.994 1.00 26.55 N ATOM 651 CZ ARG A 87 22.042 53.356 5.581 1.00 30.00 C ATOM 652 NH1 ARG A 87 22.199 54.589 6.009 1.00 30.00 N ATOM 653 NH2 ARG A 87 22.922 52.846 4.730 1.00 29.59 N ATOM 654 N ALA A 88 17.362 49.318 9.097 1.00 21.61 N ATOM 655 CA ALA A 88 17.679 48.293 10.097 1.00 20.95 C ATOM 656 C ALA A 88 18.751 47.274 9.647 1.00 21.61 C ATOM 657 O ALA A 88 19.144 47.220 8.463 1.00 21.00 O ATOM 658 CB ALA A 88 16.418 47.553 10.513 1.00 21.45 C ATOM 659 N ARG A 89 19.239 46.501 10.616 1.00 21.20 N ATOM 660 CA ARG A 89 20.154 45.376 10.373 1.00 21.57 C ATOM 661 C ARG A 89 19.695 44.194 11.214 1.00 21.96 C ATOM 662 O ARG A 89 19.012 44.373 12.257 1.00 21.50 O ATOM 663 CB ARG A 89 21.613 45.764 10.731 1.00 20.98 C ATOM 664 CG ARG A 89 21.869 45.980 12.223 1.00 19.77 C ATOM 665 CD ARG A 89 23.319 46.440 12.496 1.00 21.57 C ATOM 666 NE ARG A 89 23.500 46.936 13.863 1.00 20.57 N ATOM 667 CZ ARG A 89 23.630 46.151 14.929 1.00 21.84 C ATOM 668 NH1 ARG A 89 23.633 44.840 14.798 1.00 19.04 N ATOM 669 NH2 ARG A 89 23.774 46.671 16.132 1.00 24.53 N ATOM 670 N ALA A 90 20.093 42.985 10.816 1.00 22.44 N ATOM 671 CA ALA A 90 19.509 41.774 11.382 1.00 23.02 C ATOM 672 C ALA A 90 20.309 41.265 12.545 1.00 23.69 C ATOM 673 O ALA A 90 21.524 41.444 12.591 1.00 24.80 O ATOM 674 CB ALA A 90 19.382 40.685 10.333 1.00 23.51 C ATOM 675 N LEU A 91 19.625 40.629 13.495 1.00 24.22 N ATOM 676 CA LEU A 91 20.296 39.970 14.629 1.00 24.39 C ATOM 677 C LEU A 91 20.118 38.460 14.517 1.00 24.55 C ATOM 678 O LEU A 91 20.957 37.687 15.007 1.00 25.20 O ATOM 679 CB LEU A 91 19.727 40.438 15.986 1.00 23.48 C ATOM 680 CG LEU A 91 19.877 41.904 16.414 1.00 22.92 C ATOM 681 CD1 LEU A 91 19.353 42.033 17.849 1.00 22.77 C ATOM 682 CD2 LEU A 91 21.316 42.376 16.328 1.00 23.57 C ATOM 683 N GLY A 92 19.021 38.032 13.890 1.00 25.11 N ATOM 684 CA GLY A 92 18.676 36.607 13.886 1.00 24.76 C ATOM 685 C GLY A 92 17.206 36.405 13.589 1.00 25.72 C ATOM 686 O GLY A 92 16.566 37.253 12.962 1.00 24.40 O ATOM 687 N MET A 93 16.646 35.283 14.026 1.00 26.58 N ATOM 688 CA MET A 93 15.233 35.027 13.722 1.00 28.72 C ATOM 689 C MET A 93 14.593 34.024 14.653 1.00 28.92 C ATOM 690 O MET A 93 15.277 33.173 15.231 1.00 29.48 O ATOM 691 CB MET A 93 15.019 34.623 12.238 1.00 29.18 C ATOM 692 CG MET A 93 15.660 33.304 11.809 1.00 33.11 C ATOM 693 SD MET A 93 15.636 33.076 9.990 1.00 40.50 S ATOM 694 CE MET A 93 13.962 32.560 9.708 1.00 37.67 C ATOM 695 N LEU A 94 13.278 34.144 14.810 1.00 29.01 N ATOM 696 CA LEU A 94 12.506 33.156 15.553 1.00 30.00 C ATOM 697 C LEU A 94 11.801 32.247 14.556 1.00 30.90 C ATOM 698 O LEU A 94 11.070 32.735 13.699 1.00 30.26 O ATOM 699 CB LEU A 94 11.484 33.838 16.460 1.00 29.19 C ATOM 700 CG LEU A 94 10.751 32.998 17.514 1.00 30.25 C ATOM 701 CD1 LEU A 94 11.717 32.305 18.452 1.00 29.45 C ATOM 702 CD2 LEU A 94 9.800 33.894 18.320 1.00 28.35 C ATOM 703 N LYS A 95 12.034 30.934 14.648 1.00 32.44 N ATOM 704 CA LYS A 95 11.368 29.980 13.755 1.00 34.21 C ATOM 705 C LYS A 95 10.137 29.384 14.420 1.00 34.50 C ATOM 706 O LYS A 95 10.183 28.971 15.569 1.00 33.94 O ATOM 707 CB LYS A 95 12.338 28.865 13.332 1.00 35.22 C ATOM 708 CG LYS A 95 13.401 29.320 12.297 1.00 38.73 C ATOM 709 CD LYS A 95 14.737 28.595 12.495 1.00 44.84 C ATOM 710 CE LYS A 95 14.583 27.069 12.322 1.00 48.49 C ATOM 711 NZ LYS A 95 15.502 26.237 13.209 1.00 50.26 N ATOM 712 N MET A 96 9.029 29.351 13.698 1.00 35.87 N ATOM 713 CA MET A 96 7.770 28.871 14.259 1.00 37.62 C ATOM 714 C MET A 96 6.990 28.206 13.144 1.00 38.88 C ATOM 715 O MET A 96 7.303 28.406 11.969 1.00 38.99 O ATOM 716 CB MET A 96 6.915 30.046 14.783 1.00 36.87 C ATOM 717 CG MET A 96 7.445 30.766 16.014 1.00 36.05 C ATOM 718 SD MET A 96 6.661 32.397 16.227 1.00 32.47 S ATOM 719 CE MET A 96 7.289 33.359 14.839 1.00 33.43 C ATOM 720 N THR A 97 5.953 27.458 13.519 1.00 40.89 N ATOM 721 CA THR A 97 4.894 27.078 12.584 1.00 43.05 C ATOM 722 C THR A 97 3.560 27.461 13.229 1.00 43.77 C ATOM 723 O THR A 97 3.380 27.280 14.438 1.00 44.35 O ATOM 724 CB THR A 97 4.920 25.547 12.208 1.00 43.28 C ATOM 725 OG1 THR A 97 5.127 24.765 13.384 1.00 45.70 O ATOM 726 CG2 THR A 97 6.061 25.231 11.257 1.00 43.69 C ATOM 727 N ASP A 98 2.644 28.028 12.446 1.00 44.41 N ATOM 728 CA ASP A 98 1.321 28.342 12.967 1.00 45.30 C ATOM 729 C ASP A 98 0.228 27.653 12.151 1.00 46.22 C ATOM 730 O ASP A 98 0.517 26.775 11.331 1.00 46.61 O ATOM 731 CB ASP A 98 1.088 29.858 13.021 1.00 45.20 C ATOM 732 CG ASP A 98 0.949 30.472 11.652 1.00 45.80 C ATOM 733 OD1 ASP A 98 1.027 29.722 10.662 1.00 45.37 O ATOM 734 OD2 ASP A 98 0.764 31.704 11.562 1.00 44.84 O ATOM 735 N GLU A 99 -1.028 28.042 12.377 1.00 46.47 N ATOM 736 CA GLU A 99 -2.141 27.402 11.687 1.00 46.80 C ATOM 737 C GLU A 99 -2.006 27.467 10.147 1.00 47.27 C ATOM 738 O GLU A 99 -2.538 26.623 9.442 1.00 47.92 O ATOM 739 CB GLU A 99 -3.483 27.973 12.161 1.00 45.98 C ATOM 740 CG GLU A 99 -3.807 29.333 11.593 1.00 44.99 C ATOM 741 CD GLU A 99 -3.196 30.497 12.389 1.00 42.89 C ATOM 742 OE1 GLU A 99 -3.428 31.661 11.987 1.00 42.58 O ATOM 743 OE2 GLU A 99 -2.503 30.248 13.405 1.00 41.44 O ATOM 744 N SER A 100 -1.279 28.448 9.624 1.00 47.51 N ATOM 745 CA SER A 100 -1.091 28.565 8.177 1.00 47.27 C ATOM 746 C SER A 100 0.262 28.046 7.694 1.00 47.08 C ATOM 747 O SER A 100 0.694 28.388 6.592 1.00 47.42 O ATOM 748 CB SER A 100 -1.245 30.025 7.730 1.00 47.15 C ATOM 749 OG SER A 100 -2.525 30.535 8.068 1.00 48.79 O ATOM 750 N GLY A 101 0.939 27.237 8.507 1.00 46.73 N ATOM 751 CA GLY A 101 2.222 26.653 8.110 1.00 45.72 C ATOM 752 C GLY A 101 3.430 27.411 8.650 1.00 45.34 C ATOM 753 O GLY A 101 3.320 28.159 9.633 1.00 45.08 O ATOM 754 N VAL A 102 4.585 27.222 8.008 1.00 44.18 N ATOM 755 CA VAL A 102 5.851 27.802 8.476 1.00 43.13 C ATOM 756 C VAL A 102 5.795 29.319 8.668 1.00 42.11 C ATOM 757 O VAL A 102 5.204 30.039 7.858 1.00 41.60 O ATOM 758 CB VAL A 102 7.015 27.444 7.524 1.00 43.66 C ATOM 759 CG1 VAL A 102 8.164 28.428 7.684 1.00 43.30 C ATOM 760 CG2 VAL A 102 7.488 25.988 7.764 1.00 43.78 C ATOM 761 N ASP A 103 6.415 29.804 9.744 1.00 41.05 N ATOM 762 CA ASP A 103 6.375 31.242 10.062 1.00 39.44 C ATOM 763 C ASP A 103 7.649 31.697 10.761 1.00 37.83 C ATOM 764 O ASP A 103 7.784 31.562 11.973 1.00 38.58 O ATOM 765 CB ASP A 103 5.182 31.541 10.962 1.00 39.54 C ATOM 766 CG ASP A 103 4.926 33.029 11.126 1.00 40.16 C ATOM 767 OD1 ASP A 103 5.544 33.843 10.396 1.00 42.27 O ATOM 768 OD2 ASP A 103 4.081 33.379 11.977 1.00 38.14 O ATOM 769 N ALA A 104 8.591 32.226 9.995 1.00 35.52 N ATOM 770 CA ALA A 104 9.799 32.789 10.562 1.00 32.80 C ATOM 771 C ALA A 104 9.611 34.300 10.727 1.00 30.91 C ATOM 772 O ALA A 104 9.037 34.959 9.857 1.00 30.17 O ATOM 773 CB ALA A 104 10.955 32.514 9.651 1.00 33.11 C ATOM 774 N LYS A 105 10.079 34.838 11.847 1.00 29.57 N ATOM 775 CA LYS A 105 10.147 36.293 12.036 1.00 28.05 C ATOM 776 C LYS A 105 11.562 36.720 12.391 1.00 27.06 C ATOM 777 O LYS A 105 12.174 36.150 13.289 1.00 27.14 O ATOM 778 CB LYS A 105 9.142 36.750 13.090 1.00 27.30 C ATOM 779 CG LYS A 105 7.712 36.235 12.749 1.00 27.03 C ATOM 780 CD LYS A 105 6.645 37.016 13.447 1.00 26.83 C ATOM 781 CE LYS A 105 5.287 36.300 13.367 1.00 24.94 C ATOM 782 NZ LYS A 105 4.698 36.387 11.996 1.00 23.03 N ATOM 783 N LEU A 106 12.058 37.734 11.691 1.00 25.68 N ATOM 784 CA LEU A 106 13.374 38.275 11.962 1.00 25.87 C ATOM 785 C LEU A 106 13.354 39.143 13.222 1.00 25.22 C ATOM 786 O LEU A 106 12.314 39.719 13.598 1.00 24.89 O ATOM 787 CB LEU A 106 13.857 39.118 10.784 1.00 25.38 C ATOM 788 CG LEU A 106 14.443 38.394 9.564 1.00 27.94 C ATOM 789 CD1 LEU A 106 13.727 37.094 9.184 1.00 27.95 C ATOM 790 CD2 LEU A 106 14.567 39.332 8.388 1.00 26.61 C ATOM 791 N VAL A 107 14.523 39.257 13.838 1.00 23.51 N ATOM 792 CA VAL A 107 14.716 40.131 14.964 1.00 22.73 C ATOM 793 C VAL A 107 15.811 41.090 14.512 1.00 22.68 C ATOM 794 O VAL A 107 16.854 40.661 14.003 1.00 22.46 O ATOM 795 CB VAL A 107 15.080 39.338 16.238 1.00 22.27 C ATOM 796 CG1 VAL A 107 15.343 40.270 17.373 1.00 22.46 C ATOM 797 CG2 VAL A 107 13.939 38.318 16.594 1.00 23.92 C ATOM 798 N ALA A 108 15.553 42.392 14.645 1.00 21.45 N ATOM 799 CA ALA A 108 16.439 43.391 14.095 1.00 20.74 C ATOM 800 C ALA A 108 16.607 44.559 15.068 1.00 21.23 C ATOM 801 O ALA A 108 15.871 44.634 16.070 1.00 21.11 O ATOM 802 CB ALA A 108 15.903 43.883 12.721 1.00 19.22 C ATOM 803 N VAL A 109 17.600 45.423 14.790 1.00 20.09 N ATOM 804 CA VAL A 109 17.739 46.729 15.426 1.00 21.46 C ATOM 805 C VAL A 109 17.973 47.762 14.319 1.00 21.87 C ATOM 806 O VAL A 109 18.314 47.381 13.202 1.00 21.72 O ATOM 807 CB VAL A 109 18.928 46.784 16.409 1.00 20.91 C ATOM 808 CG1 VAL A 109 18.614 46.011 17.652 1.00 20.05 C ATOM 809 CG2 VAL A 109 20.208 46.218 15.733 1.00 22.26 C ATOM 810 N PRO A 110 17.804 49.068 14.626 1.00 22.19 N ATOM 811 CA PRO A 110 18.094 50.056 13.594 1.00 22.34 C ATOM 812 C PRO A 110 19.597 50.067 13.216 1.00 23.74 C ATOM 813 O PRO A 110 20.435 49.546 13.963 1.00 23.41 O ATOM 814 CB PRO A 110 17.717 51.405 14.280 1.00 22.83 C ATOM 815 CG PRO A 110 16.791 51.058 15.399 1.00 21.11 C ATOM 816 CD PRO A 110 17.289 49.695 15.870 1.00 21.07 C ATOM 817 N HIS A 111 19.905 50.663 12.062 1.00 24.43 N ATOM 818 CA HIS A 111 21.269 51.039 11.680 1.00 25.10 C ATOM 819 C HIS A 111 21.948 51.765 12.839 1.00 25.61 C ATOM 820 O HIS A 111 21.322 52.588 13.518 1.00 26.10 O ATOM 821 CB HIS A 111 21.182 51.975 10.450 1.00 24.91 C ATOM 822 CG HIS A 111 22.509 52.407 9.893 1.00 26.79 C ATOM 823 ND1 HIS A 111 23.070 51.820 8.770 1.00 29.91 N ATOM 824 CD2 HIS A 111 23.393 53.348 10.305 1.00 23.68 C ATOM 825 CE1 HIS A 111 24.235 52.393 8.514 1.00 26.42 C ATOM 826 NE2 HIS A 111 24.442 53.336 9.416 1.00 26.73 N ATOM 827 N ASP A 112 23.234 51.504 13.051 1.00 25.54 N ATOM 828 CA ASP A 112 23.979 52.129 14.147 1.00 25.57 C ATOM 829 C ASP A 112 23.942 53.667 14.222 1.00 25.64 C ATOM 830 O ASP A 112 24.009 54.219 15.303 1.00 25.60 O ATOM 831 CB ASP A 112 25.433 51.655 14.148 1.00 26.15 C ATOM 832 CG ASP A 112 25.577 50.191 14.586 1.00 25.67 C ATOM 833 OD1 ASP A 112 24.592 49.558 15.018 1.00 29.82 O ATOM 834 OD2 ASP A 112 26.687 49.675 14.528 1.00 26.95 O ATOM 835 N LYS A 113 23.866 54.355 13.095 1.00 25.60 N ATOM 836 CA LYS A 113 23.786 55.819 13.100 1.00 26.31 C ATOM 837 C LYS A 113 22.358 56.299 13.405 1.00 26.01 C ATOM 838 O LYS A 113 22.150 57.398 13.891 1.00 27.30 O ATOM 839 CB LYS A 113 24.288 56.390 11.768 1.00 26.96 C ATOM 840 N VAL A 114 21.370 55.453 13.158 1.00 25.69 N ATOM 841 CA VAL A 114 19.998 55.764 13.562 1.00 24.61 C ATOM 842 C VAL A 114 19.806 55.525 15.065 1.00 25.10 C ATOM 843 O VAL A 114 19.249 56.379 15.773 1.00 24.38 O ATOM 844 CB VAL A 114 19.001 54.950 12.751 1.00 25.32 C ATOM 845 CG1 VAL A 114 17.528 55.198 13.246 1.00 23.89 C ATOM 846 CG2 VAL A 114 19.202 55.234 11.260 1.00 22.62 C ATOM 847 N CYS A 115 20.318 54.395 15.563 1.00 24.30 N ATOM 848 CA CYS A 115 20.191 54.054 16.978 1.00 24.45 C ATOM 849 C CYS A 115 21.523 53.611 17.614 1.00 25.28 C ATOM 850 O CYS A 115 21.821 52.409 17.705 1.00 25.35 O ATOM 851 CB CYS A 115 19.111 52.977 17.168 1.00 24.20 C ATOM 852 SG CYS A 115 18.644 52.733 18.908 1.00 23.28 S ATOM 853 N PRO A 116 22.343 54.583 18.036 1.00 25.64 N ATOM 854 CA PRO A 116 23.601 54.246 18.715 1.00 25.83 C ATOM 855 C PRO A 116 23.382 53.386 19.946 1.00 26.76 C ATOM 856 O PRO A 116 24.274 52.606 20.303 1.00 27.28 O ATOM 857 CB PRO A 116 24.150 55.613 19.142 1.00 25.73 C ATOM 858 CG PRO A 116 23.576 56.573 18.005 1.00 26.37 C ATOM 859 CD PRO A 116 22.177 56.038 17.826 1.00 24.59 C ATOM 860 N MET A 117 22.213 53.510 20.569 1.00 25.92 N ATOM 861 CA MET A 117 21.880 52.798 21.806 1.00 25.99 C ATOM 862 C MET A 117 21.872 51.286 21.630 1.00 26.46 C ATOM 863 O MET A 117 22.001 50.553 22.613 1.00 25.60 O ATOM 864 CB MET A 117 20.492 53.211 22.307 1.00 25.61 C ATOM 865 CG MET A 117 20.329 54.735 22.551 1.00 25.77 C ATOM 866 SD MET A 117 19.862 55.666 21.073 1.00 23.51 S ATOM 867 CE MET A 117 20.351 57.314 21.549 1.00 23.67 C ATOM 868 N THR A 118 21.643 50.816 20.396 1.00 26.44 N ATOM 869 CA THR A 118 21.572 49.368 20.159 1.00 26.45 C ATOM 870 C THR A 118 22.833 48.825 19.435 1.00 26.58 C ATOM 871 O THR A 118 22.882 47.643 19.071 1.00 25.87 O ATOM 872 CB THR A 118 20.255 48.931 19.388 1.00 26.23 C ATOM 873 OG1 THR A 118 20.061 49.752 18.255 1.00 25.67 O ATOM 874 CG2 THR A 118 18.975 49.004 20.277 1.00 24.93 C ATOM 875 N ALA A 119 23.848 49.673 19.264 1.00 26.81 N ATOM 876 CA ALA A 119 25.069 49.285 18.509 1.00 27.89 C ATOM 877 C ALA A 119 25.785 48.057 19.057 1.00 28.60 C ATOM 878 O ALA A 119 26.365 47.295 18.299 1.00 28.79 O ATOM 879 CB ALA A 119 26.024 50.442 18.375 1.00 27.47 C ATOM 880 N ASN A 120 25.712 47.837 20.364 1.00 30.19 N ATOM 881 CA ASN A 120 26.394 46.697 20.978 1.00 31.83 C ATOM 882 C ASN A 120 25.633 45.400 20.871 1.00 31.62 C ATOM 883 O ASN A 120 26.124 44.389 21.335 1.00 30.93 O ATOM 884 CB ASN A 120 26.733 46.965 22.447 1.00 33.05 C ATOM 885 CG ASN A 120 27.805 48.055 22.605 1.00 38.99 C ATOM 886 OD1 ASN A 120 28.787 48.097 21.842 1.00 44.64 O ATOM 887 ND2 ASN A 120 27.610 48.953 23.578 1.00 43.69 N ATOM 888 N LEU A 121 24.427 45.424 20.298 1.00 30.32 N ATOM 889 CA LEU A 121 23.756 44.177 19.945 1.00 30.28 C ATOM 890 C LEU A 121 24.232 43.750 18.545 1.00 30.14 C ATOM 891 O LEU A 121 23.838 44.354 17.529 1.00 29.66 O ATOM 892 CB LEU A 121 22.221 44.314 19.994 1.00 29.43 C ATOM 893 CG LEU A 121 21.655 44.833 21.312 1.00 29.47 C ATOM 894 CD1 LEU A 121 20.133 45.148 21.240 1.00 28.60 C ATOM 895 CD2 LEU A 121 21.981 43.867 22.439 1.00 30.01 C ATOM 896 N LYS A 122 25.104 42.739 18.514 1.00 30.23 N ATOM 897 CA LYS A 122 25.692 42.242 17.272 1.00 30.77 C ATOM 898 C LYS A 122 24.963 41.015 16.720 1.00 30.31 C ATOM 899 O LYS A 122 24.994 40.748 15.520 1.00 30.97 O ATOM 900 CB LYS A 122 27.150 41.856 17.492 1.00 31.10 C ATOM 901 CG LYS A 122 27.932 42.857 18.270 1.00 34.55 C ATOM 902 CD LYS A 122 28.254 44.068 17.435 1.00 37.21 C ATOM 903 CE LYS A 122 29.578 44.637 17.921 1.00 41.85 C ATOM 904 NZ LYS A 122 29.647 46.122 17.779 1.00 45.04 N ATOM 905 N SER A 123 24.353 40.234 17.590 1.00 28.89 N ATOM 906 CA SER A 123 23.593 39.080 17.119 1.00 29.25 C ATOM 907 C SER A 123 22.504 38.756 18.130 1.00 29.01 C ATOM 908 O SER A 123 22.439 39.361 19.199 1.00 29.07 O ATOM 909 CB SER A 123 24.514 37.847 16.919 1.00 28.38 C ATOM 910 OG SER A 123 24.909 37.328 18.187 1.00 30.05 O ATOM 911 N ILE A 124 21.657 37.797 17.779 1.00 30.11 N ATOM 912 CA ILE A 124 20.560 37.354 18.616 1.00 30.40 C ATOM 913 C ILE A 124 21.044 36.980 20.043 1.00 31.66 C ATOM 914 O ILE A 124 20.308 37.162 21.020 1.00 30.63 O ATOM 915 CB ILE A 124 19.830 36.168 17.921 1.00 30.97 C ATOM 916 CG1 ILE A 124 18.526 35.811 18.648 1.00 31.32 C ATOM 917 CG2 ILE A 124 20.760 34.954 17.775 1.00 29.74 C ATOM 918 CD1 ILE A 124 17.435 36.836 18.440 1.00 33.00 C ATOM 919 N ASP A 125 22.286 36.472 20.155 1.00 32.15 N ATOM 920 CA ASP A 125 22.858 36.041 21.449 1.00 32.32 C ATOM 921 C ASP A 125 23.117 37.191 22.390 1.00 31.43 C ATOM 922 O ASP A 125 23.291 36.996 23.591 1.00 30.73 O ATOM 923 CB ASP A 125 24.180 35.287 21.239 1.00 33.54 C ATOM 924 CG ASP A 125 24.027 34.128 20.295 1.00 36.42 C ATOM 925 OD1 ASP A 125 23.000 33.427 20.372 1.00 38.93 O ATOM 926 OD2 ASP A 125 24.912 33.948 19.440 1.00 41.72 O ATOM 927 N ASP A 126 23.151 38.402 21.849 1.00 30.57 N ATOM 928 CA ASP A 126 23.341 39.566 22.696 1.00 29.73 C ATOM 929 C ASP A 126 22.028 40.092 23.290 1.00 29.14 C ATOM 930 O ASP A 126 22.059 40.903 24.202 1.00 28.18 O ATOM 931 CB ASP A 126 24.023 40.693 21.927 1.00 29.86 C ATOM 932 CG ASP A 126 25.409 40.308 21.440 1.00 31.45 C ATOM 933 OD1 ASP A 126 26.168 39.758 22.245 1.00 32.98 O ATOM 934 OD2 ASP A 126 25.732 40.556 20.265 1.00 29.33 O ATOM 935 N VAL A 127 20.891 39.663 22.750 1.00 28.12 N ATOM 936 CA VAL A 127 19.600 40.132 23.270 1.00 27.54 C ATOM 937 C VAL A 127 19.398 39.543 24.680 1.00 27.24 C ATOM 938 O VAL A 127 19.603 38.361 24.881 1.00 26.18 O ATOM 939 CB VAL A 127 18.442 39.723 22.332 1.00 27.46 C ATOM 940 CG1 VAL A 127 17.094 40.157 22.913 1.00 26.88 C ATOM 941 CG2 VAL A 127 18.645 40.294 20.923 1.00 27.36 C ATOM 942 N PRO A 128 19.011 40.375 25.658 1.00 27.18 N ATOM 943 CA PRO A 128 18.809 39.845 26.999 1.00 27.22 C ATOM 944 C PRO A 128 17.902 38.614 26.998 1.00 27.86 C ATOM 945 O PRO A 128 16.919 38.562 26.249 1.00 27.80 O ATOM 946 CB PRO A 128 18.130 41.002 27.724 1.00 26.62 C ATOM 947 CG PRO A 128 18.769 42.235 27.104 1.00 28.03 C ATOM 948 CD PRO A 128 18.898 41.850 25.616 1.00 27.41 C ATOM 949 N ALA A 129 18.221 37.627 27.834 1.00 27.80 N ATOM 950 CA ALA A 129 17.410 36.415 27.870 1.00 28.35 C ATOM 951 C ALA A 129 15.934 36.714 28.217 1.00 28.08 C ATOM 952 O ALA A 129 15.010 36.049 27.696 1.00 27.99 O ATOM 953 CB ALA A 129 18.005 35.402 28.850 1.00 28.21 C ATOM 954 N TYR A 130 15.720 37.696 29.098 1.00 27.53 N ATOM 955 CA TYR A 130 14.362 38.016 29.546 1.00 27.52 C ATOM 956 C TYR A 130 13.523 38.512 28.358 1.00 27.66 C ATOM 957 O TYR A 130 12.357 38.146 28.241 1.00 27.90 O ATOM 958 CB TYR A 130 14.350 39.024 30.720 1.00 27.57 C ATOM 959 CG TYR A 130 14.359 40.464 30.262 1.00 27.15 C ATOM 960 CD1 TYR A 130 13.183 41.099 29.871 1.00 29.10 C ATOM 961 CD2 TYR A 130 15.554 41.175 30.181 1.00 27.46 C ATOM 962 CE1 TYR A 130 13.203 42.410 29.409 1.00 28.74 C ATOM 963 CE2 TYR A 130 15.584 42.465 29.730 1.00 28.56 C ATOM 964 CZ TYR A 130 14.398 43.072 29.348 1.00 29.54 C ATOM 965 OH TYR A 130 14.443 44.369 28.916 1.00 34.94 O ATOM 966 N LEU A 131 14.121 39.315 27.477 1.00 27.44 N ATOM 967 CA LEU A 131 13.440 39.796 26.273 1.00 27.71 C ATOM 968 C LEU A 131 13.166 38.664 25.271 1.00 27.69 C ATOM 969 O LEU A 131 12.027 38.483 24.788 1.00 27.08 O ATOM 970 CB LEU A 131 14.240 40.910 25.608 1.00 27.68 C ATOM 971 CG LEU A 131 13.453 41.705 24.555 1.00 29.36 C ATOM 972 CD1 LEU A 131 12.160 42.314 25.137 1.00 28.92 C ATOM 973 CD2 LEU A 131 14.328 42.790 23.943 1.00 29.57 C ATOM 974 N LYS A 132 14.211 37.901 24.953 1.00 27.29 N ATOM 975 CA LYS A 132 14.038 36.681 24.180 1.00 27.37 C ATOM 976 C LYS A 132 12.846 35.869 24.734 1.00 26.26 C ATOM 977 O LYS A 132 11.948 35.517 23.986 1.00 26.14 O ATOM 978 CB LYS A 132 15.336 35.843 24.172 1.00 28.31 C ATOM 979 CG LYS A 132 16.386 36.314 23.170 1.00 30.56 C ATOM 980 CD LYS A 132 17.511 35.269 22.990 1.00 33.45 C ATOM 981 CE LYS A 132 18.727 35.625 23.835 1.00 35.02 C ATOM 982 NZ LYS A 132 19.939 34.745 23.591 1.00 37.99 N ATOM 983 N ASP A 133 12.839 35.580 26.034 1.00 25.23 N ATOM 984 CA ASP A 133 11.757 34.796 26.662 1.00 24.89 C ATOM 985 C ASP A 133 10.358 35.406 26.531 1.00 24.44 C ATOM 986 O ASP A 133 9.383 34.687 26.328 1.00 23.26 O ATOM 987 CB ASP A 133 12.027 34.569 28.159 1.00 24.84 C ATOM 988 CG ASP A 133 13.166 33.593 28.417 1.00 28.52 C ATOM 989 OD1 ASP A 133 13.562 32.849 27.490 1.00 31.06 O ATOM 990 OD2 ASP A 133 13.678 33.593 29.552 1.00 31.64 O ATOM 991 N GLN A 134 10.272 36.724 26.710 1.00 24.07 N ATOM 992 CA GLN A 134 9.018 37.455 26.504 1.00 24.53 C ATOM 993 C GLN A 134 8.504 37.351 25.062 1.00 24.16 C ATOM 994 O GLN A 134 7.301 37.181 24.843 1.00 23.95 O ATOM 995 CB GLN A 134 9.182 38.943 26.874 1.00 24.01 C ATOM 996 CG GLN A 134 9.537 39.176 28.333 1.00 25.53 C ATOM 997 CD GLN A 134 9.354 40.607 28.741 1.00 25.83 C ATOM 998 OE1 GLN A 134 9.357 40.934 29.927 1.00 27.07 O ATOM 999 NE2 GLN A 134 9.165 41.470 27.766 1.00 26.58 N ATOM 1000 N ILE A 135 9.399 37.479 24.086 1.00 23.99 N ATOM 1001 CA ILE A 135 8.997 37.405 22.674 1.00 24.11 C ATOM 1002 C ILE A 135 8.444 36.023 22.366 1.00 25.38 C ATOM 1003 O ILE A 135 7.381 35.878 21.727 1.00 25.45 O ATOM 1004 CB ILE A 135 10.163 37.749 21.719 1.00 24.40 C ATOM 1005 CG1 ILE A 135 10.565 39.216 21.892 1.00 23.65 C ATOM 1006 CG2 ILE A 135 9.834 37.373 20.230 1.00 20.81 C ATOM 1007 CD1 ILE A 135 11.932 39.561 21.290 1.00 21.20 C ATOM 1008 N LYS A 136 9.138 35.006 22.859 1.00 25.73 N ATOM 1009 CA LYS A 136 8.711 33.639 22.643 1.00 26.35 C ATOM 1010 C LYS A 136 7.365 33.315 23.315 1.00 25.70 C ATOM 1011 O LYS A 136 6.482 32.730 22.684 1.00 24.73 O ATOM 1012 CB LYS A 136 9.839 32.696 23.079 1.00 27.12 C ATOM 1013 CG LYS A 136 9.491 31.210 23.059 1.00 30.98 C ATOM 1014 CD LYS A 136 10.754 30.398 23.454 1.00 38.08 C ATOM 1015 CE LYS A 136 10.456 28.907 23.637 1.00 40.93 C ATOM 1016 NZ LYS A 136 9.113 28.719 24.265 1.00 44.61 N ATOM 1017 N HIS A 137 7.192 33.740 24.575 1.00 25.25 N ATOM 1018 CA HIS A 137 5.900 33.625 25.278 1.00 24.60 C ATOM 1019 C HIS A 137 4.757 34.338 24.511 1.00 23.92 C ATOM 1020 O HIS A 137 3.645 33.784 24.345 1.00 23.75 O ATOM 1021 CB HIS A 137 6.011 34.201 26.735 1.00 24.77 C ATOM 1022 CG HIS A 137 4.761 34.005 27.551 1.00 25.29 C ATOM 1023 ND1 HIS A 137 3.872 35.028 27.824 1.00 25.11 N ATOM 1024 CD2 HIS A 137 4.228 32.888 28.111 1.00 22.39 C ATOM 1025 CE1 HIS A 137 2.856 34.556 28.526 1.00 22.79 C ATOM 1026 NE2 HIS A 137 3.047 33.259 28.714 1.00 26.13 N ATOM 1027 N PHE A 138 5.022 35.573 24.066 1.00 23.23 N ATOM 1028 CA PHE A 138 4.054 36.330 23.261 1.00 23.01 C ATOM 1029 C PHE A 138 3.523 35.499 22.087 1.00 23.59 C ATOM 1030 O PHE A 138 2.313 35.315 21.948 1.00 22.99 O ATOM 1031 CB PHE A 138 4.588 37.688 22.737 1.00 21.76 C ATOM 1032 CG PHE A 138 3.581 38.410 21.879 1.00 22.65 C ATOM 1033 CD1 PHE A 138 2.538 39.114 22.458 1.00 20.19 C ATOM 1034 CD2 PHE A 138 3.626 38.326 20.481 1.00 22.75 C ATOM 1035 CE1 PHE A 138 1.566 39.746 21.672 1.00 20.14 C ATOM 1036 CE2 PHE A 138 2.661 38.960 19.693 1.00 18.78 C ATOM 1037 CZ PHE A 138 1.624 39.658 20.306 1.00 18.64 C ATOM 1038 N PHE A 139 4.418 34.995 21.238 1.00 24.32 N ATOM 1039 CA PHE A 139 3.966 34.206 20.091 1.00 25.35 C ATOM 1040 C PHE A 139 3.302 32.873 20.431 1.00 26.07 C ATOM 1041 O PHE A 139 2.369 32.435 19.751 1.00 26.11 O ATOM 1042 CB PHE A 139 5.084 34.060 19.068 1.00 25.90 C ATOM 1043 CG PHE A 139 5.393 35.342 18.370 1.00 27.31 C ATOM 1044 CD1 PHE A 139 4.535 35.827 17.393 1.00 27.14 C ATOM 1045 CD2 PHE A 139 6.515 36.088 18.718 1.00 26.77 C ATOM 1046 CE1 PHE A 139 4.796 37.021 16.763 1.00 26.81 C ATOM 1047 CE2 PHE A 139 6.786 37.279 18.088 1.00 27.38 C ATOM 1048 CZ PHE A 139 5.915 37.750 17.096 1.00 27.03 C ATOM 1049 N GLU A 140 3.747 32.247 21.508 1.00 27.11 N ATOM 1050 CA GLU A 140 3.095 31.047 22.009 1.00 28.38 C ATOM 1051 C GLU A 140 1.679 31.261 22.518 1.00 27.76 C ATOM 1052 O GLU A 140 0.889 30.341 22.460 1.00 28.49 O ATOM 1053 CB GLU A 140 3.937 30.396 23.110 1.00 28.39 C ATOM 1054 CG GLU A 140 5.150 29.725 22.513 1.00 32.77 C ATOM 1055 CD GLU A 140 5.926 28.953 23.534 1.00 35.86 C ATOM 1056 OE1 GLU A 140 5.978 29.397 24.707 1.00 36.53 O ATOM 1057 OE2 GLU A 140 6.491 27.914 23.149 1.00 38.06 O ATOM 1058 N GLN A 141 1.358 32.463 22.996 1.00 27.27 N ATOM 1059 CA GLN A 141 0.098 32.706 23.718 1.00 26.49 C ATOM 1060 C GLN A 141 -0.891 33.712 23.103 1.00 26.43 C ATOM 1061 O GLN A 141 -2.081 33.621 23.367 1.00 26.26 O ATOM 1062 CB GLN A 141 0.390 33.129 25.170 1.00 26.70 C ATOM 1063 CG GLN A 141 1.054 32.012 26.000 1.00 25.87 C ATOM 1064 CD GLN A 141 0.143 30.811 26.137 1.00 27.04 C ATOM 1065 OE1 GLN A 141 -1.078 30.964 26.127 1.00 26.18 O ATOM 1066 NE2 GLN A 141 0.725 29.604 26.246 1.00 24.08 N ATOM 1067 N TYR A 142 -0.431 34.650 22.283 1.00 25.24 N ATOM 1068 CA TYR A 142 -1.324 35.723 21.835 1.00 25.93 C ATOM 1069 C TYR A 142 -2.589 35.291 21.046 1.00 26.85 C ATOM 1070 O TYR A 142 -3.600 36.023 21.036 1.00 25.86 O ATOM 1071 CB TYR A 142 -0.550 36.851 21.122 1.00 24.57 C ATOM 1072 CG TYR A 142 -0.237 36.657 19.645 1.00 24.88 C ATOM 1073 CD1 TYR A 142 -0.614 37.636 18.697 1.00 23.74 C ATOM 1074 CD2 TYR A 142 0.484 35.536 19.189 1.00 23.36 C ATOM 1075 CE1 TYR A 142 -0.311 37.485 17.323 1.00 24.35 C ATOM 1076 CE2 TYR A 142 0.795 35.381 17.840 1.00 23.20 C ATOM 1077 CZ TYR A 142 0.408 36.350 16.908 1.00 24.71 C ATOM 1078 OH TYR A 142 0.726 36.189 15.570 1.00 23.16 O ATOM 1079 N LYS A 143 -2.538 34.106 20.425 1.00 27.36 N ATOM 1080 CA LYS A 143 -3.656 33.620 19.616 1.00 28.59 C ATOM 1081 C LYS A 143 -4.517 32.628 20.383 1.00 28.24 C ATOM 1082 O LYS A 143 -5.450 32.069 19.814 1.00 28.26 O ATOM 1083 CB LYS A 143 -3.179 32.956 18.314 1.00 28.24 C ATOM 1084 CG LYS A 143 -2.845 33.904 17.177 1.00 30.18 C ATOM 1085 CD LYS A 143 -2.035 33.123 16.136 1.00 31.30 C ATOM 1086 CE LYS A 143 -2.057 33.788 14.782 1.00 32.46 C ATOM 1087 NZ LYS A 143 -1.094 33.108 13.850 1.00 31.69 N ATOM 1088 N ALA A 144 -4.214 32.446 21.666 1.00 28.11 N ATOM 1089 CA ALA A 144 -4.911 31.489 22.514 1.00 28.53 C ATOM 1090 C ALA A 144 -6.436 31.578 22.439 1.00 29.33 C ATOM 1091 O ALA A 144 -7.109 30.576 22.625 1.00 29.02 O ATOM 1092 CB ALA A 144 -4.446 31.610 23.979 1.00 27.54 C ATOM 1093 N LEU A 145 -6.986 32.755 22.160 1.00 30.11 N ATOM 1094 CA LEU A 145 -8.442 32.926 22.243 1.00 31.34 C ATOM 1095 C LEU A 145 -9.115 33.091 20.884 1.00 33.19 C ATOM 1096 O LEU A 145 -10.278 33.527 20.799 1.00 34.02 O ATOM 1097 CB LEU A 145 -8.836 34.068 23.184 1.00 30.04 C ATOM 1098 CG LEU A 145 -8.451 33.803 24.646 1.00 29.77 C ATOM 1099 CD1 LEU A 145 -8.766 35.020 25.539 1.00 27.97 C ATOM 1100 CD2 LEU A 145 -9.158 32.558 25.178 1.00 28.92 C ATOM 1101 N GLU A 146 -8.404 32.722 19.826 1.00 34.54 N ATOM 1102 CA GLU A 146 -9.007 32.685 18.497 1.00 36.61 C ATOM 1103 C GLU A 146 -9.127 31.241 18.018 1.00 36.98 C ATOM 1104 O GLU A 146 -8.131 30.520 17.940 1.00 37.28 O ATOM 1105 CB GLU A 146 -8.198 33.548 17.528 1.00 36.66 C ATOM 1106 CG GLU A 146 -8.473 35.038 17.752 1.00 39.16 C ATOM 1107 CD GLU A 146 -7.212 35.867 17.769 1.00 41.76 C ATOM 1108 OE1 GLU A 146 -6.523 35.925 16.724 1.00 46.57 O ATOM 1109 OE2 GLU A 146 -6.907 36.480 18.809 1.00 41.40 O ATOM 1110 N LYS A 147 -10.355 30.810 17.733 1.00 38.45 N ATOM 1111 CA LYS A 147 -10.597 29.436 17.247 1.00 39.30 C ATOM 1112 C LYS A 147 -9.881 29.202 15.918 1.00 39.80 C ATOM 1113 O LYS A 147 -9.942 30.031 15.004 1.00 39.70 O ATOM 1114 CB LYS A 147 -12.107 29.141 17.099 1.00 39.10 C ATOM 1115 N GLY A 148 -9.196 28.069 15.813 1.00 40.78 N ATOM 1116 CA GLY A 148 -8.523 27.724 14.574 1.00 41.89 C ATOM 1117 C GLY A 148 -7.129 28.302 14.423 1.00 42.81 C ATOM 1118 O GLY A 148 -6.505 28.152 13.366 1.00 43.25 O ATOM 1119 N LYS A 149 -6.631 28.970 15.467 1.00 42.74 N ATOM 1120 CA LYS A 149 -5.309 29.594 15.395 1.00 42.54 C ATOM 1121 C LYS A 149 -4.401 29.040 16.468 1.00 42.14 C ATOM 1122 O LYS A 149 -4.838 28.797 17.587 1.00 42.29 O ATOM 1123 CB LYS A 149 -5.433 31.099 15.551 1.00 42.68 C ATOM 1124 CG LYS A 149 -6.172 31.762 14.419 1.00 43.87 C ATOM 1125 CD LYS A 149 -6.153 33.241 14.672 1.00 47.65 C ATOM 1126 CE LYS A 149 -6.746 34.013 13.534 1.00 49.81 C ATOM 1127 NZ LYS A 149 -6.712 35.448 13.904 1.00 50.78 N ATOM 1128 N TRP A 150 -3.132 28.836 16.131 1.00 41.69 N ATOM 1129 CA TRP A 150 -2.195 28.252 17.077 1.00 41.16 C ATOM 1130 C TRP A 150 -0.741 28.515 16.617 1.00 40.09 C ATOM 1131 O TRP A 150 -0.498 28.906 15.467 1.00 39.90 O ATOM 1132 CB TRP A 150 -2.482 26.751 17.256 1.00 42.09 C ATOM 1133 CG TRP A 150 -2.424 25.994 15.941 1.00 44.48 C ATOM 1134 CD1 TRP A 150 -3.473 25.731 15.085 1.00 46.23 C ATOM 1135 CD2 TRP A 150 -1.253 25.441 15.319 1.00 47.04 C ATOM 1136 NE1 TRP A 150 -3.018 25.043 13.976 1.00 47.57 N ATOM 1137 CE2 TRP A 150 -1.664 24.847 14.098 1.00 48.31 C ATOM 1138 CE3 TRP A 150 0.104 25.389 15.673 1.00 47.74 C ATOM 1139 CZ2 TRP A 150 -0.759 24.213 13.228 1.00 49.44 C ATOM 1140 CZ3 TRP A 150 1.004 24.752 14.797 1.00 48.88 C ATOM 1141 CH2 TRP A 150 0.565 24.178 13.597 1.00 48.25 C ATOM 1142 N VAL A 151 0.209 28.336 17.527 1.00 38.25 N ATOM 1143 CA VAL A 151 1.612 28.584 17.228 1.00 37.22 C ATOM 1144 C VAL A 151 2.497 27.650 18.003 1.00 37.01 C ATOM 1145 O VAL A 151 2.385 27.567 19.224 1.00 37.18 O ATOM 1146 CB VAL A 151 2.064 29.984 17.683 1.00 36.92 C ATOM 1147 CG1 VAL A 151 3.609 30.090 17.614 1.00 36.17 C ATOM 1148 CG2 VAL A 151 1.374 31.052 16.887 1.00 37.01 C ATOM 1149 N LYS A 152 3.411 26.983 17.306 1.00 37.00 N ATOM 1150 CA LYS A 152 4.498 26.276 17.985 1.00 37.07 C ATOM 1151 C LYS A 152 5.842 26.914 17.600 1.00 36.86 C ATOM 1152 O LYS A 152 6.130 27.120 16.424 1.00 36.56 O ATOM 1153 CB LYS A 152 4.462 24.764 17.671 1.00 37.12 C ATOM 1154 N VAL A 153 6.626 27.265 18.610 1.00 37.55 N ATOM 1155 CA VAL A 153 7.952 27.825 18.420 1.00 38.67 C ATOM 1156 C VAL A 153 8.974 26.699 18.221 1.00 39.79 C ATOM 1157 O VAL A 153 9.112 25.831 19.090 1.00 40.45 O ATOM 1158 CB VAL A 153 8.383 28.679 19.647 1.00 38.52 C ATOM 1159 CG1 VAL A 153 9.857 29.052 19.544 1.00 38.07 C ATOM 1160 CG2 VAL A 153 7.497 29.925 19.786 1.00 37.74 C ATOM 1161 N GLU A 154 9.687 26.708 17.090 1.00 40.04 N ATOM 1162 CA GLU A 154 10.734 25.724 16.843 1.00 40.39 C ATOM 1163 C GLU A 154 12.069 26.146 17.482 1.00 39.58 C ATOM 1164 O GLU A 154 12.725 25.346 18.138 1.00 39.63 O ATOM 1165 CB GLU A 154 10.906 25.461 15.339 1.00 40.95 C ATOM 1166 CG GLU A 154 9.594 25.360 14.525 1.00 44.59 C ATOM 1167 CD GLU A 154 8.715 24.132 14.863 1.00 51.27 C ATOM 1168 OE1 GLU A 154 9.167 23.234 15.624 1.00 52.36 O ATOM 1169 OE2 GLU A 154 7.557 24.071 14.356 1.00 52.58 O ATOM 1170 N GLY A 155 12.483 27.394 17.293 1.00 38.48 N ATOM 1171 CA GLY A 155 13.721 27.866 17.929 1.00 37.24 C ATOM 1172 C GLY A 155 14.311 29.122 17.304 1.00 36.18 C ATOM 1173 O GLY A 155 13.750 29.666 16.353 1.00 36.76 O ATOM 1174 N TRP A 156 15.439 29.571 17.847 1.00 34.89 N ATOM 1175 CA TRP A 156 16.155 30.742 17.367 1.00 34.38 C ATOM 1176 C TRP A 156 17.174 30.356 16.302 1.00 34.36 C ATOM 1177 O TRP A 156 17.674 29.239 16.305 1.00 35.16 O ATOM 1178 CB TRP A 156 16.906 31.397 18.520 1.00 33.47 C ATOM 1179 CG TRP A 156 16.018 31.843 19.632 1.00 33.27 C ATOM 1180 CD1 TRP A 156 15.803 31.203 20.822 1.00 33.92 C ATOM 1181 CD2 TRP A 156 15.201 33.031 19.662 1.00 30.60 C ATOM 1182 NE1 TRP A 156 14.910 31.924 21.596 1.00 32.30 N ATOM 1183 CE2 TRP A 156 14.523 33.044 20.909 1.00 31.40 C ATOM 1184 CE3 TRP A 156 14.973 34.070 18.760 1.00 31.26 C ATOM 1185 CZ2 TRP A 156 13.630 34.062 21.273 1.00 30.75 C ATOM 1186 CZ3 TRP A 156 14.095 35.104 19.135 1.00 32.01 C ATOM 1187 CH2 TRP A 156 13.444 35.090 20.380 1.00 29.67 C ATOM 1188 N ASP A 157 17.469 31.272 15.386 1.00 33.86 N ATOM 1189 CA ASP A 157 18.577 31.106 14.437 1.00 32.34 C ATOM 1190 C ASP A 157 19.263 32.457 14.275 1.00 31.51 C ATOM 1191 O ASP A 157 18.729 33.478 14.724 1.00 31.36 O ATOM 1192 CB ASP A 157 18.063 30.581 13.096 1.00 32.87 C ATOM 1193 CG ASP A 157 19.050 29.623 12.430 1.00 33.29 C ATOM 1194 OD1 ASP A 157 20.267 29.756 12.646 1.00 34.65 O ATOM 1195 OD2 ASP A 157 18.612 28.741 11.682 1.00 34.01 O ATOM 1196 N GLY A 158 20.444 32.474 13.656 1.00 29.77 N ATOM 1197 CA GLY A 158 21.324 33.641 13.683 1.00 27.83 C ATOM 1198 C GLY A 158 21.263 34.514 12.449 1.00 27.09 C ATOM 1199 O GLY A 158 20.326 34.406 11.659 1.00 26.51 O ATOM 1200 N ILE A 159 22.272 35.374 12.288 1.00 26.02 N ATOM 1201 CA ILE A 159 22.293 36.402 11.250 1.00 26.35 C ATOM 1202 C ILE A 159 22.280 35.847 9.827 1.00 26.41 C ATOM 1203 O ILE A 159 21.581 36.376 8.946 1.00 25.21 O ATOM 1204 CB ILE A 159 23.504 37.366 11.418 1.00 26.70 C ATOM 1205 CG1 ILE A 159 23.361 38.233 12.685 1.00 28.08 C ATOM 1206 CG2 ILE A 159 23.650 38.301 10.246 1.00 26.01 C ATOM 1207 CD1 ILE A 159 24.668 39.003 13.012 1.00 28.81 C ATOM 1208 N ASP A 160 23.038 34.772 9.597 1.00 26.15 N ATOM 1209 CA ASP A 160 23.112 34.177 8.249 1.00 25.96 C ATOM 1210 C ASP A 160 21.756 33.642 7.817 1.00 24.88 C ATOM 1211 O ASP A 160 21.374 33.777 6.665 1.00 24.73 O ATOM 1212 CB ASP A 160 24.116 33.010 8.205 1.00 26.67 C ATOM 1213 CG ASP A 160 25.541 33.433 8.520 1.00 29.50 C ATOM 1214 OD1 ASP A 160 25.934 34.574 8.239 1.00 30.48 O ATOM 1215 OD2 ASP A 160 26.293 32.584 9.050 1.00 35.45 O ATOM 1216 N ALA A 161 21.032 32.999 8.728 1.00 23.99 N ATOM 1217 CA ALA A 161 19.680 32.532 8.392 1.00 23.50 C ATOM 1218 C ALA A 161 18.751 33.702 8.082 1.00 23.21 C ATOM 1219 O ALA A 161 17.935 33.606 7.165 1.00 24.21 O ATOM 1220 CB ALA A 161 19.115 31.701 9.495 1.00 23.26 C ATOM 1221 N ALA A 162 18.894 34.805 8.824 1.00 23.21 N ATOM 1222 CA ALA A 162 18.103 36.027 8.571 1.00 23.79 C ATOM 1223 C ALA A 162 18.362 36.572 7.170 1.00 23.81 C ATOM 1224 O ALA A 162 17.440 36.955 6.439 1.00 23.83 O ATOM 1225 CB ALA A 162 18.394 37.118 9.643 1.00 22.09 C ATOM 1226 N HIS A 163 19.642 36.604 6.796 1.00 24.63 N ATOM 1227 CA HIS A 163 20.029 37.073 5.475 1.00 24.48 C ATOM 1228 C HIS A 163 19.483 36.211 4.326 1.00 24.40 C ATOM 1229 O HIS A 163 19.062 36.754 3.319 1.00 24.93 O ATOM 1230 CB HIS A 163 21.542 37.247 5.411 1.00 24.71 C ATOM 1231 CG HIS A 163 22.027 38.433 6.186 1.00 24.48 C ATOM 1232 ND1 HIS A 163 23.346 38.602 6.556 1.00 25.05 N ATOM 1233 CD2 HIS A 163 21.361 39.517 6.658 1.00 24.82 C ATOM 1234 CE1 HIS A 163 23.478 39.748 7.207 1.00 26.44 C ATOM 1235 NE2 HIS A 163 22.286 40.321 7.286 1.00 25.55 N ATOM 1236 N LYS A 164 19.483 34.885 4.485 1.00 24.88 N ATOM 1237 CA LYS A 164 18.856 33.977 3.518 1.00 26.27 C ATOM 1238 C LYS A 164 17.384 34.322 3.344 1.00 25.61 C ATOM 1239 O LYS A 164 16.892 34.453 2.231 1.00 25.21 O ATOM 1240 CB LYS A 164 18.864 32.524 4.009 1.00 25.32 C ATOM 1241 CG LYS A 164 20.048 31.657 3.721 1.00 30.29 C ATOM 1242 CD LYS A 164 19.613 30.121 3.720 1.00 34.26 C ATOM 1243 CE LYS A 164 18.052 29.873 3.503 1.00 36.52 C ATOM 1244 NZ LYS A 164 17.403 29.714 2.102 1.00 34.41 N ATOM 1245 N GLU A 165 16.667 34.392 4.472 1.00 25.78 N ATOM 1246 CA GLU A 165 15.244 34.755 4.441 1.00 25.93 C ATOM 1247 C GLU A 165 15.002 36.070 3.666 1.00 25.03 C ATOM 1248 O GLU A 165 14.080 36.172 2.864 1.00 25.31 O ATOM 1249 CB GLU A 165 14.664 34.826 5.886 1.00 26.24 C ATOM 1250 CG GLU A 165 13.251 35.378 5.967 1.00 28.43 C ATOM 1251 CD GLU A 165 12.136 34.349 5.679 1.00 34.26 C ATOM 1252 OE1 GLU A 165 12.441 33.135 5.549 1.00 30.46 O ATOM 1253 OE2 GLU A 165 10.938 34.777 5.629 1.00 38.23 O ATOM 1254 N ILE A 166 15.831 37.076 3.918 1.00 25.30 N ATOM 1255 CA ILE A 166 15.736 38.343 3.199 1.00 25.03 C ATOM 1256 C ILE A 166 16.037 38.168 1.671 1.00 26.31 C ATOM 1257 O ILE A 166 15.225 38.577 0.837 1.00 25.19 O ATOM 1258 CB ILE A 166 16.663 39.415 3.819 1.00 24.79 C ATOM 1259 CG1 ILE A 166 16.224 39.786 5.264 1.00 23.32 C ATOM 1260 CG2 ILE A 166 16.705 40.658 2.942 1.00 23.43 C ATOM 1261 CD1 ILE A 166 17.231 40.715 6.023 1.00 17.43 C ATOM 1262 N THR A 167 17.178 37.556 1.314 1.00 26.73 N ATOM 1263 CA THR A 167 17.499 37.327 -0.131 1.00 27.90 C ATOM 1264 C THR A 167 16.388 36.528 -0.853 1.00 27.76 C ATOM 1265 O THR A 167 15.948 36.919 -1.928 1.00 27.97 O ATOM 1266 CB THR A 167 18.896 36.655 -0.343 1.00 27.77 C ATOM 1267 OG1 THR A 167 19.912 37.462 0.265 1.00 29.19 O ATOM 1268 CG2 THR A 167 19.220 36.514 -1.852 1.00 28.06 C ATOM 1269 N ASP A 168 15.910 35.440 -0.241 1.00 28.23 N ATOM 1270 CA ASP A 168 14.773 34.697 -0.801 1.00 29.21 C ATOM 1271 C ASP A 168 13.567 35.601 -1.013 1.00 29.51 C ATOM 1272 O ASP A 168 12.931 35.580 -2.066 1.00 29.99 O ATOM 1273 CB ASP A 168 14.390 33.492 0.087 1.00 29.78 C ATOM 1274 CG ASP A 168 15.502 32.434 0.167 1.00 30.95 C ATOM 1275 OD1 ASP A 168 16.467 32.528 -0.605 1.00 30.65 O ATOM 1276 OD2 ASP A 168 15.430 31.526 1.015 1.00 33.38 O ATOM 1277 N GLY A 169 13.244 36.407 -0.004 1.00 29.89 N ATOM 1278 CA GLY A 169 12.060 37.272 -0.081 1.00 29.50 C ATOM 1279 C GLY A 169 12.136 38.287 -1.199 1.00 29.28 C ATOM 1280 O GLY A 169 11.170 38.520 -1.900 1.00 27.96 O ATOM 1281 N VAL A 170 13.285 38.927 -1.335 1.00 29.71 N ATOM 1282 CA VAL A 170 13.504 39.857 -2.440 1.00 31.10 C ATOM 1283 C VAL A 170 13.337 39.173 -3.832 1.00 33.09 C ATOM 1284 O VAL A 170 12.599 39.672 -4.699 1.00 33.41 O ATOM 1285 CB VAL A 170 14.887 40.574 -2.309 1.00 30.44 C ATOM 1286 CG1 VAL A 170 15.188 41.389 -3.551 1.00 29.32 C ATOM 1287 CG2 VAL A 170 14.898 41.459 -1.071 1.00 29.13 C ATOM 1288 N ALA A 171 14.016 38.036 -4.018 1.00 34.61 N ATOM 1289 CA ALA A 171 13.922 37.243 -5.237 1.00 36.15 C ATOM 1290 C ALA A 171 12.473 36.854 -5.526 1.00 37.93 C ATOM 1291 O ALA A 171 11.950 37.182 -6.592 1.00 38.85 O ATOM 1292 CB ALA A 171 14.792 35.993 -5.116 1.00 35.84 C ATOM 1293 N ASN A 172 11.819 36.168 -4.583 1.00 38.94 N ATOM 1294 CA ASN A 172 10.408 35.776 -4.743 1.00 40.34 C ATOM 1295 C ASN A 172 9.461 36.914 -5.139 1.00 40.57 C ATOM 1296 O ASN A 172 8.516 36.702 -5.886 1.00 40.25 O ATOM 1297 CB ASN A 172 9.869 35.131 -3.470 1.00 40.63 C ATOM 1298 CG ASN A 172 10.583 33.848 -3.112 1.00 44.22 C ATOM 1299 OD1 ASN A 172 11.398 33.318 -3.886 1.00 46.04 O ATOM 1300 ND2 ASN A 172 10.284 33.332 -1.914 1.00 48.20 N ATOM 1301 N PHE A 173 9.695 38.113 -4.617 1.00 41.30 N ATOM 1302 CA PHE A 173 8.810 39.231 -4.915 1.00 42.45 C ATOM 1303 C PHE A 173 8.895 39.652 -6.391 1.00 44.05 C ATOM 1304 O PHE A 173 7.898 40.045 -6.998 1.00 43.32 O ATOM 1305 CB PHE A 173 9.118 40.424 -4.012 1.00 41.78 C ATOM 1306 CG PHE A 173 8.245 41.622 -4.272 1.00 39.79 C ATOM 1307 CD1 PHE A 173 6.955 41.682 -3.765 1.00 39.49 C ATOM 1308 CD2 PHE A 173 8.711 42.689 -5.021 1.00 37.99 C ATOM 1309 CE1 PHE A 173 6.150 42.795 -4.005 1.00 38.53 C ATOM 1310 CE2 PHE A 173 7.911 43.802 -5.262 1.00 36.13 C ATOM 1311 CZ PHE A 173 6.631 43.850 -4.757 1.00 37.09 C ATOM 1312 N LYS A 174 10.098 39.581 -6.955 1.00 46.01 N ATOM 1313 CA LYS A 174 10.321 39.983 -8.344 1.00 48.08 C ATOM 1314 C LYS A 174 9.802 38.906 -9.300 1.00 49.84 C ATOM 1315 O LYS A 174 9.753 39.095 -10.511 1.00 50.31 O ATOM 1316 CB LYS A 174 11.802 40.337 -8.564 1.00 47.73 C ATOM 1317 CG LYS A 174 12.190 41.554 -7.729 1.00 46.64 C ATOM 1318 CD LYS A 174 13.657 41.609 -7.418 1.00 45.19 C ATOM 1319 CE LYS A 174 14.379 42.456 -8.444 1.00 45.69 C ATOM 1320 NZ LYS A 174 15.857 42.279 -8.351 1.00 44.08 N ATOM 1321 N LYS A 175 9.382 37.788 -8.715 1.00 52.11 N ATOM 1322 CA LYS A 175 8.602 36.759 -9.396 1.00 54.14 C ATOM 1323 C LYS A 175 9.423 35.473 -9.415 1.00 54.68 C ATOM 1324 O LYS A 175 9.136 34.467 -8.751 1.00 55.07 O ATOM 1325 CB LYS A 175 8.214 37.214 -10.809 1.00 54.60 C ATOM 1326 CG LYS A 175 6.957 36.545 -11.369 1.00 57.59 C ATOM 1327 CD LYS A 175 6.501 37.199 -12.700 1.00 61.87 C ATOM 1328 CE LYS A 175 7.706 37.673 -13.531 1.00 63.51 C ATOM 1329 NZ LYS A 175 8.861 36.709 -13.496 1.00 63.20 N ATOM 1330 OXT LYS A 175 10.451 35.432 -10.086 1.00 55.71 O TER 1331 LYS A 175 HETATM 1332 K K A 176 24.990 43.276 0.005 0.50 24.45 K HETATM 1333 NA NA A 177 1.633 34.181 11.897 1.00 26.73 NA HETATM 1334 NA NA A 178 6.489 35.143 8.444 1.00 30.89 NA HETATM 1335 P1 POP A 179 1.233 37.542 11.212 1.00 32.68 P HETATM 1336 O1 POP A 179 1.910 38.831 11.612 1.00 32.62 O HETATM 1337 O2 POP A 179 1.288 37.475 9.712 1.00 33.46 O HETATM 1338 O3 POP A 179 1.948 36.362 11.841 1.00 30.47 O HETATM 1339 O POP A 179 -0.339 37.641 11.573 1.00 33.48 O HETATM 1340 P2 POP A 179 -1.193 36.552 12.370 1.00 36.05 P HETATM 1341 O4 POP A 179 -2.611 36.792 11.954 1.00 33.39 O HETATM 1342 O5 POP A 179 -1.079 36.873 13.870 1.00 33.69 O HETATM 1343 O6 POP A 179 -0.735 35.128 12.124 1.00 33.11 O HETATM 1344 O1 PG4 A 180 25.225 36.156 6.596 1.00 42.63 O HETATM 1345 C1 PG4 A 180 25.070 35.591 5.302 1.00 44.20 C HETATM 1346 C2 PG4 A 180 25.728 36.597 4.386 1.00 46.03 C HETATM 1347 O2 PG4 A 180 24.774 36.857 3.380 1.00 48.37 O HETATM 1348 C3 PG4 A 180 25.201 37.981 2.614 1.00 47.94 C HETATM 1349 C4 PG4 A 180 25.268 39.174 3.548 1.00 46.48 C HETATM 1350 O3 PG4 A 180 26.617 39.507 3.811 1.00 45.59 O HETATM 1351 C5 PG4 A 180 26.819 40.888 3.597 1.00 45.33 C HETATM 1352 C6 PG4 A 180 28.266 41.161 3.954 1.00 47.26 C HETATM 1353 O4 PG4 A 180 28.982 41.378 2.738 1.00 48.16 O HETATM 1354 C7 PG4 A 180 30.163 40.616 2.604 1.00 47.41 C HETATM 1355 C8 PG4 A 180 31.331 41.437 3.117 1.00 51.14 C HETATM 1356 O5 PG4 A 180 32.081 40.607 4.011 1.00 53.41 O HETATM 1357 C1 PEG A 181 13.856 28.176 23.722 1.00 59.47 C HETATM 1358 O1 PEG A 181 14.416 29.487 23.735 1.00 59.79 O HETATM 1359 C2 PEG A 181 13.605 27.741 22.291 1.00 59.20 C HETATM 1360 O2 PEG A 181 12.908 26.499 22.379 1.00 59.79 O HETATM 1361 C3 PEG A 181 11.848 26.393 21.440 1.00 59.65 C HETATM 1362 C4 PEG A 181 10.883 25.309 21.906 1.00 59.90 C HETATM 1363 O4 PEG A 181 10.045 25.835 22.942 1.00 58.85 O HETATM 1364 C1 PEG A 182 19.721 56.811 7.363 1.00 56.17 C HETATM 1365 O1 PEG A 182 18.409 56.724 7.966 1.00 55.97 O HETATM 1366 C2 PEG A 182 20.835 56.288 8.271 1.00 54.49 C HETATM 1367 O2 PEG A 182 21.824 57.291 8.516 1.00 56.31 O HETATM 1368 C3 PEG A 182 23.176 56.838 8.332 1.00 57.82 C HETATM 1369 C4 PEG A 182 23.815 57.479 7.094 1.00 58.58 C HETATM 1370 O4 PEG A 182 24.621 56.536 6.357 1.00 59.04 O HETATM 1371 O HOH A 183 -6.268 35.297 21.123 1.00 22.39 O HETATM 1372 O HOH A 184 18.291 50.223 3.964 1.00 24.68 O HETATM 1373 O HOH A 185 22.029 42.728 8.623 1.00 20.47 O HETATM 1374 O HOH A 186 15.767 55.114 9.164 1.00 20.81 O HETATM 1375 O HOH A 187 0.754 45.724 20.847 1.00 21.83 O HETATM 1376 O HOH A 188 11.338 47.709 21.125 1.00 19.21 O HETATM 1377 O HOH A 189 19.695 33.152 21.711 1.00 38.29 O HETATM 1378 O HOH A 190 10.491 50.293 22.101 1.00 18.65 O HETATM 1379 O HOH A 191 4.344 42.176 9.606 1.00 23.68 O HETATM 1380 O HOH A 192 22.154 49.578 16.234 1.00 24.18 O HETATM 1381 O HOH A 193 19.540 33.045 0.367 0.50 15.02 O HETATM 1382 O HOH A 194 -0.281 31.958 19.977 1.00 27.04 O HETATM 1383 O HOH A 195 0.714 43.186 11.724 1.00 31.86 O HETATM 1384 O HOH A 196 3.567 51.947 22.586 1.00 23.51 O HETATM 1385 O HOH A 197 -1.180 48.644 17.742 1.00 15.53 O HETATM 1386 O HOH A 198 1.948 54.836 16.377 1.00 21.93 O HETATM 1387 O HOH A 199 2.509 44.733 28.229 1.00 21.51 O HETATM 1388 O HOH A 200 2.391 38.378 14.597 1.00 23.11 O HETATM 1389 O HOH A 201 1.535 33.854 14.371 1.00 27.83 O HETATM 1390 O HOH A 202 -6.330 29.284 19.591 1.00 32.67 O HETATM 1391 O HOH A 203 -2.980 54.585 7.752 1.00 25.04 O HETATM 1392 O HOH A 204 -1.529 52.313 21.859 1.00 28.95 O HETATM 1393 O HOH A 205 -4.219 37.228 18.172 1.00 29.05 O HETATM 1394 O HOH A 206 -9.725 38.390 17.936 1.00 25.82 O HETATM 1395 O HOH A 207 -0.251 50.231 15.527 1.00 41.88 O HETATM 1396 O HOH A 208 -7.548 43.260 22.219 1.00 19.57 O HETATM 1397 O HOH A 209 24.427 35.212 14.096 1.00 31.41 O HETATM 1398 O HOH A 210 17.913 38.657 31.156 1.00 36.76 O HETATM 1399 O HOH A 211 23.606 42.865 12.451 1.00 25.35 O HETATM 1400 O HOH A 212 -10.993 36.660 20.173 1.00 34.07 O HETATM 1401 O HOH A 213 12.726 35.081 31.604 1.00 41.53 O HETATM 1402 O HOH A 214 11.555 34.813 2.535 1.00 32.40 O HETATM 1403 O HOH A 215 26.985 45.074 13.907 1.00 33.93 O HETATM 1404 O HOH A 216 22.305 31.774 11.176 1.00 27.99 O HETATM 1405 O HOH A 217 -5.311 51.156 18.105 1.00 23.06 O HETATM 1406 O HOH A 218 4.813 38.197 26.560 1.00 30.39 O HETATM 1407 O HOH A 219 16.429 31.381 6.556 1.00 31.04 O HETATM 1408 O HOH A 220 2.094 31.244 8.621 1.00 39.67 O HETATM 1409 O HOH A 221 3.282 37.464 7.811 1.00 36.79 O HETATM 1410 O HOH A 222 12.081 42.928 -4.465 1.00 35.63 O HETATM 1411 O HOH A 223 10.457 52.853 26.328 1.00 29.83 O HETATM 1412 O HOH A 224 -10.834 37.817 15.537 1.00 32.13 O HETATM 1413 O HOH A 225 11.844 46.500 23.826 1.00 35.48 O HETATM 1414 O HOH A 226 4.136 40.856 6.472 1.00 40.41 O HETATM 1415 O HOH A 227 27.046 47.404 15.617 1.00 32.79 O HETATM 1416 O HOH A 228 27.357 54.793 8.601 1.00 45.22 O HETATM 1417 O HOH A 229 23.653 47.745 22.742 1.00 50.33 O HETATM 1418 O HOH A 230 13.464 46.940 -3.502 1.00 32.04 O HETATM 1419 O HOH A 231 3.976 32.286 14.525 1.00 31.56 O HETATM 1420 O HOH A 232 20.596 34.827 26.319 1.00 49.91 O HETATM 1421 O HOH A 233 0.268 53.053 17.314 1.00 42.31 O HETATM 1422 O HOH A 234 8.635 54.732 26.919 1.00 33.52 O HETATM 1423 O HOH A 235 8.723 45.643 25.830 1.00 31.33 O HETATM 1424 O HOH A 236 9.525 50.219 24.646 1.00 32.19 O HETATM 1425 O HOH A 237 29.165 40.813 21.487 1.00 56.55 O HETATM 1426 O HOH A 238 2.494 40.055 8.917 1.00 36.15 O HETATM 1427 O HOH A 239 -0.777 34.809 9.090 1.00 37.11 O HETATM 1428 O HOH A 240 23.455 48.536 9.084 1.00 28.44 O HETATM 1429 O HOH A 241 24.600 49.610 11.229 1.00 23.81 O HETATM 1430 O HOH A 242 21.015 49.121 7.957 1.00 22.66 O HETATM 1431 O HOH A 243 24.242 43.201 9.915 1.00 27.87 O HETATM 1432 O HOH A 244 26.271 42.655 13.711 1.00 28.13 O HETATM 1433 O HOH A 245 5.960 36.600 6.289 1.00 41.50 O HETATM 1434 O HOH A 246 18.246 32.111 23.785 1.00 56.31 O HETATM 1435 O HOH A 247 7.627 32.876 7.134 1.00 33.79 O HETATM 1436 O HOH A 248 1.165 51.316 -0.972 1.00 46.31 O HETATM 1437 O HOH A 249 1.154 41.748 26.990 1.00 28.03 O HETATM 1438 O HOH A 250 5.939 26.535 21.149 1.00 44.12 O HETATM 1439 O HOH A 251 -5.540 43.055 28.186 1.00 26.47 O HETATM 1440 O HOH A 252 11.949 30.493 27.231 1.00 52.78 O HETATM 1441 O HOH A 253 13.331 24.495 13.440 1.00 52.00 O HETATM 1442 O HOH A 254 -1.435 29.723 20.052 1.00 52.22 O HETATM 1443 O HOH A 255 2.115 43.165 6.250 1.00 34.91 O HETATM 1444 O HOH A 256 15.992 53.085 0.933 1.00 34.04 O HETATM 1445 O HOH A 257 2.292 33.719 9.368 1.00 44.24 O HETATM 1446 O HOH A 258 3.626 29.350 26.403 1.00 42.97 O HETATM 1447 O HOH A 259 -3.063 50.429 19.160 1.00 33.64 O HETATM 1448 O HOH A 260 -4.016 34.810 12.023 1.00 43.84 O HETATM 1449 O HOH A 261 -7.025 43.005 7.425 1.00 50.38 O HETATM 1450 O HOH A 262 20.664 37.966 29.449 1.00 39.40 O HETATM 1451 O HOH A 263 8.219 36.489 7.242 1.00 45.22 O HETATM 1452 O HOH A 264 7.603 30.314 26.808 1.00 49.95 O HETATM 1453 O HOH A 265 27.192 38.462 19.035 1.00 38.71 O HETATM 1454 O HOH A 266 -3.725 41.084 29.707 1.00 44.44 O HETATM 1455 O HOH A 267 -3.184 38.130 9.900 1.00 31.98 O HETATM 1456 O HOH A 268 -6.968 37.923 11.495 1.00 40.84 O HETATM 1457 O HOH A 269 15.958 47.852 -2.923 1.00 44.94 O HETATM 1458 O HOH A 270 13.106 37.129 -9.048 1.00 35.12 O HETATM 1459 O HOH A 271 23.944 34.080 16.627 1.00 56.20 O HETATM 1460 O HOH A 272 17.584 52.420 -1.888 1.00 38.11 O HETATM 1461 O HOH A 273 5.521 45.450 -0.564 1.00 47.04 O HETATM 1462 O HOH A 274 25.459 49.006 4.506 1.00 54.02 O HETATM 1463 O HOH A 275 16.595 27.943 19.928 1.00 49.01 O HETATM 1464 O HOH A 276 22.019 36.726 26.870 1.00 56.59 O HETATM 1465 O HOH A 277 10.474 36.654 8.412 1.00 45.47 O HETATM 1466 O HOH A 278 24.611 33.020 11.703 1.00 47.62 O HETATM 1467 O HOH A 279 26.899 46.740 4.551 1.00 52.92 O HETATM 1468 O HOH A 280 6.994 29.354 29.500 1.00 59.06 O HETATM 1469 O HOH A 281 1.016 41.471 9.152 1.00 46.63 O HETATM 1470 O HOH A 282 -3.738 28.411 20.723 1.00 58.68 O HETATM 1471 O HOH A 283 14.325 31.639 5.778 1.00 49.26 O HETATM 1472 O HOH A 284 27.777 37.727 7.983 1.00 49.01 O HETATM 1473 O HOH A 285 11.301 44.913 29.125 1.00 47.44 O HETATM 1474 O HOH A 286 -3.722 51.289 27.893 1.00 28.88 O HETATM 1475 O HOH A 287 5.173 46.827 -3.289 1.00 59.99 O HETATM 1476 O HOH A 288 -9.268 38.914 11.481 1.00 39.62 O HETATM 1477 O HOH A 289 9.346 31.934 27.060 1.00 45.27 O HETATM 1478 O HOH A 290 24.327 46.350 8.439 1.00 39.23 O HETATM 1479 O HOH A 291 17.766 26.234 14.240 1.00 58.80 O HETATM 1480 O HOH A 292 14.667 53.897 27.017 1.00 44.45 O HETATM 1481 O HOH A 293 13.540 30.919 2.872 1.00 48.68 O HETATM 1482 O HOH A 294 13.812 54.578 29.178 1.00 37.62 O CONECT 70 1332 CONECT 75 1332 CONECT 94 1332 CONECT 535 1334 CONECT 734 1333 CONECT 767 1334 CONECT 768 1333 CONECT 772 1334 CONECT 1332 70 75 94 CONECT 1333 734 768 1338 1343 CONECT 1333 1389 1445 CONECT 1334 535 767 772 1433 CONECT 1334 1435 1451 CONECT 1335 1336 1337 1338 1339 CONECT 1336 1335 CONECT 1337 1335 CONECT 1338 1333 1335 CONECT 1339 1335 1340 CONECT 1340 1339 1341 1342 1343 CONECT 1341 1340 CONECT 1342 1340 CONECT 1343 1333 1340 CONECT 1344 1345 CONECT 1345 1344 1346 CONECT 1346 1345 1347 CONECT 1347 1346 1348 CONECT 1348 1347 1349 CONECT 1349 1348 1350 CONECT 1350 1349 1351 CONECT 1351 1350 1352 CONECT 1352 1351 1353 CONECT 1353 1352 1354 CONECT 1354 1353 1355 CONECT 1355 1354 1356 CONECT 1356 1355 CONECT 1357 1358 1359 CONECT 1358 1357 CONECT 1359 1357 1360 CONECT 1360 1359 1361 CONECT 1361 1360 1362 CONECT 1362 1361 1363 CONECT 1363 1362 CONECT 1364 1365 1366 CONECT 1365 1364 CONECT 1366 1364 1367 CONECT 1367 1366 1368 CONECT 1368 1367 1369 CONECT 1369 1368 1370 CONECT 1370 1369 CONECT 1389 1333 CONECT 1433 1334 CONECT 1435 1334 CONECT 1445 1333 CONECT 1451 1334 MASTER 470 0 7 5 9 0 13 6 1481 1 54 16 END