HEADER OXYGEN TRANSPORT 13-DEC-97 101M TITLE SPERM WHALE MYOGLOBIN F46V N-BUTYL ISOCYANIDE AT PH 9.0 COMPND MOL_ID: 1; COMPND 2 MOLECULE: MYOGLOBIN; COMPND 3 CHAIN: A; COMPND 4 ENGINEERED: YES; COMPND 5 MUTATION: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: PHYSETER CATODON; SOURCE 3 ORGANISM_COMMON: SPERM WHALE; SOURCE 4 ORGANISM_TAXID: 9755; SOURCE 5 ORGAN: SKELETAL; SOURCE 6 TISSUE: SKELETAL MUSCLE; SOURCE 7 CELLULAR_LOCATION: CYTOPLASM; SOURCE 8 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 9 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 10 EXPRESSION_SYSTEM_STRAIN: PHAGE RESISTANT TB1; SOURCE 11 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 12 EXPRESSION_SYSTEM_PLASMID: PEMBL 19+ KEYWDS LIGAND BINDING, OXYGEN STORAGE, OXYGEN BINDING, HEME, KEYWDS 2 OXYGEN TRANSPORT EXPDTA X-RAY DIFFRACTION AUTHOR R.D.SMITH,J.S.OLSON,G.N.PHILLIPS JR. REVDAT 4 24-FEB-09 101M 1 VERSN REVDAT 3 03-MAY-05 101M 1 AUTHOR REVDAT 2 17-MAY-99 101M 1 JRNL HELIX REVDAT 1 08-APR-98 101M 0 JRNL AUTH R.D.SMITH JRNL TITL CORRELATIONS BETWEEN BOUND N-ALKYL ISOCYANIDE JRNL TITL 2 ORIENTATIONS AND PATHWAYS FOR LIGAND BINDING IN JRNL TITL 3 RECOMBINANT MYOGLOBINS JRNL REF THESIS, RICE 1999 JRNL REFN REMARK 1 REMARK 2 REMARK 2 RESOLUTION. 2.07 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : X-PLOR 3.851 REMARK 3 AUTHORS : BRUNGER REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.07 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 5.00 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000 REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 10000000.000 REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0010 REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 97.8 REMARK 3 NUMBER OF REFLECTIONS : 12340 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM REMARK 3 R VALUE (WORKING SET) : 0.157 REMARK 3 FREE R VALUE : 0.202 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 9.900 REMARK 3 FREE R VALUE TEST SET COUNT : 1220 REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.006 REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : 8 REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.07 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.16 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 92.90 REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 1287 REMARK 3 BIN R VALUE (WORKING SET) : 0.2090 REMARK 3 BIN FREE R VALUE : 0.2110 REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 11.10 REMARK 3 BIN FREE R VALUE TEST SET COUNT : 161 REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.017 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 1221 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 49 REMARK 3 SOLVENT ATOMS : 143 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 14.00 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 24.80 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : NULL REMARK 3 B22 (A**2) : NULL REMARK 3 B33 (A**2) : NULL REMARK 3 B12 (A**2) : NULL REMARK 3 B13 (A**2) : NULL REMARK 3 B23 (A**2) : NULL REMARK 3 REMARK 3 ESTIMATED COORDINATE ERROR. REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.18 REMARK 3 ESD FROM SIGMAA (A) : 0.17 REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00 REMARK 3 REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR. REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.23 REMARK 3 ESD FROM C-V SIGMAA (A) : 0.15 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. REMARK 3 BOND LENGTHS (A) : 0.010 REMARK 3 BOND ANGLES (DEGREES) : 1.40 REMARK 3 DIHEDRAL ANGLES (DEGREES) : 18.90 REMARK 3 IMPROPER ANGLES (DEGREES) : 1.36 REMARK 3 REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED REMARK 3 REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA REMARK 3 MAIN-CHAIN BOND (A**2) : 2.470 ; 1.500 REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.860 ; 2.000 REMARK 3 SIDE-CHAIN BOND (A**2) : 8.730 ; 2.500 REMARK 3 SIDE-CHAIN ANGLE (A**2) : 12.900; 2.500 REMARK 3 REMARK 3 NCS MODEL : NULL REMARK 3 REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL REMARK 3 REMARK 3 PARAMETER FILE 1 : PARHCSDX.PRO REMARK 3 PARAMETER FILE 2 : PARAMETER.HEME REMARK 3 PARAMETER FILE 3 : PARAMETER.NBNC REMARK 3 PARAMETER FILE 4 : PARAM19.SOLV REMARK 3 PARAMETER FILE 5 : NULL REMARK 3 TOPOLOGY FILE 1 : TOPHCSDX.PRO REMARK 3 TOPOLOGY FILE 2 : TOPOLOGY.HEME REMARK 3 TOPOLOGY FILE 3 : TOPOLOGY.NBNC REMARK 3 TOPOLOGY FILE 4 : TOPH19.SOLV REMARK 3 TOPOLOGY FILE 5 : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 101M COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : SEP-94 REMARK 200 TEMPERATURE (KELVIN) : 292 REMARK 200 PH : 9.0 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : N REMARK 200 RADIATION SOURCE : NULL REMARK 200 BEAMLINE : NULL REMARK 200 X-RAY GENERATOR MODEL : SIEMENS REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418 REMARK 200 MONOCHROMATOR : GRAPHITE(002) REMARK 200 OPTICS : PINHOLE COLLIMATOR REMARK 200 REMARK 200 DETECTOR TYPE : IMAGE PLATE REMARK 200 DETECTOR MANUFACTURER : RIGAKU REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : XSCALE REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 13624 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.070 REMARK 200 RESOLUTION RANGE LOW (A) : 6.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9 REMARK 200 DATA REDUNDANCY : 7.450 REMARK 200 R MERGE (I) : 0.07000 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : NULL REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.07 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.08 REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0 REMARK 200 DATA REDUNDANCY IN SHELL : 7.10 REMARK 200 R MERGE FOR SHELL (I) : 0.29700 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : NULL REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: NULL REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: X-PLOR 3.851 REMARK 200 STARTING MODEL: SPERM WHALE MYOGLOBIN 0M, D122N (DEOXY) REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 60.20 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.09 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 3.0 M AMMONIUM SULFATE, 20 MM TRIS, REMARK 280 1MM EDTA, PH 9.0 REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 6 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 REMARK 290 5555 Y,-X+Y,Z REMARK 290 6555 X-Y,X,Z REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -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 0.00000 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 0.00000 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 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: 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 HOH A 332 LIES ON A SPECIAL POSITION. 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 20 75.97 -151.70 REMARK 500 LYS A 98 70.18 56.03 REMARK 500 TYR A 151 -71.27 -108.10 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 HEM A 155 FE REMARK 620 N RES CSSEQI ATOM REMARK 620 1 HIS A 93 NE2 REMARK 620 2 NBN A 156 C 175.7 REMARK 620 N 1 REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: HEM REMARK 800 EVIDENCE_CODE: UNKNOWN REMARK 800 SITE_DESCRIPTION: LIGAND BINDING SITE. REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 157 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM A 155 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NBN A 156 DBREF 101M A 1 153 UNP P02185 MYG_PHYCA 1 153 SEQADV 101M VAL A 46 UNP P02185 PHE 46 ENGINEERED SEQADV 101M ASN A 122 UNP P02185 ASP 122 ENGINEERED SEQRES 1 A 154 MET VAL LEU SER GLU GLY GLU TRP GLN LEU VAL LEU HIS SEQRES 2 A 154 VAL TRP ALA LYS VAL GLU ALA ASP VAL ALA GLY HIS GLY SEQRES 3 A 154 GLN ASP ILE LEU ILE ARG LEU PHE LYS SER HIS PRO GLU SEQRES 4 A 154 THR LEU GLU LYS PHE ASP ARG VAL LYS HIS LEU LYS THR SEQRES 5 A 154 GLU ALA GLU MET LYS ALA SER GLU ASP LEU LYS LYS HIS SEQRES 6 A 154 GLY VAL THR VAL LEU THR ALA LEU GLY ALA ILE LEU LYS SEQRES 7 A 154 LYS LYS GLY HIS HIS GLU ALA GLU LEU LYS PRO LEU ALA SEQRES 8 A 154 GLN SER HIS ALA THR LYS HIS LYS ILE PRO ILE LYS TYR SEQRES 9 A 154 LEU GLU PHE ILE SER GLU ALA ILE ILE HIS VAL LEU HIS SEQRES 10 A 154 SER ARG HIS PRO GLY ASN PHE GLY ALA ASP ALA GLN GLY SEQRES 11 A 154 ALA MET ASN LYS ALA LEU GLU LEU PHE ARG LYS ASP ILE SEQRES 12 A 154 ALA ALA LYS TYR LYS GLU LEU GLY TYR GLN GLY HET SO4 A 157 5 HET HEM A 155 43 HET NBN A 156 6 HETNAM SO4 SULFATE ION HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE HETNAM NBN N-BUTYL ISOCYANIDE HETSYN HEM HEME FORMUL 2 SO4 O4 S 2- FORMUL 3 HEM C34 H32 FE N4 O4 FORMUL 4 NBN C5 H9 N FORMUL 5 HOH *138(H2 O) HELIX 1 1 SER A 3 GLU A 18 1 16 HELIX 2 2 ASP A 20 SER A 35 1 16 HELIX 3 3 HIS A 36 LYS A 42 1 7 HELIX 4 4 THR A 51 ALA A 57 1 7 HELIX 5 5 SER A 58 LYS A 77 1 20 HELIX 6 6 LEU A 86 ALA A 94 1 9 HELIX 7 7 PRO A 100 ARG A 118 1 19 HELIX 8 8 GLY A 124 LEU A 149 1 26 LINK FE HEM A 155 NE2 HIS A 93 1555 1555 2.20 LINK FE HEM A 155 C NBN A 156 1555 1555 2.11 SITE 1 HEM 1 HEM A 155 SITE 1 AC1 6 SER A 3 GLU A 4 THR A 51 GLU A 52 SITE 2 AC1 6 HOH A 268 HOH A 282 SITE 1 AC2 13 LYS A 42 PHE A 43 ARG A 45 LEU A 89 SITE 2 AC2 13 SER A 92 HIS A 93 HIS A 97 ILE A 99 SITE 3 AC2 13 TYR A 103 NBN A 156 HOH A 286 HOH A 287 SITE 4 AC2 13 HOH A 304 SITE 1 AC3 5 PHE A 43 HIS A 64 THR A 67 VAL A 68 SITE 2 AC3 5 HEM A 155 CRYST1 91.670 91.670 45.970 90.00 90.00 120.00 P 6 6 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 0.010909 0.006298 0.000000 0.00000 SCALE2 0.000000 0.012596 0.000000 0.00000 SCALE3 0.000000 0.000000 0.021753 0.00000 ATOM 1 N MET A 0 24.277 8.374 -9.854 1.00 38.41 N ATOM 2 CA MET A 0 24.404 9.859 -9.939 1.00 37.90 C ATOM 3 C MET A 0 25.814 10.249 -10.359 1.00 36.65 C ATOM 4 O MET A 0 26.748 9.469 -10.197 1.00 37.13 O ATOM 5 CB MET A 0 24.070 10.495 -8.596 1.00 39.58 C ATOM 6 CG MET A 0 24.880 9.939 -7.442 1.00 41.49 C ATOM 7 SD MET A 0 24.262 10.555 -5.873 1.00 44.70 S ATOM 8 CE MET A 0 24.822 12.266 -5.967 1.00 41.59 C ATOM 9 N VAL A 1 25.964 11.453 -10.903 1.00 34.54 N ATOM 10 CA VAL A 1 27.263 11.924 -11.359 1.00 32.46 C ATOM 11 C VAL A 1 27.392 13.428 -11.115 1.00 30.70 C ATOM 12 O VAL A 1 26.443 14.184 -11.327 1.00 31.42 O ATOM 13 CB VAL A 1 27.455 11.631 -12.878 1.00 32.95 C ATOM 14 CG1 VAL A 1 28.756 12.209 -13.382 1.00 32.87 C ATOM 15 CG2 VAL A 1 27.432 10.131 -13.140 1.00 33.54 C ATOM 16 N LEU A 2 28.555 13.855 -10.636 1.00 27.76 N ATOM 17 CA LEU A 2 28.797 15.269 -10.390 1.00 25.21 C ATOM 18 C LEU A 2 29.492 15.903 -11.585 1.00 24.21 C ATOM 19 O LEU A 2 30.250 15.240 -12.306 1.00 23.80 O ATOM 20 CB LEU A 2 29.688 15.470 -9.152 1.00 24.30 C ATOM 21 CG LEU A 2 29.084 15.416 -7.751 1.00 22.96 C ATOM 22 CD1 LEU A 2 28.730 13.988 -7.390 1.00 22.03 C ATOM 23 CD2 LEU A 2 30.085 16.008 -6.776 1.00 21.94 C ATOM 24 N SER A 3 29.236 17.185 -11.800 1.00 23.04 N ATOM 25 CA SER A 3 29.898 17.894 -12.882 1.00 22.62 C ATOM 26 C SER A 3 31.282 18.336 -12.384 1.00 22.06 C ATOM 27 O SER A 3 31.565 18.268 -11.188 1.00 21.06 O ATOM 28 CB SER A 3 29.061 19.097 -13.312 1.00 22.96 C ATOM 29 OG SER A 3 28.916 20.026 -12.260 1.00 24.01 O ATOM 30 N GLU A 4 32.151 18.759 -13.296 1.00 17.46 N ATOM 31 CA GLU A 4 33.489 19.212 -12.922 1.00 24.04 C ATOM 32 C GLU A 4 33.346 20.443 -12.019 1.00 21.74 C ATOM 33 O GLU A 4 34.115 20.620 -11.076 1.00 20.06 O ATOM 34 CB GLU A 4 34.316 19.551 -14.178 1.00 22.74 C ATOM 35 CG GLU A 4 35.720 20.158 -13.921 1.00 18.42 C ATOM 36 CD GLU A 4 36.690 19.210 -13.205 1.00 27.97 C ATOM 37 OE1 GLU A 4 36.449 17.987 -13.166 1.00 27.73 O ATOM 38 OE2 GLU A 4 37.711 19.692 -12.684 1.00 28.70 O ATOM 39 N GLY A 5 32.351 21.280 -12.308 1.00 19.09 N ATOM 40 CA GLY A 5 32.118 22.472 -11.504 1.00 18.12 C ATOM 41 C GLY A 5 31.837 22.114 -10.053 1.00 18.29 C ATOM 42 O GLY A 5 32.353 22.758 -9.137 1.00 17.54 O ATOM 43 N GLU A 6 31.033 21.069 -9.845 1.00 16.68 N ATOM 44 CA GLU A 6 30.702 20.617 -8.498 1.00 13.59 C ATOM 45 C GLU A 6 31.945 20.007 -7.807 1.00 17.58 C ATOM 46 O GLU A 6 32.199 20.278 -6.638 1.00 14.97 O ATOM 47 CB GLU A 6 29.510 19.648 -8.533 1.00 13.04 C ATOM 48 CG GLU A 6 28.179 20.319 -8.911 1.00 16.58 C ATOM 49 CD GLU A 6 27.056 19.316 -9.262 1.00 18.86 C ATOM 50 OE1 GLU A 6 27.338 18.242 -9.832 1.00 23.67 O ATOM 51 OE2 GLU A 6 25.881 19.612 -8.979 1.00 29.24 O ATOM 52 N TRP A 7 32.747 19.242 -8.545 1.00 15.06 N ATOM 53 CA TRP A 7 33.970 18.675 -7.985 1.00 15.72 C ATOM 54 C TRP A 7 34.932 19.799 -7.595 1.00 16.03 C ATOM 55 O TRP A 7 35.645 19.687 -6.599 1.00 16.52 O ATOM 56 CB TRP A 7 34.672 17.733 -8.986 1.00 15.72 C ATOM 57 CG TRP A 7 34.046 16.382 -9.056 1.00 15.35 C ATOM 58 CD1 TRP A 7 33.473 15.795 -10.149 1.00 15.74 C ATOM 59 CD2 TRP A 7 33.874 15.466 -7.966 1.00 15.25 C ATOM 60 NE1 TRP A 7 32.940 14.573 -9.804 1.00 15.28 N ATOM 61 CE2 TRP A 7 33.168 14.345 -8.469 1.00 15.63 C ATOM 62 CE3 TRP A 7 34.237 15.486 -6.608 1.00 14.98 C ATOM 63 CZ2 TRP A 7 32.813 13.244 -7.652 1.00 15.14 C ATOM 64 CZ3 TRP A 7 33.884 14.394 -5.801 1.00 15.08 C ATOM 65 CH2 TRP A 7 33.178 13.290 -6.328 1.00 14.28 C ATOM 66 N GLN A 8 34.973 20.871 -8.388 1.00 15.81 N ATOM 67 CA GLN A 8 35.856 21.987 -8.080 1.00 16.01 C ATOM 68 C GLN A 8 35.445 22.668 -6.769 1.00 15.78 C ATOM 69 O GLN A 8 36.305 23.057 -5.973 1.00 15.65 O ATOM 70 CB GLN A 8 35.893 22.989 -9.235 1.00 17.95 C ATOM 71 CG GLN A 8 36.613 22.459 -10.451 1.00 25.32 C ATOM 72 CD GLN A 8 38.055 22.125 -10.145 1.00 39.60 C ATOM 73 OE1 GLN A 8 38.883 23.023 -9.983 1.00 67.02 O ATOM 74 NE2 GLN A 8 38.366 20.830 -10.043 1.00 43.80 N ATOM 75 N LEU A 9 34.141 22.788 -6.533 1.00 14.97 N ATOM 76 CA LEU A 9 33.661 23.390 -5.284 1.00 14.87 C ATOM 77 C LEU A 9 34.055 22.525 -4.081 1.00 14.68 C ATOM 78 O LEU A 9 34.515 23.031 -3.061 1.00 14.85 O ATOM 79 CB LEU A 9 32.141 23.586 -5.317 1.00 15.27 C ATOM 80 CG LEU A 9 31.668 24.723 -6.235 1.00 15.96 C ATOM 81 CD1 LEU A 9 30.164 24.757 -6.306 1.00 15.80 C ATOM 82 CD2 LEU A 9 32.205 26.043 -5.730 1.00 16.40 C ATOM 83 N VAL A 10 33.913 21.215 -4.236 1.00 13.96 N ATOM 84 CA VAL A 10 34.247 20.256 -3.195 1.00 13.50 C ATOM 85 C VAL A 10 35.742 20.293 -2.878 1.00 14.08 C ATOM 86 O VAL A 10 36.144 20.446 -1.721 1.00 14.08 O ATOM 87 CB VAL A 10 33.821 18.826 -3.640 1.00 13.81 C ATOM 88 CG1 VAL A 10 34.428 17.746 -2.739 1.00 13.51 C ATOM 89 CG2 VAL A 10 32.289 18.724 -3.657 1.00 13.28 C ATOM 90 N LEU A 11 36.563 20.208 -3.915 1.00 14.31 N ATOM 91 CA LEU A 11 38.005 20.200 -3.741 1.00 14.80 C ATOM 92 C LEU A 11 38.590 21.529 -3.282 1.00 15.08 C ATOM 93 O LEU A 11 39.613 21.537 -2.605 1.00 15.16 O ATOM 94 CB LEU A 11 38.690 19.677 -5.007 1.00 15.74 C ATOM 95 CG LEU A 11 38.310 18.212 -5.299 1.00 16.67 C ATOM 96 CD1 LEU A 11 38.911 17.765 -6.605 1.00 18.20 C ATOM 97 CD2 LEU A 11 38.778 17.300 -4.167 1.00 17.64 C ATOM 98 N HIS A 12 37.915 22.640 -3.577 1.00 15.37 N ATOM 99 CA HIS A 12 38.390 23.965 -3.145 1.00 15.95 C ATOM 100 C HIS A 12 38.229 24.124 -1.625 1.00 15.98 C ATOM 101 O HIS A 12 39.105 24.662 -0.963 1.00 16.51 O ATOM 102 CB HIS A 12 37.650 25.092 -3.887 1.00 19.33 C ATOM 103 CG HIS A 12 38.064 26.470 -3.467 1.00 28.57 C ATOM 104 ND1 HIS A 12 39.323 26.998 -3.668 1.00 38.92 N ATOM 105 CD2 HIS A 12 37.357 27.443 -2.836 1.00 35.58 C ATOM 106 CE1 HIS A 12 39.341 28.247 -3.167 1.00 37.34 C ATOM 107 NE2 HIS A 12 38.171 28.566 -2.650 1.00 33.72 N ATOM 108 N VAL A 13 37.107 23.672 -1.070 1.00 15.74 N ATOM 109 CA VAL A 13 36.934 23.758 0.379 1.00 15.64 C ATOM 110 C VAL A 13 37.792 22.681 1.085 1.00 15.33 C ATOM 111 O VAL A 13 38.342 22.921 2.160 1.00 15.39 O ATOM 112 CB VAL A 13 35.424 23.682 0.816 1.00 16.72 C ATOM 113 CG1 VAL A 13 34.851 22.287 0.601 1.00 16.66 C ATOM 114 CG2 VAL A 13 35.283 24.085 2.288 1.00 17.08 C ATOM 115 N TRP A 14 37.958 21.524 0.448 1.00 14.73 N ATOM 116 CA TRP A 14 38.770 20.457 1.017 1.00 14.75 C ATOM 117 C TRP A 14 40.241 20.879 1.166 1.00 14.64 C ATOM 118 O TRP A 14 40.921 20.456 2.099 1.00 15.14 O ATOM 119 CB TRP A 14 38.673 19.191 0.164 1.00 15.26 C ATOM 120 CG TRP A 14 39.146 17.993 0.901 1.00 16.17 C ATOM 121 CD1 TRP A 14 40.356 17.387 0.782 1.00 16.11 C ATOM 122 CD2 TRP A 14 38.458 17.320 1.969 1.00 16.43 C ATOM 123 NE1 TRP A 14 40.477 16.388 1.722 1.00 16.54 N ATOM 124 CE2 TRP A 14 39.328 16.325 2.463 1.00 15.93 C ATOM 125 CE3 TRP A 14 37.191 17.471 2.561 1.00 16.69 C ATOM 126 CZ2 TRP A 14 38.983 15.480 3.522 1.00 16.79 C ATOM 127 CZ3 TRP A 14 36.842 16.622 3.626 1.00 17.61 C ATOM 128 CH2 TRP A 14 37.744 15.638 4.093 1.00 16.93 C ATOM 129 N ALA A 15 40.726 21.722 0.254 1.00 14.42 N ATOM 130 CA ALA A 15 42.095 22.214 0.312 1.00 14.00 C ATOM 131 C ALA A 15 42.328 22.999 1.608 1.00 14.30 C ATOM 132 O ALA A 15 43.427 22.982 2.156 1.00 14.23 O ATOM 133 CB ALA A 15 42.389 23.080 -0.896 1.00 14.14 C ATOM 134 N LYS A 16 41.270 23.635 2.124 1.00 15.22 N ATOM 135 CA LYS A 16 41.345 24.400 3.376 1.00 17.82 C ATOM 136 C LYS A 16 41.371 23.426 4.548 1.00 14.95 C ATOM 137 O LYS A 16 42.124 23.616 5.491 1.00 18.06 O ATOM 138 CB LYS A 16 40.146 25.350 3.539 1.00 11.85 C ATOM 139 CG LYS A 16 39.931 26.312 2.396 1.00 15.52 C ATOM 140 CD LYS A 16 41.171 27.093 2.107 1.00 22.34 C ATOM 141 CE LYS A 16 41.010 27.867 0.817 1.00 43.61 C ATOM 142 NZ LYS A 16 42.298 28.453 0.378 1.00 41.54 N ATOM 143 N VAL A 17 40.524 22.398 4.491 1.00 12.40 N ATOM 144 CA VAL A 17 40.473 21.367 5.522 1.00 12.29 C ATOM 145 C VAL A 17 41.872 20.771 5.701 1.00 12.32 C ATOM 146 O VAL A 17 42.329 20.560 6.829 1.00 12.74 O ATOM 147 CB VAL A 17 39.496 20.242 5.116 1.00 12.43 C ATOM 148 CG1 VAL A 17 39.596 19.045 6.073 1.00 12.58 C ATOM 149 CG2 VAL A 17 38.088 20.787 5.082 1.00 13.47 C ATOM 150 N GLU A 18 42.553 20.513 4.584 1.00 13.88 N ATOM 151 CA GLU A 18 43.904 19.940 4.618 1.00 14.94 C ATOM 152 C GLU A 18 44.991 20.813 5.262 1.00 16.26 C ATOM 153 O GLU A 18 46.070 20.322 5.560 1.00 15.32 O ATOM 154 CB GLU A 18 44.327 19.461 3.235 1.00 12.91 C ATOM 155 CG GLU A 18 43.572 18.228 2.808 1.00 13.99 C ATOM 156 CD GLU A 18 44.011 17.692 1.458 1.00 16.75 C ATOM 157 OE1 GLU A 18 44.559 18.458 0.644 1.00 21.92 O ATOM 158 OE2 GLU A 18 43.791 16.493 1.217 1.00 23.33 O ATOM 159 N ALA A 19 44.708 22.090 5.501 1.00 14.20 N ATOM 160 CA ALA A 19 45.686 22.946 6.169 1.00 14.94 C ATOM 161 C ALA A 19 45.780 22.500 7.624 1.00 14.81 C ATOM 162 O ALA A 19 46.773 22.759 8.295 1.00 15.01 O ATOM 163 CB ALA A 19 45.259 24.418 6.110 1.00 14.54 C ATOM 164 N ASP A 20 44.731 21.837 8.111 1.00 12.28 N ATOM 165 CA ASP A 20 44.693 21.368 9.492 1.00 12.72 C ATOM 166 C ASP A 20 43.810 20.117 9.606 1.00 18.12 C ATOM 167 O ASP A 20 42.686 20.173 10.131 1.00 13.62 O ATOM 168 CB ASP A 20 44.157 22.490 10.403 1.00 10.25 C ATOM 169 CG ASP A 20 44.073 22.074 11.865 1.00 19.39 C ATOM 170 OD1 ASP A 20 44.848 21.187 12.301 1.00 17.74 O ATOM 171 OD2 ASP A 20 43.195 22.613 12.564 1.00 26.16 O ATOM 172 N VAL A 21 44.343 18.987 9.164 1.00 14.51 N ATOM 173 CA VAL A 21 43.597 17.741 9.183 1.00 16.06 C ATOM 174 C VAL A 21 43.223 17.273 10.588 1.00 15.92 C ATOM 175 O VAL A 21 42.095 16.857 10.810 1.00 16.38 O ATOM 176 CB VAL A 21 44.360 16.610 8.409 1.00 17.48 C ATOM 177 CG1 VAL A 21 43.603 15.292 8.507 1.00 16.78 C ATOM 178 CG2 VAL A 21 44.521 17.021 6.937 1.00 17.19 C ATOM 179 N ALA A 22 44.151 17.364 11.537 1.00 15.42 N ATOM 180 CA ALA A 22 43.871 16.937 12.907 1.00 15.58 C ATOM 181 C ALA A 22 42.787 17.773 13.591 1.00 15.11 C ATOM 182 O ALA A 22 41.894 17.227 14.221 1.00 14.57 O ATOM 183 CB ALA A 22 45.154 16.940 13.734 1.00 16.03 C ATOM 184 N GLY A 23 42.865 19.094 13.443 1.00 14.85 N ATOM 185 CA GLY A 23 41.882 19.978 14.035 1.00 13.95 C ATOM 186 C GLY A 23 40.485 19.730 13.490 1.00 13.74 C ATOM 187 O GLY A 23 39.507 19.711 14.255 1.00 13.81 O ATOM 188 N HIS A 24 40.369 19.561 12.175 1.00 13.07 N ATOM 189 CA HIS A 24 39.059 19.308 11.561 1.00 12.67 C ATOM 190 C HIS A 24 38.525 17.941 11.970 1.00 12.65 C ATOM 191 O HIS A 24 37.326 17.804 12.187 1.00 13.43 O ATOM 192 CB HIS A 24 39.138 19.392 10.037 1.00 10.49 C ATOM 193 CG HIS A 24 39.212 20.790 9.513 1.00 13.59 C ATOM 194 ND1 HIS A 24 40.371 21.531 9.447 1.00 10.53 N ATOM 195 CD2 HIS A 24 38.245 21.571 8.963 1.00 10.81 C ATOM 196 CE1 HIS A 24 40.078 22.706 8.860 1.00 11.16 C ATOM 197 NE2 HIS A 24 38.798 22.777 8.549 1.00 12.09 N ATOM 198 N GLY A 25 39.410 16.943 12.063 1.00 12.41 N ATOM 199 CA GLY A 25 39.014 15.593 12.468 1.00 13.17 C ATOM 200 C GLY A 25 38.428 15.545 13.875 1.00 13.87 C ATOM 201 O GLY A 25 37.460 14.826 14.124 1.00 13.35 O ATOM 202 N GLN A 26 39.034 16.291 14.804 1.00 14.34 N ATOM 203 CA GLN A 26 38.534 16.366 16.171 1.00 15.16 C ATOM 204 C GLN A 26 37.140 17.000 16.198 1.00 15.26 C ATOM 205 O GLN A 26 36.221 16.467 16.829 1.00 15.39 O ATOM 206 CB GLN A 26 39.448 17.215 17.054 1.00 17.03 C ATOM 207 CG GLN A 26 40.466 16.432 17.822 1.00 28.33 C ATOM 208 CD GLN A 26 41.526 17.332 18.433 1.00 40.00 C ATOM 209 OE1 GLN A 26 42.133 18.162 17.746 1.00 36.88 O ATOM 210 NE2 GLN A 26 41.709 17.218 19.740 1.00 36.42 N ATOM 211 N ASP A 27 37.003 18.168 15.568 1.00 10.78 N ATOM 212 CA ASP A 27 35.721 18.874 15.540 1.00 12.70 C ATOM 213 C ASP A 27 34.599 18.016 14.999 1.00 15.39 C ATOM 214 O ASP A 27 33.494 18.020 15.527 1.00 12.27 O ATOM 215 CB ASP A 27 35.820 20.133 14.669 1.00 11.23 C ATOM 216 CG ASP A 27 36.637 21.235 15.311 1.00 27.34 C ATOM 217 OD1 ASP A 27 37.197 21.014 16.412 1.00 27.80 O ATOM 218 OD2 ASP A 27 36.720 22.323 14.702 1.00 23.75 O ATOM 219 N ILE A 28 34.880 17.341 13.890 1.00 12.88 N ATOM 220 CA ILE A 28 33.906 16.477 13.242 1.00 13.76 C ATOM 221 C ILE A 28 33.472 15.291 14.124 1.00 14.47 C ATOM 222 O ILE A 28 32.263 15.032 14.276 1.00 14.63 O ATOM 223 CB ILE A 28 34.446 15.993 11.846 1.00 13.13 C ATOM 224 CG1 ILE A 28 34.381 17.154 10.842 1.00 13.35 C ATOM 225 CG2 ILE A 28 33.644 14.809 11.323 1.00 12.02 C ATOM 226 CD1 ILE A 28 35.210 16.957 9.578 1.00 12.89 C ATOM 227 N LEU A 29 34.440 14.596 14.731 1.00 15.19 N ATOM 228 CA LEU A 29 34.118 13.441 15.571 1.00 15.68 C ATOM 229 C LEU A 29 33.400 13.853 16.847 1.00 16.10 C ATOM 230 O LEU A 29 32.471 13.181 17.283 1.00 16.45 O ATOM 231 CB LEU A 29 35.359 12.614 15.898 1.00 15.76 C ATOM 232 CG LEU A 29 35.978 11.809 14.749 1.00 16.40 C ATOM 233 CD1 LEU A 29 37.043 10.854 15.303 1.00 16.35 C ATOM 234 CD2 LEU A 29 34.917 11.008 14.016 1.00 17.12 C ATOM 235 N ILE A 30 33.818 14.971 17.432 1.00 16.13 N ATOM 236 CA ILE A 30 33.178 15.463 18.644 1.00 16.60 C ATOM 237 C ILE A 30 31.725 15.839 18.311 1.00 17.11 C ATOM 238 O ILE A 30 30.798 15.495 19.058 1.00 17.25 O ATOM 239 CB ILE A 30 33.974 16.652 19.250 1.00 15.99 C ATOM 240 CG1 ILE A 30 35.260 16.118 19.907 1.00 16.25 C ATOM 241 CG2 ILE A 30 33.113 17.437 20.245 1.00 16.34 C ATOM 242 CD1 ILE A 30 36.262 17.204 20.328 1.00 15.83 C ATOM 243 N ARG A 31 31.529 16.494 17.168 1.00 16.96 N ATOM 244 CA ARG A 31 30.191 16.862 16.720 1.00 17.72 C ATOM 245 C ARG A 31 29.353 15.590 16.560 1.00 18.25 C ATOM 246 O ARG A 31 28.242 15.514 17.080 1.00 18.06 O ATOM 247 CB ARG A 31 30.274 17.644 15.403 1.00 19.03 C ATOM 248 CG ARG A 31 28.959 17.951 14.704 1.00 27.75 C ATOM 249 CD ARG A 31 27.820 18.210 15.662 1.00 35.54 C ATOM 250 NE ARG A 31 27.590 19.622 15.937 1.00 55.89 N ATOM 251 CZ ARG A 31 26.431 20.247 15.732 1.00 59.53 C ATOM 252 NH1 ARG A 31 25.407 19.623 15.163 1.00 55.77 N ATOM 253 NH2 ARG A 31 26.316 21.528 16.038 1.00 80.31 N ATOM 254 N LEU A 32 29.923 14.573 15.913 1.00 18.72 N ATOM 255 CA LEU A 32 29.229 13.303 15.710 1.00 18.89 C ATOM 256 C LEU A 32 28.820 12.652 17.035 1.00 19.55 C ATOM 257 O LEU A 32 27.656 12.283 17.216 1.00 19.27 O ATOM 258 CB LEU A 32 30.107 12.321 14.912 1.00 18.43 C ATOM 259 CG LEU A 32 29.518 10.900 14.774 1.00 18.35 C ATOM 260 CD1 LEU A 32 28.310 10.917 13.853 1.00 16.58 C ATOM 261 CD2 LEU A 32 30.569 9.897 14.281 1.00 17.13 C ATOM 262 N PHE A 33 29.785 12.525 17.950 1.00 20.12 N ATOM 263 CA PHE A 33 29.574 11.902 19.263 1.00 20.56 C ATOM 264 C PHE A 33 28.594 12.652 20.164 1.00 21.82 C ATOM 265 O PHE A 33 27.863 12.029 20.941 1.00 23.10 O ATOM 266 CB PHE A 33 30.905 11.724 19.981 1.00 19.32 C ATOM 267 CG PHE A 33 31.858 10.805 19.263 1.00 18.94 C ATOM 268 CD1 PHE A 33 31.375 9.740 18.495 1.00 17.83 C ATOM 269 CD2 PHE A 33 33.239 10.991 19.365 1.00 17.60 C ATOM 270 CE1 PHE A 33 32.254 8.878 17.843 1.00 17.15 C ATOM 271 CE2 PHE A 33 34.119 10.133 18.714 1.00 17.04 C ATOM 272 CZ PHE A 33 33.617 9.072 17.951 1.00 17.09 C ATOM 273 N LYS A 34 28.568 13.977 20.061 1.00 23.38 N ATOM 274 CA LYS A 34 27.645 14.757 20.863 1.00 25.09 C ATOM 275 C LYS A 34 26.242 14.704 20.284 1.00 25.17 C ATOM 276 O LYS A 34 25.273 14.626 21.026 1.00 38.31 O ATOM 277 CB LYS A 34 28.086 16.223 20.966 1.00 20.77 C ATOM 278 CG LYS A 34 29.350 16.430 21.783 1.00 42.45 C ATOM 279 CD LYS A 34 29.403 17.826 22.398 1.00 68.05 C ATOM 280 CE LYS A 34 29.075 18.906 21.384 1.00 74.10 C ATOM 281 NZ LYS A 34 29.655 20.230 21.749 1.00 58.94 N ATOM 282 N SER A 35 26.131 14.777 18.961 1.00 26.05 N ATOM 283 CA SER A 35 24.834 14.759 18.309 1.00 26.21 C ATOM 284 C SER A 35 24.189 13.390 18.335 1.00 26.05 C ATOM 285 O SER A 35 22.970 13.289 18.389 1.00 25.95 O ATOM 286 CB SER A 35 24.960 15.191 16.854 1.00 26.90 C ATOM 287 OG SER A 35 25.495 16.497 16.745 1.00 30.21 O ATOM 288 N HIS A 36 25.013 12.347 18.240 1.00 25.46 N ATOM 289 CA HIS A 36 24.534 10.971 18.219 1.00 25.07 C ATOM 290 C HIS A 36 25.441 10.076 19.042 1.00 24.90 C ATOM 291 O HIS A 36 26.194 9.289 18.490 1.00 25.25 O ATOM 292 CB HIS A 36 24.470 10.443 16.774 1.00 23.40 C ATOM 293 CG HIS A 36 23.718 11.332 15.835 1.00 21.61 C ATOM 294 ND1 HIS A 36 22.358 11.266 15.627 1.00 22.67 N ATOM 295 CD2 HIS A 36 24.160 12.339 15.040 1.00 23.65 C ATOM 296 CE1 HIS A 36 22.026 12.208 14.740 1.00 17.49 C ATOM 297 NE2 HIS A 36 23.084 12.890 14.349 1.00 22.98 N ATOM 298 N PRO A 37 25.290 10.107 20.377 1.00 25.00 N ATOM 299 CA PRO A 37 26.053 9.339 21.363 1.00 24.52 C ATOM 300 C PRO A 37 26.122 7.836 21.124 1.00 24.44 C ATOM 301 O PRO A 37 27.090 7.183 21.514 1.00 24.78 O ATOM 302 CB PRO A 37 25.321 9.652 22.666 1.00 25.11 C ATOM 303 CG PRO A 37 24.767 11.032 22.422 1.00 24.88 C ATOM 304 CD PRO A 37 24.219 10.875 21.045 1.00 25.04 C ATOM 305 N GLU A 38 25.106 7.280 20.478 1.00 20.50 N ATOM 306 CA GLU A 38 25.099 5.847 20.204 1.00 27.23 C ATOM 307 C GLU A 38 26.292 5.452 19.344 1.00 18.36 C ATOM 308 O GLU A 38 26.814 4.359 19.481 1.00 31.79 O ATOM 309 CB GLU A 38 23.779 5.401 19.539 1.00 20.46 C ATOM 310 CG GLU A 38 23.458 6.000 18.159 1.00 21.91 C ATOM 311 CD GLU A 38 22.672 7.310 18.209 1.00 38.03 C ATOM 312 OE1 GLU A 38 22.775 8.087 19.180 1.00 33.84 O ATOM 313 OE2 GLU A 38 21.940 7.573 17.243 1.00 40.21 O ATOM 314 N THR A 39 26.760 6.365 18.497 1.00 22.46 N ATOM 315 CA THR A 39 27.898 6.075 17.627 1.00 22.43 C ATOM 316 C THR A 39 29.208 5.857 18.383 1.00 22.93 C ATOM 317 O THR A 39 30.073 5.113 17.922 1.00 22.99 O ATOM 318 CB THR A 39 28.123 7.196 16.564 1.00 22.12 C ATOM 319 OG1 THR A 39 28.520 8.416 17.210 1.00 21.24 O ATOM 320 CG2 THR A 39 26.868 7.424 15.751 1.00 20.86 C ATOM 321 N LEU A 40 29.349 6.498 19.543 1.00 23.68 N ATOM 322 CA LEU A 40 30.572 6.385 20.345 1.00 24.19 C ATOM 323 C LEU A 40 30.847 4.950 20.795 1.00 24.28 C ATOM 324 O LEU A 40 32.011 4.538 20.938 1.00 23.83 O ATOM 325 CB LEU A 40 30.499 7.330 21.554 1.00 25.26 C ATOM 326 CG LEU A 40 31.720 7.466 22.478 1.00 25.40 C ATOM 327 CD1 LEU A 40 32.932 7.943 21.688 1.00 26.19 C ATOM 328 CD2 LEU A 40 31.414 8.440 23.599 1.00 25.83 C ATOM 329 N GLU A 41 29.770 4.184 20.962 1.00 26.00 N ATOM 330 CA GLU A 41 29.857 2.786 21.382 1.00 24.55 C ATOM 331 C GLU A 41 30.658 1.906 20.427 1.00 33.76 C ATOM 332 O GLU A 41 31.209 0.890 20.838 1.00 35.66 O ATOM 333 CB GLU A 41 28.461 2.190 21.522 1.00 33.39 C ATOM 334 CG GLU A 41 27.648 2.725 22.678 1.00 55.70 C ATOM 335 CD GLU A 41 26.298 2.048 22.772 1.00 67.02 C ATOM 336 OE1 GLU A 41 25.420 2.340 21.930 1.00 71.20 O ATOM 337 OE2 GLU A 41 26.125 1.206 23.678 1.00 75.40 O ATOM 338 N LYS A 42 30.696 2.286 19.151 1.00 33.33 N ATOM 339 CA LYS A 42 31.421 1.522 18.136 1.00 25.60 C ATOM 340 C LYS A 42 32.934 1.611 18.273 1.00 19.95 C ATOM 341 O LYS A 42 33.661 0.750 17.787 1.00 35.38 O ATOM 342 CB LYS A 42 31.007 1.987 16.739 1.00 17.82 C ATOM 343 CG LYS A 42 29.599 1.623 16.363 1.00 19.30 C ATOM 344 CD LYS A 42 29.501 0.142 16.074 1.00 28.08 C ATOM 345 CE LYS A 42 28.079 -0.270 15.763 1.00 28.38 C ATOM 346 NZ LYS A 42 28.051 -1.731 15.563 1.00 36.87 N ATOM 347 N PHE A 43 33.403 2.649 18.952 1.00 32.57 N ATOM 348 CA PHE A 43 34.832 2.864 19.120 1.00 32.86 C ATOM 349 C PHE A 43 35.357 2.428 20.479 1.00 32.97 C ATOM 350 O PHE A 43 35.455 3.224 21.407 1.00 33.11 O ATOM 351 CB PHE A 43 35.153 4.340 18.865 1.00 32.29 C ATOM 352 CG PHE A 43 34.782 4.803 17.490 1.00 32.34 C ATOM 353 CD1 PHE A 43 35.677 4.666 16.431 1.00 31.95 C ATOM 354 CD2 PHE A 43 33.530 5.349 17.243 1.00 31.84 C ATOM 355 CE1 PHE A 43 35.323 5.066 15.151 1.00 32.26 C ATOM 356 CE2 PHE A 43 33.172 5.751 15.970 1.00 32.01 C ATOM 357 CZ PHE A 43 34.071 5.609 14.920 1.00 32.21 C ATOM 358 N ASP A 44 35.775 1.175 20.555 1.00 34.16 N ATOM 359 CA ASP A 44 36.281 0.599 21.794 1.00 41.63 C ATOM 360 C ASP A 44 37.401 1.387 22.443 1.00 43.44 C ATOM 361 O ASP A 44 37.460 1.496 23.668 1.00 43.85 O ATOM 362 CB ASP A 44 36.725 -0.847 21.562 1.00 49.83 C ATOM 363 CG ASP A 44 35.608 -1.713 20.999 1.00 66.28 C ATOM 364 OD1 ASP A 44 34.412 -1.418 21.258 1.00 59.23 O ATOM 365 OD2 ASP A 44 35.929 -2.681 20.278 1.00 75.41 O ATOM 366 N ARG A 45 38.255 1.984 21.623 1.00 41.73 N ATOM 367 CA ARG A 45 39.378 2.737 22.144 1.00 41.45 C ATOM 368 C ARG A 45 39.011 4.085 22.736 1.00 40.97 C ATOM 369 O ARG A 45 39.814 4.665 23.468 1.00 41.65 O ATOM 370 CB ARG A 45 40.441 2.938 21.053 1.00 43.13 C ATOM 371 CG ARG A 45 41.785 2.307 21.396 1.00 53.08 C ATOM 372 CD ARG A 45 42.910 2.709 20.435 1.00 64.99 C ATOM 373 NE ARG A 45 42.767 2.098 19.118 1.00 80.05 N ATOM 374 CZ ARG A 45 42.767 2.777 17.974 1.00 97.64 C ATOM 375 NH1 ARG A 45 42.885 4.102 17.980 1.00100.00 N ATOM 376 NH2 ARG A 45 42.632 2.133 16.821 1.00 91.43 N ATOM 377 N VAL A 46 37.771 4.523 22.533 1.00 39.61 N ATOM 378 CA VAL A 46 37.375 5.854 22.974 1.00 38.33 C ATOM 379 C VAL A 46 35.954 5.971 23.580 1.00 38.11 C ATOM 380 O VAL A 46 35.542 7.041 24.037 1.00 37.45 O ATOM 381 CB VAL A 46 37.577 6.804 21.731 1.00 37.83 C ATOM 382 CG1 VAL A 46 36.278 7.176 21.064 1.00 36.87 C ATOM 383 CG2 VAL A 46 38.429 7.974 22.075 1.00 37.97 C ATOM 384 N LYS A 47 35.254 4.844 23.672 1.00 29.21 N ATOM 385 CA LYS A 47 33.882 4.813 24.172 1.00 23.48 C ATOM 386 C LYS A 47 33.669 5.225 25.628 1.00 24.52 C ATOM 387 O LYS A 47 32.547 5.503 26.027 1.00 33.62 O ATOM 388 CB LYS A 47 33.280 3.426 23.946 1.00 23.59 C ATOM 389 CG LYS A 47 33.623 2.411 25.019 1.00 40.22 C ATOM 390 CD LYS A 47 32.863 1.109 24.831 1.00 52.55 C ATOM 391 CE LYS A 47 33.774 0.036 24.272 1.00 62.41 C ATOM 392 NZ LYS A 47 33.077 -1.260 24.087 1.00 74.01 N ATOM 393 N HIS A 48 34.741 5.249 26.413 1.00 31.16 N ATOM 394 CA HIS A 48 34.674 5.606 27.836 1.00 31.22 C ATOM 395 C HIS A 48 34.701 7.112 28.107 1.00 30.83 C ATOM 396 O HIS A 48 34.532 7.529 29.249 1.00 31.04 O ATOM 397 CB HIS A 48 35.838 4.955 28.589 1.00 33.26 C ATOM 398 CG HIS A 48 37.177 5.474 28.169 1.00 43.81 C ATOM 399 ND1 HIS A 48 37.694 5.329 26.897 1.00 49.90 N ATOM 400 CD2 HIS A 48 38.087 6.210 28.857 1.00 46.44 C ATOM 401 CE1 HIS A 48 38.876 5.973 26.846 1.00 53.26 C ATOM 402 NE2 HIS A 48 39.163 6.526 28.010 1.00 56.20 N ATOM 403 N LEU A 49 35.003 7.911 27.083 1.00 30.17 N ATOM 404 CA LEU A 49 35.045 9.375 27.217 1.00 29.27 C ATOM 405 C LEU A 49 33.637 9.891 27.507 1.00 28.58 C ATOM 406 O LEU A 49 32.695 9.606 26.782 1.00 28.38 O ATOM 407 CB LEU A 49 35.611 10.026 25.952 1.00 29.06 C ATOM 408 CG LEU A 49 36.958 9.519 25.428 1.00 28.57 C ATOM 409 CD1 LEU A 49 37.293 10.245 24.158 1.00 28.23 C ATOM 410 CD2 LEU A 49 38.053 9.730 26.445 1.00 28.89 C ATOM 411 N LYS A 50 33.515 10.640 28.595 1.00 24.55 N ATOM 412 CA LYS A 50 32.237 11.165 29.068 1.00 29.94 C ATOM 413 C LYS A 50 31.906 12.604 28.683 1.00 23.26 C ATOM 414 O LYS A 50 30.742 12.950 28.517 1.00 34.91 O ATOM 415 CB LYS A 50 32.182 11.034 30.592 1.00 45.14 C ATOM 416 CG LYS A 50 32.451 9.622 31.126 1.00 30.35 C ATOM 417 CD LYS A 50 32.844 9.674 32.606 1.00 57.96 C ATOM 418 CE LYS A 50 32.941 8.289 33.243 1.00 49.95 C ATOM 419 NZ LYS A 50 31.612 7.630 33.359 1.00 51.06 N ATOM 420 N THR A 51 32.924 13.448 28.564 1.00 24.12 N ATOM 421 CA THR A 51 32.694 14.849 28.229 1.00 23.89 C ATOM 422 C THR A 51 33.500 15.330 27.025 1.00 23.81 C ATOM 423 O THR A 51 34.497 14.712 26.638 1.00 23.34 O ATOM 424 CB THR A 51 33.052 15.780 29.435 1.00 24.11 C ATOM 425 OG1 THR A 51 34.460 15.699 29.704 1.00 24.05 O ATOM 426 CG2 THR A 51 32.269 15.384 30.695 1.00 24.04 C ATOM 427 N GLU A 52 33.098 16.483 26.495 1.00 19.92 N ATOM 428 CA GLU A 52 33.783 17.091 25.373 1.00 23.72 C ATOM 429 C GLU A 52 35.220 17.425 25.737 1.00 23.12 C ATOM 430 O GLU A 52 36.100 17.350 24.887 1.00 25.70 O ATOM 431 CB GLU A 52 33.071 18.360 24.919 1.00 28.42 C ATOM 432 CG GLU A 52 33.779 19.038 23.744 1.00 41.68 C ATOM 433 CD GLU A 52 32.971 20.161 23.115 1.00 38.60 C ATOM 434 OE1 GLU A 52 31.764 20.277 23.415 1.00 41.28 O ATOM 435 OE2 GLU A 52 33.542 20.922 22.307 1.00 49.31 O ATOM 436 N ALA A 53 35.454 17.798 26.997 1.00 21.99 N ATOM 437 CA ALA A 53 36.800 18.129 27.454 1.00 21.32 C ATOM 438 C ALA A 53 37.678 16.893 27.382 1.00 21.17 C ATOM 439 O ALA A 53 38.845 16.975 27.014 1.00 20.69 O ATOM 440 CB ALA A 53 36.765 18.670 28.881 1.00 22.00 C ATOM 441 N GLU A 54 37.114 15.745 27.747 1.00 18.34 N ATOM 442 CA GLU A 54 37.860 14.489 27.694 1.00 20.60 C ATOM 443 C GLU A 54 38.137 14.149 26.245 1.00 22.25 C ATOM 444 O GLU A 54 39.231 13.717 25.892 1.00 19.44 O ATOM 445 CB GLU A 54 37.079 13.365 28.371 1.00 18.48 C ATOM 446 CG GLU A 54 37.087 13.500 29.882 1.00 27.00 C ATOM 447 CD GLU A 54 36.458 12.334 30.616 1.00 30.63 C ATOM 448 OE1 GLU A 54 35.749 11.528 29.990 1.00 34.98 O ATOM 449 OE2 GLU A 54 36.673 12.226 31.840 1.00 38.33 O ATOM 450 N MET A 55 37.151 14.420 25.398 1.00 22.52 N ATOM 451 CA MET A 55 37.272 14.165 23.970 1.00 22.24 C ATOM 452 C MET A 55 38.367 15.021 23.334 1.00 22.17 C ATOM 453 O MET A 55 39.210 14.508 22.593 1.00 21.68 O ATOM 454 CB MET A 55 35.937 14.411 23.293 1.00 21.93 C ATOM 455 CG MET A 55 34.971 13.294 23.521 1.00 22.76 C ATOM 456 SD MET A 55 33.389 13.680 22.839 1.00 25.74 S ATOM 457 CE MET A 55 32.348 12.662 23.891 1.00 25.19 C ATOM 458 N LYS A 56 38.397 16.302 23.700 1.00 18.45 N ATOM 459 CA LYS A 56 39.378 17.240 23.171 1.00 22.71 C ATOM 460 C LYS A 56 40.781 16.919 23.590 1.00 23.43 C ATOM 461 O LYS A 56 41.720 17.320 22.920 1.00 29.40 O ATOM 462 CB LYS A 56 39.070 18.667 23.607 1.00 13.80 C ATOM 463 CG LYS A 56 37.920 19.299 22.854 1.00 30.70 C ATOM 464 CD LYS A 56 37.687 20.715 23.319 1.00 42.22 C ATOM 465 CE LYS A 56 36.574 21.345 22.523 1.00 54.44 C ATOM 466 NZ LYS A 56 36.199 22.686 23.043 1.00 94.11 N ATOM 467 N ALA A 57 40.926 16.212 24.706 1.00 24.17 N ATOM 468 CA ALA A 57 42.245 15.870 25.207 1.00 24.10 C ATOM 469 C ALA A 57 42.712 14.501 24.759 1.00 24.17 C ATOM 470 O ALA A 57 43.892 14.178 24.861 1.00 24.80 O ATOM 471 CB ALA A 57 42.263 15.956 26.717 1.00 24.26 C ATOM 472 N SER A 58 41.791 13.705 24.233 1.00 24.05 N ATOM 473 CA SER A 58 42.106 12.360 23.794 1.00 23.68 C ATOM 474 C SER A 58 43.023 12.299 22.565 1.00 24.43 C ATOM 475 O SER A 58 42.718 12.859 21.509 1.00 24.53 O ATOM 476 CB SER A 58 40.813 11.598 23.535 1.00 23.20 C ATOM 477 OG SER A 58 41.107 10.316 23.022 1.00 23.93 O ATOM 478 N GLU A 59 44.156 11.618 22.716 1.00 25.17 N ATOM 479 CA GLU A 59 45.110 11.468 21.630 1.00 24.69 C ATOM 480 C GLU A 59 44.585 10.444 20.637 1.00 26.92 C ATOM 481 O GLU A 59 44.823 10.556 19.445 1.00 27.57 O ATOM 482 CB GLU A 59 46.472 11.027 22.172 1.00 33.92 C ATOM 483 CG GLU A 59 47.664 11.638 21.445 1.00 62.87 C ATOM 484 CD GLU A 59 47.721 13.156 21.577 1.00 74.28 C ATOM 485 OE1 GLU A 59 47.188 13.705 22.568 1.00 87.47 O ATOM 486 OE2 GLU A 59 48.308 13.806 20.687 1.00 76.06 O ATOM 487 N ASP A 60 43.867 9.442 21.134 1.00 22.66 N ATOM 488 CA ASP A 60 43.300 8.420 20.267 1.00 22.16 C ATOM 489 C ASP A 60 42.200 9.002 19.389 1.00 20.24 C ATOM 490 O ASP A 60 42.070 8.629 18.222 1.00 19.35 O ATOM 491 CB ASP A 60 42.712 7.267 21.079 1.00 26.97 C ATOM 492 CG ASP A 60 43.761 6.267 21.538 1.00 42.59 C ATOM 493 OD1 ASP A 60 44.819 6.131 20.876 1.00 46.70 O ATOM 494 OD2 ASP A 60 43.504 5.602 22.563 1.00 48.78 O ATOM 495 N LEU A 61 41.395 9.898 19.948 1.00 18.12 N ATOM 496 CA LEU A 61 40.315 10.489 19.167 1.00 18.57 C ATOM 497 C LEU A 61 40.906 11.316 18.024 1.00 18.43 C ATOM 498 O LEU A 61 40.434 11.243 16.889 1.00 18.14 O ATOM 499 CB LEU A 61 39.399 11.328 20.057 1.00 18.74 C ATOM 500 CG LEU A 61 38.104 11.870 19.443 1.00 19.52 C ATOM 501 CD1 LEU A 61 37.023 11.951 20.503 1.00 19.62 C ATOM 502 CD2 LEU A 61 38.343 13.244 18.821 1.00 19.57 C ATOM 503 N LYS A 62 41.992 12.027 18.313 1.00 14.10 N ATOM 504 CA LYS A 62 42.651 12.861 17.310 1.00 25.17 C ATOM 505 C LYS A 62 43.225 12.008 16.175 1.00 19.47 C ATOM 506 O LYS A 62 43.117 12.381 15.008 1.00 20.51 O ATOM 507 CB LYS A 62 43.738 13.726 17.957 1.00 36.01 C ATOM 508 CG LYS A 62 44.388 14.716 17.002 1.00 30.67 C ATOM 509 CD LYS A 62 45.100 15.820 17.763 1.00 57.97 C ATOM 510 CE LYS A 62 46.325 15.302 18.477 1.00 60.47 C ATOM 511 NZ LYS A 62 46.959 16.349 19.326 1.00 95.13 N ATOM 512 N LYS A 63 43.827 10.868 16.520 1.00 15.72 N ATOM 513 CA LYS A 63 44.365 9.952 15.510 1.00 17.84 C ATOM 514 C LYS A 63 43.220 9.405 14.638 1.00 16.64 C ATOM 515 O LYS A 63 43.347 9.344 13.420 1.00 22.11 O ATOM 516 CB LYS A 63 45.139 8.796 16.161 1.00 18.47 C ATOM 517 CG LYS A 63 46.337 9.278 16.971 1.00 43.82 C ATOM 518 CD LYS A 63 47.565 8.412 16.751 1.00 79.73 C ATOM 519 CE LYS A 63 47.522 7.129 17.559 1.00 64.33 C ATOM 520 NZ LYS A 63 47.697 7.392 19.011 1.00 81.18 N ATOM 521 N HIS A 64 42.102 9.040 15.260 1.00 16.01 N ATOM 522 CA HIS A 64 40.944 8.537 14.530 1.00 16.67 C ATOM 523 C HIS A 64 40.443 9.582 13.535 1.00 17.00 C ATOM 524 O HIS A 64 40.003 9.245 12.441 1.00 16.92 O ATOM 525 CB HIS A 64 39.799 8.244 15.501 1.00 18.21 C ATOM 526 CG HIS A 64 40.000 7.019 16.337 1.00 30.05 C ATOM 527 ND1 HIS A 64 39.083 6.654 17.294 1.00 35.15 N ATOM 528 CD2 HIS A 64 40.923 6.033 16.204 1.00 34.21 C ATOM 529 CE1 HIS A 64 39.458 5.462 17.709 1.00 36.97 C ATOM 530 NE2 HIS A 64 40.566 5.045 17.079 1.00 38.23 N ATOM 531 N GLY A 65 40.433 10.842 13.969 1.00 16.46 N ATOM 532 CA GLY A 65 39.978 11.919 13.114 1.00 15.97 C ATOM 533 C GLY A 65 40.872 12.059 11.892 1.00 15.92 C ATOM 534 O GLY A 65 40.372 12.239 10.788 1.00 15.66 O ATOM 535 N VAL A 66 42.187 11.997 12.087 1.00 15.57 N ATOM 536 CA VAL A 66 43.121 12.112 10.973 1.00 15.88 C ATOM 537 C VAL A 66 42.898 10.960 9.979 1.00 16.30 C ATOM 538 O VAL A 66 42.860 11.178 8.771 1.00 16.82 O ATOM 539 CB VAL A 66 44.599 12.114 11.473 1.00 16.69 C ATOM 540 CG1 VAL A 66 45.577 11.864 10.302 1.00 15.99 C ATOM 541 CG2 VAL A 66 44.929 13.452 12.140 1.00 15.60 C ATOM 542 N THR A 67 42.703 9.748 10.497 1.00 16.38 N ATOM 543 CA THR A 67 42.479 8.562 9.666 1.00 16.57 C ATOM 544 C THR A 67 41.226 8.663 8.791 1.00 16.36 C ATOM 545 O THR A 67 41.277 8.380 7.593 1.00 16.00 O ATOM 546 CB THR A 67 42.405 7.293 10.545 1.00 16.87 C ATOM 547 OG1 THR A 67 43.641 7.151 11.255 1.00 18.58 O ATOM 548 CG2 THR A 67 42.163 6.048 9.699 1.00 16.58 C ATOM 549 N VAL A 68 40.107 9.072 9.383 1.00 16.09 N ATOM 550 CA VAL A 68 38.866 9.207 8.628 1.00 16.32 C ATOM 551 C VAL A 68 38.986 10.263 7.531 1.00 15.35 C ATOM 552 O VAL A 68 38.536 10.046 6.420 1.00 14.58 O ATOM 553 CB VAL A 68 37.665 9.643 9.519 1.00 17.46 C ATOM 554 CG1 VAL A 68 36.378 9.662 8.695 1.00 18.23 C ATOM 555 CG2 VAL A 68 37.495 8.717 10.660 1.00 19.48 C ATOM 556 N LEU A 69 39.529 11.431 7.874 1.00 14.71 N ATOM 557 CA LEU A 69 39.654 12.522 6.907 1.00 14.96 C ATOM 558 C LEU A 69 40.646 12.233 5.800 1.00 14.27 C ATOM 559 O LEU A 69 40.445 12.656 4.669 1.00 14.38 O ATOM 560 CB LEU A 69 39.998 13.850 7.581 1.00 14.82 C ATOM 561 CG LEU A 69 38.924 14.450 8.497 1.00 17.52 C ATOM 562 CD1 LEU A 69 39.251 15.935 8.752 1.00 16.43 C ATOM 563 CD2 LEU A 69 37.543 14.324 7.863 1.00 18.33 C ATOM 564 N THR A 70 41.720 11.529 6.128 1.00 13.87 N ATOM 565 CA THR A 70 42.713 11.167 5.120 1.00 14.57 C ATOM 566 C THR A 70 42.090 10.168 4.107 1.00 14.49 C ATOM 567 O THR A 70 42.221 10.350 2.900 1.00 14.32 O ATOM 568 CB THR A 70 43.987 10.568 5.784 1.00 15.27 C ATOM 569 OG1 THR A 70 44.553 11.546 6.660 1.00 15.83 O ATOM 570 CG2 THR A 70 45.032 10.185 4.733 1.00 15.63 C ATOM 571 N ALA A 71 41.373 9.154 4.598 1.00 13.91 N ATOM 572 CA ALA A 71 40.723 8.185 3.707 1.00 13.99 C ATOM 573 C ALA A 71 39.624 8.870 2.885 1.00 13.64 C ATOM 574 O ALA A 71 39.512 8.641 1.686 1.00 13.91 O ATOM 575 CB ALA A 71 40.120 7.012 4.509 1.00 12.95 C ATOM 576 N LEU A 72 38.832 9.734 3.517 1.00 13.67 N ATOM 577 CA LEU A 72 37.762 10.433 2.812 1.00 13.56 C ATOM 578 C LEU A 72 38.342 11.348 1.756 1.00 13.74 C ATOM 579 O LEU A 72 37.851 11.380 0.633 1.00 13.66 O ATOM 580 CB LEU A 72 36.866 11.226 3.772 1.00 13.74 C ATOM 581 CG LEU A 72 35.719 12.004 3.093 1.00 14.92 C ATOM 582 CD1 LEU A 72 34.791 11.045 2.310 1.00 15.38 C ATOM 583 CD2 LEU A 72 34.929 12.829 4.128 1.00 14.89 C ATOM 584 N GLY A 73 39.400 12.070 2.109 1.00 13.67 N ATOM 585 CA GLY A 73 40.041 12.954 1.151 1.00 14.46 C ATOM 586 C GLY A 73 40.567 12.204 -0.077 1.00 14.58 C ATOM 587 O GLY A 73 40.436 12.672 -1.205 1.00 14.49 O ATOM 588 N ALA A 74 41.148 11.030 0.141 1.00 14.74 N ATOM 589 CA ALA A 74 41.682 10.233 -0.967 1.00 15.76 C ATOM 590 C ALA A 74 40.538 9.840 -1.920 1.00 15.76 C ATOM 591 O ALA A 74 40.685 9.855 -3.145 1.00 16.76 O ATOM 592 CB ALA A 74 42.388 9.006 -0.424 1.00 14.49 C ATOM 593 N ILE A 75 39.377 9.565 -1.346 1.00 15.77 N ATOM 594 CA ILE A 75 38.201 9.198 -2.121 1.00 15.47 C ATOM 595 C ILE A 75 37.675 10.400 -2.919 1.00 15.48 C ATOM 596 O ILE A 75 37.423 10.285 -4.112 1.00 15.82 O ATOM 597 CB ILE A 75 37.102 8.619 -1.183 1.00 15.70 C ATOM 598 CG1 ILE A 75 37.531 7.225 -0.698 1.00 16.61 C ATOM 599 CG2 ILE A 75 35.762 8.545 -1.889 1.00 15.10 C ATOM 600 CD1 ILE A 75 36.747 6.718 0.506 1.00 18.63 C ATOM 601 N LEU A 76 37.545 11.556 -2.277 1.00 15.31 N ATOM 602 CA LEU A 76 37.043 12.747 -2.960 1.00 15.33 C ATOM 603 C LEU A 76 37.938 13.174 -4.129 1.00 15.59 C ATOM 604 O LEU A 76 37.455 13.603 -5.184 1.00 15.95 O ATOM 605 CB LEU A 76 36.881 13.902 -1.967 1.00 15.64 C ATOM 606 CG LEU A 76 35.798 13.730 -0.892 1.00 15.76 C ATOM 607 CD1 LEU A 76 35.865 14.909 0.091 1.00 16.66 C ATOM 608 CD2 LEU A 76 34.400 13.596 -1.515 1.00 15.59 C ATOM 609 N LYS A 77 39.246 13.049 -3.939 1.00 10.96 N ATOM 610 CA LYS A 77 40.200 13.416 -4.971 1.00 13.75 C ATOM 611 C LYS A 77 40.129 12.553 -6.234 1.00 18.30 C ATOM 612 O LYS A 77 40.689 12.927 -7.257 1.00 18.04 O ATOM 613 CB LYS A 77 41.607 13.447 -4.396 1.00 14.38 C ATOM 614 CG LYS A 77 41.799 14.594 -3.398 1.00 17.01 C ATOM 615 CD LYS A 77 43.112 14.448 -2.663 1.00 16.79 C ATOM 616 CE LYS A 77 43.349 15.610 -1.763 1.00 20.59 C ATOM 617 NZ LYS A 77 44.698 15.538 -1.169 1.00 20.09 N ATOM 618 N LYS A 78 39.450 11.406 -6.151 1.00 15.24 N ATOM 619 CA LYS A 78 39.256 10.513 -7.302 1.00 18.28 C ATOM 620 C LYS A 78 38.107 11.011 -8.180 1.00 18.94 C ATOM 621 O LYS A 78 37.901 10.506 -9.282 1.00 19.00 O ATOM 622 CB LYS A 78 38.948 9.074 -6.855 1.00 12.31 C ATOM 623 CG LYS A 78 40.058 8.402 -6.058 1.00 25.64 C ATOM 624 CD LYS A 78 41.390 8.455 -6.784 1.00 27.27 C ATOM 625 CE LYS A 78 41.373 7.630 -8.053 1.00 32.49 C ATOM 626 NZ LYS A 78 41.223 6.175 -7.763 1.00 55.16 N ATOM 627 N LYS A 79 37.322 11.952 -7.656 1.00 15.11 N ATOM 628 CA LYS A 79 36.200 12.535 -8.398 1.00 14.03 C ATOM 629 C LYS A 79 35.218 11.516 -8.985 1.00 17.50 C ATOM 630 O LYS A 79 34.814 11.616 -10.145 1.00 20.85 O ATOM 631 CB LYS A 79 36.732 13.474 -9.488 1.00 12.58 C ATOM 632 CG LYS A 79 37.537 14.629 -8.915 1.00 15.77 C ATOM 633 CD LYS A 79 38.464 15.266 -9.921 1.00 26.30 C ATOM 634 CE LYS A 79 37.734 15.964 -11.026 1.00 37.31 C ATOM 635 NZ LYS A 79 38.682 16.840 -11.792 1.00 31.02 N ATOM 636 N GLY A 80 34.828 10.543 -8.165 1.00 17.74 N ATOM 637 CA GLY A 80 33.877 9.538 -8.600 1.00 17.93 C ATOM 638 C GLY A 80 34.472 8.216 -9.068 1.00 18.43 C ATOM 639 O GLY A 80 33.737 7.232 -9.162 1.00 19.23 O ATOM 640 N HIS A 81 35.772 8.178 -9.369 1.00 17.70 N ATOM 641 CA HIS A 81 36.424 6.948 -9.830 1.00 17.96 C ATOM 642 C HIS A 81 37.072 6.331 -8.609 1.00 18.07 C ATOM 643 O HIS A 81 38.284 6.169 -8.555 1.00 18.07 O ATOM 644 CB HIS A 81 37.488 7.302 -10.869 1.00 17.33 C ATOM 645 CG HIS A 81 36.923 7.926 -12.108 1.00 21.80 C ATOM 646 ND1 HIS A 81 36.884 9.285 -12.346 1.00 29.19 N ATOM 647 CD2 HIS A 81 36.331 7.349 -13.183 1.00 20.31 C ATOM 648 CE1 HIS A 81 36.285 9.484 -13.529 1.00 23.50 C ATOM 649 NE2 HIS A 81 35.932 8.338 -14.077 1.00 31.00 N ATOM 650 N HIS A 82 36.249 5.908 -7.659 1.00 18.15 N ATOM 651 CA HIS A 82 36.763 5.425 -6.381 1.00 18.12 C ATOM 652 C HIS A 82 36.469 3.977 -6.004 1.00 18.26 C ATOM 653 O HIS A 82 36.597 3.597 -4.836 1.00 17.89 O ATOM 654 CB HIS A 82 36.205 6.348 -5.294 1.00 16.77 C ATOM 655 CG HIS A 82 34.711 6.441 -5.314 1.00 15.19 C ATOM 656 ND1 HIS A 82 34.007 7.614 -5.167 1.00 16.60 N ATOM 657 CD2 HIS A 82 33.779 5.477 -5.529 1.00 16.77 C ATOM 658 CE1 HIS A 82 32.699 7.331 -5.300 1.00 20.03 C ATOM 659 NE2 HIS A 82 32.515 6.043 -5.521 1.00 21.22 N ATOM 660 N GLU A 83 36.022 3.194 -6.972 1.00 19.59 N ATOM 661 CA GLU A 83 35.699 1.797 -6.737 1.00 24.12 C ATOM 662 C GLU A 83 36.800 1.024 -5.987 1.00 31.10 C ATOM 663 O GLU A 83 36.516 0.307 -5.030 1.00 26.88 O ATOM 664 CB GLU A 83 35.340 1.110 -8.066 1.00 36.52 C ATOM 665 CG GLU A 83 36.267 1.451 -9.260 1.00 68.75 C ATOM 666 CD GLU A 83 36.009 2.830 -9.890 1.00 69.80 C ATOM 667 OE1 GLU A 83 34.877 3.359 -9.777 1.00 67.91 O ATOM 668 OE2 GLU A 83 36.949 3.385 -10.503 1.00 42.41 O ATOM 669 N ALA A 84 38.055 1.213 -6.380 1.00 25.65 N ATOM 670 CA ALA A 84 39.162 0.519 -5.732 1.00 25.65 C ATOM 671 C ALA A 84 39.333 0.911 -4.272 1.00 25.52 C ATOM 672 O ALA A 84 39.651 0.067 -3.441 1.00 24.98 O ATOM 673 CB ALA A 84 40.457 0.761 -6.482 1.00 25.75 C ATOM 674 N GLU A 85 39.158 2.197 -3.977 1.00 23.55 N ATOM 675 CA GLU A 85 39.296 2.714 -2.615 1.00 24.29 C ATOM 676 C GLU A 85 38.138 2.293 -1.712 1.00 20.43 C ATOM 677 O GLU A 85 38.310 2.139 -0.505 1.00 22.47 O ATOM 678 CB GLU A 85 39.400 4.247 -2.620 1.00 27.01 C ATOM 679 CG GLU A 85 40.721 4.830 -3.148 1.00 24.94 C ATOM 680 CD GLU A 85 40.884 4.748 -4.668 1.00 36.11 C ATOM 681 OE1 GLU A 85 39.887 4.578 -5.409 1.00 37.64 O ATOM 682 OE2 GLU A 85 42.034 4.872 -5.131 1.00 54.23 O ATOM 683 N LEU A 86 36.973 2.083 -2.310 1.00 21.53 N ATOM 684 CA LEU A 86 35.787 1.702 -1.567 1.00 22.37 C ATOM 685 C LEU A 86 35.717 0.249 -1.105 1.00 22.19 C ATOM 686 O LEU A 86 35.101 -0.046 -0.087 1.00 22.24 O ATOM 687 CB LEU A 86 34.534 2.016 -2.390 1.00 23.56 C ATOM 688 CG LEU A 86 33.610 3.127 -1.892 1.00 25.46 C ATOM 689 CD1 LEU A 86 34.361 4.444 -1.730 1.00 26.00 C ATOM 690 CD2 LEU A 86 32.480 3.286 -2.891 1.00 26.41 C ATOM 691 N LYS A 87 36.321 -0.663 -1.854 1.00 21.96 N ATOM 692 CA LYS A 87 36.268 -2.081 -1.510 1.00 30.39 C ATOM 693 C LYS A 87 36.767 -2.472 -0.118 1.00 23.62 C ATOM 694 O LYS A 87 36.003 -3.037 0.668 1.00 20.01 O ATOM 695 CB LYS A 87 36.927 -2.916 -2.610 1.00 31.09 C ATOM 696 CG LYS A 87 36.128 -2.843 -3.882 1.00 42.74 C ATOM 697 CD LYS A 87 36.898 -3.289 -5.102 1.00 56.03 C ATOM 698 CE LYS A 87 36.889 -4.783 -5.250 1.00 45.89 C ATOM 699 NZ LYS A 87 37.070 -5.172 -6.680 1.00 56.90 N ATOM 700 N PRO A 88 38.035 -2.155 0.219 1.00 19.60 N ATOM 701 CA PRO A 88 38.532 -2.521 1.549 1.00 19.38 C ATOM 702 C PRO A 88 37.775 -1.793 2.658 1.00 19.80 C ATOM 703 O PRO A 88 37.606 -2.324 3.758 1.00 19.67 O ATOM 704 CB PRO A 88 39.992 -2.080 1.495 1.00 19.32 C ATOM 705 CG PRO A 88 39.967 -0.918 0.532 1.00 18.97 C ATOM 706 CD PRO A 88 39.085 -1.462 -0.553 1.00 19.16 C ATOM 707 N LEU A 89 37.318 -0.580 2.345 1.00 19.25 N ATOM 708 CA LEU A 89 36.583 0.254 3.280 1.00 19.30 C ATOM 709 C LEU A 89 35.218 -0.349 3.610 1.00 18.74 C ATOM 710 O LEU A 89 34.814 -0.405 4.769 1.00 17.93 O ATOM 711 CB LEU A 89 36.372 1.625 2.653 1.00 21.41 C ATOM 712 CG LEU A 89 36.099 2.774 3.608 1.00 23.97 C ATOM 713 CD1 LEU A 89 37.351 2.949 4.488 1.00 25.15 C ATOM 714 CD2 LEU A 89 35.817 4.050 2.803 1.00 25.28 C ATOM 715 N ALA A 90 34.508 -0.786 2.577 1.00 17.83 N ATOM 716 CA ALA A 90 33.192 -1.367 2.745 1.00 17.79 C ATOM 717 C ALA A 90 33.278 -2.687 3.518 1.00 17.79 C ATOM 718 O ALA A 90 32.428 -2.990 4.355 1.00 17.57 O ATOM 719 CB ALA A 90 32.557 -1.585 1.375 1.00 18.05 C ATOM 720 N GLN A 91 34.328 -3.459 3.250 1.00 17.80 N ATOM 721 CA GLN A 91 34.500 -4.730 3.927 1.00 17.64 C ATOM 722 C GLN A 91 34.746 -4.568 5.411 1.00 17.96 C ATOM 723 O GLN A 91 34.133 -5.271 6.221 1.00 18.32 O ATOM 724 CB GLN A 91 35.631 -5.558 3.314 1.00 17.05 C ATOM 725 CG GLN A 91 35.748 -6.914 3.996 1.00 17.69 C ATOM 726 CD GLN A 91 36.726 -7.845 3.320 1.00 20.82 C ATOM 727 OE1 GLN A 91 37.821 -7.446 2.950 1.00 21.27 O ATOM 728 NE2 GLN A 91 36.334 -9.106 3.171 1.00 14.83 N ATOM 729 N SER A 92 35.650 -3.671 5.792 1.00 17.63 N ATOM 730 CA SER A 92 35.897 -3.509 7.213 1.00 17.93 C ATOM 731 C SER A 92 34.698 -2.906 7.964 1.00 18.26 C ATOM 732 O SER A 92 34.383 -3.345 9.072 1.00 18.48 O ATOM 733 CB SER A 92 37.194 -2.742 7.481 1.00 17.83 C ATOM 734 OG SER A 92 37.106 -1.411 7.053 1.00 19.43 O ATOM 735 N HIS A 93 33.977 -1.965 7.357 1.00 17.80 N ATOM 736 CA HIS A 93 32.830 -1.391 8.053 1.00 18.32 C ATOM 737 C HIS A 93 31.605 -2.282 8.092 1.00 19.08 C ATOM 738 O HIS A 93 30.800 -2.170 9.008 1.00 19.46 O ATOM 739 CB HIS A 93 32.471 -0.025 7.495 1.00 18.59 C ATOM 740 CG HIS A 93 33.484 1.016 7.821 1.00 17.57 C ATOM 741 ND1 HIS A 93 34.771 0.972 7.333 1.00 24.61 N ATOM 742 CD2 HIS A 93 33.431 2.086 8.645 1.00 20.34 C ATOM 743 CE1 HIS A 93 35.468 1.971 7.840 1.00 24.73 C ATOM 744 NE2 HIS A 93 34.677 2.662 8.641 1.00 23.04 N ATOM 745 N ALA A 94 31.466 -3.159 7.103 1.00 19.39 N ATOM 746 CA ALA A 94 30.336 -4.073 7.035 1.00 20.34 C ATOM 747 C ALA A 94 30.571 -5.311 7.893 1.00 21.10 C ATOM 748 O ALA A 94 29.773 -5.619 8.771 1.00 21.89 O ATOM 749 CB ALA A 94 30.087 -4.497 5.597 1.00 20.13 C ATOM 750 N THR A 95 31.723 -5.944 7.702 1.00 21.61 N ATOM 751 CA THR A 95 32.072 -7.190 8.386 1.00 22.02 C ATOM 752 C THR A 95 32.761 -7.073 9.742 1.00 22.53 C ATOM 753 O THR A 95 32.418 -7.798 10.669 1.00 23.24 O ATOM 754 CB THR A 95 32.954 -8.061 7.466 1.00 22.32 C ATOM 755 OG1 THR A 95 32.448 -7.974 6.131 1.00 21.73 O ATOM 756 CG2 THR A 95 32.952 -9.541 7.916 1.00 21.45 C ATOM 757 N LYS A 96 33.761 -6.211 9.859 1.00 21.64 N ATOM 758 CA LYS A 96 34.454 -6.079 11.130 1.00 26.88 C ATOM 759 C LYS A 96 33.743 -5.153 12.129 1.00 31.86 C ATOM 760 O LYS A 96 33.320 -5.591 13.197 1.00 36.78 O ATOM 761 CB LYS A 96 35.888 -5.612 10.898 1.00 28.79 C ATOM 762 CG LYS A 96 36.850 -6.013 12.015 1.00 35.57 C ATOM 763 CD LYS A 96 38.165 -5.271 11.876 1.00 55.25 C ATOM 764 CE LYS A 96 39.330 -6.051 12.456 1.00 80.34 C ATOM 765 NZ LYS A 96 39.794 -7.114 11.517 1.00 90.60 N ATOM 766 N HIS A 97 33.578 -3.888 11.755 1.00 32.04 N ATOM 767 CA HIS A 97 32.960 -2.882 12.619 1.00 32.23 C ATOM 768 C HIS A 97 31.424 -2.860 12.656 1.00 32.70 C ATOM 769 O HIS A 97 30.851 -2.412 13.653 1.00 33.29 O ATOM 770 CB HIS A 97 33.467 -1.491 12.230 1.00 31.70 C ATOM 771 CG HIS A 97 34.923 -1.448 11.869 1.00 33.74 C ATOM 772 ND1 HIS A 97 35.924 -2.049 12.601 1.00 32.24 N ATOM 773 CD2 HIS A 97 35.548 -0.834 10.830 1.00 33.36 C ATOM 774 CE1 HIS A 97 37.104 -1.781 12.004 1.00 28.00 C ATOM 775 NE2 HIS A 97 36.932 -1.044 10.923 1.00 33.21 N ATOM 776 N LYS A 98 30.768 -3.316 11.581 1.00 30.50 N ATOM 777 CA LYS A 98 29.296 -3.331 11.474 1.00 23.13 C ATOM 778 C LYS A 98 28.686 -1.951 11.683 1.00 32.58 C ATOM 779 O LYS A 98 27.986 -1.708 12.659 1.00 26.86 O ATOM 780 CB LYS A 98 28.678 -4.327 12.447 1.00 27.87 C ATOM 781 CG LYS A 98 28.118 -5.559 11.760 1.00 67.51 C ATOM 782 CD LYS A 98 28.648 -6.835 12.384 1.00 60.67 C ATOM 783 CE LYS A 98 30.163 -6.879 12.311 1.00 73.97 C ATOM 784 NZ LYS A 98 30.711 -8.157 12.837 1.00 83.45 N ATOM 785 N ILE A 99 28.905 -1.074 10.712 1.00 21.99 N ATOM 786 CA ILE A 99 28.442 0.291 10.773 1.00 21.17 C ATOM 787 C ILE A 99 27.270 0.460 9.842 1.00 21.88 C ATOM 788 O ILE A 99 27.426 0.358 8.624 1.00 22.43 O ATOM 789 CB ILE A 99 29.561 1.257 10.300 1.00 20.50 C ATOM 790 CG1 ILE A 99 30.873 0.961 11.034 1.00 20.26 C ATOM 791 CG2 ILE A 99 29.107 2.712 10.435 1.00 19.71 C ATOM 792 CD1 ILE A 99 30.785 0.967 12.536 1.00 20.31 C ATOM 793 N PRO A 100 26.078 0.743 10.391 1.00 22.07 N ATOM 794 CA PRO A 100 24.920 0.922 9.510 1.00 22.57 C ATOM 795 C PRO A 100 25.006 2.221 8.682 1.00 23.19 C ATOM 796 O PRO A 100 25.618 3.208 9.103 1.00 22.81 O ATOM 797 CB PRO A 100 23.738 0.925 10.494 1.00 22.51 C ATOM 798 CG PRO A 100 24.332 1.438 11.753 1.00 22.22 C ATOM 799 CD PRO A 100 25.681 0.764 11.810 1.00 21.66 C ATOM 800 N ILE A 101 24.423 2.196 7.488 1.00 23.79 N ATOM 801 CA ILE A 101 24.424 3.358 6.599 1.00 24.96 C ATOM 802 C ILE A 101 24.008 4.622 7.337 1.00 25.16 C ATOM 803 O ILE A 101 24.564 5.687 7.102 1.00 25.83 O ATOM 804 CB ILE A 101 23.487 3.124 5.362 1.00 25.80 C ATOM 805 CG1 ILE A 101 24.053 2.005 4.471 1.00 26.54 C ATOM 806 CG2 ILE A 101 23.274 4.405 4.571 1.00 26.60 C ATOM 807 CD1 ILE A 101 25.472 2.260 3.962 1.00 27.17 C ATOM 808 N LYS A 102 23.025 4.490 8.222 1.00 21.86 N ATOM 809 CA LYS A 102 22.502 5.598 9.034 1.00 20.48 C ATOM 810 C LYS A 102 23.627 6.382 9.736 1.00 17.82 C ATOM 811 O LYS A 102 23.554 7.603 9.864 1.00 18.65 O ATOM 812 CB LYS A 102 21.533 5.024 10.082 1.00 26.50 C ATOM 813 CG LYS A 102 20.949 6.017 11.042 1.00 49.26 C ATOM 814 CD LYS A 102 19.785 6.806 10.436 1.00 72.73 C ATOM 815 CE LYS A 102 18.800 7.307 11.515 1.00 95.55 C ATOM 816 NZ LYS A 102 17.820 8.291 11.055 1.00 82.64 N ATOM 817 N TYR A 103 24.650 5.676 10.212 1.00 16.72 N ATOM 818 CA TYR A 103 25.770 6.334 10.882 1.00 16.88 C ATOM 819 C TYR A 103 26.633 7.116 9.892 1.00 16.39 C ATOM 820 O TYR A 103 27.285 8.086 10.272 1.00 16.20 O ATOM 821 CB TYR A 103 26.632 5.325 11.640 1.00 16.57 C ATOM 822 CG TYR A 103 26.030 4.762 12.921 1.00 17.87 C ATOM 823 CD1 TYR A 103 24.699 4.981 13.261 1.00 18.98 C ATOM 824 CD2 TYR A 103 26.801 3.979 13.772 1.00 18.35 C ATOM 825 CE1 TYR A 103 24.154 4.420 14.429 1.00 20.22 C ATOM 826 CE2 TYR A 103 26.278 3.418 14.922 1.00 19.76 C ATOM 827 CZ TYR A 103 24.964 3.636 15.245 1.00 20.94 C ATOM 828 OH TYR A 103 24.462 3.049 16.379 1.00 22.91 O ATOM 829 N LEU A 104 26.675 6.663 8.637 1.00 16.33 N ATOM 830 CA LEU A 104 27.444 7.353 7.598 1.00 15.99 C ATOM 831 C LEU A 104 26.701 8.648 7.254 1.00 15.96 C ATOM 832 O LEU A 104 27.323 9.662 6.922 1.00 15.10 O ATOM 833 CB LEU A 104 27.647 6.465 6.369 1.00 16.49 C ATOM 834 CG LEU A 104 28.432 5.162 6.632 1.00 17.26 C ATOM 835 CD1 LEU A 104 28.544 4.350 5.344 1.00 18.13 C ATOM 836 CD2 LEU A 104 29.811 5.451 7.185 1.00 16.64 C ATOM 837 N GLU A 105 25.373 8.623 7.359 1.00 11.84 N ATOM 838 CA GLU A 105 24.583 9.832 7.142 1.00 16.11 C ATOM 839 C GLU A 105 24.880 10.814 8.294 1.00 15.21 C ATOM 840 O GLU A 105 25.044 12.013 8.066 1.00 15.53 O ATOM 841 CB GLU A 105 23.096 9.507 7.144 1.00 15.95 C ATOM 842 CG GLU A 105 22.609 8.830 5.879 1.00 30.07 C ATOM 843 CD GLU A 105 21.179 8.312 5.980 1.00 39.99 C ATOM 844 OE1 GLU A 105 20.511 8.546 6.946 1.00 37.58 O ATOM 845 OE2 GLU A 105 20.751 7.619 5.044 1.00 41.07 O ATOM 846 N PHE A 106 24.962 10.292 9.523 1.00 15.05 N ATOM 847 CA PHE A 106 25.255 11.114 10.696 1.00 15.17 C ATOM 848 C PHE A 106 26.614 11.810 10.592 1.00 14.86 C ATOM 849 O PHE A 106 26.725 12.979 10.954 1.00 14.34 O ATOM 850 CB PHE A 106 25.234 10.287 11.985 1.00 16.09 C ATOM 851 CG PHE A 106 23.864 9.765 12.376 1.00 17.81 C ATOM 852 CD1 PHE A 106 22.710 10.224 11.754 1.00 18.00 C ATOM 853 CD2 PHE A 106 23.739 8.826 13.396 1.00 17.99 C ATOM 854 CE1 PHE A 106 21.459 9.757 12.147 1.00 18.79 C ATOM 855 CE2 PHE A 106 22.487 8.360 13.790 1.00 18.31 C ATOM 856 CZ PHE A 106 21.357 8.827 13.166 1.00 18.23 C ATOM 857 N ILE A 107 27.648 11.092 10.149 1.00 14.34 N ATOM 858 CA ILE A 107 28.968 11.707 10.027 1.00 14.48 C ATOM 859 C ILE A 107 28.984 12.711 8.863 1.00 15.05 C ATOM 860 O ILE A 107 29.715 13.709 8.907 1.00 15.26 O ATOM 861 CB ILE A 107 30.134 10.663 9.904 1.00 14.62 C ATOM 862 CG1 ILE A 107 31.483 11.353 10.220 1.00 14.37 C ATOM 863 CG2 ILE A 107 30.164 10.034 8.505 1.00 13.15 C ATOM 864 CD1 ILE A 107 32.676 10.403 10.336 1.00 14.25 C ATOM 865 N SER A 108 28.159 12.460 7.842 1.00 15.26 N ATOM 866 CA SER A 108 28.047 13.363 6.693 1.00 15.68 C ATOM 867 C SER A 108 27.545 14.710 7.184 1.00 15.90 C ATOM 868 O SER A 108 28.077 15.757 6.805 1.00 16.25 O ATOM 869 CB SER A 108 27.082 12.802 5.652 1.00 15.50 C ATOM 870 OG SER A 108 27.672 11.680 5.004 1.00 17.49 O ATOM 871 N GLU A 109 26.527 14.660 8.044 1.00 17.48 N ATOM 872 CA GLU A 109 25.931 15.835 8.659 1.00 19.02 C ATOM 873 C GLU A 109 26.971 16.580 9.497 1.00 9.86 C ATOM 874 O GLU A 109 27.023 17.810 9.482 1.00 10.23 O ATOM 875 CB GLU A 109 24.769 15.399 9.554 1.00 17.30 C ATOM 876 CG GLU A 109 24.105 16.524 10.329 1.00 35.11 C ATOM 877 CD GLU A 109 23.070 16.017 11.339 1.00 74.83 C ATOM 878 OE1 GLU A 109 23.176 14.858 11.820 1.00 60.11 O ATOM 879 OE2 GLU A 109 22.145 16.795 11.664 1.00 88.99 O ATOM 880 N ALA A 110 27.790 15.836 10.231 1.00 11.06 N ATOM 881 CA ALA A 110 28.823 16.443 11.075 1.00 12.23 C ATOM 882 C ALA A 110 29.872 17.166 10.216 1.00 12.35 C ATOM 883 O ALA A 110 30.348 18.255 10.580 1.00 13.15 O ATOM 884 CB ALA A 110 29.494 15.379 11.961 1.00 11.22 C ATOM 885 N ILE A 111 30.210 16.571 9.071 1.00 11.96 N ATOM 886 CA ILE A 111 31.192 17.159 8.161 1.00 12.38 C ATOM 887 C ILE A 111 30.672 18.484 7.591 1.00 12.69 C ATOM 888 O ILE A 111 31.343 19.516 7.658 1.00 12.48 O ATOM 889 CB ILE A 111 31.555 16.179 7.013 1.00 12.70 C ATOM 890 CG1 ILE A 111 32.413 15.038 7.574 1.00 12.53 C ATOM 891 CG2 ILE A 111 32.315 16.930 5.885 1.00 11.83 C ATOM 892 CD1 ILE A 111 32.451 13.805 6.706 1.00 13.30 C ATOM 893 N ILE A 112 29.443 18.457 7.105 1.00 13.31 N ATOM 894 CA ILE A 112 28.832 19.645 6.544 1.00 14.91 C ATOM 895 C ILE A 112 28.716 20.761 7.590 1.00 15.30 C ATOM 896 O ILE A 112 28.997 21.930 7.286 1.00 15.30 O ATOM 897 CB ILE A 112 27.467 19.295 5.938 1.00 15.57 C ATOM 898 CG1 ILE A 112 27.686 18.453 4.680 1.00 15.70 C ATOM 899 CG2 ILE A 112 26.644 20.576 5.645 1.00 16.14 C ATOM 900 CD1 ILE A 112 26.396 17.872 4.128 1.00 18.03 C ATOM 901 N HIS A 113 28.366 20.386 8.825 1.00 14.97 N ATOM 902 CA HIS A 113 28.230 21.342 9.908 1.00 15.13 C ATOM 903 C HIS A 113 29.552 22.034 10.221 1.00 15.44 C ATOM 904 O HIS A 113 29.598 23.249 10.435 1.00 15.64 O ATOM 905 CB HIS A 113 27.730 20.650 11.178 1.00 17.79 C ATOM 906 CG HIS A 113 27.597 21.579 12.347 1.00 23.44 C ATOM 907 ND1 HIS A 113 26.452 22.286 12.641 1.00 29.78 N ATOM 908 CD2 HIS A 113 28.524 21.990 13.250 1.00 24.06 C ATOM 909 CE1 HIS A 113 26.719 23.099 13.675 1.00 24.39 C ATOM 910 NE2 HIS A 113 27.966 22.954 14.080 1.00 29.30 N ATOM 911 N VAL A 114 30.618 21.250 10.294 1.00 14.94 N ATOM 912 CA VAL A 114 31.931 21.791 10.611 1.00 14.73 C ATOM 913 C VAL A 114 32.499 22.683 9.505 1.00 14.66 C ATOM 914 O VAL A 114 33.068 23.740 9.813 1.00 14.94 O ATOM 915 CB VAL A 114 32.920 20.662 10.987 1.00 14.48 C ATOM 916 CG1 VAL A 114 34.340 21.219 11.164 1.00 13.11 C ATOM 917 CG2 VAL A 114 32.440 19.999 12.268 1.00 13.96 C ATOM 918 N LEU A 115 32.338 22.280 8.237 1.00 13.94 N ATOM 919 CA LEU A 115 32.835 23.092 7.122 1.00 13.91 C ATOM 920 C LEU A 115 32.080 24.408 7.094 1.00 14.23 C ATOM 921 O LEU A 115 32.648 25.463 6.832 1.00 13.51 O ATOM 922 CB LEU A 115 32.666 22.375 5.781 1.00 14.09 C ATOM 923 CG LEU A 115 33.424 21.045 5.668 1.00 15.85 C ATOM 924 CD1 LEU A 115 33.409 20.552 4.236 1.00 16.60 C ATOM 925 CD2 LEU A 115 34.834 21.202 6.155 1.00 15.79 C ATOM 926 N HIS A 116 30.786 24.333 7.380 1.00 14.42 N ATOM 927 CA HIS A 116 29.968 25.515 7.403 1.00 15.44 C ATOM 928 C HIS A 116 30.475 26.489 8.469 1.00 16.15 C ATOM 929 O HIS A 116 30.602 27.680 8.191 1.00 16.39 O ATOM 930 CB HIS A 116 28.511 25.146 7.646 1.00 15.97 C ATOM 931 CG HIS A 116 27.603 26.331 7.736 1.00 23.94 C ATOM 932 ND1 HIS A 116 27.213 27.089 6.653 1.00 27.64 N ATOM 933 CD2 HIS A 116 27.027 26.913 8.821 1.00 20.22 C ATOM 934 CE1 HIS A 116 26.432 28.083 7.102 1.00 23.91 C ATOM 935 NE2 HIS A 116 26.290 28.016 8.411 1.00 30.41 N ATOM 936 N SER A 117 30.831 25.980 9.651 1.00 16.25 N ATOM 937 CA SER A 117 31.319 26.838 10.732 1.00 17.46 C ATOM 938 C SER A 117 32.694 27.451 10.476 1.00 16.93 C ATOM 939 O SER A 117 32.892 28.658 10.634 1.00 16.79 O ATOM 940 CB SER A 117 31.411 26.060 12.046 1.00 17.33 C ATOM 941 OG SER A 117 30.143 25.595 12.424 1.00 23.22 O ATOM 942 N ARG A 118 33.642 26.604 10.099 1.00 16.00 N ATOM 943 CA ARG A 118 35.002 27.048 9.883 1.00 16.09 C ATOM 944 C ARG A 118 35.311 27.709 8.563 1.00 16.42 C ATOM 945 O ARG A 118 36.267 28.465 8.477 1.00 16.85 O ATOM 946 CB ARG A 118 35.956 25.877 10.095 1.00 16.31 C ATOM 947 CG ARG A 118 35.923 25.326 11.507 1.00 17.66 C ATOM 948 CD ARG A 118 36.833 24.121 11.658 1.00 18.91 C ATOM 949 NE ARG A 118 38.232 24.485 11.507 1.00 23.08 N ATOM 950 CZ ARG A 118 39.221 23.958 12.218 1.00 28.58 C ATOM 951 NH1 ARG A 118 38.969 23.042 13.139 1.00 19.83 N ATOM 952 NH2 ARG A 118 40.465 24.345 11.995 1.00 22.14 N ATOM 953 N HIS A 119 34.513 27.438 7.535 1.00 16.21 N ATOM 954 CA HIS A 119 34.776 27.995 6.215 1.00 16.52 C ATOM 955 C HIS A 119 33.570 28.657 5.558 1.00 16.96 C ATOM 956 O HIS A 119 33.264 28.372 4.401 1.00 16.55 O ATOM 957 CB HIS A 119 35.322 26.881 5.307 1.00 15.35 C ATOM 958 CG HIS A 119 36.503 26.173 5.887 1.00 16.81 C ATOM 959 ND1 HIS A 119 37.754 26.740 6.014 1.00 17.07 N ATOM 960 CD2 HIS A 119 36.596 24.945 6.456 1.00 12.45 C ATOM 961 CE1 HIS A 119 38.553 25.864 6.649 1.00 15.79 C ATOM 962 NE2 HIS A 119 37.906 24.754 6.940 1.00 14.56 N ATOM 963 N PRO A 120 32.924 29.613 6.253 1.00 17.60 N ATOM 964 CA PRO A 120 31.752 30.293 5.690 1.00 18.44 C ATOM 965 C PRO A 120 31.994 30.906 4.305 1.00 18.89 C ATOM 966 O PRO A 120 31.163 30.775 3.420 1.00 19.93 O ATOM 967 CB PRO A 120 31.416 31.353 6.755 1.00 18.40 C ATOM 968 CG PRO A 120 32.734 31.641 7.386 1.00 18.17 C ATOM 969 CD PRO A 120 33.343 30.256 7.512 1.00 17.55 C ATOM 970 N GLY A 121 33.168 31.490 4.101 1.00 19.23 N ATOM 971 CA GLY A 121 33.482 32.098 2.826 1.00 19.49 C ATOM 972 C GLY A 121 33.638 31.118 1.674 1.00 19.88 C ATOM 973 O GLY A 121 33.383 31.492 0.531 1.00 21.13 O ATOM 974 N ASN A 122 34.066 29.885 1.947 1.00 18.33 N ATOM 975 CA ASN A 122 34.224 28.896 0.881 1.00 17.56 C ATOM 976 C ASN A 122 33.145 27.830 0.958 1.00 17.40 C ATOM 977 O ASN A 122 33.271 26.768 0.330 1.00 18.22 O ATOM 978 CB ASN A 122 35.603 28.215 0.956 1.00 16.47 C ATOM 979 CG ASN A 122 36.744 29.175 0.651 1.00 23.94 C ATOM 980 OD1 ASN A 122 37.668 29.352 1.452 1.00 21.42 O ATOM 981 ND2 ASN A 122 36.674 29.812 -0.504 1.00 17.36 N ATOM 982 N PHE A 123 32.082 28.095 1.714 1.00 16.20 N ATOM 983 CA PHE A 123 31.031 27.091 1.861 1.00 15.22 C ATOM 984 C PHE A 123 29.638 27.707 1.810 1.00 15.07 C ATOM 985 O PHE A 123 28.854 27.581 2.755 1.00 14.90 O ATOM 986 CB PHE A 123 31.233 26.291 3.167 1.00 14.16 C ATOM 987 CG PHE A 123 30.680 24.889 3.137 1.00 13.87 C ATOM 988 CD1 PHE A 123 31.217 23.933 2.294 1.00 13.81 C ATOM 989 CD2 PHE A 123 29.654 24.508 4.002 1.00 13.82 C ATOM 990 CE1 PHE A 123 30.736 22.601 2.319 1.00 14.46 C ATOM 991 CE2 PHE A 123 29.175 23.194 4.037 1.00 13.98 C ATOM 992 CZ PHE A 123 29.714 22.240 3.198 1.00 14.00 C ATOM 993 N GLY A 124 29.374 28.424 0.723 1.00 14.89 N ATOM 994 CA GLY A 124 28.066 29.008 0.499 1.00 14.52 C ATOM 995 C GLY A 124 27.131 27.883 0.064 1.00 14.67 C ATOM 996 O GLY A 124 27.517 26.713 0.061 1.00 13.74 O ATOM 997 N ALA A 125 25.924 28.240 -0.357 1.00 14.54 N ATOM 998 CA ALA A 125 24.917 27.259 -0.746 1.00 14.94 C ATOM 999 C ALA A 125 25.330 26.324 -1.882 1.00 15.13 C ATOM 1000 O ALA A 125 25.058 25.124 -1.837 1.00 15.68 O ATOM 1001 CB ALA A 125 23.600 27.970 -1.090 1.00 14.69 C ATOM 1002 N ASP A 126 25.955 26.880 -2.913 1.00 13.43 N ATOM 1003 CA ASP A 126 26.388 26.088 -4.051 1.00 10.99 C ATOM 1004 C ASP A 126 27.429 25.070 -3.619 1.00 14.91 C ATOM 1005 O ASP A 126 27.315 23.908 -3.964 1.00 15.09 O ATOM 1006 CB ASP A 126 26.948 26.989 -5.153 1.00 21.24 C ATOM 1007 CG ASP A 126 25.867 27.804 -5.856 1.00 26.37 C ATOM 1008 OD1 ASP A 126 24.685 27.408 -5.820 1.00 25.47 O ATOM 1009 OD2 ASP A 126 26.209 28.840 -6.458 1.00 35.73 O ATOM 1010 N ALA A 127 28.446 25.508 -2.875 1.00 13.00 N ATOM 1011 CA ALA A 127 29.495 24.603 -2.377 1.00 13.19 C ATOM 1012 C ALA A 127 28.926 23.532 -1.425 1.00 13.50 C ATOM 1013 O ALA A 127 29.358 22.381 -1.455 1.00 14.17 O ATOM 1014 CB ALA A 127 30.631 25.403 -1.677 1.00 12.59 C ATOM 1015 N GLN A 128 27.973 23.902 -0.575 1.00 12.96 N ATOM 1016 CA GLN A 128 27.375 22.922 0.329 1.00 13.45 C ATOM 1017 C GLN A 128 26.566 21.885 -0.482 1.00 13.71 C ATOM 1018 O GLN A 128 26.579 20.692 -0.161 1.00 14.19 O ATOM 1019 CB GLN A 128 26.479 23.596 1.390 1.00 13.18 C ATOM 1020 CG GLN A 128 25.765 22.583 2.295 1.00 15.46 C ATOM 1021 CD GLN A 128 25.069 23.195 3.504 1.00 17.66 C ATOM 1022 OE1 GLN A 128 25.372 24.311 3.925 1.00 19.04 O ATOM 1023 NE2 GLN A 128 24.140 22.445 4.081 1.00 16.30 N ATOM 1024 N GLY A 129 25.861 22.348 -1.516 1.00 13.17 N ATOM 1025 CA GLY A 129 25.088 21.443 -2.354 1.00 13.25 C ATOM 1026 C GLY A 129 26.014 20.439 -3.043 1.00 13.29 C ATOM 1027 O GLY A 129 25.688 19.247 -3.146 1.00 13.24 O ATOM 1028 N ALA A 130 27.172 20.913 -3.501 1.00 12.37 N ATOM 1029 CA ALA A 130 28.145 20.044 -4.156 1.00 13.20 C ATOM 1030 C ALA A 130 28.715 19.001 -3.176 1.00 13.32 C ATOM 1031 O ALA A 130 28.837 17.822 -3.517 1.00 13.58 O ATOM 1032 CB ALA A 130 29.268 20.869 -4.757 1.00 12.82 C ATOM 1033 N MET A 131 29.046 19.439 -1.963 1.00 13.52 N ATOM 1034 CA MET A 131 29.592 18.553 -0.926 1.00 14.15 C ATOM 1035 C MET A 131 28.563 17.476 -0.540 1.00 13.73 C ATOM 1036 O MET A 131 28.891 16.292 -0.427 1.00 12.90 O ATOM 1037 CB MET A 131 30.018 19.379 0.312 1.00 14.76 C ATOM 1038 CG MET A 131 30.675 18.564 1.445 1.00 15.74 C ATOM 1039 SD MET A 131 32.201 17.676 0.927 1.00 18.67 S ATOM 1040 CE MET A 131 33.349 18.957 1.034 1.00 16.91 C ATOM 1041 N ASN A 132 27.317 17.899 -0.341 1.00 13.80 N ATOM 1042 CA ASN A 132 26.253 16.967 -0.011 1.00 14.77 C ATOM 1043 C ASN A 132 26.109 15.913 -1.129 1.00 15.12 C ATOM 1044 O ASN A 132 25.927 14.725 -0.860 1.00 15.96 O ATOM 1045 CB ASN A 132 24.925 17.699 0.156 1.00 13.92 C ATOM 1046 CG ASN A 132 23.770 16.739 0.357 1.00 16.64 C ATOM 1047 OD1 ASN A 132 23.803 15.923 1.265 1.00 17.59 O ATOM 1048 ND2 ASN A 132 22.777 16.796 -0.521 1.00 18.26 N ATOM 1049 N LYS A 133 26.201 16.364 -2.377 1.00 17.32 N ATOM 1050 CA LYS A 133 26.084 15.489 -3.538 1.00 14.82 C ATOM 1051 C LYS A 133 27.246 14.480 -3.574 1.00 17.90 C ATOM 1052 O LYS A 133 27.050 13.289 -3.860 1.00 13.48 O ATOM 1053 CB LYS A 133 26.057 16.345 -4.803 1.00 19.71 C ATOM 1054 CG LYS A 133 25.420 15.682 -5.984 1.00 28.22 C ATOM 1055 CD LYS A 133 25.308 16.625 -7.163 1.00 27.62 C ATOM 1056 CE LYS A 133 24.914 15.859 -8.413 1.00 52.97 C ATOM 1057 NZ LYS A 133 24.905 16.725 -9.614 1.00 74.53 N ATOM 1058 N ALA A 134 28.442 14.950 -3.229 1.00 12.87 N ATOM 1059 CA ALA A 134 29.630 14.091 -3.218 1.00 13.47 C ATOM 1060 C ALA A 134 29.534 13.030 -2.115 1.00 13.87 C ATOM 1061 O ALA A 134 29.860 11.859 -2.339 1.00 14.49 O ATOM 1062 CB ALA A 134 30.910 14.939 -3.056 1.00 12.22 C ATOM 1063 N LEU A 135 29.034 13.434 -0.946 1.00 13.82 N ATOM 1064 CA LEU A 135 28.879 12.522 0.189 1.00 13.98 C ATOM 1065 C LEU A 135 27.727 11.537 -0.044 1.00 14.11 C ATOM 1066 O LEU A 135 27.775 10.407 0.425 1.00 14.20 O ATOM 1067 CB LEU A 135 28.695 13.310 1.496 1.00 13.75 C ATOM 1068 CG LEU A 135 29.929 14.062 2.025 1.00 14.13 C ATOM 1069 CD1 LEU A 135 29.580 14.870 3.284 1.00 13.81 C ATOM 1070 CD2 LEU A 135 31.034 13.075 2.339 1.00 13.90 C ATOM 1071 N GLU A 136 26.679 11.973 -0.744 1.00 13.49 N ATOM 1072 CA GLU A 136 25.573 11.074 -1.066 1.00 16.04 C ATOM 1073 C GLU A 136 26.067 9.999 -2.047 1.00 14.96 C ATOM 1074 O GLU A 136 25.653 8.831 -1.963 1.00 16.34 O ATOM 1075 CB GLU A 136 24.414 11.828 -1.707 1.00 12.46 C ATOM 1076 CG GLU A 136 23.703 12.789 -0.789 1.00 44.80 C ATOM 1077 CD GLU A 136 22.473 13.394 -1.432 1.00 52.55 C ATOM 1078 OE1 GLU A 136 22.235 13.142 -2.637 1.00 48.81 O ATOM 1079 OE2 GLU A 136 21.740 14.118 -0.728 1.00 56.19 O ATOM 1080 N LEU A 137 26.900 10.421 -3.008 1.00 15.12 N ATOM 1081 CA LEU A 137 27.482 9.515 -4.002 1.00 15.96 C ATOM 1082 C LEU A 137 28.283 8.449 -3.238 1.00 15.89 C ATOM 1083 O LEU A 137 28.123 7.250 -3.486 1.00 15.91 O ATOM 1084 CB LEU A 137 28.393 10.273 -4.992 1.00 16.54 C ATOM 1085 CG LEU A 137 29.149 9.382 -5.990 1.00 17.78 C ATOM 1086 CD1 LEU A 137 28.184 8.728 -6.969 1.00 19.20 C ATOM 1087 CD2 LEU A 137 30.192 10.163 -6.740 1.00 18.22 C ATOM 1088 N PHE A 138 29.104 8.901 -2.290 1.00 15.56 N ATOM 1089 CA PHE A 138 29.901 8.016 -1.440 1.00 16.09 C ATOM 1090 C PHE A 138 29.003 7.006 -0.703 1.00 15.97 C ATOM 1091 O PHE A 138 29.276 5.805 -0.743 1.00 16.01 O ATOM 1092 CB PHE A 138 30.706 8.854 -0.438 1.00 17.10 C ATOM 1093 CG PHE A 138 31.336 8.055 0.682 1.00 18.65 C ATOM 1094 CD1 PHE A 138 32.408 7.211 0.438 1.00 19.08 C ATOM 1095 CD2 PHE A 138 30.851 8.152 1.981 1.00 18.98 C ATOM 1096 CE1 PHE A 138 32.983 6.479 1.465 1.00 19.60 C ATOM 1097 CE2 PHE A 138 31.426 7.417 3.011 1.00 19.50 C ATOM 1098 CZ PHE A 138 32.496 6.579 2.748 1.00 19.07 C ATOM 1099 N ARG A 139 27.936 7.487 -0.055 1.00 15.51 N ATOM 1100 CA ARG A 139 27.002 6.615 0.673 1.00 16.38 C ATOM 1101 C ARG A 139 26.266 5.598 -0.209 1.00 16.38 C ATOM 1102 O ARG A 139 25.990 4.478 0.225 1.00 17.17 O ATOM 1103 CB ARG A 139 25.967 7.431 1.468 1.00 14.71 C ATOM 1104 CG ARG A 139 26.585 8.244 2.606 1.00 21.56 C ATOM 1105 CD ARG A 139 25.567 8.664 3.645 1.00 14.30 C ATOM 1106 NE ARG A 139 24.454 9.404 3.064 1.00 18.17 N ATOM 1107 CZ ARG A 139 24.460 10.703 2.777 1.00 21.08 C ATOM 1108 NH1 ARG A 139 25.530 11.459 3.004 1.00 20.58 N ATOM 1109 NH2 ARG A 139 23.378 11.247 2.255 1.00 16.97 N ATOM 1110 N LYS A 140 25.890 6.026 -1.411 1.00 16.09 N ATOM 1111 CA LYS A 140 25.192 5.173 -2.374 1.00 20.00 C ATOM 1112 C LYS A 140 26.098 4.014 -2.808 1.00 21.76 C ATOM 1113 O LYS A 140 25.676 2.863 -2.836 1.00 14.42 O ATOM 1114 CB LYS A 140 24.790 5.986 -3.611 1.00 27.06 C ATOM 1115 CG LYS A 140 23.972 5.206 -4.634 1.00 45.99 C ATOM 1116 CD LYS A 140 23.402 6.100 -5.741 1.00 79.30 C ATOM 1117 CE LYS A 140 24.365 6.287 -6.920 1.00 85.35 C ATOM 1118 NZ LYS A 140 25.631 6.990 -6.564 1.00 82.64 N ATOM 1119 N ASP A 141 27.341 4.329 -3.160 1.00 13.76 N ATOM 1120 CA ASP A 141 28.285 3.302 -3.582 1.00 14.64 C ATOM 1121 C ASP A 141 28.650 2.361 -2.438 1.00 18.09 C ATOM 1122 O ASP A 141 28.698 1.146 -2.626 1.00 18.83 O ATOM 1123 CB ASP A 141 29.519 3.943 -4.215 1.00 17.81 C ATOM 1124 CG ASP A 141 29.211 4.607 -5.550 1.00 21.65 C ATOM 1125 OD1 ASP A 141 28.120 4.365 -6.097 1.00 22.33 O ATOM 1126 OD2 ASP A 141 30.043 5.385 -6.048 1.00 22.08 O ATOM 1127 N ILE A 142 28.849 2.907 -1.243 1.00 19.69 N ATOM 1128 CA ILE A 142 29.172 2.078 -0.082 1.00 20.48 C ATOM 1129 C ILE A 142 28.030 1.100 0.235 1.00 20.33 C ATOM 1130 O ILE A 142 28.283 -0.080 0.528 1.00 20.05 O ATOM 1131 CB ILE A 142 29.456 2.930 1.190 1.00 21.51 C ATOM 1132 CG1 ILE A 142 30.911 3.387 1.209 1.00 23.16 C ATOM 1133 CG2 ILE A 142 29.196 2.110 2.455 1.00 22.03 C ATOM 1134 CD1 ILE A 142 31.869 2.331 1.774 1.00 24.63 C ATOM 1135 N ALA A 143 26.786 1.591 0.204 1.00 19.87 N ATOM 1136 CA ALA A 143 25.639 0.732 0.505 1.00 20.12 C ATOM 1137 C ALA A 143 25.446 -0.353 -0.549 1.00 20.01 C ATOM 1138 O ALA A 143 25.058 -1.458 -0.215 1.00 20.33 O ATOM 1139 CB ALA A 143 24.379 1.531 0.717 1.00 19.82 C ATOM 1140 N ALA A 144 25.776 -0.058 -1.804 1.00 19.98 N ATOM 1141 CA ALA A 144 25.681 -1.066 -2.853 1.00 20.13 C ATOM 1142 C ALA A 144 26.718 -2.168 -2.538 1.00 20.63 C ATOM 1143 O ALA A 144 26.431 -3.366 -2.671 1.00 20.63 O ATOM 1144 CB ALA A 144 25.962 -0.444 -4.200 1.00 19.92 C ATOM 1145 N LYS A 145 27.908 -1.759 -2.090 1.00 14.94 N ATOM 1146 CA LYS A 145 28.961 -2.703 -1.733 1.00 18.47 C ATOM 1147 C LYS A 145 28.572 -3.526 -0.501 1.00 19.66 C ATOM 1148 O LYS A 145 28.871 -4.722 -0.426 1.00 17.53 O ATOM 1149 CB LYS A 145 30.280 -1.969 -1.501 1.00 17.80 C ATOM 1150 CG LYS A 145 31.031 -1.636 -2.759 1.00 36.20 C ATOM 1151 CD LYS A 145 30.080 -1.244 -3.902 1.00 73.26 C ATOM 1152 CE LYS A 145 30.622 -0.117 -4.755 1.00 63.31 C ATOM 1153 NZ LYS A 145 29.511 0.471 -5.560 1.00 26.86 N ATOM 1154 N TYR A 146 27.903 -2.885 0.455 1.00 19.77 N ATOM 1155 CA TYR A 146 27.428 -3.564 1.666 1.00 19.91 C ATOM 1156 C TYR A 146 26.536 -4.755 1.286 1.00 19.89 C ATOM 1157 O TYR A 146 26.667 -5.858 1.817 1.00 19.66 O ATOM 1158 CB TYR A 146 26.589 -2.598 2.503 1.00 20.59 C ATOM 1159 CG TYR A 146 27.328 -1.832 3.587 1.00 21.16 C ATOM 1160 CD1 TYR A 146 28.716 -1.668 3.565 1.00 20.53 C ATOM 1161 CD2 TYR A 146 26.618 -1.268 4.649 1.00 22.22 C ATOM 1162 CE1 TYR A 146 29.372 -0.960 4.584 1.00 20.93 C ATOM 1163 CE2 TYR A 146 27.263 -0.561 5.660 1.00 22.12 C ATOM 1164 CZ TYR A 146 28.625 -0.411 5.625 1.00 21.42 C ATOM 1165 OH TYR A 146 29.207 0.309 6.636 1.00 20.90 O ATOM 1166 N LYS A 147 25.611 -4.506 0.371 1.00 19.69 N ATOM 1167 CA LYS A 147 24.702 -5.535 -0.111 1.00 21.47 C ATOM 1168 C LYS A 147 25.451 -6.695 -0.780 1.00 18.52 C ATOM 1169 O LYS A 147 25.205 -7.858 -0.464 1.00 21.47 O ATOM 1170 CB LYS A 147 23.851 -4.999 -1.248 1.00 20.52 C ATOM 1171 CG LYS A 147 22.578 -5.867 -1.484 1.00 32.74 C ATOM 1172 CD LYS A 147 21.612 -5.212 -2.434 1.00 64.47 C ATOM 1173 CE LYS A 147 20.772 -6.289 -3.099 1.00 83.74 C ATOM 1174 NZ LYS A 147 20.297 -7.337 -2.134 1.00 87.66 N ATOM 1175 N GLU A 148 26.410 -6.374 -1.654 1.00 19.36 N ATOM 1176 CA GLU A 148 27.194 -7.412 -2.326 1.00 21.36 C ATOM 1177 C GLU A 148 27.942 -8.261 -1.300 1.00 26.24 C ATOM 1178 O GLU A 148 28.101 -9.471 -1.484 1.00 21.22 O ATOM 1179 CB GLU A 148 28.203 -6.801 -3.310 1.00 16.10 C ATOM 1180 CG GLU A 148 27.557 -6.172 -4.525 1.00 36.64 C ATOM 1181 CD GLU A 148 28.537 -5.386 -5.393 1.00 49.34 C ATOM 1182 OE1 GLU A 148 29.722 -5.777 -5.460 1.00 47.38 O ATOM 1183 OE2 GLU A 148 28.121 -4.372 -5.998 1.00 59.66 O ATOM 1184 N LEU A 149 28.362 -7.623 -0.207 1.00 25.00 N ATOM 1185 CA LEU A 149 29.106 -8.294 0.852 1.00 25.80 C ATOM 1186 C LEU A 149 28.219 -9.028 1.854 1.00 26.62 C ATOM 1187 O LEU A 149 28.722 -9.698 2.749 1.00 26.63 O ATOM 1188 CB LEU A 149 30.013 -7.299 1.577 1.00 25.40 C ATOM 1189 CG LEU A 149 31.141 -6.664 0.762 1.00 25.18 C ATOM 1190 CD1 LEU A 149 31.713 -5.460 1.501 1.00 24.78 C ATOM 1191 CD2 LEU A 149 32.225 -7.672 0.488 1.00 24.81 C ATOM 1192 N GLY A 150 26.907 -8.890 1.717 1.00 27.83 N ATOM 1193 CA GLY A 150 26.003 -9.589 2.616 1.00 30.10 C ATOM 1194 C GLY A 150 25.544 -8.856 3.861 1.00 31.94 C ATOM 1195 O GLY A 150 24.929 -9.453 4.737 1.00 31.56 O ATOM 1196 N TYR A 151 25.821 -7.560 3.935 1.00 34.23 N ATOM 1197 CA TYR A 151 25.428 -6.776 5.085 1.00 36.68 C ATOM 1198 C TYR A 151 24.287 -5.834 4.754 1.00 38.75 C ATOM 1199 O TYR A 151 23.153 -6.046 5.173 1.00 39.40 O ATOM 1200 CB TYR A 151 26.624 -5.986 5.613 1.00 37.13 C ATOM 1201 CG TYR A 151 26.319 -5.078 6.788 1.00 37.85 C ATOM 1202 CD1 TYR A 151 25.674 -5.557 7.914 1.00 38.50 C ATOM 1203 CD2 TYR A 151 26.670 -3.732 6.762 1.00 38.39 C ATOM 1204 CE1 TYR A 151 25.377 -4.720 8.988 1.00 38.95 C ATOM 1205 CE2 TYR A 151 26.380 -2.884 7.830 1.00 38.63 C ATOM 1206 CZ TYR A 151 25.727 -3.385 8.936 1.00 39.03 C ATOM 1207 OH TYR A 151 25.362 -2.543 9.964 1.00 39.21 O ATOM 1208 N GLN A 152 24.585 -4.802 3.977 1.00 41.07 N ATOM 1209 CA GLN A 152 23.594 -3.777 3.632 1.00 43.96 C ATOM 1210 C GLN A 152 22.790 -3.325 4.860 1.00 45.06 C ATOM 1211 O GLN A 152 21.587 -3.090 4.787 1.00 45.47 O ATOM 1212 CB GLN A 152 22.653 -4.233 2.507 1.00 45.87 C ATOM 1213 CG GLN A 152 21.736 -3.105 1.997 1.00 54.47 C ATOM 1214 CD GLN A 152 22.377 -1.722 2.103 1.00 56.21 C ATOM 1215 OE1 GLN A 152 23.513 -1.506 1.692 1.00 52.86 O ATOM 1216 NE2 GLN A 152 21.644 -0.789 2.691 1.00 71.86 N ATOM 1217 N GLY A 153 23.474 -3.227 5.994 1.00 45.98 N ATOM 1218 CA GLY A 153 22.818 -2.798 7.211 1.00 47.07 C ATOM 1219 C GLY A 153 22.695 -1.282 7.219 1.00 47.54 C ATOM 1220 O GLY A 153 21.870 -0.745 7.992 1.00 48.11 O ATOM 1221 OXT GLY A 153 23.431 -0.634 6.445 1.00 48.02 O TER 1222 GLY A 153 HETATM 1223 S SO4 A 157 30.746 18.706 28.896 1.00 47.98 S HETATM 1224 O1 SO4 A 157 30.697 20.077 28.620 1.00 48.06 O HETATM 1225 O2 SO4 A 157 31.104 18.021 27.725 1.00 47.52 O HETATM 1226 O3 SO4 A 157 29.468 18.179 29.331 1.00 47.79 O HETATM 1227 O4 SO4 A 157 31.722 18.578 29.881 1.00 47.85 O HETATM 1228 FE HEM A 155 35.502 4.204 9.980 1.00 18.78 FE HETATM 1229 CHA HEM A 155 38.056 2.293 11.078 1.00 21.35 C HETATM 1230 CHB HEM A 155 37.306 5.212 7.384 1.00 18.29 C HETATM 1231 CHC HEM A 155 32.964 6.205 9.051 1.00 16.45 C HETATM 1232 CHD HEM A 155 33.598 3.200 12.667 1.00 19.12 C HETATM 1233 NA HEM A 155 37.312 3.780 9.325 1.00 19.73 N HETATM 1234 C1A HEM A 155 38.286 2.995 9.925 1.00 21.23 C HETATM 1235 C2A HEM A 155 39.557 3.037 9.214 1.00 21.38 C HETATM 1236 C3A HEM A 155 39.302 3.871 8.151 1.00 20.28 C HETATM 1237 C4A HEM A 155 37.919 4.323 8.239 1.00 19.51 C HETATM 1238 CMA HEM A 155 40.314 4.221 7.055 1.00 18.93 C HETATM 1239 CAA HEM A 155 40.877 2.216 9.299 1.00 23.71 C HETATM 1240 CBA HEM A 155 41.015 0.742 8.951 1.00 26.45 C HETATM 1241 CGA HEM A 155 39.678 0.033 8.861 1.00 28.72 C HETATM 1242 O1A HEM A 155 39.251 -0.566 9.881 1.00 30.24 O HETATM 1243 O2A HEM A 155 39.048 0.091 7.778 1.00 29.74 O HETATM 1244 NB HEM A 155 35.132 5.385 8.500 1.00 17.06 N HETATM 1245 C1B HEM A 155 36.020 5.716 7.478 1.00 17.24 C HETATM 1246 C2B HEM A 155 35.456 6.694 6.556 1.00 16.49 C HETATM 1247 C3B HEM A 155 34.224 6.980 7.014 1.00 16.26 C HETATM 1248 C4B HEM A 155 34.055 6.156 8.231 1.00 16.22 C HETATM 1249 CMB HEM A 155 36.090 7.246 5.263 1.00 16.42 C HETATM 1250 CAB HEM A 155 33.335 8.005 6.658 1.00 16.24 C HETATM 1251 CBB HEM A 155 33.491 9.122 5.794 1.00 17.32 C HETATM 1252 NC HEM A 155 33.591 4.565 10.657 1.00 17.07 N HETATM 1253 C1C HEM A 155 32.740 5.507 10.200 1.00 15.99 C HETATM 1254 C2C HEM A 155 31.615 5.707 11.080 1.00 16.52 C HETATM 1255 C3C HEM A 155 31.785 4.829 12.131 1.00 17.63 C HETATM 1256 C4C HEM A 155 33.028 4.126 11.834 1.00 17.34 C HETATM 1257 CMC HEM A 155 30.484 6.704 10.837 1.00 15.53 C HETATM 1258 CAC HEM A 155 31.081 4.630 13.357 1.00 17.63 C HETATM 1259 CBC HEM A 155 29.969 5.338 13.897 1.00 18.52 C HETATM 1260 ND HEM A 155 35.728 2.887 11.451 1.00 21.03 N HETATM 1261 C1D HEM A 155 34.852 2.615 12.500 1.00 21.31 C HETATM 1262 C2D HEM A 155 35.466 1.757 13.490 1.00 22.47 C HETATM 1263 C3D HEM A 155 36.729 1.540 13.083 1.00 23.41 C HETATM 1264 C4D HEM A 155 36.872 2.243 11.803 1.00 22.48 C HETATM 1265 CMD HEM A 155 34.783 1.147 14.698 1.00 22.53 C HETATM 1266 CAD HEM A 155 37.941 1.000 13.841 1.00 26.65 C HETATM 1267 CBD HEM A 155 38.463 1.843 15.019 1.00 30.96 C HETATM 1268 CGD HEM A 155 39.586 1.145 15.786 1.00 33.23 C HETATM 1269 O1D HEM A 155 39.326 0.697 16.930 1.00 35.48 O HETATM 1270 O2D HEM A 155 40.714 1.027 15.245 1.00 34.38 O HETATM 1271 C NBN A 156 36.437 5.629 11.224 0.68 19.01 C HETATM 1272 N NBN A 156 36.674 6.332 11.970 0.68 19.66 N HETATM 1273 C1 NBN A 156 37.691 6.621 13.103 0.68 19.98 C HETATM 1274 C2 NBN A 156 38.602 5.446 13.328 0.68 20.27 C HETATM 1275 C3 NBN A 156 39.713 5.441 12.363 0.68 20.94 C HETATM 1276 C4 NBN A 156 40.675 4.358 12.790 0.68 20.98 C HETATM 1277 O HOH A 201 35.636 -2.996 15.255 0.36 12.26 O HETATM 1278 O HOH A 202 32.694 19.805 17.167 0.84 19.38 O HETATM 1279 O HOH A 203 26.221 14.314 13.400 0.89 28.18 O HETATM 1280 O HOH A 204 22.566 7.494 2.350 0.87 36.92 O HETATM 1281 O HOH A 205 30.932 6.438 -8.815 1.00 41.84 O HETATM 1282 O HOH A 206 24.541 30.283 6.889 0.63 25.58 O HETATM 1283 O HOH A 207 25.187 14.290 2.886 0.81 26.13 O HETATM 1284 O HOH A 208 22.103 13.723 1.959 0.96 26.43 O HETATM 1285 O HOH A 209 30.014 8.951 35.439 1.00 35.90 O HETATM 1286 O HOH A 210 30.631 11.672 35.807 0.93 21.70 O HETATM 1287 O HOH A 211 31.937 13.143 -12.160 1.00 17.10 O HETATM 1288 O HOH A 212 34.706 13.187 33.417 1.00 24.72 O HETATM 1289 O HOH A 213 35.965 30.906 4.862 0.88 25.13 O HETATM 1290 O HOH A 214 37.788 28.957 4.292 1.00 23.24 O HETATM 1291 O HOH A 215 47.139 19.251 7.852 1.00 21.52 O HETATM 1292 O HOH A 216 35.554 33.553 5.043 1.00 35.51 O HETATM 1293 O HOH A 217 45.287 12.661 -0.522 0.63 28.06 O HETATM 1294 O HOH A 218 22.243 26.519 -4.167 0.53 36.19 O HETATM 1295 O HOH A 219 34.356 25.644 -2.155 0.99 18.86 O HETATM 1296 O HOH A 220 43.314 5.775 14.083 0.83 33.75 O HETATM 1297 O HOH A 221 35.554 15.655 -13.704 0.69 27.98 O HETATM 1298 O HOH A 222 35.044 10.234 -5.370 1.00 16.54 O HETATM 1299 O HOH A 223 43.738 11.098 -7.107 0.70 39.04 O HETATM 1300 O HOH A 224 41.663 19.566 -2.545 0.71 29.09 O HETATM 1301 O HOH A 225 29.014 28.495 -2.787 1.00 22.71 O HETATM 1302 O HOH A 226 47.114 17.474 10.936 0.85 16.95 O HETATM 1303 O HOH A 227 49.157 23.679 7.865 0.45 6.24 O HETATM 1304 O HOH A 228 39.456 -6.272 0.390 0.45 18.39 O HETATM 1305 O HOH A 229 47.195 20.062 12.092 0.79 27.14 O HETATM 1306 O HOH A 230 41.694 14.434 14.419 0.64 19.99 O HETATM 1307 O HOH A 231 25.279 16.763 13.167 0.91 45.56 O HETATM 1308 O HOH A 232 27.502 6.144 24.003 0.34 12.97 O HETATM 1309 O HOH A 233 32.714 -1.677 16.431 0.37 7.65 O HETATM 1310 O HOH A 234 43.562 6.760 6.302 0.56 19.34 O HETATM 1311 O HOH A 235 26.622 30.313 -3.254 0.87 35.39 O HETATM 1312 O HOH A 236 43.770 12.412 1.711 0.89 19.03 O HETATM 1313 O HOH A 237 39.271 -4.219 4.681 0.55 22.84 O HETATM 1314 O HOH A 238 34.830 29.856 12.497 0.81 23.30 O HETATM 1315 O HOH A 239 42.908 14.832 3.150 1.00 41.54 O HETATM 1316 O HOH A 240 43.209 9.837 -4.230 0.92 19.85 O HETATM 1317 O HOH A 241 40.614 6.101 0.818 0.34 2.00 O HETATM 1318 O HOH A 242 40.042 10.664 -11.016 0.76 38.98 O HETATM 1319 O HOH A 243 40.074 3.074 1.213 0.83 38.72 O HETATM 1320 O HOH A 244 27.467 25.351 11.096 1.00 41.86 O HETATM 1321 O HOH A 245 31.263 30.732 11.225 1.00 34.25 O HETATM 1322 O HOH A 246 20.885 2.219 8.815 0.51 14.38 O HETATM 1323 O HOH A 247 19.343 15.372 1.025 0.88 50.46 O HETATM 1324 O HOH A 248 33.427 28.236 -3.034 1.00 44.12 O HETATM 1325 O HOH A 249 27.534 -10.802 -3.746 0.42 14.53 O HETATM 1326 O HOH A 250 24.801 -4.357 -4.615 0.37 9.21 O HETATM 1327 O HOH A 251 26.214 23.149 -6.451 1.00 27.31 O HETATM 1328 O HOH A 252 31.921 21.850 -1.051 0.56 24.04 O HETATM 1329 O HOH A 253 44.385 26.738 -0.823 1.00 39.65 O HETATM 1330 O HOH A 254 40.900 12.361 27.622 0.35 6.66 O HETATM 1331 O HOH A 255 44.897 21.387 15.094 0.51 19.22 O HETATM 1332 O HOH A 256 39.769 26.352 9.925 1.00 24.54 O HETATM 1333 O HOH A 257 28.113 30.114 4.349 0.73 32.35 O HETATM 1334 O HOH A 258 41.236 14.703 20.600 0.98 21.47 O HETATM 1335 O HOH A 259 27.920 12.176 23.647 0.45 25.64 O HETATM 1336 O HOH A 260 40.653 19.211 27.130 0.96 35.73 O HETATM 1337 O HOH A 261 38.995 12.758 33.007 0.56 26.01 O HETATM 1338 O HOH A 262 31.185 29.366 -1.418 0.92 29.20 O HETATM 1339 O HOH A 263 23.330 1.530 -3.772 0.93 38.08 O HETATM 1340 O HOH A 264 39.105 21.814 26.599 1.00 52.76 O HETATM 1341 O HOH A 265 28.047 -8.320 9.038 0.26 2.83 O HETATM 1342 O HOH A 266 20.727 9.658 17.232 1.00 40.20 O HETATM 1343 O HOH A 267 39.824 21.447 16.984 0.48 20.91 O HETATM 1344 O HOH A 268 31.109 21.510 30.969 0.78 27.35 O HETATM 1345 O HOH A 269 25.247 20.689 -6.664 0.53 13.05 O HETATM 1346 O HOH A 270 41.890 15.172 -7.575 0.63 23.24 O HETATM 1347 O HOH A 271 32.201 10.450 -3.509 0.82 32.30 O HETATM 1348 O HOH A 272 48.852 20.024 14.408 0.96 44.55 O HETATM 1349 O HOH A 273 45.087 10.967 -2.827 0.80 23.86 O HETATM 1350 O HOH A 274 43.790 6.366 -3.654 0.72 43.34 O HETATM 1351 O HOH A 275 36.756 24.689 15.999 0.85 45.09 O HETATM 1352 O HOH A 276 21.803 13.659 9.652 0.96 43.48 O HETATM 1353 O HOH A 277 20.646 5.769 15.588 0.37 15.34 O HETATM 1354 O HOH A 278 44.830 25.158 2.252 0.98 49.70 O HETATM 1355 O HOH A 279 32.937 25.419 -9.655 0.44 16.19 O HETATM 1356 O HOH A 280 28.152 27.732 -8.564 0.94 51.07 O HETATM 1357 O HOH A 281 35.196 30.717 -2.699 1.00 51.54 O HETATM 1358 O HOH A 282 33.436 19.536 28.293 0.81 30.59 O HETATM 1359 O HOH A 283 25.107 22.125 -10.155 0.55 34.20 O HETATM 1360 O HOH A 284 39.237 3.162 -8.262 1.00 34.85 O HETATM 1361 O HOH A 285 31.346 32.729 13.318 0.42 18.95 O HETATM 1362 O HOH A 286 36.519 -0.178 17.896 0.90 38.54 O HETATM 1363 O HOH A 287 38.564 2.732 18.719 0.55 17.78 O HETATM 1364 O HOH A 288 30.132 10.659 26.140 0.36 18.38 O HETATM 1365 O HOH A 289 36.854 4.464 -13.579 0.81 38.38 O HETATM 1366 O HOH A 290 27.373 5.340 -8.830 0.54 26.40 O HETATM 1367 O HOH A 291 32.075 1.884 -6.445 0.75 37.30 O HETATM 1368 O HOH A 292 40.784 -2.354 -4.023 0.29 12.31 O HETATM 1369 O HOH A 293 38.692 31.184 -2.441 0.66 32.11 O HETATM 1370 O HOH A 294 47.194 24.955 10.604 0.84 44.93 O HETATM 1371 O HOH A 295 34.034 31.418 14.962 0.52 36.13 O HETATM 1372 O HOH A 296 31.071 7.595 27.503 0.63 32.87 O HETATM 1373 O HOH A 297 33.788 23.237 30.704 0.64 39.14 O HETATM 1374 O HOH A 298 25.278 17.607 -12.018 0.56 32.27 O HETATM 1375 O HOH A 299 21.415 7.748 -8.816 0.48 29.69 O HETATM 1376 O HOH A 300 42.482 29.132 -3.537 0.48 27.61 O HETATM 1377 O HOH A 301 23.188 23.847 -3.514 0.46 25.13 O HETATM 1378 O HOH A 302 22.959 7.257 -2.133 0.76 43.13 O HETATM 1379 O HOH A 303 23.834 15.545 5.192 0.68 34.54 O HETATM 1380 O HOH A 304 39.887 -0.633 5.129 0.60 35.31 O HETATM 1381 O HOH A 305 29.072 -9.111 6.284 0.69 37.84 O HETATM 1382 O HOH A 306 21.916 1.326 6.785 0.72 42.32 O HETATM 1383 O HOH A 307 18.377 6.767 6.900 0.66 39.04 O HETATM 1384 O HOH A 308 46.391 8.895 7.898 0.50 25.35 O HETATM 1385 O HOH A 309 48.010 9.126 10.162 0.60 34.14 O HETATM 1386 O HOH A 310 30.229 20.017 18.925 0.66 31.75 O HETATM 1387 O HOH A 311 34.675 20.639 19.217 0.54 24.69 O HETATM 1388 O HOH A 312 28.518 11.760 28.729 0.28 27.00 O HETATM 1389 O HOH A 313 32.254 6.469 30.644 0.40 30.36 O HETATM 1390 O HOH A 314 40.742 5.881 -10.852 0.37 30.46 O HETATM 1391 O HOH A 315 27.168 23.526 -8.314 0.33 28.77 O HETATM 1392 O HOH A 316 28.521 -2.349 -7.024 0.32 28.33 O HETATM 1393 O HOH A 317 25.803 2.353 -6.384 0.31 28.65 O HETATM 1394 O HOH A 318 44.136 16.467 -6.383 0.34 29.36 O HETATM 1395 O HOH A 319 42.780 18.817 -5.108 0.27 27.67 O HETATM 1396 O HOH A 320 31.586 -2.955 -4.495 0.37 29.62 O HETATM 1397 O HOH A 321 22.068 -0.590 -3.191 0.34 28.19 O HETATM 1398 O HOH A 322 31.577 -4.125 -2.549 0.35 30.63 O HETATM 1399 O HOH A 323 40.063 -4.705 -1.916 0.31 30.62 O HETATM 1400 O HOH A 324 40.744 30.579 -1.276 0.42 31.10 O HETATM 1401 O HOH A 325 22.633 -4.018 0.119 0.49 32.42 O HETATM 1402 O HOH A 326 39.728 -6.468 2.562 0.39 28.33 O HETATM 1403 O HOH A 327 23.766 17.652 5.748 0.36 30.42 O HETATM 1404 O HOH A 328 23.087 12.937 6.384 0.29 26.48 O HETATM 1405 O HOH A 329 22.747 -7.645 7.662 0.25 25.89 O HETATM 1406 O HOH A 330 19.691 9.411 8.942 0.25 28.30 O HETATM 1407 O HOH A 331 29.536 29.990 9.576 0.30 29.08 O HETATM 1408 O HOH A 332 45.870 26.406 8.824 0.07 28.54 O HETATM 1409 O HOH A 333 45.836 8.820 12.130 0.38 28.79 O HETATM 1410 O HOH A 334 19.316 5.243 12.172 0.36 28.54 O HETATM 1411 O HOH A 335 48.889 17.640 14.045 0.39 30.76 O HETATM 1412 O HOH A 336 34.630 23.523 14.046 0.26 26.99 O HETATM 1413 O HOH A 337 25.803 18.817 18.514 0.38 33.79 O HETATM 1414 O HOH A 338 31.249 21.185 20.442 0.36 29.67 O CONECT 744 1228 CONECT 1223 1224 1225 1226 1227 CONECT 1224 1223 CONECT 1225 1223 CONECT 1226 1223 CONECT 1227 1223 CONECT 1228 744 1233 1244 1252 CONECT 1228 1260 1271 CONECT 1229 1234 1264 CONECT 1230 1237 1245 CONECT 1231 1248 1253 CONECT 1232 1256 1261 CONECT 1233 1228 1234 1237 CONECT 1234 1229 1233 1235 CONECT 1235 1234 1236 1239 CONECT 1236 1235 1237 1238 CONECT 1237 1230 1233 1236 CONECT 1238 1236 CONECT 1239 1235 1240 CONECT 1240 1239 1241 CONECT 1241 1240 1242 1243 CONECT 1242 1241 CONECT 1243 1241 CONECT 1244 1228 1245 1248 CONECT 1245 1230 1244 1246 CONECT 1246 1245 1247 1249 CONECT 1247 1246 1248 1250 CONECT 1248 1231 1244 1247 CONECT 1249 1246 CONECT 1250 1247 1251 CONECT 1251 1250 CONECT 1252 1228 1253 1256 CONECT 1253 1231 1252 1254 CONECT 1254 1253 1255 1257 CONECT 1255 1254 1256 1258 CONECT 1256 1232 1252 1255 CONECT 1257 1254 CONECT 1258 1255 1259 CONECT 1259 1258 CONECT 1260 1228 1261 1264 CONECT 1261 1232 1260 1262 CONECT 1262 1261 1263 1265 CONECT 1263 1262 1264 1266 CONECT 1264 1229 1260 1263 CONECT 1265 1262 CONECT 1266 1263 1267 CONECT 1267 1266 1268 CONECT 1268 1267 1269 1270 CONECT 1269 1268 CONECT 1270 1268 CONECT 1271 1228 1272 CONECT 1272 1271 1273 CONECT 1273 1272 1274 CONECT 1274 1273 1275 CONECT 1275 1274 1276 CONECT 1276 1275 MASTER 268 0 3 8 0 0 9 6 1413 1 56 12 END