HEADER OXYGEN TRANSPORT 23-APR-82 2LH3 TITLE X-RAY STRUCTURAL INVESTIGATION OF LEGHEMOGLOBIN. VI. TITLE 2 STRUCTURE OF ACETATE-FERRILEGHEMOGLOBIN AT A RESOLUTION OF TITLE 3 2.0 ANGSTROMS (RUSSIAN) COMPND MOL_ID: 1; COMPND 2 MOLECULE: LEGHEMOGLOBIN (CYANO MET); COMPND 3 CHAIN: A; COMPND 4 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: LUPINUS LUTEUS KEYWDS OXYGEN TRANSPORT EXPDTA X-RAY DIFFRACTION AUTHOR B.K.VAINSHTEIN,E.H.HARUTYUNYAN,I.P.KURANOVA,V.V.BORISOV, AUTHOR 2 N.I.SOSFENOV,A.G.PAVLOVSKY,A.I.GREBENKO,N.V.KONAREVA REVDAT 2 30-SEP-83 2LH3 1 REVDAT REVDAT 1 20-JAN-83 2LH3 0 JRNL AUTH E.G.ARUTYUNYAN,I.P.KURANOVA,B.K.VAINSHTEIN, JRNL AUTH 2 W.STEIGEMANN JRNL TITL X-RAY STRUCTURAL INVESTIGATION OF LEGHEMOGLOBIN. JRNL TITL 2 VI. STRUCTURE OF ACETATE-FERRILEGHEMOGLOBIN AT A JRNL TITL 3 RESOLUTION OF 2.0 ANGSTROMS (RUSSIAN) JRNL REF KRISTALLOGRAFIYA V. 25 80 1980 JRNL REFN ASTM KRISAJ UR ISSN 0023-4761 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH E.G.ARUTYUNYAN,I.P.KURANOVA,B.K.VAINSHTEIN, REMARK 1 AUTH 2 W.STEIGEMANN REMARK 1 TITL X-RAY STRUCTURAL INVESTIGATION OF LEGHEMOGLOBIN. REMARK 1 TITL 2 VI. STRUCTURE OF ACETATE-FERRILEGHEMOGLOBIN AT A REMARK 1 TITL 3 RESOLUTION OF 2.0 ANGSTROMS REMARK 1 REF SOV.PHYS.CRYSTALLOGR.(ENGL. V. 25 43 1980 REMARK 1 REF 2 TRANSL.) REMARK 1 REFN ASTM SPHCA6 US ISSN 0038-5638 REMARK 1 REFERENCE 2 REMARK 1 AUTH B.K.VAINSHTEIN,E.G.ARUTYUNYAN,I.P.KURANOVA, REMARK 1 AUTH 2 V.V.BORISOV,N.I.SOSFENOV,A.G.PAVLOVSKII, REMARK 1 AUTH 3 A.I.GREBENKO,YU.V.NEKRASOV REMARK 1 TITL X-RAY DIFFRACTION STUDY OF LEGHEMOGLOBIN. IV. REMARK 1 TITL 2 DETERMINATION OF THE STRUCTURE WITH 2.8 ANGSTROMS REMARK 1 TITL 3 RESOLUTION (RUSSIAN) REMARK 1 REF KRISTALLOGRAFIYA V. 23 517 1978 REMARK 1 REFN ASTM KRISAJ UR ISSN 0023-4761 REMARK 1 REFERENCE 3 REMARK 1 AUTH B.K.VAINSHTEIN,E.G.ARUTYUNYAN,I.P.KURANOVA, REMARK 1 AUTH 2 V.V.BORISOV,N.I.SOSFENOV,A.G.PAVLOVSKII, REMARK 1 AUTH 3 A.I.GREBENKO,YU.V.NEKRASOV REMARK 1 TITL X-RAY STRUCTURAL INVESTIGATION OF LEGHEMOGLOBIN. REMARK 1 TITL 2 IV. STRUCTURE DETERMINATION AT A RESOLUTION OF 2.8 REMARK 1 TITL 3 ANGSTROMS REMARK 1 REF SOV.PHYS.CRYSTALLOGR.(ENGL. V. 23 287 1978 REMARK 1 REF 2 TRANSL.) REMARK 1 REFN ASTM SPHCA6 US ISSN 0038-5638 REMARK 1 REFERENCE 4 REMARK 1 AUTH B.K.VAINSHTEIN,E.G.ARUTIUNIAN,I.P.KURANOVA, REMARK 1 AUTH 2 V.V.BORISOV,N.I.SOSFENOV,A.G.PAVLOVSKII, REMARK 1 AUTH 3 A.I.GREBENKO,N.V.KONAREVA,IU.V.NEKRASOV REMARK 1 TITL SPATIAL STRUCTURE OF LUPINE LEGHEMOGLOBIN WITH THE REMARK 1 TITL 2 2.8 ANGSTROMS RESOLUTION (RUSSIAN) REMARK 1 REF DOKL.AKAD.NAUK SSSR V. 233 238 1977 REMARK 1 REFN ASTM DANKAS UR ISSN 0002-3264 REMARK 1 REFERENCE 5 REMARK 1 AUTH B.K.VAINSHTEIN,E.G.ARUTYUNYAN,I.P.KURANOVA, REMARK 1 AUTH 2 V.V.BORISOV,N.I.SOSFENOV,A.G.PAVLOVSKII, REMARK 1 AUTH 3 A.I.GREBENKO,N.V.KONAREVA,YU.V.NEKRASOV REMARK 1 TITL THREE-DIMENSIONAL STRUCTURE OF LUPINE REMARK 1 TITL 2 LEGHEMOGLOBIN WITH A RESOLUTION OF 2.8 ANGSTROMS REMARK 1 REF DOKL.BIOCHEM.(ENGL.TRANSL.) V. 233 67 1977 REMARK 1 REFN ASTM DBIOAM US ISSN 0012-4958 REMARK 1 REFERENCE 6 REMARK 1 AUTH E.G.ARUTYUNYAN,I.P.KURANOVA,A.I.GREBENKO, REMARK 1 AUTH 2 A.A.VORONOVA REMARK 1 TITL X-RAY STRUCTURAL STUDY OF LEGHEMOGLOBIN. III. REMARK 1 TITL 2 CRYSTALLOGRAPHIC DATA ON THE STRUCTURE OF THE REMARK 1 TITL 3 FIRST COMPONENT (RUSSIAN) REMARK 1 REF KRISTALLOGRAFIYA V. 22 634 1977 REMARK 1 REFN ASTM KRISAJ UR ISSN 0023-4761 REMARK 1 REFERENCE 7 REMARK 1 AUTH E.G.ARUTYUNYAN,I.P.KURANOVA,A.I.GREBENKO, REMARK 1 AUTH 2 A.A.VORONOVA REMARK 1 TITL X-RAY STRUCTURAL STUDY OF LEGHEMOGLOBIN. III. REMARK 1 TITL 2 CRYSTALLOGRAPHIC DATA REGARDING THE STRUCTURE OF REMARK 1 TITL 3 THE FIRST COMPONENT REMARK 1 REF SOV.PHYS.CRYSTALLOGR.(ENGL. V. 22 362 1977 REMARK 1 REF 2 TRANSL.) REMARK 1 REFN ASTM SPHCA6 US ISSN 0038-5638 REMARK 1 REFERENCE 8 REMARK 1 AUTH S.VUK-PAVLOVIC,B.BENKO,S.MARICIC, REMARK 1 AUTH 2 G.LAHAJNAR I.P.KURANOVA,B.K.VAINSHTEIN REMARK 1 TITL THE HAEM-ACCESSIBILITY IN LEGHAEMOGLOBIN OF REMARK 1 TITL 2 LUPINUS LUTEUS AS OBSERVED BY PROTON MAGNETIC REMARK 1 TITL 3 RELAXATION REMARK 1 REF INT.J.PEPT.PROTEIN RES. V. 8 427 1976 REMARK 1 REFN ASTM IJPPC3 DK ISSN 0367-8377 REMARK 1 REFERENCE 9 REMARK 1 AUTH B.K.VAINSHTEIN,E.G.ARUTYUNYAN,I.P.KURANOVA, REMARK 1 AUTH 2 V.V.BORISOV,N.I.SOSFENOV,A.G.PAVLOVSKII, REMARK 1 AUTH 3 A.I.GREBENKO,N.V.KONAREVA REMARK 1 TITL THE X-RAY STRUCTURAL STUDY OF LEGHEMOGLOBIN. II. REMARK 1 TITL 2 DETERMINATION OF THE STRUCTURE AT 5 ANGSTROMS REMARK 1 TITL 3 RESOLUTION (RUSSIAN) REMARK 1 REF KRISTALLOGRAFIYA V. 19 971 1974 REMARK 1 REFN ASTM KRISAJ UR ISSN 0023-4761 REMARK 1 REFERENCE 10 REMARK 1 AUTH B.K.VAINSHTEIN,E.G.ARUTYUNYAN,I.P.KURANOVA, REMARK 1 AUTH 2 V.V.BORISOV,N.I.SOSFENOV,A.G.PAVLOVSKII, REMARK 1 AUTH 3 A.I.GREBENKO,N.V.KONAREVA REMARK 1 TITL X-RAY STUDY OF LEGHEMOGLOBIN. II. DETERMINATION OF REMARK 1 TITL 2 THE STRUCTURE WITH RESOLUTION OF 5 ANGSTROMS REMARK 1 REF SOV.PHYS.CRYSTALLOGR.(ENGL. V. 19 602 1975 REMARK 1 REF 2 TRANSL.) REMARK 1 REFN ASTM SPHCA6 US ISSN 0038-5638 REMARK 1 REFERENCE 11 REMARK 1 AUTH B.K.VAINSHTEIN,E.G.ARUTYUNYAN,I.P.KURANOVA, REMARK 1 AUTH 2 V.V.BORISOV,N.I.SOSFENOV,A.G.PAVLOVSKII, REMARK 1 AUTH 3 A.I.GREBENKO,N.V.KONAREVA REMARK 1 TITL THE X-RAY STRUCTURAL STUDY OF LEGHEMOGLOBIN. I. REMARK 1 TITL 2 PURIFICATION, CRYSTALLIZATION, AND PRODUCTION OF REMARK 1 TITL 3 DERIVATIVES CONTAINING HEAVY ATOMS (RUSSIAN) REMARK 1 REF KRISTALLOGRAFIYA V. 19 964 1974 REMARK 1 REFN ASTM KRISAJ UR ISSN 0023-4761 REMARK 1 REFERENCE 12 REMARK 1 AUTH B.K.VAINSHTEIN,E.G.ARUTYUNYAN,I.P.KURANOVA, REMARK 1 AUTH 2 V.V.BORISOV,N.I.SOSFENOV,A.G.PAVLOVSKII, REMARK 1 AUTH 3 A.I.GREBENKO,N.V.KONAREVA REMARK 1 TITL X-RAY STUDY OF LEGHEMOGLOBIN. I.PURIFICATION, REMARK 1 TITL 2 CRYSTALLIZATION, AND PREPARATION OF DERIVATIVES REMARK 1 TITL 3 CONTAINING HEAVY ATOMS REMARK 1 REF SOV.PHYS.CRYSTALLOGR.(ENGL. V. 19 598 1975 REMARK 1 REF 2 TRANSL.) REMARK 1 REFN ASTM SPHCA6 US ISSN 0038-5638 REMARK 1 REFERENCE 13 REMARK 1 AUTH B.K.VAINSHTEIN,E.H.HARUTYUNYAN,I.P.KURANOVA, REMARK 1 AUTH 2 V.V.BORISOV,N.I.SOSFENOV,A.G.PAVLOVSKY, REMARK 1 AUTH 3 A.I.GREBENKO,N.V.KONAREVA REMARK 1 TITL STRUCTURE OF LEGHAEMOGLOBIN FROM LUPIN ROOT REMARK 1 TITL 2 NODULES AT 5 ANGSTROMS RESOLUTION REMARK 1 REF NATURE V. 254 163 1975 REMARK 1 REFN ASTM NATUAS UK ISSN 0028-0836 REMARK 1 REFERENCE 14 REMARK 1 AUTH B.K.VAINSHTEIN,E.G.ARUTIUNIAN,I.P.KURANOVA, REMARK 1 AUTH 2 V.V.BORISOV,N.I.SOSFENOV,A.G.PAVLOVSKII, REMARK 1 AUTH 3 A.I.GREBENKO,N.V.KONAREVA REMARK 1 TITL X-RAY DETERMINATION OF THREE-DIMENSIONAL STRUCTURE REMARK 1 TITL 2 OF LEGHEMOGLOBIN FROM LUPINUS LUTEUS L. AT 5 REMARK 1 TITL 3 ANGSTROMS RESOLUTION (RUSSIAN) REMARK 1 REF DOKL.AKAD.NAUK SSSR V. 216 690 1974 REMARK 1 REFN ASTM DANKAS UR ISSN 0002-3264 REMARK 1 REFERENCE 15 REMARK 1 AUTH B.K.VAINSHTEIN,E.G.ARUTYUNYAN,I.P.KURANOVA, REMARK 1 AUTH 2 V.V.BORISOV,N.I.SOSFENOV,A.G.PAVLOVSKII, REMARK 1 AUTH 3 A.I.GREBENKO,N.V.KONAREVA REMARK 1 TITL X-RAY DIFFRACTION DETERMINATION OF THE REMARK 1 TITL 2 THREE-DIMENSIONAL STRUCTURE OF LEGHEMOGLOBIN OF REMARK 1 TITL 3 LUPINUS LUTEUS L. WITH 5 ANGSTROMS RESOLUTION REMARK 1 REF DOKL.BIOCHEM.(ENGL.TRANSL.) V. 216 226 1974 REMARK 1 REFN ASTM DBIOAM US ISSN 0012-4958 REMARK 1 REFERENCE 16 REMARK 1 AUTH E.G.ARUTYUNYAN,V.N.ZAITSEV,G.YA.ZHIZNEVSKAYA, REMARK 1 AUTH 2 L.I.BORODENKO REMARK 1 TITL CELL PARAMETERS OF CRYSTALLINE PLANT (LUPINUS REMARK 1 TITL 2 LUTEUS (LUPINE)) HEMOGLOBIN (RUSSIAN) REMARK 1 REF KRISTALLOGRAFIYA V. 16 237 1971 REMARK 1 REFN ASTM KRISAJ UR ISSN 0023-4761 REMARK 1 REFERENCE 17 REMARK 1 AUTH E.G.ARUTYUNYAN,V.N.ZAITSEV,G.YA.ZHIZNEVSKAYA, REMARK 1 AUTH 2 L.I.BORODENKO REMARK 1 TITL UNIT-CELL PARAMETERS OF CRYSTALLINE PLANT REMARK 1 TITL 2 HEMOGLOBIN REMARK 1 REF SOV.PHYS.CRYSTALLOGR.(ENGL. V. 16 193 1971 REMARK 1 REF 2 TRANSL.) REMARK 1 REFN ASTM SPHCA6 US ISSN 0038-5638 REMARK 2 REMARK 2 RESOLUTION. 2.00 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : NULL REMARK 3 AUTHORS : NULL REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : NULL REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL REMARK 3 COMPLETENESS (WORKING+TEST) (%) : NULL REMARK 3 NUMBER OF REFLECTIONS : NULL REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 CROSS-VALIDATION METHOD : NULL REMARK 3 FREE R VALUE TEST SET SELECTION : NULL REMARK 3 R VALUE (WORKING SET) : NULL REMARK 3 FREE R VALUE : NULL REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL REMARK 3 FREE R VALUE TEST SET COUNT : NULL REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : NULL REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL REMARK 3 BIN R VALUE (WORKING SET) : NULL REMARK 3 BIN FREE R VALUE : NULL REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 1180 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 45 REMARK 3 SOLVENT ATOMS : 66 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL 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) : NULL REMARK 3 ESD FROM SIGMAA (A) : NULL REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL REMARK 3 REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR. REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL REMARK 3 ESD FROM C-V SIGMAA (A) : NULL REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. REMARK 3 BOND LENGTHS (A) : NULL REMARK 3 BOND ANGLES (DEGREES) : NULL REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL REMARK 3 IMPROPER ANGLES (DEGREES) : NULL REMARK 3 REMARK 3 ISOTROPIC THERMAL MODEL : NULL REMARK 3 REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL REMARK 3 REMARK 3 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 : NULL REMARK 3 TOPOLOGY FILE 1 : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 2LH3 COMPLIES WITH FORMAT V. 3.0, 1-DEC-2006 REMARK 4 REMARK 4 THIS IS THE REMEDIATED VERSION OF THIS PDB ENTRY. REMARK 4 REMEDIATED DATA FILE REVISION 3.100 (2007-03-23) REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : NULL REMARK 200 TEMPERATURE (KELVIN) : NULL REMARK 200 PH : NULL REMARK 200 NUMBER OF CRYSTALS USED : NULL REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : NULL REMARK 200 RADIATION SOURCE : NULL REMARK 200 BEAMLINE : NULL REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : NULL REMARK 200 WAVELENGTH OR RANGE (A) : NULL REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : NULL REMARK 200 DETECTOR MANUFACTURER : NULL REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL REMARK 200 DATA SCALING SOFTWARE : NULL REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : NULL REMARK 200 RESOLUTION RANGE HIGH (A) : NULL REMARK 200 RESOLUTION RANGE LOW (A) : NULL REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : NULL REMARK 200 DATA REDUNDANCY : NULL REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : NULL REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL REMARK 200 COMPLETENESS FOR SHELL (%) : NULL REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : NULL REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: NULL REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL REMARK 200 SOFTWARE USED: NULL REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 55.43 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.76 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: NULL REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: B 2 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,-Y,Z REMARK 290 3555 1/2+X,Y,1/2+Z REMARK 290 4555 1/2-X,-Y,1/2+Z REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 46.59500 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 26.03500 REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 46.59500 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 26.03500 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT REMARK 300 WHICH CONSISTS OF 1 CHAIN(S). SEE REMARK 350 FOR REMARK 300 INFORMATION ON GENERATING THE BIOLOGICAL MOLECULE(S). REMARK 350 REMARK 350 GENERATING THE BIOMOLECULE REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 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 CB LEU A 130 LIES ON A SPECIAL POSITION. REMARK 525 REMARK 525 SOLVENT REMARK 525 THE FOLLOWING SOLVENT MOLECULES LIE FARTHER THAN EXPECTED REMARK 525 FROM THE PROTEIN OR NUCLEIC ACID MOLECULE AND MAY BE REMARK 525 ASSOCIATED WITH A SYMMETRY RELATED MOLECULE (M=MODEL REMARK 525 NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE REMARK 525 NUMBER; I=INSERTION CODE): REMARK 525 REMARK 525 M RES CSSEQI REMARK 525 HOH 63 DISTANCE = 7.59 ANGSTROMS DBREF 2LH3 A 1 153 UNP P02240 LGB2_LUPLU 1 153 SEQADV 2LH3 GLU A 79 UNP P02240 GLN 79 CONFLICT SEQADV 2LH3 ASP A 150 UNP P02240 ASN 150 CONFLICT SEQRES 1 A 153 GLY ALA LEU THR GLU SER GLN ALA ALA LEU VAL LYS SER SEQRES 2 A 153 SER TRP GLU GLU PHE ASN ALA ASN ILE PRO LYS HIS THR SEQRES 3 A 153 HIS ARG PHE PHE ILE LEU VAL LEU GLU ILE ALA PRO ALA SEQRES 4 A 153 ALA LYS ASP LEU PHE SER PHE LEU LYS GLY THR SER GLU SEQRES 5 A 153 VAL PRO GLN ASN ASN PRO GLU LEU GLN ALA HIS ALA GLY SEQRES 6 A 153 LYS VAL PHE LYS LEU VAL TYR GLU ALA ALA ILE GLN LEU SEQRES 7 A 153 GLU VAL THR GLY VAL VAL VAL THR ASP ALA THR LEU LYS SEQRES 8 A 153 ASN LEU GLY SER VAL HIS VAL SER LYS GLY VAL ALA ASP SEQRES 9 A 153 ALA HIS PHE PRO VAL VAL LYS GLU ALA ILE LEU LYS THR SEQRES 10 A 153 ILE LYS GLU VAL VAL GLY ALA LYS TRP SER GLU GLU LEU SEQRES 11 A 153 ASN SER ALA TRP THR ILE ALA TYR ASP GLU LEU ALA ILE SEQRES 12 A 153 VAL ILE LYS LYS GLU MET ASP ASP ALA ALA FTNOTE 1 THIS ATOM WAS NOT RESOLVED IN THE FOURIER MAP. HET CYN 101 2 HET HEM 1 43 HETNAM CYN CYANIDE ION HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE HETSYN HEM HEME FORMUL 2 CYN C N 1- FORMUL 3 HEM C34 H32 FE N4 O4 FORMUL 4 HOH *66(H2 O) HELIX 1 A THR A 4 ALA A 20 1 17 HELIX 2 B ASN A 21 ILE A 36 1 16 HELIX 3 C ALA A 37 LEU A 43 1 7 HELIX 4 E ASN A 57 GLY A 82 1 26 HELIX 5 F ALA A 88 GLY A 101 1 14 HELIX 6 G ASP A 104 GLY A 123 1 20 HELIX 7 H SER A 127 ALA A 152 1 26 LINK FE HEM 1 C CYN 101 CRYST1 93.190 38.410 52.070 90.00 90.00 98.90 B 2 4 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 0.010731 0.001680 0.000000 0.00000 SCALE2 0.000000 0.026352 0.000000 0.00000 SCALE3 0.000000 0.000000 0.019205 0.00000 ATOM 1 N GLY A 1 35.700 49.276 32.320 1.00 67.33 N ATOM 2 CA GLY A 1 36.781 48.838 31.511 1.00 64.64 C ATOM 3 C GLY A 1 36.597 49.064 30.019 1.00 68.26 C ATOM 4 O GLY A 1 37.615 49.268 29.268 0.00 0.00 O ATOM 5 N ALA A 2 35.331 49.119 29.668 1.00 71.33 N ATOM 6 CA ALA A 2 34.808 49.414 28.344 1.00 61.44 C ATOM 7 C ALA A 2 34.651 48.244 27.354 1.00 47.12 C ATOM 8 O ALA A 2 33.669 48.123 26.560 1.00 55.83 O ATOM 9 CB ALA A 2 35.622 50.685 27.693 0.00 0.00 C ATOM 10 N LEU A 3 35.724 47.638 27.231 1.00 56.04 N ATOM 11 CA LEU A 3 36.009 46.733 26.139 1.00 30.14 C ATOM 12 C LEU A 3 36.952 47.444 25.082 1.00 34.81 C ATOM 13 O LEU A 3 36.531 47.853 23.995 1.00 29.81 O ATOM 14 CB LEU A 3 34.806 45.763 25.556 1.00 34.51 C ATOM 15 CG LEU A 3 34.518 44.467 26.403 1.00 33.15 C ATOM 16 CD1 LEU A 3 32.998 44.030 26.665 1.00 45.81 C ATOM 17 CD2 LEU A 3 35.177 43.319 25.783 1.00 35.20 C ATOM 18 N THR A 4 38.215 47.513 25.441 1.00 19.21 N ATOM 19 CA THR A 4 39.362 48.004 24.596 1.00 27.72 C ATOM 20 C THR A 4 39.670 46.872 23.690 1.00 17.70 C ATOM 21 O THR A 4 39.164 45.665 23.932 1.00 21.21 O ATOM 22 CB THR A 4 40.603 48.411 25.491 1.00 35.90 C ATOM 23 OG1 THR A 4 41.050 47.199 25.954 1.00 39.53 O ATOM 24 CG2 THR A 4 40.268 49.277 26.684 1.00 26.90 C ATOM 25 N GLU A 5 40.436 47.270 22.671 1.00 13.76 N ATOM 26 CA GLU A 5 40.823 46.330 21.690 1.00 18.20 C ATOM 27 C GLU A 5 41.567 45.275 22.336 1.00 29.88 C ATOM 28 O GLU A 5 41.337 44.068 21.943 1.00 26.20 O ATOM 29 CB GLU A 5 41.692 47.146 20.607 1.00 31.62 C ATOM 30 CG GLU A 5 41.866 46.310 19.344 1.00 58.59 C ATOM 31 CD GLU A 5 42.326 47.286 18.200 1.00 66.32 C ATOM 32 OE1 GLU A 5 41.467 47.888 17.633 1.00 55.75 O ATOM 33 OE2 GLU A 5 43.560 47.760 18.080 1.00 57.17 O ATOM 34 N SER A 6 42.263 45.673 23.423 1.00 24.30 N ATOM 35 CA SER A 6 42.959 44.731 24.178 1.00 12.63 C ATOM 36 C SER A 6 42.002 43.747 25.029 1.00 11.40 C ATOM 37 O SER A 6 42.159 42.526 25.072 1.00 18.44 O ATOM 38 CB SER A 6 44.097 45.463 25.065 1.00 16.32 C ATOM 39 OG SER A 6 43.526 45.958 26.244 1.00 52.59 O ATOM 40 N GLN A 7 41.017 44.254 25.628 1.00 8.34 N ATOM 41 CA GLN A 7 40.005 43.380 26.420 1.00 14.09 C ATOM 42 C GLN A 7 39.207 42.302 25.540 1.00 14.53 C ATOM 43 O GLN A 7 38.937 41.103 25.950 1.00 19.78 O ATOM 44 CB GLN A 7 39.008 44.186 27.113 1.00 13.29 C ATOM 45 CG GLN A 7 39.620 44.900 28.385 1.00 21.45 C ATOM 46 CD GLN A 7 38.599 45.710 28.991 1.00 32.54 C ATOM 47 OE1 GLN A 7 38.229 46.643 28.310 1.00 34.21 O ATOM 48 NE2 GLN A 7 38.525 45.655 30.311 1.00 39.26 N ATOM 49 N ALA A 8 38.916 42.731 24.350 1.00 18.20 N ATOM 50 CA ALA A 8 38.154 41.822 23.378 1.00 35.86 C ATOM 51 C ALA A 8 38.959 40.736 22.908 1.00 30.98 C ATOM 52 O ALA A 8 38.386 39.532 22.779 1.00 19.47 O ATOM 53 CB ALA A 8 37.735 42.622 22.171 1.00 17.94 C ATOM 54 N ALA A 9 40.267 41.154 22.761 1.00 24.53 N ATOM 55 CA ALA A 9 41.190 40.226 22.357 1.00 17.90 C ATOM 56 C ALA A 9 41.276 39.151 23.419 1.00 22.87 C ATOM 57 O ALA A 9 41.307 37.944 23.084 1.00 24.17 O ATOM 58 CB ALA A 9 42.613 41.009 22.100 1.00 15.94 C ATOM 59 N LEU A 10 41.195 39.579 24.655 1.00 18.74 N ATOM 60 CA LEU A 10 41.196 38.657 25.792 1.00 18.63 C ATOM 61 C LEU A 10 39.892 37.654 25.877 1.00 16.89 C ATOM 62 O LEU A 10 39.954 36.438 26.149 1.00 11.80 O ATOM 63 CB LEU A 10 41.442 39.432 27.118 1.00 20.12 C ATOM 64 CG LEU A 10 42.916 40.140 27.245 1.00 20.87 C ATOM 65 CD1 LEU A 10 43.107 41.051 28.491 1.00 27.20 C ATOM 66 CD2 LEU A 10 43.905 39.103 27.252 1.00 23.88 C ATOM 67 N VAL A 11 38.769 38.131 25.583 1.00 15.54 N ATOM 68 CA VAL A 11 37.483 37.200 25.573 1.00 15.35 C ATOM 69 C VAL A 11 37.454 36.161 24.454 1.00 23.80 C ATOM 70 O VAL A 11 37.075 34.930 24.702 1.00 20.13 O ATOM 71 CB VAL A 11 36.249 37.949 25.487 1.00 13.24 C ATOM 72 CG1 VAL A 11 34.907 36.972 25.300 1.00 8.63 C ATOM 73 CG2 VAL A 11 36.164 38.841 26.724 1.00 12.02 C ATOM 74 N LYS A 12 37.973 36.632 23.303 1.00 21.89 N ATOM 75 CA LYS A 12 37.984 35.741 22.143 1.00 11.53 C ATOM 76 C LYS A 12 38.857 34.641 22.343 1.00 11.94 C ATOM 77 O LYS A 12 38.378 33.428 22.103 1.00 16.98 O ATOM 78 CB LYS A 12 38.407 36.539 20.854 1.00 18.87 C ATOM 79 CG LYS A 12 38.277 35.579 19.643 1.00 26.76 C ATOM 80 CD LYS A 12 38.458 36.324 18.297 1.00 38.90 C ATOM 81 CE LYS A 12 38.411 35.310 17.133 1.00 42.24 C ATOM 82 NZ LYS A 12 37.200 34.278 17.245 0.00 0.00 N ATOM 83 N SER A 13 40.055 35.054 22.863 1.00 7.37 N ATOM 84 CA SER A 13 41.000 34.111 23.149 1.00 12.60 C ATOM 85 C SER A 13 40.467 33.024 24.172 1.00 24.72 C ATOM 86 O SER A 13 40.607 31.810 23.980 1.00 13.23 O ATOM 87 CB SER A 13 42.335 34.894 23.670 1.00 5.10 C ATOM 88 OG SER A 13 43.263 33.956 23.861 1.00 48.45 O ATOM 89 N SER A 14 39.908 33.457 25.247 1.00 21.53 N ATOM 90 CA SER A 14 39.375 32.518 26.318 1.00 10.70 C ATOM 91 C SER A 14 38.093 31.606 25.878 1.00 12.10 C ATOM 92 O SER A 14 37.839 30.404 26.276 1.00 13.21 O ATOM 93 CB SER A 14 39.075 33.287 27.588 1.00 18.07 C ATOM 94 OG SER A 14 38.100 34.147 27.293 1.00 20.97 O ATOM 95 N TRP A 15 37.387 32.129 24.970 1.00 14.58 N ATOM 96 CA TRP A 15 36.197 31.307 24.397 1.00 21.10 C ATOM 97 C TRP A 15 36.586 30.219 23.470 1.00 28.14 C ATOM 98 O TRP A 15 35.926 29.039 23.480 1.00 10.19 O ATOM 99 CB TRP A 15 35.297 32.195 23.674 1.00 15.28 C ATOM 100 CG TRP A 15 34.049 31.303 23.086 1.00 39.87 C ATOM 101 CD1 TRP A 15 32.940 30.648 23.705 1.00 28.42 C ATOM 102 CD2 TRP A 15 33.899 30.940 21.742 1.00 18.55 C ATOM 103 NE1 TRP A 15 32.095 29.893 22.758 1.00 27.82 N ATOM 104 CE2 TRP A 15 32.658 30.073 21.615 1.00 37.36 C ATOM 105 CE3 TRP A 15 34.747 31.289 20.665 1.00 12.34 C ATOM 106 CZ2 TRP A 15 32.197 29.531 20.398 1.00 33.08 C ATOM 107 CZ3 TRP A 15 34.288 30.737 19.442 1.00 44.98 C ATOM 108 CH2 TRP A 15 33.049 29.889 19.313 1.00 56.69 C ATOM 109 N GLU A 16 37.707 30.573 22.786 1.00 19.70 N ATOM 110 CA GLU A 16 38.207 29.560 21.948 1.00 28.26 C ATOM 111 C GLU A 16 38.709 28.454 22.773 1.00 30.82 C ATOM 112 O GLU A 16 38.308 27.237 22.469 1.00 22.43 O ATOM 113 CB GLU A 16 39.280 30.215 20.948 1.00 21.85 C ATOM 114 CG GLU A 16 38.655 31.089 19.922 1.00 30.80 C ATOM 115 CD GLU A 16 39.771 31.816 19.028 1.00 45.83 C ATOM 116 OE1 GLU A 16 40.949 32.113 19.491 1.00 46.38 O ATOM 117 OE2 GLU A 16 39.451 32.454 18.026 1.00 47.30 O ATOM 118 N GLU A 17 39.343 28.854 23.903 1.00 12.42 N ATOM 119 CA GLU A 17 39.700 27.853 24.858 1.00 5.18 C ATOM 120 C GLU A 17 38.474 26.919 25.404 1.00 16.86 C ATOM 121 O GLU A 17 38.540 25.684 25.550 1.00 17.37 O ATOM 122 CB GLU A 17 40.541 28.491 26.043 1.00 7.36 C ATOM 123 CG GLU A 17 42.045 28.892 25.685 1.00 33.58 C ATOM 124 CD GLU A 17 42.838 29.108 26.991 1.00 48.42 C ATOM 125 OE1 GLU A 17 43.274 28.116 27.512 1.00 45.51 O ATOM 126 OE2 GLU A 17 42.596 30.039 27.750 1.00 46.20 O ATOM 127 N PHE A 18 37.396 27.485 25.654 1.00 21.16 N ATOM 128 CA PHE A 18 36.127 26.694 26.141 1.00 9.85 C ATOM 129 C PHE A 18 35.567 25.633 25.106 1.00 12.52 C ATOM 130 O PHE A 18 35.152 24.421 25.418 1.00 17.41 O ATOM 131 CB PHE A 18 35.080 27.651 26.420 1.00 11.74 C ATOM 132 CG PHE A 18 33.661 26.899 26.789 1.00 15.12 C ATOM 133 CD1 PHE A 18 33.382 26.474 28.083 1.00 19.58 C ATOM 134 CD2 PHE A 18 32.671 26.638 25.822 1.00 20.71 C ATOM 135 CE1 PHE A 18 32.114 25.772 28.410 1.00 17.44 C ATOM 136 CE2 PHE A 18 31.403 25.932 26.140 1.00 13.99 C ATOM 137 CZ PHE A 18 31.126 25.496 27.436 1.00 8.76 C ATOM 138 N ASN A 19 35.532 26.102 23.895 1.00 19.94 N ATOM 139 CA ASN A 19 34.885 25.257 22.820 1.00 14.69 C ATOM 140 C ASN A 19 35.693 24.137 22.453 1.00 23.87 C ATOM 141 O ASN A 19 35.179 23.161 21.734 1.00 27.20 O ATOM 142 CB ASN A 19 34.759 26.162 21.601 1.00 17.56 C ATOM 143 CG ASN A 19 33.414 25.681 20.916 1.00 35.14 C ATOM 144 OD1 ASN A 19 32.342 25.836 21.512 1.00 39.45 O ATOM 145 ND2 ASN A 19 33.507 25.557 19.612 1.00 44.50 N ATOM 146 N ALA A 20 36.929 24.292 22.958 1.00 20.69 N ATOM 147 CA ALA A 20 37.858 23.331 22.685 1.00 11.76 C ATOM 148 C ALA A 20 37.477 22.010 23.440 1.00 28.05 C ATOM 149 O ALA A 20 37.971 20.981 23.097 1.00 28.67 O ATOM 150 CB ALA A 20 39.331 23.929 23.030 1.00 28.65 C ATOM 151 N ASN A 21 36.624 22.042 24.431 1.00 17.03 N ATOM 152 CA ASN A 21 36.154 20.813 25.207 1.00 14.11 C ATOM 153 C ASN A 21 34.741 20.778 25.779 1.00 10.88 C ATOM 154 O ASN A 21 34.555 20.708 27.020 1.00 16.63 O ATOM 155 CB ASN A 21 37.158 20.609 26.323 1.00 5.26 C ATOM 156 CG ASN A 21 36.965 19.121 26.728 1.00 8.59 C ATOM 157 OD1 ASN A 21 37.830 18.696 27.457 1.00 30.84 O ATOM 158 ND2 ASN A 21 35.857 18.369 26.298 1.00 12.46 N ATOM 159 N ILE A 22 33.808 20.840 24.873 1.00 9.67 N ATOM 160 CA ILE A 22 32.359 20.733 25.165 1.00 10.88 C ATOM 161 C ILE A 22 31.834 19.637 26.174 1.00 5.15 C ATOM 162 O ILE A 22 31.284 20.012 27.203 1.00 11.66 O ATOM 163 CB ILE A 22 31.468 20.623 23.896 1.00 12.76 C ATOM 164 CG1 ILE A 22 31.716 21.934 23.056 1.00 22.83 C ATOM 165 CG2 ILE A 22 29.948 20.166 24.198 1.00 11.45 C ATOM 166 CD1 ILE A 22 31.223 23.142 23.758 1.00 22.73 C ATOM 167 N PRO A 23 32.047 18.373 26.000 1.00 17.25 N ATOM 168 CA PRO A 23 31.487 17.315 26.952 1.00 14.69 C ATOM 169 C PRO A 23 31.995 17.577 28.378 1.00 23.07 C ATOM 170 O PRO A 23 31.158 17.432 29.324 1.00 21.26 O ATOM 171 CB PRO A 23 31.802 15.949 26.442 1.00 21.89 C ATOM 172 CG PRO A 23 32.396 16.209 25.039 1.00 19.06 C ATOM 173 CD PRO A 23 32.564 17.745 24.801 1.00 11.01 C ATOM 174 N LYS A 24 33.266 18.130 28.514 1.00 15.32 N ATOM 175 CA LYS A 24 33.805 18.471 29.850 1.00 14.81 C ATOM 176 C LYS A 24 33.291 19.703 30.438 1.00 28.90 C ATOM 177 O LYS A 24 32.751 19.636 31.577 1.00 18.17 O ATOM 178 CB LYS A 24 35.368 18.672 29.852 1.00 13.39 C ATOM 179 CG LYS A 24 35.973 18.895 31.267 1.00 28.67 C ATOM 180 CD LYS A 24 37.514 18.879 31.303 1.00 33.41 C ATOM 181 CE LYS A 24 38.316 19.972 30.410 0.00 0.00 C ATOM 182 NZ LYS A 24 39.772 19.918 30.491 0.00 0.00 N ATOM 183 N HIS A 25 33.471 20.788 29.684 1.00 16.08 N ATOM 184 CA HIS A 25 33.200 22.101 30.176 1.00 10.36 C ATOM 185 C HIS A 25 31.711 22.203 30.398 1.00 10.69 C ATOM 186 O HIS A 25 31.377 22.880 31.367 1.00 13.73 O ATOM 187 CB HIS A 25 33.869 23.238 29.259 1.00 3.00 C ATOM 188 CG HIS A 25 35.413 23.276 29.237 1.00 18.11 C ATOM 189 ND1 HIS A 25 36.118 22.938 30.367 1.00 25.31 N ATOM 190 CD2 HIS A 25 36.290 23.587 28.234 1.00 16.66 C ATOM 191 CE1 HIS A 25 37.495 23.051 30.015 1.00 16.92 C ATOM 192 NE2 HIS A 25 37.594 23.457 28.670 1.00 18.45 N ATOM 193 N THR A 26 30.842 21.514 29.574 1.00 13.68 N ATOM 194 CA THR A 26 29.385 21.527 29.727 1.00 10.00 C ATOM 195 C THR A 26 28.783 20.674 30.905 1.00 6.93 C ATOM 196 O THR A 26 27.865 21.058 31.592 1.00 10.13 O ATOM 197 CB THR A 26 28.591 21.095 28.438 1.00 26.39 C ATOM 198 OG1 THR A 26 28.697 19.722 28.104 1.00 16.79 O ATOM 199 CG2 THR A 26 29.067 22.039 27.258 1.00 9.88 C ATOM 200 N HIS A 27 29.350 19.606 31.182 1.00 14.11 N ATOM 201 CA HIS A 27 28.916 18.750 32.339 1.00 9.12 C ATOM 202 C HIS A 27 29.338 19.531 33.619 1.00 6.38 C ATOM 203 O HIS A 27 28.507 19.583 34.555 1.00 8.88 O ATOM 204 CB HIS A 27 29.569 17.450 32.248 1.00 11.41 C ATOM 205 CG HIS A 27 29.552 16.643 33.562 1.00 14.42 C ATOM 206 ND1 HIS A 27 28.382 15.808 34.037 1.00 23.61 N ATOM 207 CD2 HIS A 27 30.575 16.571 34.414 1.00 10.78 C ATOM 208 CE1 HIS A 27 28.733 15.227 35.246 1.00 16.83 C ATOM 209 NE2 HIS A 27 30.109 15.709 35.475 1.00 24.84 N ATOM 210 N ARG A 28 30.551 20.246 33.563 1.00 11.51 N ATOM 211 CA ARG A 28 31.137 21.071 34.685 1.00 9.03 C ATOM 212 C ARG A 28 30.362 22.229 35.024 1.00 16.71 C ATOM 213 O ARG A 28 30.082 22.433 36.225 1.00 15.71 O ATOM 214 CB ARG A 28 32.637 21.612 34.412 1.00 14.65 C ATOM 215 CG ARG A 28 33.330 22.351 35.637 1.00 35.41 C ATOM 216 CD ARG A 28 33.410 21.410 36.846 1.00 27.17 C ATOM 217 NE ARG A 28 33.950 22.235 37.995 1.00 43.07 N ATOM 218 CZ ARG A 28 33.728 21.898 39.259 1.00 49.11 C ATOM 219 NH1 ARG A 28 33.038 20.714 39.583 1.00 48.94 N ATOM 220 NH2 ARG A 28 34.233 22.749 40.203 1.00 44.36 N ATOM 221 N PHE A 29 29.923 22.853 33.980 1.00 17.83 N ATOM 222 CA PHE A 29 29.041 23.903 34.075 1.00 16.51 C ATOM 223 C PHE A 29 27.763 23.441 34.898 1.00 18.03 C ATOM 224 O PHE A 29 27.527 24.107 35.915 1.00 14.53 O ATOM 225 CB PHE A 29 28.682 24.368 32.657 1.00 13.78 C ATOM 226 CG PHE A 29 27.539 25.245 32.636 1.00 13.26 C ATOM 227 CD1 PHE A 29 27.749 26.548 33.135 1.00 6.69 C ATOM 228 CD2 PHE A 29 26.289 24.709 32.128 1.00 8.85 C ATOM 229 CE1 PHE A 29 26.704 27.317 33.131 1.00 12.94 C ATOM 230 CE2 PHE A 29 25.239 25.471 32.122 1.00 14.19 C ATOM 231 CZ PHE A 29 25.446 26.778 32.624 1.00 4.19 C ATOM 232 N PHE A 30 27.031 22.279 34.548 1.00 11.94 N ATOM 233 CA PHE A 30 25.793 21.716 35.284 1.00 9.69 C ATOM 234 C PHE A 30 26.026 21.235 36.700 1.00 7.50 C ATOM 235 O PHE A 30 25.172 21.378 37.588 1.00 11.34 O ATOM 236 CB PHE A 30 24.871 20.611 34.499 1.00 4.89 C ATOM 237 CG PHE A 30 23.986 21.240 33.491 1.00 13.23 C ATOM 238 CD1 PHE A 30 24.246 21.200 32.142 1.00 8.78 C ATOM 239 CD2 PHE A 30 22.935 21.857 33.950 1.00 19.15 C ATOM 240 CE1 PHE A 30 23.448 21.773 31.238 1.00 15.39 C ATOM 241 CE2 PHE A 30 22.134 22.436 33.056 1.00 17.25 C ATOM 242 CZ PHE A 30 22.389 22.392 31.697 1.00 22.18 C ATOM 243 N ILE A 31 27.205 20.838 36.934 1.00 10.00 N ATOM 244 CA ILE A 31 27.596 20.534 38.301 1.00 9.29 C ATOM 245 C ILE A 31 27.775 21.818 39.142 1.00 3.00 C ATOM 246 O ILE A 31 27.241 21.810 40.276 1.00 8.02 O ATOM 247 CB ILE A 31 28.924 19.918 38.344 1.00 18.32 C ATOM 248 CG1 ILE A 31 28.801 18.550 37.603 1.00 15.75 C ATOM 249 CG2 ILE A 31 29.425 19.782 39.789 1.00 11.48 C ATOM 250 CD1 ILE A 31 27.719 17.463 38.224 1.00 22.98 C ATOM 251 N LEU A 32 28.392 22.908 38.539 1.00 3.00 N ATOM 252 CA LEU A 32 28.601 24.225 39.217 1.00 4.24 C ATOM 253 C LEU A 32 27.291 24.797 39.435 1.00 8.58 C ATOM 254 O LEU A 32 27.134 25.409 40.504 1.00 11.79 O ATOM 255 CB LEU A 32 29.603 25.250 38.427 1.00 12.19 C ATOM 256 CG LEU A 32 31.062 24.940 38.511 1.00 16.10 C ATOM 257 CD1 LEU A 32 31.968 25.692 37.420 1.00 20.86 C ATOM 258 CD2 LEU A 32 31.672 25.254 39.912 1.00 18.11 C ATOM 259 N VAL A 33 26.345 24.539 38.516 1.00 13.03 N ATOM 260 CA VAL A 33 25.022 24.980 38.738 1.00 16.10 C ATOM 261 C VAL A 33 24.333 24.325 39.983 1.00 16.30 C ATOM 262 O VAL A 33 23.829 25.022 40.836 1.00 13.35 O ATOM 263 CB VAL A 33 24.045 24.625 37.551 1.00 13.98 C ATOM 264 CG1 VAL A 33 22.594 24.870 37.895 1.00 5.69 C ATOM 265 CG2 VAL A 33 24.567 25.372 36.262 1.00 12.47 C ATOM 266 N LEU A 34 24.329 23.016 40.045 1.00 17.66 N ATOM 267 CA LEU A 34 23.628 22.157 41.090 1.00 14.16 C ATOM 268 C LEU A 34 24.354 22.394 42.429 1.00 11.56 C ATOM 269 O LEU A 34 23.662 22.316 43.481 1.00 18.51 O ATOM 270 CB LEU A 34 23.502 20.662 40.659 1.00 8.08 C ATOM 271 CG LEU A 34 22.147 20.093 39.968 1.00 18.82 C ATOM 272 CD1 LEU A 34 21.469 21.132 39.185 1.00 14.27 C ATOM 273 CD2 LEU A 34 22.252 18.825 39.125 1.00 9.53 C ATOM 274 N GLU A 35 25.661 22.888 42.381 1.00 9.79 N ATOM 275 CA GLU A 35 26.418 23.321 43.607 1.00 12.13 C ATOM 276 C GLU A 35 26.003 24.589 44.227 1.00 14.99 C ATOM 277 O GLU A 35 26.080 24.763 45.469 1.00 15.50 O ATOM 278 CB GLU A 35 27.960 23.560 43.372 1.00 20.93 C ATOM 279 CG GLU A 35 28.505 22.230 43.081 1.00 46.35 C ATOM 280 CD GLU A 35 30.047 22.478 43.135 1.00 49.47 C ATOM 281 OE1 GLU A 35 30.663 21.478 43.039 1.00 42.48 O ATOM 282 OE2 GLU A 35 30.636 23.528 43.705 1.00 43.55 O ATOM 283 N ILE A 36 25.631 25.464 43.378 1.00 16.50 N ATOM 284 CA ILE A 36 25.271 26.772 43.801 1.00 12.60 C ATOM 285 C ILE A 36 23.786 26.641 44.205 1.00 13.50 C ATOM 286 O ILE A 36 23.433 27.224 45.230 1.00 13.47 O ATOM 287 CB ILE A 36 25.596 27.813 42.656 1.00 14.48 C ATOM 288 CG1 ILE A 36 27.133 28.092 42.364 1.00 9.25 C ATOM 289 CG2 ILE A 36 25.039 29.141 42.928 1.00 11.90 C ATOM 290 CD1 ILE A 36 27.478 28.954 41.099 1.00 13.31 C ATOM 291 N ALA A 37 22.951 25.813 43.468 1.00 8.68 N ATOM 292 CA ALA A 37 21.493 25.529 43.747 1.00 18.07 C ATOM 293 C ALA A 37 20.858 24.116 43.298 1.00 8.51 C ATOM 294 O ALA A 37 20.403 23.928 42.127 1.00 7.42 O ATOM 295 CB ALA A 37 20.751 26.585 43.059 1.00 13.39 C ATOM 296 N PRO A 38 20.947 23.155 44.173 1.00 13.68 N ATOM 297 CA PRO A 38 20.381 21.722 43.964 1.00 14.05 C ATOM 298 C PRO A 38 18.939 21.503 43.421 1.00 17.71 C ATOM 299 O PRO A 38 18.610 20.626 42.534 1.00 21.41 O ATOM 300 CB PRO A 38 20.425 21.002 45.321 1.00 17.01 C ATOM 301 CG PRO A 38 21.208 22.025 46.290 1.00 8.31 C ATOM 302 CD PRO A 38 21.510 23.378 45.537 1.00 8.22 C ATOM 303 N ALA A 39 18.144 22.332 43.888 1.00 13.18 N ATOM 304 CA ALA A 39 16.724 22.280 43.485 1.00 21.01 C ATOM 305 C ALA A 39 16.527 22.441 41.984 1.00 17.53 C ATOM 306 O ALA A 39 15.386 22.075 41.464 1.00 13.60 O ATOM 307 CB ALA A 39 16.091 23.377 44.232 1.00 17.04 C ATOM 308 N ALA A 40 17.574 23.078 41.329 1.00 16.06 N ATOM 309 CA ALA A 40 17.466 23.420 39.908 1.00 18.67 C ATOM 310 C ALA A 40 17.294 22.176 39.009 1.00 23.84 C ATOM 311 O ALA A 40 16.988 22.285 37.800 1.00 17.70 O ATOM 312 CB ALA A 40 18.714 24.410 39.445 1.00 20.65 C ATOM 313 N LYS A 41 17.586 21.066 39.575 1.00 14.30 N ATOM 314 CA LYS A 41 17.591 19.809 38.821 1.00 17.28 C ATOM 315 C LYS A 41 16.237 19.351 38.135 1.00 27.65 C ATOM 316 O LYS A 41 16.194 18.948 36.942 1.00 29.49 O ATOM 317 CB LYS A 41 17.898 18.688 39.776 1.00 22.58 C ATOM 318 CG LYS A 41 17.857 17.310 39.078 1.00 33.97 C ATOM 319 CD LYS A 41 18.222 16.246 40.069 1.00 42.68 C ATOM 320 CE LYS A 41 18.161 14.847 39.422 1.00 27.51 C ATOM 321 NZ LYS A 41 16.762 14.290 39.061 0.00 0.00 N ATOM 322 N ASP A 42 15.183 19.529 38.866 1.00 20.03 N ATOM 323 CA ASP A 42 13.781 19.162 38.418 1.00 25.23 C ATOM 324 C ASP A 42 13.425 19.895 37.165 1.00 22.90 C ATOM 325 O ASP A 42 12.422 19.375 36.487 1.00 23.07 O ATOM 326 CB ASP A 42 12.801 19.383 39.552 1.00 37.30 C ATOM 327 CG ASP A 42 13.101 18.499 40.722 1.00 59.52 C ATOM 328 OD1 ASP A 42 13.862 19.041 41.636 1.00 53.91 O ATOM 329 OD2 ASP A 42 13.079 17.259 40.500 1.00 51.35 O ATOM 330 N LEU A 43 14.198 21.055 36.880 1.00 16.60 N ATOM 331 CA LEU A 43 13.904 21.881 35.724 1.00 3.45 C ATOM 332 C LEU A 43 14.246 21.286 34.384 1.00 23.58 C ATOM 333 O LEU A 43 13.642 21.561 33.341 1.00 16.15 O ATOM 334 CB LEU A 43 14.685 23.338 35.815 1.00 18.77 C ATOM 335 CG LEU A 43 14.279 24.148 37.022 1.00 11.98 C ATOM 336 CD1 LEU A 43 15.186 25.539 37.124 1.00 11.81 C ATOM 337 CD2 LEU A 43 12.768 24.291 36.982 1.00 14.42 C ATOM 338 N PHE A 44 15.279 20.616 34.383 1.00 18.08 N ATOM 339 CA PHE A 44 15.848 20.167 33.129 1.00 16.01 C ATOM 340 C PHE A 44 15.307 18.700 32.771 1.00 27.06 C ATOM 341 O PHE A 44 15.377 17.784 33.615 1.00 20.64 O ATOM 342 CB PHE A 44 17.407 20.355 33.197 1.00 19.37 C ATOM 343 CG PHE A 44 18.048 21.853 33.342 1.00 24.68 C ATOM 344 CD1 PHE A 44 18.332 22.408 34.590 1.00 15.35 C ATOM 345 CD2 PHE A 44 18.352 22.638 32.219 1.00 15.23 C ATOM 346 CE1 PHE A 44 18.919 23.756 34.722 1.00 19.10 C ATOM 347 CE2 PHE A 44 18.942 23.988 32.341 1.00 6.90 C ATOM 348 CZ PHE A 44 19.224 24.548 33.594 1.00 4.70 C ATOM 349 N SER A 45 14.666 18.530 31.616 1.00 22.39 N ATOM 350 CA SER A 45 13.941 17.219 31.150 1.00 26.29 C ATOM 351 C SER A 45 14.811 16.097 31.108 1.00 22.89 C ATOM 352 O SER A 45 14.336 14.924 31.497 1.00 24.37 O ATOM 353 CB SER A 45 13.256 17.350 29.781 1.00 38.25 C ATOM 354 OG SER A 45 14.234 17.816 28.766 1.00 35.56 O ATOM 355 N PHE A 46 16.079 16.484 30.774 1.00 10.53 N ATOM 356 CA PHE A 46 17.070 15.548 30.750 1.00 9.18 C ATOM 357 C PHE A 46 17.724 15.352 32.100 1.00 32.63 C ATOM 358 O PHE A 46 18.495 14.481 32.205 1.00 22.84 O ATOM 359 CB PHE A 46 18.158 15.936 29.662 1.00 9.16 C ATOM 360 CG PHE A 46 18.788 17.443 29.711 1.00 20.98 C ATOM 361 CD1 PHE A 46 18.343 18.342 28.837 1.00 21.99 C ATOM 362 CD2 PHE A 46 19.783 17.897 30.628 1.00 30.85 C ATOM 363 CE1 PHE A 46 18.883 19.704 28.882 1.00 19.57 C ATOM 364 CE2 PHE A 46 20.331 19.258 30.680 1.00 26.50 C ATOM 365 CZ PHE A 46 19.879 20.163 29.805 1.00 16.74 C ATOM 366 N LEU A 47 17.369 16.051 33.128 1.00 29.65 N ATOM 367 CA LEU A 47 17.868 15.819 34.488 1.00 19.52 C ATOM 368 C LEU A 47 16.772 15.068 35.390 1.00 30.30 C ATOM 369 O LEU A 47 17.094 14.349 36.335 1.00 21.57 O ATOM 370 CB LEU A 47 18.461 17.144 35.195 1.00 22.26 C ATOM 371 CG LEU A 47 19.739 17.881 34.503 1.00 31.18 C ATOM 372 CD1 LEU A 47 20.305 19.193 35.251 1.00 22.17 C ATOM 373 CD2 LEU A 47 20.817 16.949 34.332 1.00 27.77 C ATOM 374 N LYS A 48 15.532 15.294 35.130 1.00 51.97 N ATOM 375 CA LYS A 48 14.359 14.639 35.894 1.00 58.91 C ATOM 376 C LYS A 48 14.275 13.107 35.879 1.00 51.69 C ATOM 377 O LYS A 48 14.184 12.483 34.785 1.00 49.86 O ATOM 378 CB LYS A 48 13.016 14.939 35.303 1.00 45.82 C ATOM 379 CG LYS A 48 12.867 16.443 35.344 0.00 0.00 C ATOM 380 CD LYS A 48 11.457 16.651 34.847 0.00 0.00 C ATOM 381 CE LYS A 48 11.150 16.058 33.440 0.00 0.00 C ATOM 382 NZ LYS A 48 9.786 16.254 33.026 0.00 0.00 N ATOM 383 N GLY A 49 14.270 12.532 37.051 1.00 50.11 N ATOM 384 CA GLY A 49 14.078 11.062 37.182 1.00 55.72 C ATOM 385 C GLY A 49 15.405 10.515 37.333 1.00 56.34 C ATOM 386 O GLY A 49 15.417 9.434 37.971 1.00 54.20 O ATOM 387 N THR A 50 16.496 11.272 36.836 1.00 40.66 N ATOM 388 CA THR A 50 17.833 10.864 37.029 1.00 53.69 C ATOM 389 C THR A 50 18.279 11.033 38.488 1.00 59.94 C ATOM 390 O THR A 50 17.695 11.748 39.258 1.00 55.32 O ATOM 391 CB THR A 50 18.931 11.669 36.131 1.00 44.61 C ATOM 392 OG1 THR A 50 19.441 12.945 36.726 1.00 32.67 O ATOM 393 CG2 THR A 50 18.436 11.878 34.701 1.00 27.33 C ATOM 394 N SER A 51 19.309 10.470 38.870 1.00 48.81 N ATOM 395 CA SER A 51 19.851 10.739 40.221 1.00 48.61 C ATOM 396 C SER A 51 21.168 11.720 40.163 1.00 52.53 C ATOM 397 O SER A 51 21.310 12.832 40.779 1.00 50.93 O ATOM 398 CB SER A 51 20.132 9.434 40.899 1.00 57.84 C ATOM 399 OG SER A 51 20.705 9.770 42.194 0.00 0.00 O ATOM 400 N GLU A 52 21.994 11.377 39.261 1.00 41.31 N ATOM 401 CA GLU A 52 23.243 12.238 38.869 1.00 50.13 C ATOM 402 C GLU A 52 23.093 12.853 37.496 1.00 47.05 C ATOM 403 O GLU A 52 22.268 12.249 36.665 1.00 36.99 O ATOM 404 CB GLU A 52 24.417 11.407 38.836 1.00 42.98 C ATOM 405 CG GLU A 52 24.652 10.774 40.203 0.00 0.00 C ATOM 406 CD GLU A 52 25.851 10.007 40.084 0.00 0.00 C ATOM 407 OE1 GLU A 52 26.691 10.299 39.154 0.00 0.00 O ATOM 408 OE2 GLU A 52 26.173 9.337 41.064 0.00 0.00 O ATOM 409 N VAL A 53 23.885 14.001 37.272 1.00 22.83 N ATOM 410 CA VAL A 53 23.955 14.673 35.973 1.00 23.58 C ATOM 411 C VAL A 53 24.625 13.859 34.950 1.00 23.69 C ATOM 412 O VAL A 53 25.746 13.495 35.210 1.00 20.24 O ATOM 413 CB VAL A 53 24.720 16.129 36.147 1.00 25.49 C ATOM 414 CG1 VAL A 53 25.025 16.917 34.828 1.00 11.17 C ATOM 415 CG2 VAL A 53 23.942 16.913 37.121 1.00 13.52 C ATOM 416 N PRO A 54 23.837 13.384 33.943 1.00 16.25 N ATOM 417 CA PRO A 54 24.259 12.557 32.846 1.00 11.44 C ATOM 418 C PRO A 54 25.559 13.221 32.168 1.00 23.91 C ATOM 419 O PRO A 54 25.825 14.487 32.058 1.00 22.85 O ATOM 420 CB PRO A 54 23.125 12.374 31.797 1.00 13.62 C ATOM 421 CG PRO A 54 22.087 13.259 32.241 1.00 23.52 C ATOM 422 CD PRO A 54 22.509 13.786 33.646 1.00 12.15 C ATOM 423 N GLN A 55 26.407 12.399 31.844 1.00 20.83 N ATOM 424 CA GLN A 55 27.746 12.921 31.320 1.00 16.45 C ATOM 425 C GLN A 55 27.840 12.921 29.799 1.00 18.13 C ATOM 426 O GLN A 55 28.620 13.838 29.205 1.00 26.04 O ATOM 427 CB GLN A 55 28.791 12.143 31.956 1.00 22.48 C ATOM 428 CG GLN A 55 28.579 12.066 33.479 1.00 23.70 C ATOM 429 CD GLN A 55 29.744 11.495 34.132 1.00 52.30 C ATOM 430 OE1 GLN A 55 30.903 11.764 33.624 1.00 54.57 O ATOM 431 NE2 GLN A 55 29.528 11.147 35.392 1.00 52.48 N ATOM 432 N ASN A 56 27.078 11.922 29.181 1.00 15.18 N ATOM 433 CA ASN A 56 27.056 11.784 27.715 1.00 13.70 C ATOM 434 C ASN A 56 25.660 11.829 27.121 1.00 15.10 C ATOM 435 O ASN A 56 25.172 10.976 26.259 1.00 17.38 O ATOM 436 CB ASN A 56 27.545 10.461 27.272 1.00 9.81 C ATOM 437 CG ASN A 56 29.025 10.502 27.664 1.00 30.97 C ATOM 438 OD1 ASN A 56 29.297 10.134 28.824 1.00 18.53 O ATOM 439 ND2 ASN A 56 29.853 11.405 26.981 1.00 22.87 N ATOM 440 N ASN A 57 25.040 12.811 27.550 1.00 10.70 N ATOM 441 CA ASN A 57 23.701 12.991 27.049 1.00 11.03 C ATOM 442 C ASN A 57 23.795 14.143 26.041 1.00 15.23 C ATOM 443 O ASN A 57 24.301 15.312 26.404 1.00 18.46 O ATOM 444 CB ASN A 57 22.784 13.267 28.226 1.00 10.89 C ATOM 445 CG ASN A 57 21.338 13.265 27.736 1.00 15.71 C ATOM 446 OD1 ASN A 57 21.054 14.278 27.120 1.00 23.38 O ATOM 447 ND2 ASN A 57 20.419 12.430 28.399 1.00 14.02 N ATOM 448 N PRO A 58 23.341 13.831 24.825 1.00 15.08 N ATOM 449 CA PRO A 58 23.475 14.794 23.697 1.00 13.47 C ATOM 450 C PRO A 58 22.620 15.927 23.821 1.00 15.59 C ATOM 451 O PRO A 58 23.030 17.044 23.268 1.00 14.81 O ATOM 452 CB PRO A 58 23.067 13.996 22.414 1.00 13.64 C ATOM 453 CG PRO A 58 22.544 12.542 22.850 1.00 13.56 C ATOM 454 CD PRO A 58 22.755 12.466 24.370 1.00 12.93 C ATOM 455 N GLU A 59 21.492 15.659 24.531 1.00 16.51 N ATOM 456 CA GLU A 59 20.646 16.710 24.782 1.00 10.57 C ATOM 457 C GLU A 59 21.380 17.783 25.704 1.00 11.24 C ATOM 458 O GLU A 59 21.481 19.008 25.389 1.00 14.37 O ATOM 459 CB GLU A 59 19.306 16.173 25.486 1.00 14.12 C ATOM 460 CG GLU A 59 18.159 15.592 24.531 1.00 51.96 C ATOM 461 CD GLU A 59 16.836 15.694 25.257 1.00 68.81 C ATOM 462 OE1 GLU A 59 16.588 16.854 25.552 1.00 61.08 O ATOM 463 OE2 GLU A 59 16.288 14.706 25.943 1.00 52.30 O ATOM 464 N LEU A 60 21.870 17.300 26.784 1.00 11.43 N ATOM 465 CA LEU A 60 22.671 18.180 27.744 1.00 9.12 C ATOM 466 C LEU A 60 23.877 19.019 27.051 1.00 7.78 C ATOM 467 O LEU A 60 24.165 20.264 27.287 1.00 14.12 O ATOM 468 CB LEU A 60 23.125 17.324 28.900 1.00 14.40 C ATOM 469 CG LEU A 60 23.910 18.152 30.040 1.00 18.96 C ATOM 470 CD1 LEU A 60 23.626 17.455 31.405 1.00 7.99 C ATOM 471 CD2 LEU A 60 25.451 18.483 29.788 1.00 9.70 C ATOM 472 N GLN A 61 24.561 18.347 26.240 1.00 5.54 N ATOM 473 CA GLN A 61 25.790 19.016 25.578 1.00 9.83 C ATOM 474 C GLN A 61 25.511 20.089 24.582 1.00 15.66 C ATOM 475 O GLN A 61 26.274 21.216 24.569 1.00 6.99 O ATOM 476 CB GLN A 61 26.564 17.988 24.892 1.00 9.63 C ATOM 477 CG GLN A 61 27.190 17.131 25.931 1.00 9.02 C ATOM 478 CD GLN A 61 27.872 16.062 25.227 1.00 15.30 C ATOM 479 OE1 GLN A 61 28.258 15.141 25.916 1.00 20.21 O ATOM 480 NE2 GLN A 61 27.617 15.943 23.941 1.00 7.92 N ATOM 481 N ALA A 62 24.411 19.759 23.848 1.00 14.07 N ATOM 482 CA ALA A 62 23.991 20.682 22.845 1.00 19.01 C ATOM 483 C ALA A 62 23.455 21.879 23.474 1.00 21.34 C ATOM 484 O ALA A 62 23.864 23.049 23.045 1.00 15.25 O ATOM 485 CB ALA A 62 22.903 19.946 21.911 1.00 16.56 C ATOM 486 N HIS A 63 22.698 21.598 24.545 1.00 11.96 N ATOM 487 CA HIS A 63 22.214 22.657 25.343 1.00 15.61 C ATOM 488 C HIS A 63 23.373 23.681 25.908 1.00 19.33 C ATOM 489 O HIS A 63 23.453 24.921 25.636 1.00 13.78 O ATOM 490 CB HIS A 63 21.339 21.996 26.503 1.00 4.87 C ATOM 491 CG HIS A 63 20.860 23.055 27.433 1.00 11.15 C ATOM 492 ND1 HIS A 63 19.606 23.473 27.256 1.00 24.20 N ATOM 493 CD2 HIS A 63 21.477 23.695 28.500 1.00 18.17 C ATOM 494 CE1 HIS A 63 19.466 24.408 28.271 1.00 21.65 C ATOM 495 NE2 HIS A 63 20.645 24.546 29.046 1.00 12.92 N ATOM 496 N ALA A 64 24.212 23.175 26.717 1.00 15.06 N ATOM 497 CA ALA A 64 25.308 24.055 27.396 1.00 9.28 C ATOM 498 C ALA A 64 26.326 24.814 26.420 1.00 16.21 C ATOM 499 O ALA A 64 26.805 26.027 26.651 1.00 16.20 O ATOM 500 CB ALA A 64 26.022 23.267 28.425 1.00 10.77 C ATOM 501 N GLY A 65 26.468 24.186 25.278 1.00 12.00 N ATOM 502 CA GLY A 65 27.295 24.828 24.174 1.00 13.51 C ATOM 503 C GLY A 65 26.773 26.087 23.651 1.00 34.28 C ATOM 504 O GLY A 65 27.586 27.169 23.486 1.00 16.61 O ATOM 505 N LYS A 66 25.446 25.944 23.473 1.00 18.40 N ATOM 506 CA LYS A 66 24.747 27.044 22.980 1.00 11.99 C ATOM 507 C LYS A 66 24.861 28.234 23.944 1.00 25.30 C ATOM 508 O LYS A 66 25.028 29.418 23.487 1.00 19.06 O ATOM 509 CB LYS A 66 23.233 26.539 22.725 1.00 15.55 C ATOM 510 CG LYS A 66 23.016 25.557 21.532 1.00 57.86 C ATOM 511 CD LYS A 66 21.546 24.819 21.422 1.00 60.29 C ATOM 512 CE LYS A 66 20.525 25.774 21.088 1.00 57.85 C ATOM 513 NZ LYS A 66 19.174 24.981 20.900 0.00 0.00 N ATOM 514 N VAL A 67 24.748 27.914 25.222 1.00 15.22 N ATOM 515 CA VAL A 67 24.848 28.965 26.257 1.00 21.09 C ATOM 516 C VAL A 67 26.223 29.867 26.237 1.00 17.15 C ATOM 517 O VAL A 67 26.294 31.134 26.194 1.00 16.31 O ATOM 518 CB VAL A 67 24.584 28.342 27.660 1.00 15.55 C ATOM 519 CG1 VAL A 67 24.820 29.427 28.768 1.00 11.37 C ATOM 520 CG2 VAL A 67 23.153 27.518 27.756 1.00 8.50 C ATOM 521 N PHE A 68 27.271 29.218 26.168 1.00 12.01 N ATOM 522 CA PHE A 68 28.645 29.976 26.152 1.00 15.38 C ATOM 523 C PHE A 68 28.960 30.757 24.857 1.00 18.03 C ATOM 524 O PHE A 68 29.635 31.926 24.901 1.00 17.25 O ATOM 525 CB PHE A 68 29.718 29.066 26.422 1.00 11.69 C ATOM 526 CG PHE A 68 29.838 28.758 27.924 1.00 19.55 C ATOM 527 CD1 PHE A 68 30.924 29.401 28.647 1.00 15.85 C ATOM 528 CD2 PHE A 68 28.885 27.814 28.538 1.00 8.41 C ATOM 529 CE1 PHE A 68 31.064 29.095 29.989 1.00 9.72 C ATOM 530 CE2 PHE A 68 29.016 27.500 29.876 1.00 7.53 C ATOM 531 CZ PHE A 68 30.107 28.141 30.604 1.00 18.59 C ATOM 532 N LYS A 69 28.359 30.190 23.784 1.00 11.46 N ATOM 533 CA LYS A 69 28.546 30.879 22.495 1.00 7.08 C ATOM 534 C LYS A 69 27.903 32.166 22.434 1.00 9.72 C ATOM 535 O LYS A 69 28.555 33.215 21.925 1.00 11.70 O ATOM 536 CB LYS A 69 28.031 29.943 21.330 1.00 9.23 C ATOM 537 CG LYS A 69 28.623 30.541 19.998 1.00 18.74 C ATOM 538 CD LYS A 69 27.750 29.967 18.806 1.00 48.40 C ATOM 539 CE LYS A 69 26.290 30.256 18.976 1.00 56.54 C ATOM 540 NZ LYS A 69 25.495 29.861 17.767 0.00 0.00 N ATOM 541 N LEU A 70 26.723 32.124 23.035 1.00 10.57 N ATOM 542 CA LEU A 70 26.034 33.319 23.105 1.00 8.07 C ATOM 543 C LEU A 70 26.808 34.465 23.926 1.00 19.49 C ATOM 544 O LEU A 70 26.861 35.658 23.518 1.00 14.71 O ATOM 545 CB LEU A 70 24.593 32.999 23.680 1.00 4.39 C ATOM 546 CG LEU A 70 23.616 32.128 22.728 1.00 21.85 C ATOM 547 CD1 LEU A 70 22.193 31.798 23.344 1.00 26.44 C ATOM 548 CD2 LEU A 70 23.583 32.807 21.348 1.00 27.22 C ATOM 549 N VAL A 71 27.383 34.122 25.035 1.00 8.81 N ATOM 550 CA VAL A 71 28.154 35.185 25.870 1.00 10.98 C ATOM 551 C VAL A 71 29.471 35.828 25.205 1.00 21.60 C ATOM 552 O VAL A 71 29.799 37.095 25.187 1.00 13.59 O ATOM 553 CB VAL A 71 28.401 34.682 27.295 1.00 11.33 C ATOM 554 CG1 VAL A 71 29.251 35.790 28.147 1.00 4.01 C ATOM 555 CG2 VAL A 71 27.055 34.144 28.002 1.00 3.64 C ATOM 556 N TYR A 72 30.071 34.983 24.497 1.00 21.55 N ATOM 557 CA TYR A 72 31.266 35.431 23.663 1.00 11.99 C ATOM 558 C TYR A 72 30.945 36.358 22.535 1.00 12.40 C ATOM 559 O TYR A 72 31.725 37.449 22.311 1.00 16.96 O ATOM 560 CB TYR A 72 31.842 34.177 23.135 1.00 11.36 C ATOM 561 CG TYR A 72 32.673 34.429 21.837 1.00 5.46 C ATOM 562 CD1 TYR A 72 32.132 33.867 20.662 1.00 24.66 C ATOM 563 CD2 TYR A 72 33.931 35.224 21.834 1.00 10.46 C ATOM 564 CE1 TYR A 72 32.838 34.104 19.473 1.00 24.31 C ATOM 565 CE2 TYR A 72 34.645 35.467 20.647 1.00 8.48 C ATOM 566 CZ TYR A 72 34.092 34.907 19.468 1.00 21.56 C ATOM 567 OH TYR A 72 34.817 35.159 18.235 1.00 34.94 O ATOM 568 N GLU A 73 29.812 35.957 21.871 1.00 16.27 N ATOM 569 CA GLU A 73 29.424 36.753 20.744 1.00 13.49 C ATOM 570 C GLU A 73 29.057 38.104 21.200 1.00 14.57 C ATOM 571 O GLU A 73 29.467 39.155 20.537 1.00 15.41 O ATOM 572 CB GLU A 73 28.254 35.963 19.926 1.00 11.70 C ATOM 573 CG GLU A 73 28.701 34.763 19.169 1.00 30.57 C ATOM 574 CD GLU A 73 27.554 34.082 18.277 1.00 38.32 C ATOM 575 OE1 GLU A 73 27.815 33.296 17.366 1.00 40.55 O ATOM 576 OE2 GLU A 73 26.340 34.094 18.598 1.00 34.04 O ATOM 577 N ALA A 74 28.449 38.074 22.373 1.00 12.42 N ATOM 578 CA ALA A 74 28.111 39.298 23.022 1.00 14.79 C ATOM 579 C ALA A 74 29.366 40.323 23.317 1.00 8.32 C ATOM 580 O ALA A 74 29.380 41.551 23.044 1.00 12.98 O ATOM 581 CB ALA A 74 27.335 38.953 24.337 1.00 16.37 C ATOM 582 N ALA A 75 30.399 39.802 23.792 1.00 10.41 N ATOM 583 CA ALA A 75 31.696 40.644 24.101 1.00 7.31 C ATOM 584 C ALA A 75 32.373 41.335 22.866 1.00 12.23 C ATOM 585 O ALA A 75 32.968 42.535 22.938 1.00 18.11 O ATOM 586 CB ALA A 75 32.678 39.806 24.763 1.00 4.69 C ATOM 587 N ILE A 76 32.275 40.606 21.767 1.00 17.49 N ATOM 588 CA ILE A 76 32.894 41.197 20.531 1.00 14.30 C ATOM 589 C ILE A 76 32.081 42.238 19.980 1.00 25.10 C ATOM 590 O ILE A 76 32.676 43.386 19.633 1.00 12.02 O ATOM 591 CB ILE A 76 33.003 40.112 19.455 1.00 19.75 C ATOM 592 CG1 ILE A 76 33.775 38.994 19.970 1.00 20.87 C ATOM 593 CG2 ILE A 76 33.620 40.743 18.141 1.00 16.69 C ATOM 594 CD1 ILE A 76 35.241 39.549 20.381 1.00 15.26 C ATOM 595 N GLN A 77 30.757 41.878 20.042 1.00 4.50 N ATOM 596 CA GLN A 77 29.863 42.813 19.602 1.00 8.41 C ATOM 597 C GLN A 77 30.021 44.123 20.418 1.00 21.07 C ATOM 598 O GLN A 77 30.152 45.241 19.829 1.00 15.59 O ATOM 599 CB GLN A 77 28.381 42.103 19.530 1.00 11.74 C ATOM 600 CG GLN A 77 27.495 42.961 18.747 1.00 20.31 C ATOM 601 CD GLN A 77 26.113 42.123 18.498 1.00 21.68 C ATOM 602 OE1 GLN A 77 25.765 41.757 17.329 1.00 21.90 O ATOM 603 NE2 GLN A 77 25.454 41.680 19.582 1.00 4.66 N ATOM 604 N LEU A 78 30.266 44.019 21.704 1.00 17.79 N ATOM 605 CA LEU A 78 30.595 45.226 22.561 1.00 10.83 C ATOM 606 C LEU A 78 31.924 46.093 22.166 1.00 8.20 C ATOM 607 O LEU A 78 32.008 47.356 22.107 1.00 21.08 O ATOM 608 CB LEU A 78 30.713 44.812 24.030 1.00 15.78 C ATOM 609 CG LEU A 78 29.337 44.546 24.741 1.00 18.95 C ATOM 610 CD1 LEU A 78 29.405 43.673 26.001 1.00 16.51 C ATOM 611 CD2 LEU A 78 28.826 45.889 25.065 1.00 9.93 C ATOM 612 N GLU A 79 32.904 45.424 21.851 1.00 11.43 N ATOM 613 CA GLU A 79 34.226 46.150 21.468 1.00 4.52 C ATOM 614 C GLU A 79 34.173 46.875 20.133 1.00 17.80 C ATOM 615 O GLU A 79 34.733 48.083 20.016 1.00 23.04 O ATOM 616 CB GLU A 79 35.277 45.176 21.438 1.00 14.71 C ATOM 617 CG GLU A 79 36.749 45.909 21.346 1.00 10.56 C ATOM 618 CD GLU A 79 37.304 45.739 19.947 1.00 39.06 C ATOM 619 OE1 GLU A 79 36.982 44.631 19.348 1.00 36.77 O ATOM 620 OE2 GLU A 79 37.764 46.777 19.283 1.00 36.87 O ATOM 621 N VAL A 80 33.510 46.155 19.178 1.00 11.29 N ATOM 622 CA VAL A 80 33.367 46.658 17.811 1.00 20.43 C ATOM 623 C VAL A 80 32.462 47.752 17.712 1.00 28.29 C ATOM 624 O VAL A 80 32.843 48.806 17.042 1.00 24.52 O ATOM 625 CB VAL A 80 32.833 45.459 16.882 1.00 5.35 C ATOM 626 CG1 VAL A 80 32.415 45.906 15.488 1.00 14.93 C ATOM 627 CG2 VAL A 80 33.901 44.514 16.759 1.00 14.25 C ATOM 628 N THR A 81 31.251 47.447 18.237 1.00 11.10 N ATOM 629 CA THR A 81 30.202 48.287 18.016 1.00 16.50 C ATOM 630 C THR A 81 29.973 49.173 19.204 1.00 12.06 C ATOM 631 O THR A 81 29.398 50.186 19.020 1.00 15.44 O ATOM 632 CB THR A 81 28.849 47.410 17.646 1.00 3.64 C ATOM 633 OG1 THR A 81 28.263 46.697 18.803 1.00 17.24 O ATOM 634 CG2 THR A 81 29.011 46.409 16.514 1.00 11.93 C ATOM 635 N GLY A 82 30.277 48.734 20.387 1.00 11.09 N ATOM 636 CA GLY A 82 30.009 49.463 21.609 1.00 8.94 C ATOM 637 C GLY A 82 28.693 48.882 22.312 1.00 13.00 C ATOM 638 O GLY A 82 28.392 49.349 23.420 1.00 14.54 O ATOM 639 N VAL A 83 27.883 47.942 21.668 1.00 15.33 N ATOM 640 CA VAL A 83 26.594 47.304 22.265 1.00 17.15 C ATOM 641 C VAL A 83 26.389 45.761 22.189 1.00 14.22 C ATOM 642 O VAL A 83 26.999 45.200 21.304 1.00 16.66 O ATOM 643 CB VAL A 83 25.378 47.828 21.596 1.00 8.46 C ATOM 644 CG1 VAL A 83 25.416 49.359 21.797 1.00 17.66 C ATOM 645 CG2 VAL A 83 25.236 47.456 20.101 1.00 14.89 C ATOM 646 N VAL A 84 25.335 45.136 22.854 1.00 15.85 N ATOM 647 CA VAL A 84 24.705 43.751 22.515 1.00 22.06 C ATOM 648 C VAL A 84 23.393 43.802 21.756 1.00 12.88 C ATOM 649 O VAL A 84 22.506 44.397 22.281 1.00 20.73 O ATOM 650 CB VAL A 84 24.397 42.864 23.777 1.00 15.13 C ATOM 651 CG1 VAL A 84 23.572 41.474 23.446 1.00 14.88 C ATOM 652 CG2 VAL A 84 25.696 42.690 24.535 1.00 19.37 C ATOM 653 N VAL A 85 23.335 43.350 20.515 1.00 13.02 N ATOM 654 CA VAL A 85 22.152 43.388 19.649 1.00 16.50 C ATOM 655 C VAL A 85 21.002 42.233 19.936 1.00 17.06 C ATOM 656 O VAL A 85 21.168 41.024 19.762 1.00 23.08 O ATOM 657 CB VAL A 85 22.560 43.360 18.162 1.00 16.21 C ATOM 658 CG1 VAL A 85 21.349 43.328 17.198 1.00 20.06 C ATOM 659 CG2 VAL A 85 23.697 44.534 17.824 1.00 27.40 C ATOM 660 N THR A 86 19.866 42.598 20.354 1.00 20.73 N ATOM 661 CA THR A 86 18.651 41.600 20.555 1.00 38.64 C ATOM 662 C THR A 86 18.045 41.092 19.219 1.00 26.97 C ATOM 663 O THR A 86 17.520 41.887 18.483 1.00 40.02 O ATOM 664 CB THR A 86 17.556 42.221 21.310 1.00 34.66 C ATOM 665 OG1 THR A 86 18.126 43.003 22.429 1.00 40.82 O ATOM 666 CG2 THR A 86 16.390 41.124 21.765 1.00 39.65 C ATOM 667 N ASP A 87 18.118 39.825 18.915 1.00 25.14 N ATOM 668 CA ASP A 87 17.476 39.205 17.702 1.00 24.02 C ATOM 669 C ASP A 87 16.306 38.065 17.970 1.00 35.59 C ATOM 670 O ASP A 87 15.868 37.861 19.144 1.00 30.42 O ATOM 671 CB ASP A 87 18.509 38.729 16.747 1.00 15.42 C ATOM 672 CG ASP A 87 19.038 37.491 17.305 1.00 43.80 C ATOM 673 OD1 ASP A 87 18.903 37.201 18.527 1.00 45.40 O ATOM 674 OD2 ASP A 87 19.948 37.038 16.660 1.00 42.92 O ATOM 675 N ALA A 88 15.841 37.360 16.912 1.00 28.01 N ATOM 676 CA ALA A 88 14.693 36.254 16.981 1.00 44.26 C ATOM 677 C ALA A 88 14.961 35.119 17.910 1.00 39.27 C ATOM 678 O ALA A 88 14.066 34.609 18.718 1.00 39.31 O ATOM 679 CB ALA A 88 14.333 35.664 15.583 1.00 45.37 C ATOM 680 N THR A 89 16.202 34.847 17.857 1.00 20.42 N ATOM 681 CA THR A 89 16.691 33.840 18.709 1.00 29.94 C ATOM 682 C THR A 89 16.609 34.172 20.191 1.00 34.77 C ATOM 683 O THR A 89 16.147 33.259 21.005 1.00 33.77 O ATOM 684 CB THR A 89 18.165 33.755 18.328 1.00 40.36 C ATOM 685 OG1 THR A 89 18.216 33.454 16.929 1.00 48.91 O ATOM 686 CG2 THR A 89 18.773 32.688 19.146 1.00 41.74 C ATOM 687 N LEU A 90 17.030 35.437 20.527 1.00 16.86 N ATOM 688 CA LEU A 90 17.061 35.808 21.942 1.00 13.98 C ATOM 689 C LEU A 90 15.655 35.911 22.464 1.00 28.54 C ATOM 690 O LEU A 90 15.345 35.572 23.648 1.00 22.70 O ATOM 691 CB LEU A 90 18.016 37.133 22.240 1.00 16.87 C ATOM 692 CG LEU A 90 19.503 37.058 21.884 1.00 34.73 C ATOM 693 CD1 LEU A 90 20.443 38.377 22.256 1.00 32.51 C ATOM 694 CD2 LEU A 90 20.002 35.808 22.492 1.00 31.31 C ATOM 695 N LYS A 91 14.820 36.286 21.572 1.00 24.78 N ATOM 696 CA LYS A 91 13.402 36.297 21.939 1.00 38.05 C ATOM 697 C LYS A 91 12.683 34.859 22.175 1.00 34.51 C ATOM 698 O LYS A 91 11.872 34.589 23.132 1.00 36.16 O ATOM 699 CB LYS A 91 12.625 36.949 20.851 1.00 32.62 C ATOM 700 CG LYS A 91 13.207 38.441 20.589 1.00 25.81 C ATOM 701 CD LYS A 91 12.177 39.173 19.855 0.00 0.00 C ATOM 702 CE LYS A 91 12.738 40.669 19.577 0.00 0.00 C ATOM 703 NZ LYS A 91 13.889 40.765 18.651 0.00 0.00 N ATOM 704 N ASN A 92 13.069 33.952 21.377 1.00 23.11 N ATOM 705 CA ASN A 92 12.514 32.526 21.532 1.00 15.47 C ATOM 706 C ASN A 92 13.051 31.935 22.787 1.00 15.96 C ATOM 707 O ASN A 92 12.226 31.229 23.549 1.00 28.19 O ATOM 708 CB ASN A 92 12.813 31.698 20.309 1.00 33.65 C ATOM 709 CG ASN A 92 12.119 30.250 20.544 1.00 57.45 C ATOM 710 OD1 ASN A 92 10.849 30.033 20.643 1.00 54.63 O ATOM 711 ND2 ASN A 92 12.908 29.476 21.116 1.00 52.86 N ATOM 712 N LEU A 93 14.339 32.393 23.070 1.00 16.82 N ATOM 713 CA LEU A 93 14.969 32.049 24.330 1.00 15.25 C ATOM 714 C LEU A 93 14.212 32.442 25.550 1.00 17.08 C ATOM 715 O LEU A 93 13.931 31.601 26.478 1.00 22.13 O ATOM 716 CB LEU A 93 16.459 32.707 24.483 1.00 17.26 C ATOM 717 CG LEU A 93 17.458 31.839 23.904 1.00 31.64 C ATOM 718 CD1 LEU A 93 18.917 32.416 24.321 1.00 34.23 C ATOM 719 CD2 LEU A 93 17.086 30.349 24.331 1.00 37.19 C ATOM 720 N GLY A 94 13.827 33.641 25.491 1.00 25.17 N ATOM 721 CA GLY A 94 13.067 34.161 26.579 1.00 17.51 C ATOM 722 C GLY A 94 11.730 33.247 26.861 1.00 19.39 C ATOM 723 O GLY A 94 11.361 32.953 28.042 1.00 23.04 O ATOM 724 N SER A 95 11.082 32.755 25.786 1.00 26.82 N ATOM 725 CA SER A 95 9.796 31.836 25.862 1.00 28.35 C ATOM 726 C SER A 95 9.956 30.483 26.493 1.00 22.52 C ATOM 727 O SER A 95 9.163 30.005 27.410 1.00 29.33 O ATOM 728 CB SER A 95 9.187 31.591 24.454 1.00 24.03 C ATOM 729 OG SER A 95 8.011 30.577 24.525 1.00 50.49 O ATOM 730 N VAL A 96 10.960 29.906 26.016 1.00 19.55 N ATOM 731 CA VAL A 96 11.215 28.591 26.528 1.00 10.87 C ATOM 732 C VAL A 96 11.573 28.601 28.010 1.00 28.26 C ATOM 733 O VAL A 96 11.031 27.642 28.739 1.00 27.79 O ATOM 734 CB VAL A 96 12.160 27.871 25.639 1.00 16.71 C ATOM 735 CG1 VAL A 96 13.335 28.814 24.989 1.00 46.61 C ATOM 736 CG2 VAL A 96 12.682 26.677 26.339 1.00 33.00 C ATOM 737 N HIS A 97 12.254 29.735 28.490 1.00 12.08 N ATOM 738 CA HIS A 97 12.584 29.830 29.925 1.00 9.02 C ATOM 739 C HIS A 97 11.380 29.956 30.812 1.00 13.07 C ATOM 740 O HIS A 97 11.245 29.326 31.905 1.00 23.05 O ATOM 741 CB HIS A 97 13.733 30.991 30.237 1.00 15.17 C ATOM 742 CG HIS A 97 15.073 30.648 29.690 1.00 18.61 C ATOM 743 ND1 HIS A 97 15.605 31.149 28.465 1.00 24.20 N ATOM 744 CD2 HIS A 97 15.885 29.851 30.214 1.00 13.33 C ATOM 745 CE1 HIS A 97 16.804 30.633 28.235 1.00 18.40 C ATOM 746 NE2 HIS A 97 16.974 29.819 29.339 1.00 8.02 N ATOM 747 N VAL A 98 10.504 30.672 30.310 1.00 17.39 N ATOM 748 CA VAL A 98 9.259 30.747 31.049 1.00 9.27 C ATOM 749 C VAL A 98 8.388 29.354 31.133 1.00 19.42 C ATOM 750 O VAL A 98 7.947 28.905 32.249 1.00 25.08 O ATOM 751 CB VAL A 98 8.470 31.817 30.452 1.00 15.01 C ATOM 752 CG1 VAL A 98 7.112 31.836 31.168 1.00 26.40 C ATOM 753 CG2 VAL A 98 9.316 33.236 30.515 1.00 4.89 C ATOM 754 N SER A 99 8.346 28.623 30.033 1.00 18.85 N ATOM 755 CA SER A 99 7.620 27.227 29.965 1.00 26.52 C ATOM 756 C SER A 99 8.160 26.285 30.953 1.00 31.44 C ATOM 757 O SER A 99 7.375 25.304 31.440 1.00 35.00 O ATOM 758 CB SER A 99 7.711 26.628 28.557 1.00 15.07 C ATOM 759 OG SER A 99 7.201 27.477 27.588 1.00 52.90 O ATOM 760 N LYS A 100 9.468 26.545 31.178 1.00 23.26 N ATOM 761 CA LYS A 100 10.162 25.649 32.001 1.00 14.97 C ATOM 762 C LYS A 100 10.194 25.991 33.486 1.00 16.04 C ATOM 763 O LYS A 100 10.729 25.271 34.295 1.00 31.32 O ATOM 764 CB LYS A 100 11.619 25.651 31.496 1.00 21.44 C ATOM 765 CG LYS A 100 11.652 24.888 30.163 1.00 30.85 C ATOM 766 CD LYS A 100 11.103 23.369 30.314 1.00 45.00 C ATOM 767 CE LYS A 100 11.211 22.592 29.000 1.00 40.69 C ATOM 768 NZ LYS A 100 10.784 21.135 29.207 0.00 0.00 N ATOM 769 N GLY A 101 9.604 27.020 33.840 1.00 19.91 N ATOM 770 CA GLY A 101 9.548 27.417 35.250 1.00 15.12 C ATOM 771 C GLY A 101 10.871 28.209 35.775 1.00 24.70 C ATOM 772 O GLY A 101 11.089 28.295 37.013 1.00 21.25 O ATOM 773 N VAL A 102 11.678 28.854 34.866 1.00 20.44 N ATOM 774 CA VAL A 102 12.936 29.744 35.227 1.00 11.09 C ATOM 775 C VAL A 102 12.672 31.157 35.607 1.00 19.12 C ATOM 776 O VAL A 102 11.933 31.744 34.870 1.00 24.51 O ATOM 777 CB VAL A 102 13.935 29.830 34.045 1.00 16.79 C ATOM 778 CG1 VAL A 102 15.275 30.780 34.318 1.00 13.70 C ATOM 779 CG2 VAL A 102 14.180 28.412 33.611 1.00 11.64 C ATOM 780 N ALA A 103 13.218 31.684 36.721 1.00 17.19 N ATOM 781 CA ALA A 103 13.118 33.059 37.168 1.00 3.00 C ATOM 782 C ALA A 103 14.496 33.955 37.168 1.00 12.11 C ATOM 783 O ALA A 103 15.547 33.436 36.992 1.00 11.35 O ATOM 784 CB ALA A 103 12.528 33.024 38.589 1.00 7.45 C ATOM 785 N ASP A 104 14.479 35.256 37.323 1.00 13.09 N ATOM 786 CA ASP A 104 15.710 36.264 37.365 1.00 9.85 C ATOM 787 C ASP A 104 16.734 35.945 38.399 1.00 17.47 C ATOM 788 O ASP A 104 17.976 36.327 38.206 1.00 20.16 O ATOM 789 CB ASP A 104 15.344 37.659 37.715 1.00 15.48 C ATOM 790 CG ASP A 104 14.493 38.133 36.598 1.00 33.58 C ATOM 791 OD1 ASP A 104 14.269 39.334 36.598 1.00 45.38 O ATOM 792 OD2 ASP A 104 14.314 37.461 35.535 1.00 44.39 O ATOM 793 N ALA A 105 16.238 35.349 39.503 1.00 11.49 N ATOM 794 CA ALA A 105 17.152 35.094 40.594 1.00 13.10 C ATOM 795 C ALA A 105 17.885 33.893 40.327 1.00 11.29 C ATOM 796 O ALA A 105 18.884 33.733 41.037 1.00 17.85 O ATOM 797 CB ALA A 105 16.428 34.929 41.957 1.00 4.58 C ATOM 798 N HIS A 106 17.502 33.178 39.243 1.00 15.55 N ATOM 799 CA HIS A 106 18.221 32.084 38.792 1.00 15.21 C ATOM 800 C HIS A 106 19.564 32.623 38.128 1.00 20.42 C ATOM 801 O HIS A 106 20.500 31.919 38.142 1.00 21.99 O ATOM 802 CB HIS A 106 17.376 31.145 37.784 1.00 5.00 C ATOM 803 CG HIS A 106 16.339 30.058 38.462 1.00 12.37 C ATOM 804 ND1 HIS A 106 14.947 29.983 38.237 1.00 17.57 N ATOM 805 CD2 HIS A 106 16.543 29.043 39.281 1.00 21.99 C ATOM 806 CE1 HIS A 106 14.272 28.870 38.960 1.00 16.61 C ATOM 807 NE2 HIS A 106 15.283 28.284 39.618 1.00 17.66 N ATOM 808 N PHE A 107 19.579 33.750 37.442 1.00 15.92 N ATOM 809 CA PHE A 107 20.746 34.370 36.629 1.00 22.89 C ATOM 810 C PHE A 107 22.154 34.523 37.269 1.00 9.80 C ATOM 811 O PHE A 107 23.104 34.162 36.607 1.00 11.13 O ATOM 812 CB PHE A 107 20.498 35.634 35.829 1.00 22.22 C ATOM 813 CG PHE A 107 19.526 35.267 34.637 1.00 15.38 C ATOM 814 CD1 PHE A 107 18.145 35.036 34.833 1.00 16.84 C ATOM 815 CD2 PHE A 107 20.042 35.148 33.371 1.00 13.74 C ATOM 816 CE1 PHE A 107 17.270 34.672 33.764 1.00 18.43 C ATOM 817 CE2 PHE A 107 19.177 34.785 32.296 1.00 14.15 C ATOM 818 CZ PHE A 107 17.786 34.542 32.492 1.00 4.71 C ATOM 819 N PRO A 108 22.326 34.936 38.523 1.00 13.39 N ATOM 820 CA PRO A 108 23.647 34.989 39.188 1.00 8.82 C ATOM 821 C PRO A 108 24.105 33.612 39.374 1.00 21.11 C ATOM 822 O PRO A 108 25.350 33.553 39.436 1.00 11.00 O ATOM 823 CB PRO A 108 23.571 35.705 40.543 1.00 16.95 C ATOM 824 CG PRO A 108 22.214 36.233 40.577 1.00 5.47 C ATOM 825 CD PRO A 108 21.408 35.617 39.360 1.00 5.04 C ATOM 826 N VAL A 109 23.145 32.534 39.367 1.00 8.28 N ATOM 827 CA VAL A 109 23.479 31.154 39.479 1.00 3.51 C ATOM 828 C VAL A 109 24.234 30.745 38.262 1.00 9.35 C ATOM 829 O VAL A 109 25.352 30.333 38.413 1.00 15.77 O ATOM 830 CB VAL A 109 22.208 30.096 39.698 1.00 17.33 C ATOM 831 CG1 VAL A 109 22.532 28.640 39.648 1.00 14.43 C ATOM 832 CG2 VAL A 109 21.476 30.367 41.000 1.00 7.51 C ATOM 833 N VAL A 110 23.673 30.923 37.097 1.00 8.97 N ATOM 834 CA VAL A 110 24.328 30.593 35.850 1.00 14.80 C ATOM 835 C VAL A 110 25.636 31.565 35.585 1.00 12.13 C ATOM 836 O VAL A 110 26.656 31.137 35.119 1.00 10.11 O ATOM 837 CB VAL A 110 23.335 30.491 34.653 1.00 16.03 C ATOM 838 CG1 VAL A 110 24.038 30.416 33.288 1.00 12.84 C ATOM 839 CG2 VAL A 110 22.183 29.285 34.811 1.00 4.71 C ATOM 840 N LYS A 111 25.688 32.780 36.092 1.00 11.85 N ATOM 841 CA LYS A 111 26.922 33.779 35.985 1.00 5.51 C ATOM 842 C LYS A 111 28.141 33.358 36.691 1.00 7.57 C ATOM 843 O LYS A 111 29.210 33.284 36.046 1.00 8.65 O ATOM 844 CB LYS A 111 26.650 35.141 36.547 1.00 4.78 C ATOM 845 CG LYS A 111 27.863 36.282 36.419 1.00 24.40 C ATOM 846 CD LYS A 111 27.418 37.607 36.884 1.00 17.21 C ATOM 847 CE LYS A 111 28.550 38.825 36.858 1.00 23.05 C ATOM 848 NZ LYS A 111 27.951 40.024 37.223 1.00 30.86 N ATOM 849 N GLU A 112 27.963 33.054 37.961 1.00 9.88 N ATOM 850 CA GLU A 112 29.063 32.626 38.730 1.00 13.80 C ATOM 851 C GLU A 112 29.489 31.337 38.186 1.00 7.90 C ATOM 852 O GLU A 112 30.724 31.235 38.126 1.00 12.49 O ATOM 853 CB GLU A 112 28.701 32.462 40.220 1.00 8.39 C ATOM 854 CG GLU A 112 28.447 33.812 40.842 1.00 21.02 C ATOM 855 CD GLU A 112 29.699 34.879 40.644 1.00 35.06 C ATOM 856 OE1 GLU A 112 30.823 34.685 41.105 1.00 20.79 O ATOM 857 OE2 GLU A 112 29.585 36.019 40.164 1.00 19.16 O ATOM 858 N ALA A 113 28.503 30.448 37.706 1.00 11.79 N ATOM 859 CA ALA A 113 28.782 29.155 37.183 1.00 4.79 C ATOM 860 C ALA A 113 29.650 29.349 35.930 1.00 3.00 C ATOM 861 O ALA A 113 30.616 28.693 35.799 1.00 9.94 O ATOM 862 CB ALA A 113 27.457 28.182 36.910 1.00 7.13 C ATOM 863 N ILE A 114 29.388 30.318 35.119 1.00 11.68 N ATOM 864 CA ILE A 114 30.188 30.657 33.898 1.00 7.19 C ATOM 865 C ILE A 114 31.620 31.345 34.222 1.00 11.99 C ATOM 866 O ILE A 114 32.616 30.990 33.626 1.00 11.73 O ATOM 867 CB ILE A 114 29.486 31.547 32.937 1.00 8.54 C ATOM 868 CG1 ILE A 114 28.188 30.748 32.332 1.00 3.90 C ATOM 869 CG2 ILE A 114 30.435 32.198 31.819 1.00 7.81 C ATOM 870 CD1 ILE A 114 27.500 31.613 31.354 1.00 7.47 C ATOM 871 N LEU A 115 31.719 32.242 35.197 1.00 11.88 N ATOM 872 CA LEU A 115 33.044 32.982 35.588 1.00 11.89 C ATOM 873 C LEU A 115 33.941 32.046 36.201 1.00 5.56 C ATOM 874 O LEU A 115 35.150 32.122 35.830 1.00 16.57 O ATOM 875 CB LEU A 115 32.906 34.151 36.561 1.00 10.23 C ATOM 876 CG LEU A 115 32.284 35.311 35.902 1.00 16.19 C ATOM 877 CD1 LEU A 115 32.015 36.377 36.936 1.00 12.68 C ATOM 878 CD2 LEU A 115 33.150 35.983 34.734 1.00 6.62 C ATOM 879 N LYS A 116 33.322 31.103 36.999 1.00 8.70 N ATOM 880 CA LYS A 116 34.057 30.091 37.592 1.00 5.54 C ATOM 881 C LYS A 116 34.488 29.125 36.552 1.00 6.41 C ATOM 882 O LYS A 116 35.670 28.844 36.592 1.00 14.73 O ATOM 883 CB LYS A 116 33.226 29.294 38.710 1.00 7.23 C ATOM 884 CG LYS A 116 33.125 30.178 39.958 1.00 45.14 C ATOM 885 CD LYS A 116 32.169 29.452 41.032 1.00 48.36 C ATOM 886 CE LYS A 116 32.144 30.321 42.303 1.00 50.44 C ATOM 887 NZ LYS A 116 31.818 31.666 41.967 1.00 60.14 N ATOM 888 N THR A 117 33.589 28.711 35.613 1.00 10.75 N ATOM 889 CA THR A 117 33.880 27.808 34.530 1.00 3.67 C ATOM 890 C THR A 117 35.081 28.444 33.689 1.00 12.37 C ATOM 891 O THR A 117 36.055 27.811 33.501 1.00 21.62 O ATOM 892 CB THR A 117 32.641 27.374 33.619 1.00 12.80 C ATOM 893 OG1 THR A 117 31.574 26.597 34.369 1.00 10.32 O ATOM 894 CG2 THR A 117 32.976 26.530 32.404 1.00 8.11 C ATOM 895 N ILE A 118 35.048 29.687 33.281 1.00 15.01 N ATOM 896 CA ILE A 118 36.167 30.413 32.496 1.00 9.37 C ATOM 897 C ILE A 118 37.482 30.639 33.293 1.00 13.28 C ATOM 898 O ILE A 118 38.574 30.484 32.736 1.00 13.37 O ATOM 899 CB ILE A 118 35.812 31.762 31.966 1.00 14.31 C ATOM 900 CG1 ILE A 118 34.696 31.508 30.891 1.00 16.78 C ATOM 901 CG2 ILE A 118 37.064 32.704 31.433 1.00 11.85 C ATOM 902 CD1 ILE A 118 35.161 30.787 29.649 1.00 12.77 C ATOM 903 N LYS A 119 37.347 30.754 34.597 1.00 12.84 N ATOM 904 CA LYS A 119 38.557 30.891 35.445 1.00 13.32 C ATOM 905 C LYS A 119 39.231 29.627 35.438 1.00 10.31 C ATOM 906 O LYS A 119 40.493 29.726 35.301 1.00 13.50 O ATOM 907 CB LYS A 119 38.267 31.289 36.892 1.00 23.06 C ATOM 908 CG LYS A 119 39.594 31.722 37.671 1.00 23.61 C ATOM 909 CD LYS A 119 39.356 32.136 39.123 1.00 31.56 C ATOM 910 CE LYS A 119 38.475 33.265 39.217 0.00 0.00 C ATOM 911 NZ LYS A 119 38.357 33.674 40.617 0.00 0.00 N ATOM 912 N GLU A 120 38.393 28.483 35.361 1.00 14.08 N ATOM 913 CA GLU A 120 38.915 27.196 35.266 1.00 13.32 C ATOM 914 C GLU A 120 39.451 26.927 33.882 1.00 16.57 C ATOM 915 O GLU A 120 40.511 26.406 33.777 1.00 27.38 O ATOM 916 CB GLU A 120 37.850 26.005 35.727 1.00 18.43 C ATOM 917 CG GLU A 120 37.417 26.193 37.186 1.00 43.35 C ATOM 918 CD GLU A 120 36.336 25.009 37.576 1.00 50.07 C ATOM 919 OE1 GLU A 120 35.911 24.904 38.761 1.00 43.18 O ATOM 920 OE2 GLU A 120 36.139 23.990 36.827 1.00 33.47 O ATOM 921 N VAL A 121 38.771 27.313 32.868 1.00 16.87 N ATOM 922 CA VAL A 121 39.193 27.159 31.479 1.00 5.07 C ATOM 923 C VAL A 121 40.614 27.905 31.182 1.00 8.45 C ATOM 924 O VAL A 121 41.455 27.300 30.595 1.00 16.73 O ATOM 925 CB VAL A 121 38.152 27.616 30.514 1.00 7.52 C ATOM 926 CG1 VAL A 121 38.669 27.760 29.067 1.00 6.84 C ATOM 927 CG2 VAL A 121 36.780 26.668 30.589 1.00 11.25 C ATOM 928 N VAL A 122 40.890 29.179 31.554 1.00 17.69 N ATOM 929 CA VAL A 122 42.172 30.008 31.156 1.00 3.64 C ATOM 930 C VAL A 122 43.353 29.900 32.086 1.00 12.52 C ATOM 931 O VAL A 122 44.546 30.242 31.673 1.00 20.01 O ATOM 932 CB VAL A 122 42.003 31.497 30.931 1.00 4.66 C ATOM 933 CG1 VAL A 122 40.952 31.610 29.829 1.00 5.55 C ATOM 934 CG2 VAL A 122 41.631 32.176 32.231 1.00 6.37 C ATOM 935 N GLY A 123 43.007 29.339 33.254 1.00 15.67 N ATOM 936 CA GLY A 123 44.003 29.139 34.278 1.00 21.70 C ATOM 937 C GLY A 123 44.963 30.436 34.601 1.00 24.17 C ATOM 938 O GLY A 123 44.489 31.481 34.923 1.00 16.12 O ATOM 939 N ALA A 124 46.263 30.352 34.548 1.00 21.19 N ATOM 940 CA ALA A 124 47.330 31.465 34.938 1.00 23.63 C ATOM 941 C ALA A 124 47.351 32.739 34.104 1.00 16.82 C ATOM 942 O ALA A 124 48.081 33.815 34.469 1.00 23.00 O ATOM 943 CB ALA A 124 48.739 31.038 34.861 1.00 20.35 C ATOM 944 N LYS A 125 46.604 32.604 33.012 1.00 13.37 N ATOM 945 CA LYS A 125 46.542 33.766 32.135 1.00 21.11 C ATOM 946 C LYS A 125 45.513 34.623 32.623 1.00 22.78 C ATOM 947 O LYS A 125 45.260 35.600 31.933 1.00 16.04 O ATOM 948 CB LYS A 125 46.201 33.345 30.677 1.00 23.79 C ATOM 949 CG LYS A 125 47.275 32.593 30.044 1.00 37.08 C ATOM 950 CD LYS A 125 47.067 32.415 28.525 1.00 30.25 C ATOM 951 CE LYS A 125 45.659 31.642 28.163 1.00 40.08 C ATOM 952 NZ LYS A 125 45.495 30.232 28.633 1.00 37.75 N ATOM 953 N TRP A 126 44.875 34.209 33.728 1.00 15.25 N ATOM 954 CA TRP A 126 43.795 34.902 34.243 1.00 10.05 C ATOM 955 C TRP A 126 44.334 36.351 34.678 1.00 15.10 C ATOM 956 O TRP A 126 45.490 36.610 35.194 1.00 17.44 O ATOM 957 CB TRP A 126 43.076 34.083 35.414 1.00 11.41 C ATOM 958 CG TRP A 126 41.755 34.590 35.802 1.00 23.10 C ATOM 959 CD1 TRP A 126 40.534 34.348 35.210 1.00 20.11 C ATOM 960 CD2 TRP A 126 41.605 35.454 36.869 1.00 19.80 C ATOM 961 NE1 TRP A 126 39.624 35.042 35.897 1.00 26.61 N ATOM 962 CE2 TRP A 126 40.252 35.682 36.863 1.00 14.57 C ATOM 963 CE3 TRP A 126 42.531 36.051 37.800 1.00 29.86 C ATOM 964 CZ2 TRP A 126 39.766 36.513 37.788 1.00 35.96 C ATOM 965 CZ3 TRP A 126 42.043 36.897 38.726 1.00 43.53 C ATOM 966 CH2 TRP A 126 40.701 37.118 38.722 1.00 36.89 C ATOM 967 N SER A 127 43.574 37.283 34.396 1.00 19.52 N ATOM 968 CA SER A 127 43.918 38.703 34.827 1.00 18.26 C ATOM 969 C SER A 127 42.686 39.332 35.239 1.00 20.34 C ATOM 970 O SER A 127 41.521 38.813 34.863 1.00 11.54 O ATOM 971 CB SER A 127 44.668 39.600 33.728 1.00 7.61 C ATOM 972 OG SER A 127 43.745 39.769 32.671 1.00 11.79 O ATOM 973 N GLU A 128 42.955 40.457 35.927 1.00 17.36 N ATOM 974 CA GLU A 128 41.886 41.225 36.324 1.00 18.05 C ATOM 975 C GLU A 128 41.227 41.754 35.108 1.00 5.80 C ATOM 976 O GLU A 128 39.966 41.690 35.069 1.00 15.51 O ATOM 977 CB GLU A 128 42.446 42.427 37.231 1.00 17.95 C ATOM 978 CG GLU A 128 42.926 41.947 38.587 1.00 56.84 C ATOM 979 CD GLU A 128 43.475 43.182 39.429 0.00 0.00 C ATOM 980 OE1 GLU A 128 44.481 43.146 40.175 0.00 0.00 O ATOM 981 OE2 GLU A 128 42.763 44.097 39.607 0.00 0.00 O ATOM 982 N GLU A 129 42.071 42.205 34.145 1.00 8.94 N ATOM 983 CA GLU A 129 41.628 42.706 32.872 1.00 6.46 C ATOM 984 C GLU A 129 40.614 41.647 32.160 1.00 9.71 C ATOM 985 O GLU A 129 39.596 41.977 31.591 1.00 14.81 O ATOM 986 CB GLU A 129 42.867 43.076 31.958 1.00 10.40 C ATOM 987 CG GLU A 129 42.515 43.792 30.672 1.00 27.50 C ATOM 988 CD GLU A 129 42.534 45.294 30.950 1.00 44.10 C ATOM 989 OE1 GLU A 129 43.194 46.146 30.180 1.00 45.82 O ATOM 990 OE2 GLU A 129 41.763 45.685 31.812 1.00 37.82 O ATOM 991 N LEU A 130 40.893 40.408 32.205 1.00 22.22 N ATOM 992 CA LEU A 130 40.005 39.279 31.578 1.00 14.02 C ATOM 993 C LEU A 130 38.665 39.006 32.331 1.00 6.71 C ATOM 994 O LEU A 130 37.560 38.784 31.714 1.00 14.49 O ATOM 995 CB LEU A 130 40.719 38.016 31.614 1.00 13.39 C ATOM 996 CG LEU A 130 39.884 36.725 31.021 1.00 9.55 C ATOM 997 CD1 LEU A 130 39.616 36.854 29.514 1.00 21.25 C ATOM 998 CD2 LEU A 130 40.543 35.467 31.323 1.00 21.09 C ATOM 999 N ASN A 131 38.781 39.084 33.638 1.00 22.47 N ATOM 1000 CA ASN A 131 37.611 38.838 34.526 1.00 8.58 C ATOM 1001 C ASN A 131 36.675 39.876 34.318 1.00 8.90 C ATOM 1002 O ASN A 131 35.426 39.500 34.174 1.00 11.69 O ATOM 1003 CB ASN A 131 38.079 38.937 35.988 1.00 10.26 C ATOM 1004 CG ASN A 131 36.829 38.639 36.873 1.00 25.01 C ATOM 1005 OD1 ASN A 131 36.433 39.567 37.541 1.00 28.22 O ATOM 1006 ND2 ASN A 131 36.190 37.391 36.803 1.00 22.64 N ATOM 1007 N SER A 132 37.301 41.128 34.201 1.00 12.86 N ATOM 1008 CA SER A 132 36.560 42.254 33.934 1.00 8.09 C ATOM 1009 C SER A 132 35.881 42.149 32.566 1.00 6.40 C ATOM 1010 O SER A 132 34.691 42.387 32.454 1.00 14.95 O ATOM 1011 CB SER A 132 37.476 43.633 34.076 1.00 3.00 C ATOM 1012 OG ASER A 132 38.374 43.892 32.956 1.00 17.00 O ATOM 1013 OG BSER A 132 38.192 43.663 35.316 1.00 6.93 O ATOM 1014 OG CSER A 132 37.030 44.589 33.174 1.00 3.06 O ATOM 1015 N ALA A 133 36.589 41.740 31.579 1.00 12.35 N ATOM 1016 CA ALA A 133 36.030 41.570 30.220 1.00 13.38 C ATOM 1017 C ALA A 133 34.754 40.510 30.114 1.00 18.59 C ATOM 1018 O ALA A 133 33.710 40.806 29.558 1.00 16.27 O ATOM 1019 CB ALA A 133 37.112 41.245 29.230 1.00 9.44 C ATOM 1020 N TRP A 134 34.792 39.345 30.722 1.00 16.15 N ATOM 1021 CA TRP A 134 33.600 38.288 30.730 1.00 5.19 C ATOM 1022 C TRP A 134 32.471 38.690 31.592 1.00 15.96 C ATOM 1023 O TRP A 134 31.260 38.275 31.282 1.00 17.22 O ATOM 1024 CB TRP A 134 33.929 36.920 31.237 1.00 8.43 C ATOM 1025 CG TRP A 134 34.588 36.103 30.185 1.00 8.00 C ATOM 1026 CD1 TRP A 134 35.907 36.074 29.954 1.00 3.92 C ATOM 1027 CD2 TRP A 134 33.894 35.172 29.284 1.00 12.72 C ATOM 1028 NE1 TRP A 134 36.045 35.163 28.911 1.00 9.43 N ATOM 1029 CE2 TRP A 134 34.868 34.640 28.521 1.00 12.49 C ATOM 1030 CE3 TRP A 134 32.522 34.764 29.080 1.00 24.77 C ATOM 1031 CZ2 TRP A 134 34.521 33.694 27.519 1.00 11.55 C ATOM 1032 CZ3 TRP A 134 32.171 33.813 28.069 1.00 9.97 C ATOM 1033 CH2 TRP A 134 33.141 33.298 27.308 1.00 14.95 C ATOM 1034 N THR A 135 32.857 39.490 32.618 1.00 14.77 N ATOM 1035 CA THR A 135 31.857 39.944 33.524 1.00 17.56 C ATOM 1036 C THR A 135 31.036 40.919 32.853 1.00 9.04 C ATOM 1037 O THR A 135 29.767 40.685 32.892 1.00 15.10 O ATOM 1038 CB THR A 135 32.533 40.581 34.803 1.00 5.05 C ATOM 1039 OG1 THR A 135 33.099 39.572 35.537 1.00 11.97 O ATOM 1040 CG2 THR A 135 31.535 41.189 35.705 1.00 18.64 C ATOM 1041 N ILE A 136 31.731 41.883 32.139 1.00 8.03 N ATOM 1042 CA ILE A 136 31.055 42.841 31.394 1.00 5.18 C ATOM 1043 C ILE A 136 30.130 42.145 30.314 1.00 5.36 C ATOM 1044 O ILE A 136 28.943 42.400 30.215 1.00 20.73 O ATOM 1045 CB ILE A 136 32.093 43.953 30.746 1.00 20.69 C ATOM 1046 CG1 ILE A 136 33.023 44.756 31.789 1.00 27.95 C ATOM 1047 CG2 ILE A 136 31.413 44.915 29.862 1.00 25.26 C ATOM 1048 CD1 ILE A 136 34.237 45.638 31.119 1.00 19.11 C ATOM 1049 N ALA A 137 30.656 41.288 29.556 1.00 10.19 N ATOM 1050 CA ALA A 137 29.882 40.590 28.446 1.00 17.51 C ATOM 1051 C ALA A 137 28.594 39.685 28.913 1.00 16.88 C ATOM 1052 O ALA A 137 27.511 39.628 28.260 1.00 9.07 O ATOM 1053 CB ALA A 137 30.770 39.744 27.654 1.00 10.05 C ATOM 1054 N TYR A 138 28.694 39.090 30.076 1.00 9.80 N ATOM 1055 CA TYR A 138 27.507 38.276 30.674 1.00 7.71 C ATOM 1056 C TYR A 138 26.476 39.166 31.101 1.00 12.48 C ATOM 1057 O TYR A 138 25.287 38.892 30.671 1.00 18.52 O ATOM 1058 CB TYR A 138 27.881 37.429 31.870 1.00 8.15 C ATOM 1059 CG TYR A 138 26.642 36.446 32.377 1.00 15.31 C ATOM 1060 CD1 TYR A 138 25.780 36.871 33.305 1.00 14.76 C ATOM 1061 CD2 TYR A 138 26.382 35.147 31.885 1.00 8.05 C ATOM 1062 CE1 TYR A 138 24.656 36.005 33.745 1.00 5.46 C ATOM 1063 CE2 TYR A 138 25.264 34.266 32.331 1.00 8.67 C ATOM 1064 CZ TYR A 138 24.404 34.699 33.262 1.00 6.25 C ATOM 1065 OH TYR A 138 23.259 33.785 33.753 1.00 8.67 O ATOM 1066 N ASP A 139 26.923 40.188 31.911 1.00 12.89 N ATOM 1067 CA ASP A 139 26.036 41.121 32.421 1.00 12.18 C ATOM 1068 C ASP A 139 25.262 41.739 31.331 1.00 5.17 C ATOM 1069 O ASP A 139 24.025 41.786 31.481 1.00 8.92 O ATOM 1070 CB ASP A 139 26.850 42.295 33.202 1.00 8.62 C ATOM 1071 CG ASP A 139 27.175 41.761 34.567 1.00 20.42 C ATOM 1072 OD1 ASP A 139 26.662 40.573 34.868 1.00 14.26 O ATOM 1073 OD2 ASP A 139 28.206 42.320 35.185 1.00 17.95 O ATOM 1074 N GLU A 140 25.974 42.196 30.286 1.00 4.63 N ATOM 1075 CA GLU A 140 25.357 42.834 29.172 1.00 17.02 C ATOM 1076 C GLU A 140 24.341 41.831 28.401 1.00 15.88 C ATOM 1077 O GLU A 140 23.225 42.147 28.048 1.00 9.70 O ATOM 1078 CB GLU A 140 26.445 43.546 28.209 1.00 4.43 C ATOM 1079 CG GLU A 140 27.425 44.694 28.889 1.00 17.12 C ATOM 1080 CD GLU A 140 26.670 45.788 29.448 1.00 35.02 C ATOM 1081 OE1 GLU A 140 25.605 46.034 28.900 1.00 16.04 O ATOM 1082 OE2 GLU A 140 27.216 46.589 30.329 1.00 18.34 O ATOM 1083 N LEU A 141 24.677 40.624 28.239 1.00 10.24 N ATOM 1084 CA LEU A 141 23.733 39.584 27.570 1.00 3.00 C ATOM 1085 C LEU A 141 22.485 39.155 28.440 1.00 16.24 C ATOM 1086 O LEU A 141 21.318 38.966 27.935 1.00 19.37 O ATOM 1087 CB LEU A 141 24.434 38.355 27.210 1.00 13.54 C ATOM 1088 CG LEU A 141 23.506 37.246 26.415 1.00 11.54 C ATOM 1089 CD1 LEU A 141 23.070 37.776 25.062 1.00 9.02 C ATOM 1090 CD2 LEU A 141 24.156 35.960 26.225 1.00 6.20 C ATOM 1091 N ALA A 142 22.734 39.120 29.730 1.00 13.91 N ATOM 1092 CA ALA A 142 21.665 38.716 30.709 1.00 13.86 C ATOM 1093 C ALA A 142 20.671 39.721 30.791 1.00 21.31 C ATOM 1094 O ALA A 142 19.425 39.282 30.814 1.00 14.30 O ATOM 1095 CB ALA A 142 22.251 38.509 32.105 1.00 7.41 C ATOM 1096 N ILE A 143 21.206 41.012 30.700 1.00 12.38 N ATOM 1097 CA ILE A 143 20.338 42.077 30.690 1.00 9.24 C ATOM 1098 C ILE A 143 19.334 41.897 29.533 1.00 17.13 C ATOM 1099 O ILE A 143 18.107 41.972 29.737 1.00 14.42 O ATOM 1100 CB ILE A 143 21.210 43.493 30.632 1.00 9.83 C ATOM 1101 CG1 ILE A 143 21.989 43.830 31.942 1.00 6.34 C ATOM 1102 CG2 ILE A 143 20.391 44.625 30.272 1.00 23.04 C ATOM 1103 CD1 ILE A 143 23.039 45.124 31.807 1.00 16.33 C ATOM 1104 N VAL A 144 19.821 41.510 28.399 1.00 13.56 N ATOM 1105 CA VAL A 144 18.992 41.274 27.188 1.00 19.41 C ATOM 1106 C VAL A 144 17.910 40.028 27.300 1.00 20.37 C ATOM 1107 O VAL A 144 16.705 40.110 27.002 1.00 18.78 O ATOM 1108 CB VAL A 144 19.890 41.160 25.953 1.00 27.67 C ATOM 1109 CG1 VAL A 144 19.051 40.784 24.678 1.00 22.50 C ATOM 1110 CG2 VAL A 144 20.925 42.457 25.744 1.00 23.82 C ATOM 1111 N ILE A 145 18.309 38.938 27.795 1.00 16.29 N ATOM 1112 CA ILE A 145 17.341 37.688 27.951 1.00 24.90 C ATOM 1113 C ILE A 145 16.262 37.797 29.006 1.00 28.54 C ATOM 1114 O ILE A 145 15.039 37.419 28.721 1.00 24.62 O ATOM 1115 CB ILE A 145 18.064 36.452 28.193 1.00 32.02 C ATOM 1116 CG1 ILE A 145 18.995 36.239 27.003 1.00 19.27 C ATOM 1117 CG2 ILE A 145 17.052 35.157 28.477 1.00 22.13 C ATOM 1118 CD1 ILE A 145 19.823 35.088 27.259 1.00 21.94 C ATOM 1119 N LYS A 146 16.685 38.433 30.119 1.00 10.58 N ATOM 1120 CA LYS A 146 15.746 38.703 31.174 1.00 8.11 C ATOM 1121 C LYS A 146 14.749 39.594 30.670 1.00 24.69 C ATOM 1122 O LYS A 146 13.545 39.397 31.072 1.00 31.76 O ATOM 1123 CB LYS A 146 16.530 39.377 32.389 1.00 16.46 C ATOM 1124 CG LYS A 146 17.015 38.314 33.306 1.00 8.31 C ATOM 1125 CD LYS A 146 18.376 38.820 33.995 1.00 6.26 C ATOM 1126 CE LYS A 146 18.353 40.054 34.898 1.00 21.78 C ATOM 1127 NZ LYS A 146 19.724 40.497 35.425 1.00 33.82 N ATOM 1128 N LYS A 147 15.213 40.469 29.743 1.00 20.85 N ATOM 1129 CA LYS A 147 14.341 41.350 29.141 1.00 27.44 C ATOM 1130 C LYS A 147 13.239 40.547 28.279 1.00 15.85 C ATOM 1131 O LYS A 147 12.015 40.662 28.448 1.00 28.77 O ATOM 1132 CB LYS A 147 15.196 42.466 28.306 1.00 36.29 C ATOM 1133 CG LYS A 147 14.418 43.631 27.952 1.00 41.80 C ATOM 1134 CD LYS A 147 15.237 44.681 27.022 0.00 0.00 C ATOM 1135 CE LYS A 147 15.548 44.045 25.678 0.00 0.00 C ATOM 1136 NZ LYS A 147 16.253 45.079 24.776 0.00 0.00 N ATOM 1137 N GLU A 148 13.659 39.650 27.482 1.00 16.91 N ATOM 1138 CA GLU A 148 12.710 38.735 26.659 1.00 13.94 C ATOM 1139 C GLU A 148 11.766 37.706 27.480 1.00 31.55 C ATOM 1140 O GLU A 148 10.655 37.168 26.989 1.00 31.27 O ATOM 1141 CB GLU A 148 13.483 37.983 25.652 1.00 10.50 C ATOM 1142 CG GLU A 148 14.491 38.965 24.819 1.00 28.92 C ATOM 1143 CD GLU A 148 13.740 39.990 24.133 1.00 46.94 C ATOM 1144 OE1 GLU A 148 12.679 39.596 23.479 1.00 41.46 O ATOM 1145 OE2 GLU A 148 14.123 41.237 24.293 1.00 47.75 O ATOM 1146 N MET A 149 12.200 37.452 28.687 1.00 26.40 N ATOM 1147 CA MET A 149 11.388 36.500 29.599 1.00 20.95 C ATOM 1148 C MET A 149 10.232 37.123 30.198 1.00 24.32 C ATOM 1149 O MET A 149 9.062 36.452 30.254 1.00 26.22 O ATOM 1150 CB MET A 149 12.257 36.110 30.761 1.00 21.07 C ATOM 1151 CG MET A 149 13.162 35.070 30.350 1.00 12.99 C ATOM 1152 SD MET A 149 14.330 34.716 31.620 1.00 20.73 S ATOM 1153 CE MET A 149 13.149 34.296 32.964 1.00 12.91 C ATOM 1154 N ASP A 150 10.580 38.351 30.675 1.00 35.85 N ATOM 1155 CA ASP A 150 9.569 39.081 31.272 1.00 56.08 C ATOM 1156 C ASP A 150 8.526 39.333 30.232 1.00 50.15 C ATOM 1157 O ASP A 150 7.283 39.081 30.496 1.00 48.77 O ATOM 1158 CB ASP A 150 10.239 40.433 31.883 1.00 53.23 C ATOM 1159 CG ASP A 150 10.947 40.148 33.181 1.00 51.51 C ATOM 1160 OD1 ASP A 150 11.272 38.997 33.369 0.00 0.00 O ATOM 1161 OD2 ASP A 150 10.855 40.892 34.178 0.00 0.00 O ATOM 1162 N ASP A 151 9.022 39.562 29.025 1.00 40.25 N ATOM 1163 CA ASP A 151 8.133 39.654 27.874 1.00 47.65 C ATOM 1164 C ASP A 151 7.338 38.293 27.455 1.00 62.47 C ATOM 1165 O ASP A 151 6.188 38.248 26.934 1.00 59.32 O ATOM 1166 CB ASP A 151 8.924 40.343 26.674 1.00 56.06 C ATOM 1167 CG ASP A 151 9.187 41.869 26.908 1.00 49.88 C ATOM 1168 OD1 ASP A 151 9.727 42.315 27.987 0.00 0.00 O ATOM 1169 OD2 ASP A 151 8.485 42.598 26.278 0.00 0.00 O ATOM 1170 N ALA A 152 7.876 37.209 27.748 1.00 52.70 N ATOM 1171 CA ALA A 152 7.139 35.857 27.430 1.00 52.64 C ATOM 1172 C ALA A 152 6.156 35.310 28.535 1.00 61.67 C ATOM 1173 O ALA A 152 5.421 34.178 28.402 1.00 53.59 O ATOM 1174 CB ALA A 152 8.113 34.833 27.175 1.00 48.19 C ATOM 1175 N ALA A 153 6.219 36.069 29.621 1.00 52.71 N ATOM 1176 CA ALA A 153 5.454 35.632 30.841 1.00 58.79 C ATOM 1177 C ALA A 153 4.030 36.002 30.879 1.00 55.43 C ATOM 1178 O ALA A 153 3.848 37.119 31.365 0.00 0.00 O ATOM 1179 CB ALA A 153 6.242 36.217 32.088 1.00 55.90 C ATOM 1180 OXT ALA A 153 3.098 35.330 30.205 0.00 0.00 O TER 1181 ALA A 153 HETATM 1182 C CYN 101 20.670 27.507 30.303 1.00 3.00 C HETATM 1183 N CYN 101 21.140 26.671 30.810 1.00 15.44 N HETATM 1184 FE HEM 1 18.756 28.667 29.850 1.00 13.96 FE HETATM 1185 CHA HEM 1 16.978 26.198 27.795 1.00 14.14 C HETATM 1186 CHB HEM 1 20.622 29.959 27.024 1.00 10.76 C HETATM 1187 CHC HEM 1 20.229 31.442 31.607 1.00 6.71 C HETATM 1188 CHD HEM 1 17.178 27.258 32.523 1.00 14.08 C HETATM 1189 NA HEM 1 18.787 28.185 27.780 1.00 19.07 N HETATM 1190 C1A HEM 1 17.961 27.126 27.166 1.00 8.47 C HETATM 1191 C2A HEM 1 18.345 27.095 25.762 1.00 11.64 C HETATM 1192 C3A HEM 1 19.395 28.106 25.561 1.00 16.31 C HETATM 1193 C4A HEM 1 19.662 28.815 26.828 1.00 25.21 C HETATM 1194 CMA HEM 1 20.171 28.487 24.252 1.00 19.79 C HETATM 1195 CAA HEM 1 17.665 26.083 24.721 1.00 26.51 C HETATM 1196 CBA HEM 1 16.633 26.748 23.919 1.00 50.52 C HETATM 1197 CGA HEM 1 16.049 25.793 22.808 1.00 61.71 C HETATM 1198 O1A HEM 1 14.820 25.279 22.843 1.00 59.48 O HETATM 1199 O2A HEM 1 16.726 25.692 21.763 1.00 58.37 O HETATM 1200 NB HEM 1 20.142 30.436 29.364 1.00 13.65 N HETATM 1201 C1B HEM 1 20.831 30.720 28.185 1.00 14.24 C HETATM 1202 C2B HEM 1 21.802 31.953 28.341 1.00 17.46 C HETATM 1203 C3B HEM 1 21.649 32.420 29.604 1.00 13.10 C HETATM 1204 C4B HEM 1 20.618 31.432 30.265 1.00 9.04 C HETATM 1205 CMB HEM 1 22.779 32.554 27.228 1.00 6.41 C HETATM 1206 CAB HEM 1 22.424 33.694 30.285 1.00 13.72 C HETATM 1207 CBB HEM 1 22.896 34.809 29.594 1.00 6.14 C HETATM 1208 NC HEM 1 18.688 29.269 31.713 1.00 10.15 N HETATM 1209 C1C HEM 1 19.372 30.428 32.284 1.00 14.53 C HETATM 1210 C2C HEM 1 19.090 30.384 33.715 1.00 16.52 C HETATM 1211 C3C HEM 1 18.312 29.179 33.978 1.00 15.16 C HETATM 1212 C4C HEM 1 18.018 28.489 32.705 1.00 19.22 C HETATM 1213 CMC HEM 1 19.641 31.498 34.719 1.00 9.55 C HETATM 1214 CAC HEM 1 17.798 28.608 35.345 1.00 14.02 C HETATM 1215 CBC HEM 1 18.475 27.767 35.998 1.00 5.29 C HETATM 1216 ND HEM 1 17.281 27.042 30.089 1.00 18.46 N HETATM 1217 C1D HEM 1 16.810 26.604 31.324 1.00 13.49 C HETATM 1218 C2D HEM 1 15.871 25.338 31.168 1.00 16.31 C HETATM 1219 C3D HEM 1 15.790 25.056 29.848 1.00 17.34 C HETATM 1220 C4D HEM 1 16.692 26.129 29.157 1.00 28.30 C HETATM 1221 CMD HEM 1 15.146 24.492 32.318 1.00 9.55 C HETATM 1222 CAD HEM 1 14.961 23.805 29.192 1.00 17.17 C HETATM 1223 CBD HEM 1 15.836 22.690 28.961 1.00 21.34 C HETATM 1224 CGD HEM 1 14.891 21.362 28.727 1.00 41.06 C HETATM 1225 O1D HEM 1 14.152 20.849 29.669 1.00 38.18 O HETATM 1226 O2D HEM 1 15.053 20.650 27.722 1.00 44.36 O HETATM 1227 O HOH 2 25.931 15.090 29.267 1.00 12.43 O HETATM 1228 O HOH 3 28.451 16.636 28.850 1.00 8.43 O HETATM 1229 O HOH 4 23.324 44.985 27.486 1.00 20.76 O HETATM 1230 O HOH 5 47.234 35.449 36.897 1.00 23.81 O HETATM 1231 O HOH 6 24.916 36.686 21.985 1.00 21.58 O HETATM 1232 O HOH 7 26.790 36.363 40.213 1.00 31.38 O HETATM 1233 O HOH 8 26.477 19.341 41.853 1.00 36.88 O HETATM 1234 O HOH 9 31.774 50.607 15.087 1.00 28.05 O HETATM 1235 O HOH 10 29.427 38.962 17.672 1.00 28.73 O HETATM 1236 O HOH 11 27.915 52.056 19.905 1.00 10.94 O HETATM 1237 O HOH 12 19.378 45.327 20.062 1.00 30.59 O HETATM 1238 O HOH 13 21.522 47.746 20.830 1.00 19.03 O HETATM 1239 O HOH 14 22.038 46.981 23.475 1.00 26.77 O HETATM 1240 O HOH 15 24.429 46.737 25.236 1.00 21.81 O HETATM 1241 O HOH 16 21.695 48.346 29.235 1.00 24.25 O HETATM 1242 O HOH 17 24.555 48.301 29.793 1.00 15.26 O HETATM 1243 O HOH 18 25.759 47.956 32.242 1.00 17.03 O HETATM 1244 O HOH 19 16.025 30.463 20.749 1.00 42.24 O HETATM 1245 O HOH 20 34.446 20.180 22.212 1.00 37.97 O HETATM 1246 O HOH 21 19.071 19.613 24.065 1.00 53.19 O HETATM 1247 O HOH 22 30.512 38.862 40.078 1.00 23.14 O HETATM 1248 O HOH 23 33.043 39.811 38.393 1.00 21.62 O HETATM 1249 O HOH 24 42.372 26.184 36.113 1.00 46.35 O HETATM 1250 O HOH 25 29.763 51.446 24.994 1.00 15.17 O HETATM 1251 O HOH 26 23.333 39.642 17.681 1.00 36.08 O HETATM 1252 O HOH 27 29.619 25.953 20.332 1.00 52.74 O HETATM 1253 O HOH 28 40.853 45.561 34.700 1.00 44.43 O HETATM 1254 O HOH 29 13.363 35.834 40.544 1.00 27.43 O HETATM 1255 O HOH 30 22.650 41.468 34.110 1.00 28.51 O HETATM 1256 O HOH 31 13.367 23.775 41.432 1.00 47.45 O HETATM 1257 O HOH 32 17.016 42.953 31.992 1.00 34.45 O HETATM 1258 O HOH 33 25.696 38.758 39.338 1.00 43.36 O HETATM 1259 O HOH 34 17.414 21.590 25.728 1.00 41.22 O HETATM 1260 O HOH 35 21.290 46.625 27.013 1.00 41.47 O HETATM 1261 O HOH 36 29.523 44.573 33.774 1.00 40.78 O HETATM 1262 O HOH 37 38.326 42.061 37.465 1.00 42.39 O HETATM 1263 O HOH 38 44.189 37.833 30.883 1.00 36.56 O HETATM 1264 O HOH 39 47.347 27.991 33.578 1.00 48.42 O HETATM 1265 O HOH 40 37.960 49.187 21.258 1.00 45.43 O HETATM 1266 O HOH 41 25.012 39.392 21.150 1.00 50.73 O HETATM 1267 O HOH 42 25.519 23.615 20.762 1.00 40.89 O HETATM 1268 O HOH 43 31.809 48.572 24.712 1.00 43.11 O HETATM 1269 O HOH 44 21.840 9.944 34.939 1.00 36.08 O HETATM 1270 O HOH 45 19.979 9.637 31.559 1.00 38.09 O HETATM 1271 O HOH 46 18.395 11.845 30.916 1.00 49.04 O HETATM 1272 O HOH 47 35.895 15.577 25.956 1.00 41.92 O HETATM 1273 O HOH 48 40.111 23.818 26.807 1.00 43.60 O HETATM 1274 O HOH 49 42.734 32.380 26.300 1.00 43.35 O HETATM 1275 O HOH 50 42.240 34.812 19.287 1.00 46.53 O HETATM 1276 O HOH 51 42.076 37.474 20.405 1.00 48.86 O HETATM 1277 O HOH 52 42.739 30.969 22.511 1.00 36.51 O HETATM 1278 O HOH 53 17.199 12.121 43.334 1.00 55.59 O HETATM 1279 O HOH 54 27.025 38.490 16.111 1.00 45.39 O HETATM 1280 O HOH 55 29.364 15.027 21.902 1.00 43.70 O HETATM 1281 O HOH 56 23.384 37.799 37.490 1.00 44.56 O HETATM 1282 O HOH 57 20.796 38.790 37.729 1.00 41.87 O HETATM 1283 O HOH 58 36.832 34.800 35.450 1.00 37.27 O HETATM 1284 O HOH 59 11.607 35.912 37.024 1.00 36.20 O HETATM 1285 O HOH 60 24.017 39.446 35.235 1.00 36.66 O HETATM 1286 O HOH 61 30.353 27.368 22.793 1.00 37.47 O HETATM 1287 O HOH 62 36.066 23.675 33.475 1.00 44.96 O HETATM 1288 O HOH 63 27.911 51.373 36.184 1.00 40.84 O HETATM 1289 O HOH 64 46.633 37.277 29.917 1.00 33.89 O HETATM 1290 O HOH 65 20.648 15.492 37.335 1.00 32.36 O HETATM 1291 O HOH 66 45.476 42.246 24.707 1.00 32.66 O HETATM 1292 O HOH 67 43.913 49.300 24.183 1.00 36.61 O CONECT 1182 1183 1184 CONECT 1183 1182 CONECT 1184 1182 1189 1200 1208 CONECT 1184 1216 CONECT 1185 1190 1220 CONECT 1186 1193 1201 CONECT 1187 1204 1209 CONECT 1188 1212 1217 CONECT 1189 1184 1190 1193 CONECT 1190 1185 1189 1191 CONECT 1191 1190 1192 1195 CONECT 1192 1191 1193 1194 CONECT 1193 1186 1189 1192 CONECT 1194 1192 CONECT 1195 1191 1196 CONECT 1196 1195 1197 CONECT 1197 1196 1198 1199 CONECT 1198 1197 CONECT 1199 1197 CONECT 1200 1184 1201 1204 CONECT 1201 1186 1200 1202 CONECT 1202 1201 1203 1205 CONECT 1203 1202 1204 1206 CONECT 1204 1187 1200 1203 CONECT 1205 1202 CONECT 1206 1203 1207 CONECT 1207 1206 CONECT 1208 1184 1209 1212 CONECT 1209 1187 1208 1210 CONECT 1210 1209 1211 1213 CONECT 1211 1210 1212 1214 CONECT 1212 1188 1208 1211 CONECT 1213 1210 CONECT 1214 1211 1215 CONECT 1215 1214 CONECT 1216 1184 1217 1220 CONECT 1217 1188 1216 1218 CONECT 1218 1217 1219 1221 CONECT 1219 1218 1220 1222 CONECT 1220 1185 1216 1219 CONECT 1221 1218 CONECT 1222 1219 1223 CONECT 1223 1222 1224 CONECT 1224 1223 1225 1226 CONECT 1225 1224 CONECT 1226 1224 MASTER 363 1 2 7 0 0 0 6 1291 1 46 12 END