HEADER LYASE 23-JUL-04 1U40 TITLE ISPF WITH 4-DIPHOSPHOCYTIDYL-2C-METHYL-D-ERYTHRITOL COMPND MOL_ID: 1; COMPND 2 MOLECULE: 2-C-METHYL-D-ERYTHRITOL 2,4-CYCLODIPHOSPHATE SYNTHASE; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: MECPS, MECDP-SYNTHASE, ISPF; COMPND 5 EC: 4.6.1.12; COMPND 6 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI; SOURCE 3 ORGANISM_TAXID: 562; SOURCE 4 GENE: ISPF; SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562 KEYWDS LYASE, MEP PATHWAY, TERPENE BIOSYNTHESIS EXPDTA X-RAY DIFFRACTION AUTHOR S.STEINBACHER,J.KAISER,J.WUNGSINTAWEEKUL,S.HECHT,W.EISENREICH, AUTHOR 2 S.GERHARDT,A.BACHER,F.ROHDICH REVDAT 3 13-JUL-11 1U40 1 VERSN REVDAT 2 24-FEB-09 1U40 1 VERSN REVDAT 1 31-AUG-04 1U40 0 JRNL AUTH S.STEINBACHER,J.KAISER,J.WUNGSINTAWEEKUL,S.HECHT, JRNL AUTH 2 W.EISENREICH,S.GERHARDT,A.BACHER,F.ROHDICH JRNL TITL STRUCTURE OF 2C-METHYL-D-ERYTHRITOL-2,4-CYCLODIPHOSPHATE JRNL TITL 2 SYNTHASE INVOLVED IN MEVALONATE INDEPENDENT BIOSYNTHESIS OF JRNL TITL 3 ISOPRENOIDS JRNL REF J.MOL.BIOL. V. 316 79 2002 JRNL REFN ISSN 0022-2836 JRNL PMID 11829504 JRNL DOI 10.1006/JMBI.2001.5341 REMARK 2 REMARK 2 RESOLUTION. 2.80 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : X-PLOR REMARK 3 AUTHORS : BRUNGER REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 8.00 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000 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 : 12023 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 CROSS-VALIDATION METHOD : NULL REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM REMARK 3 R VALUE (WORKING SET) : 0.233 REMARK 3 FREE R VALUE : 0.264 REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL REMARK 3 FREE R VALUE TEST SET COUNT : 601 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 : 1157 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 34 REMARK 3 SOLVENT ATOMS : 0 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) : 0.010 REMARK 3 BOND ANGLES (DEGREES) : 1.85 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 1U40 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 28-JUL-04. REMARK 100 THE RCSB ID CODE IS RCSB023216. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 08-APR-01 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 7 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : N REMARK 200 RADIATION SOURCE : ROTATING ANODE REMARK 200 BEAMLINE : NULL REMARK 200 X-RAY GENERATOR MODEL : RIGAKU RU200 REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.541 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : IMAGE PLATE REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM REMARK 200 DATA SCALING SOFTWARE : CCP4 (SCALA) REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 12586 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.800 REMARK 200 RESOLUTION RANGE LOW (A) : 20.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8 REMARK 200 DATA REDUNDANCY : 3.840 REMARK 200 R MERGE (I) : 0.10600 REMARK 200 R SYM (I) : NULL REMARK 200 <I/SIGMA(I)> 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 <I/SIGMA(I)> FOR SHELL : NULL REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS REMARK 200 SOFTWARE USED: X-PLOR REMARK 200 STARTING MODEL: 1JY8 REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): NULL REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): NULL REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: AMMONIUM FORMATE, PH 7, VAPOR REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 21 3 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X+1/2,-Y,Z+1/2 REMARK 290 3555 -X,Y+1/2,-Z+1/2 REMARK 290 4555 X+1/2,-Y+1/2,-Z REMARK 290 5555 Z,X,Y REMARK 290 6555 Z+1/2,-X+1/2,-Y REMARK 290 7555 -Z+1/2,-X,Y+1/2 REMARK 290 8555 -Z,X+1/2,-Y+1/2 REMARK 290 9555 Y,Z,X REMARK 290 10555 -Y,Z+1/2,-X+1/2 REMARK 290 11555 Y+1/2,-Z+1/2,-X REMARK 290 12555 -Y+1/2,-Z,X+1/2 REMARK 290 13555 X+1/2,Y+1/2,Z+1/2 REMARK 290 14555 -X,-Y+1/2,Z REMARK 290 15555 -X+1/2,Y,-Z REMARK 290 16555 X,-Y,-Z+1/2 REMARK 290 17555 Z+1/2,X+1/2,Y+1/2 REMARK 290 18555 Z,-X,-Y+1/2 REMARK 290 19555 -Z,-X+1/2,Y REMARK 290 20555 -Z+1/2,X,-Y REMARK 290 21555 Y+1/2,Z+1/2,X+1/2 REMARK 290 22555 -Y+1/2,Z,-X REMARK 290 23555 Y,-Z,-X+1/2 REMARK 290 24555 -Y,-Z+1/2,X 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 72.40500 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 72.40500 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 72.40500 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 72.40500 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 72.40500 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 72.40500 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 5 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY2 5 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY3 5 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY1 6 0.000000 0.000000 1.000000 72.40500 REMARK 290 SMTRY2 6 -1.000000 0.000000 0.000000 72.40500 REMARK 290 SMTRY3 6 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY1 7 0.000000 0.000000 -1.000000 72.40500 REMARK 290 SMTRY2 7 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY3 7 0.000000 1.000000 0.000000 72.40500 REMARK 290 SMTRY1 8 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY2 8 1.000000 0.000000 0.000000 72.40500 REMARK 290 SMTRY3 8 0.000000 -1.000000 0.000000 72.40500 REMARK 290 SMTRY1 9 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY2 9 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY3 9 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY1 10 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY2 10 0.000000 0.000000 1.000000 72.40500 REMARK 290 SMTRY3 10 -1.000000 0.000000 0.000000 72.40500 REMARK 290 SMTRY1 11 0.000000 1.000000 0.000000 72.40500 REMARK 290 SMTRY2 11 0.000000 0.000000 -1.000000 72.40500 REMARK 290 SMTRY3 11 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY1 12 0.000000 -1.000000 0.000000 72.40500 REMARK 290 SMTRY2 12 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY3 12 1.000000 0.000000 0.000000 72.40500 REMARK 290 SMTRY1 13 1.000000 0.000000 0.000000 72.40500 REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 72.40500 REMARK 290 SMTRY3 13 0.000000 0.000000 1.000000 72.40500 REMARK 290 SMTRY1 14 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 14 0.000000 -1.000000 0.000000 72.40500 REMARK 290 SMTRY3 14 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 15 -1.000000 0.000000 0.000000 72.40500 REMARK 290 SMTRY2 15 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 15 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 16 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 16 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 16 0.000000 0.000000 -1.000000 72.40500 REMARK 290 SMTRY1 17 0.000000 0.000000 1.000000 72.40500 REMARK 290 SMTRY2 17 1.000000 0.000000 0.000000 72.40500 REMARK 290 SMTRY3 17 0.000000 1.000000 0.000000 72.40500 REMARK 290 SMTRY1 18 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY2 18 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY3 18 0.000000 -1.000000 0.000000 72.40500 REMARK 290 SMTRY1 19 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY2 19 -1.000000 0.000000 0.000000 72.40500 REMARK 290 SMTRY3 19 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY1 20 0.000000 0.000000 -1.000000 72.40500 REMARK 290 SMTRY2 20 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY3 20 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY1 21 0.000000 1.000000 0.000000 72.40500 REMARK 290 SMTRY2 21 0.000000 0.000000 1.000000 72.40500 REMARK 290 SMTRY3 21 1.000000 0.000000 0.000000 72.40500 REMARK 290 SMTRY1 22 0.000000 -1.000000 0.000000 72.40500 REMARK 290 SMTRY2 22 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY3 22 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY1 23 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY2 23 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY3 23 -1.000000 0.000000 0.000000 72.40500 REMARK 290 SMTRY1 24 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY2 24 0.000000 0.000000 -1.000000 72.40500 REMARK 290 SMTRY3 24 1.000000 0.000000 0.000000 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: TRIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC REMARK 350 SOFTWARE USED: PISA,PQS REMARK 350 TOTAL BURIED SURFACE AREA: 9200 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 15410 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -167.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 350 BIOMT1 2 0.000000 0.000000 1.000000 0.00000 REMARK 350 BIOMT2 2 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT3 2 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT1 3 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT2 3 0.000000 0.000000 1.000000 0.00000 REMARK 350 BIOMT3 3 1.000000 0.000000 0.000000 0.00000 REMARK 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 LYS A 156 REMARK 465 ALA A 157 REMARK 465 THR A 158 REMARK 465 LYS A 159 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 SER A 35 -151.07 -76.78 REMARK 500 ASP A 38 84.58 -68.47 REMARK 500 ASN A 93 160.40 179.67 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 ZN A 160 ZN REMARK 620 N RES CSSEQI ATOM REMARK 620 1 HIS A 10 NE2 REMARK 620 2 CDM A 669 O1B 128.5 REMARK 620 3 ASP A 8 OD1 103.3 113.3 REMARK 620 4 HIS A 42 ND1 112.1 99.1 96.1 REMARK 620 N 1 2 3 REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 160 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CDM A 669 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1U3P RELATED DB: PDB REMARK 900 ISPF NATIVE REMARK 900 RELATED ID: 1U3L RELATED DB: PDB REMARK 900 ISPF WITH MG AND CDP REMARK 900 RELATED ID: 1JY8 RELATED DB: PDB REMARK 900 ISPF WITH CMP AND 2C-METHYL-D-ERYTHRITOL 2,4- REMARK 900 CYCLODIPHOSPHATE REMARK 900 RELATED ID: 1U43 RELATED DB: PDB REMARK 900 ISPF WITH 4-DIPHOSPHOCYTIDYL-2C-METHYL-D-ERYTHRITOL 2- REMARK 900 PHOSPHATE DBREF 1U40 A 1 159 UNP P62617 ISPF_ECOLI 1 159 SEQRES 1 A 159 MET ARG ILE GLY HIS GLY PHE ASP VAL HIS ALA PHE GLY SEQRES 2 A 159 GLY GLU GLY PRO ILE ILE ILE GLY GLY VAL ARG ILE PRO SEQRES 3 A 159 TYR GLU LYS GLY LEU LEU ALA HIS SER ASP GLY ASP VAL SEQRES 4 A 159 ALA LEU HIS ALA LEU THR ASP ALA LEU LEU GLY ALA ALA SEQRES 5 A 159 ALA LEU GLY ASP ILE GLY LYS LEU PHE PRO ASP THR ASP SEQRES 6 A 159 PRO ALA PHE LYS GLY ALA ASP SER ARG GLU LEU LEU ARG SEQRES 7 A 159 GLU ALA TRP ARG ARG ILE GLN ALA LYS GLY TYR THR LEU SEQRES 8 A 159 GLY ASN VAL ASP VAL THR ILE ILE ALA GLN ALA PRO LYS SEQRES 9 A 159 MET LEU PRO HIS ILE PRO GLN MET ARG VAL PHE ILE ALA SEQRES 10 A 159 GLU ASP LEU GLY CYS HIS MET ASP ASP VAL ASN VAL LYS SEQRES 11 A 159 ALA THR THR THR GLU LYS LEU GLY PHE THR GLY ARG GLY SEQRES 12 A 159 GLU GLY ILE ALA CYS GLU ALA VAL ALA LEU LEU ILE LYS SEQRES 13 A 159 ALA THR LYS HET ZN A 160 1 HET CDM A 669 33 HETNAM ZN ZINC ION HETNAM CDM 4-DIPHOSPHOCYTIDYL-2-C-METHYL-D-ERYTHRITOL FORMUL 2 ZN ZN 2+ FORMUL 3 CDM C14 H25 N3 O14 P2 HELIX 1 1 ASP A 38 ALA A 53 1 16 HELIX 2 2 ASP A 56 PHE A 61 1 6 HELIX 3 3 ASP A 65 LYS A 69 5 5 HELIX 4 4 ASP A 72 LYS A 87 1 16 HELIX 5 5 MET A 105 PRO A 107 5 3 HELIX 6 6 HIS A 108 GLY A 121 1 14 HELIX 7 7 HIS A 123 ASP A 125 5 3 HELIX 8 8 LEU A 137 ARG A 142 1 6 SHEET 1 A 5 LYS A 29 LEU A 31 0 SHEET 2 A 5 ARG A 2 GLU A 15 -1 N GLY A 13 O GLY A 30 SHEET 3 A 5 GLY A 145 ILE A 155 -1 O LEU A 154 N ARG A 2 SHEET 4 A 5 THR A 90 ILE A 99 -1 N THR A 90 O ILE A 155 SHEET 5 A 5 VAL A 127 THR A 132 1 O LYS A 130 N ILE A 98 SHEET 1 B 2 ILE A 18 ILE A 20 0 SHEET 2 B 2 VAL A 23 ILE A 25 -1 O ILE A 25 N ILE A 18 LINK ZN ZN A 160 NE2 HIS A 10 1555 1555 1.95 LINK ZN ZN A 160 O1B CDM A 669 1555 1555 1.94 LINK ZN ZN A 160 OD1 ASP A 8 1555 1555 1.94 LINK ZN ZN A 160 ND1 HIS A 42 1555 1555 1.96 CISPEP 1 GLY A 16 PRO A 17 0 -0.01 CISPEP 2 ALA A 102 PRO A 103 0 0.42 SITE 1 AC1 4 ASP A 8 HIS A 10 HIS A 42 CDM A 669 SITE 1 AC2 22 ASP A 8 HIS A 10 HIS A 34 HIS A 42 SITE 2 AC2 22 ASP A 56 ILE A 57 GLY A 58 LYS A 59 SITE 3 AC2 22 PHE A 61 ASP A 63 PHE A 68 LEU A 76 SITE 4 AC2 22 ALA A 100 PRO A 103 LYS A 104 MET A 105 SITE 5 AC2 22 LEU A 106 ALA A 131 THR A 132 THR A 133 SITE 6 AC2 22 GLU A 135 ZN A 160 CRYST1 144.810 144.810 144.810 90.00 90.00 90.00 I 21 3 24 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 0.006906 0.000000 0.000000 0.00000 SCALE2 0.000000 0.006906 0.000000 0.00000 SCALE3 0.000000 0.000000 0.006906 0.00000 ATOM 1 N MET A 1 29.134 36.411 30.109 1.00 49.87 N ATOM 2 CA MET A 1 29.029 35.383 29.027 1.00 48.64 C ATOM 3 C MET A 1 27.618 34.868 28.791 1.00 44.93 C ATOM 4 O MET A 1 26.901 34.556 29.739 1.00 45.18 O ATOM 5 CB MET A 1 29.962 34.223 29.311 1.00 52.63 C ATOM 6 CG MET A 1 31.362 34.497 28.846 1.00 61.65 C ATOM 7 SD MET A 1 32.459 33.172 29.304 1.00 74.65 S ATOM 8 CE MET A 1 33.589 34.038 30.482 1.00 72.98 C ATOM 9 N ARG A 2 27.228 34.789 27.522 1.00 41.63 N ATOM 10 CA ARG A 2 25.900 34.331 27.141 1.00 38.93 C ATOM 11 C ARG A 2 25.965 33.144 26.194 1.00 37.41 C ATOM 12 O ARG A 2 26.865 33.052 25.375 1.00 38.48 O ATOM 13 CB ARG A 2 25.110 35.484 26.536 1.00 38.34 C ATOM 14 CG ARG A 2 24.889 36.600 27.537 1.00 40.15 C ATOM 15 CD ARG A 2 24.159 37.780 26.946 1.00 43.49 C ATOM 16 NE ARG A 2 22.803 37.432 26.546 1.00 49.86 N ATOM 17 CZ ARG A 2 21.702 37.669 27.261 1.00 52.16 C ATOM 18 NH1 ARG A 2 20.524 37.290 26.773 1.00 52.11 N ATOM 19 NH2 ARG A 2 21.773 38.258 28.460 1.00 52.43 N ATOM 20 N ILE A 3 24.993 32.247 26.308 1.00 36.39 N ATOM 21 CA ILE A 3 24.935 31.032 25.503 1.00 33.51 C ATOM 22 C ILE A 3 23.805 31.111 24.494 1.00 30.73 C ATOM 23 O ILE A 3 22.780 31.695 24.770 1.00 30.26 O ATOM 24 CB ILE A 3 24.694 29.816 26.429 1.00 33.84 C ATOM 25 CG1 ILE A 3 24.695 28.515 25.641 1.00 36.12 C ATOM 26 CG2 ILE A 3 23.364 29.945 27.128 1.00 33.49 C ATOM 27 CD1 ILE A 3 24.494 27.301 26.514 1.00 36.98 C ATOM 28 N GLY A 4 23.979 30.501 23.335 1.00 30.42 N ATOM 29 CA GLY A 4 22.925 30.528 22.337 1.00 29.96 C ATOM 30 C GLY A 4 22.779 29.187 21.645 1.00 30.41 C ATOM 31 O GLY A 4 23.725 28.395 21.615 1.00 31.83 O ATOM 32 N HIS A 5 21.600 28.914 21.101 1.00 29.48 N ATOM 33 CA HIS A 5 21.348 27.661 20.405 1.00 28.78 C ATOM 34 C HIS A 5 20.555 27.903 19.141 1.00 30.08 C ATOM 35 O HIS A 5 19.550 28.629 19.153 1.00 30.89 O ATOM 36 CB HIS A 5 20.560 26.674 21.277 1.00 27.53 C ATOM 37 CG HIS A 5 20.211 25.392 20.574 1.00 28.39 C ATOM 38 ND1 HIS A 5 19.008 25.203 19.922 1.00 26.84 N ATOM 39 CD2 HIS A 5 20.928 24.254 20.379 1.00 25.67 C ATOM 40 CE1 HIS A 5 19.003 24.008 19.352 1.00 29.50 C ATOM 41 NE2 HIS A 5 20.153 23.413 19.616 1.00 27.00 N ATOM 42 N GLY A 6 20.983 27.252 18.065 1.00 28.82 N ATOM 43 CA GLY A 6 20.285 27.369 16.803 1.00 29.21 C ATOM 44 C GLY A 6 20.037 25.986 16.233 1.00 30.47 C ATOM 45 O GLY A 6 20.679 25.017 16.654 1.00 32.59 O ATOM 46 N PHE A 7 19.082 25.881 15.316 1.00 29.56 N ATOM 47 CA PHE A 7 18.766 24.614 14.673 1.00 28.22 C ATOM 48 C PHE A 7 18.127 24.926 13.334 1.00 28.47 C ATOM 49 O PHE A 7 17.363 25.884 13.238 1.00 29.91 O ATOM 50 CB PHE A 7 17.794 23.818 15.532 1.00 29.32 C ATOM 51 CG PHE A 7 17.322 22.558 14.889 1.00 29.49 C ATOM 52 CD1 PHE A 7 18.010 21.377 15.067 1.00 30.04 C ATOM 53 CD2 PHE A 7 16.208 22.559 14.068 1.00 31.25 C ATOM 54 CE1 PHE A 7 17.599 20.215 14.430 1.00 29.25 C ATOM 55 CE2 PHE A 7 15.792 21.396 13.427 1.00 29.51 C ATOM 56 CZ PHE A 7 16.491 20.226 13.609 1.00 27.89 C ATOM 57 N ASP A 8 18.443 24.146 12.303 1.00 28.72 N ATOM 58 CA ASP A 8 17.856 24.374 10.979 1.00 29.63 C ATOM 59 C ASP A 8 17.829 23.123 10.116 1.00 29.46 C ATOM 60 O ASP A 8 18.583 22.184 10.352 1.00 32.34 O ATOM 61 CB ASP A 8 18.577 25.501 10.253 1.00 32.47 C ATOM 62 CG ASP A 8 17.800 26.028 9.057 1.00 34.46 C ATOM 63 OD1 ASP A 8 18.453 26.536 8.131 1.00 37.43 O ATOM 64 OD2 ASP A 8 16.552 25.962 9.030 1.00 37.51 O ATOM 65 N VAL A 9 16.940 23.106 9.131 1.00 29.31 N ATOM 66 CA VAL A 9 16.772 21.968 8.232 1.00 28.06 C ATOM 67 C VAL A 9 16.378 22.471 6.853 1.00 30.26 C ATOM 68 O VAL A 9 15.696 23.487 6.730 1.00 32.51 O ATOM 69 CB VAL A 9 15.621 21.058 8.727 1.00 27.07 C ATOM 70 CG1 VAL A 9 15.269 20.001 7.695 1.00 24.82 C ATOM 71 CG2 VAL A 9 15.991 20.412 10.031 1.00 26.44 C ATOM 72 N HIS A 10 16.870 21.813 5.811 1.00 32.35 N ATOM 73 CA HIS A 10 16.503 22.159 4.435 1.00 32.38 C ATOM 74 C HIS A 10 16.344 20.878 3.640 1.00 32.44 C ATOM 75 O HIS A 10 17.077 19.901 3.846 1.00 33.42 O ATOM 76 CB HIS A 10 17.491 23.121 3.787 1.00 32.45 C ATOM 77 CG HIS A 10 17.316 24.531 4.244 1.00 36.74 C ATOM 78 ND1 HIS A 10 16.290 25.333 3.796 1.00 38.43 N ATOM 79 CD2 HIS A 10 17.974 25.254 5.184 1.00 38.47 C ATOM 80 CE1 HIS A 10 16.322 26.487 4.442 1.00 40.50 C ATOM 81 NE2 HIS A 10 17.336 26.467 5.292 1.00 40.65 N ATOM 82 N ALA A 11 15.319 20.846 2.806 1.00 31.37 N ATOM 83 CA ALA A 11 15.045 19.665 2.012 1.00 31.14 C ATOM 84 C ALA A 11 15.852 19.640 0.722 1.00 31.16 C ATOM 85 O ALA A 11 16.132 20.691 0.139 1.00 31.48 O ATOM 86 CB ALA A 11 13.558 19.591 1.704 1.00 31.96 C ATOM 87 N PHE A 12 16.244 18.442 0.292 1.00 30.80 N ATOM 88 CA PHE A 12 16.988 18.291 -0.946 1.00 29.21 C ATOM 89 C PHE A 12 16.016 18.577 -2.061 1.00 33.33 C ATOM 90 O PHE A 12 14.806 18.411 -1.904 1.00 35.03 O ATOM 91 CB PHE A 12 17.534 16.878 -1.103 1.00 24.76 C ATOM 92 CG PHE A 12 18.799 16.639 -0.354 1.00 20.58 C ATOM 93 CD1 PHE A 12 19.885 17.472 -0.531 1.00 20.76 C ATOM 94 CD2 PHE A 12 18.889 15.620 0.567 1.00 18.78 C ATOM 95 CE1 PHE A 12 21.043 17.294 0.205 1.00 20.14 C ATOM 96 CE2 PHE A 12 20.041 15.436 1.305 1.00 19.08 C ATOM 97 CZ PHE A 12 21.121 16.280 1.122 1.00 19.86 C ATOM 98 N GLY A 13 16.542 19.022 -3.187 1.00 37.05 N ATOM 99 CA GLY A 13 15.696 19.326 -4.312 1.00 41.25 C ATOM 100 C GLY A 13 16.552 19.874 -5.422 1.00 45.25 C ATOM 101 O GLY A 13 17.495 20.641 -5.179 1.00 47.14 O ATOM 102 N GLY A 14 16.257 19.430 -6.637 1.00 47.30 N ATOM 103 CA GLY A 14 16.992 19.895 -7.793 1.00 50.54 C ATOM 104 C GLY A 14 18.341 19.241 -7.953 1.00 52.09 C ATOM 105 O GLY A 14 18.606 18.176 -7.378 1.00 51.16 O ATOM 106 N GLU A 15 19.187 19.908 -8.730 1.00 54.27 N ATOM 107 CA GLU A 15 20.532 19.441 -9.016 1.00 57.13 C ATOM 108 C GLU A 15 21.514 20.048 -8.025 1.00 54.95 C ATOM 109 O GLU A 15 21.261 21.130 -7.483 1.00 55.59 O ATOM 110 CB GLU A 15 20.927 19.851 -10.441 1.00 64.20 C ATOM 111 CG GLU A 15 20.057 19.252 -11.542 1.00 72.91 C ATOM 112 CD GLU A 15 20.120 17.730 -11.567 1.00 79.20 C ATOM 113 OE1 GLU A 15 19.107 17.080 -11.207 1.00 83.00 O ATOM 114 OE2 GLU A 15 21.186 17.189 -11.944 1.00 82.31 O ATOM 115 N GLY A 16 22.621 19.347 -7.784 1.00 52.26 N ATOM 116 CA GLY A 16 23.639 19.840 -6.871 1.00 48.46 C ATOM 117 C GLY A 16 24.331 21.061 -7.448 1.00 45.84 C ATOM 118 O GLY A 16 23.980 21.503 -8.540 1.00 47.51 O ATOM 119 N PRO A 17 25.349 21.609 -6.775 1.00 41.94 N ATOM 120 CA PRO A 17 25.960 21.231 -5.509 1.00 40.08 C ATOM 121 C PRO A 17 25.210 21.918 -4.375 1.00 39.29 C ATOM 122 O PRO A 17 24.285 22.703 -4.610 1.00 42.86 O ATOM 123 CB PRO A 17 27.352 21.809 -5.659 1.00 40.53 C ATOM 124 CG PRO A 17 27.054 23.144 -6.290 1.00 38.02 C ATOM 125 CD PRO A 17 25.972 22.834 -7.306 1.00 39.38 C ATOM 126 N ILE A 18 25.625 21.652 -3.149 1.00 33.98 N ATOM 127 CA ILE A 18 24.983 22.253 -2.008 1.00 29.60 C ATOM 128 C ILE A 18 25.980 23.202 -1.413 1.00 28.18 C ATOM 129 O ILE A 18 27.170 23.071 -1.663 1.00 30.26 O ATOM 130 CB ILE A 18 24.595 21.187 -0.959 1.00 29.23 C ATOM 131 CG1 ILE A 18 25.835 20.514 -0.378 1.00 28.24 C ATOM 132 CG2 ILE A 18 23.732 20.126 -1.597 1.00 29.74 C ATOM 133 CD1 ILE A 18 25.505 19.420 0.602 1.00 26.36 C ATOM 134 N ILE A 19 25.499 24.173 -0.648 1.00 27.10 N ATOM 135 CA ILE A 19 26.380 25.128 0.003 1.00 24.05 C ATOM 136 C ILE A 19 26.156 24.923 1.491 1.00 26.28 C ATOM 137 O ILE A 19 25.030 25.086 1.956 1.00 28.20 O ATOM 138 CB ILE A 19 26.003 26.580 -0.335 1.00 20.68 C ATOM 139 CG1 ILE A 19 25.810 26.768 -1.838 1.00 21.49 C ATOM 140 CG2 ILE A 19 27.085 27.500 0.104 1.00 16.94 C ATOM 141 CD1 ILE A 19 27.035 26.543 -2.658 1.00 24.27 C ATOM 142 N ILE A 20 27.192 24.479 2.208 1.00 25.84 N ATOM 143 CA ILE A 20 27.118 24.254 3.651 1.00 24.42 C ATOM 144 C ILE A 20 28.333 24.897 4.297 1.00 26.42 C ATOM 145 O ILE A 20 29.458 24.528 3.976 1.00 31.07 O ATOM 146 CB ILE A 20 27.207 22.764 4.009 1.00 24.98 C ATOM 147 CG1 ILE A 20 26.151 21.937 3.270 1.00 25.62 C ATOM 148 CG2 ILE A 20 27.050 22.589 5.511 1.00 26.34 C ATOM 149 CD1 ILE A 20 24.726 22.232 3.660 1.00 23.56 C ATOM 150 N GLY A 21 28.128 25.817 5.232 1.00 25.27 N ATOM 151 CA GLY A 21 29.248 26.466 5.896 1.00 23.72 C ATOM 152 C GLY A 21 30.060 27.295 4.932 1.00 24.12 C ATOM 153 O GLY A 21 31.249 27.525 5.117 1.00 24.95 O ATOM 154 N GLY A 22 29.408 27.741 3.874 1.00 26.31 N ATOM 155 CA GLY A 22 30.096 28.539 2.884 1.00 27.65 C ATOM 156 C GLY A 22 30.710 27.706 1.779 1.00 27.87 C ATOM 157 O GLY A 22 30.843 28.182 0.655 1.00 30.93 O ATOM 158 N VAL A 23 31.027 26.449 2.064 1.00 25.46 N ATOM 159 CA VAL A 23 31.651 25.593 1.073 1.00 24.12 C ATOM 160 C VAL A 23 30.685 25.019 0.058 1.00 25.36 C ATOM 161 O VAL A 23 29.579 24.605 0.395 1.00 28.86 O ATOM 162 CB VAL A 23 32.418 24.469 1.745 1.00 22.39 C ATOM 163 CG1 VAL A 23 33.115 23.635 0.726 1.00 24.07 C ATOM 164 CG2 VAL A 23 33.431 25.051 2.696 1.00 24.78 C ATOM 165 N ARG A 24 31.091 25.032 -1.200 1.00 25.46 N ATOM 166 CA ARG A 24 30.258 24.502 -2.262 1.00 27.56 C ATOM 167 C ARG A 24 30.620 23.040 -2.334 1.00 27.25 C ATOM 168 O ARG A 24 31.692 22.691 -2.799 1.00 32.64 O ATOM 169 CB ARG A 24 30.579 25.195 -3.575 1.00 29.86 C ATOM 170 CG ARG A 24 29.628 24.826 -4.680 1.00 41.26 C ATOM 171 CD ARG A 24 30.103 25.337 -6.039 1.00 51.22 C ATOM 172 NE ARG A 24 29.019 25.971 -6.786 1.00 57.32 N ATOM 173 CZ ARG A 24 28.648 25.634 -8.016 1.00 61.81 C ATOM 174 NH1 ARG A 24 27.644 26.291 -8.589 1.00 63.83 N ATOM 175 NH2 ARG A 24 29.267 24.639 -8.664 1.00 64.56 N ATOM 176 N ILE A 25 29.764 22.193 -1.797 1.00 25.99 N ATOM 177 CA ILE A 25 30.011 20.764 -1.765 1.00 24.92 C ATOM 178 C ILE A 25 29.273 20.071 -2.890 1.00 26.06 C ATOM 179 O ILE A 25 28.073 20.253 -3.055 1.00 30.52 O ATOM 180 CB ILE A 25 29.503 20.198 -0.442 1.00 24.93 C ATOM 181 CG1 ILE A 25 30.295 20.786 0.719 1.00 23.99 C ATOM 182 CG2 ILE A 25 29.585 18.713 -0.437 1.00 23.98 C ATOM 183 CD1 ILE A 25 29.583 20.645 2.021 1.00 22.12 C ATOM 184 N PRO A 26 29.977 19.284 -3.702 1.00 24.96 N ATOM 185 CA PRO A 26 29.295 18.592 -4.797 1.00 25.14 C ATOM 186 C PRO A 26 28.394 17.466 -4.289 1.00 27.42 C ATOM 187 O PRO A 26 28.814 16.674 -3.442 1.00 29.24 O ATOM 188 CB PRO A 26 30.463 18.047 -5.618 1.00 20.80 C ATOM 189 CG PRO A 26 31.534 17.854 -4.617 1.00 18.97 C ATOM 190 CD PRO A 26 31.433 19.105 -3.800 1.00 23.95 C ATOM 191 N TYR A 27 27.178 17.379 -4.820 1.00 28.10 N ATOM 192 CA TYR A 27 26.239 16.336 -4.417 1.00 31.96 C ATOM 193 C TYR A 27 25.252 16.117 -5.547 1.00 35.50 C ATOM 194 O TYR A 27 25.030 17.032 -6.341 1.00 36.76 O ATOM 195 CB TYR A 27 25.482 16.759 -3.165 1.00 32.60 C ATOM 196 CG TYR A 27 24.597 15.686 -2.575 1.00 33.02 C ATOM 197 CD1 TYR A 27 25.109 14.436 -2.253 1.00 31.99 C ATOM 198 CD2 TYR A 27 23.253 15.934 -2.310 1.00 33.37 C ATOM 199 CE1 TYR A 27 24.311 13.459 -1.680 1.00 32.46 C ATOM 200 CE2 TYR A 27 22.449 14.967 -1.737 1.00 34.43 C ATOM 201 CZ TYR A 27 22.984 13.727 -1.424 1.00 33.33 C ATOM 202 OH TYR A 27 22.188 12.755 -0.859 1.00 34.28 O ATOM 203 N GLU A 28 24.655 14.923 -5.614 1.00 38.61 N ATOM 204 CA GLU A 28 23.690 14.604 -6.677 1.00 41.66 C ATOM 205 C GLU A 28 22.570 15.628 -6.707 1.00 40.86 C ATOM 206 O GLU A 28 22.339 16.286 -7.721 1.00 43.08 O ATOM 207 CB GLU A 28 23.047 13.236 -6.478 1.00 44.28 C ATOM 208 CG GLU A 28 23.827 12.246 -5.650 1.00 54.43 C ATOM 209 CD GLU A 28 22.917 11.161 -5.061 1.00 60.42 C ATOM 210 OE1 GLU A 28 23.446 10.142 -4.561 1.00 66.13 O ATOM 211 OE2 GLU A 28 21.673 11.337 -5.073 1.00 61.99 O ATOM 212 N LYS A 29 21.868 15.738 -5.587 1.00 39.17 N ATOM 213 CA LYS A 29 20.769 16.676 -5.458 1.00 36.85 C ATOM 214 C LYS A 29 21.256 17.919 -4.735 1.00 36.56 C ATOM 215 O LYS A 29 22.350 17.917 -4.171 1.00 36.77 O ATOM 216 CB LYS A 29 19.600 16.023 -4.714 1.00 35.30 C ATOM 217 CG LYS A 29 19.966 14.771 -3.921 1.00 34.23 C ATOM 218 CD LYS A 29 18.712 14.066 -3.425 1.00 36.41 C ATOM 219 CE LYS A 29 19.013 12.756 -2.687 1.00 37.65 C ATOM 220 NZ LYS A 29 19.568 12.901 -1.303 1.00 34.69 N ATOM 221 N GLY A 30 20.457 18.980 -4.787 1.00 36.51 N ATOM 222 CA GLY A 30 20.797 20.232 -4.132 1.00 35.30 C ATOM 223 C GLY A 30 19.829 20.532 -3.003 1.00 36.21 C ATOM 224 O GLY A 30 19.037 19.664 -2.630 1.00 35.69 O ATOM 225 N LEU A 31 19.871 21.748 -2.461 1.00 36.21 N ATOM 226 CA LEU A 31 18.992 22.119 -1.347 1.00 36.48 C ATOM 227 C LEU A 31 17.957 23.174 -1.695 1.00 38.76 C ATOM 228 O LEU A 31 18.275 24.195 -2.293 1.00 41.30 O ATOM 229 CB LEU A 31 19.805 22.589 -0.136 1.00 29.57 C ATOM 230 CG LEU A 31 20.512 21.499 0.664 1.00 27.34 C ATOM 231 CD1 LEU A 31 21.354 22.077 1.790 1.00 25.59 C ATOM 232 CD2 LEU A 31 19.463 20.585 1.221 1.00 27.62 C ATOM 233 N LEU A 32 16.715 22.914 -1.323 1.00 40.81 N ATOM 234 CA LEU A 32 15.630 23.845 -1.566 1.00 45.91 C ATOM 235 C LEU A 32 15.601 24.964 -0.515 1.00 50.68 C ATOM 236 O LEU A 32 15.556 24.684 0.695 1.00 52.06 O ATOM 237 CB LEU A 32 14.316 23.089 -1.536 1.00 44.32 C ATOM 238 CG LEU A 32 14.188 22.075 -2.656 1.00 45.12 C ATOM 239 CD1 LEU A 32 12.850 21.384 -2.546 1.00 44.88 C ATOM 240 CD2 LEU A 32 14.320 22.787 -3.992 1.00 45.65 C ATOM 241 N ALA A 33 15.613 26.220 -0.970 1.00 54.52 N ATOM 242 CA ALA A 33 15.580 27.363 -0.059 1.00 59.97 C ATOM 243 C ALA A 33 15.463 28.757 -0.722 1.00 64.08 C ATOM 244 O ALA A 33 15.836 28.934 -1.889 1.00 65.41 O ATOM 245 CB ALA A 33 16.803 27.324 0.865 1.00 59.56 C ATOM 246 N HIS A 34 14.908 29.719 0.038 1.00 67.03 N ATOM 247 CA HIS A 34 14.741 31.131 -0.373 1.00 67.24 C ATOM 248 C HIS A 34 16.171 31.649 -0.552 1.00 65.90 C ATOM 249 O HIS A 34 16.536 32.117 -1.628 1.00 65.51 O ATOM 250 CB HIS A 34 14.000 31.907 0.751 1.00 72.32 C ATOM 251 CG HIS A 34 13.873 33.401 0.546 1.00 76.89 C ATOM 252 ND1 HIS A 34 13.255 33.969 -0.552 1.00 78.35 N ATOM 253 CD2 HIS A 34 14.181 34.435 1.373 1.00 75.97 C ATOM 254 CE1 HIS A 34 13.180 35.281 -0.388 1.00 76.83 C ATOM 255 NE2 HIS A 34 13.733 35.588 0.772 1.00 75.92 N ATOM 256 N SER A 35 16.973 31.511 0.506 1.00 64.16 N ATOM 257 CA SER A 35 18.376 31.921 0.525 1.00 60.63 C ATOM 258 C SER A 35 19.153 30.857 -0.245 1.00 57.29 C ATOM 259 O SER A 35 18.612 30.211 -1.139 1.00 57.11 O ATOM 260 CB SER A 35 18.865 31.959 1.980 1.00 62.00 C ATOM 261 OG SER A 35 18.815 30.658 2.570 1.00 62.99 O ATOM 262 N ASP A 36 20.417 30.666 0.109 1.00 54.08 N ATOM 263 CA ASP A 36 21.233 29.642 -0.530 1.00 51.85 C ATOM 264 C ASP A 36 21.065 28.318 0.244 1.00 51.40 C ATOM 265 O ASP A 36 21.747 27.318 -0.031 1.00 52.74 O ATOM 266 CB ASP A 36 22.698 30.076 -0.565 1.00 49.85 C ATOM 267 CG ASP A 36 23.241 30.373 0.801 1.00 50.76 C ATOM 268 OD1 ASP A 36 24.445 30.681 0.907 1.00 51.55 O ATOM 269 OD2 ASP A 36 22.458 30.302 1.775 1.00 51.70 O ATOM 270 N GLY A 37 20.163 28.336 1.230 1.00 48.41 N ATOM 271 CA GLY A 37 19.875 27.151 2.021 1.00 41.92 C ATOM 272 C GLY A 37 21.020 26.572 2.826 1.00 38.34 C ATOM 273 O GLY A 37 20.995 25.390 3.186 1.00 38.23 O ATOM 274 N ASP A 38 21.989 27.410 3.165 1.00 33.46 N ATOM 275 CA ASP A 38 23.126 26.962 3.946 1.00 31.23 C ATOM 276 C ASP A 38 22.695 26.609 5.376 1.00 31.85 C ATOM 277 O ASP A 38 22.786 27.426 6.295 1.00 35.84 O ATOM 278 CB ASP A 38 24.185 28.053 3.953 1.00 29.96 C ATOM 279 CG ASP A 38 25.513 27.551 4.401 1.00 30.43 C ATOM 280 OD1 ASP A 38 25.554 26.670 5.275 1.00 32.57 O ATOM 281 OD2 ASP A 38 26.532 28.031 3.881 1.00 36.04 O ATOM 282 N VAL A 39 22.217 25.387 5.561 1.00 30.29 N ATOM 283 CA VAL A 39 21.740 24.921 6.858 1.00 28.04 C ATOM 284 C VAL A 39 22.688 25.208 8.001 1.00 28.76 C ATOM 285 O VAL A 39 22.249 25.612 9.079 1.00 29.24 O ATOM 286 CB VAL A 39 21.500 23.413 6.867 1.00 27.61 C ATOM 287 CG1 VAL A 39 20.493 23.070 7.911 1.00 31.92 C ATOM 288 CG2 VAL A 39 21.011 22.948 5.542 1.00 32.02 C ATOM 289 N ALA A 40 23.983 25.005 7.762 1.00 27.09 N ATOM 290 CA ALA A 40 25.001 25.205 8.791 1.00 25.12 C ATOM 291 C ALA A 40 25.110 26.652 9.225 1.00 24.93 C ATOM 292 O ALA A 40 25.220 26.944 10.416 1.00 25.52 O ATOM 293 CB ALA A 40 26.353 24.707 8.306 1.00 23.59 C ATOM 294 N LEU A 41 25.093 27.573 8.274 1.00 23.93 N ATOM 295 CA LEU A 41 25.207 28.970 8.657 1.00 23.03 C ATOM 296 C LEU A 41 23.909 29.531 9.215 1.00 24.96 C ATOM 297 O LEU A 41 23.937 30.437 10.040 1.00 27.46 O ATOM 298 CB LEU A 41 25.775 29.816 7.535 1.00 19.10 C ATOM 299 CG LEU A 41 27.207 29.415 7.166 1.00 19.20 C ATOM 300 CD1 LEU A 41 27.704 30.280 6.018 1.00 21.52 C ATOM 301 CD2 LEU A 41 28.139 29.544 8.345 1.00 15.61 C ATOM 302 N HIS A 42 22.769 28.975 8.822 1.00 24.89 N ATOM 303 CA HIS A 42 21.523 29.459 9.403 1.00 24.51 C ATOM 304 C HIS A 42 21.549 29.028 10.848 1.00 23.69 C ATOM 305 O HIS A 42 21.398 29.846 11.739 1.00 27.63 O ATOM 306 CB HIS A 42 20.294 28.854 8.744 1.00 28.41 C ATOM 307 CG HIS A 42 20.033 29.363 7.365 1.00 31.02 C ATOM 308 ND1 HIS A 42 18.947 28.956 6.613 1.00 36.32 N ATOM 309 CD2 HIS A 42 20.727 30.239 6.600 1.00 29.56 C ATOM 310 CE1 HIS A 42 18.991 29.569 5.440 1.00 35.41 C ATOM 311 NE2 HIS A 42 20.059 30.350 5.409 1.00 32.24 N ATOM 312 N ALA A 43 21.825 27.753 11.087 1.00 22.23 N ATOM 313 CA ALA A 43 21.855 27.262 12.448 1.00 19.62 C ATOM 314 C ALA A 43 22.843 28.070 13.251 1.00 21.22 C ATOM 315 O ALA A 43 22.501 28.552 14.319 1.00 26.43 O ATOM 316 CB ALA A 43 22.177 25.796 12.490 1.00 18.99 C ATOM 317 N LEU A 44 24.026 28.328 12.703 1.00 22.40 N ATOM 318 CA LEU A 44 25.027 29.114 13.438 1.00 22.69 C ATOM 319 C LEU A 44 24.527 30.519 13.776 1.00 24.10 C ATOM 320 O LEU A 44 24.678 30.982 14.907 1.00 26.06 O ATOM 321 CB LEU A 44 26.350 29.199 12.663 1.00 16.66 C ATOM 322 CG LEU A 44 27.404 30.156 13.232 1.00 14.73 C ATOM 323 CD1 LEU A 44 27.760 29.786 14.653 1.00 12.76 C ATOM 324 CD2 LEU A 44 28.649 30.132 12.368 1.00 12.68 C ATOM 325 N THR A 45 23.917 31.182 12.798 1.00 25.51 N ATOM 326 CA THR A 45 23.398 32.538 12.964 1.00 25.86 C ATOM 327 C THR A 45 22.402 32.642 14.121 1.00 28.14 C ATOM 328 O THR A 45 22.522 33.519 14.980 1.00 30.79 O ATOM 329 CB THR A 45 22.731 33.009 11.668 1.00 24.86 C ATOM 330 OG1 THR A 45 23.692 32.962 10.604 1.00 25.33 O ATOM 331 CG2 THR A 45 22.184 34.423 11.814 1.00 24.66 C ATOM 332 N ASP A 46 21.421 31.750 14.146 1.00 26.75 N ATOM 333 CA ASP A 46 20.434 31.743 15.205 1.00 24.52 C ATOM 334 C ASP A 46 21.069 31.557 16.563 1.00 24.69 C ATOM 335 O ASP A 46 20.557 32.044 17.559 1.00 25.32 O ATOM 336 CB ASP A 46 19.475 30.598 14.994 1.00 26.82 C ATOM 337 CG ASP A 46 18.305 30.970 14.149 1.00 30.17 C ATOM 338 OD1 ASP A 46 17.470 30.079 13.883 1.00 34.74 O ATOM 339 OD2 ASP A 46 18.208 32.143 13.761 1.00 30.76 O ATOM 340 N ALA A 47 22.145 30.784 16.618 1.00 24.43 N ATOM 341 CA ALA A 47 22.808 30.536 17.882 1.00 24.93 C ATOM 342 C ALA A 47 23.399 31.820 18.400 1.00 26.94 C ATOM 343 O ALA A 47 23.284 32.113 19.587 1.00 28.62 O ATOM 344 CB ALA A 47 23.874 29.500 17.724 1.00 26.61 C ATOM 345 N LEU A 48 24.029 32.583 17.505 1.00 28.67 N ATOM 346 CA LEU A 48 24.651 33.870 17.852 1.00 27.90 C ATOM 347 C LEU A 48 23.578 34.896 18.222 1.00 28.79 C ATOM 348 O LEU A 48 23.641 35.511 19.284 1.00 32.12 O ATOM 349 CB LEU A 48 25.496 34.380 16.687 1.00 25.91 C ATOM 350 CG LEU A 48 26.744 33.557 16.351 1.00 26.67 C ATOM 351 CD1 LEU A 48 27.262 33.963 14.997 1.00 25.57 C ATOM 352 CD2 LEU A 48 27.821 33.745 17.426 1.00 23.31 C ATOM 353 N LEU A 49 22.583 35.072 17.358 1.00 28.14 N ATOM 354 CA LEU A 49 21.487 35.993 17.643 1.00 26.15 C ATOM 355 C LEU A 49 20.826 35.549 18.942 1.00 26.40 C ATOM 356 O LEU A 49 20.511 36.373 19.785 1.00 28.17 O ATOM 357 CB LEU A 49 20.460 35.970 16.518 1.00 24.50 C ATOM 358 CG LEU A 49 20.932 36.598 15.215 1.00 23.51 C ATOM 359 CD1 LEU A 49 19.845 36.474 14.169 1.00 22.06 C ATOM 360 CD2 LEU A 49 21.297 38.055 15.456 1.00 20.33 C ATOM 361 N GLY A 50 20.650 34.242 19.107 1.00 26.69 N ATOM 362 CA GLY A 50 20.048 33.700 20.313 1.00 28.15 C ATOM 363 C GLY A 50 20.789 34.128 21.568 1.00 29.68 C ATOM 364 O GLY A 50 20.181 34.639 22.497 1.00 33.11 O ATOM 365 N ALA A 51 22.106 33.965 21.587 1.00 29.26 N ATOM 366 CA ALA A 51 22.901 34.359 22.737 1.00 28.13 C ATOM 367 C ALA A 51 22.905 35.875 22.924 1.00 29.71 C ATOM 368 O ALA A 51 23.142 36.370 24.017 1.00 32.11 O ATOM 369 CB ALA A 51 24.307 33.854 22.588 1.00 26.67 C ATOM 370 N ALA A 52 22.671 36.622 21.858 1.00 30.50 N ATOM 371 CA ALA A 52 22.653 38.078 21.956 1.00 30.50 C ATOM 372 C ALA A 52 21.269 38.570 22.320 1.00 30.01 C ATOM 373 O ALA A 52 21.080 39.748 22.579 1.00 34.80 O ATOM 374 CB ALA A 52 23.080 38.696 20.638 1.00 28.66 C ATOM 375 N ALA A 53 20.306 37.660 22.339 1.00 29.91 N ATOM 376 CA ALA A 53 18.904 37.971 22.632 1.00 28.51 C ATOM 377 C ALA A 53 18.317 38.844 21.538 1.00 28.42 C ATOM 378 O ALA A 53 17.545 39.755 21.812 1.00 31.64 O ATOM 379 CB ALA A 53 18.760 38.647 23.976 1.00 27.64 C ATOM 380 N LEU A 54 18.704 38.584 20.296 1.00 26.86 N ATOM 381 CA LEU A 54 18.191 39.355 19.183 1.00 24.75 C ATOM 382 C LEU A 54 17.143 38.580 18.397 1.00 25.21 C ATOM 383 O LEU A 54 16.660 39.034 17.364 1.00 27.05 O ATOM 384 CB LEU A 54 19.329 39.848 18.288 1.00 25.73 C ATOM 385 CG LEU A 54 20.369 40.761 18.962 1.00 24.74 C ATOM 386 CD1 LEU A 54 21.500 41.101 18.017 1.00 20.59 C ATOM 387 CD2 LEU A 54 19.698 42.018 19.421 1.00 23.57 C ATOM 388 N GLY A 55 16.735 37.439 18.923 1.00 26.88 N ATOM 389 CA GLY A 55 15.704 36.664 18.265 1.00 29.06 C ATOM 390 C GLY A 55 16.218 35.536 17.419 1.00 32.14 C ATOM 391 O GLY A 55 16.748 34.554 17.948 1.00 31.73 O ATOM 392 N ASP A 56 16.045 35.678 16.107 1.00 34.49 N ATOM 393 CA ASP A 56 16.468 34.675 15.145 1.00 36.60 C ATOM 394 C ASP A 56 16.633 35.266 13.735 1.00 38.92 C ATOM 395 O ASP A 56 16.233 36.405 13.469 1.00 40.18 O ATOM 396 CB ASP A 56 15.489 33.490 15.144 1.00 36.58 C ATOM 397 CG ASP A 56 14.094 33.861 14.653 1.00 37.68 C ATOM 398 OD1 ASP A 56 13.999 34.687 13.724 1.00 37.97 O ATOM 399 OD2 ASP A 56 13.090 33.310 15.169 1.00 37.56 O ATOM 400 N ILE A 57 17.152 34.455 12.820 1.00 40.46 N ATOM 401 CA ILE A 57 17.418 34.860 11.447 1.00 40.58 C ATOM 402 C ILE A 57 16.165 35.347 10.716 1.00 42.57 C ATOM 403 O ILE A 57 16.182 36.405 10.093 1.00 42.45 O ATOM 404 CB ILE A 57 18.151 33.714 10.672 1.00 37.87 C ATOM 405 CG1 ILE A 57 18.925 34.277 9.499 1.00 37.95 C ATOM 406 CG2 ILE A 57 17.185 32.653 10.173 1.00 36.56 C ATOM 407 CD1 ILE A 57 19.577 33.205 8.687 1.00 40.74 C ATOM 408 N GLY A 58 15.058 34.633 10.882 1.00 44.81 N ATOM 409 CA GLY A 58 13.822 35.010 10.220 1.00 50.33 C ATOM 410 C GLY A 58 13.205 36.289 10.752 1.00 54.11 C ATOM 411 O GLY A 58 12.212 36.779 10.218 1.00 56.15 O ATOM 412 N LYS A 59 13.736 36.790 11.855 1.00 57.85 N ATOM 413 CA LYS A 59 13.229 38.024 12.423 1.00 61.69 C ATOM 414 C LYS A 59 13.985 39.146 11.747 1.00 62.99 C ATOM 415 O LYS A 59 13.380 40.061 11.210 1.00 65.98 O ATOM 416 CB LYS A 59 13.457 38.071 13.936 1.00 64.55 C ATOM 417 CG LYS A 59 13.014 39.365 14.597 1.00 67.40 C ATOM 418 CD LYS A 59 13.396 39.378 16.062 1.00 71.44 C ATOM 419 CE LYS A 59 13.779 40.782 16.526 1.00 75.40 C ATOM 420 NZ LYS A 59 14.401 40.784 17.891 1.00 78.67 N ATOM 421 N LEU A 60 15.309 39.058 11.749 1.00 63.24 N ATOM 422 CA LEU A 60 16.133 40.082 11.120 1.00 64.25 C ATOM 423 C LEU A 60 16.016 40.129 9.592 1.00 66.25 C ATOM 424 O LEU A 60 15.972 41.211 9.005 1.00 67.84 O ATOM 425 CB LEU A 60 17.598 39.892 11.495 1.00 62.01 C ATOM 426 CG LEU A 60 18.060 40.343 12.873 1.00 60.09 C ATOM 427 CD1 LEU A 60 17.318 39.592 13.967 1.00 57.96 C ATOM 428 CD2 LEU A 60 19.562 40.113 12.955 1.00 59.64 C ATOM 429 N PHE A 61 16.000 38.963 8.952 1.00 67.62 N ATOM 430 CA PHE A 61 15.920 38.890 7.500 1.00 69.09 C ATOM 431 C PHE A 61 14.761 37.991 7.077 1.00 73.13 C ATOM 432 O PHE A 61 14.954 36.808 6.803 1.00 73.94 O ATOM 433 CB PHE A 61 17.234 38.341 6.923 1.00 67.05 C ATOM 434 CG PHE A 61 18.454 38.726 7.710 1.00 64.58 C ATOM 435 CD1 PHE A 61 18.883 40.041 7.756 1.00 63.51 C ATOM 436 CD2 PHE A 61 19.144 37.772 8.449 1.00 65.04 C ATOM 437 CE1 PHE A 61 19.977 40.403 8.533 1.00 64.54 C ATOM 438 CE2 PHE A 61 20.241 38.123 9.231 1.00 65.04 C ATOM 439 CZ PHE A 61 20.658 39.442 9.275 1.00 64.92 C ATOM 440 N PRO A 62 13.545 38.553 6.987 1.00 76.93 N ATOM 441 CA PRO A 62 12.313 37.860 6.601 1.00 80.94 C ATOM 442 C PRO A 62 12.389 36.898 5.417 1.00 85.73 C ATOM 443 O PRO A 62 12.815 37.256 4.313 1.00 85.79 O ATOM 444 CB PRO A 62 11.360 39.012 6.312 1.00 78.76 C ATOM 445 CG PRO A 62 11.733 39.980 7.360 1.00 78.88 C ATOM 446 CD PRO A 62 13.254 39.962 7.302 1.00 78.61 C ATOM 447 N ASP A 63 11.891 35.690 5.662 1.00 90.76 N ATOM 448 CA ASP A 63 11.839 34.617 4.671 1.00 94.44 C ATOM 449 C ASP A 63 11.080 35.118 3.431 1.00 96.02 C ATOM 450 O ASP A 63 11.437 34.811 2.288 1.00 96.14 O ATOM 451 CB ASP A 63 11.105 33.414 5.292 1.00 94.82 C ATOM 452 CG ASP A 63 11.585 32.074 4.749 1.00 94.81 C ATOM 453 OD1 ASP A 63 12.810 31.886 4.583 1.00 95.75 O ATOM 454 OD2 ASP A 63 10.733 31.191 4.518 1.00 94.23 O ATOM 455 N THR A 64 10.069 35.948 3.677 1.00 97.90 N ATOM 456 CA THR A 64 9.227 36.510 2.623 1.00 99.75 C ATOM 457 C THR A 64 9.799 37.716 1.868 1.00 99.98 C ATOM 458 O THR A 64 9.396 37.976 0.730 1.00100.00 O ATOM 459 CB THR A 64 7.839 36.890 3.180 1.00100.00 C ATOM 460 OG1 THR A 64 7.999 37.727 4.338 1.00100.00 O ATOM 461 CG2 THR A 64 7.050 35.633 3.554 1.00100.00 C ATOM 462 N ASP A 65 10.693 38.471 2.506 1.00 99.66 N ATOM 463 CA ASP A 65 11.294 39.632 1.856 1.00 99.22 C ATOM 464 C ASP A 65 12.095 39.097 0.660 1.00 99.82 C ATOM 465 O ASP A 65 13.013 38.271 0.823 1.00 99.02 O ATOM 466 CB ASP A 65 12.192 40.387 2.838 1.00 98.59 C ATOM 467 CG ASP A 65 12.582 41.774 2.343 1.00 98.43 C ATOM 468 OD1 ASP A 65 13.186 41.885 1.252 1.00 98.79 O ATOM 469 OD2 ASP A 65 12.299 42.757 3.060 1.00 97.43 O ATOM 470 N PRO A 66 11.716 39.521 -0.567 1.00100.00 N ATOM 471 CA PRO A 66 12.327 39.136 -1.850 1.00100.00 C ATOM 472 C PRO A 66 13.828 39.405 -2.053 1.00100.00 C ATOM 473 O PRO A 66 14.459 38.752 -2.893 1.00100.00 O ATOM 474 CB PRO A 66 11.464 39.879 -2.879 1.00100.00 C ATOM 475 CG PRO A 66 11.002 41.098 -2.129 1.00100.00 C ATOM 476 CD PRO A 66 10.638 40.509 -0.785 1.00100.00 C ATOM 477 N ALA A 67 14.401 40.339 -1.292 1.00 99.87 N ATOM 478 CA ALA A 67 15.830 40.661 -1.409 1.00 99.67 C ATOM 479 C ALA A 67 16.731 39.498 -0.941 1.00 98.83 C ATOM 480 O ALA A 67 17.858 39.310 -1.429 1.00 98.18 O ATOM 481 CB ALA A 67 16.143 41.932 -0.620 1.00 99.96 C ATOM 482 N PHE A 68 16.212 38.711 -0.004 1.00 96.83 N ATOM 483 CA PHE A 68 16.936 37.572 0.536 1.00 94.17 C ATOM 484 C PHE A 68 16.778 36.354 -0.359 1.00 92.77 C ATOM 485 O PHE A 68 17.168 35.247 0.019 1.00 92.99 O ATOM 486 CB PHE A 68 16.424 37.248 1.935 1.00 93.68 C ATOM 487 CG PHE A 68 16.255 38.449 2.796 1.00 92.75 C ATOM 488 CD1 PHE A 68 15.087 38.642 3.509 1.00 92.82 C ATOM 489 CD2 PHE A 68 17.256 39.411 2.870 1.00 92.49 C ATOM 490 CE1 PHE A 68 14.912 39.784 4.289 1.00 93.37 C ATOM 491 CE2 PHE A 68 17.091 40.557 3.646 1.00 93.07 C ATOM 492 CZ PHE A 68 15.914 40.744 4.358 1.00 92.90 C ATOM 493 N LYS A 69 16.170 36.541 -1.524 1.00 90.94 N ATOM 494 CA LYS A 69 15.979 35.438 -2.445 1.00 89.95 C ATOM 495 C LYS A 69 17.306 35.129 -3.140 1.00 88.12 C ATOM 496 O LYS A 69 17.767 35.883 -4.006 1.00 88.21 O ATOM 497 CB LYS A 69 14.896 35.762 -3.469 1.00 92.31 C ATOM 498 CG LYS A 69 14.495 34.562 -4.301 1.00 95.88 C ATOM 499 CD LYS A 69 14.257 34.956 -5.748 1.00 99.53 C ATOM 500 CE LYS A 69 14.335 33.738 -6.666 1.00100.00 C ATOM 501 NZ LYS A 69 14.309 34.114 -8.111 1.00100.00 N ATOM 502 N GLY A 70 17.916 34.024 -2.718 1.00 85.08 N ATOM 503 CA GLY A 70 19.190 33.584 -3.254 1.00 79.78 C ATOM 504 C GLY A 70 20.317 34.159 -2.419 1.00 76.22 C ATOM 505 O GLY A 70 21.492 33.883 -2.682 1.00 76.33 O ATOM 506 N ALA A 71 19.949 34.916 -1.380 1.00 72.78 N ATOM 507 CA ALA A 71 20.909 35.577 -0.488 1.00 69.50 C ATOM 508 C ALA A 71 22.010 34.676 0.079 1.00 66.00 C ATOM 509 O ALA A 71 21.754 33.572 0.574 1.00 69.09 O ATOM 510 CB ALA A 71 20.182 36.318 0.648 1.00 67.54 C ATOM 511 N ASP A 72 23.237 35.175 -0.015 1.00 58.89 N ATOM 512 CA ASP A 72 24.425 34.499 0.467 1.00 50.29 C ATOM 513 C ASP A 72 24.294 34.448 1.997 1.00 46.29 C ATOM 514 O ASP A 72 24.260 35.483 2.662 1.00 46.35 O ATOM 515 CB ASP A 72 25.624 35.328 -0.004 1.00 49.48 C ATOM 516 CG ASP A 72 26.937 34.867 0.559 1.00 51.87 C ATOM 517 OD1 ASP A 72 27.069 34.752 1.787 1.00 58.78 O ATOM 518 OD2 ASP A 72 27.891 34.698 -0.220 1.00 52.96 O ATOM 519 N SER A 73 24.162 33.249 2.552 1.00 40.41 N ATOM 520 CA SER A 73 24.021 33.107 3.988 1.00 36.55 C ATOM 521 C SER A 73 25.164 33.687 4.799 1.00 35.32 C ATOM 522 O SER A 73 25.001 33.946 5.994 1.00 37.10 O ATOM 523 CB SER A 73 23.797 31.656 4.374 1.00 37.80 C ATOM 524 OG SER A 73 22.470 31.246 4.085 1.00 39.02 O ATOM 525 N ARG A 74 26.329 33.854 4.186 1.00 32.72 N ATOM 526 CA ARG A 74 27.452 34.442 4.896 1.00 32.85 C ATOM 527 C ARG A 74 27.150 35.910 5.018 1.00 35.25 C ATOM 528 O ARG A 74 27.612 36.563 5.944 1.00 37.83 O ATOM 529 CB ARG A 74 28.768 34.262 4.157 1.00 30.87 C ATOM 530 CG ARG A 74 29.291 32.853 4.140 1.00 31.13 C ATOM 531 CD ARG A 74 30.595 32.794 3.374 1.00 33.89 C ATOM 532 NE ARG A 74 31.667 33.487 4.083 1.00 38.69 N ATOM 533 CZ ARG A 74 32.892 33.690 3.606 1.00 39.76 C ATOM 534 NH1 ARG A 74 33.793 34.322 4.348 1.00 43.59 N ATOM 535 NH2 ARG A 74 33.215 33.284 2.387 1.00 38.65 N ATOM 536 N GLU A 75 26.396 36.449 4.068 1.00 38.00 N ATOM 537 CA GLU A 75 26.025 37.855 4.137 1.00 41.91 C ATOM 538 C GLU A 75 25.140 38.052 5.352 1.00 40.94 C ATOM 539 O GLU A 75 25.371 38.949 6.155 1.00 43.39 O ATOM 540 CB GLU A 75 25.272 38.298 2.900 1.00 47.23 C ATOM 541 CG GLU A 75 26.137 38.858 1.805 1.00 57.23 C ATOM 542 CD GLU A 75 25.298 39.591 0.772 1.00 64.29 C ATOM 543 OE1 GLU A 75 25.021 40.792 0.997 1.00 67.70 O ATOM 544 OE2 GLU A 75 24.890 38.965 -0.239 1.00 67.50 O ATOM 545 N LEU A 76 24.134 37.202 5.501 1.00 38.04 N ATOM 546 CA LEU A 76 23.254 37.302 6.650 1.00 35.70 C ATOM 547 C LEU A 76 24.059 37.080 7.916 1.00 33.52 C ATOM 548 O LEU A 76 23.874 37.784 8.898 1.00 34.49 O ATOM 549 CB LEU A 76 22.138 36.271 6.568 1.00 39.63 C ATOM 550 CG LEU A 76 21.312 36.292 5.282 1.00 42.54 C ATOM 551 CD1 LEU A 76 20.119 35.376 5.446 1.00 44.33 C ATOM 552 CD2 LEU A 76 20.837 37.701 4.985 1.00 45.69 C ATOM 553 N LEU A 77 24.965 36.111 7.894 1.00 31.57 N ATOM 554 CA LEU A 77 25.777 35.842 9.067 1.00 30.39 C ATOM 555 C LEU A 77 26.556 37.075 9.496 1.00 31.14 C ATOM 556 O LEU A 77 26.525 37.455 10.662 1.00 32.46 O ATOM 557 CB LEU A 77 26.742 34.685 8.816 1.00 28.75 C ATOM 558 CG LEU A 77 27.762 34.433 9.937 1.00 28.05 C ATOM 559 CD1 LEU A 77 27.044 34.201 11.255 1.00 25.52 C ATOM 560 CD2 LEU A 77 28.659 33.258 9.589 1.00 22.53 C ATOM 561 N ARG A 78 27.223 37.722 8.549 1.00 32.65 N ATOM 562 CA ARG A 78 28.021 38.900 8.866 1.00 34.44 C ATOM 563 C ARG A 78 27.213 40.068 9.426 1.00 35.38 C ATOM 564 O ARG A 78 27.694 40.779 10.304 1.00 37.61 O ATOM 565 CB ARG A 78 28.841 39.339 7.657 1.00 34.46 C ATOM 566 CG ARG A 78 29.878 38.331 7.209 1.00 37.09 C ATOM 567 CD ARG A 78 30.672 38.838 6.015 1.00 40.02 C ATOM 568 NE ARG A 78 30.774 37.832 4.958 1.00 48.15 N ATOM 569 CZ ARG A 78 30.091 37.883 3.815 1.00 51.62 C ATOM 570 NH1 ARG A 78 30.229 36.923 2.897 1.00 54.51 N ATOM 571 NH2 ARG A 78 29.263 38.903 3.589 1.00 53.87 N ATOM 572 N GLU A 79 25.992 40.256 8.928 1.00 35.23 N ATOM 573 CA GLU A 79 25.115 41.323 9.397 1.00 36.05 C ATOM 574 C GLU A 79 24.666 41.023 10.818 1.00 38.06 C ATOM 575 O GLU A 79 24.827 41.850 11.716 1.00 40.86 O ATOM 576 CB GLU A 79 23.888 41.457 8.492 1.00 37.93 C ATOM 577 CG GLU A 79 22.874 42.523 8.922 1.00 43.20 C ATOM 578 CD GLU A 79 23.438 43.957 8.978 1.00 49.20 C ATOM 579 OE1 GLU A 79 24.641 44.191 8.707 1.00 52.30 O ATOM 580 OE2 GLU A 79 22.657 44.874 9.305 1.00 50.39 O ATOM 581 N ALA A 80 24.101 39.837 11.021 1.00 37.90 N ATOM 582 CA ALA A 80 23.653 39.421 12.335 1.00 35.54 C ATOM 583 C ALA A 80 24.800 39.616 13.308 1.00 36.02 C ATOM 584 O ALA A 80 24.589 40.058 14.433 1.00 37.90 O ATOM 585 CB ALA A 80 23.245 37.981 12.306 1.00 36.59 C ATOM 586 N TRP A 81 26.021 39.335 12.857 1.00 34.84 N ATOM 587 CA TRP A 81 27.202 39.501 13.702 1.00 34.08 C ATOM 588 C TRP A 81 27.513 40.981 13.943 1.00 37.02 C ATOM 589 O TRP A 81 27.911 41.367 15.041 1.00 37.25 O ATOM 590 CB TRP A 81 28.410 38.781 13.096 1.00 28.57 C ATOM 591 CG TRP A 81 29.659 38.869 13.918 1.00 25.44 C ATOM 592 CD1 TRP A 81 30.855 39.346 13.506 1.00 26.77 C ATOM 593 CD2 TRP A 81 29.830 38.498 15.301 1.00 24.78 C ATOM 594 NE1 TRP A 81 31.765 39.309 14.536 1.00 27.33 N ATOM 595 CE2 TRP A 81 31.162 38.794 15.648 1.00 23.97 C ATOM 596 CE3 TRP A 81 28.988 37.948 16.275 1.00 25.49 C ATOM 597 CZ2 TRP A 81 31.675 38.563 16.924 1.00 22.40 C ATOM 598 CZ3 TRP A 81 29.498 37.717 17.544 1.00 23.10 C ATOM 599 CH2 TRP A 81 30.830 38.025 17.855 1.00 23.72 C ATOM 600 N ARG A 82 27.320 41.814 12.926 1.00 39.86 N ATOM 601 CA ARG A 82 27.571 43.242 13.065 1.00 41.81 C ATOM 602 C ARG A 82 26.634 43.770 14.130 1.00 43.13 C ATOM 603 O ARG A 82 27.050 44.464 15.060 1.00 44.01 O ATOM 604 CB ARG A 82 27.288 43.978 11.760 1.00 44.88 C ATOM 605 CG ARG A 82 27.469 45.492 11.862 1.00 51.33 C ATOM 606 CD ARG A 82 26.946 46.249 10.625 1.00 55.23 C ATOM 607 NE ARG A 82 25.485 46.234 10.481 1.00 56.62 N ATOM 608 CZ ARG A 82 24.636 46.835 11.309 1.00 57.16 C ATOM 609 NH1 ARG A 82 23.333 46.763 11.082 1.00 58.31 N ATOM 610 NH2 ARG A 82 25.089 47.494 12.371 1.00 58.27 N ATOM 611 N ARG A 83 25.364 43.422 13.988 1.00 43.63 N ATOM 612 CA ARG A 83 24.345 43.853 14.923 1.00 45.45 C ATOM 613 C ARG A 83 24.636 43.347 16.325 1.00 46.09 C ATOM 614 O ARG A 83 24.457 44.079 17.310 1.00 48.29 O ATOM 615 CB ARG A 83 22.979 43.373 14.459 1.00 46.37 C ATOM 616 CG ARG A 83 22.706 43.775 13.048 1.00 52.37 C ATOM 617 CD ARG A 83 21.240 43.723 12.718 1.00 60.02 C ATOM 618 NE ARG A 83 21.063 44.018 11.303 1.00 66.19 N ATOM 619 CZ ARG A 83 19.895 44.084 10.671 1.00 69.32 C ATOM 620 NH1 ARG A 83 19.870 44.358 9.368 1.00 72.83 N ATOM 621 NH2 ARG A 83 18.761 43.870 11.334 1.00 72.50 N ATOM 622 N ILE A 84 25.114 42.110 16.414 1.00 43.31 N ATOM 623 CA ILE A 84 25.425 41.522 17.702 1.00 41.01 C ATOM 624 C ILE A 84 26.560 42.277 18.376 1.00 41.06 C ATOM 625 O ILE A 84 26.479 42.606 19.554 1.00 41.58 O ATOM 626 CB ILE A 84 25.775 40.028 17.554 1.00 41.01 C ATOM 627 CG1 ILE A 84 24.530 39.242 17.135 1.00 37.86 C ATOM 628 CG2 ILE A 84 26.346 39.478 18.852 1.00 39.70 C ATOM 629 CD1 ILE A 84 24.825 37.844 16.710 1.00 35.45 C ATOM 630 N GLN A 85 27.600 42.591 17.619 1.00 41.70 N ATOM 631 CA GLN A 85 28.739 43.305 18.176 1.00 44.62 C ATOM 632 C GLN A 85 28.338 44.687 18.651 1.00 45.56 C ATOM 633 O GLN A 85 28.828 45.167 19.675 1.00 46.65 O ATOM 634 CB GLN A 85 29.852 43.428 17.146 1.00 46.34 C ATOM 635 CG GLN A 85 30.418 42.104 16.693 1.00 51.43 C ATOM 636 CD GLN A 85 31.683 42.268 15.880 1.00 54.36 C ATOM 637 OE1 GLN A 85 32.789 42.110 16.397 1.00 57.50 O ATOM 638 NE2 GLN A 85 31.530 42.587 14.599 1.00 56.44 N ATOM 639 N ALA A 86 27.461 45.327 17.885 1.00 45.95 N ATOM 640 CA ALA A 86 26.965 46.658 18.207 1.00 45.73 C ATOM 641 C ALA A 86 26.253 46.628 19.538 1.00 46.82 C ATOM 642 O ALA A 86 26.351 47.575 20.303 1.00 50.37 O ATOM 643 CB ALA A 86 26.020 47.146 17.136 1.00 46.24 C ATOM 644 N LYS A 87 25.534 45.541 19.818 1.00 47.14 N ATOM 645 CA LYS A 87 24.830 45.409 21.091 1.00 45.26 C ATOM 646 C LYS A 87 25.865 45.210 22.220 1.00 44.28 C ATOM 647 O LYS A 87 25.503 45.017 23.380 1.00 44.29 O ATOM 648 CB LYS A 87 23.826 44.247 21.043 1.00 46.60 C ATOM 649 CG LYS A 87 22.704 44.342 22.089 1.00 51.56 C ATOM 650 CD LYS A 87 21.957 43.004 22.311 1.00 53.53 C ATOM 651 CE LYS A 87 20.940 43.086 23.475 1.00 54.41 C ATOM 652 NZ LYS A 87 20.820 41.817 24.280 1.00 52.49 N ATOM 653 N GLY A 88 27.149 45.231 21.861 1.00 42.24 N ATOM 654 CA GLY A 88 28.214 45.100 22.832 1.00 41.90 C ATOM 655 C GLY A 88 28.833 43.734 23.059 1.00 44.70 C ATOM 656 O GLY A 88 29.646 43.574 23.972 1.00 47.95 O ATOM 657 N TYR A 89 28.523 42.750 22.224 1.00 44.81 N ATOM 658 CA TYR A 89 29.079 41.418 22.442 1.00 41.14 C ATOM 659 C TYR A 89 30.343 41.116 21.653 1.00 40.19 C ATOM 660 O TYR A 89 30.662 41.801 20.686 1.00 40.57 O ATOM 661 CB TYR A 89 28.023 40.353 22.151 1.00 39.42 C ATOM 662 CG TYR A 89 26.771 40.490 22.978 1.00 37.02 C ATOM 663 CD1 TYR A 89 25.698 41.242 22.516 1.00 37.68 C ATOM 664 CD2 TYR A 89 26.639 39.836 24.202 1.00 34.82 C ATOM 665 CE1 TYR A 89 24.520 41.335 23.242 1.00 39.43 C ATOM 666 CE2 TYR A 89 25.464 39.924 24.943 1.00 36.55 C ATOM 667 CZ TYR A 89 24.402 40.674 24.451 1.00 40.43 C ATOM 668 OH TYR A 89 23.205 40.763 25.140 1.00 44.43 O ATOM 669 N THR A 90 31.081 40.113 22.118 1.00 39.81 N ATOM 670 CA THR A 90 32.303 39.646 21.472 1.00 40.28 C ATOM 671 C THR A 90 32.173 38.135 21.446 1.00 38.82 C ATOM 672 O THR A 90 31.545 37.557 22.333 1.00 39.78 O ATOM 673 CB THR A 90 33.575 40.028 22.253 1.00 40.25 C ATOM 674 OG1 THR A 90 33.448 39.634 23.623 1.00 44.55 O ATOM 675 CG2 THR A 90 33.794 41.500 22.195 1.00 40.88 C ATOM 676 N LEU A 91 32.759 37.498 20.443 1.00 36.74 N ATOM 677 CA LEU A 91 32.665 36.049 20.311 1.00 35.28 C ATOM 678 C LEU A 91 33.467 35.257 21.340 1.00 37.01 C ATOM 679 O LEU A 91 34.619 35.578 21.620 1.00 40.47 O ATOM 680 CB LEU A 91 33.105 35.620 18.917 1.00 29.08 C ATOM 681 CG LEU A 91 32.733 34.201 18.528 1.00 25.21 C ATOM 682 CD1 LEU A 91 31.266 34.188 18.173 1.00 27.56 C ATOM 683 CD2 LEU A 91 33.541 33.763 17.346 1.00 23.92 C ATOM 684 N GLY A 92 32.836 34.238 21.915 1.00 37.24 N ATOM 685 CA GLY A 92 33.504 33.369 22.867 1.00 34.94 C ATOM 686 C GLY A 92 33.987 32.243 21.979 1.00 34.60 C ATOM 687 O GLY A 92 35.179 32.068 21.775 1.00 38.02 O ATOM 688 N ASN A 93 33.039 31.511 21.407 1.00 32.07 N ATOM 689 CA ASN A 93 33.326 30.424 20.482 1.00 26.94 C ATOM 690 C ASN A 93 32.022 29.808 20.034 1.00 25.91 C ATOM 691 O ASN A 93 30.979 29.998 20.669 1.00 23.90 O ATOM 692 CB ASN A 93 34.199 29.357 21.108 1.00 27.02 C ATOM 693 CG ASN A 93 33.450 28.492 22.078 1.00 29.80 C ATOM 694 OD1 ASN A 93 33.345 27.286 21.888 1.00 28.34 O ATOM 695 ND2 ASN A 93 32.945 29.098 23.144 1.00 33.69 N ATOM 696 N VAL A 94 32.081 29.102 18.917 1.00 25.02 N ATOM 697 CA VAL A 94 30.917 28.447 18.356 1.00 24.27 C ATOM 698 C VAL A 94 31.265 26.997 18.031 1.00 24.45 C ATOM 699 O VAL A 94 32.449 26.645 17.868 1.00 27.29 O ATOM 700 CB VAL A 94 30.448 29.163 17.071 1.00 23.55 C ATOM 701 CG1 VAL A 94 30.331 30.654 17.322 1.00 22.32 C ATOM 702 CG2 VAL A 94 31.406 28.903 15.943 1.00 21.89 C ATOM 703 N ASP A 95 30.240 26.154 18.013 1.00 23.44 N ATOM 704 CA ASP A 95 30.392 24.745 17.688 1.00 21.25 C ATOM 705 C ASP A 95 29.179 24.382 16.863 1.00 22.63 C ATOM 706 O ASP A 95 28.036 24.684 17.259 1.00 25.02 O ATOM 707 CB ASP A 95 30.422 23.884 18.939 1.00 23.01 C ATOM 708 CG ASP A 95 30.791 22.452 18.639 1.00 26.62 C ATOM 709 OD1 ASP A 95 30.651 21.578 19.506 1.00 29.80 O ATOM 710 OD2 ASP A 95 31.223 22.167 17.513 1.00 32.05 O ATOM 711 N VAL A 96 29.430 23.797 15.694 1.00 19.17 N ATOM 712 CA VAL A 96 28.375 23.395 14.769 1.00 17.05 C ATOM 713 C VAL A 96 28.339 21.859 14.598 1.00 18.22 C ATOM 714 O VAL A 96 29.372 21.181 14.637 1.00 20.48 O ATOM 715 CB VAL A 96 28.592 24.083 13.407 1.00 15.66 C ATOM 716 CG1 VAL A 96 27.452 23.799 12.455 1.00 14.07 C ATOM 717 CG2 VAL A 96 28.738 25.563 13.606 1.00 12.94 C ATOM 718 N THR A 97 27.151 21.299 14.459 1.00 17.29 N ATOM 719 CA THR A 97 27.014 19.872 14.283 1.00 19.85 C ATOM 720 C THR A 97 26.105 19.693 13.097 1.00 23.19 C ATOM 721 O THR A 97 24.924 20.017 13.192 1.00 28.25 O ATOM 722 CB THR A 97 26.326 19.235 15.476 1.00 19.40 C ATOM 723 OG1 THR A 97 27.101 19.467 16.656 1.00 25.91 O ATOM 724 CG2 THR A 97 26.193 17.751 15.264 1.00 17.54 C ATOM 725 N ILE A 98 26.659 19.260 11.969 1.00 22.00 N ATOM 726 CA ILE A 98 25.885 19.032 10.753 1.00 20.74 C ATOM 727 C ILE A 98 25.366 17.612 10.820 1.00 22.10 C ATOM 728 O ILE A 98 26.138 16.671 11.029 1.00 26.94 O ATOM 729 CB ILE A 98 26.765 19.161 9.514 1.00 21.16 C ATOM 730 CG1 ILE A 98 27.372 20.563 9.462 1.00 20.63 C ATOM 731 CG2 ILE A 98 25.971 18.822 8.266 1.00 17.85 C ATOM 732 CD1 ILE A 98 28.524 20.693 8.513 1.00 21.51 C ATOM 733 N ILE A 99 24.062 17.451 10.684 1.00 20.82 N ATOM 734 CA ILE A 99 23.460 16.130 10.752 1.00 21.43 C ATOM 735 C ILE A 99 23.039 15.784 9.340 1.00 23.75 C ATOM 736 O ILE A 99 22.059 16.316 8.841 1.00 26.97 O ATOM 737 CB ILE A 99 22.244 16.135 11.687 1.00 17.80 C ATOM 738 CG1 ILE A 99 22.677 16.586 13.076 1.00 18.10 C ATOM 739 CG2 ILE A 99 21.659 14.770 11.782 1.00 14.32 C ATOM 740 CD1 ILE A 99 21.577 17.117 13.907 1.00 15.38 C ATOM 741 N ALA A 100 23.814 14.938 8.676 1.00 24.64 N ATOM 742 CA ALA A 100 23.513 14.548 7.310 1.00 26.07 C ATOM 743 C ALA A 100 24.065 13.159 7.064 1.00 29.22 C ATOM 744 O ALA A 100 25.136 12.819 7.573 1.00 30.46 O ATOM 745 CB ALA A 100 24.136 15.531 6.343 1.00 25.49 C ATOM 746 N GLN A 101 23.305 12.343 6.334 1.00 29.41 N ATOM 747 CA GLN A 101 23.718 10.977 6.003 1.00 29.10 C ATOM 748 C GLN A 101 24.779 11.078 4.918 1.00 27.91 C ATOM 749 O GLN A 101 25.688 10.262 4.827 1.00 29.56 O ATOM 750 CB GLN A 101 22.516 10.180 5.486 1.00 31.28 C ATOM 751 CG GLN A 101 22.748 8.697 5.291 1.00 30.93 C ATOM 752 CD GLN A 101 22.941 7.981 6.592 1.00 32.69 C ATOM 753 OE1 GLN A 101 23.689 7.010 6.677 1.00 38.81 O ATOM 754 NE2 GLN A 101 22.265 8.452 7.627 1.00 33.76 N ATOM 755 N ALA A 102 24.620 12.088 4.079 1.00 28.48 N ATOM 756 CA ALA A 102 25.529 12.375 2.986 1.00 27.81 C ATOM 757 C ALA A 102 25.083 13.737 2.487 1.00 28.36 C ATOM 758 O ALA A 102 23.899 14.070 2.616 1.00 29.75 O ATOM 759 CB ALA A 102 25.379 11.347 1.908 1.00 26.45 C ATOM 760 N PRO A 103 25.974 14.487 1.804 1.00 28.84 N ATOM 761 CA PRO A 103 27.359 14.139 1.465 1.00 28.46 C ATOM 762 C PRO A 103 28.347 14.116 2.628 1.00 31.59 C ATOM 763 O PRO A 103 27.978 14.392 3.772 1.00 35.44 O ATOM 764 CB PRO A 103 27.719 15.186 0.409 1.00 25.60 C ATOM 765 CG PRO A 103 26.919 16.358 0.801 1.00 25.38 C ATOM 766 CD PRO A 103 25.591 15.762 1.164 1.00 28.31 C ATOM 767 N LYS A 104 29.593 13.740 2.333 1.00 32.69 N ATOM 768 CA LYS A 104 30.657 13.662 3.340 1.00 30.58 C ATOM 769 C LYS A 104 31.136 15.073 3.641 1.00 30.14 C ATOM 770 O LYS A 104 31.777 15.709 2.804 1.00 34.01 O ATOM 771 CB LYS A 104 31.821 12.831 2.798 1.00 32.54 C ATOM 772 CG LYS A 104 32.845 12.424 3.840 1.00 37.79 C ATOM 773 CD LYS A 104 32.225 11.458 4.827 1.00 45.14 C ATOM 774 CE LYS A 104 33.218 10.983 5.881 1.00 49.57 C ATOM 775 NZ LYS A 104 32.616 9.902 6.738 1.00 54.87 N ATOM 776 N MET A 105 30.830 15.568 4.826 1.00 25.53 N ATOM 777 CA MET A 105 31.220 16.908 5.175 1.00 22.89 C ATOM 778 C MET A 105 32.675 16.990 5.539 1.00 24.55 C ATOM 779 O MET A 105 33.337 17.980 5.260 1.00 28.11 O ATOM 780 CB MET A 105 30.408 17.383 6.366 1.00 22.69 C ATOM 781 CG MET A 105 28.914 17.332 6.160 1.00 25.26 C ATOM 782 SD MET A 105 28.444 18.320 4.749 1.00 27.75 S ATOM 783 CE MET A 105 26.705 17.837 4.522 1.00 22.62 C ATOM 784 N LEU A 106 33.202 15.917 6.086 1.00 25.36 N ATOM 785 CA LEU A 106 34.572 15.931 6.569 1.00 29.44 C ATOM 786 C LEU A 106 35.654 16.702 5.825 1.00 29.32 C ATOM 787 O LEU A 106 36.290 17.581 6.387 1.00 31.29 O ATOM 788 CB LEU A 106 35.067 14.523 6.881 1.00 33.70 C ATOM 789 CG LEU A 106 36.272 14.558 7.833 1.00 37.95 C ATOM 790 CD1 LEU A 106 35.946 15.379 9.101 1.00 38.15 C ATOM 791 CD2 LEU A 106 36.670 13.140 8.204 1.00 40.76 C ATOM 792 N PRO A 107 35.876 16.399 4.553 1.00 29.19 N ATOM 793 CA PRO A 107 36.923 17.129 3.835 1.00 29.15 C ATOM 794 C PRO A 107 36.714 18.626 3.636 1.00 29.69 C ATOM 795 O PRO A 107 37.662 19.355 3.328 1.00 29.34 O ATOM 796 CB PRO A 107 36.976 16.394 2.496 1.00 30.23 C ATOM 797 CG PRO A 107 35.576 15.890 2.320 1.00 28.09 C ATOM 798 CD PRO A 107 35.246 15.384 3.694 1.00 29.61 C ATOM 799 N HIS A 108 35.476 19.081 3.794 1.00 30.02 N ATOM 800 CA HIS A 108 35.138 20.487 3.586 1.00 29.58 C ATOM 801 C HIS A 108 35.161 21.340 4.843 1.00 30.69 C ATOM 802 O HIS A 108 35.093 22.569 4.779 1.00 32.65 O ATOM 803 CB HIS A 108 33.765 20.575 2.947 1.00 27.33 C ATOM 804 CG HIS A 108 33.623 19.716 1.738 1.00 26.43 C ATOM 805 ND1 HIS A 108 34.233 20.012 0.540 1.00 28.00 N ATOM 806 CD2 HIS A 108 32.974 18.545 1.550 1.00 28.75 C ATOM 807 CE1 HIS A 108 33.970 19.058 -0.336 1.00 27.12 C ATOM 808 NE2 HIS A 108 33.208 18.155 0.253 1.00 31.32 N ATOM 809 N ILE A 109 35.302 20.697 5.987 1.00 28.24 N ATOM 810 CA ILE A 109 35.298 21.413 7.234 1.00 23.92 C ATOM 811 C ILE A 109 36.402 22.425 7.451 1.00 26.23 C ATOM 812 O ILE A 109 36.133 23.509 7.958 1.00 32.63 O ATOM 813 CB ILE A 109 35.141 20.442 8.395 1.00 22.78 C ATOM 814 CG1 ILE A 109 33.726 19.857 8.338 1.00 20.82 C ATOM 815 CG2 ILE A 109 35.385 21.131 9.708 1.00 19.58 C ATOM 816 CD1 ILE A 109 33.548 18.605 9.093 1.00 21.50 C ATOM 817 N PRO A 110 37.652 22.124 7.065 1.00 26.64 N ATOM 818 CA PRO A 110 38.704 23.125 7.282 1.00 25.96 C ATOM 819 C PRO A 110 38.341 24.434 6.607 1.00 27.69 C ATOM 820 O PRO A 110 38.423 25.511 7.215 1.00 27.07 O ATOM 821 CB PRO A 110 39.905 22.494 6.608 1.00 24.86 C ATOM 822 CG PRO A 110 39.689 21.056 6.846 1.00 24.40 C ATOM 823 CD PRO A 110 38.229 20.895 6.505 1.00 27.77 C ATOM 824 N GLN A 111 37.909 24.321 5.352 1.00 29.37 N ATOM 825 CA GLN A 111 37.500 25.481 4.566 1.00 29.01 C ATOM 826 C GLN A 111 36.259 26.131 5.182 1.00 30.54 C ATOM 827 O GLN A 111 36.150 27.351 5.196 1.00 35.14 O ATOM 828 CB GLN A 111 37.243 25.071 3.120 1.00 26.32 C ATOM 829 CG GLN A 111 37.017 26.226 2.172 1.00 24.89 C ATOM 830 CD GLN A 111 38.087 27.278 2.259 1.00 23.81 C ATOM 831 OE1 GLN A 111 37.789 28.452 2.372 1.00 31.55 O ATOM 832 NE2 GLN A 111 39.338 26.867 2.229 1.00 26.26 N ATOM 833 N MET A 112 35.333 25.320 5.696 1.00 30.78 N ATOM 834 CA MET A 112 34.124 25.831 6.345 1.00 27.53 C ATOM 835 C MET A 112 34.560 26.700 7.500 1.00 28.92 C ATOM 836 O MET A 112 34.046 27.804 7.677 1.00 31.65 O ATOM 837 CB MET A 112 33.280 24.694 6.913 1.00 27.13 C ATOM 838 CG MET A 112 32.235 24.127 5.984 1.00 25.22 C ATOM 839 SD MET A 112 31.275 22.888 6.846 1.00 25.29 S ATOM 840 CE MET A 112 30.638 22.029 5.536 1.00 24.12 C ATOM 841 N ARG A 113 35.529 26.211 8.274 1.00 28.19 N ATOM 842 CA ARG A 113 36.040 26.957 9.426 1.00 29.54 C ATOM 843 C ARG A 113 36.761 28.246 9.060 1.00 31.05 C ATOM 844 O ARG A 113 36.826 29.161 9.869 1.00 33.27 O ATOM 845 CB ARG A 113 36.968 26.099 10.270 1.00 25.68 C ATOM 846 CG ARG A 113 36.273 25.006 10.983 1.00 23.70 C ATOM 847 CD ARG A 113 37.267 24.163 11.680 1.00 22.63 C ATOM 848 NE ARG A 113 37.843 24.852 12.819 1.00 24.17 N ATOM 849 CZ ARG A 113 39.027 24.549 13.340 1.00 26.90 C ATOM 850 NH1 ARG A 113 39.487 25.205 14.401 1.00 24.81 N ATOM 851 NH2 ARG A 113 39.776 23.618 12.760 1.00 27.84 N ATOM 852 N VAL A 114 37.350 28.293 7.871 1.00 31.23 N ATOM 853 CA VAL A 114 38.063 29.476 7.405 1.00 29.99 C ATOM 854 C VAL A 114 37.057 30.581 7.092 1.00 31.42 C ATOM 855 O VAL A 114 37.240 31.737 7.484 1.00 33.80 O ATOM 856 CB VAL A 114 38.876 29.140 6.155 1.00 29.99 C ATOM 857 CG1 VAL A 114 39.383 30.393 5.498 1.00 29.97 C ATOM 858 CG2 VAL A 114 40.021 28.209 6.522 1.00 29.75 C ATOM 859 N PHE A 115 35.990 30.207 6.397 1.00 29.02 N ATOM 860 CA PHE A 115 34.933 31.135 6.048 1.00 27.18 C ATOM 861 C PHE A 115 34.258 31.694 7.290 1.00 28.13 C ATOM 862 O PHE A 115 34.139 32.903 7.443 1.00 29.19 O ATOM 863 CB PHE A 115 33.887 30.422 5.214 1.00 23.61 C ATOM 864 CG PHE A 115 34.290 30.215 3.806 1.00 22.50 C ATOM 865 CD1 PHE A 115 33.589 29.341 2.997 1.00 24.86 C ATOM 866 CD2 PHE A 115 35.322 30.947 3.257 1.00 23.68 C ATOM 867 CE1 PHE A 115 33.908 29.212 1.664 1.00 22.96 C ATOM 868 CE2 PHE A 115 35.649 30.821 1.917 1.00 22.85 C ATOM 869 CZ PHE A 115 34.937 29.955 1.123 1.00 22.00 C ATOM 870 N ILE A 116 33.803 30.807 8.169 1.00 27.94 N ATOM 871 CA ILE A 116 33.129 31.227 9.387 1.00 27.20 C ATOM 872 C ILE A 116 33.996 32.128 10.251 1.00 27.34 C ATOM 873 O ILE A 116 33.555 33.185 10.664 1.00 30.09 O ATOM 874 CB ILE A 116 32.650 30.028 10.218 1.00 26.48 C ATOM 875 CG1 ILE A 116 31.599 29.235 9.436 1.00 26.91 C ATOM 876 CG2 ILE A 116 32.060 30.511 11.522 1.00 26.73 C ATOM 877 CD1 ILE A 116 31.164 27.945 10.105 1.00 23.85 C ATOM 878 N ALA A 117 35.230 31.727 10.519 1.00 28.85 N ATOM 879 CA ALA A 117 36.123 32.535 11.350 1.00 30.45 C ATOM 880 C ALA A 117 36.358 33.877 10.706 1.00 32.39 C ATOM 881 O ALA A 117 36.632 34.854 11.388 1.00 33.20 O ATOM 882 CB ALA A 117 37.439 31.834 11.571 1.00 31.08 C ATOM 883 N GLU A 118 36.305 33.912 9.381 1.00 35.98 N ATOM 884 CA GLU A 118 36.475 35.168 8.670 1.00 37.92 C ATOM 885 C GLU A 118 35.272 36.039 8.986 1.00 36.35 C ATOM 886 O GLU A 118 35.413 37.090 9.592 1.00 35.36 O ATOM 887 CB GLU A 118 36.563 34.950 7.158 1.00 42.92 C ATOM 888 CG GLU A 118 37.970 34.659 6.628 1.00 51.90 C ATOM 889 CD GLU A 118 38.066 34.762 5.098 1.00 56.76 C ATOM 890 OE1 GLU A 118 39.155 34.434 4.572 1.00 58.80 O ATOM 891 OE2 GLU A 118 37.066 35.161 4.426 1.00 56.13 O ATOM 892 N ASP A 119 34.088 35.553 8.622 1.00 35.47 N ATOM 893 CA ASP A 119 32.837 36.262 8.845 1.00 33.93 C ATOM 894 C ASP A 119 32.658 36.743 10.282 1.00 34.15 C ATOM 895 O ASP A 119 32.042 37.779 10.520 1.00 36.18 O ATOM 896 CB ASP A 119 31.658 35.370 8.471 1.00 35.10 C ATOM 897 CG ASP A 119 31.610 35.033 6.996 1.00 37.67 C ATOM 898 OD1 ASP A 119 30.794 34.161 6.637 1.00 38.81 O ATOM 899 OD2 ASP A 119 32.356 35.635 6.187 1.00 35.75 O ATOM 900 N LEU A 120 33.181 35.983 11.238 1.00 32.94 N ATOM 901 CA LEU A 120 33.057 36.333 12.646 1.00 32.55 C ATOM 902 C LEU A 120 34.245 37.136 13.146 1.00 34.93 C ATOM 903 O LEU A 120 34.213 37.687 14.245 1.00 37.86 O ATOM 904 CB LEU A 120 32.908 35.069 13.493 1.00 29.86 C ATOM 905 CG LEU A 120 31.676 34.214 13.211 1.00 28.39 C ATOM 906 CD1 LEU A 120 31.666 33.004 14.124 1.00 27.63 C ATOM 907 CD2 LEU A 120 30.427 35.048 13.405 1.00 27.40 C ATOM 908 N GLY A 121 35.311 37.162 12.357 1.00 36.43 N ATOM 909 CA GLY A 121 36.501 37.894 12.740 1.00 35.75 C ATOM 910 C GLY A 121 37.178 37.320 13.962 1.00 37.82 C ATOM 911 O GLY A 121 37.576 38.074 14.845 1.00 42.07 O ATOM 912 N CYS A 122 37.318 35.998 14.020 1.00 38.40 N ATOM 913 CA CYS A 122 37.964 35.328 15.153 1.00 39.41 C ATOM 914 C CYS A 122 39.015 34.398 14.596 1.00 41.74 C ATOM 915 O CYS A 122 39.247 34.392 13.392 1.00 43.67 O ATOM 916 CB CYS A 122 36.945 34.507 15.937 1.00 37.17 C ATOM 917 SG CYS A 122 36.146 33.232 14.975 1.00 31.14 S ATOM 918 N HIS A 123 39.668 33.626 15.457 1.00 45.03 N ATOM 919 CA HIS A 123 40.664 32.677 14.974 1.00 50.03 C ATOM 920 C HIS A 123 39.840 31.441 14.716 1.00 46.69 C ATOM 921 O HIS A 123 38.776 31.270 15.299 1.00 45.10 O ATOM 922 CB HIS A 123 41.734 32.311 16.024 1.00 64.56 C ATOM 923 CG HIS A 123 42.050 33.404 17.009 1.00 81.64 C ATOM 924 ND1 HIS A 123 43.342 33.812 17.280 1.00 88.26 N ATOM 925 CD2 HIS A 123 41.248 34.139 17.823 1.00 86.90 C ATOM 926 CE1 HIS A 123 43.323 34.746 18.218 1.00 90.93 C ATOM 927 NE2 HIS A 123 42.064 34.963 18.564 1.00 91.75 N ATOM 928 N MET A 124 40.338 30.567 13.858 1.00 44.77 N ATOM 929 CA MET A 124 39.632 29.336 13.564 1.00 42.57 C ATOM 930 C MET A 124 39.483 28.572 14.858 1.00 42.03 C ATOM 931 O MET A 124 38.580 27.759 14.996 1.00 44.04 O ATOM 932 CB MET A 124 40.436 28.462 12.608 1.00 42.31 C ATOM 933 CG MET A 124 40.263 28.742 11.150 1.00 43.76 C ATOM 934 SD MET A 124 41.359 27.661 10.222 1.00 47.19 S ATOM 935 CE MET A 124 40.461 26.135 10.250 1.00 48.89 C ATOM 936 N ASP A 125 40.390 28.815 15.795 1.00 40.95 N ATOM 937 CA ASP A 125 40.380 28.108 17.067 1.00 42.02 C ATOM 938 C ASP A 125 39.104 28.317 17.864 1.00 38.07 C ATOM 939 O ASP A 125 38.752 27.507 18.714 1.00 36.19 O ATOM 940 CB ASP A 125 41.595 28.509 17.901 1.00 52.60 C ATOM 941 CG ASP A 125 42.101 27.372 18.789 1.00 63.14 C ATOM 942 OD1 ASP A 125 43.305 27.042 18.650 1.00 69.07 O ATOM 943 OD2 ASP A 125 41.318 26.806 19.613 1.00 65.60 O ATOM 944 N ASP A 126 38.406 29.406 17.588 1.00 34.39 N ATOM 945 CA ASP A 126 37.167 29.689 18.278 1.00 30.28 C ATOM 946 C ASP A 126 35.999 29.156 17.484 1.00 28.73 C ATOM 947 O ASP A 126 34.850 29.413 17.825 1.00 31.02 O ATOM 948 CB ASP A 126 37.005 31.185 18.444 1.00 31.50 C ATOM 949 CG ASP A 126 38.133 31.795 19.202 1.00 34.50 C ATOM 950 OD1 ASP A 126 38.444 32.966 18.917 1.00 39.77 O ATOM 951 OD2 ASP A 126 38.727 31.103 20.062 1.00 36.20 O ATOM 952 N VAL A 127 36.288 28.406 16.429 1.00 25.83 N ATOM 953 CA VAL A 127 35.256 27.862 15.569 1.00 23.89 C ATOM 954 C VAL A 127 35.464 26.383 15.303 1.00 24.47 C ATOM 955 O VAL A 127 36.514 25.970 14.813 1.00 24.00 O ATOM 956 CB VAL A 127 35.231 28.599 14.223 1.00 22.97 C ATOM 957 CG1 VAL A 127 34.192 27.997 13.327 1.00 26.09 C ATOM 958 CG2 VAL A 127 34.927 30.066 14.434 1.00 23.33 C ATOM 959 N ASN A 128 34.450 25.587 15.607 1.00 25.25 N ATOM 960 CA ASN A 128 34.511 24.149 15.381 1.00 25.99 C ATOM 961 C ASN A 128 33.279 23.687 14.585 1.00 25.09 C ATOM 962 O ASN A 128 32.193 24.257 14.719 1.00 26.50 O ATOM 963 CB ASN A 128 34.586 23.420 16.724 1.00 29.64 C ATOM 964 CG ASN A 128 34.928 21.949 16.575 1.00 30.61 C ATOM 965 OD1 ASN A 128 36.071 21.590 16.308 1.00 33.30 O ATOM 966 ND2 ASN A 128 33.945 21.092 16.773 1.00 33.38 N ATOM 967 N VAL A 129 33.465 22.714 13.699 1.00 22.54 N ATOM 968 CA VAL A 129 32.365 22.176 12.906 1.00 19.85 C ATOM 969 C VAL A 129 32.556 20.666 12.887 1.00 21.67 C ATOM 970 O VAL A 129 33.684 20.192 12.828 1.00 23.70 O ATOM 971 CB VAL A 129 32.386 22.684 11.461 1.00 15.64 C ATOM 972 CG1 VAL A 129 31.288 22.028 10.675 1.00 17.08 C ATOM 973 CG2 VAL A 129 32.201 24.169 11.417 1.00 13.92 C ATOM 974 N LYS A 130 31.479 19.907 13.019 1.00 21.70 N ATOM 975 CA LYS A 130 31.590 18.455 12.989 1.00 23.02 C ATOM 976 C LYS A 130 30.381 17.939 12.258 1.00 24.73 C ATOM 977 O LYS A 130 29.464 18.716 11.965 1.00 27.86 O ATOM 978 CB LYS A 130 31.653 17.873 14.397 1.00 24.96 C ATOM 979 CG LYS A 130 30.365 17.939 15.183 1.00 26.97 C ATOM 980 CD LYS A 130 30.584 17.490 16.613 1.00 24.71 C ATOM 981 CE LYS A 130 31.087 18.625 17.452 1.00 22.91 C ATOM 982 NZ LYS A 130 30.057 19.691 17.524 1.00 21.04 N ATOM 983 N ALA A 131 30.356 16.647 11.962 1.00 23.88 N ATOM 984 CA ALA A 131 29.226 16.088 11.244 1.00 22.87 C ATOM 985 C ALA A 131 28.834 14.733 11.789 1.00 25.34 C ATOM 986 O ALA A 131 29.617 14.085 12.497 1.00 25.97 O ATOM 987 CB ALA A 131 29.556 15.982 9.779 1.00 21.64 C ATOM 988 N THR A 132 27.601 14.327 11.503 1.00 25.94 N ATOM 989 CA THR A 132 27.124 13.030 11.933 1.00 28.47 C ATOM 990 C THR A 132 25.956 12.589 11.077 1.00 28.81 C ATOM 991 O THR A 132 25.256 13.418 10.497 1.00 29.53 O ATOM 992 CB THR A 132 26.683 13.043 13.400 1.00 31.26 C ATOM 993 OG1 THR A 132 26.505 11.694 13.850 1.00 37.32 O ATOM 994 CG2 THR A 132 25.367 13.788 13.564 1.00 32.90 C ATOM 995 N THR A 133 25.770 11.280 10.963 1.00 29.72 N ATOM 996 CA THR A 133 24.648 10.751 10.195 1.00 29.86 C ATOM 997 C THR A 133 23.670 10.285 11.243 1.00 30.68 C ATOM 998 O THR A 133 24.014 10.198 12.425 1.00 32.02 O ATOM 999 CB THR A 133 25.012 9.503 9.346 1.00 28.71 C ATOM 1000 OG1 THR A 133 25.238 8.382 10.199 1.00 27.75 O ATOM 1001 CG2 THR A 133 26.238 9.729 8.509 1.00 27.82 C ATOM 1002 N THR A 134 22.455 9.982 10.824 1.00 29.98 N ATOM 1003 CA THR A 134 21.474 9.476 11.766 1.00 31.97 C ATOM 1004 C THR A 134 21.234 7.975 11.487 1.00 34.41 C ATOM 1005 O THR A 134 20.143 7.435 11.703 1.00 36.08 O ATOM 1006 CB THR A 134 20.210 10.303 11.697 1.00 29.14 C ATOM 1007 OG1 THR A 134 19.783 10.397 10.338 1.00 31.67 O ATOM 1008 CG2 THR A 134 20.513 11.684 12.174 1.00 26.94 C ATOM 1009 N GLU A 135 22.282 7.328 10.974 1.00 34.44 N ATOM 1010 CA GLU A 135 22.301 5.904 10.649 1.00 34.92 C ATOM 1011 C GLU A 135 21.115 5.424 9.838 1.00 32.81 C ATOM 1012 O GLU A 135 20.434 4.476 10.202 1.00 33.96 O ATOM 1013 CB GLU A 135 22.448 5.092 11.926 1.00 37.94 C ATOM 1014 CG GLU A 135 23.610 5.554 12.782 1.00 46.91 C ATOM 1015 CD GLU A 135 24.759 4.578 12.776 1.00 53.68 C ATOM 1016 OE1 GLU A 135 25.908 5.005 12.500 1.00 54.16 O ATOM 1017 OE2 GLU A 135 24.504 3.383 13.078 1.00 59.91 O ATOM 1018 N LYS A 136 20.891 6.080 8.711 1.00 32.41 N ATOM 1019 CA LYS A 136 19.792 5.743 7.825 1.00 32.02 C ATOM 1020 C LYS A 136 18.402 5.952 8.413 1.00 31.66 C ATOM 1021 O LYS A 136 17.406 5.706 7.741 1.00 34.88 O ATOM 1022 CB LYS A 136 19.952 4.325 7.307 1.00 33.56 C ATOM 1023 CG LYS A 136 21.043 4.174 6.273 1.00 38.46 C ATOM 1024 CD LYS A 136 20.608 4.810 4.980 1.00 46.59 C ATOM 1025 CE LYS A 136 21.547 4.452 3.838 1.00 54.78 C ATOM 1026 NZ LYS A 136 21.009 4.962 2.534 1.00 60.41 N ATOM 1027 N LEU A 137 18.329 6.448 9.642 1.00 29.30 N ATOM 1028 CA LEU A 137 17.052 6.714 10.278 1.00 26.15 C ATOM 1029 C LEU A 137 16.616 8.166 10.044 1.00 26.29 C ATOM 1030 O LEU A 137 17.451 9.080 9.977 1.00 27.61 O ATOM 1031 CB LEU A 137 17.161 6.485 11.784 1.00 25.03 C ATOM 1032 CG LEU A 137 17.562 5.102 12.264 1.00 21.54 C ATOM 1033 CD1 LEU A 137 17.596 5.086 13.761 1.00 21.89 C ATOM 1034 CD2 LEU A 137 16.552 4.130 11.780 1.00 19.81 C ATOM 1035 N GLY A 138 15.306 8.369 9.924 1.00 23.39 N ATOM 1036 CA GLY A 138 14.758 9.705 9.761 1.00 21.88 C ATOM 1037 C GLY A 138 14.825 10.366 8.405 1.00 24.04 C ATOM 1038 O GLY A 138 15.345 9.791 7.455 1.00 27.06 O ATOM 1039 N PHE A 139 14.312 11.590 8.309 1.00 22.08 N ATOM 1040 CA PHE A 139 14.326 12.275 7.037 1.00 21.96 C ATOM 1041 C PHE A 139 15.752 12.493 6.593 1.00 23.69 C ATOM 1042 O PHE A 139 16.040 12.523 5.411 1.00 25.47 O ATOM 1043 CB PHE A 139 13.520 13.573 7.081 1.00 22.31 C ATOM 1044 CG PHE A 139 14.159 14.694 7.866 1.00 25.89 C ATOM 1045 CD1 PHE A 139 15.099 15.530 7.280 1.00 26.36 C ATOM 1046 CD2 PHE A 139 13.766 14.963 9.168 1.00 23.00 C ATOM 1047 CE1 PHE A 139 15.626 16.606 7.975 1.00 23.91 C ATOM 1048 CE2 PHE A 139 14.297 16.046 9.865 1.00 19.11 C ATOM 1049 CZ PHE A 139 15.223 16.862 9.266 1.00 20.65 C ATOM 1050 N THR A 140 16.656 12.598 7.555 1.00 25.92 N ATOM 1051 CA THR A 140 18.061 12.789 7.247 1.00 27.92 C ATOM 1052 C THR A 140 18.615 11.449 6.802 1.00 30.25 C ATOM 1053 O THR A 140 19.300 11.370 5.784 1.00 32.63 O ATOM 1054 CB THR A 140 18.852 13.277 8.473 1.00 25.74 C ATOM 1055 OG1 THR A 140 18.504 12.475 9.610 1.00 29.71 O ATOM 1056 CG2 THR A 140 18.549 14.734 8.760 1.00 23.98 C ATOM 1057 N GLY A 141 18.311 10.399 7.566 1.00 30.57 N ATOM 1058 CA GLY A 141 18.783 9.066 7.236 1.00 27.52 C ATOM 1059 C GLY A 141 18.269 8.621 5.887 1.00 28.40 C ATOM 1060 O GLY A 141 18.932 7.879 5.169 1.00 31.36 O ATOM 1061 N ARG A 142 17.101 9.115 5.512 1.00 27.14 N ATOM 1062 CA ARG A 142 16.529 8.752 4.237 1.00 26.43 C ATOM 1063 C ARG A 142 17.001 9.662 3.120 1.00 27.65 C ATOM 1064 O ARG A 142 16.570 9.537 1.976 1.00 30.73 O ATOM 1065 CB ARG A 142 15.022 8.774 4.315 1.00 24.81 C ATOM 1066 CG ARG A 142 14.487 7.713 5.206 1.00 27.61 C ATOM 1067 CD ARG A 142 13.017 7.558 4.976 1.00 30.19 C ATOM 1068 NE ARG A 142 12.382 8.836 5.192 1.00 30.84 N ATOM 1069 CZ ARG A 142 11.960 9.248 6.373 1.00 33.19 C ATOM 1070 NH1 ARG A 142 11.412 10.443 6.498 1.00 36.93 N ATOM 1071 NH2 ARG A 142 12.061 8.443 7.417 1.00 34.52 N ATOM 1072 N GLY A 143 17.873 10.596 3.451 1.00 26.31 N ATOM 1073 CA GLY A 143 18.382 11.491 2.436 1.00 26.04 C ATOM 1074 C GLY A 143 17.366 12.493 1.954 1.00 26.67 C ATOM 1075 O GLY A 143 17.518 13.039 0.853 1.00 31.16 O ATOM 1076 N GLU A 144 16.348 12.753 2.768 1.00 25.56 N ATOM 1077 CA GLU A 144 15.309 13.705 2.423 1.00 22.74 C ATOM 1078 C GLU A 144 15.751 15.137 2.642 1.00 23.10 C ATOM 1079 O GLU A 144 15.248 16.038 1.978 1.00 24.19 O ATOM 1080 CB GLU A 144 14.054 13.424 3.221 1.00 22.07 C ATOM 1081 CG GLU A 144 13.480 12.061 2.943 1.00 25.86 C ATOM 1082 CD GLU A 144 12.239 11.751 3.758 1.00 30.35 C ATOM 1083 OE1 GLU A 144 11.601 10.711 3.465 1.00 29.02 O ATOM 1084 OE2 GLU A 144 11.898 12.525 4.698 1.00 33.79 O ATOM 1085 N GLY A 145 16.704 15.348 3.546 1.00 21.95 N ATOM 1086 CA GLY A 145 17.183 16.695 3.820 1.00 21.94 C ATOM 1087 C GLY A 145 18.362 16.701 4.766 1.00 23.67 C ATOM 1088 O GLY A 145 18.848 15.640 5.154 1.00 27.13 O ATOM 1089 N ILE A 146 18.868 17.882 5.098 1.00 23.66 N ATOM 1090 CA ILE A 146 20.004 17.995 6.011 1.00 22.98 C ATOM 1091 C ILE A 146 19.515 18.842 7.163 1.00 23.17 C ATOM 1092 O ILE A 146 18.695 19.738 6.973 1.00 27.99 O ATOM 1093 CB ILE A 146 21.224 18.739 5.382 1.00 22.94 C ATOM 1094 CG1 ILE A 146 21.852 17.946 4.255 1.00 23.49 C ATOM 1095 CG2 ILE A 146 22.337 18.889 6.388 1.00 26.90 C ATOM 1096 CD1 ILE A 146 23.118 18.578 3.774 1.00 25.00 C ATOM 1097 N ALA A 147 20.007 18.561 8.356 1.00 20.78 N ATOM 1098 CA ALA A 147 19.635 19.321 9.530 1.00 18.10 C ATOM 1099 C ALA A 147 20.958 19.749 10.105 1.00 18.07 C ATOM 1100 O ALA A 147 21.989 19.230 9.713 1.00 20.10 O ATOM 1101 CB ALA A 147 18.906 18.436 10.503 1.00 18.01 C ATOM 1102 N CYS A 148 20.950 20.729 10.987 1.00 19.44 N ATOM 1103 CA CYS A 148 22.179 21.176 11.612 1.00 21.10 C ATOM 1104 C CYS A 148 21.872 21.897 12.910 1.00 21.84 C ATOM 1105 O CYS A 148 20.861 22.591 13.021 1.00 23.33 O ATOM 1106 CB CYS A 148 22.950 22.088 10.679 1.00 24.72 C ATOM 1107 SG CYS A 148 24.473 22.729 11.412 1.00 36.01 S ATOM 1108 N GLU A 149 22.710 21.679 13.912 1.00 21.80 N ATOM 1109 CA GLU A 149 22.542 22.322 15.208 1.00 23.33 C ATOM 1110 C GLU A 149 23.791 23.111 15.502 1.00 23.69 C ATOM 1111 O GLU A 149 24.850 22.810 14.950 1.00 27.17 O ATOM 1112 CB GLU A 149 22.391 21.297 16.298 1.00 21.78 C ATOM 1113 CG GLU A 149 21.179 20.496 16.175 1.00 27.92 C ATOM 1114 CD GLU A 149 20.722 20.061 17.518 1.00 33.04 C ATOM 1115 OE1 GLU A 149 20.545 20.949 18.381 1.00 34.62 O ATOM 1116 OE2 GLU A 149 20.604 18.840 17.721 1.00 38.76 O ATOM 1117 N ALA A 150 23.693 24.083 16.399 1.00 21.91 N ATOM 1118 CA ALA A 150 24.855 24.888 16.735 1.00 22.23 C ATOM 1119 C ALA A 150 24.688 25.579 18.054 1.00 21.56 C ATOM 1120 O ALA A 150 23.568 25.826 18.500 1.00 23.41 O ATOM 1121 CB ALA A 150 25.104 25.921 15.661 1.00 22.94 C ATOM 1122 N VAL A 151 25.804 25.827 18.714 1.00 21.13 N ATOM 1123 CA VAL A 151 25.773 26.544 19.968 1.00 21.99 C ATOM 1124 C VAL A 151 26.854 27.596 19.872 1.00 24.67 C ATOM 1125 O VAL A 151 27.799 27.445 19.096 1.00 28.39 O ATOM 1126 CB VAL A 151 26.038 25.647 21.169 1.00 19.52 C ATOM 1127 CG1 VAL A 151 24.895 24.669 21.352 1.00 18.30 C ATOM 1128 CG2 VAL A 151 27.353 24.952 21.016 1.00 17.36 C ATOM 1129 N ALA A 152 26.686 28.676 20.625 1.00 26.23 N ATOM 1130 CA ALA A 152 27.637 29.781 20.653 1.00 26.91 C ATOM 1131 C ALA A 152 27.727 30.377 22.052 1.00 28.23 C ATOM 1132 O ALA A 152 26.777 30.309 22.836 1.00 30.70 O ATOM 1133 CB ALA A 152 27.222 30.843 19.683 1.00 25.69 C ATOM 1134 N LEU A 153 28.887 30.927 22.374 1.00 28.90 N ATOM 1135 CA LEU A 153 29.099 31.552 23.660 1.00 28.89 C ATOM 1136 C LEU A 153 29.608 32.949 23.340 1.00 31.48 C ATOM 1137 O LEU A 153 30.561 33.092 22.573 1.00 33.68 O ATOM 1138 CB LEU A 153 30.127 30.764 24.440 1.00 28.40 C ATOM 1139 CG LEU A 153 30.339 31.140 25.895 1.00 31.89 C ATOM 1140 CD1 LEU A 153 30.578 29.892 26.700 1.00 33.79 C ATOM 1141 CD2 LEU A 153 31.532 32.071 26.020 1.00 37.99 C ATOM 1142 N LEU A 154 28.889 33.969 23.803 1.00 30.64 N ATOM 1143 CA LEU A 154 29.268 35.355 23.582 1.00 27.82 C ATOM 1144 C LEU A 154 29.756 35.900 24.900 1.00 29.35 C ATOM 1145 O LEU A 154 29.374 35.420 25.962 1.00 26.36 O ATOM 1146 CB LEU A 154 28.091 36.184 23.111 1.00 25.01 C ATOM 1147 CG LEU A 154 27.412 35.772 21.816 1.00 23.83 C ATOM 1148 CD1 LEU A 154 26.184 36.643 21.637 1.00 20.87 C ATOM 1149 CD2 LEU A 154 28.368 35.877 20.638 1.00 20.24 C ATOM 1150 N ILE A 155 30.548 36.957 24.822 1.00 33.77 N ATOM 1151 CA ILE A 155 31.147 37.565 25.994 1.00 37.56 C ATOM 1152 C ILE A 155 30.698 38.998 26.260 1.00 39.78 C ATOM 1153 O ILE A 155 30.220 39.685 25.358 1.00 45.46 O ATOM 1154 CB ILE A 155 32.649 37.529 25.835 1.00 38.25 C ATOM 1155 CG1 ILE A 155 33.113 36.083 25.796 1.00 39.34 C ATOM 1156 CG2 ILE A 155 33.312 38.264 26.951 1.00 41.51 C ATOM 1157 CD1 ILE A 155 34.560 35.958 25.502 1.00 43.17 C TER 1158 ILE A 155 HETATM 1159 ZN ZN A 160 17.514 27.639 6.845 1.00 46.53 ZN HETATM 1160 N1 CDM A 669 8.512 30.521 12.641 1.00 34.81 N HETATM 1161 C2 CDM A 669 7.404 30.610 13.395 1.00 35.06 C HETATM 1162 N3 CDM A 669 6.724 29.477 13.678 1.00 33.19 N HETATM 1163 C4 CDM A 669 7.117 28.284 13.237 1.00 30.19 C HETATM 1164 C5 CDM A 669 8.331 28.194 12.419 1.00 29.30 C HETATM 1165 C6 CDM A 669 8.970 29.334 12.161 1.00 31.06 C HETATM 1166 O2 CDM A 669 7.012 31.682 13.821 1.00 37.83 O HETATM 1167 N4 CDM A 669 6.389 27.217 13.562 1.00 29.45 N HETATM 1168 C1' CDM A 669 9.270 31.736 12.314 1.00 39.26 C HETATM 1169 C2' CDM A 669 10.512 32.023 13.152 1.00 44.03 C HETATM 1170 O2' CDM A 669 10.305 33.151 14.018 1.00 50.70 O HETATM 1171 C3' CDM A 669 11.651 32.240 12.149 1.00 44.36 C HETATM 1172 C4' CDM A 669 10.987 32.244 10.754 1.00 42.71 C HETATM 1173 O4' CDM A 669 9.678 31.693 10.926 1.00 39.67 O HETATM 1174 O3' CDM A 669 12.253 33.510 12.342 1.00 46.07 O HETATM 1175 C5' CDM A 669 11.869 31.442 9.714 1.00 45.27 C HETATM 1176 O5' CDM A 669 11.440 30.076 9.471 1.00 50.96 O HETATM 1177 PA CDM A 669 12.155 28.998 8.477 1.00 49.68 P HETATM 1178 O1A CDM A 669 11.881 27.525 9.034 1.00 53.26 O HETATM 1179 O2A CDM A 669 11.541 29.133 7.002 1.00 55.80 O HETATM 1180 O3A CDM A 669 13.758 29.217 8.557 1.00 59.44 O HETATM 1181 PB CDM A 669 14.699 29.269 7.221 1.00 62.77 P HETATM 1182 O1B CDM A 669 16.173 28.784 7.652 1.00 58.86 O HETATM 1183 O2B CDM A 669 14.191 28.335 6.019 1.00 63.75 O HETATM 1184 O3B CDM A 669 14.788 30.775 6.696 1.00 67.21 O HETATM 1185 C1M CDM A 669 15.216 31.821 7.568 1.00 71.79 C HETATM 1186 C2M CDM A 669 15.158 33.136 6.741 1.00 73.86 C HETATM 1187 O2M CDM A 669 15.560 34.235 7.570 1.00 78.73 O HETATM 1188 C3M CDM A 669 16.061 33.211 5.457 1.00 74.19 C HETATM 1189 C4M CDM A 669 15.597 34.476 4.643 1.00 74.40 C HETATM 1190 C5M CDM A 669 17.563 33.361 5.828 1.00 72.22 C HETATM 1191 O3M CDM A 669 15.895 32.070 4.562 1.00 74.90 O HETATM 1192 O4M CDM A 669 16.370 34.642 3.439 1.00 76.36 O CONECT 63 1159 CONECT 81 1159 CONECT 308 1159 CONECT 1159 63 81 308 1182 CONECT 1160 1161 1165 1168 CONECT 1161 1160 1162 1166 CONECT 1162 1161 1163 CONECT 1163 1162 1164 1167 CONECT 1164 1163 1165 CONECT 1165 1160 1164 CONECT 1166 1161 CONECT 1167 1163 CONECT 1168 1160 1169 1173 CONECT 1169 1168 1170 1171 CONECT 1170 1169 CONECT 1171 1169 1172 1174 CONECT 1172 1171 1173 1175 CONECT 1173 1168 1172 CONECT 1174 1171 CONECT 1175 1172 1176 CONECT 1176 1175 1177 CONECT 1177 1176 1178 1179 1180 CONECT 1178 1177 CONECT 1179 1177 CONECT 1180 1177 1181 CONECT 1181 1180 1182 1183 1184 CONECT 1182 1159 1181 CONECT 1183 1181 CONECT 1184 1181 1185 CONECT 1185 1184 1186 CONECT 1186 1185 1187 1188 CONECT 1187 1186 CONECT 1188 1186 1189 1190 1191 CONECT 1189 1188 1192 CONECT 1190 1188 CONECT 1191 1188 CONECT 1192 1189 MASTER 355 0 2 8 7 0 7 6 1191 1 37 13 END