HEADER COMPLEX (DNA-BINDING PROTEIN/DNA) 26-JUN-97 1AN2 TITLE RECOGNITION BY MAX OF ITS COGNATE DNA COMPND MOL_ID: 1; COMPND 2 MOLECULE: MAX PROTEIN; COMPND 3 CHAIN: A, C; COMPND 4 FRAGMENT: DNA BINDING DOMAIN; COMPND 5 SYNONYM: MYN PROTEIN; COMPND 6 ENGINEERED: YES; COMPND 7 BIOLOGICAL_UNIT: BINDS DNA AS A HETERODIMER WITH MYC OR COMPND 8 MAD; COMPND 9 MOL_ID: 2; COMPND 10 MOLECULE: DNA; COMPND 11 CHAIN: B, D; COMPND 12 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 3 ORGANISM_COMMON: MOUSE; SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 5 OTHER_DETAILS: THE EXPRESSION VECTOR USED FOR PROTEIN SOURCE 6 PRODUCTION WAS INADVERTENTLY DERIVED FROM THE HUMAN GENE SOURCE 7 INSTEAD OF THE MOUSE GENE; SOURCE 8 MOL_ID: 2; SOURCE 9 SYNTHETIC: 22 BP DNA CONTAINING ADENOVIRUS MAJOR LATE SOURCE 10 PROMOTER KEYWDS MAX, DNA BINDING, BASIC-HELIX-LOOP-HELIX-LEUCINE ZIPPER, KEYWDS 2 TRANSCRIPTION FACTOR, COMPLEX (DNA-BINDING PROTEIN/DNA) EXPDTA X-RAY DIFFRACTION AUTHOR A.R.FERRE-D'AMARE,G.C.PRENDERGAST,E.B.ZIFF,S.K.BURLEY REVDAT 1 17-SEP-97 1AN2 0 JRNL AUTH A.R.FERRE-D'AMARE,G.C.PRENDERGAST,E.B.ZIFF, JRNL AUTH 2 S.K.BURLEY JRNL TITL RECOGNITION BY MAX OF ITS COGNATE DNA THROUGH A JRNL TITL 2 DIMERIC B/HLH/Z DOMAIN JRNL REF NATURE V. 363 38 1993 JRNL REFN ASTM NATUAS UK ISSN 0028-0836 0006 REMARK 1 REMARK 2 REMARK 2 RESOLUTION. 2.9 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : X-PLOR 3.1 REMARK 3 AUTHORS : BRUNGER REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.9 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 6.0 REMARK 3 DATA CUTOFF (SIGMA(F)) : 1.0 REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 84.6 REMARK 3 NUMBER OF REFLECTIONS : 3916 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) : 0.232 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 : 717 REMARK 3 NUCLEIC ACID ATOMS : 448 REMARK 3 HETEROGEN ATOMS : NULL REMARK 3 SOLVENT ATOMS : NULL 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) : 0.013 REMARK 3 BOND ANGLES (DEGREES) : 2.29 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 PARAMETER FILE 2 : NULL REMARK 3 TOPOLOGY FILE 1 : NULL REMARK 3 TOPOLOGY FILE 2 : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1AN2 COMPLIES WITH FORMAT V. 2.2, 16-DEC-1996 REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : SEP-1992 REMARK 200 TEMPERATURE (KELVIN) : 258 REMARK 200 PH : 5.5 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : CHESS REMARK 200 BEAMLINE : F1 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.910 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : IMAGE PLATE REMARK 200 DETECTOR MANUFACTURER : NULL REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO REMARK 200 DATA SCALING SOFTWARE : SCALEPACK REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 4507 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.9 REMARK 200 RESOLUTION RANGE LOW (A) : 20.0 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0. REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 85.3 REMARK 200 DATA REDUNDANCY : NULL REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : 0.065 REMARK 200 FOR THE DATA SET : 13.9 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.9 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.0 REMARK 200 COMPLETENESS FOR SHELL (%) : 61.0 REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : 0.26 REMARK 200 FOR SHELL : 2.96 REMARK 200 REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MIR 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 (%): NULL REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.6 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: NULL REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61 2 2 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -Y,X-Y,1/3+Z REMARK 290 3555 Y-X,-X,2/3+Z REMARK 290 4555 -X,-Y,1/2+Z REMARK 290 5555 Y,Y-X,5/6+Z REMARK 290 6555 X-Y,X,1/6+Z REMARK 290 7555 Y,X,1/3-Z REMARK 290 8555 X-Y,-Y,-Z REMARK 290 9555 -X,Y-X,2/3-Z REMARK 290 10555 -Y,-X,5/6-Z REMARK 290 11555 Y-X,Y,1/2-Z REMARK 290 12555 X,X-Y,1/6-Z REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -0.500031 -0.866047 0.000000 0.00000 REMARK 290 SMTRY2 2 0.866004 -0.499969 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 48.79715 REMARK 290 SMTRY1 3 -0.499969 0.866047 0.000000 0.00000 REMARK 290 SMTRY2 3 -0.866004 -0.500031 0.000000 0.00000 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 97.59430 REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 73.19572 REMARK 290 SMTRY1 5 0.500031 0.866047 0.000000 0.00000 REMARK 290 SMTRY2 5 -0.866004 0.499969 0.000000 0.00000 REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 121.99287 REMARK 290 SMTRY1 6 0.499969 -0.866047 0.000000 0.00000 REMARK 290 SMTRY2 6 0.866004 0.500031 0.000000 0.00000 REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 24.39857 REMARK 290 SMTRY1 7 -0.500031 0.866011 0.000000 0.00000 REMARK 290 SMTRY2 7 0.866004 0.500031 0.000000 0.00000 REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 48.79715 REMARK 290 SMTRY1 8 1.000000 0.000072 0.000000 0.00000 REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 9 -0.499969 -0.866083 0.000000 0.00000 REMARK 290 SMTRY2 9 -0.866004 0.499969 0.000000 0.00000 REMARK 290 SMTRY3 9 0.000000 0.000000 -1.000000 97.59430 REMARK 290 SMTRY1 10 0.500031 -0.866011 0.000000 0.00000 REMARK 290 SMTRY2 10 -0.866004 -0.500031 0.000000 0.00000 REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 121.99287 REMARK 290 SMTRY1 11 -1.000000 -0.000072 0.000000 0.00000 REMARK 290 SMTRY2 11 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 73.19572 REMARK 290 SMTRY1 12 0.499969 0.866083 0.000000 0.00000 REMARK 290 SMTRY2 12 0.866004 -0.499969 0.000000 0.00000 REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 24.39857 REMARK 290 REMARK 290 REMARK: NULL REMARK 295 REMARK 295 NON-CRYSTALLOGRAPHIC SYMMETRY REMARK 295 THE TRANSFORMATIONS PRESENTED ON THE MTRIX RECORDS BELOW REMARK 295 DESCRIBE NON-CRYSTALLOGRAPHIC RELATIONSHIPS AMONG ATOMS REMARK 295 IN THIS ENTRY. APPLYING THE APPROPRIATE MTRIX REMARK 295 TRANSFORMATION TO THE RESIDUES LISTED FIRST WILL YIELD REMARK 295 APPROXIMATE COORDINATES FOR THE RESIDUES LISTED SECOND. REMARK 295 CHAIN IDENTIFIERS GIVEN AS "?" REFER TO CHAINS FOR WHICH REMARK 295 ATOMS ARE NOT FOUND IN THIS ENTRY. REMARK 295 REMARK 295 APPLIED TO TRANSFORMED TO REMARK 295 TRANSFORM CHAIN RESIDUES CHAIN RESIDUES RMSD REMARK 295 SSS REMARK 295 M 1 A 22 .. 107 C 22 .. 107 0.002 REMARK 295 M 1 B 1 .. 22 D 1 .. 22 0.003 REMARK 295 REMARK 295 WHERE SSS -> COLUMNS 8-10 OF MTRIX RECORDS REMARK 295 REMARK 295 REMARK: NULL REMARK 999 REMARK 999 SEQUENCE REMARK 999 1AN2 A SWS P28574 1 - 21 NOT IN ATOMS LIST REMARK 999 1AN2 A SWS P28574 108 - 160 NOT IN ATOMS LIST REMARK 999 1AN2 C SWS P28574 1 - 21 NOT IN ATOMS LIST REMARK 999 1AN2 C SWS P28574 108 - 160 NOT IN ATOMS LIST REMARK 999 REMARK 999 THE EXPRESSION VECTOR USED FOR PROTEIN PRODUCTION WAS REMARK 999 INADVERTENTLY DERIVED FROM THE HUMAN GENE INSTEAD OF THE REMARK 999 MOUSE GENE. HENCE THE SEQUENCE IN THIS ENTRY CORRESPONDS REMARK 999 TO HUMAN MAX. THERE IS ONLY A SINGLE AMINO ACID DIFFERENCE REMARK 999 BETWEEN THE HUMAN AND MOUSE SEQUENCES. DBREF 1AN2 A 22 107 SWS P28574 MAX_MOUSE 22 107 DBREF 1AN2 B 1 22 PDB 1AN2 1AN2 1 22 DBREF 1AN2 C 22 107 SWS P28574 MAX_MOUSE 22 107 DBREF 1AN2 D 1 22 PDB 1AN2 1AN2 1 22 SEQADV 1AN2 HIS A 79 SWS P28574 ASP 79 CONFLICT SEQADV 1AN2 HIS C 79 SWS P28574 ASP 79 CONFLICT SEQRES 1 A 86 ALA ASP LYS ARG ALA HIS HIS ASN ALA LEU GLU ARG LYS SEQRES 2 A 86 ARG ARG ASP HIS ILE LYS ASP SER PHE HIS SER LEU ARG SEQRES 3 A 86 ASP SER VAL PRO SER LEU GLN GLY GLU LYS ALA SER ARG SEQRES 4 A 86 ALA GLN ILE LEU ASP LYS ALA THR GLU TYR ILE GLN TYR SEQRES 5 A 86 MET ARG ARG LYS ASN HIS THR HIS GLN GLN ASP ILE ASP SEQRES 6 A 86 ASP LEU LYS ARG GLN ASN ALA LEU LEU GLU GLN GLN VAL SEQRES 7 A 86 ARG ALA LEU GLU LYS ALA ARG SER SEQRES 1 B 22 G T G T A G G T C A C G T SEQRES 2 B 22 G A C C T A C A C SEQRES 1 C 86 ALA ASP LYS ARG ALA HIS HIS ASN ALA LEU GLU ARG LYS SEQRES 2 C 86 ARG ARG ASP HIS ILE LYS ASP SER PHE HIS SER LEU ARG SEQRES 3 C 86 ASP SER VAL PRO SER LEU GLN GLY GLU LYS ALA SER ARG SEQRES 4 C 86 ALA GLN ILE LEU ASP LYS ALA THR GLU TYR ILE GLN TYR SEQRES 5 C 86 MET ARG ARG LYS ASN HIS THR HIS GLN GLN ASP ILE ASP SEQRES 6 C 86 ASP LEU LYS ARG GLN ASN ALA LEU LEU GLU GLN GLN VAL SEQRES 7 C 86 ARG ALA LEU GLU LYS ALA ARG SER SEQRES 1 D 22 G T G T A G G T C A C G T SEQRES 2 D 22 G A C C T A C A C HELIX 1 1 ALA A 26 ARG A 47 1 22 HELIX 2 2 GLN A 62 LEU A 102 1 41 HELIX 3 3 ALA C 26 ARG C 47 1 22 HELIX 4 4 GLN C 62 LEU C 102 1 41 CRYST1 72.200 72.200 146.400 90.00 90.00 120.00 P 61 2 2 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 0.013850 0.007997 0.000000 0.00000 SCALE2 0.000000 0.015993 0.000000 0.00000 SCALE3 0.000000 0.000000 0.006831 0.00000 MTRIX1 1 -1.000000 0.000100 0.000000 0.00170 1 MTRIX2 1 0.000100 1.000000 0.000000 0.00040 1 MTRIX3 1 0.000000 0.000000 -1.000000 73.20040 1 ATOM 1 N ALA A 22 -4.642 -1.360 18.302 1.00 35.48 N ATOM 2 CA ALA A 22 -5.109 0.039 18.015 1.00 33.20 C ATOM 3 C ALA A 22 -4.488 1.059 18.957 1.00 36.83 C ATOM 4 O ALA A 22 -4.674 0.985 20.183 1.00 43.38 O ATOM 5 CB ALA A 22 -6.627 0.119 18.130 1.00 21.72 C ATOM 6 N ASP A 23 -3.732 2.007 18.413 1.00 35.85 N ATOM 7 CA ASP A 23 -3.159 3.024 19.279 1.00 18.29 C ATOM 8 C ASP A 23 -4.365 3.681 19.915 1.00 13.81 C ATOM 9 O ASP A 23 -5.190 4.300 19.224 1.00 15.67 O ATOM 10 CB ASP A 23 -2.440 4.130 18.500 1.00 24.72 C ATOM 11 CG ASP A 23 -1.403 3.615 17.549 1.00 32.35 C ATOM 12 OD1 ASP A 23 -0.366 3.061 18.015 1.00 34.67 O ATOM 13 OD2 ASP A 23 -1.626 3.803 16.325 1.00 36.54 O ATOM 14 N LYS A 24 -4.584 3.377 21.174 1.00 16.66 N ATOM 15 CA LYS A 24 -5.653 4.045 21.907 1.00 25.47 C ATOM 16 C LYS A 24 -4.977 4.523 23.184 1.00 21.40 C ATOM 17 O LYS A 24 -5.589 5.103 24.059 1.00 12.48 O ATOM 18 CB LYS A 24 -6.849 3.133 22.176 1.00 36.86 C ATOM 19 CG LYS A 24 -8.184 3.914 22.204 1.00 44.68 C ATOM 20 CD LYS A 24 -8.315 4.913 21.016 1.00 39.67 C ATOM 21 CE LYS A 24 -8.001 6.362 21.414 1.00 34.21 C ATOM 22 NZ LYS A 24 -8.389 7.316 20.325 1.00 31.52 N ATOM 23 N ARG A 25 -3.712 4.140 23.309 1.00 25.19 N ATOM 24 CA ARG A 25 -2.863 4.564 24.383 1.00 2.00 C ATOM 25 C ARG A 25 -2.233 5.643 23.535 1.00 8.92 C ATOM 26 O ARG A 25 -2.754 6.749 23.500 1.00 10.04 O ATOM 27 CB ARG A 25 -1.834 3.497 24.751 1.00 20.76 C ATOM 28 CG ARG A 25 -2.374 2.336 25.633 1.00 36.75 C ATOM 29 CD ARG A 25 -1.234 1.418 26.141 1.00 38.88 C ATOM 30 NE ARG A 25 -1.731 0.286 26.925 1.00 45.41 N ATOM 31 CZ ARG A 25 -1.037 -0.831 27.167 1.00 55.20 C ATOM 32 NH1 ARG A 25 0.203 -0.991 26.684 1.00 42.21 N ATOM 33 NH2 ARG A 25 -1.578 -1.791 27.921 1.00 54.15 N ATOM 34 N ALA A 26 -1.304 5.257 22.659 1.00 2.15 N ATOM 35 CA ALA A 26 -0.590 6.212 21.791 1.00 5.25 C ATOM 36 C ALA A 26 -1.194 7.619 21.604 1.00 10.01 C ATOM 37 O ALA A 26 -0.883 8.509 22.394 1.00 27.71 O ATOM 38 CB ALA A 26 -0.286 5.592 20.471 1.00 11.95 C ATOM 39 N HIS A 27 -2.072 7.829 20.621 1.00 13.49 N ATOM 40 CA HIS A 27 -2.668 9.153 20.414 1.00 18.13 C ATOM 41 C HIS A 27 -3.191 9.814 21.705 1.00 24.19 C ATOM 42 O HIS A 27 -3.416 11.019 21.727 1.00 35.36 O ATOM 43 CB HIS A 27 -3.751 9.139 19.327 1.00 23.15 C ATOM 44 CG HIS A 27 -3.218 9.275 17.919 1.00 43.57 C ATOM 45 ND1 HIS A 27 -2.605 10.424 17.454 1.00 49.45 N ATOM 46 CD2 HIS A 27 -3.246 8.419 16.863 1.00 42.32 C ATOM 47 CE1 HIS A 27 -2.280 10.271 16.178 1.00 40.59 C ATOM 48 NE2 HIS A 27 -2.656 9.063 15.796 1.00 33.58 N ATOM 49 N HIS A 28 -3.421 9.039 22.763 1.00 19.20 N ATOM 50 CA HIS A 28 -3.843 9.610 24.046 1.00 14.55 C ATOM 51 C HIS A 28 -2.553 10.005 24.787 1.00 28.32 C ATOM 52 O HIS A 28 -2.243 11.200 24.916 1.00 27.92 O ATOM 53 CB HIS A 28 -4.654 8.609 24.889 1.00 3.37 C ATOM 54 CG HIS A 28 -5.357 9.213 26.075 1.00 3.93 C ATOM 55 ND1 HIS A 28 -5.797 10.523 26.109 1.00 9.66 N ATOM 56 CD2 HIS A 28 -5.697 8.681 27.275 1.00 5.88 C ATOM 57 CE1 HIS A 28 -6.363 10.776 27.276 1.00 5.51 C ATOM 58 NE2 HIS A 28 -6.316 9.673 28.002 1.00 14.30 N ATOM 59 N ASN A 29 -1.760 9.014 25.204 1.00 27.16 N ATOM 60 CA ASN A 29 -0.515 9.280 25.928 1.00 13.58 C ATOM 61 C ASN A 29 0.234 10.405 25.291 1.00 22.03 C ATOM 62 O ASN A 29 1.102 11.004 25.927 1.00 40.91 O ATOM 63 CB ASN A 29 0.414 8.080 25.913 1.00 12.49 C ATOM 64 CG ASN A 29 -0.131 6.910 26.659 1.00 10.35 C ATOM 65 OD1 ASN A 29 0.336 5.791 26.481 1.00 16.34 O ATOM 66 ND2 ASN A 29 -1.140 7.144 27.497 1.00 16.93 N ATOM 67 N ALA A 30 -0.019 10.616 24.001 1.00 22.02 N ATOM 68 CA ALA A 30 0.630 11.680 23.259 1.00 20.55 C ATOM 69 C ALA A 30 -0.173 12.948 23.354 1.00 12.26 C ATOM 70 O ALA A 30 0.399 14.037 23.374 1.00 25.70 O ATOM 71 CB ALA A 30 0.839 11.286 21.813 1.00 20.01 C ATOM 72 N LEU A 31 -1.497 12.830 23.390 1.00 17.02 N ATOM 73 CA LEU A 31 -2.327 14.029 23.492 1.00 9.45 C ATOM 74 C LEU A 31 -1.957 14.712 24.774 1.00 14.87 C ATOM 75 O LEU A 31 -1.539 15.873 24.726 1.00 18.45 O ATOM 76 CB LEU A 31 -3.814 13.723 23.422 1.00 10.75 C ATOM 77 CG LEU A 31 -4.414 13.943 22.024 1.00 2.72 C ATOM 78 CD1 LEU A 31 -5.795 13.287 21.857 1.00 2.00 C ATOM 79 CD2 LEU A 31 -4.522 15.422 21.845 1.00 16.39 C ATOM 80 N GLU A 32 -1.922 13.960 25.883 1.00 2.23 N ATOM 81 CA GLU A 32 -1.558 14.563 27.188 1.00 4.89 C ATOM 82 C GLU A 32 -0.127 15.097 27.242 1.00 9.09 C ATOM 83 O GLU A 32 0.250 15.838 28.168 1.00 17.04 O ATOM 84 CB GLU A 32 -1.785 13.610 28.355 1.00 2.00 C ATOM 85 CG GLU A 32 -3.056 13.838 29.039 1.00 2.00 C ATOM 86 CD GLU A 32 -2.895 14.675 30.276 1.00 16.17 C ATOM 87 OE1 GLU A 32 -2.012 14.327 31.095 1.00 16.62 O ATOM 88 OE2 GLU A 32 -3.669 15.654 30.450 1.00 11.05 O ATOM 89 N ARG A 33 0.696 14.710 26.281 1.00 2.00 N ATOM 90 CA ARG A 33 2.037 15.234 26.314 1.00 5.61 C ATOM 91 C ARG A 33 2.124 16.533 25.541 1.00 7.60 C ATOM 92 O ARG A 33 3.067 17.303 25.738 1.00 13.94 O ATOM 93 CB ARG A 33 3.072 14.213 25.889 1.00 2.00 C ATOM 94 CG ARG A 33 3.782 13.655 27.078 1.00 4.59 C ATOM 95 CD ARG A 33 4.758 12.615 26.699 1.00 5.48 C ATOM 96 NE ARG A 33 4.145 11.613 25.833 1.00 10.04 N ATOM 97 CZ ARG A 33 4.319 11.599 24.519 1.00 10.37 C ATOM 98 NH1 ARG A 33 5.069 12.531 23.956 1.00 23.89 N ATOM 99 NH2 ARG A 33 3.771 10.663 23.769 1.00 20.13 N ATOM 100 N LYS A 34 1.148 16.803 24.675 1.00 3.01 N ATOM 101 CA LYS A 34 1.169 18.083 23.980 1.00 3.05 C ATOM 102 C LYS A 34 0.481 19.083 24.926 1.00 12.10 C ATOM 103 O LYS A 34 0.899 20.228 25.017 1.00 15.75 O ATOM 104 CB LYS A 34 0.434 18.007 22.658 1.00 10.08 C ATOM 105 CG LYS A 34 0.850 19.091 21.673 1.00 26.99 C ATOM 106 CD LYS A 34 2.293 18.877 21.148 1.00 31.04 C ATOM 107 CE LYS A 34 2.422 19.044 19.611 1.00 29.56 C ATOM 108 NZ LYS A 34 2.023 20.400 19.036 1.00 23.59 N ATOM 109 N ARG A 35 -0.533 18.637 25.678 1.00 8.81 N ATOM 110 CA ARG A 35 -1.217 19.522 26.602 1.00 2.00 C ATOM 111 C ARG A 35 -0.154 19.904 27.575 1.00 2.00 C ATOM 112 O ARG A 35 0.295 21.018 27.538 1.00 23.42 O ATOM 113 CB ARG A 35 -2.356 18.823 27.337 1.00 2.00 C ATOM 114 CG ARG A 35 -2.871 19.598 28.560 1.00 2.00 C ATOM 115 CD ARG A 35 -3.985 18.901 29.349 1.00 2.00 C ATOM 116 NE ARG A 35 -3.604 18.647 30.745 1.00 2.31 N ATOM 117 CZ ARG A 35 -3.362 19.595 31.671 1.00 20.93 C ATOM 118 NH1 ARG A 35 -3.447 20.898 31.376 1.00 8.73 N ATOM 119 NH2 ARG A 35 -3.060 19.248 32.929 1.00 18.33 N ATOM 120 N ARG A 36 0.343 18.966 28.372 1.00 2.00 N ATOM 121 CA ARG A 36 1.398 19.292 29.358 1.00 11.60 C ATOM 122 C ARG A 36 2.552 20.228 28.902 1.00 16.75 C ATOM 123 O ARG A 36 3.027 21.060 29.695 1.00 28.71 O ATOM 124 CB ARG A 36 2.011 18.030 29.924 1.00 11.51 C ATOM 125 CG ARG A 36 1.101 17.180 30.702 1.00 2.00 C ATOM 126 CD ARG A 36 1.926 16.046 31.208 1.00 13.51 C ATOM 127 NE ARG A 36 1.782 14.829 30.428 1.00 8.69 N ATOM 128 CZ ARG A 36 1.015 13.815 30.827 1.00 17.48 C ATOM 129 NH1 ARG A 36 0.353 13.922 31.987 1.00 5.38 N ATOM 130 NH2 ARG A 36 0.901 12.703 30.086 1.00 5.14 N ATOM 131 N ASP A 37 3.064 20.033 27.683 1.00 15.37 N ATOM 132 CA ASP A 37 4.112 20.908 27.148 1.00 17.05 C ATOM 133 C ASP A 37 3.511 22.293 27.158 1.00 11.53 C ATOM 134 O ASP A 37 4.073 23.229 27.719 1.00 15.85 O ATOM 135 CB ASP A 37 4.413 20.598 25.685 1.00 24.08 C ATOM 136 CG ASP A 37 5.533 19.640 25.517 1.00 25.22 C ATOM 137 OD1 ASP A 37 6.593 19.873 26.134 1.00 35.35 O ATOM 138 OD2 ASP A 37 5.354 18.669 24.749 1.00 24.41 O ATOM 139 N HIS A 38 2.327 22.388 26.564 1.00 2.00 N ATOM 140 CA HIS A 38 1.580 23.640 26.461 1.00 10.42 C ATOM 141 C HIS A 38 1.560 24.432 27.747 1.00 16.19 C ATOM 142 O HIS A 38 1.331 25.632 27.722 1.00 32.83 O ATOM 143 CB HIS A 38 0.166 23.361 26.056 1.00 15.88 C ATOM 144 CG HIS A 38 -0.487 24.494 25.362 1.00 24.67 C ATOM 145 ND1 HIS A 38 -0.466 25.774 25.858 1.00 20.70 N ATOM 146 CD2 HIS A 38 -1.215 24.534 24.220 1.00 34.46 C ATOM 147 CE1 HIS A 38 -1.160 26.559 25.056 1.00 37.12 C ATOM 148 NE2 HIS A 38 -1.626 25.830 24.053 1.00 36.37 N ATOM 149 N ILE A 39 1.766 23.773 28.878 1.00 13.97 N ATOM 150 CA ILE A 39 1.815 24.510 30.114 1.00 10.92 C ATOM 151 C ILE A 39 3.312 24.868 30.309 1.00 9.82 C ATOM 152 O ILE A 39 3.680 26.032 30.139 1.00 9.00 O ATOM 153 CB ILE A 39 1.176 23.716 31.277 1.00 6.99 C ATOM 154 CG1 ILE A 39 -0.122 23.082 30.797 1.00 2.00 C ATOM 155 CG2 ILE A 39 0.779 24.657 32.412 1.00 2.00 C ATOM 156 CD1 ILE A 39 -1.189 24.057 30.472 1.00 11.16 C ATOM 157 N LYS A 40 4.184 23.879 30.525 1.00 4.97 N ATOM 158 CA LYS A 40 5.633 24.137 30.704 1.00 8.93 C ATOM 159 C LYS A 40 6.177 25.238 29.787 1.00 13.08 C ATOM 160 O LYS A 40 7.233 25.803 30.034 1.00 32.77 O ATOM 161 CB LYS A 40 6.455 22.877 30.454 1.00 2.00 C ATOM 162 CG LYS A 40 7.922 23.154 30.253 1.00 2.00 C ATOM 163 CD LYS A 40 8.514 22.359 29.090 1.00 16.23 C ATOM 164 CE LYS A 40 7.704 22.447 27.764 1.00 15.70 C ATOM 165 NZ LYS A 40 8.330 21.672 26.607 1.00 3.39 N ATOM 166 N ASP A 41 5.548 25.455 28.648 1.00 17.84 N ATOM 167 CA ASP A 41 6.001 26.541 27.824 1.00 10.05 C ATOM 168 C ASP A 41 5.177 27.729 28.287 1.00 17.44 C ATOM 169 O ASP A 41 5.728 28.613 28.944 1.00 19.67 O ATOM 170 CB ASP A 41 5.833 26.255 26.346 1.00 11.83 C ATOM 171 CG ASP A 41 6.752 25.140 25.868 1.00 20.57 C ATOM 172 OD1 ASP A 41 7.910 25.064 26.359 1.00 4.25 O ATOM 173 OD2 ASP A 41 6.301 24.333 25.014 1.00 18.23 O ATOM 174 N SER A 42 3.852 27.679 28.143 1.00 11.14 N ATOM 175 CA SER A 42 3.062 28.835 28.577 1.00 18.07 C ATOM 176 C SER A 42 3.205 29.186 30.090 1.00 18.05 C ATOM 177 O SER A 42 2.681 30.218 30.566 1.00 24.21 O ATOM 178 CB SER A 42 1.591 28.747 28.076 1.00 27.05 C ATOM 179 OG SER A 42 1.481 28.825 26.623 1.00 10.10 O ATOM 180 N PHE A 43 4.066 28.441 30.797 1.00 19.95 N ATOM 181 CA PHE A 43 4.311 28.714 32.223 1.00 24.55 C ATOM 182 C PHE A 43 5.401 29.711 32.407 1.00 24.18 C ATOM 183 O PHE A 43 5.251 30.623 33.216 1.00 36.28 O ATOM 184 CB PHE A 43 4.671 27.480 33.038 1.00 27.05 C ATOM 185 CG PHE A 43 3.883 27.372 34.314 1.00 19.66 C ATOM 186 CD1 PHE A 43 4.303 28.004 35.448 1.00 9.23 C ATOM 187 CD2 PHE A 43 2.669 26.690 34.340 1.00 16.30 C ATOM 188 CE1 PHE A 43 3.516 27.963 36.589 1.00 17.83 C ATOM 189 CE2 PHE A 43 1.884 26.649 35.477 1.00 18.77 C ATOM 190 CZ PHE A 43 2.300 27.283 36.599 1.00 3.76 C ATOM 191 N HIS A 44 6.523 29.518 31.709 1.00 24.23 N ATOM 192 CA HIS A 44 7.619 30.492 31.794 1.00 24.89 C ATOM 193 C HIS A 44 7.113 31.820 31.208 1.00 21.47 C ATOM 194 O HIS A 44 7.562 32.898 31.596 1.00 18.30 O ATOM 195 CB HIS A 44 8.835 30.027 31.031 1.00 23.35 C ATOM 196 CG HIS A 44 8.641 30.020 29.560 1.00 32.03 C ATOM 197 ND1 HIS A 44 8.396 28.864 28.850 1.00 40.54 N ATOM 198 CD2 HIS A 44 8.618 31.031 28.660 1.00 43.63 C ATOM 199 CE1 HIS A 44 8.226 29.163 27.574 1.00 50.51 C ATOM 200 NE2 HIS A 44 8.353 30.472 27.431 1.00 52.92 N ATOM 201 N SER A 45 6.175 31.722 30.268 1.00 18.64 N ATOM 202 CA SER A 45 5.561 32.896 29.671 1.00 23.49 C ATOM 203 C SER A 45 4.992 33.677 30.851 1.00 18.98 C ATOM 204 O SER A 45 5.087 34.906 30.846 1.00 18.58 O ATOM 205 CB SER A 45 4.488 32.518 28.628 1.00 31.13 C ATOM 206 OG SER A 45 5.033 31.740 27.532 1.00 28.42 O ATOM 207 N LEU A 46 4.467 32.982 31.881 1.00 19.48 N ATOM 208 CA LEU A 46 3.996 33.709 33.095 1.00 10.80 C ATOM 209 C LEU A 46 5.195 34.210 33.914 1.00 16.00 C ATOM 210 O LEU A 46 5.329 35.410 34.110 1.00 29.51 O ATOM 211 CB LEU A 46 3.118 32.873 34.031 1.00 2.00 C ATOM 212 CG LEU A 46 2.042 33.648 34.839 1.00 11.17 C ATOM 213 CD1 LEU A 46 1.706 33.039 36.203 1.00 7.33 C ATOM 214 CD2 LEU A 46 2.450 35.052 35.075 1.00 8.15 C ATOM 215 N ARG A 47 6.052 33.308 34.409 1.00 30.17 N ATOM 216 CA ARG A 47 7.246 33.698 35.218 1.00 33.20 C ATOM 217 C ARG A 47 8.099 34.869 34.675 1.00 36.15 C ATOM 218 O ARG A 47 8.235 35.901 35.341 1.00 22.16 O ATOM 219 CB ARG A 47 8.186 32.505 35.437 1.00 34.51 C ATOM 220 CG ARG A 47 9.590 32.903 35.900 1.00 13.80 C ATOM 221 CD ARG A 47 10.434 31.682 36.113 1.00 20.75 C ATOM 222 NE ARG A 47 11.290 31.389 34.964 1.00 22.37 N ATOM 223 CZ ARG A 47 11.271 30.253 34.269 1.00 19.40 C ATOM 224 NH1 ARG A 47 10.425 29.287 34.581 1.00 17.88 N ATOM 225 NH2 ARG A 47 12.168 30.038 33.314 1.00 28.98 N ATOM 226 N ASP A 48 8.730 34.658 33.510 1.00 32.66 N ATOM 227 CA ASP A 48 9.557 35.675 32.865 1.00 21.19 C ATOM 228 C ASP A 48 8.663 36.908 32.702 1.00 21.38 C ATOM 229 O ASP A 48 9.143 38.038 32.749 1.00 22.55 O ATOM 230 CB ASP A 48 10.131 35.177 31.513 1.00 17.95 C ATOM 231 CG ASP A 48 11.360 34.182 31.668 1.00 21.19 C ATOM 232 OD1 ASP A 48 11.768 33.773 32.781 1.00 16.46 O ATOM 233 OD2 ASP A 48 11.940 33.788 30.641 1.00 16.86 O ATOM 234 N SER A 49 7.346 36.707 32.622 1.00 24.46 N ATOM 235 CA SER A 49 6.443 37.855 32.526 1.00 25.12 C ATOM 236 C SER A 49 6.395 38.576 33.879 1.00 27.32 C ATOM 237 O SER A 49 5.390 39.208 34.242 1.00 13.04 O ATOM 238 CB SER A 49 5.039 37.407 32.068 1.00 29.46 C ATOM 239 OG SER A 49 3.981 38.151 32.643 1.00 22.29 O ATOM 240 N VAL