PDB Short entry for 1AOI HEADER COMPLEX (NUCLEOSOME CORE/DNA) 03-JUL-97 1AOI TITLE X-RAY STRUCTURE OF THE NUCLEOSOME CORE PARTICLE AT 2.8 A TITLE 2 RESOLUTION COMPND MOL_ID: 1; COMPND 2 MOLECULE: HISTONE H3; COMPND 3 CHAIN: A, E; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: HISTONE H4; COMPND 7 CHAIN: B, F; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: HISTONE H2A; COMPND 11 CHAIN: C, G; COMPND 12 ENGINEERED: YES; COMPND 13 MOL_ID: 4; COMPND 14 MOLECULE: HISTONE H2B; COMPND 15 CHAIN: D, H; COMPND 16 ENGINEERED: YES; COMPND 17 MUTATION: A7P; COMPND 18 MOL_ID: 5; COMPND 19 MOLECULE: DNA COMPND 20 (5'(ATCAATATCCACCTGCAGATTCTACCAAAAGTGTATTTGGAAACTGCTCCATCAA COMPND 21 AAGGCATGTTCAGCTGAATTCAGCTGAACATGCCTTTTGATGGAGCAGTTTCCAAATAC COMPND 22 ACTTTTGGTAGAATCTGCAGGTGGATATTGAT)3'); COMPND 23 CHAIN: I, J; COMPND 24 ENGINEERED: YES; COMPND 25 OTHER_DETAILS: PALINDROMIC 146 BP DNA FRAGMENT, REPEAT 8/9 COMPND 26 FROM HUMAN X-CHROMOSOME ALPHA SATELLITE DNA. REMOVED 5' COMPND 27 PHOSPHATES WITH PHOSPHATASE. SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: XENOPUS LAEVIS; SOURCE 3 ORGANISM_COMMON: AFRICAN CLAWED FROG; SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 5 MOL_ID: 2; SOURCE 6 ORGANISM_SCIENTIFIC: XENOPUS LAEVIS; SOURCE 7 ORGANISM_COMMON: AFRICAN CLAWED FROG; SOURCE 8 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 9 OTHER_DETAILS: SYNTHETIC GENE, OPTIMIZED CODON USAGE FOR SOURCE 10 ESCHERICHIA COLI; SOURCE 11 MOL_ID: 3; SOURCE 12 ORGANISM_SCIENTIFIC: XENOPUS LAEVIS; SOURCE 13 ORGANISM_COMMON: AFRICAN CLAWED FROG; SOURCE 14 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 15 MOL_ID: 4; SOURCE 16 ORGANISM_SCIENTIFIC: XENOPUS LAEVIS; SOURCE 17 ORGANISM_COMMON: AFRICAN CLAWED FROG; SOURCE 18 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 19 MOL_ID: 5; SOURCE 20 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 21 ORGANISM_COMMON: HUMAN; SOURCE 22 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 23 OTHER_DETAILS: DNA SEQUENCE SYNTHESIZED, CLONED, SOURCE 24 MULTIMERIZED, AND EXCISED FROM PLASMID KEYWDS NUCLEOSOME, CHROMATIN, HISTONE, PROTEIN DNA INTERACTION, KEYWDS 2 NUCLEOPROTEIN, SUPERCOILED DNA, KEYWDS 3 COMPLEX (NUCLEOSOME CORE/DNA) EXPDTA X-RAY DIFFRACTION AUTHOR K.LUGER,A.W.MAEDER,R.K.RICHMOND,D.F.SARGENT, AUTHOR 2 T.J.RICHMOND REVDAT 2 02-DEC-98 1AOIA 3 COMPND REMARK HETATM DBREF REVDAT 2 2 3 HEADER SOURCE JRNL KEYWDS REVDAT 1 30-SEP-98 1AOI 0 JRNL AUTH K.LUGER,A.W.MADER,R.K.RICHMOND,D.F.SARGENT, JRNL AUTH 2 T.J.RICHMOND JRNL TITL CRYSTAL STRUCTURE OF THE NUCLEOSOME CORE PARTICLE JRNL TITL 2 AT 2.8 A RESOLUTION JRNL REF NATURE V. 389 251 1997 JRNL REFN ASTM NATUAS UK ISSN 0028-0836 0006 REMARK 1 REMARK 2 REMARK 2 RESOLUTION. 2.8 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : X-PLOR 3.843 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) : 25.00 REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL REMARK 3 COMPLETENESS (WORKING+TEST) (%) : NULL REMARK 3 NUMBER OF REFLECTIONS : 51237 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM REMARK 3 R VALUE (WORKING SET) : 0.224 REMARK 3 FREE R VALUE : 0.302 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 : NULL REMARK 3 NUCLEIC ACID ATOMS : NULL 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) : 0.009 REMARK 3 BOND ANGLES (DEGREES) : 1.3 REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL REMARK 3 IMPROPER ANGLES (DEGREES) : NULL REMARK 3 REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED REMARK 3 REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA REMARK 3 MAIN-CHAIN BOND (A**2) : 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 GROUP 2 POSITIONAL (A) : NULL ; NULL REMARK 3 GROUP 2 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: BULK SOLVENT MODEL USED REMARK 4 REMARK 4 1AOI 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 : AUG-1995 REMARK 200 TEMPERATURE (KELVIN) : 110 REMARK 200 PH : NULL REMARK 200 NUMBER OF CRYSTALS USED : NULL REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : ESRF REMARK 200 BEAMLINE : ID13 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.971 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : 300MM IMAGE PLATE REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH REMARK 200 INTENSITY-INTEGRATION SOFTWARE : LOCAL REMARK 200 DATA SCALING SOFTWARE : LOCAL REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 52487 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.8 REMARK 200 RESOLUTION RANGE LOW (A) : 25 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99 REMARK 200 DATA REDUNDANCY : 5.7 REMARK 200 R MERGE (I) : 0.056 REMARK 200 R SYM (I) : 0.036 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) : 2.8 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.85 REMARK 200 COMPLETENESS FOR SHELL (%) : 95 REMARK 200 DATA REDUNDANCY IN SHELL : 6.3 REMARK 200 R MERGE FOR SHELL (I) : 0.132 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: NULL REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MIR REMARK 200 SOFTWARE USED: LOCAL 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): NULL REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: NULL REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 1/2-X,-Y,1/2+Z REMARK 290 3555 -X,1/2+Y,1/2-Z REMARK 290 4555 1/2+X,1/2-Y,-Z REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 53.02227 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 55.06002 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 90.89256 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 55.06002 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 53.02227 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 90.89256 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS REMARK 500 REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15 REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375 REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS. REMARK 500 REMARK 500 DISTANCE CUTOFF: REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE REMARK 500 O HOH 6 O VAL D 45 2564 2.18 REMARK 500 REMARK 500 REMARK: NULL REMARK 550 REMARK 550 SEGID REMARK 550 1H3, 2H3: HISTONE H3 REMARK 550 1H4, 2H4: HISTONE H4 REMARK 550 1HA, 2HA: HISTONE H2A REMARK 550 1HB, 2HB: HISTONE H2B REMARK 550 ADA, BDA: PALINDROMIC 146 BP DNA FRAGMENT REMARK 860 REMARK 860 CORRECTION AFTER RELEASE REMARK 860 DATE: 02-DEC-98 REMARK 860 MODID: 1AOIA REMARK 860 MODIFIED BY: PDB REMARK 860 DESCRIPTION: CONVERTED FROM LAYER 1 OR NDB TO LAYER 2 REMARK 999 REMARK 999 SEQUENCE REMARK 999 1AOI A SWS P02302 1 - 37 NOT IN ATOMS LIST REMARK 999 1AOI B SWS P02304 1 - 19 NOT IN ATOMS LIST REMARK 999 1AOI C SWS P06897 1 - 3 NOT IN ATOMS LIST REMARK 999 1AOI C SWS P06897 119 - 129 NOT IN ATOMS LIST REMARK 999 1AOI D SWS P02281 1 - 26 NOT IN ATOMS LIST REMARK 999 1AOI E SWS P02302 1 - 19 NOT IN ATOMS LIST REMARK 999 1AOI F SWS P02304 1 - 15 NOT IN ATOMS LIST REMARK 999 1AOI G SWS P06897 1 - 11 NOT IN ATOMS LIST REMARK 999 1AOI G SWS P06897 120 - 129 NOT IN ATOMS LIST REMARK 999 1AOI H SWS P02281 1 - 26 NOT IN ATOMS LIST DBREF 1AOI A 38 135 SWS P02302 H32_XENLA 38 135 DBREF 1AOI B 20 102 SWS P02304 H4_HUMAN 20 102 DBREF 1AOI C 4 118 SWS P06897 H2A1_XENLA 4 118 DBREF 1AOI D 24 122 SWS P02281 H2B1_XENLA 27 125 DBREF 1AOI E 20 135 SWS P02302 H32_XENLA 20 135 DBREF 1AOI F 16 102 SWS P02304 H4_HUMAN 16 102 DBREF 1AOI G 12 119 SWS P06897 H2A2_XENLA 12 119 DBREF 1AOI H 24 122 SWS P02281 H2B1_XENLA 27 125 DBREF 1AOI I 1 146 PDB 1AOI 1AOI 1 146 DBREF 1AOI J 147 292 PDB 1AOI 1AOI 147 292 SEQADV 1AOI SER A 86 SWS P02302 ARG 86 CONFLICT SEQADV 1AOI ARG C 99 SWS P06897 GLY 99 VARIANT SEQADV 1AOI THR D 29 SWS P02281 SER 32 VARIANT SEQADV 1AOI ALA E 21 SWS P02302 VAL 21 CONFLICT SEQADV 1AOI ARG E 26 SWS P02302 LYS 26 CONFLICT SEQADV 1AOI SER E 28 SWS P02302 CYS 28 CONFLICT SEQADV 1AOI SER E 86 SWS P02302 ARG 86 CONFLICT SEQADV 1AOI ARG G 99 SWS P06897 GLY 99 VARIANT SEQADV 1AOI THR H 29 SWS P02281 SER 32 VARIANT SEQRES 1 A 116 LEU ALA THR LYS ALA ALA ARG LYS SER ALA PRO ALA THR SEQRES 2 A 116 GLY GLY VAL LYS LYS PRO HIS ARG TYR ARG PRO GLY THR SEQRES 3 A 116 VAL ALA LEU ARG GLU ILE ARG ARG TYR GLN LYS SER THR SEQRES 4 A 116 GLU LEU LEU ILE ARG LYS LEU PRO PHE GLN ARG LEU VAL SEQRES 5 A 116 ARG GLU ILE ALA GLN ASP PHE LYS THR ASP LEU ARG PHE SEQRES 6 A 116 GLN SER SER ALA VAL MET ALA LEU GLN GLU ALA SER GLU SEQRES 7 A 116 ALA TYR LEU VAL ALA LEU PHE GLU ASP THR ASN LEU CYS SEQRES 8 A 116 ALA ILE HIS ALA LYS ARG VAL THR ILE MET PRO LYS ASP SEQRES 9 A 116 ILE GLN LEU ALA ARG ARG ILE ARG GLY GLU ARG ALA SEQRES 1 B 87 LYS ARG HIS ARG LYS VAL LEU ARG ASP ASN ILE GLN GLY SEQRES 2 B 87 ILE THR LYS PRO ALA ILE ARG ARG LEU ALA ARG ARG GLY SEQRES 3 B 87 GLY VAL LYS ARG ILE SER GLY LEU ILE TYR GLU GLU THR SEQRES 4 B 87 ARG GLY VAL LEU LYS VAL PHE LEU GLU ASN VAL ILE ARG SEQRES 5 B 87 ASP ALA VAL THR TYR THR GLU HIS ALA LYS ARG LYS THR SEQRES 6 B 87 VAL THR ALA MET ASP VAL VAL TYR ALA LEU LYS ARG GLN SEQRES 7 B 87 GLY ARG THR LEU TYR GLY PHE GLY GLY SEQRES 1 C 116 GLY LYS GLN GLY GLY LYS THR ARG ALA LYS ALA LYS THR SEQRES 2 C 116 ARG SER SER ARG ALA GLY LEU GLN PHE PRO VAL GLY ARG SEQRES 3 C 116 VAL HIS ARG LEU LEU ARG LYS GLY ASN TYR ALA GLU ARG SEQRES 4 C 116 VAL GLY ALA GLY ALA PRO VAL TYR LEU ALA ALA VAL LEU SEQRES 5 C 116 GLU TYR LEU THR ALA GLU ILE LEU GLU LEU ALA GLY ASN SEQRES 6 C 116 ALA ALA ARG ASP ASN LYS LYS THR ARG ILE ILE PRO ARG SEQRES 7 C 116 HIS LEU GLN LEU ALA VAL ARG ASN ASP GLU GLU LEU ASN SEQRES 8 C 116 LYS LEU LEU GLY ARG VAL THR ILE ALA GLN GLY GLY VAL SEQRES 9 C 116 LEU PRO ASN ILE GLN SER VAL LEU LEU PRO LYS LYS SEQRES 1 D 99 LYS LYS ARG ARG LYS THR ARG LYS GLU SER TYR ALA ILE SEQRES 2 D 99 TYR VAL TYR LYS VAL LEU LYS GLN VAL HIS PRO ASP THR SEQRES 3 D 99 GLY ILE SER SER LYS ALA MET SER ILE MET ASN SER PHE SEQRES 4 D 99 VAL ASN ASP VAL PHE GLU ARG ILE ALA GLY GLU ALA SER SEQRES 5 D 99 ARG LEU ALA HIS TYR ASN LYS ARG SER THR ILE THR SER SEQRES 6 D 99 ARG GLU ILE GLN THR ALA VAL ARG LEU LEU LEU PRO GLY SEQRES 7 D 99 GLU LEU ALA LYS HIS ALA VAL SER GLU GLY THR LYS ALA SEQRES 8 D 99 VAL THR LYS TYR THR SER ALA LYS SEQRES 1 E 116 LEU ALA THR LYS ALA ALA ARG LYS SER ALA PRO ALA THR SEQRES 2 E 116 GLY GLY VAL LYS LYS PRO HIS ARG TYR ARG PRO GLY THR SEQRES 3 E 116 VAL ALA LEU ARG GLU ILE ARG ARG TYR GLN LYS SER THR SEQRES 4 E 116 GLU LEU LEU ILE ARG LYS LEU PRO PHE GLN ARG LEU VAL SEQRES 5 E 116 ARG GLU ILE ALA GLN ASP PHE LYS THR ASP LEU ARG PHE SEQRES 6 E 116 GLN SER SER ALA VAL MET ALA LEU GLN GLU ALA SER GLU SEQRES 7 E 116 ALA TYR LEU VAL ALA LEU PHE GLU ASP THR ASN LEU CYS SEQRES 8 E 116 ALA ILE HIS ALA LYS ARG VAL THR ILE MET PRO LYS ASP SEQRES 9 E 116 ILE GLN LEU ALA ARG ARG ILE ARG GLY GLU ARG ALA SEQRES 1 F 87 LYS ARG HIS ARG LYS VAL LEU ARG ASP ASN ILE GLN GLY SEQRES 2 F 87 ILE THR LYS PRO ALA ILE ARG ARG LEU ALA ARG ARG GLY SEQRES 3 F 87 GLY VAL LYS ARG ILE SER GLY LEU ILE TYR GLU GLU THR SEQRES 4 F 87 ARG GLY VAL LEU LYS VAL PHE LEU GLU ASN VAL ILE ARG SEQRES 5 F 87 ASP ALA VAL THR TYR THR GLU HIS ALA LYS ARG LYS THR SEQRES 6 F 87 VAL THR ALA MET ASP VAL VAL TYR ALA LEU LYS ARG GLN SEQRES 7 F 87 GLY ARG THR LEU TYR GLY PHE GLY GLY SEQRES 1 G 116 GLY LYS GLN GLY GLY LYS THR ARG ALA LYS ALA LYS THR SEQRES 2 G 116 ARG SER SER ARG ALA GLY LEU GLN PHE PRO VAL GLY ARG SEQRES 3 G 116 VAL HIS ARG LEU LEU ARG LYS GLY ASN TYR ALA GLU ARG SEQRES 4 G 116 VAL GLY ALA GLY ALA PRO VAL TYR LEU ALA ALA VAL LEU SEQRES 5 G 116 GLU TYR LEU THR ALA GLU ILE LEU GLU LEU ALA GLY ASN SEQRES 6 G 116 ALA ALA ARG ASP ASN LYS LYS THR ARG ILE ILE PRO ARG SEQRES 7 G 116 HIS LEU GLN LEU ALA VAL ARG ASN ASP GLU GLU LEU ASN SEQRES 8 G 116 LYS LEU LEU GLY ARG VAL THR ILE ALA GLN GLY GLY VAL SEQRES 9 G 116 LEU PRO ASN ILE GLN SER VAL LEU LEU PRO LYS LYS SEQRES 1 H 99 LYS LYS ARG ARG LYS THR ARG LYS GLU SER TYR ALA ILE SEQRES 2 H 99 TYR VAL TYR LYS VAL LEU LYS GLN VAL HIS PRO ASP THR SEQRES 3 H 99 GLY ILE SER SER LYS ALA MET SER ILE MET ASN SER PHE SEQRES 4 H 99 VAL ASN ASP VAL PHE GLU ARG ILE ALA GLY GLU ALA SER SEQRES 5 H 99 ARG LEU ALA HIS TYR ASN LYS ARG SER THR ILE THR SER SEQRES 6 H 99 ARG GLU ILE GLN THR ALA VAL ARG LEU LEU LEU PRO GLY SEQRES 7 H 99 GLU LEU ALA LYS HIS ALA VAL SER GLU GLY THR LYS ALA SEQRES 8 H 99 VAL THR LYS TYR THR SER ALA LYS SEQRES 1 I 146 A T C A A T A T C C A C C SEQRES 2 I 146 T G C A G A T T C T A C C SEQRES 3 I 146 A A A A G T G T A T T T G SEQRES 4 I 146 G A A A C T G C T C C A T SEQRES 5 I 146 C A A A A G G C A T G T T SEQRES 6 I 146 C A G C T G A A T T C A G SEQRES 7 I 146 C T G A A C A T G C C T T SEQRES 8 I 146 T T G A T G G A G C A G T SEQRES 9 I 146 T T C C A A A T A C A C T SEQRES 10 I 146 T T T G G T A G A A T C T SEQRES 11 I 146 G C A G G T G G A T A T T SEQRES 12 I 146 G A T SEQRES 1 J 146 A T C A A T A T C C A C C SEQRES 2 J 146 T G C A G A T T C T A C C SEQRES 3 J 146 A A A A G T G T A T T T G SEQRES 4 J 146 G A A A C T G C T C C A T SEQRES 5 J 146 C A A A A G G C A T G T T SEQRES 6 J 146 C A G C T G A A T T C A G SEQRES 7 J 146 C T G A A C A T G C C T T SEQRES 8 J 146 T T G A T G G A G C A G T SEQRES 9 J 146 T T C C A A A T A C A C T SEQRES 10 J 146 T T T G G T A G A A T C T SEQRES 11 J 146 G C A G G T G G A T A T T SEQRES 12 J 146 G A T HET MN 1 1 HET MN 2 1 HET MN 3 1 HET MN 4 1 HET MN 5 1 HET MN 6 1 HETNAM MN MANGANESE (II) ION FORMUL 11 MN 6(MN1 2+) FORMUL 12 HOH *13(H2 O1) HELIX 1 1 THR A 45 LYS A 56 1 12 HELIX 2 2 LYS A 64 PHE A 78 1 15 HELIX 3 3 SER A 86 HIS A 113 1 28 HELIX 4 4 PRO A 121 ARG A 131 1 11 HELIX 5 5 ILE B 26 GLY B 28 5 3 HELIX 6 6 LYS B 31 ARG B 40 1 10 HELIX 7 7 GLY B 48 HIS B 75 5 28 HELIX 8 8 ALA B 83 GLN B 93 1 11 HELIX 9 9 LYS C 5 GLY C 7 5 3 HELIX 10 10 ARG C 17 ALA C 21 1 5 HELIX 11 11 VAL C 27 ARG C 35 1 9 HELIX 12 12 ALA C 45 ASP C 72 1 28 HELIX 13 13 PRO C 80 ARG C 88 1 9 HELIX 14 14 GLU C 91 LEU C 96 1 6 HELIX 15 15 SER C 113 LEU C 115 5 3 HELIX 16 16 ALA D 35 VAL D 45 1 11 HELIX 17 17 SER D 53 ASN D 81 1 29 HELIX 18 18 SER D 88 LEU D 98 1 11 HELIX 19 19 GLY D 101 THR D 119 1 19 HELIX 20 20 THR E 45 LYS E 56 1 12 HELIX 21 21 LYS E 64 ASP E 77 1 14 HELIX 22 22 SER E 86 ALA E 114 1 29 HELIX 23 23 PRO E 121 ARG E 131 1 11 HELIX 24 24 ASN F 25 GLY F 28 5 4 HELIX 25 25 LYS F 31 ARG F 40 1 10 HELIX 26 26 ILE F 50 ALA F 76 1 27 HELIX 27 27 ALA F 83 ARG F 92 1 10 HELIX 28 28 ARG G 17 ALA G 21 1 5 HELIX 29 29 VAL G 27 GLY G 37 1 11 HELIX 30 30 ALA G 47 ASN G 73 1 27 HELIX 31 31 PRO G 80 ARG G 88 1 9 HELIX 32 32 GLU G 91 LEU G 96 1 6 HELIX 33 33 SER G 113 LEU G 115 5 3 HELIX 34 34 TYR H 34 VAL H 45 5 12 HELIX 35 35 SER H 53 TYR H 80 1 28 HELIX 36 36 SER H 88 LEU H 98 1 11 HELIX 37 37 GLY H 101 THR H 119 1 19 CRYST1 106.040 181.780 110.120 90.00 90.00 90.00 P 21 21 21 8 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 0.009430 0.000000 0.000000 0.00000 SCALE2 0.000000 0.005501 0.000000 0.00000 SCALE3 0.000000 0.000000 0.009081 0.00000