HEADER TRANSCRIPTION/DNA 01-APR-05 1Z9C
TITLE CRYSTAL STRUCTURE OF OHRR BOUND TO THE OHRA PROMOTER: STRUCTURE OF
TITLE 2 MARR FAMILY PROTEIN WITH OPERATOR DNA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DNA (29-MER);
COMPND 3 CHAIN: G, I, K;
COMPND 4 ENGINEERED: YES;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: DNA (29-MER);
COMPND 7 CHAIN: H, J, L;
COMPND 8 ENGINEERED: YES;
COMPND 9 MOL_ID: 3;
COMPND 10 MOLECULE: ORGANIC HYDROPEROXIDE RESISTANCE TRANSCRIPTIONAL REGULATOR;
COMPND 11 CHAIN: A, B, C, D, E, F;
COMPND 12 ENGINEERED: YES;
COMPND 13 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 MOL_ID: 2;
SOURCE 4 SYNTHETIC: YES;
SOURCE 5 MOL_ID: 3;
SOURCE 6 ORGANISM_SCIENTIFIC: BACILLUS SUBTILIS;
SOURCE 7 ORGANISM_TAXID: 1423;
SOURCE 8 GENE: OHRR;
SOURCE 9 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 10 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 11 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)/PLYSS;
SOURCE 12 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 13 EXPRESSION_SYSTEM_PLASMID: PET16X
KEYWDS OHRR, MARR FAMILY PROTEIN, BACTERIAL TRANSCRIPTION FACTOR, WINGED HTH
KEYWDS 2 PROTEIN, TRANSCRIPTION-DNA COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR M.HONG,M.FUANGTHONG,J.D.HELMANN,R.G.BRENNAN
REVDAT 4 14-FEB-24 1Z9C 1 REMARK
REVDAT 3 20-OCT-21 1Z9C 1 SEQADV
REVDAT 2 24-FEB-09 1Z9C 1 VERSN
REVDAT 1 25-OCT-05 1Z9C 0
JRNL AUTH M.HONG,M.FUANGTHONG,J.D.HELMANN,R.G.BRENNAN
JRNL TITL STRUCTURE OF AN OHRR-OHRA OPERATOR COMPLEX REVEALS THE DNA
JRNL TITL 2 BINDING MECHANISM OF THE MARR FAMILY.
JRNL REF MOL.CELL V. 20 131 2005
JRNL REFN ISSN 1097-2765
JRNL PMID 16209951
JRNL DOI 10.1016/J.MOLCEL.2005.09.013
REMARK 2
REMARK 2 RESOLUTION. 2.64 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.64
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 59.65
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 1281466.375
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 96.0
REMARK 3 NUMBER OF REFLECTIONS : 39953
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) : 0.216
REMARK 3 FREE R VALUE : 0.277
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2012
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.006
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.64
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.81
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.00
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 6447
REMARK 3 BIN R VALUE (WORKING SET) : 0.3180
REMARK 3 BIN FREE R VALUE : 0.3810
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.70
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 317
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.021
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6413
REMARK 3 NUCLEIC ACID ATOMS : 3486
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 174
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 49.20
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -8.15000
REMARK 3 B22 (A**2) : -1.81000
REMARK 3 B33 (A**2) : 9.96000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.07000
REMARK 3 B23 (A**2) : 0.00000
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) : 0.007
REMARK 3 BOND ANGLES (DEGREES) : 1.200
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 19.60
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.540
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 ; 0.000
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; 0.000
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; 0.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; 0.000
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.33
REMARK 3 BSOL : 47.59
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 : PROTEIN.TOP
REMARK 3 PARAMETER FILE 2 : DNA-RNA.TOP
REMARK 3 PARAMETER FILE 3 : WATER.TOP
REMARK 3 PARAMETER FILE 4 : ION.TOP
REMARK 3 PARAMETER FILE 5 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN_REP.PARAM
REMARK 3 TOPOLOGY FILE 2 : DNA-RNA_REP.PARAM
REMARK 3 TOPOLOGY FILE 3 : WATER_REP.PARAM
REMARK 3 TOPOLOGY FILE 4 : ION.PARAM
REMARK 3 TOPOLOGY FILE 5 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1Z9C COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 18-MAY-05.
REMARK 100 THE DEPOSITION ID IS D_1000032461.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-OCT-04
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 3.7
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 8.2.1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9794
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA, CCP4 (SCALA)
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 47153
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.640
REMARK 200 RESOLUTION RANGE LOW (A) : 59.650
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.9
REMARK 200 DATA REDUNDANCY : 2.300
REMARK 200 R MERGE (I) : 0.05400
REMARK 200 R SYM (I) : 0.05400
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.64
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.76
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.9
REMARK 200 DATA REDUNDANCY IN SHELL : 2.00
REMARK 200 R MERGE FOR SHELL (I) : 0.38600
REMARK 200 R SYM FOR SHELL (I) : 0.38600
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: EPMR 2.5
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 45.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.20
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 3.7, 0.1 M MGCL2 AND 5 TO 8 % OF
REMARK 280 PEG 8000, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 40.48000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3
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 300 REMARK: BIOLOGICAL DIMER WAS OBSERVED IN THE STRUCTURE OF OHRR-DNA
REMARK 300 COMPLEX
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: TETRAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: G, H, A, B
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
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: I, J, C, D
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
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: K, L, E, F
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 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 DT I 1
REMARK 465 DT J 29
REMARK 465 DT L 29
REMARK 465 MET A 1
REMARK 465 GLU A 2
REMARK 465 ASN A 3
REMARK 465 LYS A 4
REMARK 465 PHE A 5
REMARK 465 ASP A 6
REMARK 465 HIS A 7
REMARK 465 MET A 8
REMARK 465 LYS A 146
REMARK 465 ASN A 147
REMARK 465 MET B 1
REMARK 465 GLU B 2
REMARK 465 ASN B 3
REMARK 465 LYS B 4
REMARK 465 PHE B 5
REMARK 465 ASP B 6
REMARK 465 HIS B 7
REMARK 465 GLN B 145
REMARK 465 LYS B 146
REMARK 465 ASN B 147
REMARK 465 MET C 1
REMARK 465 GLU C 2
REMARK 465 ASN C 3
REMARK 465 LYS C 4
REMARK 465 PHE C 5
REMARK 465 ASP C 6
REMARK 465 GLN C 145
REMARK 465 LYS C 146
REMARK 465 ASN C 147
REMARK 465 MET D 1
REMARK 465 GLU D 2
REMARK 465 ASN D 3
REMARK 465 LYS D 4
REMARK 465 PHE D 5
REMARK 465 ASP D 6
REMARK 465 HIS D 7
REMARK 465 GLN D 145
REMARK 465 LYS D 146
REMARK 465 ASN D 147
REMARK 465 MET E 1
REMARK 465 GLU E 2
REMARK 465 ASN E 3
REMARK 465 LYS E 4
REMARK 465 PHE E 5
REMARK 465 ASP E 6
REMARK 465 HIS E 7
REMARK 465 GLN E 145
REMARK 465 LYS E 146
REMARK 465 ASN E 147
REMARK 465 MET F 1
REMARK 465 GLU F 2
REMARK 465 ASN F 3
REMARK 465 LYS F 4
REMARK 465 PHE F 5
REMARK 465 ASP F 6
REMARK 465 GLN F 145
REMARK 465 LYS F 146
REMARK 465 ASN F 147
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 DA I 2 P OP1 OP2
REMARK 470 LYS A 9 CG CD CE NZ
REMARK 470 GLU A 11 CG CD OE1 OE2
REMARK 470 LYS A 30 CG CD CE NZ
REMARK 470 GLU A 53 CG CD OE1 OE2
REMARK 470 GLU A 127 CG CD OE1 OE2
REMARK 470 ASP A 128 CG OD1 OD2
REMARK 470 LYS A 130 CG CD CE NZ
REMARK 470 LYS B 9 CG CD CE NZ
REMARK 470 ASN B 12 CG OD1 ND2
REMARK 470 ARG B 88 CG CD NE CZ NH1 NH2
REMARK 470 GLU B 93 CG CD OE1 OE2
REMARK 470 LYS B 123 CG CD CE NZ
REMARK 470 LYS B 130 CG CD CE NZ
REMARK 470 LYS B 133 CG CD CE NZ
REMARK 470 GLU B 141 CG CD OE1 OE2
REMARK 470 LYS C 9 CG CD CE NZ
REMARK 470 LYS C 27 CG CD CE NZ
REMARK 470 LYS C 35 CG CD CE NZ
REMARK 470 GLU C 51 CG CD OE1 OE2
REMARK 470 GLU C 53 CG CD OE1 OE2
REMARK 470 LYS C 58 CG CD CE NZ
REMARK 470 LYS C 59 CG CD CE NZ
REMARK 470 GLU C 62 CG CD OE1 OE2
REMARK 470 LYS C 87 CG CD CE NZ
REMARK 470 ARG C 88 CG CD NE CZ NH1 NH2
REMARK 470 GLU C 90 CG CD OE1 OE2
REMARK 470 GLU C 109 CG CD OE1 OE2
REMARK 470 GLN C 124 CG CD OE1 NE2
REMARK 470 LYS D 30 CG CD CE NZ
REMARK 470 LEU D 32 CG CD1 CD2
REMARK 470 LYS D 35 CG CD CE NZ
REMARK 470 GLU D 53 CG CD OE1 OE2
REMARK 470 LYS D 58 CG CD CE NZ
REMARK 470 LYS D 76 CG CD CE NZ
REMARK 470 LYS D 87 CG CD CE NZ
REMARK 470 GLU D 93 CG CD OE1 OE2
REMARK 470 GLU D 109 CG CD OE1 OE2
REMARK 470 LEU D 121 CG CD1 CD2
REMARK 470 GLN D 124 CG CD OE1 NE2
REMARK 470 LYS D 130 CG CD CE NZ
REMARK 470 GLU D 141 CG CD OE1 OE2
REMARK 470 LYS E 9 CG CD CE NZ
REMARK 470 LYS E 35 CG CD CE NZ
REMARK 470 LYS E 123 CG CD CE NZ
REMARK 470 GLU E 141 CG CD OE1 OE2
REMARK 470 HIS F 7 CG ND1 CD2 CE1 NE2
REMARK 470 GLU F 53 CG CD OE1 OE2
REMARK 470 LYS F 87 CG CD CE NZ
REMARK 470 GLU F 93 CG CD OE1 OE2
REMARK 470 GLN F 124 CG CD OE1 NE2
REMARK 470 LYS F 130 CG CD CE NZ
REMARK 470 GLN F 131 CG CD OE1 NE2
REMARK 470 HIS F 144 CG ND1 CD2 CE1 NE2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 DT G 7 C5 DT G 7 C7 0.133
REMARK 500 DT G 14 C5 DT G 14 C7 0.188
REMARK 500 DT H 14 C5 DT H 14 C7 0.164
REMARK 500 DT I 7 C5 DT I 7 C7 0.139
REMARK 500 DT I 14 C5 DT I 14 C7 0.128
REMARK 500 DT J 7 C5 DT J 7 C7 0.110
REMARK 500 DT J 14 C5 DT J 14 C7 0.125
REMARK 500 DT K 7 C5 DT K 7 C7 0.137
REMARK 500 DT K 14 C5 DT K 14 C7 0.175
REMARK 500 DT L 7 C5 DT L 7 C7 0.137
REMARK 500 DT L 14 C5 DT L 14 C7 0.142
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 DT K 1 C1' - O4' - C4' ANGL. DEV. = -8.9 DEGREES
REMARK 500 DT K 1 C2' - C3' - O3' ANGL. DEV. = -17.0 DEGREES
REMARK 500 DT K 1 C4' - C3' - C2' ANGL. DEV. = -5.3 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
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 LEU A 10 -40.63 -136.81
REMARK 500 GLU A 53 -37.11 -32.55
REMARK 500 ASP A 92 83.28 -157.85
REMARK 500 GLU A 93 3.72 -50.75
REMARK 500 GLN A 124 6.34 -65.28
REMARK 500 SER A 125 -77.42 -76.03
REMARK 500 THR A 142 -70.35 -62.24
REMARK 500 LEU A 143 -7.65 -53.55
REMARK 500 GLU B 11 -10.68 -46.05
REMARK 500 HIS B 52 89.04 -162.04
REMARK 500 GLU B 53 -47.98 -24.34
REMARK 500 ASP B 92 83.22 179.60
REMARK 500 GLU B 93 1.52 -49.07
REMARK 500 LYS B 123 13.90 -61.95
REMARK 500 GLU B 127 173.08 174.94
REMARK 500 LEU C 10 -72.74 -43.96
REMARK 500 GLU C 11 5.26 -49.00
REMARK 500 GLU C 53 -29.75 -37.40
REMARK 500 GLU C 93 -0.21 -59.18
REMARK 500 VAL C 112 -38.83 -38.43
REMARK 500 SER C 122 -73.62 -90.46
REMARK 500 SER C 125 101.36 174.64
REMARK 500 GLU C 127 79.45 51.64
REMARK 500 LEU C 143 4.15 -63.83
REMARK 500 TRP D 50 10.75 -69.27
REMARK 500 GLU D 51 23.94 -143.17
REMARK 500 HIS D 52 68.87 178.77
REMARK 500 GLU D 53 -84.63 -13.92
REMARK 500 LEU D 66 -154.73 -116.46
REMARK 500 ASP D 67 -178.72 -173.18
REMARK 500 ASP D 92 90.01 -166.47
REMARK 500 GLU D 93 -4.26 -54.87
REMARK 500 GLN D 124 -147.79 -168.84
REMARK 500 SER D 125 -119.85 47.21
REMARK 500 GLU E 53 -43.55 -24.92
REMARK 500 GLU E 93 -8.58 -53.16
REMARK 500 LEU E 121 -52.31 -138.91
REMARK 500 GLN E 124 2.18 -61.48
REMARK 500 SER E 125 -143.78 -123.91
REMARK 500 GLU E 127 62.95 -47.14
REMARK 500 LEU E 129 -34.82 -30.28
REMARK 500 GLU F 53 -58.81 -23.64
REMARK 500 GLU F 93 -9.15 56.21
REMARK 500 SER F 122 55.26 -101.26
REMARK 500 LYS F 123 31.49 -94.30
REMARK 500 GLN F 124 106.29 -58.07
REMARK 500 SER F 125 12.10 38.22
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1Z9C A 1 147 UNP O34777 OHRR_BACSU 1 147
DBREF 1Z9C B 1 147 UNP O34777 OHRR_BACSU 1 147
DBREF 1Z9C C 1 147 UNP O34777 OHRR_BACSU 1 147
DBREF 1Z9C D 1 147 UNP O34777 OHRR_BACSU 1 147
DBREF 1Z9C E 1 147 UNP O34777 OHRR_BACSU 1 147
DBREF 1Z9C F 1 147 UNP O34777 OHRR_BACSU 1 147
DBREF 1Z9C G 1 29 PDB 1Z9C 1Z9C 1 29
DBREF 1Z9C H 1 29 PDB 1Z9C 1Z9C 1 29
DBREF 1Z9C I 1 29 PDB 1Z9C 1Z9C 1 29
DBREF 1Z9C J 1 29 PDB 1Z9C 1Z9C 1 29
DBREF 1Z9C K 1 29 PDB 1Z9C 1Z9C 1 29
DBREF 1Z9C L 1 29 PDB 1Z9C 1Z9C 1 29
SEQADV 1Z9C SER A 15 UNP O34777 CYS 15 ENGINEERED MUTATION
SEQADV 1Z9C SER B 15 UNP O34777 CYS 15 ENGINEERED MUTATION
SEQADV 1Z9C SER C 15 UNP O34777 CYS 15 ENGINEERED MUTATION
SEQADV 1Z9C SER D 15 UNP O34777 CYS 15 ENGINEERED MUTATION
SEQADV 1Z9C SER E 15 UNP O34777 CYS 15 ENGINEERED MUTATION
SEQADV 1Z9C SER F 15 UNP O34777 CYS 15 ENGINEERED MUTATION
SEQRES 1 G 29 DT DA DC DA DA DT DT DT DA DA DT DT DG
SEQRES 2 G 29 DT DA DT DA DC DA DA DT DT DT DA DA DT
SEQRES 3 G 29 DT DG DT
SEQRES 1 H 29 DT DA DC DA DA DT DT DA DA DA DT DT DG
SEQRES 2 H 29 DT DA DT DA DC DA DA DT DT DA DA DA DT
SEQRES 3 H 29 DT DG DT
SEQRES 1 I 29 DT DA DC DA DA DT DT DT DA DA DT DT DG
SEQRES 2 I 29 DT DA DT DA DC DA DA DT DT DT DA DA DT
SEQRES 3 I 29 DT DG DT
SEQRES 1 J 29 DT DA DC DA DA DT DT DA DA DA DT DT DG
SEQRES 2 J 29 DT DA DT DA DC DA DA DT DT DA DA DA DT
SEQRES 3 J 29 DT DG DT
SEQRES 1 K 29 DT DA DC DA DA DT DT DT DA DA DT DT DG
SEQRES 2 K 29 DT DA DT DA DC DA DA DT DT DT DA DA DT
SEQRES 3 K 29 DT DG DT
SEQRES 1 L 29 DT DA DC DA DA DT DT DA DA DA DT DT DG
SEQRES 2 L 29 DT DA DT DA DC DA DA DT DT DA DA DA DT
SEQRES 3 L 29 DT DG DT
SEQRES 1 A 147 MET GLU ASN LYS PHE ASP HIS MET LYS LEU GLU ASN GLN
SEQRES 2 A 147 LEU SER PHE LEU LEU TYR ALA SER SER ARG GLU MET THR
SEQRES 3 A 147 LYS GLN TYR LYS PRO LEU LEU ASP LYS LEU ASN ILE THR
SEQRES 4 A 147 TYR PRO GLN TYR LEU ALA LEU LEU LEU LEU TRP GLU HIS
SEQRES 5 A 147 GLU THR LEU THR VAL LYS LYS MET GLY GLU GLN LEU TYR
SEQRES 6 A 147 LEU ASP SER GLY THR LEU THR PRO MET LEU LYS ARG MET
SEQRES 7 A 147 GLU GLN GLN GLY LEU ILE THR ARG LYS ARG SER GLU GLU
SEQRES 8 A 147 ASP GLU ARG SER VAL LEU ILE SER LEU THR GLU ASP GLY
SEQRES 9 A 147 ALA LEU LEU LYS GLU LYS ALA VAL ASP ILE PRO GLY THR
SEQRES 10 A 147 ILE LEU GLY LEU SER LYS GLN SER GLY GLU ASP LEU LYS
SEQRES 11 A 147 GLN LEU LYS SER ALA LEU TYR THR LEU LEU GLU THR LEU
SEQRES 12 A 147 HIS GLN LYS ASN
SEQRES 1 B 147 MET GLU ASN LYS PHE ASP HIS MET LYS LEU GLU ASN GLN
SEQRES 2 B 147 LEU SER PHE LEU LEU TYR ALA SER SER ARG GLU MET THR
SEQRES 3 B 147 LYS GLN TYR LYS PRO LEU LEU ASP LYS LEU ASN ILE THR
SEQRES 4 B 147 TYR PRO GLN TYR LEU ALA LEU LEU LEU LEU TRP GLU HIS
SEQRES 5 B 147 GLU THR LEU THR VAL LYS LYS MET GLY GLU GLN LEU TYR
SEQRES 6 B 147 LEU ASP SER GLY THR LEU THR PRO MET LEU LYS ARG MET
SEQRES 7 B 147 GLU GLN GLN GLY LEU ILE THR ARG LYS ARG SER GLU GLU
SEQRES 8 B 147 ASP GLU ARG SER VAL LEU ILE SER LEU THR GLU ASP GLY
SEQRES 9 B 147 ALA LEU LEU LYS GLU LYS ALA VAL ASP ILE PRO GLY THR
SEQRES 10 B 147 ILE LEU GLY LEU SER LYS GLN SER GLY GLU ASP LEU LYS
SEQRES 11 B 147 GLN LEU LYS SER ALA LEU TYR THR LEU LEU GLU THR LEU
SEQRES 12 B 147 HIS GLN LYS ASN
SEQRES 1 C 147 MET GLU ASN LYS PHE ASP HIS MET LYS LEU GLU ASN GLN
SEQRES 2 C 147 LEU SER PHE LEU LEU TYR ALA SER SER ARG GLU MET THR
SEQRES 3 C 147 LYS GLN TYR LYS PRO LEU LEU ASP LYS LEU ASN ILE THR
SEQRES 4 C 147 TYR PRO GLN TYR LEU ALA LEU LEU LEU LEU TRP GLU HIS
SEQRES 5 C 147 GLU THR LEU THR VAL LYS LYS MET GLY GLU GLN LEU TYR
SEQRES 6 C 147 LEU ASP SER GLY THR LEU THR PRO MET LEU LYS ARG MET
SEQRES 7 C 147 GLU GLN GLN GLY LEU ILE THR ARG LYS ARG SER GLU GLU
SEQRES 8 C 147 ASP GLU ARG SER VAL LEU ILE SER LEU THR GLU ASP GLY
SEQRES 9 C 147 ALA LEU LEU LYS GLU LYS ALA VAL ASP ILE PRO GLY THR
SEQRES 10 C 147 ILE LEU GLY LEU SER LYS GLN SER GLY GLU ASP LEU LYS
SEQRES 11 C 147 GLN LEU LYS SER ALA LEU TYR THR LEU LEU GLU THR LEU
SEQRES 12 C 147 HIS GLN LYS ASN
SEQRES 1 D 147 MET GLU ASN LYS PHE ASP HIS MET LYS LEU GLU ASN GLN
SEQRES 2 D 147 LEU SER PHE LEU LEU TYR ALA SER SER ARG GLU MET THR
SEQRES 3 D 147 LYS GLN TYR LYS PRO LEU LEU ASP LYS LEU ASN ILE THR
SEQRES 4 D 147 TYR PRO GLN TYR LEU ALA LEU LEU LEU LEU TRP GLU HIS
SEQRES 5 D 147 GLU THR LEU THR VAL LYS LYS MET GLY GLU GLN LEU TYR
SEQRES 6 D 147 LEU ASP SER GLY THR LEU THR PRO MET LEU LYS ARG MET
SEQRES 7 D 147 GLU GLN GLN GLY LEU ILE THR ARG LYS ARG SER GLU GLU
SEQRES 8 D 147 ASP GLU ARG SER VAL LEU ILE SER LEU THR GLU ASP GLY
SEQRES 9 D 147 ALA LEU LEU LYS GLU LYS ALA VAL ASP ILE PRO GLY THR
SEQRES 10 D 147 ILE LEU GLY LEU SER LYS GLN SER GLY GLU ASP LEU LYS
SEQRES 11 D 147 GLN LEU LYS SER ALA LEU TYR THR LEU LEU GLU THR LEU
SEQRES 12 D 147 HIS GLN LYS ASN
SEQRES 1 E 147 MET GLU ASN LYS PHE ASP HIS MET LYS LEU GLU ASN GLN
SEQRES 2 E 147 LEU SER PHE LEU LEU TYR ALA SER SER ARG GLU MET THR
SEQRES 3 E 147 LYS GLN TYR LYS PRO LEU LEU ASP LYS LEU ASN ILE THR
SEQRES 4 E 147 TYR PRO GLN TYR LEU ALA LEU LEU LEU LEU TRP GLU HIS
SEQRES 5 E 147 GLU THR LEU THR VAL LYS LYS MET GLY GLU GLN LEU TYR
SEQRES 6 E 147 LEU ASP SER GLY THR LEU THR PRO MET LEU LYS ARG MET
SEQRES 7 E 147 GLU GLN GLN GLY LEU ILE THR ARG LYS ARG SER GLU GLU
SEQRES 8 E 147 ASP GLU ARG SER VAL LEU ILE SER LEU THR GLU ASP GLY
SEQRES 9 E 147 ALA LEU LEU LYS GLU LYS ALA VAL ASP ILE PRO GLY THR
SEQRES 10 E 147 ILE LEU GLY LEU SER LYS GLN SER GLY GLU ASP LEU LYS
SEQRES 11 E 147 GLN LEU LYS SER ALA LEU TYR THR LEU LEU GLU THR LEU
SEQRES 12 E 147 HIS GLN LYS ASN
SEQRES 1 F 147 MET GLU ASN LYS PHE ASP HIS MET LYS LEU GLU ASN GLN
SEQRES 2 F 147 LEU SER PHE LEU LEU TYR ALA SER SER ARG GLU MET THR
SEQRES 3 F 147 LYS GLN TYR LYS PRO LEU LEU ASP LYS LEU ASN ILE THR
SEQRES 4 F 147 TYR PRO GLN TYR LEU ALA LEU LEU LEU LEU TRP GLU HIS
SEQRES 5 F 147 GLU THR LEU THR VAL LYS LYS MET GLY GLU GLN LEU TYR
SEQRES 6 F 147 LEU ASP SER GLY THR LEU THR PRO MET LEU LYS ARG MET
SEQRES 7 F 147 GLU GLN GLN GLY LEU ILE THR ARG LYS ARG SER GLU GLU
SEQRES 8 F 147 ASP GLU ARG SER VAL LEU ILE SER LEU THR GLU ASP GLY
SEQRES 9 F 147 ALA LEU LEU LYS GLU LYS ALA VAL ASP ILE PRO GLY THR
SEQRES 10 F 147 ILE LEU GLY LEU SER LYS GLN SER GLY GLU ASP LEU LYS
SEQRES 11 F 147 GLN LEU LYS SER ALA LEU TYR THR LEU LEU GLU THR LEU
SEQRES 12 F 147 HIS GLN LYS ASN
FORMUL 13 HOH *174(H2 O)
HELIX 1 1 GLN A 13 LEU A 36 1 24
HELIX 2 2 THR A 39 TRP A 50 1 12
HELIX 3 3 VAL A 57 TYR A 65 1 9
HELIX 4 4 ASP A 67 GLN A 81 1 15
HELIX 5 5 THR A 101 LEU A 107 1 7
HELIX 6 6 LYS A 108 VAL A 112 5 5
HELIX 7 7 ASP A 113 LYS A 123 1 11
HELIX 8 8 ASP A 128 LEU A 143 1 16
HELIX 9 9 LYS B 9 ASN B 12 5 4
HELIX 10 10 GLN B 13 LYS B 35 1 23
HELIX 11 11 THR B 39 GLU B 51 1 13
HELIX 12 12 VAL B 57 TYR B 65 1 9
HELIX 13 13 THR B 70 GLN B 81 1 12
HELIX 14 14 THR B 101 LEU B 107 1 7
HELIX 15 15 LYS B 108 VAL B 112 5 5
HELIX 16 16 ASP B 113 LYS B 123 1 11
HELIX 17 17 ASP B 128 HIS B 144 1 17
HELIX 18 18 LYS C 9 ASN C 12 5 4
HELIX 19 19 GLN C 13 LEU C 36 1 24
HELIX 20 20 THR C 39 TRP C 50 1 12
HELIX 21 21 VAL C 57 TYR C 65 1 9
HELIX 22 22 ASP C 67 GLN C 81 1 15
HELIX 23 23 THR C 101 VAL C 112 1 12
HELIX 24 24 ASP C 113 LYS C 123 1 11
HELIX 25 25 LYS C 130 LEU C 143 1 14
HELIX 26 26 LYS D 9 ASN D 12 5 4
HELIX 27 27 GLN D 13 LYS D 35 1 23
HELIX 28 28 THR D 39 TRP D 50 1 12
HELIX 29 29 VAL D 57 LEU D 64 1 8
HELIX 30 30 THR D 70 GLN D 81 1 12
HELIX 31 31 THR D 101 LYS D 108 1 8
HELIX 32 32 GLU D 109 ALA D 111 5 3
HELIX 33 33 VAL D 112 LYS D 123 1 12
HELIX 34 34 ASP D 128 LEU D 143 1 16
HELIX 35 35 LYS E 9 ASN E 12 5 4
HELIX 36 36 GLN E 13 LYS E 35 1 23
HELIX 37 37 THR E 39 HIS E 52 1 14
HELIX 38 38 VAL E 57 TYR E 65 1 9
HELIX 39 39 ASP E 67 GLN E 81 1 15
HELIX 40 40 THR E 101 LEU E 107 1 7
HELIX 41 41 LYS E 108 VAL E 112 5 5
HELIX 42 42 ASP E 113 LYS E 123 1 11
HELIX 43 43 ASP E 128 HIS E 144 1 17
HELIX 44 44 LYS F 9 ASN F 12 5 4
HELIX 45 45 GLN F 13 LYS F 35 1 23
HELIX 46 46 THR F 39 HIS F 52 1 14
HELIX 47 47 VAL F 57 TYR F 65 1 9
HELIX 48 48 THR F 70 GLN F 81 1 12
HELIX 49 49 THR F 101 LEU F 107 1 7
HELIX 50 50 LYS F 108 ALA F 111 5 4
HELIX 51 51 VAL F 112 SER F 122 1 11
HELIX 52 52 ASP F 128 LEU F 143 1 16
SHEET 1 A 3 THR A 54 THR A 56 0
SHEET 2 A 3 VAL A 96 LEU A 100 -1 O ILE A 98 N LEU A 55
SHEET 3 A 3 ILE A 84 ARG A 88 -1 N LYS A 87 O LEU A 97
SHEET 1 B 3 THR B 54 THR B 56 0
SHEET 2 B 3 VAL B 96 LEU B 100 -1 O ILE B 98 N LEU B 55
SHEET 3 B 3 ILE B 84 ARG B 88 -1 N THR B 85 O SER B 99
SHEET 1 C 3 THR C 54 THR C 56 0
SHEET 2 C 3 VAL C 96 LEU C 100 -1 O ILE C 98 N LEU C 55
SHEET 3 C 3 ILE C 84 ARG C 88 -1 N LYS C 87 O LEU C 97
SHEET 1 D 3 THR D 54 THR D 56 0
SHEET 2 D 3 VAL D 96 LEU D 100 -1 O ILE D 98 N LEU D 55
SHEET 3 D 3 ILE D 84 ARG D 88 -1 N THR D 85 O SER D 99
SHEET 1 E 3 THR E 54 THR E 56 0
SHEET 2 E 3 VAL E 96 LEU E 100 -1 O ILE E 98 N LEU E 55
SHEET 3 E 3 ILE E 84 ARG E 88 -1 N THR E 85 O SER E 99
SHEET 1 F 3 THR F 54 THR F 56 0
SHEET 2 F 3 VAL F 96 LEU F 100 -1 O ILE F 98 N LEU F 55
SHEET 3 F 3 ILE F 84 ARG F 88 -1 N LYS F 87 O LEU F 97
CRYST1 81.899 80.960 109.340 90.00 100.20 90.00 P 1 21 1 12
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 0.012210 0.000000 0.002197 0.00000
SCALE2 0.000000 0.012352 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009293 0.00000
(ATOM LINES ARE NOT SHOWN.)
END