HEADER DNA BINDING PROTEIN/DNA 08-SEP-09 3JRH
TITLE CRYSTAL STRUCTURE OF FIS BOUND TO 27 BP NON CONSENSUS SEQUENCE DNA F21
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DNA-BINDING PROTEIN FIS;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: DNA (27-MER);
COMPND 7 CHAIN: C;
COMPND 8 ENGINEERED: YES;
COMPND 9 MOL_ID: 3;
COMPND 10 MOLECULE: DNA (27-MER);
COMPND 11 CHAIN: D;
COMPND 12 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 83333;
SOURCE 4 STRAIN: K-12;
SOURCE 5 GENE: FIS, B3261, JW3229;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET11A;
SOURCE 11 MOL_ID: 2;
SOURCE 12 SYNTHETIC: YES;
SOURCE 13 MOL_ID: 3;
SOURCE 14 SYNTHETIC: YES
KEYWDS HTH DOMAIN, PROTEIN-DNA COMPLEX, MINOR GROOVE COMPRESSION, DNA
KEYWDS 2 BENDING, INDIRECT RECOGNITION, ACTIVATOR, DNA-BINDING,
KEYWDS 3 TRANSCRIPTION, TRANSCRIPTION REGULATION, DNA BINDING PROTEIN-DNA
KEYWDS 4 COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR S.STELLA,D.CASCIO,R.C.JOHNSON
REVDAT 4 06-SEP-23 3JRH 1 REMARK
REVDAT 3 01-NOV-17 3JRH 1 REMARK
REVDAT 2 13-JUL-11 3JRH 1 VERSN
REVDAT 1 28-APR-10 3JRH 0
JRNL AUTH S.STELLA,D.CASCIO,R.C.JOHNSON
JRNL TITL THE SHAPE OF THE DNA MINOR GROOVE DIRECTS BINDING BY THE
JRNL TITL 2 DNA-BENDING PROTEIN FIS.
JRNL REF GENES DEV. V. 24 814 2010
JRNL REFN ISSN 0890-9369
JRNL PMID 20395367
JRNL DOI 10.1101/GAD.1900610
REMARK 2
REMARK 2 RESOLUTION. 2.88 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.88
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.3
REMARK 3 NUMBER OF REFLECTIONS : 14332
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 + TEST SET) : 0.224
REMARK 3 R VALUE (WORKING SET) : 0.222
REMARK 3 FREE R VALUE : 0.253
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 727
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) : 2.88
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.95
REMARK 3 REFLECTION IN BIN (WORKING SET) : 965
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 94.49
REMARK 3 BIN R VALUE (WORKING SET) : 0.3440
REMARK 3 BIN FREE R VALUE SET COUNT : 46
REMARK 3 BIN FREE R VALUE : 0.3810
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1505
REMARK 3 NUCLEIC ACID ATOMS : 1101
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 14
REMARK 3
REMARK 3 B VALUES.
REMARK 3 B VALUE TYPE : LIKELY RESIDUAL
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 75.84
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 OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): NULL
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.255
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.951
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.934
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2752 ; 0.014 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 1523 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3942 ; 1.913 ; 2.470
REMARK 3 BOND ANGLES OTHERS (DEGREES): 3785 ; 1.140 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 187 ; 5.268 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 75 ;38.806 ;25.600
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 303 ;19.205 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 11 ;16.176 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): NULL ; NULL ; NULL
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2232 ; 0.005 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 274 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 660 ; 0.221 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 1731 ; 0.215 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 1246 ; 0.217 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): 1177 ; 0.094 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 55 ; 0.187 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 17 ; 0.246 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 28 ; 0.224 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 7 ; 0.208 ; 0.200
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 4
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 8 A 98
REMARK 3 ORIGIN FOR THE GROUP (A): -12.7734 10.8198 -8.9196
REMARK 3 T TENSOR
REMARK 3 T11: -0.2030 T22: -0.1203
REMARK 3 T33: -0.3038 T12: 0.0194
REMARK 3 T13: -0.0270 T23: 0.0398
REMARK 3 L TENSOR
REMARK 3 L11: 1.6972 L22: 4.4391
REMARK 3 L33: 2.9864 L12: 0.8890
REMARK 3 L13: -0.0792 L23: 0.1211
REMARK 3 S TENSOR
REMARK 3 S11: -0.1328 S12: 0.2544 S13: -0.0577
REMARK 3 S21: -0.4080 S22: 0.1694 S23: 0.1827
REMARK 3 S31: 0.4932 S32: -0.1405 S33: -0.0366
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 1 B 98
REMARK 3 ORIGIN FOR THE GROUP (A): -9.7827 11.2040 -2.1920
REMARK 3 T TENSOR
REMARK 3 T11: -0.2726 T22: -0.2293
REMARK 3 T33: -0.2824 T12: -0.0741
REMARK 3 T13: -0.0227 T23: 0.0009
REMARK 3 L TENSOR
REMARK 3 L11: 3.1479 L22: 3.7375
REMARK 3 L33: 3.7626 L12: -1.0240
REMARK 3 L13: -0.1719 L23: 0.0870
REMARK 3 S TENSOR
REMARK 3 S11: -0.1208 S12: 0.2188 S13: 0.0529
REMARK 3 S21: -0.1118 S22: 0.0481 S23: -0.2814
REMARK 3 S31: 0.1708 S32: 0.1118 S33: 0.0728
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 1 C 27
REMARK 3 ORIGIN FOR THE GROUP (A): -11.6642 -10.0797 -5.5194
REMARK 3 T TENSOR
REMARK 3 T11: 0.3542 T22: 0.0041
REMARK 3 T33: -0.0040 T12: -0.0581
REMARK 3 T13: -0.0757 T23: -0.0475
REMARK 3 L TENSOR
REMARK 3 L11: 1.2582 L22: 0.7436
REMARK 3 L33: 9.8066 L12: -0.1616
REMARK 3 L13: 2.6705 L23: -0.6546
REMARK 3 S TENSOR
REMARK 3 S11: 0.5251 S12: 0.1318 S13: -0.6627
REMARK 3 S21: -0.1785 S22: 0.2127 S23: -0.0447
REMARK 3 S31: 1.8154 S32: -0.1450 S33: -0.7377
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 1 D 27
REMARK 3 ORIGIN FOR THE GROUP (A): -10.7457 -10.0801 -6.0911
REMARK 3 T TENSOR
REMARK 3 T11: 0.2960 T22: -0.0797
REMARK 3 T33: -0.0132 T12: 0.0145
REMARK 3 T13: -0.0768 T23: 0.0256
REMARK 3 L TENSOR
REMARK 3 L11: 1.3382 L22: 0.6484
REMARK 3 L33: 15.1896 L12: -0.0699
REMARK 3 L13: 3.4503 L23: -0.6678
REMARK 3 S TENSOR
REMARK 3 S11: 0.4696 S12: 0.0162 S13: -0.6480
REMARK 3 S21: -0.2061 S22: 0.1890 S23: 0.0879
REMARK 3 S31: 2.0070 S32: -0.1429 S33: -0.6587
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : NULL
REMARK 3 ION PROBE RADIUS : NULL
REMARK 3 SHRINKAGE RADIUS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 3JRH COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-SEP-09.
REMARK 100 THE DEPOSITION ID IS D_1000055066.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 24-ID-C
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : NULL
REMARK 200 WAVELENGTH OR RANGE (A) : 1.000
REMARK 200 MONOCHROMATOR : SI (111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 14365
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.880
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.5
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
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) : 2.88
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.00
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.9
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.78400
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: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 3IV5
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 69.25
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.00
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M SODIUM CITRATE, 0.1 M TRIS-HCL
REMARK 280 PH 8.5, 36% PEG 400, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE
REMARK 280 277K
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 -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
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 21.56300
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 77.27000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 46.93100
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 77.27000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 21.56300
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 46.93100
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 8700 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 19130 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -56.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, 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 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 MET A 1
REMARK 465 PHE A 2
REMARK 465 GLU A 3
REMARK 465 GLN A 4
REMARK 465 ARG A 5
REMARK 465 VAL A 6
REMARK 465 ASN A 7
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 DA C 3 O3' DA C 3 C3' -0.039
REMARK 500 DT C 5 O3' DT C 5 C3' -0.036
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 C 8 O4' - C1' - N1 ANGL. DEV. = 5.0 DEGREES
REMARK 500 DT C 8 N3 - C2 - O2 ANGL. DEV. = -3.9 DEGREES
REMARK 500 DT C 9 O4' - C1' - N1 ANGL. DEV. = 4.6 DEGREES
REMARK 500 DT C 14 O4' - C1' - C2' ANGL. DEV. = -6.3 DEGREES
REMARK 500 DT C 14 N3 - C2 - O2 ANGL. DEV. = -4.4 DEGREES
REMARK 500 DT C 14 C3' - O3' - P ANGL. DEV. = 9.0 DEGREES
REMARK 500 DT C 15 C3' - O3' - P ANGL. DEV. = 10.0 DEGREES
REMARK 500 DA C 19 C1' - O4' - C4' ANGL. DEV. = -6.2 DEGREES
REMARK 500 DA C 19 C3' - O3' - P ANGL. DEV. = 7.8 DEGREES
REMARK 500 DA C 23 C3' - O3' - P ANGL. DEV. = 7.8 DEGREES
REMARK 500 DA D 1 C4' - C3' - C2' ANGL. DEV. = -4.7 DEGREES
REMARK 500 DA D 1 O4' - C1' - N9 ANGL. DEV. = 4.9 DEGREES
REMARK 500 DA D 1 C3' - O3' - P ANGL. DEV. = 8.2 DEGREES
REMARK 500 DG D 7 O4' - C1' - N9 ANGL. DEV. = 2.1 DEGREES
REMARK 500 DC D 8 O4' - C1' - N1 ANGL. DEV. = 4.2 DEGREES
REMARK 500 DT D 9 C4' - C3' - C2' ANGL. DEV. = 5.5 DEGREES
REMARK 500 DT D 9 O4' - C1' - N1 ANGL. DEV. = 4.9 DEGREES
REMARK 500 DC D 11 O4' - C1' - N1 ANGL. DEV. = 4.1 DEGREES
REMARK 500 DA D 12 O4' - C1' - N9 ANGL. DEV. = 3.2 DEGREES
REMARK 500 DA D 12 C3' - O3' - P ANGL. DEV. = 12.5 DEGREES
REMARK 500 DA D 14 N1 - C6 - N6 ANGL. DEV. = 3.9 DEGREES
REMARK 500 DA D 14 C3' - O3' - P ANGL. DEV. = 8.1 DEGREES
REMARK 500 DA D 18 C3' - O3' - P ANGL. DEV. = 9.3 DEGREES
REMARK 500 DA D 19 C3' - C2' - C1' ANGL. DEV. = -5.5 DEGREES
REMARK 500 DA D 20 O4' - C1' - N9 ANGL. DEV. = 5.5 DEGREES
REMARK 500 DC D 21 O4' - C1' - N1 ANGL. DEV. = 2.2 DEGREES
REMARK 500 DA D 22 O3' - P - O5' ANGL. DEV. = -12.2 DEGREES
REMARK 500 DA D 23 C3' - C2' - C1' ANGL. DEV. = -5.6 DEGREES
REMARK 500 DA D 23 O4' - C1' - N9 ANGL. DEV. = 3.9 DEGREES
REMARK 500 DT D 25 O4' - C1' - N1 ANGL. DEV. = 6.3 DEGREES
REMARK 500 DT D 25 N3 - C4 - O4 ANGL. DEV. = 4.3 DEGREES
REMARK 500 DT D 25 C5 - C4 - O4 ANGL. DEV. = -6.0 DEGREES
REMARK 500 DT D 26 O4' - C1' - N1 ANGL. DEV. = -5.2 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 ASN A 43 76.29 -109.03
REMARK 500 ARG A 71 61.84 36.04
REMARK 500 SER B 18 1.26 -53.31
REMARK 500 ASN B 43 79.90 42.23
REMARK 500 ARG B 71 44.37 35.19
REMARK 500 MET B 97 73.30 -107.51
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3IV5 RELATED DB: PDB
REMARK 900 RELATED ID: 3JR9 RELATED DB: PDB
REMARK 900 RELATED ID: 3JRA RELATED DB: PDB
REMARK 900 RELATED ID: 3JRB RELATED DB: PDB
REMARK 900 RELATED ID: 3JRC RELATED DB: PDB
REMARK 900 RELATED ID: 3JRD RELATED DB: PDB
REMARK 900 RELATED ID: 3JRE RELATED DB: PDB
REMARK 900 RELATED ID: 3JRF RELATED DB: PDB
REMARK 900 RELATED ID: 3JRG RELATED DB: PDB
REMARK 900 RELATED ID: 3JRI RELATED DB: PDB
DBREF 3JRH A 1 98 UNP P0A6R3 FIS_ECOLI 1 98
DBREF 3JRH B 1 98 UNP P0A6R3 FIS_ECOLI 1 98
DBREF 3JRH C 1 27 PDB 3JRH 3JRH 1 27
DBREF 3JRH D 1 27 PDB 3JRH 3JRH 1 27
SEQRES 1 A 98 MET PHE GLU GLN ARG VAL ASN SER ASP VAL LEU THR VAL
SEQRES 2 A 98 SER THR VAL ASN SER GLN ASP GLN VAL THR GLN LYS PRO
SEQRES 3 A 98 LEU ARG ASP SER VAL LYS GLN ALA LEU LYS ASN TYR PHE
SEQRES 4 A 98 ALA GLN LEU ASN GLY GLN ASP VAL ASN ASP LEU TYR GLU
SEQRES 5 A 98 LEU VAL LEU ALA GLU VAL GLU GLN PRO LEU LEU ASP MET
SEQRES 6 A 98 VAL MET GLN TYR THR ARG GLY ASN GLN THR ARG ALA ALA
SEQRES 7 A 98 LEU MET MET GLY ILE ASN ARG GLY THR LEU ARG LYS LYS
SEQRES 8 A 98 LEU LYS LYS TYR GLY MET ASN
SEQRES 1 B 98 MET PHE GLU GLN ARG VAL ASN SER ASP VAL LEU THR VAL
SEQRES 2 B 98 SER THR VAL ASN SER GLN ASP GLN VAL THR GLN LYS PRO
SEQRES 3 B 98 LEU ARG ASP SER VAL LYS GLN ALA LEU LYS ASN TYR PHE
SEQRES 4 B 98 ALA GLN LEU ASN GLY GLN ASP VAL ASN ASP LEU TYR GLU
SEQRES 5 B 98 LEU VAL LEU ALA GLU VAL GLU GLN PRO LEU LEU ASP MET
SEQRES 6 B 98 VAL MET GLN TYR THR ARG GLY ASN GLN THR ARG ALA ALA
SEQRES 7 B 98 LEU MET MET GLY ILE ASN ARG GLY THR LEU ARG LYS LYS
SEQRES 8 B 98 LEU LYS LYS TYR GLY MET ASN
SEQRES 1 C 27 DA DA DA DT DT DT DG DT DT DT DC DA DA
SEQRES 2 C 27 DT DT DT DG DG DA DG DC DA DA DA DT DT
SEQRES 3 C 27 DT
SEQRES 1 D 27 DA DA DA DT DT DT DG DC DT DC DC DA DA
SEQRES 2 D 27 DA DT DT DG DA DA DA DC DA DA DA DT DT
SEQRES 3 D 27 DT
FORMUL 5 HOH *14(H2 O)
HELIX 1 1 LEU A 27 LEU A 42 1 16
HELIX 2 2 ASP A 49 THR A 70 1 22
HELIX 3 3 ASN A 73 GLY A 82 1 10
HELIX 4 4 ASN A 84 TYR A 95 1 12
HELIX 5 5 VAL B 6 VAL B 10 5 5
HELIX 6 6 LEU B 27 ASN B 43 1 17
HELIX 7 7 ASP B 49 THR B 70 1 22
HELIX 8 8 ASN B 73 GLY B 82 1 10
HELIX 9 9 ASN B 84 TYR B 95 1 12
SHEET 1 A 2 THR A 12 VAL A 16 0
SHEET 2 A 2 VAL A 22 PRO A 26 -1 O THR A 23 N THR A 15
SHEET 1 B 2 THR B 12 ASN B 17 0
SHEET 2 B 2 GLN B 21 PRO B 26 -1 O LYS B 25 N VAL B 13
CRYST1 43.126 93.862 154.540 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 0.023188 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010654 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006471 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
