HEADER CHAPERONE/PEPTIDE BINDING PROTEIN 03-MAY-12 4EZX
TITLE CRYSTAL STRUCTURE OF THE SUBSTRATE BINDING DOMAIN OF E.COLI DNAK IN
TITLE 2 COMPLEX WITH THE DESIGNER PEPTIDE NRLMLTG
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CHAPERONE PROTEIN DNAK;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: UNP RESIDUES 389-607;
COMPND 5 SYNONYM: HSP70, HEAT SHOCK 70 KDA PROTEIN, HEAT SHOCK PROTEIN 70;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: SYNTHETIC PEPTIDE NRLMLTG;
COMPND 9 CHAIN: C, D;
COMPND 10 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: B0014, DNAK, GROP, GRPF, JW0013, SEG;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 MOL_ID: 2;
SOURCE 9 SYNTHETIC: YES;
SOURCE 10 OTHER_DETAILS: SYNTHETIC PEPTIDE
KEYWDS CHAPERONE, CHAPERONE-PEPTIDE BINDING PROTEIN COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR M.ZAHN,N.STRAETER
REVDAT 4 28-FEB-24 4EZX 1 REMARK
REVDAT 3 15-NOV-17 4EZX 1 REMARK
REVDAT 2 17-JUL-13 4EZX 1 JRNL
REVDAT 1 17-APR-13 4EZX 0
JRNL AUTH M.ZAHN,N.BERTHOLD,B.KIESLICH,D.KNAPPE,R.HOFFMANN,N.STRATER
JRNL TITL STRUCTURAL STUDIES ON THE FORWARD AND REVERSE BINDING MODES
JRNL TITL 2 OF PEPTIDES TO THE CHAPERONE DNAK.
JRNL REF J.MOL.BIOL. V. 425 2463 2013
JRNL REFN ISSN 0022-2836
JRNL PMID 23562829
JRNL DOI 10.1016/J.JMB.2013.03.041
REMARK 2
REMARK 2 RESOLUTION. 1.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.6.0117
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) : 1.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 25.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 3 NUMBER OF REFLECTIONS : 57368
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 + TEST SET) : 0.177
REMARK 3 R VALUE (WORKING SET) : 0.177
REMARK 3 FREE R VALUE : 0.209
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 2.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1195
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.70
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.75
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3713
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 94.09
REMARK 3 BIN R VALUE (WORKING SET) : 0.2750
REMARK 3 BIN FREE R VALUE SET COUNT : 78
REMARK 3 BIN FREE R VALUE : 0.3020
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3321
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 25
REMARK 3 SOLVENT ATOMS : 337
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 25.44
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.57000
REMARK 3 B22 (A**2) : 0.15000
REMARK 3 B33 (A**2) : 0.42000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.090
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.092
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.059
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.417
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.959
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.940
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3460 ; 0.022 ; 0.020
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4689 ; 2.246 ; 1.982
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 464 ; 5.173 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 158 ;38.386 ;26.709
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 672 ;15.265 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 16 ;22.396 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 559 ; 0.174 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2548 ; 0.011 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
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): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
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 : 6
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 389 A 512
REMARK 3 ORIGIN FOR THE GROUP (A): 6.5536 -33.9260 0.5008
REMARK 3 T TENSOR
REMARK 3 T11: 0.0552 T22: 0.0647
REMARK 3 T33: 0.0559 T12: 0.0013
REMARK 3 T13: -0.0033 T23: -0.0082
REMARK 3 L TENSOR
REMARK 3 L11: 1.2554 L22: 0.1749
REMARK 3 L33: 0.2652 L12: 0.1297
REMARK 3 L13: 0.4492 L23: 0.1036
REMARK 3 S TENSOR
REMARK 3 S11: 0.0009 S12: 0.0131 S13: -0.0463
REMARK 3 S21: 0.0077 S22: 0.0188 S23: 0.0038
REMARK 3 S31: 0.0058 S32: -0.0139 S33: -0.0197
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 : A 513 A 558
REMARK 3 ORIGIN FOR THE GROUP (A): -3.2804 -17.6552 -6.6688
REMARK 3 T TENSOR
REMARK 3 T11: 0.0656 T22: 0.0347
REMARK 3 T33: 0.0936 T12: 0.0193
REMARK 3 T13: -0.0145 T23: 0.0098
REMARK 3 L TENSOR
REMARK 3 L11: 5.5912 L22: 1.2351
REMARK 3 L33: 2.3006 L12: -0.9890
REMARK 3 L13: 3.2035 L23: -0.7227
REMARK 3 S TENSOR
REMARK 3 S11: 0.0688 S12: 0.0533 S13: 0.0667
REMARK 3 S21: -0.1458 S22: 0.0181 S23: 0.1570
REMARK 3 S31: 0.0208 S32: -0.0436 S33: -0.0868
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 : A 559 A 600
REMARK 3 ORIGIN FOR THE GROUP (A): -13.0642 -10.8438 -15.2656
REMARK 3 T TENSOR
REMARK 3 T11: 0.1127 T22: 0.0848
REMARK 3 T33: 0.0722 T12: 0.0342
REMARK 3 T13: -0.0223 T23: 0.0547
REMARK 3 L TENSOR
REMARK 3 L11: 5.7425 L22: 3.8367
REMARK 3 L33: 6.5174 L12: -1.2789
REMARK 3 L13: 3.5164 L23: 0.9541
REMARK 3 S TENSOR
REMARK 3 S11: 0.1837 S12: 0.2315 S13: 0.1058
REMARK 3 S21: -0.3466 S22: -0.1326 S23: 0.0888
REMARK 3 S31: -0.1599 S32: -0.3230 S33: -0.0511
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 : B 389 B 508
REMARK 3 ORIGIN FOR THE GROUP (A): -28.5329 21.1840 -14.8269
REMARK 3 T TENSOR
REMARK 3 T11: 0.0595 T22: 0.0808
REMARK 3 T33: 0.0618 T12: -0.0167
REMARK 3 T13: 0.0041 T23: 0.0372
REMARK 3 L TENSOR
REMARK 3 L11: 0.6394 L22: 0.8980
REMARK 3 L33: 0.8327 L12: -0.0637
REMARK 3 L13: 0.1070 L23: -0.3409
REMARK 3 S TENSOR
REMARK 3 S11: 0.0580 S12: -0.0684 S13: -0.0879
REMARK 3 S21: 0.0850 S22: 0.0275 S23: 0.1381
REMARK 3 S31: 0.0409 S32: -0.1181 S33: -0.0855
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 509 B 547
REMARK 3 ORIGIN FOR THE GROUP (A): -14.1478 12.7736 -12.7913
REMARK 3 T TENSOR
REMARK 3 T11: 0.0812 T22: 0.0639
REMARK 3 T33: 0.1050 T12: 0.0150
REMARK 3 T13: -0.0213 T23: 0.0273
REMARK 3 L TENSOR
REMARK 3 L11: 1.0967 L22: 6.2702
REMARK 3 L33: 2.3424 L12: 0.9924
REMARK 3 L13: -0.4279 L23: -3.4600
REMARK 3 S TENSOR
REMARK 3 S11: -0.0280 S12: -0.0415 S13: -0.2236
REMARK 3 S21: -0.1960 S22: -0.0856 S23: -0.2904
REMARK 3 S31: 0.1786 S32: 0.1660 S33: 0.1136
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 548 B 599
REMARK 3 ORIGIN FOR THE GROUP (A): -18.8402 -6.3137 2.9943
REMARK 3 T TENSOR
REMARK 3 T11: 0.1836 T22: 0.1229
REMARK 3 T33: 0.1316 T12: 0.0749
REMARK 3 T13: 0.0147 T23: 0.1009
REMARK 3 L TENSOR
REMARK 3 L11: 3.8137 L22: 7.1995
REMARK 3 L33: 4.9850 L12: -0.1474
REMARK 3 L13: -1.5163 L23: -3.1295
REMARK 3 S TENSOR
REMARK 3 S11: -0.1592 S12: -0.4076 S13: -0.2106
REMARK 3 S21: 0.5952 S22: 0.4719 S23: 0.4239
REMARK 3 S31: -0.0204 S32: -0.2547 S33: -0.3127
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN USED IF PRESENT IN
REMARK 3 THE INPUT
REMARK 4
REMARK 4 4EZX COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 31-MAY-12.
REMARK 100 THE DEPOSITION ID IS D_1000072279.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-JAN-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : BESSY
REMARK 200 BEAMLINE : 14.1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.918
REMARK 200 MONOCHROMATOR : SI 111
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 58626
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.700
REMARK 200 RESOLUTION RANGE LOW (A) : 25.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.05300
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) : 1.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.79
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.3
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.43900
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: MOLREP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 53.91
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.67
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 2.1 M AMMONIUM SULFATE, 0.1 M CITRIC
REMARK 280 ACID PH 4.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 292K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -X+1/2,Y+1/2,-Z
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 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 38.80550
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 74.67250
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 38.80550
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 74.67250
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4440 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 22770 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -102.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C
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 APPLY THE FOLLOWING TO CHAINS: B, D
REMARK 350 BIOMT1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4980 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 22230 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -87.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C
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 APPLY THE FOLLOWING TO CHAINS: B, D
REMARK 350 BIOMT1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 45.35500
REMARK 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1970 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 12080 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -66.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C
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: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1130 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 12040 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -9.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, 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 ILE A 601
REMARK 465 ALA A 602
REMARK 465 GLN A 603
REMARK 465 GLN A 604
REMARK 465 GLN A 605
REMARK 465 HIS A 606
REMARK 465 ALA A 607
REMARK 465 GLU B 600
REMARK 465 ILE B 601
REMARK 465 ALA B 602
REMARK 465 GLN B 603
REMARK 465 GLN B 604
REMARK 465 GLN B 605
REMARK 465 HIS B 606
REMARK 465 ALA B 607
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 HIS A 439 CG HIS A 439 CD2 0.064
REMARK 500 GLU A 444 CD GLU A 444 OE1 -0.069
REMARK 500 HIS A 541 CG HIS A 541 CD2 0.054
REMARK 500 HIS B 422 CG HIS B 422 CD2 0.072
REMARK 500 HIS B 439 CG HIS B 439 CD2 0.054
REMARK 500 GLU B 444 CD GLU B 444 OE1 -0.071
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 LEU A 391 CB - CG - CD1 ANGL. DEV. = 12.2 DEGREES
REMARK 500 ARG A 467 NE - CZ - NH1 ANGL. DEV. = -4.0 DEGREES
REMARK 500 ASP A 580 CB - CG - OD1 ANGL. DEV. = 6.2 DEGREES
REMARK 500 LEU B 411 CA - CB - CG ANGL. DEV. = -14.7 DEGREES
REMARK 500 ARG B 447 NE - CZ - NH2 ANGL. DEV. = -3.0 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 MET A 599 -3.96 -58.48
REMARK 500 MET B 404 128.20 -37.90
REMARK 500 SER B 427 -169.01 -128.86
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 702
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 703
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 704
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 101
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1DKX RELATED DB: PDB
REMARK 900 RELATED ID: 1DKY RELATED DB: PDB
REMARK 900 RELATED ID: 1DKZ RELATED DB: PDB
REMARK 900 RELATED ID: 3DPO RELATED DB: PDB
REMARK 900 RELATED ID: 3DPP RELATED DB: PDB
REMARK 900 RELATED ID: 3DPQ RELATED DB: PDB
REMARK 900 RELATED ID: 3QNJ RELATED DB: PDB
REMARK 900 RELATED ID: 4E81 RELATED DB: PDB
REMARK 900 RELATED ID: 4EZN RELATED DB: PDB
REMARK 900 RELATED ID: 4EZO RELATED DB: PDB
REMARK 900 RELATED ID: 4EZP RELATED DB: PDB
REMARK 900 RELATED ID: 4EZQ RELATED DB: PDB
REMARK 900 RELATED ID: 4EZR RELATED DB: PDB
REMARK 900 RELATED ID: 4EZS RELATED DB: PDB
REMARK 900 RELATED ID: 4EZT RELATED DB: PDB
REMARK 900 RELATED ID: 4EZU RELATED DB: PDB
REMARK 900 RELATED ID: 4EZV RELATED DB: PDB
REMARK 900 RELATED ID: 4EZW RELATED DB: PDB
REMARK 900 RELATED ID: 4EZY RELATED DB: PDB
REMARK 900 RELATED ID: 4EZZ RELATED DB: PDB
REMARK 900 RELATED ID: 4F00 RELATED DB: PDB
REMARK 900 RELATED ID: 4F01 RELATED DB: PDB
DBREF 4EZX A 389 607 UNP P0A6Y8 DNAK_ECOLI 389 607
DBREF 4EZX B 389 607 UNP P0A6Y8 DNAK_ECOLI 389 607
DBREF 4EZX C 1 7 PDB 4EZX 4EZX 1 7
DBREF 4EZX D 1 7 PDB 4EZX 4EZX 1 7
SEQRES 1 A 219 VAL LEU LEU LEU ASP VAL THR PRO LEU SER LEU GLY ILE
SEQRES 2 A 219 GLU THR MET GLY GLY VAL MET THR THR LEU ILE ALA LYS
SEQRES 3 A 219 ASN THR THR ILE PRO THR LYS HIS SER GLN VAL PHE SER
SEQRES 4 A 219 THR ALA GLU ASP ASN GLN SER ALA VAL THR ILE HIS VAL
SEQRES 5 A 219 LEU GLN GLY GLU ARG LYS ARG ALA ALA ASP ASN LYS SER
SEQRES 6 A 219 LEU GLY GLN PHE ASN LEU ASP GLY ILE ASN PRO ALA PRO
SEQRES 7 A 219 ARG GLY MET PRO GLN ILE GLU VAL THR PHE ASP ILE ASP
SEQRES 8 A 219 ALA ASP GLY ILE LEU HIS VAL SER ALA LYS ASP LYS ASN
SEQRES 9 A 219 SER GLY LYS GLU GLN LYS ILE THR ILE LYS ALA SER SER
SEQRES 10 A 219 GLY LEU ASN GLU ASP GLU ILE GLN LYS MET VAL ARG ASP
SEQRES 11 A 219 ALA GLU ALA ASN ALA GLU ALA ASP ARG LYS PHE GLU GLU
SEQRES 12 A 219 LEU VAL GLN THR ARG ASN GLN GLY ASP HIS LEU LEU HIS
SEQRES 13 A 219 SER THR ARG LYS GLN VAL GLU GLU ALA GLY ASP LYS LEU
SEQRES 14 A 219 PRO ALA ASP ASP LYS THR ALA ILE GLU SER ALA LEU THR
SEQRES 15 A 219 ALA LEU GLU THR ALA LEU LYS GLY GLU ASP LYS ALA ALA
SEQRES 16 A 219 ILE GLU ALA LYS MET GLN GLU LEU ALA GLN VAL SER GLN
SEQRES 17 A 219 LYS LEU MET GLU ILE ALA GLN GLN GLN HIS ALA
SEQRES 1 B 219 VAL LEU LEU LEU ASP VAL THR PRO LEU SER LEU GLY ILE
SEQRES 2 B 219 GLU THR MET GLY GLY VAL MET THR THR LEU ILE ALA LYS
SEQRES 3 B 219 ASN THR THR ILE PRO THR LYS HIS SER GLN VAL PHE SER
SEQRES 4 B 219 THR ALA GLU ASP ASN GLN SER ALA VAL THR ILE HIS VAL
SEQRES 5 B 219 LEU GLN GLY GLU ARG LYS ARG ALA ALA ASP ASN LYS SER
SEQRES 6 B 219 LEU GLY GLN PHE ASN LEU ASP GLY ILE ASN PRO ALA PRO
SEQRES 7 B 219 ARG GLY MET PRO GLN ILE GLU VAL THR PHE ASP ILE ASP
SEQRES 8 B 219 ALA ASP GLY ILE LEU HIS VAL SER ALA LYS ASP LYS ASN
SEQRES 9 B 219 SER GLY LYS GLU GLN LYS ILE THR ILE LYS ALA SER SER
SEQRES 10 B 219 GLY LEU ASN GLU ASP GLU ILE GLN LYS MET VAL ARG ASP
SEQRES 11 B 219 ALA GLU ALA ASN ALA GLU ALA ASP ARG LYS PHE GLU GLU
SEQRES 12 B 219 LEU VAL GLN THR ARG ASN GLN GLY ASP HIS LEU LEU HIS
SEQRES 13 B 219 SER THR ARG LYS GLN VAL GLU GLU ALA GLY ASP LYS LEU
SEQRES 14 B 219 PRO ALA ASP ASP LYS THR ALA ILE GLU SER ALA LEU THR
SEQRES 15 B 219 ALA LEU GLU THR ALA LEU LYS GLY GLU ASP LYS ALA ALA
SEQRES 16 B 219 ILE GLU ALA LYS MET GLN GLU LEU ALA GLN VAL SER GLN
SEQRES 17 B 219 LYS LEU MET GLU ILE ALA GLN GLN GLN HIS ALA
SEQRES 1 C 7 ASN ARG LEU MET LEU THR GLY
SEQRES 1 D 7 ASN ARG LEU MET LEU THR GLY
HET SO4 A 701 5
HET SO4 A 702 5
HET SO4 A 703 5
HET SO4 A 704 5
HET SO4 C 101 5
HETNAM SO4 SULFATE ION
FORMUL 5 SO4 5(O4 S 2-)
FORMUL 10 HOH *337(H2 O)
HELIX 1 1 ARG A 447 ASN A 451 5 5
HELIX 2 2 ASN A 508 ASN A 522 1 15
HELIX 3 3 ASN A 522 GLY A 554 1 33
HELIX 4 4 ASP A 555 LEU A 557 5 3
HELIX 5 5 PRO A 558 LYS A 577 1 20
HELIX 6 6 ASP A 580 VAL A 594 1 15
HELIX 7 7 ARG B 447 ASN B 451 5 5
HELIX 8 8 ASN B 508 ASN B 522 1 15
HELIX 9 9 ASN B 522 GLY B 554 1 33
HELIX 10 10 ASP B 555 LEU B 557 5 3
HELIX 11 11 PRO B 558 LYS B 577 1 20
HELIX 12 12 ASP B 580 SER B 595 1 16
SHEET 1 A 4 VAL A 407 ILE A 412 0
SHEET 2 A 4 LEU A 399 THR A 403 -1 N LEU A 399 O LEU A 411
SHEET 3 A 4 VAL A 436 GLN A 442 -1 O LEU A 441 N GLY A 400
SHEET 4 A 4 LYS A 452 LEU A 459 -1 O PHE A 457 N ILE A 438
SHEET 1 B 5 GLU A 496 ILE A 501 0
SHEET 2 B 5 LEU A 484 ASP A 490 -1 N LEU A 484 O ILE A 501
SHEET 3 B 5 ILE A 472 ILE A 478 -1 N ASP A 477 O HIS A 485
SHEET 4 B 5 THR A 420 THR A 428 -1 N PHE A 426 O ILE A 472
SHEET 5 B 5 MET C 4 LEU C 5 1 O LEU C 5 N SER A 427
SHEET 1 C 4 VAL B 407 ILE B 412 0
SHEET 2 C 4 LEU B 399 THR B 403 -1 N LEU B 399 O LEU B 411
SHEET 3 C 4 VAL B 436 GLN B 442 -1 O LEU B 441 N GLY B 400
SHEET 4 C 4 LYS B 452 LEU B 459 -1 O PHE B 457 N ILE B 438
SHEET 1 D 5 GLU B 496 ILE B 501 0
SHEET 2 D 5 LEU B 484 ASP B 490 -1 N LEU B 484 O ILE B 501
SHEET 3 D 5 ILE B 472 ILE B 478 -1 N ASP B 477 O HIS B 485
SHEET 4 D 5 THR B 420 THR B 428 -1 N GLN B 424 O VAL B 474
SHEET 5 D 5 MET D 4 LEU D 5 1 O LEU D 5 N SER B 427
CISPEP 1 ILE A 418 PRO A 419 0 1.01
CISPEP 2 ILE B 418 PRO B 419 0 -2.76
SITE 1 AC1 9 ASN A 451 LYS A 452 SER A 453 HOH A 935
SITE 2 AC1 9 ASN B 451 LYS B 452 SER B 453 HOH B 786
SITE 3 AC1 9 HOH B 839
SITE 1 AC2 4 SER A 453 GLY A 455 GLN A 456 LYS B 452
SITE 1 AC3 7 ARG A 467 ASP A 481 SER A 545 LYS A 548
SITE 2 AC3 7 HOH A 880 HOH A 939 HOH A 946
SITE 1 AC4 6 ARG A 447 ARG A 536 GLU A 579 ARG B 447
SITE 2 AC4 6 HOH B 773 HOH B 824
SITE 1 AC5 6 GLN A 471 LYS A 502 HOH A 898 ASN C 1
SITE 2 AC5 6 ARG C 2 HOH C 207
CRYST1 77.611 149.345 45.355 90.00 90.00 90.00 P 21 21 2 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 0.012885 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006696 0.000000 0.00000
SCALE3 0.000000 0.000000 0.022048 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
