HEADER CHAPERONE 04-JUL-13 4LJ8
TITLE CLPB NBD2 R621Q FROM T. THERMOPHILUS IN COMPLEX WITH ADP
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CHAPERONE PROTEIN CLPB;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: NUCLEOTIDE BINDING DOMAIN 2, UNP RESIDUES 520-854;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;
SOURCE 3 ORGANISM_TAXID: 300852;
SOURCE 4 STRAIN: HB8;
SOURCE 5 GENE: CLPB;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3) RIL;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET28A
KEYWDS AAA+ PROTEIN, NUCLEOTIDE BINDING DOMAIN, MOLECULAR CHAPERONE,
KEYWDS 2 DISAGGREGASE, CHAPERONE
EXPDTA X-RAY DIFFRACTION
AUTHOR C.ZEYMER,T.R.M.BARENDS,N.D.WERBECK,I.SCHLICHTING,J.REINSTEIN
REVDAT 4 08-NOV-23 4LJ8 1 REMARK SEQADV
REVDAT 3 15-NOV-17 4LJ8 1 REMARK
REVDAT 2 09-APR-14 4LJ8 1 JRNL
REVDAT 1 12-FEB-14 4LJ8 0
JRNL AUTH C.ZEYMER,T.R.M.BARENDS,N.D.WERBECK,I.SCHLICHTING,J.REINSTEIN
JRNL TITL ELEMENTS IN NUCLEOTIDE SENSING AND HYDROLYSIS OF THE AAA+
JRNL TITL 2 DISAGGREGATION MACHINE CLPB: A STRUCTURE-BASED MECHANISTIC
JRNL TITL 3 DISSECTION OF A MOLECULAR MOTOR
JRNL REF ACTA CRYSTALLOGR.,SECT.D V. 70 582 2014
JRNL REFN ISSN 0907-4449
JRNL PMID 24531492
JRNL DOI 10.1107/S1399004713030629
REMARK 2
REMARK 2 RESOLUTION. 2.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0102
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) : 2.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 43.78
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 21811
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) : 0.190
REMARK 3 R VALUE (WORKING SET) : 0.188
REMARK 3 FREE R VALUE : 0.233
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.700
REMARK 3 FREE R VALUE TEST SET COUNT : 1030
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) : 2.10
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.16
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1527
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.81
REMARK 3 BIN R VALUE (WORKING SET) : 0.2380
REMARK 3 BIN FREE R VALUE SET COUNT : 70
REMARK 3 BIN FREE R VALUE : 0.3280
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2555
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 27
REMARK 3 SOLVENT ATOMS : 47
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 40.40
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 47.53
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -6.38000
REMARK 3 B22 (A**2) : -6.38000
REMARK 3 B33 (A**2) : 12.77000
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): 0.043
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.038
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.136
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 8.979
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.959
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.926
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2626 ; 0.008 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 2608 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3556 ; 1.276 ; 1.999
REMARK 3 BOND ANGLES OTHERS (DEGREES): 5979 ; 0.754 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 320 ; 5.693 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 122 ;34.188 ;23.115
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 470 ;14.750 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 29 ;16.284 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 408 ; 0.066 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2906 ; 0.005 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 582 ; 0.001 ; 0.020
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 TWIN DETAILS
REMARK 3 NUMBER OF TWIN DOMAINS : 2
REMARK 3 TWIN DOMAIN : 1
REMARK 3 TWIN OPERATOR : H, K, L
REMARK 3 TWIN FRACTION : 0.222
REMARK 3 TWIN DOMAIN : 2
REMARK 3 TWIN OPERATOR : K, H, -L
REMARK 3 TWIN FRACTION : 0.778
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 3
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 550 A 709
REMARK 3 RESIDUE RANGE : A 741 A 755
REMARK 3 ORIGIN FOR THE GROUP (A): 8.7860 25.9410 -9.0610
REMARK 3 T TENSOR
REMARK 3 T11: 0.1351 T22: 0.1478
REMARK 3 T33: 0.0477 T12: 0.0442
REMARK 3 T13: -0.0147 T23: 0.0186
REMARK 3 L TENSOR
REMARK 3 L11: 1.1489 L22: 1.0901
REMARK 3 L33: 1.0016 L12: -0.2773
REMARK 3 L13: 0.1277 L23: 0.3187
REMARK 3 S TENSOR
REMARK 3 S11: 0.0381 S12: 0.1731 S13: 0.0665
REMARK 3 S21: 0.0044 S22: -0.1694 S23: -0.0993
REMARK 3 S31: 0.0719 S32: 0.0292 S33: 0.1313
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 710 A 740
REMARK 3 ORIGIN FOR THE GROUP (A): -4.6660 17.9390 11.7410
REMARK 3 T TENSOR
REMARK 3 T11: 0.2768 T22: 0.1402
REMARK 3 T33: 0.0416 T12: -0.0390
REMARK 3 T13: 0.0259 T23: 0.0340
REMARK 3 L TENSOR
REMARK 3 L11: 9.5792 L22: 3.0216
REMARK 3 L33: 4.8680 L12: -3.3377
REMARK 3 L13: -3.7538 L23: 2.7611
REMARK 3 S TENSOR
REMARK 3 S11: -0.3017 S12: -0.2819 S13: -0.5196
REMARK 3 S21: 0.4288 S22: 0.0097 S23: 0.1683
REMARK 3 S31: 0.5094 S32: -0.2115 S33: 0.2920
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 756 A 849
REMARK 3 ORIGIN FOR THE GROUP (A): -21.9280 40.2480 -10.8730
REMARK 3 T TENSOR
REMARK 3 T11: 0.1094 T22: 0.1245
REMARK 3 T33: 0.3199 T12: 0.0645
REMARK 3 T13: -0.0648 T23: -0.1053
REMARK 3 L TENSOR
REMARK 3 L11: 3.0126 L22: 1.1737
REMARK 3 L33: 1.4908 L12: 0.1862
REMARK 3 L13: 1.7430 L23: -0.2207
REMARK 3 S TENSOR
REMARK 3 S11: -0.2738 S12: -0.1758 S13: 0.5341
REMARK 3 S21: 0.0639 S22: -0.0145 S23: 0.4219
REMARK 3 S31: -0.1828 S32: -0.0322 S33: 0.2882
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: U VALUES: WITH TLS ADDED HYDROGENS HAVE
REMARK 3 BEEN ADDED IN THE RIDING POSITIONS
REMARK 4
REMARK 4 4LJ8 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 16-JUL-13.
REMARK 100 THE DEPOSITION ID IS D_1000080697.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 13-JUN-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SLS
REMARK 200 BEAMLINE : X10SA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9170
REMARK 200 MONOCHROMATOR : SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : PSI PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 21813
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100
REMARK 200 RESOLUTION RANGE LOW (A) : 44.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 6.400
REMARK 200 R MERGE (I) : 0.05300
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 19.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.20
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 4.20
REMARK 200 R MERGE FOR SHELL (I) : 0.39500
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.200
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: 4LJ5
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.49
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.48
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M TRIS/HCL, 15% ISOPROPANOL, 50MM
REMARK 280 MAGNESIUM CHLORIDE, 2MM ADP, PH 7.5, VAPOR DIFFUSION, HANGING
REMARK 280 DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+1/6
REMARK 290 6555 X-Y,X,Z+5/6
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 79.66667
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 39.83333
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 59.75000
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 19.91667
REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 99.58333
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 300 REMARK: THE FULL PROTEIN FORMS A RANGE OF OLIGOMERS, AND THIS
REMARK 300 DOMAIN FORMS DIMERS IN SOLUTION UNDER CERTAIN CIRCUMSTANCES.
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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
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 GLY A 516
REMARK 465 SER A 517
REMARK 465 ARG A 546
REMARK 465 GLU A 547
REMARK 465 LYS A 548
REMARK 465 TYR A 643
REMARK 465 VAL A 644
REMARK 465 GLY A 645
REMARK 465 TYR A 646
REMARK 465 GLU A 647
REMARK 465 GLU A 648
REMARK 465 ALA A 850
REMARK 465 ARG A 851
REMARK 465 VAL A 852
REMARK 465 GLU A 853
REMARK 465 ALA A 854
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 GLU A 545 CG CD OE1 OE2
REMARK 470 ARG A 551 CB CG CD NE CZ NH1 NH2
REMARK 470 GLU A 629 CG CD OE1 OE2
REMARK 470 PRO A 849 O
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 ASP A 614 -12.56 72.80
REMARK 500 GLU A 629 58.10 -118.51
REMARK 500 LYS A 630 -76.63 76.55
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 ADP A 901
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4LJ4 RELATED DB: PDB
REMARK 900 RELATED ID: 4LJ5 RELATED DB: PDB
REMARK 900 RELATED ID: 4LJ6 RELATED DB: PDB
REMARK 900 RELATED ID: 4LJ7 RELATED DB: PDB
REMARK 900 RELATED ID: 4LJ9 RELATED DB: PDB
REMARK 900 RELATED ID: 4LJA RELATED DB: PDB
DBREF 4LJ8 A 520 854 UNP Q9RA63 CLPB_THET8 520 854
SEQADV 4LJ8 GLY A 516 UNP Q9RA63 EXPRESSION TAG
SEQADV 4LJ8 SER A 517 UNP Q9RA63 EXPRESSION TAG
SEQADV 4LJ8 HIS A 518 UNP Q9RA63 EXPRESSION TAG
SEQADV 4LJ8 MET A 519 UNP Q9RA63 EXPRESSION TAG
SEQADV 4LJ8 GLN A 621 UNP Q9RA63 ARG 621 ENGINEERED MUTATION
SEQRES 1 A 339 GLY SER HIS MET GLU VAL THR GLU GLU ASP ILE ALA GLU
SEQRES 2 A 339 ILE VAL SER ARG TRP THR GLY ILE PRO VAL SER LYS LEU
SEQRES 3 A 339 LEU GLU GLY GLU ARG GLU LYS LEU LEU ARG LEU GLU GLU
SEQRES 4 A 339 GLU LEU HIS LYS ARG VAL VAL GLY GLN ASP GLU ALA ILE
SEQRES 5 A 339 ARG ALA VAL ALA ASP ALA ILE ARG ARG ALA ARG ALA GLY
SEQRES 6 A 339 LEU LYS ASP PRO ASN ARG PRO ILE GLY SER PHE LEU PHE
SEQRES 7 A 339 LEU GLY PRO THR GLY VAL GLY LYS THR GLU LEU ALA LYS
SEQRES 8 A 339 THR LEU ALA ALA THR LEU PHE ASP THR GLU GLU ALA MET
SEQRES 9 A 339 ILE GLN ILE ASP MET THR GLU TYR MET GLU LYS HIS ALA
SEQRES 10 A 339 VAL SER ARG LEU ILE GLY ALA PRO PRO GLY TYR VAL GLY
SEQRES 11 A 339 TYR GLU GLU GLY GLY GLN LEU THR GLU ALA VAL ARG ARG
SEQRES 12 A 339 ARG PRO TYR SER VAL ILE LEU PHE ASP GLU ILE GLU LYS
SEQRES 13 A 339 ALA HIS PRO ASP VAL PHE ASN ILE LEU LEU GLN ILE LEU
SEQRES 14 A 339 ASP ASP GLY ARG LEU THR ASP SER HIS GLY ARG THR VAL
SEQRES 15 A 339 ASP PHE ARG ASN THR VAL ILE ILE LEU THR SER ASN LEU
SEQRES 16 A 339 GLY SER PRO LEU ILE LEU GLU GLY LEU GLN LYS GLY TRP
SEQRES 17 A 339 PRO TYR GLU ARG ILE ARG ASP GLU VAL PHE LYS VAL LEU
SEQRES 18 A 339 GLN GLN HIS PHE ARG PRO GLU PHE LEU ASN ARG LEU ASP
SEQRES 19 A 339 GLU ILE VAL VAL PHE ARG PRO LEU THR LYS GLU GLN ILE
SEQRES 20 A 339 ARG GLN ILE VAL GLU ILE GLN LEU SER TYR LEU ARG ALA
SEQRES 21 A 339 ARG LEU ALA GLU LYS ARG ILE SER LEU GLU LEU THR GLU
SEQRES 22 A 339 ALA ALA LYS ASP PHE LEU ALA GLU ARG GLY TYR ASP PRO
SEQRES 23 A 339 VAL PHE GLY ALA ARG PRO LEU ARG ARG VAL ILE GLN ARG
SEQRES 24 A 339 GLU LEU GLU THR PRO LEU ALA GLN LYS ILE LEU ALA GLY
SEQRES 25 A 339 GLU VAL LYS GLU GLY ASP ARG VAL GLN VAL ASP VAL GLY
SEQRES 26 A 339 PRO ALA GLY LEU VAL PHE ALA VAL PRO ALA ARG VAL GLU
SEQRES 27 A 339 ALA
HET ADP A 901 27
HETNAM ADP ADENOSINE-5'-DIPHOSPHATE
FORMUL 2 ADP C10 H15 N5 O10 P2
FORMUL 3 HOH *47(H2 O)
HELIX 1 1 THR A 522 GLY A 535 1 14
HELIX 2 2 PRO A 537 LEU A 542 1 6
HELIX 3 3 ARG A 551 VAL A 560 1 10
HELIX 4 4 GLN A 563 ALA A 579 1 17
HELIX 5 5 GLY A 600 ASP A 614 1 15
HELIX 6 6 THR A 615 GLU A 617 5 3
HELIX 7 7 THR A 625 TYR A 627 5 3
HELIX 8 8 HIS A 631 GLY A 638 1 8
HELIX 9 9 GLY A 650 ARG A 659 1 10
HELIX 10 10 ILE A 669 ALA A 672 5 4
HELIX 11 11 HIS A 673 GLY A 687 1 15
HELIX 12 12 GLY A 711 GLY A 722 1 12
HELIX 13 13 PRO A 724 PHE A 740 1 17
HELIX 14 14 ARG A 741 ASN A 746 1 6
HELIX 15 15 THR A 758 LEU A 770 1 13
HELIX 16 16 LEU A 770 GLU A 779 1 10
HELIX 17 17 THR A 787 TYR A 799 1 13
HELIX 18 18 PRO A 807 LEU A 816 1 10
HELIX 19 19 LEU A 816 ALA A 826 1 11
SHEET 1 A 5 MET A 619 ASP A 623 0
SHEET 2 A 5 SER A 662 ASP A 667 1 O LEU A 665 N ILE A 622
SHEET 3 A 5 THR A 702 THR A 707 1 O VAL A 703 N ILE A 664
SHEET 4 A 5 GLY A 589 LEU A 594 1 N PHE A 593 O LEU A 706
SHEET 5 A 5 GLU A 750 VAL A 753 1 O VAL A 752 N LEU A 594
SHEET 1 B 2 ARG A 688 THR A 690 0
SHEET 2 B 2 THR A 696 ASP A 698 -1 O VAL A 697 N LEU A 689
SHEET 1 C 3 SER A 783 LEU A 786 0
SHEET 2 C 3 ARG A 834 GLY A 840 1 O VAL A 835 N GLU A 785
SHEET 3 C 3 GLY A 843 ALA A 847 -1 O GLY A 843 N GLY A 840
SITE 1 AC1 16 ARG A 559 VAL A 560 VAL A 561 THR A 597
SITE 2 AC1 16 GLY A 598 VAL A 599 GLY A 600 LYS A 601
SITE 3 AC1 16 THR A 602 ILE A 765 GLN A 769 ALA A 805
SITE 4 AC1 16 ARG A 806 HOH A1001 HOH A1024 HOH A1028
CRYST1 74.300 74.300 119.500 90.00 90.00 120.00 P 65 6
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 0.013459 0.007771 0.000000 0.00000
SCALE2 0.000000 0.015541 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008368 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
