HEADER CHAPERONE 04-JUL-13 4LJA
TITLE CLPB NBD2 R621Q FROM T. THERMOPHILUS IN COMPLEX WITH AMPPCP AND
TITLE 2 GUANIDINIUM CHLORIDE
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 4LJA 1 REMARK SEQADV LINK
REVDAT 3 15-NOV-17 4LJA 1 REMARK
REVDAT 2 09-APR-14 4LJA 1 JRNL
REVDAT 1 12-FEB-14 4LJA 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. 2.00 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) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 43.92
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 24325
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) : 0.219
REMARK 3 R VALUE (WORKING SET) : 0.217
REMARK 3 FREE R VALUE : 0.263
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 1256
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) : 2.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.05
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1797
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 BIN R VALUE (WORKING SET) : 0.2750
REMARK 3 BIN FREE R VALUE SET COUNT : 91
REMARK 3 BIN FREE R VALUE : 0.3420
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2550
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 36
REMARK 3 SOLVENT ATOMS : 77
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 41.10
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 46.84
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.30000
REMARK 3 B22 (A**2) : 0.30000
REMARK 3 B33 (A**2) : -0.45000
REMARK 3 B12 (A**2) : 0.15000
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): 0.195
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.177
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.128
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 8.218
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.954
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.917
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2634 ; 0.010 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3569 ; 1.256 ; 2.000
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 320 ; 5.090 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 124 ;33.567 ;23.065
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 472 ;15.486 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 30 ;15.694 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 408 ; 0.079 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1968 ; 0.005 ; 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): 1602 ; 0.489 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2588 ; 0.924 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1032 ; 1.613 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 980 ; 2.766 ; 4.500
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 : 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): 8.9822 26.5167 -9.1661
REMARK 3 T TENSOR
REMARK 3 T11: 0.0768 T22: 0.0995
REMARK 3 T33: 0.0677 T12: 0.0666
REMARK 3 T13: 0.0221 T23: 0.0288
REMARK 3 L TENSOR
REMARK 3 L11: 4.3668 L22: 3.0169
REMARK 3 L33: 2.6364 L12: -0.3580
REMARK 3 L13: -0.0696 L23: -0.0847
REMARK 3 S TENSOR
REMARK 3 S11: 0.1149 S12: 0.5046 S13: 0.0054
REMARK 3 S21: -0.2927 S22: -0.2983 S23: -0.3784
REMARK 3 S31: 0.0949 S32: 0.1062 S33: 0.1833
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): -4.2571 17.8513 11.7143
REMARK 3 T TENSOR
REMARK 3 T11: 0.2955 T22: 0.1975
REMARK 3 T33: 0.0640 T12: -0.0645
REMARK 3 T13: 0.0176 T23: 0.0315
REMARK 3 L TENSOR
REMARK 3 L11: 14.0622 L22: 5.3066
REMARK 3 L33: 7.0046 L12: -3.9353
REMARK 3 L13: -3.6150 L23: 0.7387
REMARK 3 S TENSOR
REMARK 3 S11: -0.4709 S12: -0.8545 S13: -0.7934
REMARK 3 S21: 0.8213 S22: 0.1758 S23: 0.3551
REMARK 3 S31: 0.4917 S32: -0.4396 S33: 0.2951
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): -21.8456 40.5552 -10.5264
REMARK 3 T TENSOR
REMARK 3 T11: 0.1109 T22: 0.1242
REMARK 3 T33: 0.2874 T12: 0.0532
REMARK 3 T13: -0.0415 T23: -0.0936
REMARK 3 L TENSOR
REMARK 3 L11: 5.2864 L22: 2.8926
REMARK 3 L33: 4.1198 L12: -1.0219
REMARK 3 L13: 3.7308 L23: -0.8983
REMARK 3 S TENSOR
REMARK 3 S11: -0.3449 S12: -0.2097 S13: 0.6165
REMARK 3 S21: 0.0198 S22: 0.1131 S23: 0.4526
REMARK 3 S31: -0.4931 S32: -0.2135 S33: 0.2318
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 4LJA COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 17-JUL-13.
REMARK 100 THE DEPOSITION ID IS D_1000080699.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-MAY-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) : 0.9120
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 : 25581
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
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 (%) : 100.0
REMARK 200 DATA REDUNDANCY : 10.30
REMARK 200 R MERGE (I) : 0.04300
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 29.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.10
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 10.60
REMARK 200 R MERGE FOR SHELL (I) : 0.82100
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.000
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 (%): 51.15
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.52
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M TRIS/HCL, 15% ISOPROPANOL, 10MM
REMARK 280 MAGNESIUM CHLORIDE, 2MM AMPPCP, 100MM GUANIDINIUM CHLORIDE, PH
REMARK 280 7.5, VAPOR DIFFUSION, HANGING 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 LEU A 549
REMARK 465 GLY A 642
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 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 ASN A 585 30.77 -94.94
REMARK 500 ASP A 614 -32.39 75.58
REMARK 500 LEU A 816 -56.89 -120.68
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 902 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR A 602 OG1
REMARK 620 2 ACP A 901 O1G 176.2
REMARK 620 3 ACP A 901 O1B 81.8 98.5
REMARK 620 4 HOH A1001 O 92.7 91.1 91.8
REMARK 620 5 HOH A1002 O 90.4 85.8 86.4 176.2
REMARK 620 6 HOH A1003 O 87.7 92.0 169.5 89.0 93.4
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACP A 901
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 902
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GAI A 903
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: 4LJ8 RELATED DB: PDB
REMARK 900 RELATED ID: 4LJ9 RELATED DB: PDB
DBREF 4LJA A 520 854 UNP Q9RA63 CLPB_THET8 520 854
SEQADV 4LJA GLY A 516 UNP Q9RA63 EXPRESSION TAG
SEQADV 4LJA SER A 517 UNP Q9RA63 EXPRESSION TAG
SEQADV 4LJA HIS A 518 UNP Q9RA63 EXPRESSION TAG
SEQADV 4LJA MET A 519 UNP Q9RA63 EXPRESSION TAG
SEQADV 4LJA 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 ACP A 901 31
HET MG A 902 1
HET GAI A 903 4
HETNAM ACP PHOSPHOMETHYLPHOSPHONIC ACID ADENYLATE ESTER
HETNAM MG MAGNESIUM ION
HETNAM GAI GUANIDINE
HETSYN ACP ADENOSINE-5'-[BETA, GAMMA-METHYLENE]TRIPHOSPHATE
FORMUL 2 ACP C11 H18 N5 O12 P3
FORMUL 3 MG MG 2+
FORMUL 4 GAI C H5 N3
FORMUL 5 HOH *77(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 LYS A 558 1 8
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 GLU A 629 HIS A 631 5 3
HELIX 9 9 ALA A 632 GLY A 638 1 7
HELIX 10 10 GLY A 650 ARG A 659 1 10
HELIX 11 11 GLU A 668 ALA A 672 5 5
HELIX 12 12 HIS A 673 GLY A 687 1 15
HELIX 13 13 GLY A 711 GLY A 722 1 12
HELIX 14 14 PRO A 724 PHE A 740 1 17
HELIX 15 15 ARG A 741 ASN A 746 1 6
HELIX 16 16 THR A 758 LEU A 770 1 13
HELIX 17 17 LEU A 770 GLU A 779 1 10
HELIX 18 18 THR A 787 GLY A 798 1 12
HELIX 19 19 PRO A 807 LEU A 816 1 10
HELIX 20 20 LEU A 816 ALA A 826 1 11
SHEET 1 A 5 MET A 619 ASP A 623 0
SHEET 2 A 5 VAL A 663 ASP A 667 1 O LEU A 665 N ILE A 620
SHEET 3 A 5 VAL A 703 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
LINK OG1 THR A 602 MG MG A 902 1555 1555 1.92
LINK O1G ACP A 901 MG MG A 902 1555 1555 1.97
LINK O1B ACP A 901 MG MG A 902 1555 1555 2.04
LINK MG MG A 902 O HOH A1001 1555 1555 2.17
LINK MG MG A 902 O HOH A1002 1555 1555 2.10
LINK MG MG A 902 O HOH A1003 1555 1555 2.19
SITE 1 AC1 20 ARG A 559 VAL A 560 VAL A 561 THR A 597
SITE 2 AC1 20 GLY A 598 VAL A 599 GLY A 600 LYS A 601
SITE 3 AC1 20 THR A 602 GLU A 603 ILE A 765 GLN A 769
SITE 4 AC1 20 MG A 902 GAI A 903 HOH A1001 HOH A1002
SITE 5 AC1 20 HOH A1003 HOH A1004 HOH A1006 HOH A1063
SITE 1 AC2 5 THR A 602 ACP A 901 HOH A1001 HOH A1002
SITE 2 AC2 5 HOH A1003
SITE 1 AC3 5 GLN A 621 ASP A 623 GLU A 668 GLU A 743
SITE 2 AC3 5 ACP A 901
CRYST1 74.800 74.800 119.500 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 0.013369 0.007719 0.000000 0.00000
SCALE2 0.000000 0.015437 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008368 0.00000
(ATOM LINES ARE NOT SHOWN.)
END