HEADER CHAPERONE 04-JUL-13 4LJ9
TITLE CLPB NBD2 R621Q FROM T. THERMOPHILUS IN COMPLEX WITH AMPPCP
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 4LJ9 1 REMARK SEQADV LINK
REVDAT 3 15-NOV-17 4LJ9 1 REMARK
REVDAT 2 09-APR-14 4LJ9 1 JRNL
REVDAT 1 12-FEB-14 4LJ9 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. 1.70 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) : 1.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 43.91
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 39319
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) : 0.210
REMARK 3 R VALUE (WORKING SET) : 0.208
REMARK 3 FREE R VALUE : 0.244
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2068
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) : 1.74
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2899
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 BIN R VALUE (WORKING SET) : 0.2850
REMARK 3 BIN FREE R VALUE SET COUNT : 153
REMARK 3 BIN FREE R VALUE : 0.2950
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2652
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 33
REMARK 3 SOLVENT ATOMS : 216
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 26.70
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 27.47
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.09000
REMARK 3 B22 (A**2) : 0.09000
REMARK 3 B33 (A**2) : -0.14000
REMARK 3 B12 (A**2) : 0.05000
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): 0.118
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.116
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.075
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.540
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.952
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.931
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2795 ; 0.009 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3804 ; 1.242 ; 1.999
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 351 ; 4.914 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 135 ;33.149 ;23.185
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 508 ;14.030 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 32 ;15.574 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 432 ; 0.085 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2114 ; 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): 1687 ; 0.536 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2746 ; 1.069 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1108 ; 1.914 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1050 ; 3.341 ; 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 518 A 710
REMARK 3 RESIDUE RANGE : A 741 A 755
REMARK 3 ORIGIN FOR THE GROUP (A): 9.2093 28.7328 -11.6525
REMARK 3 T TENSOR
REMARK 3 T11: 0.0441 T22: 0.0428
REMARK 3 T33: 0.0409 T12: 0.0365
REMARK 3 T13: -0.0012 T23: -0.0021
REMARK 3 L TENSOR
REMARK 3 L11: 0.6344 L22: 0.4982
REMARK 3 L33: 1.0272 L12: 0.1504
REMARK 3 L13: 0.0037 L23: -0.1245
REMARK 3 S TENSOR
REMARK 3 S11: 0.0363 S12: 0.0881 S13: -0.0607
REMARK 3 S21: -0.0953 S22: -0.0783 S23: -0.0983
REMARK 3 S31: 0.0334 S32: 0.0595 S33: 0.0420
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 756 A 849
REMARK 3 ORIGIN FOR THE GROUP (A): -22.2522 40.4934 -10.7435
REMARK 3 T TENSOR
REMARK 3 T11: 0.0538 T22: 0.0569
REMARK 3 T33: 0.1285 T12: 0.0288
REMARK 3 T13: -0.0457 T23: -0.0567
REMARK 3 L TENSOR
REMARK 3 L11: 2.5456 L22: 1.3526
REMARK 3 L33: 1.7147 L12: -0.2399
REMARK 3 L13: 1.4031 L23: -0.4665
REMARK 3 S TENSOR
REMARK 3 S11: -0.1895 S12: -0.1539 S13: 0.2959
REMARK 3 S21: 0.0179 S22: 0.0398 S23: 0.2310
REMARK 3 S31: -0.2308 S32: -0.0890 S33: 0.1497
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 711 A 740
REMARK 3 ORIGIN FOR THE GROUP (A): -5.4659 18.3944 12.0806
REMARK 3 T TENSOR
REMARK 3 T11: 0.2019 T22: 0.0776
REMARK 3 T33: 0.0478 T12: -0.0542
REMARK 3 T13: -0.0079 T23: 0.0561
REMARK 3 L TENSOR
REMARK 3 L11: 10.3154 L22: 2.4504
REMARK 3 L33: 5.4660 L12: -2.3197
REMARK 3 L13: -4.5157 L23: 1.7537
REMARK 3 S TENSOR
REMARK 3 S11: -0.1367 S12: -0.6795 S13: -0.6453
REMARK 3 S21: 0.6389 S22: -0.0460 S23: 0.0858
REMARK 3 S31: 0.2646 S32: 0.0756 S33: 0.1826
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 4LJ9 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_1000080698.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 14-FEB-11
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) : 1.0000
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 : 41388
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.700
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 : 4.800
REMARK 200 R MERGE (I) : 0.05300
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 14.7000
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) : 1.80
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 5.00
REMARK 200 R MERGE FOR SHELL (I) : 0.38700
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 (%): 51.01
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.51
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M TRIS/HCL, 15% ISOPROPANOL, 75MM
REMARK 280 MAGNESIUM CHLORIDE, 2MM AMPPCP, 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 79.78667
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 39.89333
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 59.84000
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 19.94667
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 99.73333
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 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 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 -5.08 75.97
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 174.3
REMARK 620 3 ACP A 901 O1B 82.3 95.9
REMARK 620 4 HOH A1158 O 88.5 93.5 170.6
REMARK 620 5 HOH A1159 O 84.3 90.2 87.1 93.6
REMARK 620 6 HOH A1160 O 93.2 92.2 89.0 89.8 175.7
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 903 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A1161 O
REMARK 620 2 HOH A1162 O 94.1
REMARK 620 3 HOH A1163 O 93.0 169.5
REMARK 620 4 HOH A1164 O 89.4 83.6 88.8
REMARK 620 5 HOH A1165 O 95.6 98.8 88.1 174.3
REMARK 620 6 HOH A1187 O 171.3 81.1 92.7 97.3 78.1
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 MG 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: 4LJA RELATED DB: PDB
DBREF 4LJ9 A 520 854 UNP Q9RA63 CLPB_THET8 520 854
SEQADV 4LJ9 GLY A 516 UNP Q9RA63 EXPRESSION TAG
SEQADV 4LJ9 SER A 517 UNP Q9RA63 EXPRESSION TAG
SEQADV 4LJ9 HIS A 518 UNP Q9RA63 EXPRESSION TAG
SEQADV 4LJ9 MET A 519 UNP Q9RA63 EXPRESSION TAG
SEQADV 4LJ9 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 MG A 903 1
HETNAM ACP PHOSPHOMETHYLPHOSPHONIC ACID ADENYLATE ESTER
HETNAM MG MAGNESIUM ION
HETSYN ACP ADENOSINE-5'-[BETA, GAMMA-METHYLENE]TRIPHOSPHATE
FORMUL 2 ACP C11 H18 N5 O12 P3
FORMUL 3 MG 2(MG 2+)
FORMUL 5 HOH *216(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 LEU A 542 LEU A 550 1 9
HELIX 4 4 ARG A 551 LYS A 558 1 8
HELIX 5 5 GLN A 563 ALA A 579 1 17
HELIX 6 6 GLY A 600 ASP A 614 1 15
HELIX 7 7 THR A 615 GLU A 617 5 3
HELIX 8 8 THR A 625 TYR A 627 5 3
HELIX 9 9 HIS A 631 GLY A 638 1 8
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 LYS A 780 1 11
HELIX 18 18 THR A 787 TYR A 799 1 13
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 ILE A 705 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 592
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 VAL A 839 1 O VAL A 837 N GLU A 785
SHEET 3 C 3 LEU A 844 ALA A 847 -1 O ALA A 847 N GLN A 836
LINK OG1 THR A 602 MG MG A 902 1555 1555 1.98
LINK O1G ACP A 901 MG MG A 902 1555 1555 2.03
LINK O1B ACP A 901 MG MG A 902 1555 1555 2.04
LINK MG MG A 902 O HOH A1158 1555 1555 2.09
LINK MG MG A 902 O HOH A1159 1555 1555 2.14
LINK MG MG A 902 O HOH A1160 1555 1555 2.13
LINK MG MG A 903 O HOH A1161 1555 1555 2.05
LINK MG MG A 903 O HOH A1162 1555 1555 2.20
LINK MG MG A 903 O HOH A1163 1555 1555 2.03
LINK MG MG A 903 O HOH A1164 1555 1555 2.30
LINK MG MG A 903 O HOH A1165 1555 1555 1.99
LINK MG MG A 903 O HOH A1187 1555 1555 2.20
SITE 1 AC1 26 ARG A 559 VAL A 560 VAL A 561 THR A 597
SITE 2 AC1 26 GLY A 598 VAL A 599 GLY A 600 LYS A 601
SITE 3 AC1 26 THR A 602 GLU A 603 ILE A 765 GLN A 769
SITE 4 AC1 26 ALA A 805 MG A 902 HOH A1004 HOH A1007
SITE 5 AC1 26 HOH A1045 HOH A1048 HOH A1062 HOH A1154
SITE 6 AC1 26 HOH A1158 HOH A1159 HOH A1160 HOH A1161
SITE 7 AC1 26 HOH A1162 HOH A1177
SITE 1 AC2 5 THR A 602 ACP A 901 HOH A1158 HOH A1159
SITE 2 AC2 5 HOH A1160
SITE 1 AC3 6 HOH A1161 HOH A1162 HOH A1163 HOH A1164
SITE 2 AC3 6 HOH A1165 HOH A1187
CRYST1 74.640 74.640 119.680 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 0.013398 0.007735 0.000000 0.00000
SCALE2 0.000000 0.015470 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008356 0.00000
(ATOM LINES ARE NOT SHOWN.)
END