HEADER CHAPERONE 25-MAY-12 4FCV
TITLE CRYSTAL STRUCTURE OF THE C-TERMINAL DOMAIN OF CLPB
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CHAPERONE PROTEIN CLPB;
COMPND 3 CHAIN: A, B, C;
COMPND 4 FRAGMENT: UNP RESIDUES 544-852;
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 / ATCC 27634 / DSM 579;
SOURCE 5 GENE: CLPB, TTHA1487;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)RIL CODONPLUS;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET24
KEYWDS AAA DOMAIN, CHAPERONE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.B.BITER,S.LEE,N.SUNG,F.T.F.TSAI
REVDAT 2 22-AUG-12 4FCV 1 JRNL
REVDAT 1 18-JUL-12 4FCV 0
JRNL AUTH A.B.BITER,S.LEE,N.SUNG,F.T.TSAI
JRNL TITL STRUCTURAL BASIS FOR INTERSUBUNIT SIGNALING IN A PROTEIN
JRNL TITL 2 DISAGGREGATING MACHINE.
JRNL REF PROC.NATL.ACAD.SCI.USA V. 109 12515 2012
JRNL REFN ISSN 0027-8424
JRNL PMID 22802670
JRNL DOI 10.1073/PNAS.1207040109
REMARK 2
REMARK 2 RESOLUTION. 3.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0109
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 41.85
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.0
REMARK 3 NUMBER OF REFLECTIONS : 12853
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) : 0.234
REMARK 3 R VALUE (WORKING SET) : 0.233
REMARK 3 FREE R VALUE : 0.261
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 647
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) : 3.40
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.49
REMARK 3 REFLECTION IN BIN (WORKING SET) : 876
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.19
REMARK 3 BIN R VALUE (WORKING SET) : 0.2700
REMARK 3 BIN FREE R VALUE SET COUNT : 46
REMARK 3 BIN FREE R VALUE : 0.3060
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 7446
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 81
REMARK 3 SOLVENT ATOMS : 0
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 107.90
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -4.84000
REMARK 3 B22 (A**2) : 4.19000
REMARK 3 B33 (A**2) : -1.60000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -2.28000
REMARK 3 B23 (A**2) : 0.00000
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): 0.711
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.584
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 77.890
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.912
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.890
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 7659 ; 0.009 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 10353 ; 1.191 ; 2.001
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 930 ; 5.440 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 366 ;36.119 ;22.623
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1392 ;20.163 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 96 ;17.979 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1161 ; 0.076 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5754 ; 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): 4641 ; 0.559 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 7491 ; 1.225 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 3018 ; 2.025 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2862 ; 3.619 ; 4.500
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 : 4
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : A B C
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 542 A 636 3
REMARK 3 1 B 542 B 636 3
REMARK 3 1 C 542 C 636 3
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 1 A (A): 380 ; 0.020 ; 0.050
REMARK 3 TIGHT POSITIONAL 1 B (A): 380 ; 0.020 ; 0.050
REMARK 3 TIGHT POSITIONAL 1 C (A): 380 ; 0.020 ; 0.050
REMARK 3 LOOSE POSITIONAL 1 A (A): 366 ; 0.030 ; 5.000
REMARK 3 LOOSE POSITIONAL 1 B (A): 366 ; 0.030 ; 5.000
REMARK 3 LOOSE POSITIONAL 1 C (A): 366 ; 0.030 ; 5.000
REMARK 3 TIGHT THERMAL 1 A (A**2): 380 ; 0.030 ; 0.500
REMARK 3 TIGHT THERMAL 1 B (A**2): 380 ; 0.030 ; 0.500
REMARK 3 TIGHT THERMAL 1 C (A**2): 380 ; 0.030 ; 0.500
REMARK 3 LOOSE THERMAL 1 A (A**2): 366 ; 0.040 ;10.000
REMARK 3 LOOSE THERMAL 1 B (A**2): 366 ; 0.030 ;10.000
REMARK 3 LOOSE THERMAL 1 C (A**2): 366 ; 0.030 ;10.000
REMARK 3
REMARK 3 NCS GROUP NUMBER : 2
REMARK 3 CHAIN NAMES : A B C
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 757 A 852 3
REMARK 3 1 B 757 B 852 3
REMARK 3 1 C 757 C 852 3
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 2 A (A): 384 ; 0.030 ; 0.050
REMARK 3 TIGHT POSITIONAL 2 B (A): 384 ; 0.030 ; 0.050
REMARK 3 TIGHT POSITIONAL 2 C (A): 384 ; 0.030 ; 0.050
REMARK 3 LOOSE POSITIONAL 2 A (A): 376 ; 0.030 ; 5.000
REMARK 3 LOOSE POSITIONAL 2 B (A): 376 ; 0.030 ; 5.000
REMARK 3 LOOSE POSITIONAL 2 C (A): 376 ; 0.030 ; 5.000
REMARK 3 TIGHT THERMAL 2 A (A**2): 384 ; 0.030 ; 0.500
REMARK 3 TIGHT THERMAL 2 B (A**2): 384 ; 0.040 ; 0.500
REMARK 3 TIGHT THERMAL 2 C (A**2): 384 ; 0.030 ; 0.500
REMARK 3 LOOSE THERMAL 2 A (A**2): 376 ; 0.040 ;10.000
REMARK 3 LOOSE THERMAL 2 B (A**2): 376 ; 0.050 ;10.000
REMARK 3 LOOSE THERMAL 2 C (A**2): 376 ; 0.030 ;10.000
REMARK 3
REMARK 3 NCS GROUP NUMBER : 3
REMARK 3 CHAIN NAMES : A B C
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 853 A 901 3
REMARK 3 1 B 853 B 901 3
REMARK 3 1 C 853 C 901 3
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 LOOSE POSITIONAL 3 A (A): 27 ; 0.270 ; 5.000
REMARK 3 LOOSE POSITIONAL 3 B (A): 27 ; 0.440 ; 5.000
REMARK 3 LOOSE POSITIONAL 3 C (A): 27 ; 0.240 ; 5.000
REMARK 3 LOOSE THERMAL 3 A (A**2): 27 ; 4.710 ;10.000
REMARK 3 LOOSE THERMAL 3 B (A**2): 27 ; 5.040 ;10.000
REMARK 3 LOOSE THERMAL 3 C (A**2): 27 ; 2.440 ;10.000
REMARK 3
REMARK 3 NCS GROUP NUMBER : 4
REMARK 3 CHAIN NAMES : A B C
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 651 A 756 3
REMARK 3 1 B 651 B 756 3
REMARK 3 1 C 651 C 756 3
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 4 A (A): 424 ; 0.020 ; 0.050
REMARK 3 TIGHT POSITIONAL 4 B (A): 424 ; 0.020 ; 0.050
REMARK 3 TIGHT POSITIONAL 4 C (A): 424 ; 0.020 ; 0.050
REMARK 3 LOOSE POSITIONAL 4 A (A): 456 ; 0.020 ; 5.000
REMARK 3 LOOSE POSITIONAL 4 B (A): 456 ; 0.020 ; 5.000
REMARK 3 LOOSE POSITIONAL 4 C (A): 456 ; 0.020 ; 5.000
REMARK 3 TIGHT THERMAL 4 A (A**2): 424 ; 0.030 ; 0.500
REMARK 3 TIGHT THERMAL 4 B (A**2): 424 ; 0.030 ; 0.500
REMARK 3 TIGHT THERMAL 4 C (A**2): 424 ; 0.030 ; 0.500
REMARK 3 LOOSE THERMAL 4 A (A**2): 456 ; 0.030 ;10.000
REMARK 3 LOOSE THERMAL 4 B (A**2): 456 ; 0.040 ;10.000
REMARK 3 LOOSE THERMAL 4 C (A**2): 456 ; 0.030 ;10.000
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 542 A 744
REMARK 3 ORIGIN FOR THE GROUP (A): -2.5834 -15.3249 -9.8058
REMARK 3 T TENSOR
REMARK 3 T11: 0.2054 T22: 0.3646
REMARK 3 T33: 0.1578 T12: -0.2101
REMARK 3 T13: -0.0824 T23: 0.1480
REMARK 3 L TENSOR
REMARK 3 L11: 9.3101 L22: 7.3438
REMARK 3 L33: 4.8816 L12: 3.2931
REMARK 3 L13: 2.2512 L23: 1.1483
REMARK 3 S TENSOR
REMARK 3 S11: -0.1178 S12: 0.2380 S13: -0.4539
REMARK 3 S21: -0.4002 S22: 0.5115 S23: -0.3455
REMARK 3 S31: 0.2723 S32: 0.1915 S33: -0.3937
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 745 A 852
REMARK 3 ORIGIN FOR THE GROUP (A): -25.4100 -14.3595 -29.3305
REMARK 3 T TENSOR
REMARK 3 T11: 0.2952 T22: 0.6038
REMARK 3 T33: 0.2428 T12: -0.2716
REMARK 3 T13: 0.0460 T23: -0.0820
REMARK 3 L TENSOR
REMARK 3 L11: 6.8140 L22: 3.1104
REMARK 3 L33: 8.3945 L12: -2.5431
REMARK 3 L13: 6.3874 L23: -1.9276
REMARK 3 S TENSOR
REMARK 3 S11: 0.5877 S12: -0.4526 S13: -0.4147
REMARK 3 S21: -0.0026 S22: -0.3078 S23: 0.4310
REMARK 3 S31: 0.2881 S32: -1.0316 S33: -0.2799
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 : B 542 B 744
REMARK 3 ORIGIN FOR THE GROUP (A): -8.5207 4.4515 -37.8988
REMARK 3 T TENSOR
REMARK 3 T11: 0.3398 T22: 0.0606
REMARK 3 T33: 0.0213 T12: 0.0510
REMARK 3 T13: 0.0070 T23: -0.0074
REMARK 3 L TENSOR
REMARK 3 L11: 6.5624 L22: 7.0733
REMARK 3 L33: 6.4909 L12: 0.4226
REMARK 3 L13: -0.3069 L23: 2.9169
REMARK 3 S TENSOR
REMARK 3 S11: -0.1899 S12: -0.5431 S13: -0.0265
REMARK 3 S21: 0.6964 S22: 0.1941 S23: -0.2985
REMARK 3 S31: 0.2507 S32: -0.0185 S33: -0.0041
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 745 B 852
REMARK 3 ORIGIN FOR THE GROUP (A): -4.0806 4.1182 -67.6890
REMARK 3 T TENSOR
REMARK 3 T11: 0.0967 T22: 0.2201
REMARK 3 T33: 0.1555 T12: -0.0844
REMARK 3 T13: 0.0546 T23: -0.0443
REMARK 3 L TENSOR
REMARK 3 L11: 4.1850 L22: 3.9305
REMARK 3 L33: 12.6906 L12: 0.4808
REMARK 3 L13: -2.5000 L23: -4.2957
REMARK 3 S TENSOR
REMARK 3 S11: -0.4157 S12: 0.7942 S13: 0.1138
REMARK 3 S21: -0.2209 S22: -0.0666 S23: -0.2182
REMARK 3 S31: 0.7697 S32: -0.1191 S33: 0.4823
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 : C 542 C 744
REMARK 3 ORIGIN FOR THE GROUP (A): -10.4213 -34.6432 -61.3931
REMARK 3 T TENSOR
REMARK 3 T11: 0.1212 T22: 0.0497
REMARK 3 T33: 0.3354 T12: -0.0025
REMARK 3 T13: 0.0417 T23: 0.0145
REMARK 3 L TENSOR
REMARK 3 L11: 9.4328 L22: 6.8328
REMARK 3 L33: 6.8501 L12: 2.8310
REMARK 3 L13: 0.0391 L23: -2.0937
REMARK 3 S TENSOR
REMARK 3 S11: -0.2627 S12: 0.3846 S13: 0.2591
REMARK 3 S21: -0.6372 S22: 0.3817 S23: -0.2810
REMARK 3 S31: 0.3842 S32: -0.1514 S33: -0.1189
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 : C 745 C 852
REMARK 3 ORIGIN FOR THE GROUP (A): -38.5906 -32.6426 -50.7455
REMARK 3 T TENSOR
REMARK 3 T11: 0.1779 T22: 0.5094
REMARK 3 T33: 0.2169 T12: -0.1857
REMARK 3 T13: -0.0695 T23: 0.2530
REMARK 3 L TENSOR
REMARK 3 L11: 15.5081 L22: 4.5558
REMARK 3 L33: 2.7218 L12: -5.7583
REMARK 3 L13: -4.9308 L23: 1.7408
REMARK 3 S TENSOR
REMARK 3 S11: -0.1698 S12: -1.1189 S13: -0.7048
REMARK 3 S21: 0.0737 S22: 0.2657 S23: 0.4160
REMARK 3 S31: 0.0041 S32: -0.0534 S33: -0.0959
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 U VALUES: WITH TLS ADDED
REMARK 4
REMARK 4 4FCV COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-JUN-12.
REMARK 100 THE RCSB ID CODE IS RCSB072742.
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 : 8.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 19-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9786
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 12853
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.400
REMARK 200 RESOLUTION RANGE LOW (A) : 60.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : NULL
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) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
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: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 44.96
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.23
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: AMMONIUM ACETATE, PEG 3350, PH 8.0,
REMARK 280 HANGING DROP, TEMPERATURE 294K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 58.40700
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3
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: 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 350
REMARK 350 BIOMOLECULE: 2
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: B
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: 3
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: 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 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 LEU A 543 -45.45 -132.25
REMARK 500 THR A 615 146.09 179.95
REMARK 500 ALA A 618 39.59 -77.25
REMARK 500 MSE A 624 -7.61 -59.17
REMARK 500 HIS A 631 -19.44 -45.85
REMARK 500 PRO A 641 152.24 -47.17
REMARK 500 TYR A 646 -74.87 -82.49
REMARK 500 SER A 712 -63.79 -17.15
REMARK 500 PRO A 713 -1.14 -59.53
REMARK 500 GLN A 720 82.26 -61.59
REMARK 500 LYS A 721 -72.01 17.20
REMARK 500 PRO A 724 -139.78 -89.60
REMARK 500 LEU A 745 7.23 -69.32
REMARK 500 LEU B 543 -46.64 -132.40
REMARK 500 THR B 615 146.71 -179.58
REMARK 500 ALA B 618 39.73 -78.56
REMARK 500 MSE B 624 -7.29 -57.15
REMARK 500 HIS B 631 -18.06 -46.62
REMARK 500 PRO B 641 149.94 -28.71
REMARK 500 VAL B 644 -87.21 -25.41
REMARK 500 SER B 712 -61.23 -18.36
REMARK 500 PRO B 713 -2.40 -59.75
REMARK 500 GLN B 720 79.77 -61.14
REMARK 500 LYS B 721 -69.18 18.29
REMARK 500 PRO B 724 -140.30 -91.44
REMARK 500 ASP B 730 -60.14 -92.50
REMARK 500 LEU C 543 -46.59 -131.97
REMARK 500 THR C 615 145.86 178.93
REMARK 500 ALA C 618 40.39 -76.82
REMARK 500 MSE C 624 -5.82 -57.47
REMARK 500 HIS C 631 -19.64 -46.66
REMARK 500 PRO C 640 170.81 -59.44
REMARK 500 VAL C 644 -160.66 49.01
REMARK 500 SER C 712 -62.63 -16.51
REMARK 500 GLN C 720 82.09 -61.10
REMARK 500 LYS C 721 -70.81 17.19
REMARK 500 PRO C 724 -139.99 -89.81
REMARK 500 ASP C 730 -60.53 -94.12
REMARK 500 LEU C 745 6.87 -68.72
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 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP B 901
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP C 901
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4FCT RELATED DB: PDB
REMARK 900 RELATED ID: 4FCW RELATED DB: PDB
REMARK 900 RELATED ID: 4FD2 RELATED DB: PDB
DBREF 4FCV A 544 852 UNP Q9RA63 CLPB_THET8 544 852
DBREF 4FCV B 544 852 UNP Q9RA63 CLPB_THET8 544 852
DBREF 4FCV C 544 852 UNP Q9RA63 CLPB_THET8 544 852
SEQADV 4FCV MSE A 542 UNP Q9RA63 EXPRESSION TAG
SEQADV 4FCV LEU A 543 UNP Q9RA63 EXPRESSION TAG
SEQADV 4FCV ALA A 668 UNP Q9RA63 GLU 668 ENGINEERED MUTATION
SEQADV 4FCV MSE A 683 UNP Q9RA63 ILE 683 ENGINEERED MUTATION
SEQADV 4FCV MSE A 706 UNP Q9RA63 LEU 706 ENGINEERED MUTATION
SEQADV 4FCV MSE A 770 UNP Q9RA63 LEU 770 ENGINEERED MUTATION
SEQADV 4FCV MSE B 542 UNP Q9RA63 EXPRESSION TAG
SEQADV 4FCV LEU B 543 UNP Q9RA63 EXPRESSION TAG
SEQADV 4FCV ALA B 668 UNP Q9RA63 GLU 668 ENGINEERED MUTATION
SEQADV 4FCV MSE B 683 UNP Q9RA63 ILE 683 ENGINEERED MUTATION
SEQADV 4FCV MSE B 706 UNP Q9RA63 LEU 706 ENGINEERED MUTATION
SEQADV 4FCV MSE B 770 UNP Q9RA63 LEU 770 ENGINEERED MUTATION
SEQADV 4FCV MSE C 542 UNP Q9RA63 EXPRESSION TAG
SEQADV 4FCV LEU C 543 UNP Q9RA63 EXPRESSION TAG
SEQADV 4FCV ALA C 668 UNP Q9RA63 GLU 668 ENGINEERED MUTATION
SEQADV 4FCV MSE C 683 UNP Q9RA63 ILE 683 ENGINEERED MUTATION
SEQADV 4FCV MSE C 706 UNP Q9RA63 LEU 706 ENGINEERED MUTATION
SEQADV 4FCV MSE C 770 UNP Q9RA63 LEU 770 ENGINEERED MUTATION
SEQRES 1 A 311 MSE LEU GLY GLU ARG GLU LYS LEU LEU ARG LEU GLU GLU
SEQRES 2 A 311 GLU LEU HIS LYS ARG VAL VAL GLY GLN ASP GLU ALA ILE
SEQRES 3 A 311 ARG ALA VAL ALA ASP ALA ILE ARG ARG ALA ARG ALA GLY
SEQRES 4 A 311 LEU LYS ASP PRO ASN ARG PRO ILE GLY SER PHE LEU PHE
SEQRES 5 A 311 LEU GLY PRO THR GLY VAL GLY LYS THR GLU LEU ALA LYS
SEQRES 6 A 311 THR LEU ALA ALA THR LEU PHE ASP THR GLU GLU ALA MSE
SEQRES 7 A 311 ILE ARG ILE ASP MSE THR GLU TYR MSE GLU LYS HIS ALA
SEQRES 8 A 311 VAL SER ARG LEU ILE GLY ALA PRO PRO GLY TYR VAL GLY
SEQRES 9 A 311 TYR GLU GLU GLY GLY GLN LEU THR GLU ALA VAL ARG ARG
SEQRES 10 A 311 ARG PRO TYR SER VAL ILE LEU PHE ASP ALA ILE GLU LYS
SEQRES 11 A 311 ALA HIS PRO ASP VAL PHE ASN ILE LEU LEU GLN MSE LEU
SEQRES 12 A 311 ASP ASP GLY ARG LEU THR ASP SER HIS GLY ARG THR VAL
SEQRES 13 A 311 ASP PHE ARG ASN THR VAL ILE ILE MSE THR SER ASN LEU
SEQRES 14 A 311 GLY SER PRO LEU ILE LEU GLU GLY LEU GLN LYS GLY TRP
SEQRES 15 A 311 PRO TYR GLU ARG ILE ARG ASP GLU VAL PHE LYS VAL LEU
SEQRES 16 A 311 GLN GLN HIS PHE ARG PRO GLU PHE LEU ASN ARG LEU ASP
SEQRES 17 A 311 GLU ILE VAL VAL PHE ARG PRO LEU THR LYS GLU GLN ILE
SEQRES 18 A 311 ARG GLN ILE VAL GLU ILE GLN MSE SER TYR LEU ARG ALA
SEQRES 19 A 311 ARG LEU ALA GLU LYS ARG ILE SER LEU GLU LEU THR GLU
SEQRES 20 A 311 ALA ALA LYS ASP PHE LEU ALA GLU ARG GLY TYR ASP PRO
SEQRES 21 A 311 VAL PHE GLY ALA ARG PRO LEU ARG ARG VAL ILE GLN ARG
SEQRES 22 A 311 GLU LEU GLU THR PRO LEU ALA GLN LYS ILE LEU ALA GLY
SEQRES 23 A 311 GLU VAL LYS GLU GLY ASP ARG VAL GLN VAL ASP VAL GLY
SEQRES 24 A 311 PRO ALA GLY LEU VAL PHE ALA VAL PRO ALA ARG VAL
SEQRES 1 B 311 MSE LEU GLY GLU ARG GLU LYS LEU LEU ARG LEU GLU GLU
SEQRES 2 B 311 GLU LEU HIS LYS ARG VAL VAL GLY GLN ASP GLU ALA ILE
SEQRES 3 B 311 ARG ALA VAL ALA ASP ALA ILE ARG ARG ALA ARG ALA GLY
SEQRES 4 B 311 LEU LYS ASP PRO ASN ARG PRO ILE GLY SER PHE LEU PHE
SEQRES 5 B 311 LEU GLY PRO THR GLY VAL GLY LYS THR GLU LEU ALA LYS
SEQRES 6 B 311 THR LEU ALA ALA THR LEU PHE ASP THR GLU GLU ALA MSE
SEQRES 7 B 311 ILE ARG ILE ASP MSE THR GLU TYR MSE GLU LYS HIS ALA
SEQRES 8 B 311 VAL SER ARG LEU ILE GLY ALA PRO PRO GLY TYR VAL GLY
SEQRES 9 B 311 TYR GLU GLU GLY GLY GLN LEU THR GLU ALA VAL ARG ARG
SEQRES 10 B 311 ARG PRO TYR SER VAL ILE LEU PHE ASP ALA ILE GLU LYS
SEQRES 11 B 311 ALA HIS PRO ASP VAL PHE ASN ILE LEU LEU GLN MSE LEU
SEQRES 12 B 311 ASP ASP GLY ARG LEU THR ASP SER HIS GLY ARG THR VAL
SEQRES 13 B 311 ASP PHE ARG ASN THR VAL ILE ILE MSE THR SER ASN LEU
SEQRES 14 B 311 GLY SER PRO LEU ILE LEU GLU GLY LEU GLN LYS GLY TRP
SEQRES 15 B 311 PRO TYR GLU ARG ILE ARG ASP GLU VAL PHE LYS VAL LEU
SEQRES 16 B 311 GLN GLN HIS PHE ARG PRO GLU PHE LEU ASN ARG LEU ASP
SEQRES 17 B 311 GLU ILE VAL VAL PHE ARG PRO LEU THR LYS GLU GLN ILE
SEQRES 18 B 311 ARG GLN ILE VAL GLU ILE GLN MSE SER TYR LEU ARG ALA
SEQRES 19 B 311 ARG LEU ALA GLU LYS ARG ILE SER LEU GLU LEU THR GLU
SEQRES 20 B 311 ALA ALA LYS ASP PHE LEU ALA GLU ARG GLY TYR ASP PRO
SEQRES 21 B 311 VAL PHE GLY ALA ARG PRO LEU ARG ARG VAL ILE GLN ARG
SEQRES 22 B 311 GLU LEU GLU THR PRO LEU ALA GLN LYS ILE LEU ALA GLY
SEQRES 23 B 311 GLU VAL LYS GLU GLY ASP ARG VAL GLN VAL ASP VAL GLY
SEQRES 24 B 311 PRO ALA GLY LEU VAL PHE ALA VAL PRO ALA ARG VAL
SEQRES 1 C 311 MSE LEU GLY GLU ARG GLU LYS LEU LEU ARG LEU GLU GLU
SEQRES 2 C 311 GLU LEU HIS LYS ARG VAL VAL GLY GLN ASP GLU ALA ILE
SEQRES 3 C 311 ARG ALA VAL ALA ASP ALA ILE ARG ARG ALA ARG ALA GLY
SEQRES 4 C 311 LEU LYS ASP PRO ASN ARG PRO ILE GLY SER PHE LEU PHE
SEQRES 5 C 311 LEU GLY PRO THR GLY VAL GLY LYS THR GLU LEU ALA LYS
SEQRES 6 C 311 THR LEU ALA ALA THR LEU PHE ASP THR GLU GLU ALA MSE
SEQRES 7 C 311 ILE ARG ILE ASP MSE THR GLU TYR MSE GLU LYS HIS ALA
SEQRES 8 C 311 VAL SER ARG LEU ILE GLY ALA PRO PRO GLY TYR VAL GLY
SEQRES 9 C 311 TYR GLU GLU GLY GLY GLN LEU THR GLU ALA VAL ARG ARG
SEQRES 10 C 311 ARG PRO TYR SER VAL ILE LEU PHE ASP ALA ILE GLU LYS
SEQRES 11 C 311 ALA HIS PRO ASP VAL PHE ASN ILE LEU LEU GLN MSE LEU
SEQRES 12 C 311 ASP ASP GLY ARG LEU THR ASP SER HIS GLY ARG THR VAL
SEQRES 13 C 311 ASP PHE ARG ASN THR VAL ILE ILE MSE THR SER ASN LEU
SEQRES 14 C 311 GLY SER PRO LEU ILE LEU GLU GLY LEU GLN LYS GLY TRP
SEQRES 15 C 311 PRO TYR GLU ARG ILE ARG ASP GLU VAL PHE LYS VAL LEU
SEQRES 16 C 311 GLN GLN HIS PHE ARG PRO GLU PHE LEU ASN ARG LEU ASP
SEQRES 17 C 311 GLU ILE VAL VAL PHE ARG PRO LEU THR LYS GLU GLN ILE
SEQRES 18 C 311 ARG GLN ILE VAL GLU ILE GLN MSE SER TYR LEU ARG ALA
SEQRES 19 C 311 ARG LEU ALA GLU LYS ARG ILE SER LEU GLU LEU THR GLU
SEQRES 20 C 311 ALA ALA LYS ASP PHE LEU ALA GLU ARG GLY TYR ASP PRO
SEQRES 21 C 311 VAL PHE GLY ALA ARG PRO LEU ARG ARG VAL ILE GLN ARG
SEQRES 22 C 311 GLU LEU GLU THR PRO LEU ALA GLN LYS ILE LEU ALA GLY
SEQRES 23 C 311 GLU VAL LYS GLU GLY ASP ARG VAL GLN VAL ASP VAL GLY
SEQRES 24 C 311 PRO ALA GLY LEU VAL PHE ALA VAL PRO ALA ARG VAL
MODRES 4FCV MSE A 542 MET SELENOMETHIONINE
MODRES 4FCV MSE A 619 MET SELENOMETHIONINE
MODRES 4FCV MSE A 624 MET SELENOMETHIONINE
MODRES 4FCV MSE A 628 MET SELENOMETHIONINE
MODRES 4FCV MSE A 683 MET SELENOMETHIONINE
MODRES 4FCV MSE A 706 MET SELENOMETHIONINE
MODRES 4FCV MSE A 770 MET SELENOMETHIONINE
MODRES 4FCV MSE B 542 MET SELENOMETHIONINE
MODRES 4FCV MSE B 619 MET SELENOMETHIONINE
MODRES 4FCV MSE B 624 MET SELENOMETHIONINE
MODRES 4FCV MSE B 628 MET SELENOMETHIONINE
MODRES 4FCV MSE B 683 MET SELENOMETHIONINE
MODRES 4FCV MSE B 706 MET SELENOMETHIONINE
MODRES 4FCV MSE B 770 MET SELENOMETHIONINE
MODRES 4FCV MSE C 542 MET SELENOMETHIONINE
MODRES 4FCV MSE C 619 MET SELENOMETHIONINE
MODRES 4FCV MSE C 624 MET SELENOMETHIONINE
MODRES 4FCV MSE C 628 MET SELENOMETHIONINE
MODRES 4FCV MSE C 683 MET SELENOMETHIONINE
MODRES 4FCV MSE C 706 MET SELENOMETHIONINE
MODRES 4FCV MSE C 770 MET SELENOMETHIONINE
HET MSE A 542 8
HET MSE A 619 8
HET MSE A 624 8
HET MSE A 628 8
HET MSE A 683 8
HET MSE A 706 8
HET MSE A 770 8
HET MSE B 542 8
HET MSE B 619 8
HET MSE B 624 8
HET MSE B 628 8
HET MSE B 683 8
HET MSE B 706 8
HET MSE B 770 8
HET MSE C 542 8
HET MSE C 619 8
HET MSE C 624 8
HET MSE C 628 8
HET MSE C 683 8
HET MSE C 706 8
HET MSE C 770 8
HET ADP A 901 27
HET ADP B 901 27
HET ADP C 901 27
HETNAM MSE SELENOMETHIONINE
HETNAM ADP ADENOSINE-5'-DIPHOSPHATE
FORMUL 1 MSE 21(C5 H11 N O2 SE)
FORMUL 4 ADP 3(C10 H15 N5 O10 P2)
HELIX 1 1 LEU A 543 ARG A 551 1 9
HELIX 2 2 ARG A 551 LYS A 558 1 8
HELIX 3 3 GLN A 563 GLY A 580 1 18
HELIX 4 4 GLY A 600 ASP A 614 1 15
HELIX 5 5 THR A 625 TYR A 627 5 3
HELIX 6 6 LYS A 630 GLY A 638 1 9
HELIX 7 7 GLY A 650 ARG A 659 1 10
HELIX 8 8 ALA A 668 ALA A 672 5 5
HELIX 9 9 HIS A 673 GLY A 687 1 15
HELIX 10 10 GLY A 711 LEU A 714 5 4
HELIX 11 11 ILE A 715 GLN A 720 1 6
HELIX 12 12 GLU A 726 PHE A 740 1 15
HELIX 13 13 GLU A 743 LEU A 748 1 6
HELIX 14 14 THR A 758 MSE A 770 1 13
HELIX 15 15 MSE A 770 GLU A 779 1 10
HELIX 16 16 THR A 787 TYR A 799 1 13
HELIX 17 17 PRO A 807 LEU A 816 1 10
HELIX 18 18 LEU A 816 GLY A 827 1 12
HELIX 19 19 LEU B 543 ARG B 551 1 9
HELIX 20 20 ARG B 551 LYS B 558 1 8
HELIX 21 21 GLN B 563 GLY B 580 1 18
HELIX 22 22 GLY B 600 ASP B 614 1 15
HELIX 23 23 THR B 625 TYR B 627 5 3
HELIX 24 24 HIS B 631 GLY B 638 1 8
HELIX 25 25 GLY B 650 ARG B 659 1 10
HELIX 26 26 ALA B 668 ALA B 672 5 5
HELIX 27 27 HIS B 673 GLY B 687 1 15
HELIX 28 28 GLY B 711 LEU B 714 5 4
HELIX 29 29 ILE B 715 GLN B 720 1 6
HELIX 30 30 GLU B 726 PHE B 740 1 15
HELIX 31 31 GLU B 743 LEU B 748 1 6
HELIX 32 32 THR B 758 MSE B 770 1 13
HELIX 33 33 MSE B 770 GLU B 779 1 10
HELIX 34 34 THR B 787 TYR B 799 1 13
HELIX 35 35 PRO B 807 LEU B 816 1 10
HELIX 36 36 LEU B 816 GLY B 827 1 12
HELIX 37 37 LEU C 543 ARG C 551 1 9
HELIX 38 38 ARG C 551 LYS C 558 1 8
HELIX 39 39 GLN C 563 GLY C 580 1 18
HELIX 40 40 GLY C 600 ASP C 614 1 15
HELIX 41 41 THR C 625 TYR C 627 5 3
HELIX 42 42 HIS C 631 GLY C 638 1 8
HELIX 43 43 GLY C 650 ARG C 659 1 10
HELIX 44 44 ALA C 668 ALA C 672 5 5
HELIX 45 45 HIS C 673 GLY C 687 1 15
HELIX 46 46 GLY C 711 LEU C 714 5 4
HELIX 47 47 ILE C 715 GLN C 720 1 6
HELIX 48 48 GLU C 726 PHE C 740 1 15
HELIX 49 49 GLU C 743 LEU C 748 1 6
HELIX 50 50 THR C 758 MSE C 770 1 13
HELIX 51 51 MSE C 770 GLU C 779 1 10
HELIX 52 52 THR C 787 TYR C 799 1 13
HELIX 53 53 PRO C 807 LEU C 816 1 10
HELIX 54 54 LEU C 816 GLY C 827 1 12
SHEET 1 A 5 MSE 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 SER A 708 1 O ILE A 705 N ILE A 664
SHEET 4 A 5 GLY A 589 LEU A 594 1 N GLY A 589 O ILE A 704
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 835 N SER A 783
SHEET 3 C 3 LEU A 844 ALA A 847 -1 O VAL A 845 N ASP A 838
SHEET 1 D 5 MSE B 619 ASP B 623 0
SHEET 2 D 5 SER B 662 ASP B 667 1 O LEU B 665 N ILE B 622
SHEET 3 D 5 THR B 702 SER B 708 1 O ILE B 705 N ILE B 664
SHEET 4 D 5 GLY B 589 LEU B 594 1 N GLY B 589 O ILE B 704
SHEET 5 D 5 GLU B 750 VAL B 753 1 O VAL B 752 N LEU B 592
SHEET 1 E 2 ARG B 688 THR B 690 0
SHEET 2 E 2 THR B 696 ASP B 698 -1 O VAL B 697 N LEU B 689
SHEET 1 F 3 SER B 783 LEU B 786 0
SHEET 2 F 3 ARG B 834 ASP B 838 1 O VAL B 835 N SER B 783
SHEET 3 F 3 VAL B 845 ALA B 847 -1 O VAL B 845 N ASP B 838
SHEET 1 G 5 MSE C 619 ASP C 623 0
SHEET 2 G 5 SER C 662 ASP C 667 1 O LEU C 665 N ILE C 620
SHEET 3 G 5 THR C 702 SER C 708 1 O ILE C 705 N ILE C 664
SHEET 4 G 5 GLY C 589 LEU C 594 1 N PHE C 591 O MSE C 706
SHEET 5 G 5 GLU C 750 VAL C 753 1 O VAL C 752 N LEU C 592
SHEET 1 H 2 ARG C 688 THR C 690 0
SHEET 2 H 2 THR C 696 ASP C 698 -1 O VAL C 697 N LEU C 689
SHEET 1 I 3 SER C 783 LEU C 786 0
SHEET 2 I 3 ARG C 834 VAL C 839 1 O VAL C 835 N SER C 783
SHEET 3 I 3 LEU C 844 ALA C 847 -1 O ALA C 847 N GLN C 836
LINK C MSE A 542 N LEU A 543 1555 1555 1.33
LINK C ALA A 618 N MSE A 619 1555 1555 1.33
LINK C MSE A 619 N ILE A 620 1555 1555 1.32
LINK C ASP A 623 N MSE A 624 1555 1555 1.33
LINK C MSE A 624 N THR A 625 1555 1555 1.33
LINK C TYR A 627 N MSE A 628 1555 1555 1.33
LINK C MSE A 628 N GLU A 629 1555 1555 1.33
LINK C GLN A 682 N MSE A 683 1555 1555 1.32
LINK C MSE A 683 N LEU A 684 1555 1555 1.33
LINK C ILE A 705 N MSE A 706 1555 1555 1.33
LINK C MSE A 706 N THR A 707 1555 1555 1.33
LINK C GLN A 769 N MSE A 770 1555 1555 1.33
LINK C MSE A 770 N SER A 771 1555 1555 1.33
LINK C MSE B 542 N LEU B 543 1555 1555 1.33
LINK C ALA B 618 N MSE B 619 1555 1555 1.32
LINK C MSE B 619 N ILE B 620 1555 1555 1.32
LINK C ASP B 623 N MSE B 624 1555 1555 1.33
LINK C MSE B 624 N THR B 625 1555 1555 1.33
LINK C TYR B 627 N MSE B 628 1555 1555 1.33
LINK C MSE B 628 N GLU B 629 1555 1555 1.33
LINK C GLN B 682 N MSE B 683 1555 1555 1.33
LINK C MSE B 683 N LEU B 684 1555 1555 1.33
LINK C ILE B 705 N MSE B 706 1555 1555 1.33
LINK C MSE B 706 N THR B 707 1555 1555 1.33
LINK C GLN B 769 N MSE B 770 1555 1555 1.33
LINK C MSE B 770 N SER B 771 1555 1555 1.33
LINK C MSE C 542 N LEU C 543 1555 1555 1.33
LINK C ALA C 618 N MSE C 619 1555 1555 1.33
LINK C MSE C 619 N ILE C 620 1555 1555 1.32
LINK C ASP C 623 N MSE C 624 1555 1555 1.33
LINK C MSE C 624 N THR C 625 1555 1555 1.33
LINK C TYR C 627 N MSE C 628 1555 1555 1.33
LINK C MSE C 628 N GLU C 629 1555 1555 1.33
LINK C GLN C 682 N MSE C 683 1555 1555 1.33
LINK C MSE C 683 N LEU C 684 1555 1555 1.33
LINK C ILE C 705 N MSE C 706 1555 1555 1.33
LINK C MSE C 706 N THR C 707 1555 1555 1.33
LINK C GLN C 769 N MSE C 770 1555 1555 1.33
LINK C MSE C 770 N SER C 771 1555 1555 1.32
SITE 1 AC1 10 ARG A 559 VAL A 560 VAL A 561 THR A 597
SITE 2 AC1 10 GLY A 598 VAL A 599 GLY A 600 LYS A 601
SITE 3 AC1 10 THR A 602 GLU A 603
SITE 1 AC2 10 ARG B 559 VAL B 561 THR B 597 GLY B 598
SITE 2 AC2 10 VAL B 599 GLY B 600 LYS B 601 THR B 602
SITE 3 AC2 10 GLU B 603 ALA B 805
SITE 1 AC3 10 ARG C 559 VAL C 561 THR C 597 GLY C 598
SITE 2 AC3 10 VAL C 599 GLY C 600 LYS C 601 THR C 602
SITE 3 AC3 10 GLU C 603 ILE C 765
CRYST1 68.146 116.814 68.945 90.00 119.52 90.00 P 1 21 1 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 0.014674 0.000000 0.008310 0.00000
SCALE2 0.000000 0.008561 0.000000 0.00000
SCALE3 0.000000 0.000000 0.016668 0.00000
HETATM 1 N MSE A 542 -18.164 -6.497 10.706 1.00168.01 N
ANISOU 1 N MSE A 542 16540 29711 17585 -2935 5225 -4199 N
HETATM 2 CA MSE A 542 -18.693 -6.797 9.341 1.00162.95 C
ANISOU 2 CA MSE A 542 15653 28409 17851 -2643 4864 -3678 C
HETATM 3 C MSE A 542 -19.910 -7.724 9.381 1.00165.26 C
ANISOU 3 C MSE A 542 15536 29167 18090 -2969 5216 -3370 C
HETATM 4 O MSE A 542 -19.914 -8.721 10.105 1.00167.38 O
ANISOU 4 O MSE A 542 16038 30071 17488 -3539 5420 -2955 O
HETATM 5 CB MSE A 542 -17.597 -7.392 8.442 1.00154.39 C
ANISOU 5 CB MSE A 542 15168 26723 16770 -2610 4140 -2831 C
HETATM 6 CG MSE A 542 -16.936 -8.680 8.960 1.00157.24 C
ANISOU 6 CG MSE A 542 16077 27485 16181 -3145 4000 -2102 C
HETATM 7 SE MSE A 542 -16.621 -9.997 7.532 1.00160.64 SE
ANISOU 7 SE MSE A 542 16824 27259 16952 -3163 3320 -970 SE
HETATM 8 CE MSE A 542 -14.880 -10.694 8.130 1.00154.89 C
ANISOU 8 CE MSE A 542 16904 26591 15355 -3452 2878 -451 C
(ATOM LINES ARE NOT SHOWN.)
END
