HEADER CHAPERONE 25-MAY-12 4FD2
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, D;
COMPND 4 FRAGMENT: UNP RESIDUES 545-852;
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 4 28-FEB-24 4FD2 1 REMARK SEQADV
REVDAT 3 18-APR-18 4FD2 1 REMARK
REVDAT 2 22-AUG-12 4FD2 1 JRNL
REVDAT 1 18-JUL-12 4FD2 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. 3.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0109
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) : 3.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 42.48
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.8
REMARK 3 NUMBER OF REFLECTIONS : 24567
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING + TEST SET) : 0.279
REMARK 3 R VALUE (WORKING SET) : 0.278
REMARK 3 FREE R VALUE : 0.298
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1001
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 3.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.08
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1696
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 97.53
REMARK 3 BIN R VALUE (WORKING SET) : 0.3550
REMARK 3 BIN FREE R VALUE SET COUNT : 81
REMARK 3 BIN FREE R VALUE : 0.3250
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 7386
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) : 109.4
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -25.04000
REMARK 3 B22 (A**2) : -25.04000
REMARK 3 B33 (A**2) : 50.07000
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): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): NULL
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.500
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 72.784
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.901
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.882
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 7599 ; 0.013 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 10284 ; 1.515 ; 2.001
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 921 ; 5.745 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 366 ;35.023 ;22.623
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1368 ;20.350 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 96 ;19.958 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1161 ; 0.092 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5718 ; 0.006 ; 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): 4599 ; 1.707 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 7431 ; 3.225 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 3000 ; 3.985 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2853 ; 7.443 ; 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 : 3
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : A B D
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 545 A 756 4
REMARK 3 1 B 545 B 756 4
REMARK 3 1 D 545 D 756 4
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 1 A (A): 1702 ; 0.150 ; 0.500
REMARK 3 MEDIUM POSITIONAL 1 B (A): 1702 ; 0.180 ; 0.500
REMARK 3 MEDIUM POSITIONAL 1 D (A): 1702 ; 0.140 ; 0.500
REMARK 3 MEDIUM THERMAL 1 A (A**2): 1702 ; 1.500 ; 2.000
REMARK 3 MEDIUM THERMAL 1 B (A**2): 1702 ; 1.020 ; 2.000
REMARK 3 MEDIUM THERMAL 1 D (A**2): 1702 ; 0.840 ; 2.000
REMARK 3
REMARK 3 NCS GROUP NUMBER : 2
REMARK 3 CHAIN NAMES : A B D
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 757 A 852 4
REMARK 3 1 B 757 B 852 4
REMARK 3 1 D 757 D 852 4
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 2 A (A): 760 ; 0.120 ; 0.500
REMARK 3 MEDIUM POSITIONAL 2 B (A): 760 ; 0.200 ; 0.500
REMARK 3 MEDIUM POSITIONAL 2 D (A): 760 ; 0.150 ; 0.500
REMARK 3 MEDIUM THERMAL 2 A (A**2): 760 ; 1.400 ; 2.000
REMARK 3 MEDIUM THERMAL 2 B (A**2): 760 ; 1.240 ; 2.000
REMARK 3 MEDIUM THERMAL 2 D (A**2): 760 ; 0.590 ; 2.000
REMARK 3
REMARK 3 NCS GROUP NUMBER : 3
REMARK 3 CHAIN NAMES : A B D
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 853 A 853 4
REMARK 3 1 B 853 B 853 4
REMARK 3 1 D 853 D 853 4
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 3 A (A): 27 ; 0.320 ; 0.500
REMARK 3 MEDIUM POSITIONAL 3 B (A): 27 ; 0.400 ; 0.500
REMARK 3 MEDIUM POSITIONAL 3 D (A): 27 ; 0.530 ; 0.500
REMARK 3 MEDIUM THERMAL 3 A (A**2): 27 ; 0.200 ; 2.000
REMARK 3 MEDIUM THERMAL 3 B (A**2): 27 ; 0.290 ; 2.000
REMARK 3 MEDIUM THERMAL 3 D (A**2): 27 ; 0.210 ; 2.000
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 : 0.497
REMARK 3 TWIN DOMAIN : 2
REMARK 3 TWIN OPERATOR : H+K,-K,-L
REMARK 3 TWIN FRACTION : 0.503
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 21
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 545 A 573
REMARK 3 ORIGIN FOR THE GROUP (A): -48.4804 -2.8295 41.3899
REMARK 3 T TENSOR
REMARK 3 T11: 0.4111 T22: 0.5226
REMARK 3 T33: 0.0436 T12: 0.2569
REMARK 3 T13: 0.0374 T23: 0.0271
REMARK 3 L TENSOR
REMARK 3 L11: 14.7635 L22: 23.4111
REMARK 3 L33: 1.0309 L12: 13.4796
REMARK 3 L13: -1.9313 L23: -5.2274
REMARK 3 S TENSOR
REMARK 3 S11: 0.3374 S12: 0.9198 S13: -0.7641
REMARK 3 S21: 0.4823 S22: -0.4809 S23: -0.7095
REMARK 3 S31: 0.0301 S32: 0.3771 S33: 0.1435
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 574 A 628
REMARK 3 ORIGIN FOR THE GROUP (A): -55.9172 7.3322 37.4749
REMARK 3 T TENSOR
REMARK 3 T11: 0.4081 T22: 0.5499
REMARK 3 T33: 0.1808 T12: -0.0155
REMARK 3 T13: 0.0541 T23: 0.0579
REMARK 3 L TENSOR
REMARK 3 L11: 3.0239 L22: 2.4797
REMARK 3 L33: 1.8345 L12: 0.8251
REMARK 3 L13: 1.1028 L23: 0.1019
REMARK 3 S TENSOR
REMARK 3 S11: 0.0800 S12: 0.1287 S13: 0.2115
REMARK 3 S21: -0.3104 S22: -0.1758 S23: 0.2051
REMARK 3 S31: -0.2490 S32: 0.0796 S33: 0.0958
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 629 A 640
REMARK 3 ORIGIN FOR THE GROUP (A): -67.6004 25.4094 30.4338
REMARK 3 T TENSOR
REMARK 3 T11: 1.9179 T22: 0.8976
REMARK 3 T33: 0.9235 T12: -0.3563
REMARK 3 T13: -0.6659 T23: 0.2566
REMARK 3 L TENSOR
REMARK 3 L11: 7.9238 L22: 42.8971
REMARK 3 L33: 6.2052 L12: -5.3171
REMARK 3 L13: -6.6102 L23: -8.8245
REMARK 3 S TENSOR
REMARK 3 S11: -0.7124 S12: -0.3763 S13: 2.0730
REMARK 3 S21: -4.3670 S22: 3.3573 S23: 3.6502
REMARK 3 S31: 1.4961 S32: -0.6493 S33: -2.6449
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 : A 641 A 651
REMARK 3 ORIGIN FOR THE GROUP (A): -68.6007 23.9254 20.9087
REMARK 3 T TENSOR
REMARK 3 T11: 1.1008 T22: 1.8312
REMARK 3 T33: 3.9076 T12: 0.4155
REMARK 3 T13: 0.5029 T23: -0.1480
REMARK 3 L TENSOR
REMARK 3 L11: 2.9666 L22: 68.8646
REMARK 3 L33: 15.8944 L12: -24.3745
REMARK 3 L13: 7.0618 L23: -28.0721
REMARK 3 S TENSOR
REMARK 3 S11: -2.4043 S12: 1.3486 S13: -1.2115
REMARK 3 S21: 6.9868 S22: -1.3222 S23: 1.5535
REMARK 3 S31: -2.3902 S32: -0.4457 S33: 3.7266
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 : A 652 A 712
REMARK 3 ORIGIN FOR THE GROUP (A): -64.4884 13.1780 34.3742
REMARK 3 T TENSOR
REMARK 3 T11: 0.4480 T22: 0.5466
REMARK 3 T33: 0.2361 T12: 0.1035
REMARK 3 T13: 0.0555 T23: 0.0464
REMARK 3 L TENSOR
REMARK 3 L11: 6.2041 L22: 1.5250
REMARK 3 L33: 2.6271 L12: 1.0279
REMARK 3 L13: 2.4081 L23: -1.2415
REMARK 3 S TENSOR
REMARK 3 S11: -0.1112 S12: -0.0205 S13: 0.8032
REMARK 3 S21: 0.0905 S22: 0.0163 S23: 0.3068
REMARK 3 S31: -0.2569 S32: -0.0804 S33: 0.0949
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 : A 713 A 743
REMARK 3 ORIGIN FOR THE GROUP (A): -54.8987 13.2649 57.0878
REMARK 3 T TENSOR
REMARK 3 T11: 0.3330 T22: 0.8502
REMARK 3 T33: 0.1044 T12: -0.2120
REMARK 3 T13: 0.1990 T23: 0.0141
REMARK 3 L TENSOR
REMARK 3 L11: 30.2297 L22: 10.4819
REMARK 3 L33: 18.4936 L12: -7.3139
REMARK 3 L13: 17.0310 L23: -3.8443
REMARK 3 S TENSOR
REMARK 3 S11: 0.2387 S12: -3.6177 S13: -0.6391
REMARK 3 S21: 0.4823 S22: -0.5998 S23: 0.7311
REMARK 3 S31: 0.6535 S32: -1.0340 S33: 0.3612
REMARK 3
REMARK 3 TLS GROUP : 7
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 744 A 852
REMARK 3 ORIGIN FOR THE GROUP (A): -29.2677 12.1431 36.1919
REMARK 3 T TENSOR
REMARK 3 T11: 0.4356 T22: 0.4198
REMARK 3 T33: 0.3181 T12: 0.0105
REMARK 3 T13: -0.0335 T23: 0.0996
REMARK 3 L TENSOR
REMARK 3 L11: 7.5610 L22: 0.5010
REMARK 3 L33: 2.7282 L12: 1.2435
REMARK 3 L13: -3.6866 L23: -0.5006
REMARK 3 S TENSOR
REMARK 3 S11: 0.0194 S12: -0.1726 S13: -0.2898
REMARK 3 S21: 0.1142 S22: -0.1016 S23: -0.1170
REMARK 3 S31: -0.0416 S32: 0.1837 S33: 0.0822
REMARK 3
REMARK 3 TLS GROUP : 8
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 545 B 573
REMARK 3 ORIGIN FOR THE GROUP (A): -43.1383 -5.8435 -37.0306
REMARK 3 T TENSOR
REMARK 3 T11: 0.5113 T22: 0.6207
REMARK 3 T33: 0.0875 T12: 0.1613
REMARK 3 T13: 0.0887 T23: -0.1602
REMARK 3 L TENSOR
REMARK 3 L11: 11.3320 L22: 15.0753
REMARK 3 L33: 1.6619 L12: 8.5892
REMARK 3 L13: 4.7576 L23: 3.2632
REMARK 3 S TENSOR
REMARK 3 S11: -0.0088 S12: -0.0573 S13: 0.0806
REMARK 3 S21: 0.7422 S22: -0.0708 S23: 0.6735
REMARK 3 S31: -0.0176 S32: -0.2114 S33: 0.0795
REMARK 3
REMARK 3 TLS GROUP : 9
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 574 B 628
REMARK 3 ORIGIN FOR THE GROUP (A): -30.8330 -7.4677 -32.8015
REMARK 3 T TENSOR
REMARK 3 T11: 0.6720 T22: 0.6624
REMARK 3 T33: 0.5161 T12: 0.0094
REMARK 3 T13: 0.0165 T23: -0.0503
REMARK 3 L TENSOR
REMARK 3 L11: 0.1931 L22: 3.5670
REMARK 3 L33: 2.0445 L12: -0.0816
REMARK 3 L13: -0.8021 L23: -0.9947
REMARK 3 S TENSOR
REMARK 3 S11: -0.0400 S12: -0.0788 S13: -0.0359
REMARK 3 S21: 0.3410 S22: -0.0101 S23: -0.4432
REMARK 3 S31: -0.1297 S32: 0.1865 S33: 0.0502
REMARK 3
REMARK 3 TLS GROUP : 10
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 629 B 651
REMARK 3 ORIGIN FOR THE GROUP (A): -10.1777 -9.8297 -20.5239
REMARK 3 T TENSOR
REMARK 3 T11: 0.7174 T22: 1.3684
REMARK 3 T33: 1.7801 T12: -0.0848
REMARK 3 T13: 0.0700 T23: 0.2957
REMARK 3 L TENSOR
REMARK 3 L11: 4.7765 L22: 4.4634
REMARK 3 L33: 55.0495 L12: -5.7543
REMARK 3 L13: -4.2821 L23: 7.3159
REMARK 3 S TENSOR
REMARK 3 S11: -1.3872 S12: -0.6548 S13: -0.5646
REMARK 3 S21: 1.1984 S22: 0.5658 S23: 0.1907
REMARK 3 S31: -1.7815 S32: 4.1225 S33: 0.8215
REMARK 3
REMARK 3 TLS GROUP : 11
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 652 B 708
REMARK 3 ORIGIN FOR THE GROUP (A): -21.6720 -12.9355 -28.6220
REMARK 3 T TENSOR
REMARK 3 T11: 0.5857 T22: 0.6937
REMARK 3 T33: 0.4747 T12: 0.0732
REMARK 3 T13: -0.0580 T23: -0.0916
REMARK 3 L TENSOR
REMARK 3 L11: 5.6870 L22: 5.7287
REMARK 3 L33: 0.7240 L12: 0.5316
REMARK 3 L13: 0.9633 L23: -0.9292
REMARK 3 S TENSOR
REMARK 3 S11: -0.0788 S12: -0.0569 S13: -0.1773
REMARK 3 S21: 0.1166 S22: 0.1417 S23: -0.9823
REMARK 3 S31: 0.0773 S32: 0.4161 S33: -0.0629
REMARK 3
REMARK 3 TLS GROUP : 12
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 709 B 743
REMARK 3 ORIGIN FOR THE GROUP (A): -24.9725 -2.3437 -51.5397
REMARK 3 T TENSOR
REMARK 3 T11: 0.6739 T22: 0.9724
REMARK 3 T33: 0.1443 T12: 0.1368
REMARK 3 T13: 0.3036 T23: -0.1157
REMARK 3 L TENSOR
REMARK 3 L11: 23.7923 L22: 18.3518
REMARK 3 L33: 6.5858 L12: -13.5413
REMARK 3 L13: 9.9332 L23: -8.7219
REMARK 3 S TENSOR
REMARK 3 S11: 0.2899 S12: 2.4456 S13: -0.0217
REMARK 3 S21: -1.2721 S22: -0.7307 S23: -0.4307
REMARK 3 S31: 0.5596 S32: 0.2194 S33: 0.4408
REMARK 3
REMARK 3 TLS GROUP : 13
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 744 B 780
REMARK 3 ORIGIN FOR THE GROUP (A): -37.2648 6.5815 -35.0756
REMARK 3 T TENSOR
REMARK 3 T11: 0.5972 T22: 0.6954
REMARK 3 T33: 0.4558 T12: 0.0029
REMARK 3 T13: -0.0762 T23: -0.0143
REMARK 3 L TENSOR
REMARK 3 L11: 2.4520 L22: 2.3262
REMARK 3 L33: 2.9853 L12: -0.4524
REMARK 3 L13: -0.4694 L23: 0.8996
REMARK 3 S TENSOR
REMARK 3 S11: -0.2202 S12: 0.1802 S13: 0.0473
REMARK 3 S21: -0.2206 S22: -0.1664 S23: 0.4996
REMARK 3 S31: -0.3310 S32: -0.0834 S33: 0.3867
REMARK 3
REMARK 3 TLS GROUP : 14
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 781 B 852
REMARK 3 ORIGIN FOR THE GROUP (A): -41.3794 24.5318 -29.0750
REMARK 3 T TENSOR
REMARK 3 T11: 0.6545 T22: 0.5413
REMARK 3 T33: 0.6137 T12: -0.0962
REMARK 3 T13: -0.0409 T23: -0.0573
REMARK 3 L TENSOR
REMARK 3 L11: 3.4658 L22: 4.8516
REMARK 3 L33: 4.5955 L12: -2.5609
REMARK 3 L13: -0.9892 L23: 0.6795
REMARK 3 S TENSOR
REMARK 3 S11: -0.1375 S12: 0.1113 S13: 0.3790
REMARK 3 S21: -0.0315 S22: 0.4001 S23: 0.2617
REMARK 3 S31: 0.2049 S32: -0.1254 S33: -0.2626
REMARK 3
REMARK 3 TLS GROUP : 15
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 545 D 573
REMARK 3 ORIGIN FOR THE GROUP (A): -38.2017 -3.1318 -1.7965
REMARK 3 T TENSOR
REMARK 3 T11: 0.4548 T22: 0.2982
REMARK 3 T33: 0.0206 T12: -0.1228
REMARK 3 T13: -0.0358 T23: 0.0481
REMARK 3 L TENSOR
REMARK 3 L11: 34.9651 L22: 5.9388
REMARK 3 L33: 1.0181 L12: -2.5568
REMARK 3 L13: 3.1620 L23: 2.3117
REMARK 3 S TENSOR
REMARK 3 S11: 0.7780 S12: -0.0304 S13: 0.9447
REMARK 3 S21: -0.8053 S22: -0.8724 S23: -0.1529
REMARK 3 S31: -0.3175 S32: -0.2949 S33: 0.0944
REMARK 3
REMARK 3 TLS GROUP : 16
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 574 D 628
REMARK 3 ORIGIN FOR THE GROUP (A): -43.2464 -14.6548 -5.7228
REMARK 3 T TENSOR
REMARK 3 T11: 0.4281 T22: 0.4388
REMARK 3 T33: 0.1783 T12: 0.0228
REMARK 3 T13: -0.0539 T23: -0.0065
REMARK 3 L TENSOR
REMARK 3 L11: 2.8824 L22: 2.5213
REMARK 3 L33: 1.9315 L12: -0.0001
REMARK 3 L13: -0.8024 L23: 0.6547
REMARK 3 S TENSOR
REMARK 3 S11: -0.0028 S12: 0.1611 S13: -0.5465
REMARK 3 S21: -0.3085 S22: -0.0385 S23: 0.1445
REMARK 3 S31: 0.2366 S32: -0.2975 S33: 0.0412
REMARK 3
REMARK 3 TLS GROUP : 17
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 629 D 651
REMARK 3 ORIGIN FOR THE GROUP (A): -52.1687 -33.9190 -17.2652
REMARK 3 T TENSOR
REMARK 3 T11: 1.3189 T22: 1.1511
REMARK 3 T33: 1.3305 T12: -0.2578
REMARK 3 T13: 0.0650 T23: -0.2015
REMARK 3 L TENSOR
REMARK 3 L11: 1.0050 L22: 4.1442
REMARK 3 L33: -0.0364 L12: -2.7216
REMARK 3 L13: 1.6544 L23: -1.8016
REMARK 3 S TENSOR
REMARK 3 S11: 0.4174 S12: 0.5634 S13: -0.4214
REMARK 3 S21: -0.9557 S22: -0.4280 S23: 0.3093
REMARK 3 S31: 0.3572 S32: 0.2160 S33: 0.0106
REMARK 3
REMARK 3 TLS GROUP : 18
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 652 D 708
REMARK 3 ORIGIN FOR THE GROUP (A): -43.3478 -25.4147 -9.7066
REMARK 3 T TENSOR
REMARK 3 T11: 0.5731 T22: 0.4221
REMARK 3 T33: 0.2991 T12: -0.0607
REMARK 3 T13: -0.0939 T23: -0.0204
REMARK 3 L TENSOR
REMARK 3 L11: 3.0627 L22: 5.2135
REMARK 3 L33: 3.1695 L12: -3.1135
REMARK 3 L13: -0.6817 L23: 3.1972
REMARK 3 S TENSOR
REMARK 3 S11: 0.2615 S12: 0.0994 S13: -0.9589
REMARK 3 S21: -0.1153 S22: -0.2911 S23: 0.7866
REMARK 3 S31: 0.3484 S32: -0.3977 S33: 0.0295
REMARK 3
REMARK 3 TLS GROUP : 19
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 709 D 743
REMARK 3 ORIGIN FOR THE GROUP (A): -49.4831 -16.7788 13.2936
REMARK 3 T TENSOR
REMARK 3 T11: 0.4295 T22: 0.6998
REMARK 3 T33: 0.5950 T12: 0.2640
REMARK 3 T13: -0.1042 T23: 0.2408
REMARK 3 L TENSOR
REMARK 3 L11: 10.3035 L22: 25.3438
REMARK 3 L33: 17.7046 L12: -2.2356
REMARK 3 L13: 4.9880 L23: 17.3934
REMARK 3 S TENSOR
REMARK 3 S11: -1.8868 S12: -1.8958 S13: -0.2814
REMARK 3 S21: 1.0951 S22: 2.1743 S23: -1.4618
REMARK 3 S31: -0.5134 S32: 0.7941 S33: -0.2875
REMARK 3
REMARK 3 TLS GROUP : 20
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 744 D 763
REMARK 3 ORIGIN FOR THE GROUP (A): -48.1383 -9.8032 4.9597
REMARK 3 T TENSOR
REMARK 3 T11: 0.3922 T22: 0.4858
REMARK 3 T33: 0.1003 T12: -0.1223
REMARK 3 T13: 0.1308 T23: 0.0355
REMARK 3 L TENSOR
REMARK 3 L11: 9.4105 L22: 12.4714
REMARK 3 L33: 4.7510 L12: -6.3314
REMARK 3 L13: 4.4395 L23: -1.9665
REMARK 3 S TENSOR
REMARK 3 S11: -0.3254 S12: -1.1149 S13: -0.1253
REMARK 3 S21: 0.2734 S22: 0.3133 S23: 0.2993
REMARK 3 S31: 0.0410 S32: -0.2731 S33: 0.0121
REMARK 3
REMARK 3 TLS GROUP : 21
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 764 D 852
REMARK 3 ORIGIN FOR THE GROUP (A): -63.9043 9.9587 -9.9890
REMARK 3 T TENSOR
REMARK 3 T11: 0.4211 T22: 0.4866
REMARK 3 T33: 0.3816 T12: -0.0237
REMARK 3 T13: -0.0309 T23: -0.0719
REMARK 3 L TENSOR
REMARK 3 L11: 3.1978 L22: 3.5899
REMARK 3 L33: 4.8366 L12: -2.5766
REMARK 3 L13: 1.2123 L23: -2.5563
REMARK 3 S TENSOR
REMARK 3 S11: 0.0174 S12: 0.0076 S13: 0.2812
REMARK 3 S21: -0.1147 S22: -0.1510 S23: -0.3097
REMARK 3 S31: -0.2328 S32: -0.1105 S33: 0.1336
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : NULL
REMARK 3 ION PROBE RADIUS : NULL
REMARK 3 SHRINKAGE RADIUS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE
REMARK 4
REMARK 4 4FD2 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 DEPOSITION ID IS D_1000072748.
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 : 5.0
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 : 24567
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.000
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
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 (%): 58.99
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.00
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: CITRIC ACID, ISOPROPANOL, PH 5.0,
REMARK 280 HANGING DROP, TEMPERATURE 294K
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 86.26733
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 43.13367
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 64.70050
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 21.56683
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 107.83417
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: D
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 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 ARG A 578 177.75 -58.35
REMARK 500 ALA A 579 -26.42 65.16
REMARK 500 ASN A 585 32.74 -85.23
REMARK 500 THR A 615 143.88 -174.54
REMARK 500 ALA A 618 28.93 -75.58
REMARK 500 ALA A 632 -74.19 -72.02
REMARK 500 VAL A 633 -58.32 -23.41
REMARK 500 ALA A 639 56.40 -101.03
REMARK 500 PRO A 640 -129.95 -95.26
REMARK 500 TYR A 643 93.83 -55.50
REMARK 500 VAL A 644 -145.11 48.45
REMARK 500 ASP A 685 -73.03 -75.53
REMARK 500 LYS A 721 -62.65 7.20
REMARK 500 PRO A 724 -125.13 -96.45
REMARK 500 TYR A 725 -80.61 -55.44
REMARK 500 GLU A 726 -160.94 -79.79
REMARK 500 ARG A 727 -25.34 81.74
REMARK 500 LYS A 759 -18.72 -37.10
REMARK 500 ARG A 851 -93.48 -20.30
REMARK 500 ARG B 578 178.23 -59.58
REMARK 500 ALA B 579 -27.67 64.48
REMARK 500 ASN B 585 39.62 -90.22
REMARK 500 ALA B 618 34.95 -76.36
REMARK 500 ALA B 632 -77.97 -70.71
REMARK 500 VAL B 633 -54.34 -21.68
REMARK 500 PRO B 640 -130.78 -52.48
REMARK 500 PRO B 641 -134.72 -76.46
REMARK 500 VAL B 644 -144.85 54.43
REMARK 500 ASP B 685 -73.42 -75.21
REMARK 500 ASP B 691 -165.12 -74.61
REMARK 500 LYS B 721 -56.48 -7.19
REMARK 500 PRO B 724 -127.39 -92.27
REMARK 500 LYS B 759 -12.23 -42.37
REMARK 500 LEU B 786 -167.31 -76.41
REMARK 500 LEU B 816 -65.11 -106.78
REMARK 500 PRO B 849 47.38 -88.00
REMARK 500 ALA B 850 -129.47 48.95
REMARK 500 ARG B 851 -77.10 -140.88
REMARK 500 ARG D 578 172.45 -59.13
REMARK 500 ALA D 579 -27.56 70.98
REMARK 500 ASN D 585 32.21 -86.15
REMARK 500 PRO D 587 152.99 -47.55
REMARK 500 THR D 615 140.78 -175.03
REMARK 500 ALA D 618 28.84 -75.39
REMARK 500 ALA D 632 -77.58 -72.02
REMARK 500 VAL D 633 -54.61 -21.28
REMARK 500 ALA D 639 57.09 -98.79
REMARK 500 PRO D 640 -135.06 -92.61
REMARK 500 VAL D 644 -146.47 51.47
REMARK 500 ASP D 685 -70.08 -81.49
REMARK 500
REMARK 500 THIS ENTRY HAS 55 RAMACHANDRAN OUTLIERS.
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 D 901
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4FCT RELATED DB: PDB
REMARK 900 RELATED ID: 4FCV RELATED DB: PDB
REMARK 900 RELATED ID: 4FCW RELATED DB: PDB
DBREF 4FD2 A 545 852 UNP Q9RA63 CLPB_THET8 545 852
DBREF 4FD2 B 545 852 UNP Q9RA63 CLPB_THET8 545 852
DBREF 4FD2 D 545 852 UNP Q9RA63 CLPB_THET8 545 852
SEQADV 4FD2 ALA A 668 UNP Q9RA63 GLU 668 ENGINEERED MUTATION
SEQADV 4FD2 ALA B 668 UNP Q9RA63 GLU 668 ENGINEERED MUTATION
SEQADV 4FD2 ALA D 668 UNP Q9RA63 GLU 668 ENGINEERED MUTATION
SEQRES 1 A 308 GLU ARG GLU LYS LEU LEU ARG LEU GLU GLU GLU LEU HIS
SEQRES 2 A 308 LYS ARG VAL VAL GLY GLN ASP GLU ALA ILE ARG ALA VAL
SEQRES 3 A 308 ALA ASP ALA ILE ARG ARG ALA ARG ALA GLY LEU LYS ASP
SEQRES 4 A 308 PRO ASN ARG PRO ILE GLY SER PHE LEU PHE LEU GLY PRO
SEQRES 5 A 308 THR GLY VAL GLY LYS THR GLU LEU ALA LYS THR LEU ALA
SEQRES 6 A 308 ALA THR LEU PHE ASP THR GLU GLU ALA MET ILE ARG ILE
SEQRES 7 A 308 ASP MET THR GLU TYR MET GLU LYS HIS ALA VAL SER ARG
SEQRES 8 A 308 LEU ILE GLY ALA PRO PRO GLY TYR VAL GLY TYR GLU GLU
SEQRES 9 A 308 GLY GLY GLN LEU THR GLU ALA VAL ARG ARG ARG PRO TYR
SEQRES 10 A 308 SER VAL ILE LEU PHE ASP ALA ILE GLU LYS ALA HIS PRO
SEQRES 11 A 308 ASP VAL PHE ASN ILE LEU LEU GLN ILE LEU ASP ASP GLY
SEQRES 12 A 308 ARG LEU THR ASP SER HIS GLY ARG THR VAL ASP PHE ARG
SEQRES 13 A 308 ASN THR VAL ILE ILE LEU THR SER ASN LEU GLY SER PRO
SEQRES 14 A 308 LEU ILE LEU GLU GLY LEU GLN LYS GLY TRP PRO TYR GLU
SEQRES 15 A 308 ARG ILE ARG ASP GLU VAL PHE LYS VAL LEU GLN GLN HIS
SEQRES 16 A 308 PHE ARG PRO GLU PHE LEU ASN ARG LEU ASP GLU ILE VAL
SEQRES 17 A 308 VAL PHE ARG PRO LEU THR LYS GLU GLN ILE ARG GLN ILE
SEQRES 18 A 308 VAL GLU ILE GLN LEU SER TYR LEU ARG ALA ARG LEU ALA
SEQRES 19 A 308 GLU LYS ARG ILE SER LEU GLU LEU THR GLU ALA ALA LYS
SEQRES 20 A 308 ASP PHE LEU ALA GLU ARG GLY TYR ASP PRO VAL PHE GLY
SEQRES 21 A 308 ALA ARG PRO LEU ARG ARG VAL ILE GLN ARG GLU LEU GLU
SEQRES 22 A 308 THR PRO LEU ALA GLN LYS ILE LEU ALA GLY GLU VAL LYS
SEQRES 23 A 308 GLU GLY ASP ARG VAL GLN VAL ASP VAL GLY PRO ALA GLY
SEQRES 24 A 308 LEU VAL PHE ALA VAL PRO ALA ARG VAL
SEQRES 1 B 308 GLU ARG GLU LYS LEU LEU ARG LEU GLU GLU GLU LEU HIS
SEQRES 2 B 308 LYS ARG VAL VAL GLY GLN ASP GLU ALA ILE ARG ALA VAL
SEQRES 3 B 308 ALA ASP ALA ILE ARG ARG ALA ARG ALA GLY LEU LYS ASP
SEQRES 4 B 308 PRO ASN ARG PRO ILE GLY SER PHE LEU PHE LEU GLY PRO
SEQRES 5 B 308 THR GLY VAL GLY LYS THR GLU LEU ALA LYS THR LEU ALA
SEQRES 6 B 308 ALA THR LEU PHE ASP THR GLU GLU ALA MET ILE ARG ILE
SEQRES 7 B 308 ASP MET THR GLU TYR MET GLU LYS HIS ALA VAL SER ARG
SEQRES 8 B 308 LEU ILE GLY ALA PRO PRO GLY TYR VAL GLY TYR GLU GLU
SEQRES 9 B 308 GLY GLY GLN LEU THR GLU ALA VAL ARG ARG ARG PRO TYR
SEQRES 10 B 308 SER VAL ILE LEU PHE ASP ALA ILE GLU LYS ALA HIS PRO
SEQRES 11 B 308 ASP VAL PHE ASN ILE LEU LEU GLN ILE LEU ASP ASP GLY
SEQRES 12 B 308 ARG LEU THR ASP SER HIS GLY ARG THR VAL ASP PHE ARG
SEQRES 13 B 308 ASN THR VAL ILE ILE LEU THR SER ASN LEU GLY SER PRO
SEQRES 14 B 308 LEU ILE LEU GLU GLY LEU GLN LYS GLY TRP PRO TYR GLU
SEQRES 15 B 308 ARG ILE ARG ASP GLU VAL PHE LYS VAL LEU GLN GLN HIS
SEQRES 16 B 308 PHE ARG PRO GLU PHE LEU ASN ARG LEU ASP GLU ILE VAL
SEQRES 17 B 308 VAL PHE ARG PRO LEU THR LYS GLU GLN ILE ARG GLN ILE
SEQRES 18 B 308 VAL GLU ILE GLN LEU SER TYR LEU ARG ALA ARG LEU ALA
SEQRES 19 B 308 GLU LYS ARG ILE SER LEU GLU LEU THR GLU ALA ALA LYS
SEQRES 20 B 308 ASP PHE LEU ALA GLU ARG GLY TYR ASP PRO VAL PHE GLY
SEQRES 21 B 308 ALA ARG PRO LEU ARG ARG VAL ILE GLN ARG GLU LEU GLU
SEQRES 22 B 308 THR PRO LEU ALA GLN LYS ILE LEU ALA GLY GLU VAL LYS
SEQRES 23 B 308 GLU GLY ASP ARG VAL GLN VAL ASP VAL GLY PRO ALA GLY
SEQRES 24 B 308 LEU VAL PHE ALA VAL PRO ALA ARG VAL
SEQRES 1 D 308 GLU ARG GLU LYS LEU LEU ARG LEU GLU GLU GLU LEU HIS
SEQRES 2 D 308 LYS ARG VAL VAL GLY GLN ASP GLU ALA ILE ARG ALA VAL
SEQRES 3 D 308 ALA ASP ALA ILE ARG ARG ALA ARG ALA GLY LEU LYS ASP
SEQRES 4 D 308 PRO ASN ARG PRO ILE GLY SER PHE LEU PHE LEU GLY PRO
SEQRES 5 D 308 THR GLY VAL GLY LYS THR GLU LEU ALA LYS THR LEU ALA
SEQRES 6 D 308 ALA THR LEU PHE ASP THR GLU GLU ALA MET ILE ARG ILE
SEQRES 7 D 308 ASP MET THR GLU TYR MET GLU LYS HIS ALA VAL SER ARG
SEQRES 8 D 308 LEU ILE GLY ALA PRO PRO GLY TYR VAL GLY TYR GLU GLU
SEQRES 9 D 308 GLY GLY GLN LEU THR GLU ALA VAL ARG ARG ARG PRO TYR
SEQRES 10 D 308 SER VAL ILE LEU PHE ASP ALA ILE GLU LYS ALA HIS PRO
SEQRES 11 D 308 ASP VAL PHE ASN ILE LEU LEU GLN ILE LEU ASP ASP GLY
SEQRES 12 D 308 ARG LEU THR ASP SER HIS GLY ARG THR VAL ASP PHE ARG
SEQRES 13 D 308 ASN THR VAL ILE ILE LEU THR SER ASN LEU GLY SER PRO
SEQRES 14 D 308 LEU ILE LEU GLU GLY LEU GLN LYS GLY TRP PRO TYR GLU
SEQRES 15 D 308 ARG ILE ARG ASP GLU VAL PHE LYS VAL LEU GLN GLN HIS
SEQRES 16 D 308 PHE ARG PRO GLU PHE LEU ASN ARG LEU ASP GLU ILE VAL
SEQRES 17 D 308 VAL PHE ARG PRO LEU THR LYS GLU GLN ILE ARG GLN ILE
SEQRES 18 D 308 VAL GLU ILE GLN LEU SER TYR LEU ARG ALA ARG LEU ALA
SEQRES 19 D 308 GLU LYS ARG ILE SER LEU GLU LEU THR GLU ALA ALA LYS
SEQRES 20 D 308 ASP PHE LEU ALA GLU ARG GLY TYR ASP PRO VAL PHE GLY
SEQRES 21 D 308 ALA ARG PRO LEU ARG ARG VAL ILE GLN ARG GLU LEU GLU
SEQRES 22 D 308 THR PRO LEU ALA GLN LYS ILE LEU ALA GLY GLU VAL LYS
SEQRES 23 D 308 GLU GLY ASP ARG VAL GLN VAL ASP VAL GLY PRO ALA GLY
SEQRES 24 D 308 LEU VAL PHE ALA VAL PRO ALA ARG VAL
HET ADP A 901 27
HET ADP B 901 27
HET ADP D 901 27
HETNAM ADP ADENOSINE-5'-DIPHOSPHATE
FORMUL 4 ADP 3(C10 H15 N5 O10 P2)
HELIX 1 1 GLU A 545 ARG A 551 1 7
HELIX 2 2 ARG A 551 LYS A 558 1 8
HELIX 3 3 GLN A 563 ARG A 578 1 16
HELIX 4 4 GLY A 600 ASP A 614 1 15
HELIX 5 5 GLU A 629 ILE A 637 1 9
HELIX 6 6 GLY A 650 ARG A 659 1 10
HELIX 7 7 ALA A 668 ALA A 672 5 5
HELIX 8 8 HIS A 673 ASP A 686 1 14
HELIX 9 9 GLY A 711 PRO A 713 5 3
HELIX 10 10 LEU A 714 GLN A 720 1 7
HELIX 11 11 ARG A 727 GLN A 737 1 11
HELIX 12 12 ARG A 741 ASN A 746 1 6
HELIX 13 13 THR A 758 GLU A 779 1 22
HELIX 14 14 THR A 787 TYR A 799 1 13
HELIX 15 15 PRO A 807 LEU A 816 1 10
HELIX 16 16 LEU A 816 ALA A 826 1 11
HELIX 17 17 ARG B 546 ARG B 551 1 6
HELIX 18 18 ARG B 551 LYS B 558 1 8
HELIX 19 19 GLN B 563 ARG B 578 1 16
HELIX 20 20 ALA B 579 LEU B 581 5 3
HELIX 21 21 GLY B 600 ASP B 614 1 15
HELIX 22 22 THR B 625 TYR B 627 5 3
HELIX 23 23 ALA B 632 ILE B 637 1 6
HELIX 24 24 GLY B 650 ARG B 659 1 10
HELIX 25 25 ALA B 668 ALA B 672 5 5
HELIX 26 26 HIS B 673 ASP B 686 1 14
HELIX 27 27 GLY B 711 PRO B 713 5 3
HELIX 28 28 LEU B 714 LEU B 719 1 6
HELIX 29 29 GLU B 726 GLN B 737 1 12
HELIX 30 30 ARG B 741 ASN B 746 1 6
HELIX 31 31 GLU B 760 GLU B 779 1 20
HELIX 32 32 THR B 787 TYR B 799 1 13
HELIX 33 33 PRO B 807 LEU B 816 1 10
HELIX 34 34 LEU B 816 ALA B 826 1 11
HELIX 35 35 ARG D 546 ARG D 551 1 6
HELIX 36 36 ARG D 551 LYS D 558 1 8
HELIX 37 37 GLN D 563 ARG D 578 1 16
HELIX 38 38 GLY D 600 ASP D 614 1 15
HELIX 39 39 THR D 625 TYR D 627 5 3
HELIX 40 40 GLU D 629 ILE D 637 1 9
HELIX 41 41 GLY D 650 ARG D 659 1 10
HELIX 42 42 ALA D 668 ALA D 672 5 5
HELIX 43 43 HIS D 673 ASP D 686 1 14
HELIX 44 44 GLY D 711 ILE D 715 5 5
HELIX 45 45 GLU D 726 GLN D 737 1 12
HELIX 46 46 ARG D 741 ASN D 746 1 6
HELIX 47 47 GLU D 760 GLN D 769 1 10
HELIX 48 48 LEU D 770 GLU D 779 1 10
HELIX 49 49 THR D 787 TYR D 799 1 13
HELIX 50 50 PRO D 807 LEU D 816 1 10
HELIX 51 51 LEU D 816 ALA D 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 622
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 GLY A 589 O ILE A 704
SHEET 5 A 5 GLU A 750 VAL A 753 1 O GLU A 750 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 GLU A 785 0
SHEET 2 C 3 ARG A 834 ASP A 838 1 O VAL A 835 N GLU A 785
SHEET 3 C 3 VAL A 845 ALA A 847 -1 O VAL A 845 N ASP A 838
SHEET 1 D 5 MET B 619 ASP B 623 0
SHEET 2 D 5 VAL B 663 ASP B 667 1 O LEU B 665 N ILE B 620
SHEET 3 D 5 VAL B 703 THR B 707 1 O VAL B 703 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 GLU B 750 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 GLU B 785 0
SHEET 2 F 3 ARG B 834 ASP B 838 1 O VAL B 835 N GLU B 785
SHEET 3 F 3 VAL B 845 ALA B 847 -1 O VAL B 845 N ASP B 838
SHEET 1 G 5 MET D 619 ASP D 623 0
SHEET 2 G 5 VAL D 663 ASP D 667 1 O LEU D 665 N ILE D 620
SHEET 3 G 5 VAL D 703 THR D 707 1 O VAL D 703 N ILE D 664
SHEET 4 G 5 GLY D 589 LEU D 594 1 N GLY D 589 O ILE D 704
SHEET 5 G 5 GLU D 750 VAL D 753 1 O VAL D 752 N LEU D 592
SHEET 1 H 2 ARG D 688 THR D 690 0
SHEET 2 H 2 THR D 696 ASP D 698 -1 O VAL D 697 N LEU D 689
SHEET 1 I 3 SER D 783 GLU D 785 0
SHEET 2 I 3 ARG D 834 ASP D 838 1 O VAL D 835 N GLU D 785
SHEET 3 I 3 VAL D 845 ALA D 847 -1 O VAL D 845 N ASP D 838
CISPEP 1 PRO A 640 PRO A 641 0 -2.27
CISPEP 2 PRO B 640 PRO B 641 0 2.37
CISPEP 3 PRO D 640 PRO D 641 0 -1.28
SITE 1 AC1 13 ARG A 559 VAL A 560 VAL A 561 THR A 597
SITE 2 AC1 13 GLY A 598 VAL A 599 GLY A 600 LYS A 601
SITE 3 AC1 13 THR A 602 GLU A 603 GLN A 769 ALA A 805
SITE 4 AC1 13 ARG A 806
SITE 1 AC2 12 ARG B 559 VAL B 561 THR B 597 GLY B 598
SITE 2 AC2 12 VAL B 599 GLY B 600 LYS B 601 THR B 602
SITE 3 AC2 12 GLU B 603 ILE B 765 GLN B 769 ALA B 805
SITE 1 AC3 12 ARG D 559 VAL D 560 VAL D 561 THR D 597
SITE 2 AC3 12 GLY D 598 VAL D 599 GLY D 600 THR D 602
SITE 3 AC3 12 GLU D 603 ILE D 765 GLN D 769 ARG D 806
CRYST1 129.775 129.775 129.401 90.00 90.00 120.00 P 65 18
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 0.007706 0.004449 0.000000 0.00000
SCALE2 0.000000 0.008898 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007728 0.00000
(ATOM LINES ARE NOT SHOWN.)
END