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HEADER HYDROLASE 30-APR-24 9BLE
TITLE CRYSTAL STRUCTURE OF THERMOSTABLE DIENELACTONE HYDROLASE. MONOCLINIC
TITLE 2 SPACE GROUP.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CARBOXYMETHYLENEBUTENOLIDASE;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HYDROGENOBACTER THERMOPHILUS;
SOURCE 3 ORGANISM_TAXID: 940;
SOURCE 4 GENE: HTH_1817;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS DIENELACTONE HYDROLASE, ESTERASE ACTIVITY, PETASE, BHETASE,
KEYWDS 2 THERMOSTABLE ENZYME, PET DEPOLYMERIZATION, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.R.C.MUNIZ,D.ALMEIDA,V.BRITO,I.CIANCAGLINI,A.L.H.SANDANO,F.SQUINA,
AUTHOR 2 W.GARCIA
REVDAT 1 14-MAY-25 9BLE 0
JRNL AUTH J.R.C.MUNIZ,D.ALMEIDA,V.BRITO,I.CIANCAGLINI,A.L.H.SANDANO,
JRNL AUTH 2 F.SQUINA,W.GARCIA
JRNL TITL CRYSTAL STRUCTURE OF THERMOSTABLE DIENELACTONE HYDROLASE
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.79 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0425
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.79
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 74.40
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 91.1
REMARK 3 NUMBER OF REFLECTIONS : 84616
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : FREE R-VALUE
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING + TEST SET) : NULL
REMARK 3 R VALUE (WORKING SET) : 0.161
REMARK 3 FREE R VALUE : 0.190
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.964
REMARK 3 FREE R VALUE TEST SET COUNT : 4200
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) : 1.79
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.84
REMARK 3 REFLECTION IN BIN (WORKING SET) : 6476
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.97
REMARK 3 BIN R VALUE (WORKING SET) : 0.2770
REMARK 3 BIN FREE R VALUE SET COUNT : 317
REMARK 3 BIN FREE R VALUE : 0.2880
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 7435
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 642
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 26.08
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 2.26800
REMARK 3 B22 (A**2) : -1.91800
REMARK 3 B33 (A**2) : -0.35000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.03700
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.125
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.114
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.084
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.490
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.968
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.953
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 7729 ; 0.008 ; 0.012
REMARK 3 BOND LENGTHS OTHERS (A): 7083 ; 0.001 ; 0.016
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 10483 ; 1.556 ; 1.826
REMARK 3 BOND ANGLES OTHERS (DEGREES): 16351 ; 0.547 ; 1.753
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 966 ; 5.782 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 36 ; 6.122 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1235 ;12.126 ;10.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1092 ; 0.079 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 9149 ; 0.007 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 1845 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1313 ; 0.212 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 122 ; 0.244 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 3874 ; 0.184 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 520 ; 0.162 ; 0.200
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): 3786 ; 1.570 ; 1.586
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 3786 ; 1.570 ; 1.585
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 4733 ; 2.381 ; 2.842
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 4734 ; 2.381 ; 2.842
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 3943 ; 2.799 ; 1.945
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 3944 ; 2.799 ; 1.945
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 5735 ; 4.348 ; 3.407
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 5736 ; 4.348 ; 3.407
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 : 6
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : A
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 2 A 233 NULL
REMARK 3 1 A 2 A 233 NULL
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3
REMARK 3 NCS GROUP NUMBER : 2
REMARK 3 CHAIN NAMES : A
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 2
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 2 A 2 A 233 NULL
REMARK 3 2 A 2 A 233 NULL
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3
REMARK 3 NCS GROUP NUMBER : 3
REMARK 3 CHAIN NAMES : A
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 3
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 3 A 2 A 233 NULL
REMARK 3 3 A 2 A 233 NULL
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3
REMARK 3 NCS GROUP NUMBER : 4
REMARK 3 CHAIN NAMES : A
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 4
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 4 A 2 A 233 NULL
REMARK 3 4 A 2 A 233 NULL
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3
REMARK 3 NCS GROUP NUMBER : 5
REMARK 3 CHAIN NAMES : A
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 5
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 5 A 2 A 234 NULL
REMARK 3 5 A 2 A 234 NULL
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3
REMARK 3 NCS GROUP NUMBER : 6
REMARK 3 CHAIN NAMES : A
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 6
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 6 A 2 A 233 NULL
REMARK 3 6 A 2 A 233 NULL
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 16
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 2 A 69
REMARK 3 ORIGIN FOR THE GROUP (A): -16.7901 32.1169 -41.4019
REMARK 3 T TENSOR
REMARK 3 T11: 0.1262 T22: 0.0739
REMARK 3 T33: 0.0893 T12: 0.0090
REMARK 3 T13: -0.0095 T23: 0.0184
REMARK 3 L TENSOR
REMARK 3 L11: 0.6291 L22: 1.8737
REMARK 3 L33: 1.2364 L12: 0.4074
REMARK 3 L13: 0.4099 L23: 0.0391
REMARK 3 S TENSOR
REMARK 3 S11: -0.0076 S12: -0.0791 S13: -0.0428
REMARK 3 S21: 0.0921 S22: -0.0156 S23: -0.1912
REMARK 3 S31: 0.0905 S32: -0.0124 S33: 0.0232
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 70 A 103
REMARK 3 ORIGIN FOR THE GROUP (A): -22.7457 27.8313 -50.2867
REMARK 3 T TENSOR
REMARK 3 T11: 0.1138 T22: 0.0146
REMARK 3 T33: 0.1701 T12: 0.0008
REMARK 3 T13: 0.0035 T23: -0.0079
REMARK 3 L TENSOR
REMARK 3 L11: 0.8037 L22: 2.1696
REMARK 3 L33: 1.4462 L12: 1.0382
REMARK 3 L13: -0.9242 L23: -1.1220
REMARK 3 S TENSOR
REMARK 3 S11: -0.0645 S12: 0.1028 S13: -0.1300
REMARK 3 S21: -0.1078 S22: 0.1208 S23: -0.0345
REMARK 3 S31: 0.1172 S32: -0.1318 S33: -0.0563
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 104 A 158
REMARK 3 ORIGIN FOR THE GROUP (A): -27.9136 39.5660 -47.6044
REMARK 3 T TENSOR
REMARK 3 T11: 0.1128 T22: 0.0995
REMARK 3 T33: 0.0826 T12: 0.0342
REMARK 3 T13: 0.0148 T23: -0.0165
REMARK 3 L TENSOR
REMARK 3 L11: 0.0528 L22: 1.2941
REMARK 3 L33: 0.8068 L12: 0.2478
REMARK 3 L13: 0.0694 L23: 0.1866
REMARK 3 S TENSOR
REMARK 3 S11: -0.0428 S12: -0.0263 S13: 0.0093
REMARK 3 S21: -0.1203 S22: -0.0508 S23: 0.0640
REMARK 3 S31: -0.0365 S32: -0.0614 S33: 0.0936
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 159 A 234
REMARK 3 ORIGIN FOR THE GROUP (A): -19.1356 49.4313 -50.8644
REMARK 3 T TENSOR
REMARK 3 T11: 0.1626 T22: 0.0606
REMARK 3 T33: 0.0594 T12: -0.0227
REMARK 3 T13: -0.0091 T23: -0.0227
REMARK 3 L TENSOR
REMARK 3 L11: 0.3552 L22: 1.2363
REMARK 3 L33: 0.2363 L12: 0.4242
REMARK 3 L13: 0.0898 L23: 0.1641
REMARK 3 S TENSOR
REMARK 3 S11: -0.0586 S12: -0.0942 S13: 0.0355
REMARK 3 S21: -0.1639 S22: 0.0354 S23: 0.0031
REMARK 3 S31: -0.1916 S32: 0.0172 S33: 0.0232
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 NUMBER OF COMPONENTS GROUP : 0
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 ORIGIN FOR THE GROUP (A): -0.5654 16.7251 3.7276
REMARK 3 T TENSOR
REMARK 3 T11: 0.0875 T22: 0.0822
REMARK 3 T33: 0.1046 T12: -0.0051
REMARK 3 T13: -0.0085 T23: 0.0336
REMARK 3 L TENSOR
REMARK 3 L11: 2.6318 L22: 7.0392
REMARK 3 L33: 4.2725 L12: -2.5157
REMARK 3 L13: -2.7024 L23: 4.1643
REMARK 3 S TENSOR
REMARK 3 S11: 0.0483 S12: 0.1237 S13: 0.0437
REMARK 3 S21: -0.1909 S22: -0.0760 S23: -0.0129
REMARK 3 S31: -0.1447 S32: -0.2157 S33: 0.0277
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 NUMBER OF COMPONENTS GROUP : 0
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 ORIGIN FOR THE GROUP (A): -7.1174 4.2033 -7.3264
REMARK 3 T TENSOR
REMARK 3 T11: 0.1389 T22: 0.2259
REMARK 3 T33: 0.4668 T12: -0.0300
REMARK 3 T13: -0.1531 T23: 0.0672
REMARK 3 L TENSOR
REMARK 3 L11: 9.0639 L22: 0.8785
REMARK 3 L33: 18.8369 L12: 1.1276
REMARK 3 L13: -10.9017 L23: 0.6992
REMARK 3 S TENSOR
REMARK 3 S11: -0.5033 S12: 1.1005 S13: -0.1586
REMARK 3 S21: -0.2994 S22: -0.0544 S23: 0.1008
REMARK 3 S31: -0.0473 S32: -1.8755 S33: 0.5577
REMARK 3
REMARK 3 TLS GROUP : 7
REMARK 3 NUMBER OF COMPONENTS GROUP : 0
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 ORIGIN FOR THE GROUP (A): 5.3087 9.4410 8.5626
REMARK 3 T TENSOR
REMARK 3 T11: 0.0685 T22: 0.0649
REMARK 3 T33: 0.1254 T12: -0.0416
REMARK 3 T13: 0.0204 T23: 0.0023
REMARK 3 L TENSOR
REMARK 3 L11: 0.1983 L22: 1.4413
REMARK 3 L33: 0.4696 L12: 0.0058
REMARK 3 L13: 0.1802 L23: -0.0614
REMARK 3 S TENSOR
REMARK 3 S11: -0.0346 S12: 0.0511 S13: 0.0407
REMARK 3 S21: 0.0266 S22: 0.0573 S23: -0.0773
REMARK 3 S31: -0.0706 S32: 0.0305 S33: -0.0227
REMARK 3
REMARK 3 TLS GROUP : 8
REMARK 3 NUMBER OF COMPONENTS GROUP : 0
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 ORIGIN FOR THE GROUP (A): 3.4988 -4.5463 12.6166
REMARK 3 T TENSOR
REMARK 3 T11: 0.0522 T22: 0.0877
REMARK 3 T33: 0.1282 T12: -0.0347
REMARK 3 T13: 0.0196 T23: -0.0114
REMARK 3 L TENSOR
REMARK 3 L11: 0.3290 L22: 1.0042
REMARK 3 L33: 0.0656 L12: 0.0903
REMARK 3 L13: 0.0549 L23: -0.1642
REMARK 3 S TENSOR
REMARK 3 S11: -0.0087 S12: 0.0310 S13: 0.0159
REMARK 3 S21: 0.0762 S22: 0.0351 S23: -0.0401
REMARK 3 S31: 0.0020 S32: -0.0293 S33: -0.0263
REMARK 3
REMARK 3 TLS GROUP : 9
REMARK 3 NUMBER OF COMPONENTS GROUP : 0
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 ORIGIN FOR THE GROUP (A): -14.6492 8.9492 -32.8016
REMARK 3 T TENSOR
REMARK 3 T11: 0.2030 T22: 0.0512
REMARK 3 T33: 0.0590 T12: -0.0595
REMARK 3 T13: -0.0307 T23: -0.0024
REMARK 3 L TENSOR
REMARK 3 L11: 0.0740 L22: 1.2650
REMARK 3 L33: 0.9419 L12: 0.2678
REMARK 3 L13: 0.0716 L23: -0.0983
REMARK 3 S TENSOR
REMARK 3 S11: -0.0373 S12: 0.0239 S13: -0.0440
REMARK 3 S21: 0.0788 S22: 0.0144 S23: -0.2106
REMARK 3 S31: -0.1618 S32: -0.0062 S33: 0.0229
REMARK 3
REMARK 3 TLS GROUP : 10
REMARK 3 NUMBER OF COMPONENTS GROUP : 0
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 ORIGIN FOR THE GROUP (A): -27.1513 9.7890 -30.0303
REMARK 3 T TENSOR
REMARK 3 T11: 0.2508 T22: 0.0374
REMARK 3 T33: 0.0825 T12: 0.0023
REMARK 3 T13: 0.0442 T23: 0.0119
REMARK 3 L TENSOR
REMARK 3 L11: 0.5123 L22: 1.2478
REMARK 3 L33: 2.2790 L12: -0.1899
REMARK 3 L13: 0.7173 L23: 0.8885
REMARK 3 S TENSOR
REMARK 3 S11: -0.1079 S12: 0.1005 S13: -0.0598
REMARK 3 S21: 0.1934 S22: -0.0122 S23: 0.2634
REMARK 3 S31: -0.1437 S32: 0.1156 S33: 0.1201
REMARK 3
REMARK 3 TLS GROUP : 11
REMARK 3 NUMBER OF COMPONENTS GROUP : 0
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 ORIGIN FOR THE GROUP (A): -17.7015 -4.0057 -20.4248
REMARK 3 T TENSOR
REMARK 3 T11: 0.2472 T22: 0.0278
REMARK 3 T33: 0.0361 T12: -0.0138
REMARK 3 T13: -0.0362 T23: -0.0029
REMARK 3 L TENSOR
REMARK 3 L11: 0.7670 L22: 1.1475
REMARK 3 L33: 0.1293 L12: -0.0820
REMARK 3 L13: -0.0630 L23: -0.3688
REMARK 3 S TENSOR
REMARK 3 S11: -0.0499 S12: 0.1366 S13: -0.0161
REMARK 3 S21: 0.4166 S22: 0.0149 S23: -0.0952
REMARK 3 S31: -0.1275 S32: -0.0214 S33: 0.0350
REMARK 3
REMARK 3 TLS GROUP : 12
REMARK 3 NUMBER OF COMPONENTS GROUP : 0
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 ORIGIN FOR THE GROUP (A): -17.4741 -9.4607 -33.8121
REMARK 3 T TENSOR
REMARK 3 T11: 0.1723 T22: 0.0668
REMARK 3 T33: 0.0861 T12: -0.0084
REMARK 3 T13: -0.0072 T23: -0.0194
REMARK 3 L TENSOR
REMARK 3 L11: 7.5575 L22: 1.9105
REMARK 3 L33: 1.8621 L12: -1.7323
REMARK 3 L13: 1.7409 L23: -0.5817
REMARK 3 S TENSOR
REMARK 3 S11: 0.1050 S12: 0.1854 S13: -0.1750
REMARK 3 S21: -0.0665 S22: -0.0472 S23: -0.0762
REMARK 3 S31: 0.1443 S32: 0.0482 S33: -0.0578
REMARK 3
REMARK 3 TLS GROUP : 13
REMARK 3 NUMBER OF COMPONENTS GROUP : 0
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 ORIGIN FOR THE GROUP (A): -3.5224 22.5613 -0.6588
REMARK 3 T TENSOR
REMARK 3 T11: 0.1515 T22: 0.0817
REMARK 3 T33: 0.1269 T12: -0.0089
REMARK 3 T13: 0.0399 T23: 0.0055
REMARK 3 L TENSOR
REMARK 3 L11: 9.3992 L22: 4.6257
REMARK 3 L33: 0.5942 L12: 3.0106
REMARK 3 L13: 1.5538 L23: -0.6015
REMARK 3 S TENSOR
REMARK 3 S11: -0.0362 S12: -0.2737 S13: 0.0557
REMARK 3 S21: -0.0671 S22: -0.0137 S23: 0.0152
REMARK 3 S31: 0.0326 S32: -0.0633 S33: 0.0500
REMARK 3
REMARK 3 TLS GROUP : 14
REMARK 3 NUMBER OF COMPONENTS GROUP : 0
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 ORIGIN FOR THE GROUP (A): 1.0709 33.2602 -6.5791
REMARK 3 T TENSOR
REMARK 3 T11: 0.0828 T22: 0.0767
REMARK 3 T33: 0.1099 T12: 0.0228
REMARK 3 T13: 0.0067 T23: 0.0036
REMARK 3 L TENSOR
REMARK 3 L11: 0.4089 L22: 1.8862
REMARK 3 L33: 2.1663 L12: 0.0500
REMARK 3 L13: 0.2547 L23: 0.1509
REMARK 3 S TENSOR
REMARK 3 S11: 0.0517 S12: -0.0436 S13: -0.0434
REMARK 3 S21: -0.1143 S22: -0.0376 S23: -0.0764
REMARK 3 S31: 0.1262 S32: 0.0516 S33: -0.0141
REMARK 3
REMARK 3 TLS GROUP : 15
REMARK 3 NUMBER OF COMPONENTS GROUP : 0
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 ORIGIN FOR THE GROUP (A): -10.9519 28.0578 -6.3132
REMARK 3 T TENSOR
REMARK 3 T11: 0.0917 T22: 0.0561
REMARK 3 T33: 0.1682 T12: -0.0196
REMARK 3 T13: -0.0322 T23: 0.0070
REMARK 3 L TENSOR
REMARK 3 L11: 1.1293 L22: 1.2573
REMARK 3 L33: 9.2656 L12: 0.2756
REMARK 3 L13: 0.8223 L23: -0.6024
REMARK 3 S TENSOR
REMARK 3 S11: 0.0160 S12: 0.0305 S13: -0.1544
REMARK 3 S21: -0.0892 S22: 0.1334 S23: 0.3198
REMARK 3 S31: 0.1705 S32: -0.2180 S33: -0.1495
REMARK 3
REMARK 3 TLS GROUP : 16
REMARK 3 NUMBER OF COMPONENTS GROUP : 0
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 ORIGIN FOR THE GROUP (A): -7.1905 45.5426 -10.3208
REMARK 3 T TENSOR
REMARK 3 T11: 0.0581 T22: 0.0844
REMARK 3 T33: 0.1196 T12: 0.0034
REMARK 3 T13: 0.0109 T23: 0.0034
REMARK 3 L TENSOR
REMARK 3 L11: 0.0255 L22: 1.5664
REMARK 3 L33: 0.4879 L12: -0.1866
REMARK 3 L13: 0.0695 L23: -0.6067
REMARK 3 S TENSOR
REMARK 3 S11: 0.0232 S12: -0.0138 S13: -0.0073
REMARK 3 S21: -0.1016 S22: 0.0767 S23: 0.1926
REMARK 3 S31: 0.0455 S32: 0.0196 S33: -0.0999
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK BULK SOLVENT
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THEIR
REMARK 3 RIDING POSITIONS
REMARK 4
REMARK 4 9BLE COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-MAY-24.
REMARK 100 THE DEPOSITION ID IS D_1000283646.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 05-MAY-22
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : LNLS SIRIUS
REMARK 200 BEAMLINE : MANACA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97718
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 2M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 137099
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.530
REMARK 200 RESOLUTION RANGE LOW (A) : 74.402
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 92.3
REMARK 200 DATA REDUNDANCY : 4.700
REMARK 200 R MERGE (I) : 0.12100
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 6.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.53
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.56
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.3
REMARK 200 DATA REDUNDANCY IN SHELL : 5.00
REMARK 200 R MERGE FOR SHELL (I) : 4.08200
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 0.500
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: NULL
REMARK 200
REMARK 200 REMARK: LONG RODS
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 48.67
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.40
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M SODIUM FLUORIDE, 0.1 M BIS-TRIS
REMARK 280 PROPANE 8.5, 20% PEG 3350, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 293K
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 71.33450
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
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2410 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 18240 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -6.0 KCAL/MOL
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 APPLY THE FOLLOWING TO CHAINS: C
REMARK 350 BIOMT1 2 -1.000000 0.000000 0.000000 -38.96538
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 71.33450
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 -74.40206
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2430 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 18250 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -5.0 KCAL/MOL
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 APPLY THE FOLLOWING TO CHAINS: D
REMARK 350 BIOMT1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 -71.33450
REMARK 350 BIOMT3 2 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 HIS A -5
REMARK 465 HIS A -4
REMARK 465 HIS A -3
REMARK 465 HIS A -2
REMARK 465 HIS A -1
REMARK 465 HIS A 0
REMARK 465 MET A 1
REMARK 465 HIS B -5
REMARK 465 HIS B -4
REMARK 465 HIS B -3
REMARK 465 HIS B -2
REMARK 465 HIS B -1
REMARK 465 HIS B 0
REMARK 465 HIS C -5
REMARK 465 HIS D -5
REMARK 465 HIS D -4
REMARK 465 HIS D -3
REMARK 465 HIS D -2
REMARK 465 HIS D -1
REMARK 465 HIS D 0
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 PHE A 23 CD1 CD2 CE1 CE2 CZ
REMARK 470 LYS A 25 CG CD CE NZ
REMARK 470 LYS A 65 CE NZ
REMARK 470 MET B 1 CG SD CE
REMARK 470 GLU B 13 CG CD OE1 OE2
REMARK 470 GLU B 22 CG CD OE1 OE2
REMARK 470 PHE B 23 CE1 CE2 CZ
REMARK 470 LYS B 25 CG CD CE NZ
REMARK 470 LYS B 191 CE NZ
REMARK 470 HIS C -4 ND1 CD2 CE1 NE2
REMARK 470 HIS C -3 CD2 CE1 NE2
REMARK 470 HIS C -1 CD2 CE1 NE2
REMARK 470 HIS C 0 CG ND1 CD2 CE1 NE2
REMARK 470 ARG C 75 CG CD NE CZ NH1 NH2
REMARK 470 LYS C 180 CG CD CE NZ
REMARK 470 LYS C 191 CD CE NZ
REMARK 470 MET D 1 CG SD CE
REMARK 470 LYS D 25 CE NZ
REMARK 470 GLN D 78 CD OE1 NE2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 OE1 GLU C 20 O HOH C 301 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 CYS A 121 CB - CA - C ANGL. DEV. = 7.6 DEGREES
REMARK 500 CYS A 121 CB - CA - C ANGL. DEV. = 10.5 DEGREES
REMARK 500 CYS A 121 CA - CB - SG ANGL. DEV. = 6.8 DEGREES
REMARK 500 CYS B 121 CB - CA - C ANGL. DEV. = 10.1 DEGREES
REMARK 500 CYS B 121 CA - CB - SG ANGL. DEV. = 7.7 DEGREES
REMARK 500 LEU B 195 CB - CG - CD2 ANGL. DEV. = -10.4 DEGREES
REMARK 500 TYR B 217 CB - CG - CD2 ANGL. DEV. = -3.8 DEGREES
REMARK 500 ARG C 114 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 CYS C 121 CB - CA - C ANGL. DEV. = 7.7 DEGREES
REMARK 500 CYS C 121 N - CA - CB ANGL. DEV. = 9.6 DEGREES
REMARK 500 CYS D 121 CB - CA - C ANGL. DEV. = 8.9 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
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 CYS A 121 -126.87 66.33
REMARK 500 CYS A 121 -127.50 67.07
REMARK 500 PHE A 134 54.87 -116.40
REMARK 500 CYS B 121 -125.54 65.60
REMARK 500 CYS B 121 -126.58 66.91
REMARK 500 PHE B 134 55.45 -115.28
REMARK 500 THR C 24 78.45 -105.55
REMARK 500 CYS C 121 -126.22 63.70
REMARK 500 CYS C 121 -122.09 56.13
REMARK 500 PHE C 134 54.87 -114.44
REMARK 500 CYS D 121 -125.47 63.97
REMARK 500 PHE D 134 53.75 -114.65
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 ARG B 84 0.10 SIDE CHAIN
REMARK 500 ARG B 209 0.07 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A 455 DISTANCE = 6.06 ANGSTROMS
REMARK 525 HOH A 456 DISTANCE = 6.23 ANGSTROMS
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 9BLD RELATED DB: PDB
DBREF 9BLE A 1 234 UNP D3DKA9 D3DKA9_HYDTT 1 234
DBREF 9BLE B 1 234 UNP D3DKA9 D3DKA9_HYDTT 1 234
DBREF 9BLE C 1 234 UNP D3DKA9 D3DKA9_HYDTT 1 234
DBREF 9BLE D 1 234 UNP D3DKA9 D3DKA9_HYDTT 1 234
SEQADV 9BLE HIS A -5 UNP D3DKA9 EXPRESSION TAG
SEQADV 9BLE HIS A -4 UNP D3DKA9 EXPRESSION TAG
SEQADV 9BLE HIS A -3 UNP D3DKA9 EXPRESSION TAG
SEQADV 9BLE HIS A -2 UNP D3DKA9 EXPRESSION TAG
SEQADV 9BLE HIS A -1 UNP D3DKA9 EXPRESSION TAG
SEQADV 9BLE HIS A 0 UNP D3DKA9 EXPRESSION TAG
SEQADV 9BLE HIS B -5 UNP D3DKA9 EXPRESSION TAG
SEQADV 9BLE HIS B -4 UNP D3DKA9 EXPRESSION TAG
SEQADV 9BLE HIS B -3 UNP D3DKA9 EXPRESSION TAG
SEQADV 9BLE HIS B -2 UNP D3DKA9 EXPRESSION TAG
SEQADV 9BLE HIS B -1 UNP D3DKA9 EXPRESSION TAG
SEQADV 9BLE HIS B 0 UNP D3DKA9 EXPRESSION TAG
SEQADV 9BLE HIS C -5 UNP D3DKA9 EXPRESSION TAG
SEQADV 9BLE HIS C -4 UNP D3DKA9 EXPRESSION TAG
SEQADV 9BLE HIS C -3 UNP D3DKA9 EXPRESSION TAG
SEQADV 9BLE HIS C -2 UNP D3DKA9 EXPRESSION TAG
SEQADV 9BLE HIS C -1 UNP D3DKA9 EXPRESSION TAG
SEQADV 9BLE HIS C 0 UNP D3DKA9 EXPRESSION TAG
SEQADV 9BLE HIS D -5 UNP D3DKA9 EXPRESSION TAG
SEQADV 9BLE HIS D -4 UNP D3DKA9 EXPRESSION TAG
SEQADV 9BLE HIS D -3 UNP D3DKA9 EXPRESSION TAG
SEQADV 9BLE HIS D -2 UNP D3DKA9 EXPRESSION TAG
SEQADV 9BLE HIS D -1 UNP D3DKA9 EXPRESSION TAG
SEQADV 9BLE HIS D 0 UNP D3DKA9 EXPRESSION TAG
SEQRES 1 A 240 HIS HIS HIS HIS HIS HIS MET GLY ARG GLU LEU LYS PHE
SEQRES 2 A 240 LYS LYS ASP GLY VAL GLU ILE SER GLY TYR LEU ALA GLU
SEQRES 3 A 240 PRO GLU PHE THR LYS GLY PRO LEU VAL ILE VAL ILE HIS
SEQRES 4 A 240 GLU TRP TRP GLY LEU VAL PRO HIS ILE LYS ASP VAL CYS
SEQRES 5 A 240 ASP ARG TYR ALA ARG GLU GLY PHE PHE ALA PHE GLY ILE
SEQRES 6 A 240 ASP LEU TYR LYS GLY LYS THR ALA ASP ASN PRO ASP ASP
SEQRES 7 A 240 ALA GLY ARG LEU MET GLN GLU LEU LEU GLY GLN ARG LEU
SEQRES 8 A 240 SER GLU ALA GLU ALA MET ILE LYS ALA SER LEU ASP TYR
SEQRES 9 A 240 PHE LYS GLU ASN ASP ILE GLY PHE VAL GLY ARG VAL GLN
SEQRES 10 A 240 ASP TYR ARG ILE GLY MET THR GLY PHE CYS CYS GLY GLY
SEQRES 11 A 240 THR CYS THR TRP TYR PHE GLY ALA LYS PHE SER ASP GLU
SEQRES 12 A 240 PHE SER ALA LEU ALA PRO TYR TYR GLY LEU TYR SER LEU
SEQRES 13 A 240 VAL PRO ILE ASP PHE SER ALA ILE LYS ALA PRO VAL LEU
SEQRES 14 A 240 ALA VAL HIS ALA GLY LYS ASP ALA PHE VAL PRO LEU SER
SEQRES 15 A 240 GLU VAL LEU LYS ALA ILE GLU GLU CYS ASN LYS TYR GLY
SEQRES 16 A 240 VAL LYS ALA GLN PHE LEU ILE TYR SER GLY VAL ASP HIS
SEQRES 17 A 240 ALA PHE PHE ASN ASP THR ARG PRO GLU VAL TYR ASN GLU
SEQRES 18 A 240 GLU TYR ALA VAL ASP VAL TRP GLY LYS THR VAL GLU PHE
SEQRES 19 A 240 MET LYS ARG HIS LEU THR
SEQRES 1 B 240 HIS HIS HIS HIS HIS HIS MET GLY ARG GLU LEU LYS PHE
SEQRES 2 B 240 LYS LYS ASP GLY VAL GLU ILE SER GLY TYR LEU ALA GLU
SEQRES 3 B 240 PRO GLU PHE THR LYS GLY PRO LEU VAL ILE VAL ILE HIS
SEQRES 4 B 240 GLU TRP TRP GLY LEU VAL PRO HIS ILE LYS ASP VAL CYS
SEQRES 5 B 240 ASP ARG TYR ALA ARG GLU GLY PHE PHE ALA PHE GLY ILE
SEQRES 6 B 240 ASP LEU TYR LYS GLY LYS THR ALA ASP ASN PRO ASP ASP
SEQRES 7 B 240 ALA GLY ARG LEU MET GLN GLU LEU LEU GLY GLN ARG LEU
SEQRES 8 B 240 SER GLU ALA GLU ALA MET ILE LYS ALA SER LEU ASP TYR
SEQRES 9 B 240 PHE LYS GLU ASN ASP ILE GLY PHE VAL GLY ARG VAL GLN
SEQRES 10 B 240 ASP TYR ARG ILE GLY MET THR GLY PHE CYS CYS GLY GLY
SEQRES 11 B 240 THR CYS THR TRP TYR PHE GLY ALA LYS PHE SER ASP GLU
SEQRES 12 B 240 PHE SER ALA LEU ALA PRO TYR TYR GLY LEU TYR SER LEU
SEQRES 13 B 240 VAL PRO ILE ASP PHE SER ALA ILE LYS ALA PRO VAL LEU
SEQRES 14 B 240 ALA VAL HIS ALA GLY LYS ASP ALA PHE VAL PRO LEU SER
SEQRES 15 B 240 GLU VAL LEU LYS ALA ILE GLU GLU CYS ASN LYS TYR GLY
SEQRES 16 B 240 VAL LYS ALA GLN PHE LEU ILE TYR SER GLY VAL ASP HIS
SEQRES 17 B 240 ALA PHE PHE ASN ASP THR ARG PRO GLU VAL TYR ASN GLU
SEQRES 18 B 240 GLU TYR ALA VAL ASP VAL TRP GLY LYS THR VAL GLU PHE
SEQRES 19 B 240 MET LYS ARG HIS LEU THR
SEQRES 1 C 240 HIS HIS HIS HIS HIS HIS MET GLY ARG GLU LEU LYS PHE
SEQRES 2 C 240 LYS LYS ASP GLY VAL GLU ILE SER GLY TYR LEU ALA GLU
SEQRES 3 C 240 PRO GLU PHE THR LYS GLY PRO LEU VAL ILE VAL ILE HIS
SEQRES 4 C 240 GLU TRP TRP GLY LEU VAL PRO HIS ILE LYS ASP VAL CYS
SEQRES 5 C 240 ASP ARG TYR ALA ARG GLU GLY PHE PHE ALA PHE GLY ILE
SEQRES 6 C 240 ASP LEU TYR LYS GLY LYS THR ALA ASP ASN PRO ASP ASP
SEQRES 7 C 240 ALA GLY ARG LEU MET GLN GLU LEU LEU GLY GLN ARG LEU
SEQRES 8 C 240 SER GLU ALA GLU ALA MET ILE LYS ALA SER LEU ASP TYR
SEQRES 9 C 240 PHE LYS GLU ASN ASP ILE GLY PHE VAL GLY ARG VAL GLN
SEQRES 10 C 240 ASP TYR ARG ILE GLY MET THR GLY PHE CYS CYS GLY GLY
SEQRES 11 C 240 THR CYS THR TRP TYR PHE GLY ALA LYS PHE SER ASP GLU
SEQRES 12 C 240 PHE SER ALA LEU ALA PRO TYR TYR GLY LEU TYR SER LEU
SEQRES 13 C 240 VAL PRO ILE ASP PHE SER ALA ILE LYS ALA PRO VAL LEU
SEQRES 14 C 240 ALA VAL HIS ALA GLY LYS ASP ALA PHE VAL PRO LEU SER
SEQRES 15 C 240 GLU VAL LEU LYS ALA ILE GLU GLU CYS ASN LYS TYR GLY
SEQRES 16 C 240 VAL LYS ALA GLN PHE LEU ILE TYR SER GLY VAL ASP HIS
SEQRES 17 C 240 ALA PHE PHE ASN ASP THR ARG PRO GLU VAL TYR ASN GLU
SEQRES 18 C 240 GLU TYR ALA VAL ASP VAL TRP GLY LYS THR VAL GLU PHE
SEQRES 19 C 240 MET LYS ARG HIS LEU THR
SEQRES 1 D 240 HIS HIS HIS HIS HIS HIS MET GLY ARG GLU LEU LYS PHE
SEQRES 2 D 240 LYS LYS ASP GLY VAL GLU ILE SER GLY TYR LEU ALA GLU
SEQRES 3 D 240 PRO GLU PHE THR LYS GLY PRO LEU VAL ILE VAL ILE HIS
SEQRES 4 D 240 GLU TRP TRP GLY LEU VAL PRO HIS ILE LYS ASP VAL CYS
SEQRES 5 D 240 ASP ARG TYR ALA ARG GLU GLY PHE PHE ALA PHE GLY ILE
SEQRES 6 D 240 ASP LEU TYR LYS GLY LYS THR ALA ASP ASN PRO ASP ASP
SEQRES 7 D 240 ALA GLY ARG LEU MET GLN GLU LEU LEU GLY GLN ARG LEU
SEQRES 8 D 240 SER GLU ALA GLU ALA MET ILE LYS ALA SER LEU ASP TYR
SEQRES 9 D 240 PHE LYS GLU ASN ASP ILE GLY PHE VAL GLY ARG VAL GLN
SEQRES 10 D 240 ASP TYR ARG ILE GLY MET THR GLY PHE CYS CYS GLY GLY
SEQRES 11 D 240 THR CYS THR TRP TYR PHE GLY ALA LYS PHE SER ASP GLU
SEQRES 12 D 240 PHE SER ALA LEU ALA PRO TYR TYR GLY LEU TYR SER LEU
SEQRES 13 D 240 VAL PRO ILE ASP PHE SER ALA ILE LYS ALA PRO VAL LEU
SEQRES 14 D 240 ALA VAL HIS ALA GLY LYS ASP ALA PHE VAL PRO LEU SER
SEQRES 15 D 240 GLU VAL LEU LYS ALA ILE GLU GLU CYS ASN LYS TYR GLY
SEQRES 16 D 240 VAL LYS ALA GLN PHE LEU ILE TYR SER GLY VAL ASP HIS
SEQRES 17 D 240 ALA PHE PHE ASN ASP THR ARG PRO GLU VAL TYR ASN GLU
SEQRES 18 D 240 GLU TYR ALA VAL ASP VAL TRP GLY LYS THR VAL GLU PHE
SEQRES 19 D 240 MET LYS ARG HIS LEU THR
FORMUL 5 HOH *642(H2 O)
HELIX 1 AA1 VAL A 39 GLU A 52 1 14
HELIX 2 AA2 ASN A 69 ARG A 84 1 16
HELIX 3 AA3 ARG A 84 ASN A 102 1 19
HELIX 4 AA4 CYS A 121 PHE A 134 1 14
HELIX 5 AA5 ASP A 154 ILE A 158 5 5
HELIX 6 AA6 PRO A 174 GLY A 189 1 16
HELIX 7 AA7 ASN A 214 THR A 234 1 21
HELIX 8 AA8 VAL B 39 GLU B 52 1 14
HELIX 9 AA9 ASN B 69 GLY B 82 1 14
HELIX 10 AB1 ARG B 84 ASN B 102 1 19
HELIX 11 AB2 CYS B 121 PHE B 134 1 14
HELIX 12 AB3 ASP B 154 ILE B 158 5 5
HELIX 13 AB4 PRO B 174 GLY B 189 1 16
HELIX 14 AB5 ASN B 214 THR B 234 1 21
HELIX 15 AB6 VAL C 39 GLU C 52 1 14
HELIX 16 AB7 ASN C 69 GLY C 82 1 14
HELIX 17 AB8 ARG C 84 ASN C 102 1 19
HELIX 18 AB9 CYS C 121 PHE C 134 1 14
HELIX 19 AC1 ASP C 154 ILE C 158 5 5
HELIX 20 AC2 PRO C 174 GLY C 189 1 16
HELIX 21 AC3 ASN C 214 THR C 234 1 21
HELIX 22 AC4 VAL D 39 GLU D 52 1 14
HELIX 23 AC5 ASN D 69 ARG D 84 1 16
HELIX 24 AC6 ARG D 84 ASN D 102 1 19
HELIX 25 AC7 CYS D 121 PHE D 134 1 14
HELIX 26 AC8 ASP D 154 ILE D 158 5 5
HELIX 27 AC9 PRO D 174 GLY D 189 1 16
HELIX 28 AD1 ASN D 214 THR D 234 1 21
SHEET 1 AA1 6 ARG A 3 LYS A 9 0
SHEET 2 AA1 6 VAL A 12 ALA A 19 -1 O ILE A 14 N PHE A 7
SHEET 3 AA1 6 PHE A 55 ILE A 59 -1 O GLY A 58 N TYR A 17
SHEET 4 AA1 6 LEU A 28 ILE A 32 1 N VAL A 29 O PHE A 55
SHEET 5 AA1 6 ILE A 115 PHE A 120 1 O GLY A 116 N LEU A 28
SHEET 6 AA1 6 ALA A 140 TYR A 144 1 O TYR A 144 N GLY A 119
SHEET 1 AA2 2 PHE A 106 VAL A 107 0
SHEET 2 AA2 2 ASP A 112 TYR A 113 -1 O ASP A 112 N VAL A 107
SHEET 1 AA3 2 VAL A 162 ALA A 167 0
SHEET 2 AA3 2 ALA A 192 TYR A 197 1 O LEU A 195 N HIS A 166
SHEET 1 AA4 6 GLY B 2 LYS B 9 0
SHEET 2 AA4 6 VAL B 12 ALA B 19 -1 O ILE B 14 N PHE B 7
SHEET 3 AA4 6 PHE B 55 ILE B 59 -1 O GLY B 58 N TYR B 17
SHEET 4 AA4 6 LEU B 28 ILE B 32 1 N VAL B 31 O PHE B 57
SHEET 5 AA4 6 ILE B 115 PHE B 120 1 O GLY B 116 N LEU B 28
SHEET 6 AA4 6 ALA B 140 TYR B 144 1 O TYR B 144 N GLY B 119
SHEET 1 AA5 2 PHE B 106 VAL B 107 0
SHEET 2 AA5 2 ASP B 112 TYR B 113 -1 O ASP B 112 N VAL B 107
SHEET 1 AA6 2 VAL B 162 ALA B 167 0
SHEET 2 AA6 2 ALA B 192 TYR B 197 1 O LEU B 195 N HIS B 166
SHEET 1 AA7 6 HIS C 0 LYS C 9 0
SHEET 2 AA7 6 VAL C 12 PRO C 21 -1 O ILE C 14 N PHE C 7
SHEET 3 AA7 6 PHE C 55 ILE C 59 -1 O GLY C 58 N TYR C 17
SHEET 4 AA7 6 LEU C 28 ILE C 32 1 N VAL C 31 O PHE C 57
SHEET 5 AA7 6 ILE C 115 PHE C 120 1 O GLY C 116 N LEU C 28
SHEET 6 AA7 6 ALA C 140 TYR C 144 1 O TYR C 144 N GLY C 119
SHEET 1 AA8 2 PHE C 106 VAL C 107 0
SHEET 2 AA8 2 ASP C 112 TYR C 113 -1 O ASP C 112 N VAL C 107
SHEET 1 AA9 2 VAL C 162 ALA C 167 0
SHEET 2 AA9 2 ALA C 192 TYR C 197 1 O LEU C 195 N HIS C 166
SHEET 1 AB1 6 ARG D 3 LYS D 9 0
SHEET 2 AB1 6 VAL D 12 ALA D 19 -1 O ILE D 14 N PHE D 7
SHEET 3 AB1 6 PHE D 55 ILE D 59 -1 O GLY D 58 N TYR D 17
SHEET 4 AB1 6 LEU D 28 ILE D 32 1 N VAL D 31 O PHE D 57
SHEET 5 AB1 6 ILE D 115 PHE D 120 1 O GLY D 116 N LEU D 28
SHEET 6 AB1 6 ALA D 140 TYR D 144 1 O TYR D 144 N GLY D 119
SHEET 1 AB2 2 PHE D 106 VAL D 107 0
SHEET 2 AB2 2 ASP D 112 TYR D 113 -1 O ASP D 112 N VAL D 107
SHEET 1 AB3 2 VAL D 162 ALA D 167 0
SHEET 2 AB3 2 ALA D 192 TYR D 197 1 O LEU D 195 N HIS D 166
CRYST1 47.474 142.669 74.887 90.00 96.52 90.00 P 1 21 1 8
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 0.021064 0.000000 0.002409 0.00000
SCALE2 0.000000 0.007009 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013440 0.00000
TER 1856 THR A 234
TER 3733 THR B 234
TER 5624 THR C 234
TER 7515 THR D 234
MASTER 730 0 0 28 40 0 0 6 8077 4 0 76
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