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HEADER HYDROLASE 30-APR-24 9BLD
TITLE CRYSTAL STRUCTURE OF THERMOSTABLE DIENELACTONE HYDROLASE
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 9BLD 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. 1.67 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) : 1.67
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 74.55
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 112892
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) : 0.164
REMARK 3 FREE R VALUE : 0.189
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.112
REMARK 3 FREE R VALUE TEST SET COUNT : 5771
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) : 1.67
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.71
REMARK 3 REFLECTION IN BIN (WORKING SET) : 7777
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.62
REMARK 3 BIN R VALUE (WORKING SET) : 0.3460
REMARK 3 BIN FREE R VALUE SET COUNT : 411
REMARK 3 BIN FREE R VALUE : 0.3510
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 7410
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 768
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 29.32
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.44600
REMARK 3 B22 (A**2) : 0.02000
REMARK 3 B33 (A**2) : -0.46600
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): 0.093
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.089
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.075
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.785
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.974
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.967
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 7734 ; 0.008 ; 0.012
REMARK 3 BOND LENGTHS OTHERS (A): 7119 ; 0.001 ; 0.016
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 10496 ; 1.602 ; 1.827
REMARK 3 BOND ANGLES OTHERS (DEGREES): 16442 ; 0.553 ; 1.754
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 969 ; 5.690 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 36 ; 7.121 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1249 ;11.447 ;10.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1094 ; 0.081 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 9145 ; 0.008 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 1843 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1365 ; 0.209 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 48 ; 0.149 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 3820 ; 0.185 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 626 ; 0.159 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): 1 ; 0.011 ; 0.200
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): 3774 ; 1.951 ; 1.859
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 3774 ; 1.951 ; 1.859
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 4720 ; 2.860 ; 3.334
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 4721 ; 2.862 ; 3.334
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 3960 ; 3.305 ; 2.281
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 3961 ; 3.305 ; 2.281
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 5757 ; 5.237 ; 3.996
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 5758 ; 5.237 ; 3.996
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 1 A 234 NULL
REMARK 3 1 A 1 A 234 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 1 A 234 NULL
REMARK 3 3 A 1 A 234 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 1 A 234 NULL
REMARK 3 5 A 1 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 1 A 12
REMARK 3 ORIGIN FOR THE GROUP (A): 20.2865 -3.9962 -40.0744
REMARK 3 T TENSOR
REMARK 3 T11: 0.1838 T22: 0.2008
REMARK 3 T33: 0.1270 T12: -0.0546
REMARK 3 T13: 0.0278 T23: 0.0286
REMARK 3 L TENSOR
REMARK 3 L11: 2.0982 L22: 2.6986
REMARK 3 L33: 8.3809 L12: -2.3553
REMARK 3 L13: -4.1846 L23: 4.7015
REMARK 3 S TENSOR
REMARK 3 S11: 0.1932 S12: 0.0288 S13: 0.1634
REMARK 3 S21: -0.2593 S22: 0.0614 S23: -0.2203
REMARK 3 S31: -0.3248 S32: 0.0116 S33: -0.2546
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 13 A 68
REMARK 3 ORIGIN FOR THE GROUP (A): 14.5284 -2.9652 -28.8869
REMARK 3 T TENSOR
REMARK 3 T11: 0.1060 T22: 0.1499
REMARK 3 T33: 0.0463 T12: 0.0025
REMARK 3 T13: -0.0279 T23: 0.0419
REMARK 3 L TENSOR
REMARK 3 L11: 1.3853 L22: 1.0440
REMARK 3 L33: 2.2526 L12: 0.7007
REMARK 3 L13: 0.1517 L23: 0.2962
REMARK 3 S TENSOR
REMARK 3 S11: -0.0195 S12: 0.1828 S13: 0.1248
REMARK 3 S21: -0.0436 S22: 0.0896 S23: -0.0037
REMARK 3 S31: -0.0967 S32: -0.1230 S33: -0.0701
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 69 A 92
REMARK 3 ORIGIN FOR THE GROUP (A): 9.8987 -18.6696 -34.3827
REMARK 3 T TENSOR
REMARK 3 T11: 0.4245 T22: 0.1500
REMARK 3 T33: 0.0896 T12: -0.1172
REMARK 3 T13: -0.0371 T23: -0.0223
REMARK 3 L TENSOR
REMARK 3 L11: 12.6065 L22: 0.3023
REMARK 3 L33: 2.0220 L12: -0.1966
REMARK 3 L13: -0.3336 L23: -0.3229
REMARK 3 S TENSOR
REMARK 3 S11: -0.3143 S12: 0.0040 S13: -0.6806
REMARK 3 S21: -0.3459 S22: 0.1139 S23: 0.0613
REMARK 3 S31: 0.4634 S32: -0.1696 S33: 0.2004
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 93 A 234
REMARK 3 ORIGIN FOR THE GROUP (A): 17.6778 -12.2768 -18.5257
REMARK 3 T TENSOR
REMARK 3 T11: 0.1067 T22: 0.1234
REMARK 3 T33: 0.0531 T12: 0.0078
REMARK 3 T13: 0.0073 T23: 0.0015
REMARK 3 L TENSOR
REMARK 3 L11: 0.4844 L22: 0.0541
REMARK 3 L33: 1.4413 L12: 0.1428
REMARK 3 L13: -0.3758 L23: -0.1423
REMARK 3 S TENSOR
REMARK 3 S11: -0.1357 S12: 0.0486 S13: 0.0648
REMARK 3 S21: -0.0276 S22: 0.0466 S23: 0.0223
REMARK 3 S31: 0.1661 S32: 0.0288 S33: 0.0891
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): 17.5494 -1.6537 26.1264
REMARK 3 T TENSOR
REMARK 3 T11: 0.1795 T22: 0.1608
REMARK 3 T33: 0.0712 T12: -0.0131
REMARK 3 T13: 0.0023 T23: -0.0375
REMARK 3 L TENSOR
REMARK 3 L11: 10.0958 L22: 0.7456
REMARK 3 L33: 6.6200 L12: 1.9661
REMARK 3 L13: -7.2212 L23: -0.9162
REMARK 3 S TENSOR
REMARK 3 S11: 0.0863 S12: -0.3038 S13: 0.3547
REMARK 3 S21: 0.1563 S22: 0.0509 S23: 0.0131
REMARK 3 S31: 0.2390 S32: 0.2262 S33: -0.1372
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): 22.4934 -4.6746 14.6680
REMARK 3 T TENSOR
REMARK 3 T11: 0.1242 T22: 0.1625
REMARK 3 T33: 0.0355 T12: 0.0063
REMARK 3 T13: -0.0118 T23: -0.0049
REMARK 3 L TENSOR
REMARK 3 L11: 0.7217 L22: 2.7072
REMARK 3 L33: 1.8351 L12: -0.7160
REMARK 3 L13: -0.0136 L23: -0.6374
REMARK 3 S TENSOR
REMARK 3 S11: 0.0416 S12: -0.0555 S13: 0.1284
REMARK 3 S21: 0.1244 S22: 0.0224 S23: -0.0266
REMARK 3 S31: 0.1078 S32: 0.2330 S33: -0.0640
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): 12.8756 -12.4634 21.9130
REMARK 3 T TENSOR
REMARK 3 T11: 0.2236 T22: 0.1316
REMARK 3 T33: 0.0333 T12: -0.0132
REMARK 3 T13: 0.0146 T23: 0.0127
REMARK 3 L TENSOR
REMARK 3 L11: 1.6830 L22: 3.1391
REMARK 3 L33: 1.1916 L12: -1.0627
REMARK 3 L13: -0.6565 L23: 1.5117
REMARK 3 S TENSOR
REMARK 3 S11: 0.0179 S12: -0.1869 S13: -0.1524
REMARK 3 S21: 0.3945 S22: -0.1193 S23: 0.2769
REMARK 3 S31: 0.3364 S32: 0.0053 S33: 0.1013
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): 13.5553 -10.4559 4.7713
REMARK 3 T TENSOR
REMARK 3 T11: 0.1168 T22: 0.1109
REMARK 3 T33: 0.0535 T12: 0.0246
REMARK 3 T13: 0.0351 T23: 0.0210
REMARK 3 L TENSOR
REMARK 3 L11: 0.3164 L22: 0.3022
REMARK 3 L33: 0.9085 L12: -0.0919
REMARK 3 L13: -0.3324 L23: 0.2935
REMARK 3 S TENSOR
REMARK 3 S11: -0.0125 S12: -0.0033 S13: 0.0623
REMARK 3 S21: 0.0747 S22: -0.0375 S23: 0.0371
REMARK 3 S31: 0.1522 S32: 0.0540 S33: 0.0500
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): -21.8525 -1.1587 -24.1114
REMARK 3 T TENSOR
REMARK 3 T11: 0.1077 T22: 0.1973
REMARK 3 T33: 0.1226 T12: -0.0307
REMARK 3 T13: -0.0370 T23: -0.0409
REMARK 3 L TENSOR
REMARK 3 L11: 1.8809 L22: 0.3935
REMARK 3 L33: 4.3434 L12: -0.8262
REMARK 3 L13: 2.6065 L23: -1.2657
REMARK 3 S TENSOR
REMARK 3 S11: 0.1725 S12: 0.2015 S13: -0.2914
REMARK 3 S21: -0.0610 S22: 0.0022 S23: 0.1067
REMARK 3 S31: 0.1130 S32: 0.1187 S33: -0.1748
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): -14.7281 6.3315 -17.0809
REMARK 3 T TENSOR
REMARK 3 T11: 0.0874 T22: 0.1550
REMARK 3 T33: 0.0692 T12: -0.0195
REMARK 3 T13: 0.0091 T23: -0.0093
REMARK 3 L TENSOR
REMARK 3 L11: 1.6173 L22: 1.7326
REMARK 3 L33: 1.5071 L12: 0.1614
REMARK 3 L13: 0.0178 L23: -0.4578
REMARK 3 S TENSOR
REMARK 3 S11: -0.0385 S12: 0.2036 S13: 0.0187
REMARK 3 S21: -0.0162 S22: 0.0336 S23: -0.0599
REMARK 3 S31: -0.0407 S32: 0.2379 S33: 0.0048
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): -24.7848 11.4082 -23.7570
REMARK 3 T TENSOR
REMARK 3 T11: 0.1381 T22: 0.2154
REMARK 3 T33: 0.0421 T12: 0.0059
REMARK 3 T13: -0.0336 T23: 0.0107
REMARK 3 L TENSOR
REMARK 3 L11: 1.5204 L22: 4.5649
REMARK 3 L33: 0.6513 L12: 1.8023
REMARK 3 L13: -0.0945 L23: -0.7589
REMARK 3 S TENSOR
REMARK 3 S11: 0.0279 S12: 0.2401 S13: -0.0068
REMARK 3 S21: -0.0734 S22: -0.1309 S23: -0.0677
REMARK 3 S31: -0.1431 S32: -0.0369 S33: 0.1030
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): -21.8866 11.7903 -5.9215
REMARK 3 T TENSOR
REMARK 3 T11: 0.0669 T22: 0.1190
REMARK 3 T33: 0.0954 T12: -0.0218
REMARK 3 T13: -0.0096 T23: 0.0308
REMARK 3 L TENSOR
REMARK 3 L11: 0.6734 L22: 0.2682
REMARK 3 L33: 0.6867 L12: 0.0675
REMARK 3 L13: 0.0065 L23: 0.3822
REMARK 3 S TENSOR
REMARK 3 S11: -0.0892 S12: 0.0158 S13: -0.0007
REMARK 3 S21: -0.0184 S22: 0.0727 S23: 0.0105
REMARK 3 S31: -0.0375 S32: 0.0046 S33: 0.0165
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): -20.3719 3.2591 29.1330
REMARK 3 T TENSOR
REMARK 3 T11: 0.0752 T22: 0.1540
REMARK 3 T33: 0.0658 T12: -0.0091
REMARK 3 T13: 0.0214 T23: 0.0039
REMARK 3 L TENSOR
REMARK 3 L11: 0.6797 L22: 0.5251
REMARK 3 L33: 0.8992 L12: 0.2530
REMARK 3 L13: 0.4258 L23: -0.2751
REMARK 3 S TENSOR
REMARK 3 S11: 0.0898 S12: -0.1470 S13: -0.0967
REMARK 3 S21: 0.0013 S22: 0.0152 S23: -0.0600
REMARK 3 S31: -0.0183 S32: -0.2038 S33: -0.1049
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): -18.2719 15.1458 33.6030
REMARK 3 T TENSOR
REMARK 3 T11: 0.1967 T22: 0.1857
REMARK 3 T33: 0.0401 T12: -0.0677
REMARK 3 T13: 0.0092 T23: -0.0528
REMARK 3 L TENSOR
REMARK 3 L11: 0.8614 L22: 1.1946
REMARK 3 L33: 1.1934 L12: -0.3232
REMARK 3 L13: 0.2896 L23: -0.4053
REMARK 3 S TENSOR
REMARK 3 S11: 0.1188 S12: -0.2094 S13: 0.1046
REMARK 3 S21: 0.3118 S22: -0.1938 S23: -0.0234
REMARK 3 S31: -0.2193 S32: -0.0461 S33: 0.0750
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): -11.3521 11.5810 20.8271
REMARK 3 T TENSOR
REMARK 3 T11: 0.0847 T22: 0.1327
REMARK 3 T33: 0.0734 T12: -0.0060
REMARK 3 T13: 0.0004 T23: -0.0170
REMARK 3 L TENSOR
REMARK 3 L11: 0.3760 L22: 1.4360
REMARK 3 L33: 0.5934 L12: 0.1010
REMARK 3 L13: -0.0270 L23: -0.2440
REMARK 3 S TENSOR
REMARK 3 S11: -0.0295 S12: -0.0677 S13: -0.0212
REMARK 3 S21: 0.0748 S22: -0.0222 S23: -0.0405
REMARK 3 S31: -0.1481 S32: 0.0759 S33: 0.0517
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): -22.1896 14.1029 11.7911
REMARK 3 T TENSOR
REMARK 3 T11: 0.0739 T22: 0.1400
REMARK 3 T33: 0.0954 T12: -0.0113
REMARK 3 T13: -0.0115 T23: -0.0081
REMARK 3 L TENSOR
REMARK 3 L11: 0.8135 L22: 0.1445
REMARK 3 L33: 0.9113 L12: 0.0568
REMARK 3 L13: 0.4950 L23: -0.2022
REMARK 3 S TENSOR
REMARK 3 S11: -0.0786 S12: 0.0087 S13: 0.0307
REMARK 3 S21: -0.0544 S22: 0.0768 S23: 0.0328
REMARK 3 S31: -0.0447 S32: -0.0580 S33: 0.0017
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 9BLD 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_1000283645.
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 : 113000
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.670
REMARK 200 RESOLUTION RANGE LOW (A) : 74.545
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 13.40
REMARK 200 R MERGE (I) : 0.12300
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 11.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.67
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.70
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 12.70
REMARK 200 R MERGE FOR SHELL (I) : 3.78500
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 0.800
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 (%): 46.54
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.30
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M SODIUM FORMATE, 0.1 M OF BIS
REMARK 280 -TRIS PROPANE PH 7.5, AND 20% W/V OF PEG 3350, VAPOR DIFFUSION,
REMARK 280 SITTING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-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 38.69250
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 71.62250
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 43.64900
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 71.62250
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 38.69250
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 43.64900
REMARK 290 SMTRY3 4 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: 2490 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 18340 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -6.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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: 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: 2340 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 18310 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -6.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, 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 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 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 C -4
REMARK 465 HIS C -3
REMARK 465 HIS C -2
REMARK 465 HIS C -1
REMARK 465 HIS C 0
REMARK 465 MET C 1
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 MET A 1 CG SD CE
REMARK 470 LYS A 8 CE NZ
REMARK 470 LYS A 25 CE NZ
REMARK 470 GLN A 78 CG CD OE1 NE2
REMARK 470 MET B 1 CG SD CE
REMARK 470 LYS B 25 CE NZ
REMARK 470 LYS B 65 CD CE NZ
REMARK 470 PHE B 172 CE2 CZ
REMARK 470 PHE C 23 CE1 CE2 CZ
REMARK 470 LYS C 25 CD CE NZ
REMARK 470 GLN C 78 CG CD OE1 NE2
REMARK 470 MET D 1 CG SD CE
REMARK 470 GLN D 78 CG CD OE1 NE2
REMARK 470 GLN D 83 CG 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 227 O HOH C 301 2.13
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 PHE A 23 -43.23 70.93
REMARK 500 GLN A 83 -33.94 -137.51
REMARK 500 CYS A 121 -122.51 64.80
REMARK 500 CYS A 121 -122.16 64.41
REMARK 500 PHE A 134 54.38 -112.96
REMARK 500 CYS B 121 -122.31 63.73
REMARK 500 CYS B 121 -122.56 63.97
REMARK 500 PHE B 134 56.95 -113.21
REMARK 500 GLN C 83 -31.73 -136.88
REMARK 500 CYS C 121 -122.27 64.50
REMARK 500 CYS C 121 -121.86 64.05
REMARK 500 PHE C 134 55.13 -111.77
REMARK 500 TYR C 145 55.80 39.96
REMARK 500 PHE D 23 -5.99 78.20
REMARK 500 GLN D 83 -30.61 -134.28
REMARK 500 CYS D 121 -122.77 63.87
REMARK 500 CYS D 121 -122.80 64.02
REMARK 500 PHE D 134 52.76 -112.15
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 D 75 0.13 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 473 DISTANCE = 5.85 ANGSTROMS
REMARK 525 HOH B 496 DISTANCE = 6.18 ANGSTROMS
REMARK 525 HOH C 502 DISTANCE = 6.03 ANGSTROMS
REMARK 525 HOH D 497 DISTANCE = 5.88 ANGSTROMS
DBREF 9BLD A 1 234 UNP D3DKA9 D3DKA9_HYDTT 1 234
DBREF 9BLD B 1 234 UNP D3DKA9 D3DKA9_HYDTT 1 234
DBREF 9BLD C 1 234 UNP D3DKA9 D3DKA9_HYDTT 1 234
DBREF 9BLD D 1 234 UNP D3DKA9 D3DKA9_HYDTT 1 234
SEQADV 9BLD HIS A -5 UNP D3DKA9 EXPRESSION TAG
SEQADV 9BLD HIS A -4 UNP D3DKA9 EXPRESSION TAG
SEQADV 9BLD HIS A -3 UNP D3DKA9 EXPRESSION TAG
SEQADV 9BLD HIS A -2 UNP D3DKA9 EXPRESSION TAG
SEQADV 9BLD HIS A -1 UNP D3DKA9 EXPRESSION TAG
SEQADV 9BLD HIS A 0 UNP D3DKA9 EXPRESSION TAG
SEQADV 9BLD HIS B -5 UNP D3DKA9 EXPRESSION TAG
SEQADV 9BLD HIS B -4 UNP D3DKA9 EXPRESSION TAG
SEQADV 9BLD HIS B -3 UNP D3DKA9 EXPRESSION TAG
SEQADV 9BLD HIS B -2 UNP D3DKA9 EXPRESSION TAG
SEQADV 9BLD HIS B -1 UNP D3DKA9 EXPRESSION TAG
SEQADV 9BLD HIS B 0 UNP D3DKA9 EXPRESSION TAG
SEQADV 9BLD HIS C -5 UNP D3DKA9 EXPRESSION TAG
SEQADV 9BLD HIS C -4 UNP D3DKA9 EXPRESSION TAG
SEQADV 9BLD HIS C -3 UNP D3DKA9 EXPRESSION TAG
SEQADV 9BLD HIS C -2 UNP D3DKA9 EXPRESSION TAG
SEQADV 9BLD HIS C -1 UNP D3DKA9 EXPRESSION TAG
SEQADV 9BLD HIS C 0 UNP D3DKA9 EXPRESSION TAG
SEQADV 9BLD HIS D -5 UNP D3DKA9 EXPRESSION TAG
SEQADV 9BLD HIS D -4 UNP D3DKA9 EXPRESSION TAG
SEQADV 9BLD HIS D -3 UNP D3DKA9 EXPRESSION TAG
SEQADV 9BLD HIS D -2 UNP D3DKA9 EXPRESSION TAG
SEQADV 9BLD HIS D -1 UNP D3DKA9 EXPRESSION TAG
SEQADV 9BLD 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 *768(H2 O)
HELIX 1 AA1 VAL A 39 GLU A 52 1 14
HELIX 2 AA2 ASN A 69 GLN A 83 1 15
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 GLN C 83 1 15
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 PRO D 21 LYS D 25 5 5
HELIX 23 AC5 VAL D 39 GLU D 52 1 14
HELIX 24 AC6 ASN D 69 GLN D 83 1 15
HELIX 25 AC7 ARG D 84 ASN D 102 1 19
HELIX 26 AC8 CYS D 121 PHE D 134 1 14
HELIX 27 AC9 ASP D 154 ILE D 158 5 5
HELIX 28 AD1 PRO D 174 GLY D 189 1 16
HELIX 29 AD2 ASN D 214 THR D 234 1 21
SHEET 1 AA1 6 GLY A 2 LYS A 9 0
SHEET 2 AA1 6 VAL A 12 ALA A 19 -1 O GLY A 16 N LEU A 5
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 31 O PHE A 57
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 4 VAL A 162 ALA A 167 0
SHEET 2 AA3 4 ALA A 192 TYR A 197 1 O LEU A 195 N HIS A 166
SHEET 3 AA3 4 ALA B 192 TYR B 197 -1 O PHE B 194 N ILE A 196
SHEET 4 AA3 4 VAL B 162 ALA B 167 1 N HIS B 166 O LEU B 195
SHEET 1 AA4 6 ARG B 3 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 6 ARG C 3 LYS C 9 0
SHEET 2 AA6 6 VAL C 12 ALA C 19 -1 O ILE C 14 N PHE C 7
SHEET 3 AA6 6 PHE C 55 ILE C 59 -1 O GLY C 58 N TYR C 17
SHEET 4 AA6 6 LEU C 28 ILE C 32 1 N VAL C 31 O PHE C 57
SHEET 5 AA6 6 ILE C 115 PHE C 120 1 O GLY C 116 N LEU C 28
SHEET 6 AA6 6 ALA C 140 TYR C 144 1 O TYR C 144 N GLY C 119
SHEET 1 AA7 2 PHE C 106 VAL C 107 0
SHEET 2 AA7 2 ASP C 112 TYR C 113 -1 O ASP C 112 N VAL C 107
SHEET 1 AA8 4 VAL C 162 ALA C 167 0
SHEET 2 AA8 4 ALA C 192 TYR C 197 1 O LEU C 195 N HIS C 166
SHEET 3 AA8 4 ALA D 192 TYR D 197 -1 O PHE D 194 N ILE C 196
SHEET 4 AA8 4 VAL D 162 ALA D 167 1 N HIS D 166 O LEU D 195
SHEET 1 AA9 6 ARG D 3 LYS D 9 0
SHEET 2 AA9 6 VAL D 12 ALA D 19 -1 O LEU D 18 N ARG D 3
SHEET 3 AA9 6 PHE D 55 ILE D 59 -1 O GLY D 58 N TYR D 17
SHEET 4 AA9 6 LEU D 28 ILE D 32 1 N VAL D 31 O PHE D 57
SHEET 5 AA9 6 ILE D 115 PHE D 120 1 O GLY D 116 N LEU D 28
SHEET 6 AA9 6 ALA D 140 TYR D 144 1 O TYR D 144 N GLY D 119
SHEET 1 AB1 2 PHE D 106 VAL D 107 0
SHEET 2 AB1 2 ASP D 112 TYR D 113 -1 O ASP D 112 N VAL D 107
CRYST1 77.385 87.298 143.245 90.00 90.00 90.00 P 21 21 21 16
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 0.012922 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011455 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006981 0.00000
TER 1880 THR A 234
TER 3750 THR B 234
TER 5617 THR C 234
TER 7515 THR D 234
MASTER 705 0 0 29 40 0 0 6 8178 4 0 76
END |