HEADER HORMONE RECEPTOR 18-FEB-12 4DSC
TITLE COMPLEX STRUCTURE OF ABSCISIC ACID RECEPTOR PYL3 WITH (+)-ABA IN
TITLE 2 SPACEGROUP OF H32 AT 1.95A
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ABSCISIC ACID RECEPTOR PYL3;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: UNP RESIDUES 25-209;
COMPND 5 SYNONYM: PYR1-LIKE PROTEIN 3, REGULATORY COMPONENTS OF ABA RECEPTOR
COMPND 6 13;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ARABIDOPSIS THALIANA;
SOURCE 3 ORGANISM_COMMON: MOUSE-EAR CRESS;
SOURCE 4 ORGANISM_TAXID: 3702;
SOURCE 5 GENE: AT1G73000, PYL3;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: ROSETTA 2 (DE3) CELLS;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PGEX 4T-2
KEYWDS ABSCISIC ACID RECEPTOR, ABA, PYL3, HORMONE RECEPTOR
EXPDTA X-RAY DIFFRACTION
AUTHOR X.ZHANG,Z.CHEN
REVDAT 2 08-NOV-23 4DSC 1 REMARK SEQADV HETSYN LINK
REVDAT 1 06-JUN-12 4DSC 0
JRNL AUTH X.ZHANG,Q.ZHANG,Q.XIN,L.YU,Z.WANG,W.WU,L.JIANG,G.WANG,
JRNL AUTH 2 W.TIAN,Z.DENG,Y.WANG,Z.LIU,J.LONG,Z.GONG,Z.CHEN
JRNL TITL COMPLEX STRUCTURES OF THE ABSCISIC ACID RECEPTOR PYL3/RCAR13
JRNL TITL 2 REVEAL A UNIQUE REGULATORY MECHANISM
JRNL REF STRUCTURE V. 20 780 2012
JRNL REFN ISSN 0969-2126
JRNL PMID 22579247
JRNL DOI 10.1016/J.STR.2012.02.019
REMARK 2
REMARK 2 RESOLUTION. 1.95 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.6.0117
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.95
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 38.81
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 37938
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.186
REMARK 3 R VALUE (WORKING SET) : 0.185
REMARK 3 FREE R VALUE : 0.211
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1997
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) : 1.95
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.00
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2707
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.48
REMARK 3 BIN R VALUE (WORKING SET) : 0.2200
REMARK 3 BIN FREE R VALUE SET COUNT : 139
REMARK 3 BIN FREE R VALUE : 0.2800
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2653
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 40
REMARK 3 SOLVENT ATOMS : 607
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 31.88
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.74000
REMARK 3 B22 (A**2) : 0.74000
REMARK 3 B33 (A**2) : -1.11000
REMARK 3 B12 (A**2) : 0.37000
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): 0.236
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.124
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.084
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.482
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.948
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.936
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2767 ; 0.009 ; 0.020
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3783 ; 1.323 ; 1.955
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 355 ; 5.209 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 107 ;33.696 ;23.364
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 427 ;12.621 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 17 ;17.117 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 465 ; 0.261 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2060 ; 0.005 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
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): 2767 ; 3.435 ; 3.000
REMARK 3 SPHERICITY; FREE ATOMS (A**2): 117 ;25.248 ; 5.000
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): 3208 ;14.228 ; 5.000
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 20
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 26 A 46
REMARK 3 ORIGIN FOR THE GROUP (A): 47.8795 -42.3219 27.1460
REMARK 3 T TENSOR
REMARK 3 T11: 0.2709 T22: 0.1784
REMARK 3 T33: 0.1457 T12: 0.0347
REMARK 3 T13: -0.0430 T23: 0.0183
REMARK 3 L TENSOR
REMARK 3 L11: 4.4400 L22: 2.8782
REMARK 3 L33: 0.1559 L12: 1.4083
REMARK 3 L13: -0.3452 L23: -0.2728
REMARK 3 S TENSOR
REMARK 3 S11: -0.0710 S12: -0.0429 S13: -0.3024
REMARK 3 S21: 0.0421 S22: 0.0680 S23: -0.2850
REMARK 3 S31: 0.1784 S32: 0.0066 S33: 0.0030
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 47 A 67
REMARK 3 ORIGIN FOR THE GROUP (A): 44.3166 -32.0812 23.4816
REMARK 3 T TENSOR
REMARK 3 T11: 0.1685 T22: 0.1644
REMARK 3 T33: 0.1502 T12: 0.0086
REMARK 3 T13: -0.0087 T23: 0.0139
REMARK 3 L TENSOR
REMARK 3 L11: 0.6432 L22: 1.5875
REMARK 3 L33: 0.6669 L12: 0.4024
REMARK 3 L13: -0.0569 L23: 0.3945
REMARK 3 S TENSOR
REMARK 3 S11: 0.0105 S12: -0.0041 S13: -0.0076
REMARK 3 S21: -0.0564 S22: 0.0369 S23: -0.0582
REMARK 3 S31: 0.0019 S32: 0.0309 S33: -0.0474
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 68 A 88
REMARK 3 ORIGIN FOR THE GROUP (A): 31.3923 -24.6164 21.8240
REMARK 3 T TENSOR
REMARK 3 T11: 0.1505 T22: 0.1601
REMARK 3 T33: 0.1599 T12: -0.0040
REMARK 3 T13: 0.0023 T23: 0.0020
REMARK 3 L TENSOR
REMARK 3 L11: 0.4854 L22: 0.7204
REMARK 3 L33: 1.0475 L12: -0.0643
REMARK 3 L13: -0.6923 L23: -0.1017
REMARK 3 S TENSOR
REMARK 3 S11: 0.0110 S12: 0.0458 S13: 0.0226
REMARK 3 S21: 0.0150 S22: 0.0145 S23: 0.0853
REMARK 3 S31: -0.0256 S32: -0.0825 S33: -0.0255
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 89 A 99
REMARK 3 ORIGIN FOR THE GROUP (A): 25.5399 -28.6997 33.6521
REMARK 3 T TENSOR
REMARK 3 T11: 0.2008 T22: 0.1706
REMARK 3 T33: 0.1951 T12: -0.0017
REMARK 3 T13: -0.0069 T23: -0.0181
REMARK 3 L TENSOR
REMARK 3 L11: 4.6500 L22: 1.1446
REMARK 3 L33: 1.0801 L12: 2.3069
REMARK 3 L13: 1.3900 L23: 0.6957
REMARK 3 S TENSOR
REMARK 3 S11: -0.0943 S12: -0.0184 S13: 0.2955
REMARK 3 S21: -0.0496 S22: -0.0090 S23: 0.1499
REMARK 3 S31: -0.2198 S32: -0.0379 S33: 0.1033
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 100 A 120
REMARK 3 ORIGIN FOR THE GROUP (A): 26.3249 -31.0312 18.0641
REMARK 3 T TENSOR
REMARK 3 T11: 0.1622 T22: 0.1684
REMARK 3 T33: 0.1617 T12: -0.0024
REMARK 3 T13: 0.0027 T23: -0.0044
REMARK 3 L TENSOR
REMARK 3 L11: 1.0917 L22: 0.6139
REMARK 3 L33: 1.3763 L12: 0.2945
REMARK 3 L13: 0.0516 L23: -0.1317
REMARK 3 S TENSOR
REMARK 3 S11: 0.0014 S12: 0.0791 S13: -0.0131
REMARK 3 S21: -0.0572 S22: 0.0330 S23: 0.0509
REMARK 3 S31: 0.0952 S32: -0.1477 S33: -0.0344
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 121 A 137
REMARK 3 ORIGIN FOR THE GROUP (A): 35.0929 -34.5721 30.1503
REMARK 3 T TENSOR
REMARK 3 T11: 0.1750 T22: 0.1808
REMARK 3 T33: 0.1716 T12: -0.0006
REMARK 3 T13: 0.0047 T23: 0.0015
REMARK 3 L TENSOR
REMARK 3 L11: 0.8828 L22: 0.3520
REMARK 3 L33: 1.7672 L12: 0.5144
REMARK 3 L13: 1.0013 L23: 0.5221
REMARK 3 S TENSOR
REMARK 3 S11: -0.0056 S12: -0.0712 S13: -0.0408
REMARK 3 S21: 0.0640 S22: 0.0021 S23: -0.0060
REMARK 3 S31: 0.0382 S32: -0.0506 S33: 0.0035
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 138 A 143
REMARK 3 ORIGIN FOR THE GROUP (A): 27.0981 -39.9128 14.1347
REMARK 3 T TENSOR
REMARK 3 T11: 0.5438 T22: 0.5256
REMARK 3 T33: 0.5696 T12: -0.0934
REMARK 3 T13: 0.1357 T23: -0.0647
REMARK 3 L TENSOR
REMARK 3 L11: 3.5924 L22: 2.6932
REMARK 3 L33: 20.0935 L12: 3.1093
REMARK 3 L13: -8.4935 L23: -7.3511
REMARK 3 S TENSOR
REMARK 3 S11: -0.8962 S12: 0.2071 S13: -0.5768
REMARK 3 S21: -0.4916 S22: -0.1297 S23: -0.5024
REMARK 3 S31: 1.3966 S32: -0.5459 S33: 1.0259
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 : A 144 A 162
REMARK 3 ORIGIN FOR THE GROUP (A): 47.1239 -31.7870 27.5018
REMARK 3 T TENSOR
REMARK 3 T11: 0.1723 T22: 0.1887
REMARK 3 T33: 0.1722 T12: -0.0009
REMARK 3 T13: 0.0061 T23: 0.0064
REMARK 3 L TENSOR
REMARK 3 L11: 0.5695 L22: 0.2051
REMARK 3 L33: 0.4451 L12: -0.3139
REMARK 3 L13: 0.0945 L23: 0.0648
REMARK 3 S TENSOR
REMARK 3 S11: 0.0474 S12: 0.0280 S13: 0.0241
REMARK 3 S21: -0.0048 S22: 0.0051 S23: -0.0298
REMARK 3 S31: 0.1050 S32: 0.0876 S33: -0.0524
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 : A 163 A 176
REMARK 3 ORIGIN FOR THE GROUP (A): 44.5480 -35.1679 22.0184
REMARK 3 T TENSOR
REMARK 3 T11: 0.1651 T22: 0.1634
REMARK 3 T33: 0.1609 T12: -0.0084
REMARK 3 T13: -0.0031 T23: -0.0054
REMARK 3 L TENSOR
REMARK 3 L11: 1.1056 L22: 1.0965
REMARK 3 L33: 0.7223 L12: 0.5435
REMARK 3 L13: 0.5796 L23: 0.6459
REMARK 3 S TENSOR
REMARK 3 S11: 0.0332 S12: 0.0102 S13: -0.1013
REMARK 3 S21: 0.0225 S22: 0.0106 S23: -0.0778
REMARK 3 S31: 0.0934 S32: 0.0581 S33: -0.0438
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 : A 177 A 188
REMARK 3 ORIGIN FOR THE GROUP (A): 37.4986 -43.7781 7.5285
REMARK 3 T TENSOR
REMARK 3 T11: 0.5317 T22: 0.3136
REMARK 3 T33: 0.1150 T12: -0.2961
REMARK 3 T13: -0.1666 T23: 0.0297
REMARK 3 L TENSOR
REMARK 3 L11: 3.5428 L22: 10.1672
REMARK 3 L33: 7.4106 L12: 2.4382
REMARK 3 L13: 3.7742 L23: 7.3929
REMARK 3 S TENSOR
REMARK 3 S11: -0.3717 S12: 0.4016 S13: -0.0766
REMARK 3 S21: -1.0221 S22: 0.5120 S23: 0.2428
REMARK 3 S31: -0.3669 S32: 0.2802 S33: -0.1402
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 : A 189 A 202
REMARK 3 ORIGIN FOR THE GROUP (A): 42.2692 -28.7854 15.8505
REMARK 3 T TENSOR
REMARK 3 T11: 0.1361 T22: 0.1528
REMARK 3 T33: 0.1428 T12: -0.0027
REMARK 3 T13: 0.0026 T23: 0.0041
REMARK 3 L TENSOR
REMARK 3 L11: 0.1222 L22: 3.4577
REMARK 3 L33: 1.6998 L12: -0.6294
REMARK 3 L13: -0.1839 L23: 0.4643
REMARK 3 S TENSOR
REMARK 3 S11: 0.0083 S12: -0.0013 S13: 0.0008
REMARK 3 S21: -0.0608 S22: 0.0203 S23: -0.0785
REMARK 3 S31: 0.0743 S32: 0.0186 S33: -0.0286
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 : A 203 A 209
REMARK 3 ORIGIN FOR THE GROUP (A): 47.9589 -14.7576 22.8547
REMARK 3 T TENSOR
REMARK 3 T11: 0.3154 T22: 0.2018
REMARK 3 T33: 0.3381 T12: -0.0371
REMARK 3 T13: 0.0199 T23: 0.0115
REMARK 3 L TENSOR
REMARK 3 L11: 10.1506 L22: 5.9925
REMARK 3 L33: 3.4952 L12: 6.8371
REMARK 3 L13: 2.2326 L23: 3.5434
REMARK 3 S TENSOR
REMARK 3 S11: -0.1941 S12: 0.4437 S13: 1.1718
REMARK 3 S21: -0.4691 S22: 0.5632 S23: 0.3658
REMARK 3 S31: -0.5414 S32: 0.4498 S33: -0.3690
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 22 B 45
REMARK 3 ORIGIN FOR THE GROUP (A): 59.6928 -22.9603 -1.8351
REMARK 3 T TENSOR
REMARK 3 T11: 0.1639 T22: 0.1799
REMARK 3 T33: 0.1678 T12: -0.0031
REMARK 3 T13: 0.0009 T23: 0.0084
REMARK 3 L TENSOR
REMARK 3 L11: 0.7554 L22: 2.8138
REMARK 3 L33: 0.5172 L12: -1.1138
REMARK 3 L13: -0.0671 L23: -0.3271
REMARK 3 S TENSOR
REMARK 3 S11: 0.0210 S12: 0.0030 S13: 0.0608
REMARK 3 S21: 0.0247 S22: -0.0361 S23: -0.1187
REMARK 3 S31: 0.0025 S32: 0.0284 S33: 0.0150
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 46 B 67
REMARK 3 ORIGIN FOR THE GROUP (A): 49.7039 -22.1014 2.1494
REMARK 3 T TENSOR
REMARK 3 T11: 0.1463 T22: 0.1700
REMARK 3 T33: 0.1442 T12: 0.0091
REMARK 3 T13: 0.0208 T23: -0.0069
REMARK 3 L TENSOR
REMARK 3 L11: 0.7933 L22: 1.3504
REMARK 3 L33: 0.6056 L12: 0.4233
REMARK 3 L13: 0.2689 L23: -0.1434
REMARK 3 S TENSOR
REMARK 3 S11: 0.0772 S12: -0.0558 S13: -0.0461
REMARK 3 S21: 0.0461 S22: -0.0368 S23: -0.0770
REMARK 3 S31: 0.0579 S32: -0.0258 S33: -0.0404
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 : B 68 B 87
REMARK 3 ORIGIN FOR THE GROUP (A): 36.8903 -15.8862 4.3813
REMARK 3 T TENSOR
REMARK 3 T11: 0.1407 T22: 0.1508
REMARK 3 T33: 0.1628 T12: -0.0096
REMARK 3 T13: -0.0015 T23: -0.0034
REMARK 3 L TENSOR
REMARK 3 L11: 0.6013 L22: 0.9151
REMARK 3 L33: 1.5463 L12: -0.5638
REMARK 3 L13: -0.1763 L23: -0.5210
REMARK 3 S TENSOR
REMARK 3 S11: 0.0009 S12: 0.0145 S13: 0.0470
REMARK 3 S21: 0.0105 S22: 0.0019 S23: 0.0514
REMARK 3 S31: -0.0402 S32: -0.1132 S33: -0.0029
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 : B 88 B 135
REMARK 3 ORIGIN FOR THE GROUP (A): 41.9025 -9.7896 0.5847
REMARK 3 T TENSOR
REMARK 3 T11: 0.1553 T22: 0.1508
REMARK 3 T33: 0.1583 T12: -0.0036
REMARK 3 T13: -0.0019 T23: 0.0092
REMARK 3 L TENSOR
REMARK 3 L11: 0.5621 L22: 0.9623
REMARK 3 L33: 0.9002 L12: -0.1808
REMARK 3 L13: -0.1067 L23: 0.2296
REMARK 3 S TENSOR
REMARK 3 S11: 0.0092 S12: 0.0105 S13: 0.0229
REMARK 3 S21: -0.0444 S22: 0.0036 S23: -0.0304
REMARK 3 S31: -0.0599 S32: 0.0043 S33: -0.0128
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 : B 136 B 145
REMARK 3 ORIGIN FOR THE GROUP (A): 48.7173 -5.2547 10.2520
REMARK 3 T TENSOR
REMARK 3 T11: 0.1962 T22: 0.2108
REMARK 3 T33: 0.1909 T12: -0.0122
REMARK 3 T13: -0.0266 T23: -0.0304
REMARK 3 L TENSOR
REMARK 3 L11: 4.6333 L22: 1.9251
REMARK 3 L33: 1.3207 L12: -1.8956
REMARK 3 L13: -2.0572 L23: 0.1586
REMARK 3 S TENSOR
REMARK 3 S11: -0.0144 S12: -0.3076 S13: 0.3273
REMARK 3 S21: 0.1132 S22: 0.1006 S23: -0.2430
REMARK 3 S31: -0.0622 S32: 0.1665 S33: -0.0862
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 : B 146 B 176
REMARK 3 ORIGIN FOR THE GROUP (A): 51.7938 -24.2253 0.6644
REMARK 3 T TENSOR
REMARK 3 T11: 0.1491 T22: 0.1611
REMARK 3 T33: 0.1590 T12: -0.0001
REMARK 3 T13: -0.0031 T23: -0.0015
REMARK 3 L TENSOR
REMARK 3 L11: 0.7227 L22: 0.6341
REMARK 3 L33: 0.3601 L12: -0.0019
REMARK 3 L13: -0.0745 L23: -0.1996
REMARK 3 S TENSOR
REMARK 3 S11: -0.0241 S12: 0.0051 S13: -0.0352
REMARK 3 S21: -0.0730 S22: -0.0080 S23: -0.1055
REMARK 3 S31: 0.0766 S32: 0.0727 S33: 0.0321
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 : B 177 B 189
REMARK 3 ORIGIN FOR THE GROUP (A): 56.6234 -11.7834 17.6437
REMARK 3 T TENSOR
REMARK 3 T11: 0.1911 T22: 0.2993
REMARK 3 T33: 0.1561 T12: 0.0244
REMARK 3 T13: -0.0168 T23: -0.0164
REMARK 3 L TENSOR
REMARK 3 L11: 3.1500 L22: 6.7088
REMARK 3 L33: 4.1415 L12: 4.5473
REMARK 3 L13: 0.8827 L23: 0.7609
REMARK 3 S TENSOR
REMARK 3 S11: 0.1774 S12: -0.2933 S13: -0.0171
REMARK 3 S21: 0.3107 S22: -0.2977 S23: -0.0432
REMARK 3 S31: -0.0522 S32: 0.0444 S33: 0.1203
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 : B 190 B 207
REMARK 3 ORIGIN FOR THE GROUP (A): 43.3862 -25.5034 7.9310
REMARK 3 T TENSOR
REMARK 3 T11: 0.1406 T22: 0.1326
REMARK 3 T33: 0.1354 T12: 0.0120
REMARK 3 T13: 0.0093 T23: 0.0062
REMARK 3 L TENSOR
REMARK 3 L11: 2.5316 L22: 3.4016
REMARK 3 L33: 2.4282 L12: 1.8180
REMARK 3 L13: 0.9498 L23: 1.1118
REMARK 3 S TENSOR
REMARK 3 S11: 0.0293 S12: -0.0108 S13: -0.1025
REMARK 3 S21: -0.0078 S22: 0.0057 S23: -0.0432
REMARK 3 S31: 0.0924 S32: -0.0476 S33: -0.0350
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH MASK
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 USED IF PRESENT IN
REMARK 3 THE INPUT U VALUES: WITH TLS ADDED
REMARK 4
REMARK 4 4DSC COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 22-FEB-12.
REMARK 100 THE DEPOSITION ID IS D_1000070720.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 29-APR-10
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : BSRF
REMARK 200 BEAMLINE : 1W2B
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 39972
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.950
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 5.800
REMARK 200 R MERGE (I) : 0.09600
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) : 1.95
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.98
REMARK 200 COMPLETENESS FOR SHELL (%) : 4.9
REMARK 200 DATA REDUNDANCY IN SHELL : 5.80
REMARK 200 R MERGE FOR SHELL (I) : 0.46900
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: PHASER
REMARK 200 STARTING MODEL: 3KLX
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 62.43
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.27
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.6M (NH)2SO4, 0.1M HEPES, PH 7.6,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: H 3 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z
REMARK 290 3555 -X+Y,-X,Z
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z
REMARK 290 6555 -X,-X+Y,-Z
REMARK 290 7555 X+2/3,Y+1/3,Z+1/3
REMARK 290 8555 -Y+2/3,X-Y+1/3,Z+1/3
REMARK 290 9555 -X+Y+2/3,-X+1/3,Z+1/3
REMARK 290 10555 Y+2/3,X+1/3,-Z+1/3
REMARK 290 11555 X-Y+2/3,-Y+1/3,-Z+1/3
REMARK 290 12555 -X+2/3,-X+Y+1/3,-Z+1/3
REMARK 290 13555 X+1/3,Y+2/3,Z+2/3
REMARK 290 14555 -Y+1/3,X-Y+2/3,Z+2/3
REMARK 290 15555 -X+Y+1/3,-X+2/3,Z+2/3
REMARK 290 16555 Y+1/3,X+2/3,-Z+2/3
REMARK 290 17555 X-Y+1/3,-Y+2/3,-Z+2/3
REMARK 290 18555 -X+1/3,-X+Y+2/3,-Z+2/3
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 0.00000
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 0.00000
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 0.00000
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 0.00000
REMARK 290 SMTRY1 7 1.000000 0.000000 0.000000 116.41800
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 67.21396
REMARK 290 SMTRY3 7 0.000000 0.000000 1.000000 17.76400
REMARK 290 SMTRY1 8 -0.500000 -0.866025 0.000000 116.41800
REMARK 290 SMTRY2 8 0.866025 -0.500000 0.000000 67.21396
REMARK 290 SMTRY3 8 0.000000 0.000000 1.000000 17.76400
REMARK 290 SMTRY1 9 -0.500000 0.866025 0.000000 116.41800
REMARK 290 SMTRY2 9 -0.866025 -0.500000 0.000000 67.21396
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 17.76400
REMARK 290 SMTRY1 10 -0.500000 0.866025 0.000000 116.41800
REMARK 290 SMTRY2 10 0.866025 0.500000 0.000000 67.21396
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 17.76400
REMARK 290 SMTRY1 11 1.000000 0.000000 0.000000 116.41800
REMARK 290 SMTRY2 11 0.000000 -1.000000 0.000000 67.21396
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 17.76400
REMARK 290 SMTRY1 12 -0.500000 -0.866025 0.000000 116.41800
REMARK 290 SMTRY2 12 -0.866025 0.500000 0.000000 67.21396
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 17.76400
REMARK 290 SMTRY1 13 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 134.42793
REMARK 290 SMTRY3 13 0.000000 0.000000 1.000000 35.52800
REMARK 290 SMTRY1 14 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 14 0.866025 -0.500000 0.000000 134.42793
REMARK 290 SMTRY3 14 0.000000 0.000000 1.000000 35.52800
REMARK 290 SMTRY1 15 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 15 -0.866025 -0.500000 0.000000 134.42793
REMARK 290 SMTRY3 15 0.000000 0.000000 1.000000 35.52800
REMARK 290 SMTRY1 16 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 16 0.866025 0.500000 0.000000 134.42793
REMARK 290 SMTRY3 16 0.000000 0.000000 -1.000000 35.52800
REMARK 290 SMTRY1 17 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 17 0.000000 -1.000000 0.000000 134.42793
REMARK 290 SMTRY3 17 0.000000 0.000000 -1.000000 35.52800
REMARK 290 SMTRY1 18 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 18 -0.866025 0.500000 0.000000 134.42793
REMARK 290 SMTRY3 18 0.000000 0.000000 -1.000000 35.52800
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 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: 2380 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 16100 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -36.0 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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH B 485 LIES ON A SPECIAL POSITION.
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 GLY A 22
REMARK 465 HIS A 23
REMARK 465 MET A 24
REMARK 465 LEU A 25
REMARK 465 GLY A 91
REMARK 465 ASN A 92
REMARK 465 GLY A 93
REMARK 465 ILE A 94
REMARK 465 LYS A 95
REMARK 465 LEU A 156
REMARK 465 GLU A 157
REMARK 465 LYS A 158
REMARK 465 ASP A 159
REMARK 465 LYS A 160
REMARK 465 LYS A 161
REMARK 465 GLY B 91
REMARK 465 ASN B 92
REMARK 465 GLY B 93
REMARK 465 LYS B 158
REMARK 465 ASP B 159
REMARK 465 LYS B 160
REMARK 465 LYS B 161
REMARK 465 LYS B 162
REMARK 465 PRO B 208
REMARK 465 THR B 209
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 LYS A 27 CG CD CE NZ
REMARK 470 ASP A 28 CG OD1 OD2
REMARK 470 GLU A 29 CG CD OE1 OE2
REMARK 470 PHE A 30 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 SER A 31 OG
REMARK 470 ASP A 34 OD2
REMARK 470 SER A 35 OG
REMARK 470 ARG A 38 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 45 NE CZ NH1 NH2
REMARK 470 ILE A 54 CD1
REMARK 470 LYS A 98 CG CD CE NZ
REMARK 470 ARG A 133 CZ NH1 NH2
REMARK 470 GLU A 138 CD OE1 OE2
REMARK 470 ARG A 140 CG CD NE CZ NH1 NH2
REMARK 470 LEU A 141 CD1
REMARK 470 ARG A 145 CG CD NE CZ NH1 NH2
REMARK 470 VAL A 154 CG1 CG2
REMARK 470 LYS A 162 CE NZ
REMARK 470 ARG A 163 CZ NH1 NH2
REMARK 470 GLN A 178 OE1 NE2
REMARK 470 GLU A 183 CG CD OE1 OE2
REMARK 470 LYS A 194 CD CE NZ
REMARK 470 SER A 207 O
REMARK 470 THR A 209 OG1 CG2
REMARK 470 HIS B 23 CG ND1 CD2 CE1 NE2
REMARK 470 MET B 24 CG SD CE
REMARK 470 LYS B 27 CG CD CE NZ
REMARK 470 SER B 31 OG
REMARK 470 ARG B 38 NE CZ NH1 NH2
REMARK 470 ARG B 45 CG CD NE CZ NH1 NH2
REMARK 470 SER B 46 OG
REMARK 470 ASN B 48 ND2
REMARK 470 ILE B 54 CD1
REMARK 470 LYS B 83 CE NZ
REMARK 470 ILE B 94 CG1 CG2 CD1
REMARK 470 LYS B 95 CG CD CE NZ
REMARK 470 GLU B 96 CD OE1 OE2
REMARK 470 LYS B 98 CD CE NZ
REMARK 470 GLU B 138 CD OE1 OE2
REMARK 470 LEU B 141 CG CD1 CD2
REMARK 470 VAL B 154 CG1 CG2
REMARK 470 VAL B 155 CG1 CG2
REMARK 470 LEU B 156 CG CD1 CD2
REMARK 470 GLU B 157 CG CD OE1 OE2
REMARK 470 ARG B 163 CG CD NE CZ NH1 NH2
REMARK 470 GLN B 178 OE1 NE2
REMARK 470 GLU B 183 CD OE1 OE2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 LEU A 141 72.68 -112.22
REMARK 500 LEU B 141 63.46 -100.92
REMARK 500 LEU B 156 -98.18 -82.63
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 302 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 TYR A 144 OH
REMARK 620 2 SER A 146 OG 95.3
REMARK 620 3 GLU A 170 OE1 104.3 117.6
REMARK 620 4 A8S A 301 O12 109.6 127.8 100.1
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B 302 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 TYR B 144 OH
REMARK 620 2 SER B 146 OG 95.5
REMARK 620 3 GLU B 170 OE1 106.4 114.9
REMARK 620 4 A8S B 301 O12 112.4 126.8 99.9
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE A8S A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE A8S B 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 302
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3KLX RELATED DB: PDB
REMARK 900 RELATED ID: 3OJI RELATED DB: PDB
REMARK 900 RELATED ID: 4DS8 RELATED DB: PDB
REMARK 900 RELATED ID: 4DSB RELATED DB: PDB
DBREF 4DSC A 25 209 UNP Q9SSM7 PYL3_ARATH 25 209
DBREF 4DSC B 25 209 UNP Q9SSM7 PYL3_ARATH 25 209
SEQADV 4DSC GLY A 22 UNP Q9SSM7 EXPRESSION TAG
SEQADV 4DSC HIS A 23 UNP Q9SSM7 EXPRESSION TAG
SEQADV 4DSC MET A 24 UNP Q9SSM7 EXPRESSION TAG
SEQADV 4DSC GLY B 22 UNP Q9SSM7 EXPRESSION TAG
SEQADV 4DSC HIS B 23 UNP Q9SSM7 EXPRESSION TAG
SEQADV 4DSC MET B 24 UNP Q9SSM7 EXPRESSION TAG
SEQRES 1 A 188 GLY HIS MET LEU THR LYS ASP GLU PHE SER THR LEU ASP
SEQRES 2 A 188 SER ILE ILE ARG THR HIS HIS THR PHE PRO ARG SER PRO
SEQRES 3 A 188 ASN THR CYS THR SER LEU ILE ALA HIS ARG VAL ASP ALA
SEQRES 4 A 188 PRO ALA HIS ALA ILE TRP ARG PHE VAL ARG ASP PHE ALA
SEQRES 5 A 188 ASN PRO ASN LYS TYR LYS HIS PHE ILE LYS SER CYS THR
SEQRES 6 A 188 ILE ARG VAL ASN GLY ASN GLY ILE LYS GLU ILE LYS VAL
SEQRES 7 A 188 GLY THR ILE ARG GLU VAL SER VAL VAL SER GLY LEU PRO
SEQRES 8 A 188 ALA SER THR SER VAL GLU ILE LEU GLU VAL LEU ASP GLU
SEQRES 9 A 188 GLU LYS ARG ILE LEU SER PHE ARG VAL LEU GLY GLY GLU
SEQRES 10 A 188 HIS ARG LEU ASN ASN TYR ARG SER VAL THR SER VAL ASN
SEQRES 11 A 188 GLU PHE VAL VAL LEU GLU LYS ASP LYS LYS LYS ARG VAL
SEQRES 12 A 188 TYR SER VAL VAL LEU GLU SER TYR ILE VAL ASP ILE PRO
SEQRES 13 A 188 GLN GLY ASN THR GLU GLU ASP THR ARG MET PHE VAL ASP
SEQRES 14 A 188 THR VAL VAL LYS SER ASN LEU GLN ASN LEU ALA VAL ILE
SEQRES 15 A 188 SER THR ALA SER PRO THR
SEQRES 1 B 188 GLY HIS MET LEU THR LYS ASP GLU PHE SER THR LEU ASP
SEQRES 2 B 188 SER ILE ILE ARG THR HIS HIS THR PHE PRO ARG SER PRO
SEQRES 3 B 188 ASN THR CYS THR SER LEU ILE ALA HIS ARG VAL ASP ALA
SEQRES 4 B 188 PRO ALA HIS ALA ILE TRP ARG PHE VAL ARG ASP PHE ALA
SEQRES 5 B 188 ASN PRO ASN LYS TYR LYS HIS PHE ILE LYS SER CYS THR
SEQRES 6 B 188 ILE ARG VAL ASN GLY ASN GLY ILE LYS GLU ILE LYS VAL
SEQRES 7 B 188 GLY THR ILE ARG GLU VAL SER VAL VAL SER GLY LEU PRO
SEQRES 8 B 188 ALA SER THR SER VAL GLU ILE LEU GLU VAL LEU ASP GLU
SEQRES 9 B 188 GLU LYS ARG ILE LEU SER PHE ARG VAL LEU GLY GLY GLU
SEQRES 10 B 188 HIS ARG LEU ASN ASN TYR ARG SER VAL THR SER VAL ASN
SEQRES 11 B 188 GLU PHE VAL VAL LEU GLU LYS ASP LYS LYS LYS ARG VAL
SEQRES 12 B 188 TYR SER VAL VAL LEU GLU SER TYR ILE VAL ASP ILE PRO
SEQRES 13 B 188 GLN GLY ASN THR GLU GLU ASP THR ARG MET PHE VAL ASP
SEQRES 14 B 188 THR VAL VAL LYS SER ASN LEU GLN ASN LEU ALA VAL ILE
SEQRES 15 B 188 SER THR ALA SER PRO THR
HET A8S A 301 19
HET MG A 302 1
HET A8S B 301 19
HET MG B 302 1
HETNAM A8S (2Z,4E)-5-[(1S)-1-HYDROXY-2,6,6-TRIMETHYL-4-
HETNAM 2 A8S OXOCYCLOHEX-2-EN-1-YL]-3-METHYLPENTA-2,4-DIENOIC ACID
HETNAM MG MAGNESIUM ION
HETSYN A8S (+)-ABSCISIC ACID; (2Z,4E)-5-[(1S)-1-HYDROXY-2,6,6-
HETSYN 2 A8S TRIMETHYL-4-OXO-2-CYCLOHEXEN-1-YL]-3-METHYL-2,4-
HETSYN 3 A8S PENTADIENOIC ACID
FORMUL 3 A8S 2(C15 H20 O4)
FORMUL 4 MG 2(MG 2+)
FORMUL 7 HOH *607(H2 O)
HELIX 1 1 THR A 26 HIS A 41 1 16
HELIX 2 2 PRO A 61 ARG A 70 1 10
HELIX 3 3 ASN A 74 TYR A 78 5 5
HELIX 4 4 THR A 181 THR A 205 1 25
HELIX 5 5 THR B 26 HIS B 41 1 16
HELIX 6 6 PRO B 61 ARG B 70 1 10
HELIX 7 7 ASN B 74 TYR B 78 5 5
HELIX 8 8 THR B 181 THR B 205 1 25
SHEET 1 A 7 THR A 49 VAL A 58 0
SHEET 2 A 7 VAL A 164 ASP A 175 -1 O GLU A 170 N ILE A 54
SHEET 3 A 7 ARG A 145 VAL A 154 -1 N PHE A 153 O TYR A 165
SHEET 4 A 7 ILE A 129 GLY A 136 -1 N LEU A 130 O THR A 148
SHEET 5 A 7 THR A 115 ASP A 124 -1 N VAL A 117 O LEU A 135
SHEET 6 A 7 ILE A 102 VAL A 107 -1 N ARG A 103 O GLU A 118
SHEET 7 A 7 ILE A 82 VAL A 89 -1 N ARG A 88 O ILE A 102
SHEET 1 B 7 THR B 49 VAL B 58 0
SHEET 2 B 7 VAL B 164 ASP B 175 -1 O VAL B 168 N HIS B 56
SHEET 3 B 7 ARG B 145 VAL B 154 -1 N PHE B 153 O TYR B 165
SHEET 4 B 7 ILE B 129 GLY B 136 -1 N LEU B 130 O THR B 148
SHEET 5 B 7 THR B 115 ASP B 124 -1 N VAL B 117 O LEU B 135
SHEET 6 B 7 ILE B 102 VAL B 107 -1 N VAL B 105 O SER B 116
SHEET 7 B 7 ILE B 82 VAL B 89 -1 N ARG B 88 O ILE B 102
LINK OH TYR A 144 MG MG A 302 1555 1555 2.80
LINK OG SER A 146 MG MG A 302 1555 1555 2.74
LINK OE1 GLU A 170 MG MG A 302 1555 1555 2.63
LINK O12 A8S A 301 MG MG A 302 1555 1555 2.66
LINK OH TYR B 144 MG MG B 302 1555 1555 2.67
LINK OG SER B 146 MG MG B 302 1555 1555 2.84
LINK OE1 GLU B 170 MG MG B 302 1555 1555 2.60
LINK O12 A8S B 301 MG MG B 302 1555 1555 2.78
SITE 1 AC1 9 LYS A 79 ALA A 113 PHE A 132 TYR A 144
SITE 2 AC1 9 ASN A 196 MG A 302 HOH A 428 HOH A 432
SITE 3 AC1 9 HOH A 442
SITE 1 AC2 5 PHE A 132 TYR A 144 SER A 146 GLU A 170
SITE 2 AC2 5 A8S A 301
SITE 1 AC3 11 LYS B 79 ALA B 113 PHE B 132 LEU B 141
SITE 2 AC3 11 TYR B 144 ASN B 196 MG B 302 HOH B 436
SITE 3 AC3 11 HOH B 447 HOH B 481 HOH B 546
SITE 1 AC4 5 PHE B 132 TYR B 144 SER B 146 GLU B 170
SITE 2 AC4 5 A8S B 301
CRYST1 232.836 232.836 53.292 90.00 90.00 120.00 H 3 2 36
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 0.004295 0.002480 0.000000 0.00000
SCALE2 0.000000 0.004959 0.000000 0.00000
SCALE3 0.000000 0.000000 0.018765 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
