HEADER HORMONE RECEPTOR 02-MAR-07 2P15
TITLE CRYSTAL STRUCTURE OF THE ER ALPHA LIGAND BINDING DOMAIN WITH THE
TITLE 2 AGONIST ORTHO-TRIFLUOROMETHYLPHENYLVINYL ESTRADIOL
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ESTROGEN RECEPTOR;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: LIGAND BINDING DOMAIN (RESIDUES 298-554);
COMPND 5 SYNONYM: ER, ESTRADIOL RECEPTOR, ER-ALPHA;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: GRIP PEPTIDE;
COMPND 10 CHAIN: C, D;
COMPND 11 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: ESR1, ESR, NR3A1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3) ROSETTA;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET;
SOURCE 11 MOL_ID: 2;
SOURCE 12 SYNTHETIC: YES;
SOURCE 13 OTHER_DETAILS: THE PEPTIDE WAS CHEMICALLY SYNTHESIZED. THE SEQUENCE
SOURCE 14 CAN BE NATURALLY FOUND IN HOMO SAPIENS (HUMAN).
KEYWDS NULEAR RECEPTOR, LIGAND BINDING DOMAIN, HELIX 12, HORMONE RECEPTOR
EXPDTA X-RAY DIFFRACTION
AUTHOR J.B.BRUNING,K.W.NETTLES,G.L.GREENE,Y.KIM
REVDAT 8 21-FEB-24 2P15 1 REMARK
REVDAT 7 20-OCT-21 2P15 1 REMARK SEQADV
REVDAT 6 18-OCT-17 2P15 1 REMARK
REVDAT 5 13-JUL-11 2P15 1 VERSN
REVDAT 4 24-FEB-09 2P15 1 VERSN
REVDAT 3 17-JUL-07 2P15 1 JRNL
REVDAT 2 26-JUN-07 2P15 1 JRNL
REVDAT 1 01-MAY-07 2P15 0
JRNL AUTH K.W.NETTLES,J.B.BRUNING,G.GIL,E.E.O'NEILL,J.NOWAK,Y.GUO,
JRNL AUTH 2 Y.KIM,E.R.DESOMBRE,R.DILIS,R.N.HANSON,A.JOACHIMIAK,
JRNL AUTH 3 G.L.GREENE
JRNL TITL STRUCTURAL PLASTICITY IN THE OESTROGEN RECEPTOR
JRNL TITL 2 LIGAND-BINDING DOMAIN.
JRNL REF EMBO REP. V. 8 563 2007
JRNL REFN ISSN 1469-221X
JRNL PMID 17468738
JRNL DOI 10.1038/SJ.EMBOR.7400963
REMARK 2
REMARK 2 RESOLUTION. 1.94 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
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) : 1.94
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 27.71
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.0
REMARK 3 NUMBER OF REFLECTIONS : 36913
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) : 0.161
REMARK 3 R VALUE (WORKING SET) : 0.158
REMARK 3 FREE R VALUE : 0.216
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1871
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) : 1.94
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.99
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1917
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 72.98
REMARK 3 BIN R VALUE (WORKING SET) : 0.1810
REMARK 3 BIN FREE R VALUE SET COUNT : 98
REMARK 3 BIN FREE R VALUE : 0.2440
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4007
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 64
REMARK 3 SOLVENT ATOMS : 461
REMARK 3
REMARK 3 B VALUES.
REMARK 3 B VALUE TYPE : LIKELY RESIDUAL
REMARK 3 FROM WILSON PLOT (A**2) : 20.06
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 20.06
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.08000
REMARK 3 B22 (A**2) : 0.12000
REMARK 3 B33 (A**2) : -0.04000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.01000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.167
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.156
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.097
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.303
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.960
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.933
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4247 ; 0.015 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 5779 ; 1.358 ; 2.000
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 536 ; 5.005 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 175 ;38.211 ;24.171
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 802 ;14.976 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 23 ;22.581 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 685 ; 0.098 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3063 ; 0.006 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 2153 ; 0.209 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 2944 ; 0.305 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 331 ; 0.189 ; 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): 61 ; 0.232 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 28 ; 0.409 ; 0.200
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): 2686 ; 1.003 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 4151 ; 1.194 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1780 ; 2.164 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1610 ; 3.140 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 32
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 306 A 338
REMARK 3 ORIGIN FOR THE GROUP (A): -17.9660 -1.3250 18.5410
REMARK 3 T TENSOR
REMARK 3 T11: -0.0091 T22: 0.0071
REMARK 3 T33: -0.0295 T12: -0.0193
REMARK 3 T13: 0.0371 T23: -0.0411
REMARK 3 L TENSOR
REMARK 3 L11: 6.9660 L22: 3.4671
REMARK 3 L33: 4.8962 L12: -3.2791
REMARK 3 L13: 3.5740 L23: -2.4629
REMARK 3 S TENSOR
REMARK 3 S11: 0.1084 S12: 0.2009 S13: -0.0390
REMARK 3 S21: -0.2578 S22: -0.1249 S23: -0.1027
REMARK 3 S31: 0.1271 S32: 0.2286 S33: 0.0165
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 339 A 367
REMARK 3 ORIGIN FOR THE GROUP (A): -27.8160 -3.8250 16.4680
REMARK 3 T TENSOR
REMARK 3 T11: 0.0590 T22: -0.0052
REMARK 3 T33: -0.0340 T12: 0.0053
REMARK 3 T13: 0.0221 T23: 0.0007
REMARK 3 L TENSOR
REMARK 3 L11: 5.9577 L22: 3.9804
REMARK 3 L33: 2.8442 L12: -3.5648
REMARK 3 L13: 3.0584 L23: -2.0099
REMARK 3 S TENSOR
REMARK 3 S11: 0.0317 S12: 0.0603 S13: -0.0396
REMARK 3 S21: -0.2544 S22: -0.0074 S23: -0.0212
REMARK 3 S31: 0.2032 S32: -0.0627 S33: -0.0242
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 368 A 382
REMARK 3 ORIGIN FOR THE GROUP (A): -26.5740 -16.0970 26.3650
REMARK 3 T TENSOR
REMARK 3 T11: 0.1126 T22: -0.0243
REMARK 3 T33: 0.0296 T12: -0.0006
REMARK 3 T13: 0.0033 T23: 0.0027
REMARK 3 L TENSOR
REMARK 3 L11: 6.6296 L22: 12.3602
REMARK 3 L33: 2.2233 L12: -5.3445
REMARK 3 L13: 1.4580 L23: -0.1154
REMARK 3 S TENSOR
REMARK 3 S11: 0.1242 S12: 0.0810 S13: -0.4588
REMARK 3 S21: 0.0144 S22: -0.0937 S23: 0.0307
REMARK 3 S31: 0.5020 S32: -0.0868 S33: -0.0306
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 383 A 397
REMARK 3 ORIGIN FOR THE GROUP (A): -25.7380 3.7640 23.6940
REMARK 3 T TENSOR
REMARK 3 T11: 0.0214 T22: 0.0125
REMARK 3 T33: -0.0440 T12: 0.0129
REMARK 3 T13: 0.0059 T23: 0.0054
REMARK 3 L TENSOR
REMARK 3 L11: 3.4764 L22: 4.8479
REMARK 3 L33: 1.4444 L12: 0.5991
REMARK 3 L13: 0.4625 L23: -1.1808
REMARK 3 S TENSOR
REMARK 3 S11: 0.0415 S12: 0.0318 S13: 0.1614
REMARK 3 S21: 0.0139 S22: -0.1107 S23: -0.1178
REMARK 3 S31: -0.0587 S32: 0.1430 S33: 0.0692
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 398 A 411
REMARK 3 ORIGIN FOR THE GROUP (A): -28.0870 13.2970 17.1640
REMARK 3 T TENSOR
REMARK 3 T11: 0.0877 T22: -0.0927
REMARK 3 T33: -0.0229 T12: 0.0187
REMARK 3 T13: -0.0288 T23: 0.0286
REMARK 3 L TENSOR
REMARK 3 L11: 2.2498 L22: 7.0924
REMARK 3 L33: 11.6250 L12: 0.9699
REMARK 3 L13: 2.7187 L23: 3.7483
REMARK 3 S TENSOR
REMARK 3 S11: -0.1391 S12: 0.1369 S13: 0.3587
REMARK 3 S21: -0.3356 S22: 0.0488 S23: 0.0328
REMARK 3 S31: -0.6160 S32: -0.0263 S33: 0.0903
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 412 A 421
REMARK 3 ORIGIN FOR THE GROUP (A): -40.8170 14.7670 20.7520
REMARK 3 T TENSOR
REMARK 3 T11: 0.2496 T22: 0.1014
REMARK 3 T33: 0.2606 T12: 0.1004
REMARK 3 T13: 0.0735 T23: -0.0414
REMARK 3 L TENSOR
REMARK 3 L11: 0.6142 L22: 30.9494
REMARK 3 L33: 1.2641 L12: 4.3600
REMARK 3 L13: -0.8812 L23: -6.2549
REMARK 3 S TENSOR
REMARK 3 S11: 0.5616 S12: -0.7152 S13: 1.0823
REMARK 3 S21: 1.1690 S22: -0.0979 S23: 0.2907
REMARK 3 S31: -0.8903 S32: -0.2144 S33: -0.4637
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 422 A 435
REMARK 3 ORIGIN FOR THE GROUP (A): -30.2320 11.4570 29.0250
REMARK 3 T TENSOR
REMARK 3 T11: 0.0694 T22: -0.0507
REMARK 3 T33: -0.0235 T12: 0.0193
REMARK 3 T13: 0.0193 T23: 0.0014
REMARK 3 L TENSOR
REMARK 3 L11: 23.1152 L22: 4.2287
REMARK 3 L33: 1.9423 L12: 0.5282
REMARK 3 L13: 6.2593 L23: -0.7686
REMARK 3 S TENSOR
REMARK 3 S11: -0.2791 S12: -0.2068 S13: 0.4829
REMARK 3 S21: 0.1576 S22: 0.0826 S23: 0.0740
REMARK 3 S31: -0.3207 S32: -0.1901 S33: 0.1965
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 436 A 460
REMARK 3 ORIGIN FOR THE GROUP (A): -19.7450 0.2620 30.7090
REMARK 3 T TENSOR
REMARK 3 T11: 0.0285 T22: 0.0202
REMARK 3 T33: -0.0030 T12: 0.0070
REMARK 3 T13: -0.0027 T23: 0.0065
REMARK 3 L TENSOR
REMARK 3 L11: 2.9026 L22: 6.1413
REMARK 3 L33: 1.5540 L12: 2.2741
REMARK 3 L13: 0.3899 L23: -0.3682
REMARK 3 S TENSOR
REMARK 3 S11: -0.0088 S12: -0.0032 S13: 0.1370
REMARK 3 S21: 0.0896 S22: -0.0229 S23: 0.1106
REMARK 3 S31: -0.0734 S32: 0.1313 S33: 0.0317
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 461 A 471
REMARK 3 ORIGIN FOR THE GROUP (A): -25.7010 -23.4030 36.4210
REMARK 3 T TENSOR
REMARK 3 T11: 0.0914 T22: -0.0229
REMARK 3 T33: 0.0802 T12: 0.0269
REMARK 3 T13: -0.0204 T23: -0.0007
REMARK 3 L TENSOR
REMARK 3 L11: 9.9794 L22: 13.2280
REMARK 3 L33: 8.5786 L12: 6.3815
REMARK 3 L13: -3.5774 L23: -2.4158
REMARK 3 S TENSOR
REMARK 3 S11: 0.4406 S12: 0.5550 S13: -0.7388
REMARK 3 S21: -0.0504 S22: -0.2911 S23: 0.1263
REMARK 3 S31: 0.4250 S32: -0.2081 S33: -0.1495
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 472 A 477
REMARK 3 ORIGIN FOR THE GROUP (A): -18.5430 -16.6850 36.2670
REMARK 3 T TENSOR
REMARK 3 T11: -0.0070 T22: -0.1171
REMARK 3 T33: -0.0121 T12: 0.0156
REMARK 3 T13: -0.0127 T23: 0.0639
REMARK 3 L TENSOR
REMARK 3 L11: 33.1432 L22: 25.7656
REMARK 3 L33: 18.3337 L12: 27.6479
REMARK 3 L13: 5.4998 L23: 5.7733
REMARK 3 S TENSOR
REMARK 3 S11: 0.4490 S12: -0.6327 S13: -1.2162
REMARK 3 S21: 0.1703 S22: -0.3330 S23: -0.8337
REMARK 3 S31: 1.1966 S32: -0.1732 S33: -0.1160
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 478 A 496
REMARK 3 ORIGIN FOR THE GROUP (A): -8.9910 -1.4580 35.5870
REMARK 3 T TENSOR
REMARK 3 T11: -0.0096 T22: 0.0725
REMARK 3 T33: 0.0570 T12: 0.0219
REMARK 3 T13: 0.0256 T23: 0.0420
REMARK 3 L TENSOR
REMARK 3 L11: 4.5421 L22: 10.4642
REMARK 3 L33: 1.2829 L12: 4.7040
REMARK 3 L13: 1.4354 L23: 1.9883
REMARK 3 S TENSOR
REMARK 3 S11: -0.0647 S12: 0.0441 S13: 0.0345
REMARK 3 S21: -0.2001 S22: 0.0155 S23: -0.2396
REMARK 3 S31: 0.0287 S32: 0.3535 S33: 0.0493
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 497 A 508
REMARK 3 ORIGIN FOR THE GROUP (A): -13.2310 5.2270 41.3710
REMARK 3 T TENSOR
REMARK 3 T11: 0.0287 T22: 0.0196
REMARK 3 T33: 0.0418 T12: -0.0114
REMARK 3 T13: 0.0067 T23: -0.0079
REMARK 3 L TENSOR
REMARK 3 L11: 9.4602 L22: 3.2087
REMARK 3 L33: 3.2294 L12: 1.4385
REMARK 3 L13: 1.9347 L23: -0.2904
REMARK 3 S TENSOR
REMARK 3 S11: -0.0087 S12: -0.1223 S13: 0.2184
REMARK 3 S21: 0.0770 S22: -0.0008 S23: -0.3091
REMARK 3 S31: -0.1374 S32: 0.1134 S33: 0.0095
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 : A 509 A 526
REMARK 3 ORIGIN FOR THE GROUP (A): -34.6820 1.2560 30.8610
REMARK 3 T TENSOR
REMARK 3 T11: 0.0608 T22: -0.0026
REMARK 3 T33: -0.0030 T12: 0.0229
REMARK 3 T13: 0.0345 T23: 0.0156
REMARK 3 L TENSOR
REMARK 3 L11: 9.3357 L22: 0.8400
REMARK 3 L33: 6.8852 L12: 0.3176
REMARK 3 L13: 6.6637 L23: 0.8326
REMARK 3 S TENSOR
REMARK 3 S11: 0.0284 S12: -0.0808 S13: 0.0124
REMARK 3 S21: 0.1006 S22: -0.0240 S23: 0.1307
REMARK 3 S31: 0.1148 S32: -0.2007 S33: -0.0044
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 : A 527 A 540
REMARK 3 ORIGIN FOR THE GROUP (A): -43.7840 -2.6510 16.2670
REMARK 3 T TENSOR
REMARK 3 T11: 0.0397 T22: 0.0560
REMARK 3 T33: 0.0475 T12: -0.0323
REMARK 3 T13: -0.1119 T23: -0.0129
REMARK 3 L TENSOR
REMARK 3 L11: 13.0204 L22: 12.3408
REMARK 3 L33: 4.8949 L12: -11.2482
REMARK 3 L13: -3.1621 L23: 2.5199
REMARK 3 S TENSOR
REMARK 3 S11: 0.5149 S12: 0.7148 S13: -0.0763
REMARK 3 S21: -0.5286 S22: -0.4928 S23: 0.7880
REMARK 3 S31: -0.1957 S32: -0.4293 S33: -0.0220
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 : A 541 A 549
REMARK 3 ORIGIN FOR THE GROUP (A): -39.3530 -10.0540 23.4950
REMARK 3 T TENSOR
REMARK 3 T11: -0.0095 T22: -0.0630
REMARK 3 T33: 0.0508 T12: -0.0155
REMARK 3 T13: -0.0225 T23: -0.0244
REMARK 3 L TENSOR
REMARK 3 L11: 10.7813 L22: 7.9972
REMARK 3 L33: 19.4172 L12: 3.2026
REMARK 3 L13: -2.6779 L23: 9.0847
REMARK 3 S TENSOR
REMARK 3 S11: -0.1880 S12: -0.2972 S13: -0.8166
REMARK 3 S21: 0.1028 S22: -0.4977 S23: 0.3945
REMARK 3 S31: 0.3273 S32: -0.8718 S33: 0.6857
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 306 B 329
REMARK 3 ORIGIN FOR THE GROUP (A): -27.0280 3.9800 60.2540
REMARK 3 T TENSOR
REMARK 3 T11: 0.0907 T22: 0.1214
REMARK 3 T33: -0.0260 T12: -0.0004
REMARK 3 T13: -0.0378 T23: -0.0422
REMARK 3 L TENSOR
REMARK 3 L11: 16.2548 L22: 3.5815
REMARK 3 L33: 2.2264 L12: 6.9807
REMARK 3 L13: -1.3512 L23: -0.2601
REMARK 3 S TENSOR
REMARK 3 S11: -0.0915 S12: -0.5377 S13: 0.2579
REMARK 3 S21: 0.1535 S22: 0.0547 S23: -0.0018
REMARK 3 S31: -0.2668 S32: 0.4756 S33: 0.0368
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 330 B 351
REMARK 3 ORIGIN FOR THE GROUP (A): -52.1050 -10.2340 53.8140
REMARK 3 T TENSOR
REMARK 3 T11: 0.0417 T22: 0.0450
REMARK 3 T33: 0.0710 T12: 0.0194
REMARK 3 T13: 0.0386 T23: 0.0278
REMARK 3 L TENSOR
REMARK 3 L11: 2.4155 L22: 5.4481
REMARK 3 L33: 2.1943 L12: 2.8643
REMARK 3 L13: 0.1169 L23: -0.6200
REMARK 3 S TENSOR
REMARK 3 S11: 0.1013 S12: -0.1002 S13: -0.1567
REMARK 3 S21: 0.4126 S22: 0.0501 S23: 0.3036
REMARK 3 S31: 0.2091 S32: -0.1744 S33: -0.1514
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 352 B 359
REMARK 3 ORIGIN FOR THE GROUP (A): -41.3830 4.1660 57.1170
REMARK 3 T TENSOR
REMARK 3 T11: 0.0506 T22: 0.0048
REMARK 3 T33: -0.0099 T12: 0.0193
REMARK 3 T13: 0.0307 T23: -0.0034
REMARK 3 L TENSOR
REMARK 3 L11: 11.2653 L22: 7.9628
REMARK 3 L33: 7.0742 L12: 4.9717
REMARK 3 L13: -3.1267 L23: -1.5056
REMARK 3 S TENSOR
REMARK 3 S11: 0.4355 S12: -0.2289 S13: 0.4622
REMARK 3 S21: 0.2339 S22: -0.0210 S23: 0.3001
REMARK 3 S31: -0.5152 S32: -0.1626 S33: -0.4144
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 360 B 395
REMARK 3 ORIGIN FOR THE GROUP (A): -34.6080 6.8100 50.4950
REMARK 3 T TENSOR
REMARK 3 T11: 0.0577 T22: 0.0111
REMARK 3 T33: 0.0120 T12: -0.0038
REMARK 3 T13: 0.0194 T23: -0.0228
REMARK 3 L TENSOR
REMARK 3 L11: 1.4070 L22: 4.7495
REMARK 3 L33: 1.8246 L12: 0.4158
REMARK 3 L13: -0.2309 L23: -0.2463
REMARK 3 S TENSOR
REMARK 3 S11: 0.0697 S12: -0.0688 S13: 0.1527
REMARK 3 S21: 0.1515 S22: 0.0054 S23: -0.0420
REMARK 3 S31: -0.2724 S32: 0.0737 S33: -0.0751
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 396 B 413
REMARK 3 ORIGIN FOR THE GROUP (A): -39.5330 -15.9870 53.3820
REMARK 3 T TENSOR
REMARK 3 T11: 0.1036 T22: 0.0018
REMARK 3 T33: 0.0850 T12: 0.0170
REMARK 3 T13: 0.0314 T23: 0.0322
REMARK 3 L TENSOR
REMARK 3 L11: 2.9135 L22: 3.0970
REMARK 3 L33: 5.6454 L12: 0.9627
REMARK 3 L13: -0.0002 L23: 0.7585
REMARK 3 S TENSOR
REMARK 3 S11: -0.0924 S12: -0.1403 S13: -0.4138
REMARK 3 S21: 0.4857 S22: -0.0549 S23: 0.1022
REMARK 3 S31: 0.4841 S32: 0.1187 S33: 0.1473
REMARK 3
REMARK 3 TLS GROUP : 21
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 414 B 421
REMARK 3 ORIGIN FOR THE GROUP (A): -49.1760 -15.5640 43.3410
REMARK 3 T TENSOR
REMARK 3 T11: 0.0492 T22: 0.0917
REMARK 3 T33: 0.0925 T12: -0.0497
REMARK 3 T13: -0.0300 T23: -0.0490
REMARK 3 L TENSOR
REMARK 3 L11: 3.4511 L22: 13.2896
REMARK 3 L33: 6.8396 L12: -3.8549
REMARK 3 L13: -0.9019 L23: -6.6950
REMARK 3 S TENSOR
REMARK 3 S11: 0.7568 S12: 0.3857 S13: -0.5235
REMARK 3 S21: 0.1785 S22: -0.3483 S23: 0.8713
REMARK 3 S31: 0.4503 S32: 0.1689 S33: -0.4085
REMARK 3
REMARK 3 TLS GROUP : 22
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 422 B 434
REMARK 3 ORIGIN FOR THE GROUP (A): -35.5360 -13.5530 43.3720
REMARK 3 T TENSOR
REMARK 3 T11: 0.0705 T22: -0.0676
REMARK 3 T33: 0.0068 T12: -0.0229
REMARK 3 T13: 0.0236 T23: -0.0130
REMARK 3 L TENSOR
REMARK 3 L11: 24.5962 L22: 5.0288
REMARK 3 L33: 4.8719 L12: 1.8944
REMARK 3 L13: 7.2718 L23: 1.9497
REMARK 3 S TENSOR
REMARK 3 S11: 0.0678 S12: 0.2413 S13: -0.6003
REMARK 3 S21: -0.3507 S22: -0.0050 S23: -0.0199
REMARK 3 S31: 0.1811 S32: -0.0356 S33: -0.0628
REMARK 3
REMARK 3 TLS GROUP : 23
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 435 B 447
REMARK 3 ORIGIN FOR THE GROUP (A): -23.5710 -8.5380 52.7060
REMARK 3 T TENSOR
REMARK 3 T11: 0.0320 T22: 0.0475
REMARK 3 T33: 0.0518 T12: 0.0166
REMARK 3 T13: -0.0051 T23: 0.0552
REMARK 3 L TENSOR
REMARK 3 L11: 5.4538 L22: 13.0176
REMARK 3 L33: 2.3859 L12: -1.0547
REMARK 3 L13: 0.4447 L23: 1.1657
REMARK 3 S TENSOR
REMARK 3 S11: -0.0719 S12: -0.3908 S13: -0.5363
REMARK 3 S21: -0.0504 S22: 0.1256 S23: -0.1413
REMARK 3 S31: 0.1973 S32: 0.2341 S33: -0.0537
REMARK 3
REMARK 3 TLS GROUP : 24
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 448 B 458
REMARK 3 ORIGIN FOR THE GROUP (A): -28.7830 5.4560 46.7090
REMARK 3 T TENSOR
REMARK 3 T11: 0.0326 T22: 0.0332
REMARK 3 T33: 0.0186 T12: -0.0274
REMARK 3 T13: 0.0225 T23: -0.0251
REMARK 3 L TENSOR
REMARK 3 L11: 3.5426 L22: 9.1538
REMARK 3 L33: 3.7125 L12: -1.2112
REMARK 3 L13: 0.2832 L23: -3.5660
REMARK 3 S TENSOR
REMARK 3 S11: 0.0481 S12: -0.0313 S13: 0.2414
REMARK 3 S21: -0.0996 S22: 0.0557 S23: -0.0049
REMARK 3 S31: -0.1090 S32: 0.0791 S33: -0.1038
REMARK 3
REMARK 3 TLS GROUP : 25
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 459 B 474
REMARK 3 ORIGIN FOR THE GROUP (A): -27.7040 19.4440 40.8570
REMARK 3 T TENSOR
REMARK 3 T11: 0.2717 T22: -0.0169
REMARK 3 T33: 0.0994 T12: -0.0310
REMARK 3 T13: 0.0713 T23: 0.0823
REMARK 3 L TENSOR
REMARK 3 L11: 5.6127 L22: 13.6004
REMARK 3 L33: 3.5492 L12: 2.0570
REMARK 3 L13: -0.0619 L23: 2.4066
REMARK 3 S TENSOR
REMARK 3 S11: -0.0650 S12: 0.6393 S13: 0.8772
REMARK 3 S21: -1.2995 S22: -0.1265 S23: 0.4033
REMARK 3 S31: -0.4954 S32: -0.1350 S33: 0.1915
REMARK 3
REMARK 3 TLS GROUP : 26
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 475 B 495
REMARK 3 ORIGIN FOR THE GROUP (A): -16.3180 4.0530 50.8630
REMARK 3 T TENSOR
REMARK 3 T11: -0.0080 T22: 0.0940
REMARK 3 T33: -0.0517 T12: -0.0657
REMARK 3 T13: -0.0343 T23: -0.0347
REMARK 3 L TENSOR
REMARK 3 L11: 11.0808 L22: 18.5769
REMARK 3 L33: 2.9087 L12: -9.8178
REMARK 3 L13: 3.1545 L23: -6.4055
REMARK 3 S TENSOR
REMARK 3 S11: -0.0394 S12: -0.6005 S13: 0.2448
REMARK 3 S21: 0.3738 S22: -0.0764 S23: -0.2016
REMARK 3 S31: -0.2268 S32: 0.3504 S33: 0.1158
REMARK 3
REMARK 3 TLS GROUP : 27
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 496 B 513
REMARK 3 ORIGIN FOR THE GROUP (A): -17.4880 -5.4420 43.7220
REMARK 3 T TENSOR
REMARK 3 T11: 0.0366 T22: 0.0216
REMARK 3 T33: 0.0226 T12: -0.0002
REMARK 3 T13: 0.0169 T23: 0.0161
REMARK 3 L TENSOR
REMARK 3 L11: 14.9819 L22: 0.9287
REMARK 3 L33: 2.1602 L12: -1.3482
REMARK 3 L13: 3.9642 L23: -1.2816
REMARK 3 S TENSOR
REMARK 3 S11: -0.0116 S12: 0.0382 S13: -0.1768
REMARK 3 S21: 0.0231 S22: -0.0477 S23: -0.0981
REMARK 3 S31: 0.0503 S32: 0.1228 S33: 0.0593
REMARK 3
REMARK 3 TLS GROUP : 28
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 514 B 535
REMARK 3 ORIGIN FOR THE GROUP (A): -46.6100 -2.8930 40.1600
REMARK 3 T TENSOR
REMARK 3 T11: 0.0560 T22: 0.0342
REMARK 3 T33: 0.0270 T12: 0.0002
REMARK 3 T13: -0.0049 T23: 0.0167
REMARK 3 L TENSOR
REMARK 3 L11: 18.2800 L22: 0.3994
REMARK 3 L33: 0.2946 L12: -0.3502
REMARK 3 L13: -2.1272 L23: 0.1562
REMARK 3 S TENSOR
REMARK 3 S11: 0.0579 S12: 0.3852 S13: 0.1836
REMARK 3 S21: -0.0849 S22: 0.0408 S23: 0.1526
REMARK 3 S31: -0.0078 S32: -0.1386 S33: -0.0986
REMARK 3
REMARK 3 TLS GROUP : 29
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 536 B 544
REMARK 3 ORIGIN FOR THE GROUP (A): -49.4570 5.6650 47.6630
REMARK 3 T TENSOR
REMARK 3 T11: -0.0663 T22: -0.0683
REMARK 3 T33: 0.0413 T12: 0.0086
REMARK 3 T13: -0.0073 T23: -0.0374
REMARK 3 L TENSOR
REMARK 3 L11: 7.7104 L22: 9.5671
REMARK 3 L33: 12.3506 L12: 5.0592
REMARK 3 L13: -0.8795 L23: 1.9717
REMARK 3 S TENSOR
REMARK 3 S11: -0.2688 S12: -0.2080 S13: 0.3232
REMARK 3 S21: -0.1950 S22: -0.0092 S23: 0.1643
REMARK 3 S31: -0.2880 S32: -0.4247 S33: 0.2779
REMARK 3
REMARK 3 TLS GROUP : 30
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 545 B 550
REMARK 3 ORIGIN FOR THE GROUP (A): -45.7190 6.9520 37.7090
REMARK 3 T TENSOR
REMARK 3 T11: 0.0885 T22: 0.0626
REMARK 3 T33: -0.0271 T12: -0.0043
REMARK 3 T13: -0.0291 T23: 0.0140
REMARK 3 L TENSOR
REMARK 3 L11: 46.4085 L22: 17.2306
REMARK 3 L33: 24.6393 L12: 4.6506
REMARK 3 L13: 16.4148 L23: 4.7420
REMARK 3 S TENSOR
REMARK 3 S11: -0.1849 S12: 1.1938 S13: 0.7934
REMARK 3 S21: -1.2351 S22: 0.2045 S23: 0.1666
REMARK 3 S31: -0.4167 S32: -0.3809 S33: -0.0196
REMARK 3
REMARK 3 TLS GROUP : 31
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 687 C 697
REMARK 3 ORIGIN FOR THE GROUP (A): -29.7250 -17.9030 15.8950
REMARK 3 T TENSOR
REMARK 3 T11: 0.0844 T22: -0.1252
REMARK 3 T33: -0.1177 T12: 0.0287
REMARK 3 T13: -0.0839 T23: -0.1074
REMARK 3 L TENSOR
REMARK 3 L11: 47.4285 L22: 32.5999
REMARK 3 L33: 24.0506 L12: -7.9678
REMARK 3 L13: 27.1896 L23: 3.7895
REMARK 3 S TENSOR
REMARK 3 S11: 1.4765 S12: 1.7677 S13: -1.6747
REMARK 3 S21: -1.0332 S22: -0.6845 S23: 1.2185
REMARK 3 S31: 1.4588 S32: 0.0370 S33: -0.7921
REMARK 3
REMARK 3 TLS GROUP : 32
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 686 D 696
REMARK 3 ORIGIN FOR THE GROUP (A): -44.8830 15.9920 53.3760
REMARK 3 T TENSOR
REMARK 3 T11: -0.1238 T22: -0.1168
REMARK 3 T33: 0.1235 T12: 0.0341
REMARK 3 T13: 0.0859 T23: -0.0752
REMARK 3 L TENSOR
REMARK 3 L11: 33.9081 L22: 30.1053
REMARK 3 L33: 26.5868 L12: 11.1826
REMARK 3 L13: 5.7905 L23: 9.1767
REMARK 3 S TENSOR
REMARK 3 S11: -0.1686 S12: -0.2317 S13: 2.4130
REMARK 3 S21: 0.3283 S22: -0.3055 S23: 1.6850
REMARK 3 S31: -0.7634 S32: -1.5735 S33: 0.4741
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 2P15 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-MAR-07.
REMARK 100 THE DEPOSITION ID IS D_1000041836.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 23-AUG-04
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 19-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97921
REMARK 200 MONOCHROMATOR : SI 111 CHANNEL
REMARK 200 OPTICS : SI 111 MONOCHROMATOR
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : SBC-2
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO, HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK, HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 39661
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.870
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 92.4
REMARK 200 DATA REDUNDANCY : 4.700
REMARK 200 R MERGE (I) : 0.08000
REMARK 200 R SYM (I) : 0.08000
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 6.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.87
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.94
REMARK 200 COMPLETENESS FOR SHELL (%) : 55.2
REMARK 200 DATA REDUNDANCY IN SHELL : 3.00
REMARK 200 R MERGE FOR SHELL (I) : 0.39500
REMARK 200 R SYM FOR SHELL (I) : 0.39500
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.738
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 41.62
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.11
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG 4000, 0.2M AMMONIUM SULFATE,
REMARK 280 PH 8.5, VAPOR DIFFUSION, SITTING DROP, 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 42.11000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 7190 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 20770 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -23.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, 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 SER A 297
REMARK 465 ILE A 298
REMARK 465 LYS A 299
REMARK 465 ARG A 300
REMARK 465 SER A 301
REMARK 465 LYS A 302
REMARK 465 LYS A 303
REMARK 465 ASN A 304
REMARK 465 ASP A 332
REMARK 465 PRO A 333
REMARK 465 THR A 334
REMARK 465 HIS A 550
REMARK 465 ALA A 551
REMARK 465 PRO A 552
REMARK 465 THR A 553
REMARK 465 SER A 554
REMARK 465 SER B 297
REMARK 465 ILE B 298
REMARK 465 LYS B 299
REMARK 465 ARG B 300
REMARK 465 SER B 301
REMARK 465 LYS B 302
REMARK 465 LYS B 303
REMARK 465 ASN B 304
REMARK 465 SER B 305
REMARK 465 LEU B 462
REMARK 465 SER B 463
REMARK 465 SER B 464
REMARK 465 ALA B 551
REMARK 465 PRO B 552
REMARK 465 THR B 553
REMARK 465 SER B 554
REMARK 465 LYS C 686
REMARK 465 SER C 698
REMARK 465 SER D 697
REMARK 465 SER D 698
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 SER A 305 OG
REMARK 470 LEU A 306 CG CD1 CD2
REMARK 470 ARG A 335 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 397 CG CD OE1 OE2
REMARK 470 ASN A 413 CG OD1 ND2
REMARK 470 LEU A 549 CG CD1 CD2
REMARK 470 ARG B 335 CG CD NE CZ NH1 NH2
REMARK 470 THR B 465 OG1 CG2
REMARK 470 LEU B 466 CG CD1 CD2
REMARK 470 LYS B 467 CD CE NZ
REMARK 470 HIS B 550 CG ND1 CD2 CE1 NE2
REMARK 470 LYS D 686 CG CD CE NZ
REMARK 470 HIS D 687 CG ND1 CD2 CE1 NE2
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 ASP A 321 CG OD1 OD2
REMARK 480 ASP B 321 CG OD1
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 A 330 O HOH A 779 1.83
REMARK 500 O HOH B 785 O HOH B 836 2.02
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH A 819 O HOH B 838 1554 0.75
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 ASP B 321 CG ASP B 321 OD2 0.756
REMARK 500 SER C 697 C SER C 697 O 0.239
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 ASP B 321 OD1 - CG - OD2 ANGL. DEV. = -19.9 DEGREES
REMARK 500 ASP B 321 CB - CG - OD2 ANGL. DEV. = 20.4 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 GLU B 330 33.92 -95.00
REMARK 500 HIS D 687 86.16 -65.84
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EZT A 600
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EZT B 601
DBREF 2P15 A 298 554 UNP P03372 ESR1_HUMAN 298 554
DBREF 2P15 B 298 554 UNP P03372 ESR1_HUMAN 298 554
DBREF 2P15 C 686 698 UNP Q15596 NCOA2_HUMAN 686 698
DBREF 2P15 D 686 698 UNP Q15596 NCOA2_HUMAN 686 698
SEQADV 2P15 SER A 297 UNP P03372 CLONING ARTIFACT
SEQADV 2P15 SER A 537 UNP P03372 TYR 537 ENGINEERED MUTATION
SEQADV 2P15 SER B 297 UNP P03372 CLONING ARTIFACT
SEQADV 2P15 SER B 537 UNP P03372 TYR 537 ENGINEERED MUTATION
SEQRES 1 A 258 SER ILE LYS ARG SER LYS LYS ASN SER LEU ALA LEU SER
SEQRES 2 A 258 LEU THR ALA ASP GLN MET VAL SER ALA LEU LEU ASP ALA
SEQRES 3 A 258 GLU PRO PRO ILE LEU TYR SER GLU TYR ASP PRO THR ARG
SEQRES 4 A 258 PRO PHE SER GLU ALA SER MET MET GLY LEU LEU THR ASN
SEQRES 5 A 258 LEU ALA ASP ARG GLU LEU VAL HIS MET ILE ASN TRP ALA
SEQRES 6 A 258 LYS ARG VAL PRO GLY PHE VAL ASP LEU THR LEU HIS ASP
SEQRES 7 A 258 GLN VAL HIS LEU LEU GLU CYS ALA TRP LEU GLU ILE LEU
SEQRES 8 A 258 MET ILE GLY LEU VAL TRP ARG SER MET GLU HIS PRO GLY
SEQRES 9 A 258 LYS LEU LEU PHE ALA PRO ASN LEU LEU LEU ASP ARG ASN
SEQRES 10 A 258 GLN GLY LYS CYS VAL GLU GLY MET VAL GLU ILE PHE ASP
SEQRES 11 A 258 MET LEU LEU ALA THR SER SER ARG PHE ARG MET MET ASN
SEQRES 12 A 258 LEU GLN GLY GLU GLU PHE VAL CYS LEU LYS SER ILE ILE
SEQRES 13 A 258 LEU LEU ASN SER GLY VAL TYR THR PHE LEU SER SER THR
SEQRES 14 A 258 LEU LYS SER LEU GLU GLU LYS ASP HIS ILE HIS ARG VAL
SEQRES 15 A 258 LEU ASP LYS ILE THR ASP THR LEU ILE HIS LEU MET ALA
SEQRES 16 A 258 LYS ALA GLY LEU THR LEU GLN GLN GLN HIS GLN ARG LEU
SEQRES 17 A 258 ALA GLN LEU LEU LEU ILE LEU SER HIS ILE ARG HIS MET
SEQRES 18 A 258 SER ASN LYS GLY MET GLU HIS LEU TYR SER MET LYS CYS
SEQRES 19 A 258 LYS ASN VAL VAL PRO LEU SER ASP LEU LEU LEU GLU MET
SEQRES 20 A 258 LEU ASP ALA HIS ARG LEU HIS ALA PRO THR SER
SEQRES 1 B 258 SER ILE LYS ARG SER LYS LYS ASN SER LEU ALA LEU SER
SEQRES 2 B 258 LEU THR ALA ASP GLN MET VAL SER ALA LEU LEU ASP ALA
SEQRES 3 B 258 GLU PRO PRO ILE LEU TYR SER GLU TYR ASP PRO THR ARG
SEQRES 4 B 258 PRO PHE SER GLU ALA SER MET MET GLY LEU LEU THR ASN
SEQRES 5 B 258 LEU ALA ASP ARG GLU LEU VAL HIS MET ILE ASN TRP ALA
SEQRES 6 B 258 LYS ARG VAL PRO GLY PHE VAL ASP LEU THR LEU HIS ASP
SEQRES 7 B 258 GLN VAL HIS LEU LEU GLU CYS ALA TRP LEU GLU ILE LEU
SEQRES 8 B 258 MET ILE GLY LEU VAL TRP ARG SER MET GLU HIS PRO GLY
SEQRES 9 B 258 LYS LEU LEU PHE ALA PRO ASN LEU LEU LEU ASP ARG ASN
SEQRES 10 B 258 GLN GLY LYS CYS VAL GLU GLY MET VAL GLU ILE PHE ASP
SEQRES 11 B 258 MET LEU LEU ALA THR SER SER ARG PHE ARG MET MET ASN
SEQRES 12 B 258 LEU GLN GLY GLU GLU PHE VAL CYS LEU LYS SER ILE ILE
SEQRES 13 B 258 LEU LEU ASN SER GLY VAL TYR THR PHE LEU SER SER THR
SEQRES 14 B 258 LEU LYS SER LEU GLU GLU LYS ASP HIS ILE HIS ARG VAL
SEQRES 15 B 258 LEU ASP LYS ILE THR ASP THR LEU ILE HIS LEU MET ALA
SEQRES 16 B 258 LYS ALA GLY LEU THR LEU GLN GLN GLN HIS GLN ARG LEU
SEQRES 17 B 258 ALA GLN LEU LEU LEU ILE LEU SER HIS ILE ARG HIS MET
SEQRES 18 B 258 SER ASN LYS GLY MET GLU HIS LEU TYR SER MET LYS CYS
SEQRES 19 B 258 LYS ASN VAL VAL PRO LEU SER ASP LEU LEU LEU GLU MET
SEQRES 20 B 258 LEU ASP ALA HIS ARG LEU HIS ALA PRO THR SER
SEQRES 1 C 13 LYS HIS LYS ILE LEU HIS ARG LEU LEU GLN ASP SER SER
SEQRES 1 D 13 LYS HIS LYS ILE LEU HIS ARG LEU LEU GLN ASP SER SER
HET EZT A 600 32
HET EZT B 601 32
HETNAM EZT (17BETA)-17-{(E)-2-[2-(TRIFLUOROMETHYL)
HETNAM 2 EZT PHENYL]VINYL}ESTRA-1(10),2,4-TRIENE-3,17-DIOL
FORMUL 5 EZT 2(C27 H29 F3 O2)
FORMUL 7 HOH *461(H2 O)
HELIX 1 1 LEU A 306 LEU A 310 5 5
HELIX 2 2 THR A 311 ALA A 322 1 12
HELIX 3 3 SER A 338 ARG A 363 1 26
HELIX 4 4 GLY A 366 LEU A 370 5 5
HELIX 5 5 THR A 371 MET A 396 1 26
HELIX 6 6 MET A 421 ASN A 439 1 19
HELIX 7 7 GLN A 441 SER A 456 1 16
HELIX 8 8 GLY A 457 PHE A 461 5 5
HELIX 9 9 THR A 465 ALA A 493 1 29
HELIX 10 10 THR A 496 LYS A 531 1 36
HELIX 11 11 SER A 537 ALA A 546 1 10
HELIX 12 12 LEU B 306 LEU B 310 5 5
HELIX 13 13 THR B 311 ALA B 322 1 12
HELIX 14 14 SER B 338 LYS B 362 1 25
HELIX 15 15 GLY B 366 LEU B 370 5 5
HELIX 16 16 THR B 371 MET B 396 1 26
HELIX 17 17 GLY B 420 MET B 438 1 19
HELIX 18 18 GLN B 441 GLY B 457 1 17
HELIX 19 19 VAL B 458 PHE B 461 5 4
HELIX 20 20 THR B 465 ALA B 493 1 29
HELIX 21 21 THR B 496 LYS B 531 1 36
HELIX 22 22 SER B 537 ALA B 546 1 10
HELIX 23 23 HIS C 687 ASP C 696 1 10
HELIX 24 24 LYS D 688 LEU D 694 1 7
SHEET 1 A 2 LYS A 401 ALA A 405 0
SHEET 2 A 2 LEU A 408 ASP A 411 -1 O LEU A 410 N LEU A 402
SHEET 1 B 2 LYS B 401 ALA B 405 0
SHEET 2 B 2 LEU B 408 ASP B 411 -1 O LEU B 410 N LEU B 402
SITE 1 AC1 15 MET A 343 LEU A 346 GLU A 353 LEU A 387
SITE 2 AC1 15 MET A 388 ARG A 394 LEU A 402 PHE A 404
SITE 3 AC1 15 VAL A 418 MET A 421 ILE A 424 PHE A 425
SITE 4 AC1 15 HIS A 524 LEU A 525 HOH A 604
SITE 1 AC2 15 MET B 343 LEU B 346 GLU B 353 LEU B 387
SITE 2 AC2 15 ARG B 394 LEU B 402 PHE B 404 MET B 421
SITE 3 AC2 15 ILE B 424 PHE B 425 LEU B 428 GLY B 521
SITE 4 AC2 15 HIS B 524 LEU B 525 HOH B 602
CRYST1 56.052 84.220 58.693 90.00 109.59 90.00 P 1 21 1 4
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 0.017841 0.000000 0.006349 0.00000
SCALE2 0.000000 0.011874 0.000000 0.00000
SCALE3 0.000000 0.000000 0.018085 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
