HEADER TRANSCRIPTION 05-JUN-07 2Q6J
TITLE CRYSTAL STRUCTURE OF ESTROGEN RECEPTOR ALPHA COMPLEXED TO A B-N
TITLE 2 SUBSTITUTED LIGAND
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ESTROGEN RECEPTOR;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: 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 FRAGMENT: RESIDUES 696-698;
COMPND 12 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: PMCSG7;
SOURCE 11 MOL_ID: 2;
SOURCE 12 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 13 ORGANISM_COMMON: HOUSE MOUSE;
SOURCE 14 ORGANISM_TAXID: 10090;
SOURCE 15 GENE: NCOA2;
SOURCE 16 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 17 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS PROTEIN-LIGAND COMPLEX, TRANSCRIPTION
EXPDTA X-RAY DIFFRACTION
AUTHOR H.ZHOU,K.W.NETTLES,J.B.BRUNING,Y.KIM,A.JOACHIMIAK,S.SHARMA,
AUTHOR 2 K.E.CARLSON,F.STOSSI,B.S.KATZENELLENBOGEN,G.L.GREENE,
AUTHOR 3 J.A.KATZENELLENBOGEN
REVDAT 7 30-AUG-23 2Q6J 1 REMARK
REVDAT 6 20-OCT-21 2Q6J 1 REMARK SEQADV
REVDAT 5 18-OCT-17 2Q6J 1 REMARK
REVDAT 4 13-JUL-11 2Q6J 1 VERSN
REVDAT 3 24-FEB-09 2Q6J 1 VERSN
REVDAT 2 17-JUL-07 2Q6J 1 JRNL
REVDAT 1 26-JUN-07 2Q6J 0
JRNL AUTH H.-B.ZHOU,K.W.NETTLES,J.B.BRUNING,Y.KIM,A.JOACHIMIAK,
JRNL AUTH 2 S.SHARMA,K.E.CARLSON,F.STOSSI,B.S.KATZENELLENBOGEN,
JRNL AUTH 3 G.L.GREENE,J.A.KATZENELLENBOGEN
JRNL TITL ELEMENTAL ISOMERISM: A BORON-NITROGEN SURROGATE FOR A
JRNL TITL 2 CARBON-CARBON DOUBLE BOND INCREASES THE CHEMICAL DIVERSITY
JRNL TITL 3 OF ESTROGEN RECEPTOR LIGANDS
JRNL REF CHEM.BIOL. V. 14 659 2007
JRNL REFN ISSN 1074-5521
JRNL PMID 17584613
JRNL DOI 10.1016/J.CHEMBIOL.2007.04.009
REMARK 2
REMARK 2 RESOLUTION. 2.70 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) : 2.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 12.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 94.0
REMARK 3 NUMBER OF REFLECTIONS : 12322
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) : 0.231
REMARK 3 R VALUE (WORKING SET) : 0.227
REMARK 3 FREE R VALUE : 0.297
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 633
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) : 2.70
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.77
REMARK 3 REFLECTION IN BIN (WORKING SET) : 747
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 83.73
REMARK 3 BIN R VALUE (WORKING SET) : 0.2860
REMARK 3 BIN FREE R VALUE SET COUNT : 35
REMARK 3 BIN FREE R VALUE : 0.3290
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3953
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 64
REMARK 3 SOLVENT ATOMS : 1
REMARK 3
REMARK 3 B VALUES.
REMARK 3 B VALUE TYPE : LIKELY RESIDUAL
REMARK 3 FROM WILSON PLOT (A**2) : 61.60
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 21.98
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.30000
REMARK 3 B22 (A**2) : 1.24000
REMARK 3 B33 (A**2) : -0.15000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.30000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.491
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.400
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 40.668
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.928
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.874
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4114 ; 0.010 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 5561 ; 1.381 ; 2.001
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 489 ; 5.478 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 172 ;39.377 ;24.012
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 792 ;20.139 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 25 ;23.895 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 650 ; 0.087 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2957 ; 0.005 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 2269 ; 0.286 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 2805 ; 0.315 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 114 ; 0.185 ; 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): 55 ; 0.261 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 3 ; 0.211 ; 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): 2529 ; 0.782 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3990 ; 1.225 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1766 ; 0.938 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1571 ; 1.315 ; 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 : 23
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 327
REMARK 3 ORIGIN FOR THE GROUP (A): 4.7730 7.2206 -4.8879
REMARK 3 T TENSOR
REMARK 3 T11: 0.3879 T22: 0.0802
REMARK 3 T33: 0.2617 T12: 0.0312
REMARK 3 T13: 0.0116 T23: 0.0290
REMARK 3 L TENSOR
REMARK 3 L11: 10.3583 L22: 2.0599
REMARK 3 L33: 2.4543 L12: -4.3263
REMARK 3 L13: -3.9659 L23: 2.1430
REMARK 3 S TENSOR
REMARK 3 S11: -0.2618 S12: 0.3728 S13: 0.6835
REMARK 3 S21: -0.2115 S22: 0.3260 S23: -0.2010
REMARK 3 S31: -0.1752 S32: -0.3753 S33: -0.0642
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 328 A 339
REMARK 3 ORIGIN FOR THE GROUP (A): 33.1769 -11.6743 -2.5470
REMARK 3 T TENSOR
REMARK 3 T11: 0.6961 T22: 0.2389
REMARK 3 T33: 0.4414 T12: -0.0596
REMARK 3 T13: 0.2392 T23: -0.0641
REMARK 3 L TENSOR
REMARK 3 L11: 5.7431 L22: 7.5270
REMARK 3 L33: 7.8764 L12: -5.3171
REMARK 3 L13: 3.0199 L23: -6.8427
REMARK 3 S TENSOR
REMARK 3 S11: 0.8797 S12: 1.3995 S13: 0.1233
REMARK 3 S21: -0.4237 S22: -1.3638 S23: -0.6591
REMARK 3 S31: -0.7271 S32: 0.5431 S33: 0.4840
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 340 A 359
REMARK 3 ORIGIN FOR THE GROUP (A): 26.2232 -0.2612 0.4658
REMARK 3 T TENSOR
REMARK 3 T11: 0.4180 T22: 0.0915
REMARK 3 T33: 0.3127 T12: -0.0019
REMARK 3 T13: 0.0452 T23: 0.0158
REMARK 3 L TENSOR
REMARK 3 L11: 1.0261 L22: 4.2777
REMARK 3 L33: 4.2502 L12: -1.8885
REMARK 3 L13: -1.1416 L23: 0.5553
REMARK 3 S TENSOR
REMARK 3 S11: 0.0788 S12: -0.1957 S13: 0.1011
REMARK 3 S21: -0.3874 S22: 0.0179 S23: -0.2622
REMARK 3 S31: 0.1638 S32: -0.2101 S33: -0.0968
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 360 A 376
REMARK 3 ORIGIN FOR THE GROUP (A): 12.9193 15.2457 2.3770
REMARK 3 T TENSOR
REMARK 3 T11: 0.3502 T22: -0.0789
REMARK 3 T33: 0.2996 T12: 0.0766
REMARK 3 T13: 0.0233 T23: 0.0111
REMARK 3 L TENSOR
REMARK 3 L11: 12.0618 L22: 6.5283
REMARK 3 L33: 8.8903 L12: 2.1418
REMARK 3 L13: -2.5851 L23: 2.5026
REMARK 3 S TENSOR
REMARK 3 S11: 0.2374 S12: -0.5799 S13: 0.6434
REMARK 3 S21: -0.4303 S22: -0.3279 S23: -0.0054
REMARK 3 S31: -0.5346 S32: 0.0092 S33: 0.0905
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 377 A 428
REMARK 3 ORIGIN FOR THE GROUP (A): 19.3649 -8.6795 5.7204
REMARK 3 T TENSOR
REMARK 3 T11: 0.3704 T22: 0.1299
REMARK 3 T33: 0.3058 T12: -0.0261
REMARK 3 T13: 0.0599 T23: -0.0341
REMARK 3 L TENSOR
REMARK 3 L11: 2.0314 L22: 4.8143
REMARK 3 L33: 0.6371 L12: -1.9351
REMARK 3 L13: 0.1409 L23: -0.3429
REMARK 3 S TENSOR
REMARK 3 S11: -0.1932 S12: 0.0353 S13: -0.3097
REMARK 3 S21: 0.2586 S22: 0.1385 S23: 0.0459
REMARK 3 S31: 0.1546 S32: -0.0707 S33: 0.0546
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 429 A 460
REMARK 3 ORIGIN FOR THE GROUP (A): 6.7947 -2.5192 6.1084
REMARK 3 T TENSOR
REMARK 3 T11: 0.3010 T22: 0.0162
REMARK 3 T33: 0.2384 T12: -0.0154
REMARK 3 T13: 0.0433 T23: -0.0289
REMARK 3 L TENSOR
REMARK 3 L11: 5.4501 L22: 2.5251
REMARK 3 L33: 3.3245 L12: -1.2504
REMARK 3 L13: -0.0731 L23: -1.4727
REMARK 3 S TENSOR
REMARK 3 S11: -0.0826 S12: -0.0664 S13: -0.3381
REMARK 3 S21: -0.0352 S22: -0.0240 S23: 0.1942
REMARK 3 S31: 0.1876 S32: -0.1108 S33: 0.1066
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 463 A 476
REMARK 3 ORIGIN FOR THE GROUP (A): 6.0652 21.2692 13.3020
REMARK 3 T TENSOR
REMARK 3 T11: 0.4274 T22: 0.1405
REMARK 3 T33: 0.3843 T12: 0.0329
REMARK 3 T13: 0.0018 T23: -0.1079
REMARK 3 L TENSOR
REMARK 3 L11: 5.8738 L22: 20.5179
REMARK 3 L33: 7.7439 L12: 0.0374
REMARK 3 L13: -5.6187 L23: 6.9365
REMARK 3 S TENSOR
REMARK 3 S11: 0.0560 S12: -2.2005 S13: 0.9154
REMARK 3 S21: -0.5379 S22: -0.4832 S23: -0.2098
REMARK 3 S31: -0.7237 S32: -0.7533 S33: 0.4272
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 477 A 519
REMARK 3 ORIGIN FOR THE GROUP (A): -0.7558 -0.5686 8.2786
REMARK 3 T TENSOR
REMARK 3 T11: 0.3668 T22: 0.1596
REMARK 3 T33: 0.1856 T12: 0.0263
REMARK 3 T13: 0.0895 T23: -0.0321
REMARK 3 L TENSOR
REMARK 3 L11: 6.5618 L22: 1.6743
REMARK 3 L33: 0.1962 L12: 0.5255
REMARK 3 L13: 1.1090 L23: -0.0308
REMARK 3 S TENSOR
REMARK 3 S11: -0.0095 S12: -0.0167 S13: -0.2371
REMARK 3 S21: -0.0358 S22: 0.0455 S23: 0.3371
REMARK 3 S31: 0.0787 S32: -0.1166 S33: -0.0360
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 520 A 541
REMARK 3 ORIGIN FOR THE GROUP (A): 31.0054 -0.0463 12.3863
REMARK 3 T TENSOR
REMARK 3 T11: 0.3629 T22: -0.0915
REMARK 3 T33: 0.3370 T12: 0.0765
REMARK 3 T13: 0.0840 T23: -0.0242
REMARK 3 L TENSOR
REMARK 3 L11: 6.6023 L22: 2.6374
REMARK 3 L33: 6.3526 L12: -1.0619
REMARK 3 L13: 5.2287 L23: 1.4947
REMARK 3 S TENSOR
REMARK 3 S11: 0.0363 S12: -0.6032 S13: 0.4708
REMARK 3 S21: 0.2064 S22: 0.1517 S23: -0.3332
REMARK 3 S31: -0.1676 S32: 0.4611 S33: -0.1880
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 542 A 549
REMARK 3 ORIGIN FOR THE GROUP (A): 26.0582 8.0323 14.4646
REMARK 3 T TENSOR
REMARK 3 T11: 0.2630 T22: 0.0188
REMARK 3 T33: 0.2236 T12: 0.0428
REMARK 3 T13: 0.0418 T23: -0.1591
REMARK 3 L TENSOR
REMARK 3 L11: 1.6200 L22: 23.4700
REMARK 3 L33: 28.8158 L12: -2.1171
REMARK 3 L13: 6.4499 L23: -0.3712
REMARK 3 S TENSOR
REMARK 3 S11: 0.0364 S12: -1.7203 S13: 0.4336
REMARK 3 S21: 0.3193 S22: -0.4788 S23: 0.2169
REMARK 3 S31: -0.5630 S32: 0.3878 S33: 0.4424
REMARK 3
REMARK 3 TLS GROUP : 11
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 305 B 327
REMARK 3 ORIGIN FOR THE GROUP (A): -8.3726 -5.7453 31.6273
REMARK 3 T TENSOR
REMARK 3 T11: 0.3832 T22: 0.2154
REMARK 3 T33: 0.2829 T12: -0.0953
REMARK 3 T13: 0.0804 T23: -0.0401
REMARK 3 L TENSOR
REMARK 3 L11: 5.2914 L22: 0.2014
REMARK 3 L33: 8.0469 L12: 0.9158
REMARK 3 L13: 5.6215 L23: 1.2713
REMARK 3 S TENSOR
REMARK 3 S11: 0.0373 S12: -0.0675 S13: -0.2979
REMARK 3 S21: 0.2472 S22: 0.0605 S23: 0.6333
REMARK 3 S31: 0.9491 S32: -0.2402 S33: -0.0978
REMARK 3
REMARK 3 TLS GROUP : 12
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 328 B 338
REMARK 3 ORIGIN FOR THE GROUP (A): 17.1865 12.0457 47.0251
REMARK 3 T TENSOR
REMARK 3 T11: 0.5096 T22: 0.0315
REMARK 3 T33: 0.2923 T12: -0.1654
REMARK 3 T13: 0.0048 T23: -0.0316
REMARK 3 L TENSOR
REMARK 3 L11: 13.4925 L22: 9.4154
REMARK 3 L33: 3.8044 L12: 11.2711
REMARK 3 L13: -7.1645 L23: -5.9849
REMARK 3 S TENSOR
REMARK 3 S11: 0.2635 S12: 0.8592 S13: -0.6929
REMARK 3 S21: 0.7843 S22: -0.2710 S23: -1.1838
REMARK 3 S31: 0.1414 S32: 1.1217 S33: 0.0076
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 339 B 360
REMARK 3 ORIGIN FOR THE GROUP (A): 12.3259 -0.0928 39.7835
REMARK 3 T TENSOR
REMARK 3 T11: 0.3433 T22: 0.1053
REMARK 3 T33: 0.2765 T12: 0.0488
REMARK 3 T13: 0.0190 T23: -0.0881
REMARK 3 L TENSOR
REMARK 3 L11: 1.6946 L22: 4.7192
REMARK 3 L33: 5.4429 L12: 2.0380
REMARK 3 L13: 2.3720 L23: 0.6587
REMARK 3 S TENSOR
REMARK 3 S11: 0.2826 S12: -0.1551 S13: -0.2574
REMARK 3 S21: 0.5865 S22: -0.0981 S23: -0.4334
REMARK 3 S31: 0.1023 S32: 0.1981 S33: -0.1845
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 361 B 375
REMARK 3 ORIGIN FOR THE GROUP (A): 1.4647 -15.6751 30.5043
REMARK 3 T TENSOR
REMARK 3 T11: 0.5342 T22: -0.0756
REMARK 3 T33: 0.2318 T12: -0.1112
REMARK 3 T13: -0.0409 T23: 0.0219
REMARK 3 L TENSOR
REMARK 3 L11: 25.6875 L22: 12.8188
REMARK 3 L33: 13.4210 L12: -7.6401
REMARK 3 L13: -0.7372 L23: 2.3533
REMARK 3 S TENSOR
REMARK 3 S11: -0.2959 S12: -0.6050 S13: -1.2075
REMARK 3 S21: -0.0961 S22: 0.5615 S23: 0.1530
REMARK 3 S31: 0.8275 S32: 0.0455 S33: -0.2656
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 376 B 395
REMARK 3 ORIGIN FOR THE GROUP (A): 7.8717 -0.8563 30.2412
REMARK 3 T TENSOR
REMARK 3 T11: 0.4214 T22: -0.0034
REMARK 3 T33: 0.2458 T12: 0.0081
REMARK 3 T13: 0.0117 T23: -0.0045
REMARK 3 L TENSOR
REMARK 3 L11: 1.5628 L22: 1.2027
REMARK 3 L33: 3.1634 L12: 1.3704
REMARK 3 L13: 0.4376 L23: 0.3267
REMARK 3 S TENSOR
REMARK 3 S11: 0.0833 S12: 0.1100 S13: -0.0674
REMARK 3 S21: 0.0428 S22: -0.1492 S23: -0.1119
REMARK 3 S31: -0.0565 S32: 0.2046 S33: 0.0658
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 396 B 415
REMARK 3 ORIGIN FOR THE GROUP (A): 10.1906 15.0977 35.6992
REMARK 3 T TENSOR
REMARK 3 T11: 0.4723 T22: 0.1257
REMARK 3 T33: 0.2262 T12: -0.0126
REMARK 3 T13: -0.0407 T23: -0.0481
REMARK 3 L TENSOR
REMARK 3 L11: 8.9937 L22: 4.2932
REMARK 3 L33: 13.0844 L12: 0.6192
REMARK 3 L13: -0.0537 L23: -1.8521
REMARK 3 S TENSOR
REMARK 3 S11: -0.1534 S12: -0.2325 S13: 0.5690
REMARK 3 S21: -0.3197 S22: -0.0517 S23: -0.2396
REMARK 3 S31: -0.7540 S32: 0.7306 S33: 0.2051
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 416 B 458
REMARK 3 ORIGIN FOR THE GROUP (A): 6.3939 6.7812 26.0220
REMARK 3 T TENSOR
REMARK 3 T11: 0.3824 T22: 0.1193
REMARK 3 T33: 0.1988 T12: 0.0191
REMARK 3 T13: 0.0911 T23: -0.0302
REMARK 3 L TENSOR
REMARK 3 L11: 4.0144 L22: 5.0056
REMARK 3 L33: 3.1178 L12: 2.5436
REMARK 3 L13: 1.5933 L23: 0.6246
REMARK 3 S TENSOR
REMARK 3 S11: -0.1851 S12: -0.2076 S13: 0.1107
REMARK 3 S21: -0.1168 S22: 0.1459 S23: -0.1530
REMARK 3 S31: -0.2727 S32: 0.0503 S33: 0.0392
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 470 B 479
REMARK 3 ORIGIN FOR THE GROUP (A): -1.2829 -16.1221 18.8623
REMARK 3 T TENSOR
REMARK 3 T11: 0.5684 T22: 0.1819
REMARK 3 T33: 0.2074 T12: -0.0286
REMARK 3 T13: 0.0192 T23: -0.0496
REMARK 3 L TENSOR
REMARK 3 L11: 9.4451 L22: 36.8431
REMARK 3 L33: 2.1597 L12: 1.6396
REMARK 3 L13: -1.8848 L23: -8.4023
REMARK 3 S TENSOR
REMARK 3 S11: 0.2175 S12: 2.0362 S13: -1.7263
REMARK 3 S21: -1.5415 S22: -1.1073 S23: -1.0163
REMARK 3 S31: 1.0091 S32: 0.2463 S33: 0.8899
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 480 B 527
REMARK 3 ORIGIN FOR THE GROUP (A): 0.6048 2.5615 19.3105
REMARK 3 T TENSOR
REMARK 3 T11: 0.4866 T22: 0.1113
REMARK 3 T33: 0.2879 T12: 0.0028
REMARK 3 T13: 0.0541 T23: -0.0722
REMARK 3 L TENSOR
REMARK 3 L11: 5.6984 L22: 2.1207
REMARK 3 L33: 3.4180 L12: -0.1477
REMARK 3 L13: 2.4594 L23: -0.8074
REMARK 3 S TENSOR
REMARK 3 S11: 0.0634 S12: 0.1258 S13: 0.1755
REMARK 3 S21: -0.0208 S22: -0.1233 S23: 0.0323
REMARK 3 S31: 0.1516 S32: 0.0602 S33: 0.0599
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 528 B 548
REMARK 3 ORIGIN FOR THE GROUP (A): 22.7062 -4.9704 35.1980
REMARK 3 T TENSOR
REMARK 3 T11: 0.5081 T22: 0.3747
REMARK 3 T33: 0.3856 T12: 0.1694
REMARK 3 T13: -0.0836 T23: -0.0120
REMARK 3 L TENSOR
REMARK 3 L11: 12.0975 L22: 4.8421
REMARK 3 L33: 7.9986 L12: 7.6535
REMARK 3 L13: -9.8368 L23: -6.2233
REMARK 3 S TENSOR
REMARK 3 S11: -0.0973 S12: -0.6085 S13: -0.3422
REMARK 3 S21: -0.2291 S22: -0.1679 S23: -0.6577
REMARK 3 S31: -1.0185 S32: 0.4143 S33: 0.2653
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 : C 688 C 697
REMARK 3 ORIGIN FOR THE GROUP (A): 24.4536 17.0952 0.8256
REMARK 3 T TENSOR
REMARK 3 T11: 0.3455 T22: 0.1090
REMARK 3 T33: 0.6488 T12: -0.0430
REMARK 3 T13: 0.0699 T23: 0.0414
REMARK 3 L TENSOR
REMARK 3 L11: 0.5220 L22: 42.9826
REMARK 3 L33: 7.5149 L12: 2.8047
REMARK 3 L13: 1.6809 L23: 1.3729
REMARK 3 S TENSOR
REMARK 3 S11: 0.6207 S12: -0.8755 S13: 0.7543
REMARK 3 S21: -1.3458 S22: -0.0975 S23: -0.6032
REMARK 3 S31: -0.4185 S32: 0.6325 S33: -0.5232
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 : D 687 D 691
REMARK 3 ORIGIN FOR THE GROUP (A): 13.9522 -17.5098 37.2950
REMARK 3 T TENSOR
REMARK 3 T11: 0.5259 T22: -0.0008
REMARK 3 T33: 0.2982 T12: -0.0077
REMARK 3 T13: -0.1953 T23: 0.0734
REMARK 3 L TENSOR
REMARK 3 L11: 25.2733 L22: 43.1947
REMARK 3 L33: 23.3938 L12: -12.2589
REMARK 3 L13: -16.1734 L23: -14.1972
REMARK 3 S TENSOR
REMARK 3 S11: -0.2135 S12: -0.4814 S13: -2.1094
REMARK 3 S21: 0.5493 S22: 0.4979 S23: 0.6325
REMARK 3 S31: -0.7181 S32: 1.8466 S33: -0.2845
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 : D 692 D 696
REMARK 3 ORIGIN FOR THE GROUP (A): 6.7840 -17.5121 40.4696
REMARK 3 T TENSOR
REMARK 3 T11: 0.5287 T22: 0.2182
REMARK 3 T33: 0.7629 T12: 0.0741
REMARK 3 T13: 0.0552 T23: -0.0051
REMARK 3 L TENSOR
REMARK 3 L11: 5.2613 L22: 0.0022
REMARK 3 L33: 123.1497 L12: -0.1072
REMARK 3 L13: 25.4543 L23: -0.5184
REMARK 3 S TENSOR
REMARK 3 S11: 2.2407 S12: 0.1993 S13: -2.5494
REMARK 3 S21: 1.8992 S22: -0.5651 S23: 3.9229
REMARK 3 S31: 1.3994 S32: -3.6707 S33: -1.6756
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 2Q6J COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-JUN-07.
REMARK 100 THE DEPOSITION ID IS D_1000043211.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 08-NOV-04
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 19-BM
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97934
REMARK 200 MONOCHROMATOR : ROSENBAUM-ROCK DOUBLE-CRYSTAL
REMARK 200 MONOCHROMATOR
REMARK 200 OPTICS : ROSENBAUM-ROCK VERTICAL FOCUSING
REMARK 200 MIRROR
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : SBC
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO, HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 12940
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.700
REMARK 200 RESOLUTION RANGE LOW (A) : 12.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 93.4
REMARK 200 DATA REDUNDANCY : 3.600
REMARK 200 R MERGE (I) : 0.10900
REMARK 200 R SYM (I) : 0.10900
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 6.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.80
REMARK 200 COMPLETENESS FOR SHELL (%) : 82.3
REMARK 200 DATA REDUNDANCY IN SHELL : 3.10
REMARK 200 R MERGE FOR SHELL (I) : 0.40100
REMARK 200 R SYM FOR SHELL (I) : 0.40100
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.270
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: PDB ENTRY 3ERD
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 37.15
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.96
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 25-28% (W/V) PEG MONOMETHYL ETHER
REMARK 280 2000, 0.1M BIS TRIS PH 6.5, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 298K
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 39.90100
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: 6890 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 20620 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -44.0 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 SER A 305
REMARK 465 PHE A 461
REMARK 465 LEU A 462
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 TYR B 459
REMARK 465 THR B 460
REMARK 465 PHE B 461
REMARK 465 LEU B 462
REMARK 465 SER B 463
REMARK 465 SER B 464
REMARK 465 THR B 465
REMARK 465 LEU B 466
REMARK 465 LYS B 467
REMARK 465 SER B 468
REMARK 465 LEU B 469
REMARK 465 LEU B 549
REMARK 465 HIS B 550
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 HIS C 687
REMARK 465 SER C 698
REMARK 465 LYS D 686
REMARK 465 SER D 697
REMARK 465 SER D 698
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 O MET A 343 CG2 THR A 347 1.71
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 SER A 309 22.52 -69.47
REMARK 500 GLU A 330 105.32 -48.00
REMARK 500 TYR A 331 -141.21 -68.37
REMARK 500 ASP A 332 92.23 -14.92
REMARK 500 THR A 334 70.33 -117.58
REMARK 500 ARG A 335 141.57 172.68
REMARK 500 LEU A 372 -58.99 -12.05
REMARK 500 LEU A 440 150.58 -44.79
REMARK 500 SER A 464 105.54 -161.53
REMARK 500 THR A 465 147.35 68.30
REMARK 500 LEU A 466 -8.36 -54.01
REMARK 500 ASP A 545 -7.21 -59.63
REMARK 500 GLU B 330 89.67 -51.49
REMARK 500 PRO B 336 176.32 -59.77
REMARK 500 GLU B 523 -71.20 -60.32
REMARK 500 LEU B 525 -13.21 -146.46
REMARK 500 LYS B 531 79.95 -68.39
REMARK 500 ASN B 532 80.16 -69.42
REMARK 500 SER B 537 163.21 -46.33
REMARK 500 LYS D 688 136.47 -177.86
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 A48 A 700
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE A48 B 800
DBREF 2Q6J A 298 554 UNP P03372 ESR1_HUMAN 298 554
DBREF 2Q6J B 298 554 UNP P03372 ESR1_HUMAN 298 554
DBREF 2Q6J C 686 698 UNP Q8BN74 Q8BN74_MOUSE 686 698
DBREF 2Q6J D 686 698 UNP Q8BN74 Q8BN74_MOUSE 686 698
SEQADV 2Q6J SER A 297 UNP P03372 CLONING ARTIFACT
SEQADV 2Q6J SER A 537 UNP P03372 TYR 537 ENGINEERED MUTATION
SEQADV 2Q6J SER B 297 UNP P03372 CLONING ARTIFACT
SEQADV 2Q6J 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 A48 A 700 32
HET A48 B 800 32
HETNAM A48 4-[(DIMESITYLBORYL)(2,2,2-TRIFLUOROETHYL)AMINO]PHENOL
HETSYN A48 (N-2,2,2-TRIFLUOROETHYL-P-HYDROXYLANILINO)
HETSYN 2 A48 DIMESITYLBORANE
FORMUL 5 A48 2(C26 H29 B F3 N O)
FORMUL 7 HOH *(H2 O)
HELIX 1 1 THR A 311 ASP A 321 1 11
HELIX 2 2 SER A 338 ARG A 363 1 26
HELIX 3 3 GLY A 366 LEU A 370 5 5
HELIX 4 4 THR A 371 SER A 395 1 25
HELIX 5 5 MET A 396 HIS A 398 5 3
HELIX 6 6 ASN A 413 GLY A 415 5 3
HELIX 7 7 GLY A 420 ASN A 439 1 20
HELIX 8 8 GLN A 441 GLY A 457 1 17
HELIX 9 9 SER A 464 ALA A 493 1 30
HELIX 10 10 THR A 496 LYS A 531 1 36
HELIX 11 11 SER A 537 ASP A 545 1 9
HELIX 12 12 SER B 305 LEU B 310 5 6
HELIX 13 13 THR B 311 GLU B 323 1 13
HELIX 14 14 SER B 338 ARG B 363 1 26
HELIX 15 15 GLY B 366 LEU B 370 5 5
HELIX 16 16 THR B 371 SER B 395 1 25
HELIX 17 17 ASN B 413 LYS B 416 5 4
HELIX 18 18 GLY B 420 ASN B 439 1 20
HELIX 19 19 GLN B 441 SER B 456 1 16
HELIX 20 20 GLU B 470 GLY B 494 1 25
HELIX 21 21 THR B 496 HIS B 524 1 29
HELIX 22 22 TYR B 526 LYS B 531 1 6
HELIX 23 23 SER B 537 ALA B 546 1 10
HELIX 24 24 LYS C 688 ASP C 696 1 9
HELIX 25 25 LYS D 688 LEU D 693 1 6
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 408 N ALA A 405
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 THR A 347 ALA A 350
SITE 2 AC1 15 GLU A 353 LEU A 384 PHE A 404 GLU A 419
SITE 3 AC1 15 MET A 421 ILE A 424 LEU A 428 GLY A 521
SITE 4 AC1 15 HIS A 524 LEU A 525 LEU A 540
SITE 1 AC2 13 MET B 343 LEU B 346 THR B 347 GLU B 353
SITE 2 AC2 13 LEU B 384 PHE B 404 MET B 421 ILE B 424
SITE 3 AC2 13 PHE B 425 LEU B 428 HIS B 524 LEU B 525
SITE 4 AC2 13 LEU B 540
CRYST1 55.551 79.802 58.328 90.00 109.88 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 0.018001 0.000000 0.006508 0.00000
SCALE2 0.000000 0.012531 0.000000 0.00000
SCALE3 0.000000 0.000000 0.018230 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
