HEADER TRANSCRIPTION 14-MAR-11 3R2A
TITLE CRYSTAL STRUCTURE OF RXRALPHA LIGAND-BINDING DOMAIN COMPLEXED WITH
TITLE 2 COREPRESSOR SMRT2 AND ANTAGONIST RHEIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: RETINOIC ACID RECEPTOR RXR-ALPHA;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 FRAGMENT: LIGAND BINDING DOMAIN (UNP RESIDUES 223-462);
COMPND 5 SYNONYM: RETINOID X RECEPTOR ALPHA, NUCLEAR RECEPTOR SUBFAMILY 2
COMPND 6 GROUP B MEMBER 1;
COMPND 7 ENGINEERED: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: NUCLEAR RECEPTOR COREPRESSOR 2;
COMPND 10 CHAIN: E, F;
COMPND 11 FRAGMENT: UNP RESIDUES 2346-2361;
COMPND 12 SYNONYM: SMRT, N-COR2, CTG REPEAT PROTEIN 26, SMAP270, SILENCING
COMPND 13 MEDIATOR OF RETINOIC ACID AND THYROID HORMONE RECEPTOR, T3 RECEPTOR-
COMPND 14 ASSOCIATING FACTOR, TRAC, THYROID-RECEPTOR-ASSOCIATED COREPRESSOR,
COMPND 15 RETINOIC-ACID-RECEPTOR-ASSOCIATED COREPRESSOR;
COMPND 16 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: RXRA, NR2B1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 MOL_ID: 2;
SOURCE 9 SYNTHETIC: YES;
SOURCE 10 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 11 ORGANISM_COMMON: HUMAN;
SOURCE 12 ORGANISM_TAXID: 9606
KEYWDS NUCLEAR RECEPTOR, TRANSCRIPTION FACTOR, LIGAND-BINDING DOMAIN,
KEYWDS 2 TRANSCRIPTION
EXPDTA X-RAY DIFFRACTION
AUTHOR H.ZHANG,L.CHEN,J.CHEN,H.JIANG,X.SHEN
REVDAT 3 27-JUL-11 3R2A 1 JRNL
REVDAT 2 08-JUN-11 3R2A 1 JRNL
REVDAT 1 25-MAY-11 3R2A 0
JRNL AUTH H.ZHANG,L.CHEN,J.CHEN,H.JIANG,X.SHEN
JRNL TITL STRUCTURAL BASIS FOR RETINOIC X RECEPTOR REPRESSION ON THE
JRNL TITL 2 TETRAMER.
JRNL REF J.BIOL.CHEM. V. 286 24593 2011
JRNL REFN ISSN 0021-9258
JRNL PMID 21613212
JRNL DOI 10.1074/JBC.M111.245498
REMARK 2
REMARK 2 RESOLUTION. 3.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 42.52
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 21632
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) : 0.258
REMARK 3 R VALUE (WORKING SET) : 0.254
REMARK 3 FREE R VALUE : 0.335
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1167
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) : 3.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.08
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1397
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.00
REMARK 3 BIN R VALUE (WORKING SET) : 0.2910
REMARK 3 BIN FREE R VALUE SET COUNT : 70
REMARK 3 BIN FREE R VALUE : 0.4040
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6838
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 42
REMARK 3 SOLVENT ATOMS : 60
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 71.16
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.04000
REMARK 3 B22 (A**2) : 0.06000
REMARK 3 B33 (A**2) : -0.02000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.577
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.445
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 23.862
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.900
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.819
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 6992 ; 0.010 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 9453 ; 1.353 ; 1.990
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 853 ; 6.323 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 301 ;37.360 ;23.821
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1268 ;19.782 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 48 ;19.141 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1080 ; 0.096 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5158 ; 0.004 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 3509 ; 0.234 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 4791 ; 0.310 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 256 ; 0.150 ; 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): 156 ; 0.220 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 3 ; 0.120 ; 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): 4413 ; 0.509 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 6929 ; 0.924 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2999 ; 0.828 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2524 ; 1.449 ; 4.500
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 : NULL
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 3R2A COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-MAR-11.
REMARK 100 THE RCSB ID CODE IS RCSB064398.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 18-JAN-11
REMARK 200 TEMPERATURE (KELVIN) : 277
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRF
REMARK 200 BEAMLINE : BL17U
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9793
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 : 23843
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.000
REMARK 200 RESOLUTION RANGE LOW (A) : 82.979
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.0
REMARK 200 DATA REDUNDANCY : 3.600
REMARK 200 R MERGE (I) : 0.08300
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 29.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.10
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 3.80
REMARK 200 R MERGE FOR SHELL (I) : 0.54200
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.100
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: PDB ENTRY 3NSP
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 53.39
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.64
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM SODIUM CACODYLATE, 20% PEG4000,
REMARK 280 100 MM MAGNESIUM ACETATE, PH 6.5, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 42.51500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 58.56000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 58.79000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 58.56000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 42.51500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 58.79000
REMARK 290 SMTRY3 4 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: HEXAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 13450 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 37000 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -77.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, D, F, B, C, E
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 THR A 223
REMARK 465 SER A 224
REMARK 465 SER A 225
REMARK 465 THR A 246
REMARK 465 GLU A 247
REMARK 465 THR A 248
REMARK 465 TYR A 249
REMARK 465 VAL A 250
REMARK 465 GLU A 251
REMARK 465 ALA A 252
REMARK 465 ASN A 253
REMARK 465 MET A 254
REMARK 465 GLY A 255
REMARK 465 LEU A 256
REMARK 465 ASN A 257
REMARK 465 PRO A 258
REMARK 465 SER A 259
REMARK 465 SER A 260
REMARK 465 PRO A 261
REMARK 465 ASN A 262
REMARK 465 MET A 454
REMARK 465 LEU A 455
REMARK 465 GLU A 456
REMARK 465 ALA A 457
REMARK 465 PRO A 458
REMARK 465 HIS A 459
REMARK 465 GLN A 460
REMARK 465 MET A 461
REMARK 465 THR A 462
REMARK 465 THR B 223
REMARK 465 SER B 224
REMARK 465 SER B 225
REMARK 465 ALA B 226
REMARK 465 PRO B 244
REMARK 465 LYS B 245
REMARK 465 THR B 246
REMARK 465 GLU B 247
REMARK 465 THR B 248
REMARK 465 TYR B 249
REMARK 465 VAL B 250
REMARK 465 GLU B 251
REMARK 465 ALA B 252
REMARK 465 ASN B 253
REMARK 465 MET B 254
REMARK 465 GLY B 255
REMARK 465 LEU B 256
REMARK 465 ASN B 257
REMARK 465 PRO B 258
REMARK 465 SER B 259
REMARK 465 SER B 260
REMARK 465 PRO B 261
REMARK 465 THR B 462
REMARK 465 THR C 223
REMARK 465 SER C 224
REMARK 465 SER C 225
REMARK 465 ALA C 226
REMARK 465 ASN C 227
REMARK 465 LYS C 245
REMARK 465 THR C 246
REMARK 465 GLU C 247
REMARK 465 THR C 248
REMARK 465 TYR C 249
REMARK 465 VAL C 250
REMARK 465 GLU C 251
REMARK 465 ALA C 252
REMARK 465 ASN C 253
REMARK 465 MET C 254
REMARK 465 GLY C 255
REMARK 465 LEU C 256
REMARK 465 ASN C 257
REMARK 465 PRO C 258
REMARK 465 SER C 259
REMARK 465 SER C 260
REMARK 465 PRO C 261
REMARK 465 ASN C 262
REMARK 465 ASP C 263
REMARK 465 PRO C 264
REMARK 465 VAL C 265
REMARK 465 THR C 266
REMARK 465 ASN C 267
REMARK 465 MET C 454
REMARK 465 LEU C 455
REMARK 465 GLU C 456
REMARK 465 ALA C 457
REMARK 465 PRO C 458
REMARK 465 HIS C 459
REMARK 465 GLN C 460
REMARK 465 MET C 461
REMARK 465 THR C 462
REMARK 465 THR D 223
REMARK 465 SER D 224
REMARK 465 SER D 225
REMARK 465 ALA D 226
REMARK 465 THR D 248
REMARK 465 TYR D 249
REMARK 465 VAL D 250
REMARK 465 GLU D 251
REMARK 465 ALA D 252
REMARK 465 ASN D 253
REMARK 465 MET D 254
REMARK 465 GLY D 255
REMARK 465 LEU D 256
REMARK 465 ASN D 257
REMARK 465 PRO D 258
REMARK 465 SER D 259
REMARK 465 SER D 260
REMARK 465 PRO D 261
REMARK 465 ASN D 262
REMARK 465 ASP D 263
REMARK 465 THR D 462
REMARK 465 THR E 2337
REMARK 465 ILE E 2345
REMARK 465 ARG E 2346
REMARK 465 LYS E 2347
REMARK 465 ALA E 2348
REMARK 465 LEU E 2349
REMARK 465 MET E 2350
REMARK 465 GLY E 2351
REMARK 465 LYS E 2352
REMARK 465 ARG F 2346
REMARK 465 LYS F 2347
REMARK 465 ALA F 2348
REMARK 465 LEU F 2349
REMARK 465 MET F 2350
REMARK 465 GLY F 2351
REMARK 465 LYS F 2352
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 NE2 GLN B 275 OG1 THR B 278 1.04
REMARK 500 OE1 GLU B 366 NH2 ARG B 414 1.04
REMARK 500 CD PRO D 264 OD1 ASN D 267 1.06
REMARK 500 CD2 HIS B 315 CD2 LEU B 367 1.06
REMARK 500 ND2 ASN B 267 CD1 LEU B 330 1.10
REMARK 500 NE2 GLN B 275 CB THR B 278 1.14
REMARK 500 OE2 GLU A 453 OD2 ASP D 273 1.16
REMARK 500 CD1 ILE C 447 N ASP C 448 1.17
REMARK 500 ND2 ASN B 385 OE1 GLU B 388 1.18
REMARK 500 CG LYS B 381 CG2 THR C 445 1.19
REMARK 500 CD PRO D 264 CG ASN D 267 1.26
REMARK 500 N PRO D 264 ND2 ASN D 267 1.35
REMARK 500 OE1 GLU C 390 NZ LYS D 417 1.35
REMARK 500 OD2 ASP A 263 O HOH A 59 1.40
REMARK 500 NZ LYS C 440 CE2 PHE C 450 1.46
REMARK 500 CG HIS B 315 CD2 LEU B 367 1.48
REMARK 500 OE1 GLU D 366 NH2 ARG D 414 1.50
REMARK 500 OE2 GLU C 434 OE1 GLU D 434 1.51
REMARK 500 CD PRO D 264 ND2 ASN D 267 1.53
REMARK 500 CD2 HIS D 315 CD2 LEU D 367 1.59
REMARK 500 O ASP B 444 CD PRO B 446 1.61
REMARK 500 CE LYS B 381 OG1 THR C 445 1.63
REMARK 500 O LEU D 236 CD1 LEU D 240 1.65
REMARK 500 CD LYS B 381 CG2 THR C 445 1.68
REMARK 500 OE2 GLU D 366 NH2 ARG D 414 1.69
REMARK 500 O GLU B 456 CB HIS B 459 1.71
REMARK 500 O ASP D 448 O LEU D 451 1.71
REMARK 500 OE2 GLU D 281 NH2 ARG D 285 1.72
REMARK 500 O ASP B 448 O LEU B 451 1.72
REMARK 500 CA PRO D 264 ND2 ASN D 267 1.76
REMARK 500 OD1 ASP C 296 OG SER C 384 1.77
REMARK 500 O PRO D 264 ND2 ASN D 267 1.77
REMARK 500 CD GLU D 366 NH2 ARG D 414 1.78
REMARK 500 C PRO D 264 ND2 ASN D 267 1.79
REMARK 500 OD1 ASP A 296 OG SER A 384 1.80
REMARK 500 CE LYS B 381 CG2 THR C 445 1.80
REMARK 500 CG2 ILE B 442 O HOH D 55 1.81
REMARK 500 OD1 ASN D 385 CB GLU D 388 1.83
REMARK 500 OD2 ASP A 363 OE2 GLU A 366 1.86
REMARK 500 CE LYS B 381 CB THR C 445 1.90
REMARK 500 OD1 ASN B 267 CD1 LEU B 326 1.91
REMARK 500 OG SER B 312 NH1 ARG B 371 1.92
REMARK 500 OD1 ASN D 385 N GLU D 388 1.93
REMARK 500 O LEU D 350 OG SER D 355 1.93
REMARK 500 OE1 GLU B 239 NE1 TRP B 282 1.94
REMARK 500 N PRO D 264 CG ASN D 267 1.95
REMARK 500 CD GLU B 366 NH2 ARG B 414 1.96
REMARK 500 CG HIS D 315 CD2 LEU D 367 1.99
REMARK 500 CD GLU A 453 OD2 ASP D 273 2.01
REMARK 500 CD GLN B 275 OG1 THR B 278 2.02
REMARK 500
REMARK 500 THIS ENTRY HAS 67 CLOSE CONTACTS
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 NH1 ARG B 285 OE1 GLU D 237 1655 2.00
REMARK 500 NH1 ARG B 285 OE2 GLU D 237 1655 2.15
REMARK 500 NZ LYS B 321 OD1 ASP C 273 3454 2.18
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 CYS A 369 CB CYS A 369 SG -0.109
REMARK 500 CYS A 432 CB CYS A 432 SG -0.109
REMARK 500 CYS B 369 CB CYS B 369 SG -0.102
REMARK 500 ARG B 371 CG ARG B 371 CD -0.224
REMARK 500 ARG B 371 CD ARG B 371 NE -0.119
REMARK 500 ARG B 371 CZ ARG B 371 NH1 -0.141
REMARK 500 GLU C 366 CD GLU C 366 OE2 0.076
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 PRO A 231 C - N - CD ANGL. DEV. = -19.0 DEGREES
REMARK 500 ILE A 442 N - CA - C ANGL. DEV. = -22.2 DEGREES
REMARK 500 PRO B 231 C - N - CD ANGL. DEV. = -16.9 DEGREES
REMARK 500 PRO B 287 C - N - CD ANGL. DEV. = -16.0 DEGREES
REMARK 500 ARG B 371 CG - CD - NE ANGL. DEV. = 27.0 DEGREES
REMARK 500 ARG B 371 CD - NE - CZ ANGL. DEV. = -11.6 DEGREES
REMARK 500 ARG B 371 NE - CZ - NH1 ANGL. DEV. = -4.4 DEGREES
REMARK 500 PRO B 409 C - N - CA ANGL. DEV. = 9.6 DEGREES
REMARK 500 PRO B 409 C - N - CD ANGL. DEV. = -18.1 DEGREES
REMARK 500 PRO B 446 C - N - CD ANGL. DEV. = -19.0 DEGREES
REMARK 500 LEU B 451 N - CA - C ANGL. DEV. = -18.1 DEGREES
REMARK 500 PRO B 458 C - N - CD ANGL. DEV. = -22.2 DEGREES
REMARK 500 HIS B 459 N - CA - C ANGL. DEV. = -20.5 DEGREES
REMARK 500 ASP C 273 N - CA - C ANGL. DEV. = -19.2 DEGREES
REMARK 500 GLU C 366 OE1 - CD - OE2 ANGL. DEV. = -33.5 DEGREES
REMARK 500 GLU C 366 CG - CD - OE2 ANGL. DEV. = 35.6 DEGREES
REMARK 500 THR C 449 N - CA - C ANGL. DEV. = -19.1 DEGREES
REMARK 500 PRO D 244 C - N - CD ANGL. DEV. = -15.1 DEGREES
REMARK 500 GLY D 304 N - CA - C ANGL. DEV. = -15.8 DEGREES
REMARK 500 PRO D 409 C - N - CA ANGL. DEV. = 9.6 DEGREES
REMARK 500 PRO D 409 C - N - CD ANGL. DEV. = -14.0 DEGREES
REMARK 500 ILE D 447 CB - CA - C ANGL. DEV. = -16.3 DEGREES
REMARK 500 LEU D 451 N - CA - C ANGL. DEV. = -16.4 DEGREES
REMARK 500 MET D 452 N - CA - C ANGL. DEV. = 16.4 DEGREES
REMARK 500 PRO D 458 C - N - CD ANGL. DEV. = -19.1 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 HIS A 288 -2.71 80.54
REMARK 500 LEU A 353 -63.98 -120.24
REMARK 500 THR A 445 -130.73 60.04
REMARK 500 ASP A 448 0.86 80.54
REMARK 500 LEU B 455 57.50 -143.04
REMARK 500 GLN B 460 86.85 -63.65
REMARK 500 ALA C 272 -24.38 99.02
REMARK 500 THR C 445 -129.88 59.15
REMARK 500 HIS D 288 -8.68 83.39
REMARK 500 TRP D 305 -76.86 132.25
REMARK 500 VAL D 342 30.07 -96.75
REMARK 500 ILE D 447 6.21 86.47
REMARK 500 GLU E2342 22.27 -73.58
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 GLY D 443 ASP D 444 -138.08
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500 M RES CSSEQI IMPROPER EXPECTED FOUND DETAILS
REMARK 500 PHE A 313 24.0 L L OUTSIDE RANGE
REMARK 500 TYR A 397 23.4 L L OUTSIDE RANGE
REMARK 500 ILE A 442 46.4 L L OUTSIDE RANGE
REMARK 500 ALA B 271 23.9 L L OUTSIDE RANGE
REMARK 500 ALA B 272 23.9 L L OUTSIDE RANGE
REMARK 500 HIS B 459 47.2 L L OUTSIDE RANGE
REMARK 500 PRO C 293 45.2 L L OUTSIDE RANGE
REMARK 500 GLN D 275 24.8 L L OUTSIDE RANGE
REMARK 500 PRO D 293 45.4 L L OUTSIDE RANGE
REMARK 500 LEU D 330 24.7 L L OUTSIDE RANGE
REMARK 500 MET D 452 22.2 L L OUTSIDE RANGE
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH B 31 DISTANCE = 5.10 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE RHN A 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE RHN C 2
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3R29 RELATED DB: PDB
DBREF 3R2A A 223 462 UNP P19793 RXRA_HUMAN 223 462
DBREF 3R2A B 223 462 UNP P19793 RXRA_HUMAN 223 462
DBREF 3R2A C 223 462 UNP P19793 RXRA_HUMAN 223 462
DBREF 3R2A D 223 462 UNP P19793 RXRA_HUMAN 223 462
DBREF 3R2A E 2337 2352 UNP Q9Y618 NCOR2_HUMAN 2346 2361
DBREF 3R2A F 2337 2352 UNP Q9Y618 NCOR2_HUMAN 2346 2361
SEQRES 1 A 240 THR SER SER ALA ASN GLU ASP MET PRO VAL GLU ARG ILE
SEQRES 2 A 240 LEU GLU ALA GLU LEU ALA VAL GLU PRO LYS THR GLU THR
SEQRES 3 A 240 TYR VAL GLU ALA ASN MET GLY LEU ASN PRO SER SER PRO
SEQRES 4 A 240 ASN ASP PRO VAL THR ASN ILE CYS GLN ALA ALA ASP LYS
SEQRES 5 A 240 GLN LEU PHE THR LEU VAL GLU TRP ALA LYS ARG ILE PRO
SEQRES 6 A 240 HIS PHE SER GLU LEU PRO LEU ASP ASP GLN VAL ILE LEU
SEQRES 7 A 240 LEU ARG ALA GLY TRP ASN GLU LEU LEU ILE ALA SER PHE
SEQRES 8 A 240 SER HIS ARG SER ILE ALA VAL LYS ASP GLY ILE LEU LEU
SEQRES 9 A 240 ALA THR GLY LEU HIS VAL HIS ARG ASN SER ALA HIS SER
SEQRES 10 A 240 ALA GLY VAL GLY ALA ILE PHE ASP ARG VAL LEU THR GLU
SEQRES 11 A 240 LEU VAL SER LYS MET ARG ASP MET GLN MET ASP LYS THR
SEQRES 12 A 240 GLU LEU GLY CYS LEU ARG ALA ILE VAL LEU PHE ASN PRO
SEQRES 13 A 240 ASP SER LYS GLY LEU SER ASN PRO ALA GLU VAL GLU ALA
SEQRES 14 A 240 LEU ARG GLU LYS VAL TYR ALA SER LEU GLU ALA TYR CYS
SEQRES 15 A 240 LYS HIS LYS TYR PRO GLU GLN PRO GLY ARG PHE ALA LYS
SEQRES 16 A 240 LEU LEU LEU ARG LEU PRO ALA LEU ARG SER ILE GLY LEU
SEQRES 17 A 240 LYS CYS LEU GLU HIS LEU PHE PHE PHE LYS LEU ILE GLY
SEQRES 18 A 240 ASP THR PRO ILE ASP THR PHE LEU MET GLU MET LEU GLU
SEQRES 19 A 240 ALA PRO HIS GLN MET THR
SEQRES 1 B 240 THR SER SER ALA ASN GLU ASP MET PRO VAL GLU ARG ILE
SEQRES 2 B 240 LEU GLU ALA GLU LEU ALA VAL GLU PRO LYS THR GLU THR
SEQRES 3 B 240 TYR VAL GLU ALA ASN MET GLY LEU ASN PRO SER SER PRO
SEQRES 4 B 240 ASN ASP PRO VAL THR ASN ILE CYS GLN ALA ALA ASP LYS
SEQRES 5 B 240 GLN LEU PHE THR LEU VAL GLU TRP ALA LYS ARG ILE PRO
SEQRES 6 B 240 HIS PHE SER GLU LEU PRO LEU ASP ASP GLN VAL ILE LEU
SEQRES 7 B 240 LEU ARG ALA GLY TRP ASN GLU LEU LEU ILE ALA SER PHE
SEQRES 8 B 240 SER HIS ARG SER ILE ALA VAL LYS ASP GLY ILE LEU LEU
SEQRES 9 B 240 ALA THR GLY LEU HIS VAL HIS ARG ASN SER ALA HIS SER
SEQRES 10 B 240 ALA GLY VAL GLY ALA ILE PHE ASP ARG VAL LEU THR GLU
SEQRES 11 B 240 LEU VAL SER LYS MET ARG ASP MET GLN MET ASP LYS THR
SEQRES 12 B 240 GLU LEU GLY CYS LEU ARG ALA ILE VAL LEU PHE ASN PRO
SEQRES 13 B 240 ASP SER LYS GLY LEU SER ASN PRO ALA GLU VAL GLU ALA
SEQRES 14 B 240 LEU ARG GLU LYS VAL TYR ALA SER LEU GLU ALA TYR CYS
SEQRES 15 B 240 LYS HIS LYS TYR PRO GLU GLN PRO GLY ARG PHE ALA LYS
SEQRES 16 B 240 LEU LEU LEU ARG LEU PRO ALA LEU ARG SER ILE GLY LEU
SEQRES 17 B 240 LYS CYS LEU GLU HIS LEU PHE PHE PHE LYS LEU ILE GLY
SEQRES 18 B 240 ASP THR PRO ILE ASP THR PHE LEU MET GLU MET LEU GLU
SEQRES 19 B 240 ALA PRO HIS GLN MET THR
SEQRES 1 C 240 THR SER SER ALA ASN GLU ASP MET PRO VAL GLU ARG ILE
SEQRES 2 C 240 LEU GLU ALA GLU LEU ALA VAL GLU PRO LYS THR GLU THR
SEQRES 3 C 240 TYR VAL GLU ALA ASN MET GLY LEU ASN PRO SER SER PRO
SEQRES 4 C 240 ASN ASP PRO VAL THR ASN ILE CYS GLN ALA ALA ASP LYS
SEQRES 5 C 240 GLN LEU PHE THR LEU VAL GLU TRP ALA LYS ARG ILE PRO
SEQRES 6 C 240 HIS PHE SER GLU LEU PRO LEU ASP ASP GLN VAL ILE LEU
SEQRES 7 C 240 LEU ARG ALA GLY TRP ASN GLU LEU LEU ILE ALA SER PHE
SEQRES 8 C 240 SER HIS ARG SER ILE ALA VAL LYS ASP GLY ILE LEU LEU
SEQRES 9 C 240 ALA THR GLY LEU HIS VAL HIS ARG ASN SER ALA HIS SER
SEQRES 10 C 240 ALA GLY VAL GLY ALA ILE PHE ASP ARG VAL LEU THR GLU
SEQRES 11 C 240 LEU VAL SER LYS MET ARG ASP MET GLN MET ASP LYS THR
SEQRES 12 C 240 GLU LEU GLY CYS LEU ARG ALA ILE VAL LEU PHE ASN PRO
SEQRES 13 C 240 ASP SER LYS GLY LEU SER ASN PRO ALA GLU VAL GLU ALA
SEQRES 14 C 240 LEU ARG GLU LYS VAL TYR ALA SER LEU GLU ALA TYR CYS
SEQRES 15 C 240 LYS HIS LYS TYR PRO GLU GLN PRO GLY ARG PHE ALA LYS
SEQRES 16 C 240 LEU LEU LEU ARG LEU PRO ALA LEU ARG SER ILE GLY LEU
SEQRES 17 C 240 LYS CYS LEU GLU HIS LEU PHE PHE PHE LYS LEU ILE GLY
SEQRES 18 C 240 ASP THR PRO ILE ASP THR PHE LEU MET GLU MET LEU GLU
SEQRES 19 C 240 ALA PRO HIS GLN MET THR
SEQRES 1 D 240 THR SER SER ALA ASN GLU ASP MET PRO VAL GLU ARG ILE
SEQRES 2 D 240 LEU GLU ALA GLU LEU ALA VAL GLU PRO LYS THR GLU THR
SEQRES 3 D 240 TYR VAL GLU ALA ASN MET GLY LEU ASN PRO SER SER PRO
SEQRES 4 D 240 ASN ASP PRO VAL THR ASN ILE CYS GLN ALA ALA ASP LYS
SEQRES 5 D 240 GLN LEU PHE THR LEU VAL GLU TRP ALA LYS ARG ILE PRO
SEQRES 6 D 240 HIS PHE SER GLU LEU PRO LEU ASP ASP GLN VAL ILE LEU
SEQRES 7 D 240 LEU ARG ALA GLY TRP ASN GLU LEU LEU ILE ALA SER PHE
SEQRES 8 D 240 SER HIS ARG SER ILE ALA VAL LYS ASP GLY ILE LEU LEU
SEQRES 9 D 240 ALA THR GLY LEU HIS VAL HIS ARG ASN SER ALA HIS SER
SEQRES 10 D 240 ALA GLY VAL GLY ALA ILE PHE ASP ARG VAL LEU THR GLU
SEQRES 11 D 240 LEU VAL SER LYS MET ARG ASP MET GLN MET ASP LYS THR
SEQRES 12 D 240 GLU LEU GLY CYS LEU ARG ALA ILE VAL LEU PHE ASN PRO
SEQRES 13 D 240 ASP SER LYS GLY LEU SER ASN PRO ALA GLU VAL GLU ALA
SEQRES 14 D 240 LEU ARG GLU LYS VAL TYR ALA SER LEU GLU ALA TYR CYS
SEQRES 15 D 240 LYS HIS LYS TYR PRO GLU GLN PRO GLY ARG PHE ALA LYS
SEQRES 16 D 240 LEU LEU LEU ARG LEU PRO ALA LEU ARG SER ILE GLY LEU
SEQRES 17 D 240 LYS CYS LEU GLU HIS LEU PHE PHE PHE LYS LEU ILE GLY
SEQRES 18 D 240 ASP THR PRO ILE ASP THR PHE LEU MET GLU MET LEU GLU
SEQRES 19 D 240 ALA PRO HIS GLN MET THR
SEQRES 1 E 16 THR ASN MET GLY LEU GLU ALA ILE ILE ARG LYS ALA LEU
SEQRES 2 E 16 MET GLY LYS
SEQRES 1 F 16 THR ASN MET GLY LEU GLU ALA ILE ILE ARG LYS ALA LEU
SEQRES 2 F 16 MET GLY LYS
HET RHN A 1 21
HET RHN C 2 21
HETNAM RHN 4,5-DIHYDROXY-9,10-DIOXO-9,10-DIHYDROANTHRACENE-2-
HETNAM 2 RHN CARBOXYLIC ACID
HETSYN RHN RHEIN; RHUBARB YELLOW
FORMUL 7 RHN 2(C15 H8 O6)
FORMUL 9 HOH *60(H2 O)
HELIX 1 1 PRO A 231 GLU A 243 1 13
HELIX 2 2 ASP A 263 ALA A 271 1 9
HELIX 3 3 ALA A 271 ARG A 285 1 15
HELIX 4 4 PRO A 293 GLY A 304 1 12
HELIX 5 5 GLY A 304 SER A 317 1 14
HELIX 6 6 ARG A 334 ALA A 340 1 7
HELIX 7 7 VAL A 342 LEU A 353 1 12
HELIX 8 8 LEU A 353 MET A 360 1 8
HELIX 9 9 ASP A 363 PHE A 376 1 14
HELIX 10 10 ASN A 385 TYR A 408 1 24
HELIX 11 11 GLY A 413 LEU A 420 1 8
HELIX 12 12 LEU A 420 ILE A 442 1 23
HELIX 13 13 PRO B 231 ALA B 241 1 11
HELIX 14 14 PRO B 264 ALA B 272 1 9
HELIX 15 15 ASP B 273 ARG B 285 1 13
HELIX 16 16 PRO B 293 SER B 317 1 25
HELIX 17 17 ILE B 318 VAL B 320 5 3
HELIX 18 18 HIS B 333 HIS B 338 1 6
HELIX 19 19 VAL B 342 LEU B 353 1 12
HELIX 20 20 LEU B 353 MET B 360 1 8
HELIX 21 21 ASP B 363 PHE B 376 1 14
HELIX 22 22 ASN B 385 TYR B 408 1 24
HELIX 23 23 GLY B 413 LEU B 420 1 8
HELIX 24 24 ARG B 421 ASP B 444 1 24
HELIX 25 25 PRO B 446 LEU B 451 1 6
HELIX 26 26 GLU B 456 GLN B 460 5 5
HELIX 27 27 PRO C 231 VAL C 242 1 12
HELIX 28 28 ALA C 272 ARG C 285 1 14
HELIX 29 29 HIS C 288 LEU C 292 5 5
HELIX 30 30 PRO C 293 GLY C 304 1 12
HELIX 31 31 GLY C 304 ILE C 318 1 15
HELIX 32 32 HIS C 333 ALA C 340 1 8
HELIX 33 33 VAL C 342 LEU C 353 1 12
HELIX 34 34 LEU C 353 MET C 360 1 8
HELIX 35 35 ASP C 363 PHE C 376 1 14
HELIX 36 36 ASN C 385 TYR C 408 1 24
HELIX 37 37 GLY C 413 LEU C 420 1 8
HELIX 38 38 ARG C 421 GLY C 443 1 23
HELIX 39 39 PRO D 231 VAL D 242 1 12
HELIX 40 40 PRO D 264 GLN D 275 1 12
HELIX 41 41 GLN D 275 ILE D 286 1 12
HELIX 42 42 PRO D 293 GLY D 304 1 12
HELIX 43 43 TRP D 305 SER D 317 1 13
HELIX 44 44 ILE D 318 VAL D 320 5 3
HELIX 45 45 HIS D 333 GLY D 341 1 9
HELIX 46 46 VAL D 342 LEU D 353 1 12
HELIX 47 47 LEU D 353 MET D 360 1 8
HELIX 48 48 ASP D 363 PHE D 376 1 14
HELIX 49 49 ASN D 385 TYR D 408 1 24
HELIX 50 50 GLY D 413 LEU D 420 1 8
HELIX 51 51 LEU D 420 GLY D 443 1 24
HELIX 52 52 MET F 2339 ILE F 2345 1 7
SHEET 1 A 2 GLY A 323 LEU A 325 0
SHEET 2 A 2 HIS A 331 HIS A 333 -1 O VAL A 332 N ILE A 324
SHEET 1 B 2 ILE B 324 LEU B 325 0
SHEET 2 B 2 HIS B 331 VAL B 332 -1 O VAL B 332 N ILE B 324
SHEET 1 C 2 ILE C 324 LEU C 325 0
SHEET 2 C 2 HIS C 331 VAL C 332 -1 O VAL C 332 N ILE C 324
SHEET 1 D 2 ILE D 324 LEU D 326 0
SHEET 2 D 2 GLY D 329 VAL D 332 -1 O VAL D 332 N ILE D 324
SITE 1 AC1 7 HOH A 37 ILE A 268 ASN A 306 PHE A 313
SITE 2 AC1 7 ILE A 324 CYS A 432 LEU A 436
SITE 1 AC2 6 ILE B 447 ASN C 306 LEU C 309 ILE C 345
SITE 2 AC2 6 CYS C 432 LEU C 436
CRYST1 85.030 117.580 117.120 90.00 90.00 90.00 P 21 21 21 16
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.011761 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008505 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008538 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
