HEADER TRANSCRIPTION 04-JUL-15 5AWK
TITLE CRYSTAL STRUCTURE OF VDR-LBD/PARTIAL AGONIST COMPLEX: 22S-ETHYL
TITLE 2 ANALOGUE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: VITAMIN D3 RECEPTOR,VITAMIN D3 RECEPTOR;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 116-164, 212-423;
COMPND 5 SYNONYM: VDR,1,25-DIHYDROXYVITAMIN D3 RECEPTOR,NUCLEAR RECEPTOR
COMPND 6 SUBFAMILY 1 GROUP I MEMBER 1,VDR,1,25-DIHYDROXYVITAMIN D3 RECEPTOR,
COMPND 7 NUCLEAR RECEPTOR SUBFAMILY 1 GROUP I MEMBER 1;
COMPND 8 ENGINEERED: YES;
COMPND 9 OTHER_DETAILS: DELETION MUTANT, RESIDUES 165-211;
COMPND 10 MOL_ID: 2;
COMPND 11 MOLECULE: MEDIATOR OF RNA POLYMERASE II TRANSCRIPTION SUBUNIT 1;
COMPND 12 CHAIN: C;
COMPND 13 FRAGMENT: UNP RESIDUES 640-652;
COMPND 14 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;
SOURCE 3 ORGANISM_COMMON: RAT;
SOURCE 4 ORGANISM_TAXID: 10116;
SOURCE 5 GENE: VDR, NR1I1;
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 TRANDCRIPTION, VITAMIN D, VDRE, RXR, CO-FACTORS, HORMONE,
KEYWDS 2 TRANSCRIPTION
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.ANAMI,T.ITOH,K.YAMAMOTO
REVDAT 3 20-MAR-24 5AWK 1 REMARK
REVDAT 2 26-FEB-20 5AWK 1 JRNL REMARK
REVDAT 1 18-NOV-15 5AWK 0
JRNL AUTH Y.ANAMI,Y.SAKAMAKI,T.ITOH,Y.INABA,M.NAKABAYASHI,T.IKURA,
JRNL AUTH 2 N.ITO,K.YAMAMOTO
JRNL TITL FINE TUNING OF AGONISTIC/ANTAGONISTIC ACTIVITY FOR VITAMIN D
JRNL TITL 2 RECEPTOR BY 22-ALKYL CHAIN LENGTH OF LIGANDS: 22S-HEXYL
JRNL TITL 3 COMPOUND UNEXPECTEDLY RESTORED AGONISTIC ACTIVITY.
JRNL REF BIOORG.MED.CHEM. V. 23 7274 2015
JRNL REFN ESSN 1464-3391
JRNL PMID 26515040
JRNL DOI 10.1016/J.BMC.2015.10.026
REMARK 2
REMARK 2 RESOLUTION. 2.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0049
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) : 2.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 40.48
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 74.2
REMARK 3 NUMBER OF REFLECTIONS : 4318
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) : 0.211
REMARK 3 R VALUE (WORKING SET) : 0.208
REMARK 3 FREE R VALUE : 0.267
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.600
REMARK 3 FREE R VALUE TEST SET COUNT : 207
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) : 2.90
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.98
REMARK 3 REFLECTION IN BIN (WORKING SET) : 341
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 77.09
REMARK 3 BIN R VALUE (WORKING SET) : 0.3160
REMARK 3 BIN FREE R VALUE SET COUNT : 19
REMARK 3 BIN FREE R VALUE : 0.4840
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2004
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 29
REMARK 3 SOLVENT ATOMS : 8
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 87.39
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -6.08000
REMARK 3 B22 (A**2) : 6.24000
REMARK 3 B33 (A**2) : 0.11000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -1.28000
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): 0.596
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.389
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 49.299
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.935
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.903
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2076 ; 0.009 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 2034 ; 0.000 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2810 ; 1.128 ; 1.996
REMARK 3 BOND ANGLES OTHERS (DEGREES): 4697 ; 3.471 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 248 ; 3.937 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 91 ;25.795 ;24.505
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 378 ;16.584 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 11 ;11.484 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 322 ; 0.053 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2268 ; 0.011 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 449 ; 0.021 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 1001 ; 2.715 ; 6.449
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1000 ; 2.715 ; 6.447
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1246 ; 4.610 ; 9.646
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 1247 ; 4.608 ; 9.648
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1075 ; 2.769 ; 6.660
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 1076 ; 2.768 ; 6.658
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 1565 ; 4.686 ; 9.860
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 2511 ; 7.314 ;50.991
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 2512 ; 7.312 ;50.987
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 : 4
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 123 A 420
REMARK 3 ORIGIN FOR THE GROUP (A): 19.0792 0.3727 19.1431
REMARK 3 T TENSOR
REMARK 3 T11: 0.2531 T22: 0.2832
REMARK 3 T33: 0.2763 T12: -0.0144
REMARK 3 T13: -0.0008 T23: -0.0134
REMARK 3 L TENSOR
REMARK 3 L11: 0.7109 L22: 0.0655
REMARK 3 L33: 0.0736 L12: -0.1344
REMARK 3 L13: 0.0070 L23: -0.0511
REMARK 3 S TENSOR
REMARK 3 S11: -0.0001 S12: -0.0261 S13: -0.0138
REMARK 3 S21: -0.0164 S22: -0.0083 S23: 0.0142
REMARK 3 S31: -0.0280 S32: 0.0118 S33: 0.0084
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 : C 625 C 635
REMARK 3 ORIGIN FOR THE GROUP (A): 5.9204 -11.0946 11.0565
REMARK 3 T TENSOR
REMARK 3 T11: 0.2403 T22: 0.2882
REMARK 3 T33: 0.3030 T12: 0.0139
REMARK 3 T13: 0.0091 T23: -0.0395
REMARK 3 L TENSOR
REMARK 3 L11: 2.9373 L22: 0.8313
REMARK 3 L33: 1.4871 L12: 1.4336
REMARK 3 L13: -0.5122 L23: -0.6706
REMARK 3 S TENSOR
REMARK 3 S11: 0.1053 S12: 0.0691 S13: -0.0776
REMARK 3 S21: 0.0500 S22: -0.0198 S23: 0.0267
REMARK 3 S31: 0.0369 S32: 0.1274 S33: -0.0856
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 501 A 501
REMARK 3 ORIGIN FOR THE GROUP (A): 13.3559 4.6223 24.7574
REMARK 3 T TENSOR
REMARK 3 T11: 0.2791 T22: 0.2671
REMARK 3 T33: 0.3221 T12: 0.0165
REMARK 3 T13: 0.0218 T23: -0.0058
REMARK 3 L TENSOR
REMARK 3 L11: 3.7934 L22: 8.9951
REMARK 3 L33: 11.6579 L12: 3.4191
REMARK 3 L13: 1.4496 L23: -6.7960
REMARK 3 S TENSOR
REMARK 3 S11: 0.1342 S12: -0.0839 S13: -0.1951
REMARK 3 S21: 0.1400 S22: -0.2326 S23: -0.2508
REMARK 3 S31: -0.0615 S32: 0.2531 S33: 0.0984
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 601 A 608
REMARK 3 ORIGIN FOR THE GROUP (A): 20.3945 3.5032 19.1831
REMARK 3 T TENSOR
REMARK 3 T11: 0.2197 T22: 0.0980
REMARK 3 T33: 0.3550 T12: -0.0529
REMARK 3 T13: 0.0406 T23: 0.0636
REMARK 3 L TENSOR
REMARK 3 L11: 0.1991 L22: 0.6389
REMARK 3 L33: 2.1816 L12: -0.3006
REMARK 3 L13: -0.5382 L23: 1.1779
REMARK 3 S TENSOR
REMARK 3 S11: 0.0114 S12: 0.0913 S13: 0.1041
REMARK 3 S21: 0.0082 S22: -0.0364 S23: -0.0113
REMARK 3 S31: 0.0484 S32: -0.0896 S33: 0.0250
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 5AWK COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 08-JUL-15.
REMARK 100 THE DEPOSITION ID IS D_1300000090.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 20-DEC-14
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PHOTON FACTORY
REMARK 200 BEAMLINE : BL-5A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : IMOSFLM
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 9246
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.900
REMARK 200 RESOLUTION RANGE LOW (A) : 40.480
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 75.2
REMARK 200 DATA REDUNDANCY : 2.000
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 56.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 41.20
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.09
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: MOPS-NA, NA-FORMATE, PEG 4000,
REMARK 280 ETHYLENEGLYCOL, PH 7.0, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
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 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 77.01500
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 20.98500
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 77.01500
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 20.98500
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1090 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 11750 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -10.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C
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 GLY A 106
REMARK 465 SER A 107
REMARK 465 HIS A 108
REMARK 465 MET A 109
REMARK 465 GLY A 110
REMARK 465 SER A 111
REMARK 465 PRO A 112
REMARK 465 ASN A 113
REMARK 465 SER A 114
REMARK 465 PRO A 115
REMARK 465 LEU A 116
REMARK 465 LYS A 117
REMARK 465 ASP A 118
REMARK 465 SER A 119
REMARK 465 LEU A 120
REMARK 465 ARG A 121
REMARK 465 PRO A 122
REMARK 465 ASP A 207
REMARK 465 GLY A 208
REMARK 465 SER A 209
REMARK 465 THR A 210
REMARK 465 GLY A 211
REMARK 465 SER A 212
REMARK 465 VAL A 213
REMARK 465 THR A 214
REMARK 465 LEU A 215
REMARK 465 ASP A 216
REMARK 465 LEU A 217
REMARK 465 GLU A 421
REMARK 465 ILE A 422
REMARK 465 SER A 423
REMARK 465 ASP C 636
REMARK 465 ASN C 637
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 ASP A 279 CG OD1 OD2
REMARK 470 LYS A 346 CG CD CE NZ
REMARK 470 LYS A 395 CG CD CE NZ
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 ALA A 138 OG1 THR A 142 1.85
REMARK 500 O LEU A 136 ND1 HIS A 140 2.10
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 C 627 77.22 -108.48
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 YSE A 501
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5AWJ RELATED DB: PDB
DBREF 5AWK A 116 211 UNP P13053 VDR_RAT 116 164
DBREF 5AWK A 212 423 UNP P13053 VDR_RAT 212 423
DBREF 5AWK C 625 637 UNP Q15648 MED1_HUMAN 640 652
SEQADV 5AWK GLY A 106 UNP P13053 EXPRESSION TAG
SEQADV 5AWK SER A 107 UNP P13053 EXPRESSION TAG
SEQADV 5AWK HIS A 108 UNP P13053 EXPRESSION TAG
SEQADV 5AWK MET A 109 UNP P13053 EXPRESSION TAG
SEQADV 5AWK GLY A 110 UNP P13053 EXPRESSION TAG
SEQADV 5AWK SER A 111 UNP P13053 EXPRESSION TAG
SEQADV 5AWK PRO A 112 UNP P13053 EXPRESSION TAG
SEQADV 5AWK ASN A 113 UNP P13053 EXPRESSION TAG
SEQADV 5AWK SER A 114 UNP P13053 EXPRESSION TAG
SEQADV 5AWK PRO A 115 UNP P13053 EXPRESSION TAG
SEQRES 1 A 271 GLY SER HIS MET GLY SER PRO ASN SER PRO LEU LYS ASP
SEQRES 2 A 271 SER LEU ARG PRO LYS LEU SER GLU GLU GLN GLN HIS ILE
SEQRES 3 A 271 ILE ALA ILE LEU LEU ASP ALA HIS HIS LYS THR TYR ASP
SEQRES 4 A 271 PRO THR TYR ALA ASP PHE ARG ASP PHE ARG PRO PRO VAL
SEQRES 5 A 271 ARG MET ASP GLY SER THR GLY SER VAL THR LEU ASP LEU
SEQRES 6 A 271 SER PRO LEU SER MET LEU PRO HIS LEU ALA ASP LEU VAL
SEQRES 7 A 271 SER TYR SER ILE GLN LYS VAL ILE GLY PHE ALA LYS MET
SEQRES 8 A 271 ILE PRO GLY PHE ARG ASP LEU THR SER ASP ASP GLN ILE
SEQRES 9 A 271 VAL LEU LEU LYS SER SER ALA ILE GLU VAL ILE MET LEU
SEQRES 10 A 271 ARG SER ASN GLN SER PHE THR MET ASP ASP MET SER TRP
SEQRES 11 A 271 ASP CYS GLY SER GLN ASP TYR LYS TYR ASP VAL THR ASP
SEQRES 12 A 271 VAL SER LYS ALA GLY HIS THR LEU GLU LEU ILE GLU PRO
SEQRES 13 A 271 LEU ILE LYS PHE GLN VAL GLY LEU LYS LYS LEU ASN LEU
SEQRES 14 A 271 HIS GLU GLU GLU HIS VAL LEU LEU MET ALA ILE CYS ILE
SEQRES 15 A 271 VAL SER PRO ASP ARG PRO GLY VAL GLN ASP ALA LYS LEU
SEQRES 16 A 271 VAL GLU ALA ILE GLN ASP ARG LEU SER ASN THR LEU GLN
SEQRES 17 A 271 THR TYR ILE ARG CYS ARG HIS PRO PRO PRO GLY SER HIS
SEQRES 18 A 271 GLN LEU TYR ALA LYS MET ILE GLN LYS LEU ALA ASP LEU
SEQRES 19 A 271 ARG SER LEU ASN GLU GLU HIS SER LYS GLN TYR ARG SER
SEQRES 20 A 271 LEU SER PHE GLN PRO GLU ASN SER MET LYS LEU THR PRO
SEQRES 21 A 271 LEU VAL LEU GLU VAL PHE GLY ASN GLU ILE SER
SEQRES 1 C 13 LYS ASN HIS PRO MET LEU MET ASN LEU LEU LYS ASP ASN
HET YSE A 501 29
HETNAM YSE (1R,3R)-5-[(2E)-2-[(1R,3AS,7AR)-1-[(2R,3S)-3-ETHYL-5-
HETNAM 2 YSE OXIDANYL-PENTAN-2-YL]-7A-METHYL-2,3,3A,5,6,7-
HETNAM 3 YSE HEXAHYDRO-1H-INDEN-4-YLIDENE]ETHYLIDENE]-2-
HETNAM 4 YSE METHYLIDENE-CYCLOHEXANE-1,3-DIOL
FORMUL 3 YSE C26 H42 O3
FORMUL 4 HOH *8(H2 O)
HELIX 1 AA1 SER A 125 TYR A 143 1 19
HELIX 2 AA2 TYR A 147 PHE A 153 5 7
HELIX 3 AA3 MET A 222 ILE A 244 1 23
HELIX 4 AA4 THR A 251 SER A 271 1 21
HELIX 5 AA5 ASP A 292 HIS A 301 1 10
HELIX 6 AA6 THR A 302 ASN A 320 1 19
HELIX 7 AA7 HIS A 322 VAL A 335 1 14
HELIX 8 AA8 ASP A 344 HIS A 367 1 24
HELIX 9 AA9 GLN A 374 GLN A 403 1 30
HELIX 10 AB1 GLN A 403 MET A 408 1 6
HELIX 11 AB2 THR A 411 GLY A 419 1 9
HELIX 12 AB3 HIS C 627 LYS C 635 1 9
SHEET 1 AA1 2 PHE A 275 THR A 276 0
SHEET 2 AA1 2 SER A 281 TRP A 282 -1 O SER A 281 N THR A 276
CISPEP 1 PRO A 369 PRO A 370 0 -0.55
SITE 1 AC1 11 TYR A 143 LEU A 229 SER A 233 ARG A 270
SITE 2 AC1 11 SER A 271 SER A 274 TRP A 282 VAL A 296
SITE 3 AC1 11 HIS A 301 LEU A 305 HIS A 393
CRYST1 154.030 41.970 41.860 90.00 95.96 90.00 C 1 2 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 0.006492 0.000000 0.000678 0.00000
SCALE2 0.000000 0.023827 0.000000 0.00000
SCALE3 0.000000 0.000000 0.024019 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
