HEADER HORMONE/GROWTH FACTOR RECEPTOR 05-JAN-04 1S0X
TITLE CRYSTAL STRUCTURE OF THE HUMAN RORALPHA LIGAND BINDING DOMAIN IN
TITLE 2 COMPLEX WITH CHOLESTEROL SULFATE AT 2.2A
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: NUCLEAR RECEPTOR ROR-ALPHA;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: LIGAND BINDING DOMAIN;
COMPND 5 SYNONYM: NUCLEAR RECEPTOR RZR-ALPHA;
COMPND 6 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: RORA, NR1F1, RZRA;
SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: SF9;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: BACCULOVIRUS
KEYWDS THREE-LAYERED ALPHA HELICAL SANDWICH, NUCLEAR HORMONE RECEPTOR,
KEYWDS 2 ORPHAN RECEPTOR, LIGAND BINDING DOMAIN, HORMONE-GROWTH FACTOR
KEYWDS 3 RECEPTOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR J.KALLEN,J.M.SCHLAEPPI,F.BITSCH,I.DELHON,B.FOURNIER
REVDAT 5 20-SEP-23 1S0X 1 REMARK
REVDAT 4 21-DEC-22 1S0X 1 REMARK SEQADV
REVDAT 3 24-FEB-09 1S0X 1 VERSN
REVDAT 2 04-MAY-04 1S0X 1 JRNL
REVDAT 1 10-FEB-04 1S0X 0
JRNL AUTH J.KALLEN,J.M.SCHLAEPPI,F.BITSCH,I.DELHON,B.FOURNIER
JRNL TITL CRYSTAL STRUCTURE OF THE HUMAN RORALPHA LIGAND BINDING
JRNL TITL 2 DOMAIN IN COMPLEX WITH CHOLESTEROL SULFATE AT 2.2 A
JRNL REF J.BIOL.CHEM. V. 279 14033 2004
JRNL REFN ISSN 0021-9258
JRNL PMID 14722075
JRNL DOI 10.1074/JBC.M400302200
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH J.KALLEN,J.-M.SCHLAEPPI,F.BITSCH,S.GEISSE,M.GEISER,I.DELHON,
REMARK 1 AUTH 2 B.FOURNIER
REMARK 1 TITL X-RAY STRUCTURE OF THE HRORALPHA LBD AT 1.63A: STRUCTURAL
REMARK 1 TITL 2 AND FUNCTIONAL DATA THAT CHOLESTEROL OR A CHOLESTEROL
REMARK 1 TITL 3 DERIVATIVE IS THE NATURAL LIGAND OF RORALPHA
REMARK 1 REF STRUCTURE V. 10 1697 2002
REMARK 1 REFN ISSN 0969-2126
REMARK 1 DOI 10.1016/S0969-2126(02)00912-7
REMARK 2
REMARK 2 RESOLUTION. 2.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.0
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) : 2.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 3 NUMBER OF REFLECTIONS : 15671
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) : 0.197
REMARK 3 R VALUE (WORKING SET) : 0.197
REMARK 3 FREE R VALUE : 0.209
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 830
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) : 2.20
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.26
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1130
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2950
REMARK 3 BIN FREE R VALUE SET COUNT : 75
REMARK 3 BIN FREE R VALUE : 0.2750
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2066
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 32
REMARK 3 SOLVENT ATOMS : 256
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 32.90
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 35.92
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 2.00000
REMARK 3 B22 (A**2) : -0.15000
REMARK 3 B33 (A**2) : -2.06000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.79000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.271
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.181
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.176
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.909
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.950
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.950
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2145 ; 0.014 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): 1917 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2897 ; 1.398 ; 1.967
REMARK 3 BOND ANGLES OTHERS (DEGREES): 4474 ; 0.743 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 250 ; 3.301 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 411 ;15.222 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 325 ; 0.079 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2313 ; 0.005 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 431 ; 0.002 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 563 ; 0.255 ; 0.300
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 1831 ; 0.209 ; 0.300
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): 186 ; 0.232 ; 0.500
REMARK 3 H-BOND (X...Y) OTHERS (A): 1 ; 0.323 ; 0.500
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): 16 ; 0.213 ; 0.300
REMARK 3 SYMMETRY VDW OTHERS (A): 42 ; 0.310 ; 0.300
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 8 ; 0.392 ; 0.500
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): 1252 ; 0.833 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2023 ; 1.669 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 893 ; 2.509 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 874 ; 4.207 ; 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 : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
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 1S0X COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-JAN-04.
REMARK 100 THE DEPOSITION ID IS D_1000021227.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 17-OCT-02
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 : SLS
REMARK 200 BEAMLINE : X06SA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9200
REMARK 200 MONOCHROMATOR : SAGITALLY FOCUSED SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : CCP4 (TRUNCATE)
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 16541
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 200 DATA REDUNDANCY : 3.500
REMARK 200 R MERGE (I) : 0.07900
REMARK 200 R SYM (I) : 0.07900
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 16.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.28
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.4
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: FOURIER SYNTHESIS
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: PDB ENTRY 1N83
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 55.39
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.78
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 4000, MAGNESIUM CHLORIDE, TRIS, PH
REMARK 280 8.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277K
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 24.95000
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 300 REMARK: BIOLOGICAL ASSEMBLY IS MONOMER
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: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
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 254
REMARK 465 SER A 255
REMARK 465 SER A 256
REMARK 465 HIS A 257
REMARK 465 HIS A 258
REMARK 465 HIS A 259
REMARK 465 HIS A 260
REMARK 465 THR A 512
REMARK 465 SER A 513
REMARK 465 GLU A 514
REMARK 465 PHE A 515
REMARK 465 GLU A 516
REMARK 465 PRO A 517
REMARK 465 ALA A 518
REMARK 465 MET A 519
REMARK 465 GLN A 520
REMARK 465 ILE A 521
REMARK 465 ASP A 522
REMARK 465 GLY A 523
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 HOH A 1046 O HOH A 1067 2.06
REMARK 500 NZ LYS A 473 O HOH A 1173 2.08
REMARK 500 O HOH A 1088 O HOH A 1099 2.16
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 LEU A 266 NZ LYS A 339 2555 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 A 461 59.46 -147.98
REMARK 500 ARG A 462 6.70 -56.60
REMARK 500 ASP A 464 -159.38 -146.51
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 C3S A 1001
DBREF 1S0X A 271 523 UNP P35398 RORA_HUMAN 304 556
SEQADV 1S0X GLY A 254 UNP P35398 CLONING ARTIFACT
SEQADV 1S0X SER A 255 UNP P35398 CLONING ARTIFACT
SEQADV 1S0X SER A 256 UNP P35398 CLONING ARTIFACT
SEQADV 1S0X HIS A 257 UNP P35398 EXPRESSION TAG
SEQADV 1S0X HIS A 258 UNP P35398 EXPRESSION TAG
SEQADV 1S0X HIS A 259 UNP P35398 EXPRESSION TAG
SEQADV 1S0X HIS A 260 UNP P35398 EXPRESSION TAG
SEQADV 1S0X HIS A 261 UNP P35398 EXPRESSION TAG
SEQADV 1S0X HIS A 262 UNP P35398 EXPRESSION TAG
SEQADV 1S0X LEU A 263 UNP P35398 EXPRESSION TAG
SEQADV 1S0X GLU A 264 UNP P35398 EXPRESSION TAG
SEQADV 1S0X VAL A 265 UNP P35398 EXPRESSION TAG
SEQADV 1S0X LEU A 266 UNP P35398 EXPRESSION TAG
SEQADV 1S0X PHE A 267 UNP P35398 EXPRESSION TAG
SEQADV 1S0X GLN A 268 UNP P35398 EXPRESSION TAG
SEQADV 1S0X GLY A 269 UNP P35398 EXPRESSION TAG
SEQADV 1S0X PRO A 270 UNP P35398 EXPRESSION TAG
SEQRES 1 A 270 GLY SER SER HIS HIS HIS HIS HIS HIS LEU GLU VAL LEU
SEQRES 2 A 270 PHE GLN GLY PRO ALA GLU LEU GLU HIS LEU ALA GLN ASN
SEQRES 3 A 270 ILE SER LYS SER HIS LEU GLU THR CYS GLN TYR LEU ARG
SEQRES 4 A 270 GLU GLU LEU GLN GLN ILE THR TRP GLN THR PHE LEU GLN
SEQRES 5 A 270 GLU GLU ILE GLU ASN TYR GLN ASN LYS GLN ARG GLU VAL
SEQRES 6 A 270 MET TRP GLN LEU CYS ALA ILE LYS ILE THR GLU ALA ILE
SEQRES 7 A 270 GLN TYR VAL VAL GLU PHE ALA LYS ARG ILE ASP GLY PHE
SEQRES 8 A 270 MET GLU LEU CYS GLN ASN ASP GLN ILE VAL LEU LEU LYS
SEQRES 9 A 270 ALA GLY SER LEU GLU VAL VAL PHE ILE ARG MET CYS ARG
SEQRES 10 A 270 ALA PHE ASP SER GLN ASN ASN THR VAL TYR PHE ASP GLY
SEQRES 11 A 270 LYS TYR ALA SER PRO ASP VAL PHE LYS SER LEU GLY CYS
SEQRES 12 A 270 GLU ASP PHE ILE SER PHE VAL PHE GLU PHE GLY LYS SER
SEQRES 13 A 270 LEU CYS SER MET HIS LEU THR GLU ASP GLU ILE ALA LEU
SEQRES 14 A 270 PHE SER ALA PHE VAL LEU MET SER ALA ASP ARG SER TRP
SEQRES 15 A 270 LEU GLN GLU LYS VAL LYS ILE GLU LYS LEU GLN GLN LYS
SEQRES 16 A 270 ILE GLN LEU ALA LEU GLN HIS VAL LEU GLN LYS ASN HIS
SEQRES 17 A 270 ARG GLU ASP GLY ILE LEU THR LYS LEU ILE CYS LYS VAL
SEQRES 18 A 270 SER THR LEU ARG ALA LEU CYS GLY ARG HIS THR GLU LYS
SEQRES 19 A 270 LEU MET ALA PHE LYS ALA ILE TYR PRO ASP ILE VAL ARG
SEQRES 20 A 270 LEU HIS PHE PRO PRO LEU TYR LYS GLU LEU PHE THR SER
SEQRES 21 A 270 GLU PHE GLU PRO ALA MET GLN ILE ASP GLY
HET C3S A1001 32
HETNAM C3S CHOLEST-5-EN-3-YL HYDROGEN SULFATE
HETSYN C3S CHOLESTEROL-SULFATE
FORMUL 2 C3S C27 H46 O4 S
FORMUL 3 HOH *256(H2 O)
HELIX 1 1 HIS A 261 CYS A 288 1 28
HELIX 2 2 LEU A 291 ILE A 298 1 8
HELIX 3 3 LEU A 304 LYS A 314 1 11
HELIX 4 4 GLN A 315 ARG A 340 1 26
HELIX 5 5 CYS A 348 MET A 368 1 21
HELIX 6 6 SER A 387 GLY A 395 5 9
HELIX 7 7 CYS A 396 SER A 412 1 17
HELIX 8 8 THR A 416 MET A 429 1 14
HELIX 9 9 GLU A 438 ARG A 462 1 25
HELIX 10 10 ILE A 466 TYR A 495 1 30
HELIX 11 11 TYR A 495 PHE A 503 1 9
HELIX 12 12 PRO A 504 PHE A 511 1 8
SHEET 1 A 3 PHE A 372 ASP A 373 0
SHEET 2 A 3 THR A 378 PHE A 381 -1 O THR A 378 N ASP A 373
SHEET 3 A 3 LYS A 384 ALA A 386 -1 O LYS A 384 N PHE A 381
SITE 1 AC1 10 CYS A 288 GLN A 289 TYR A 290 TRP A 320
SITE 2 AC1 10 CYS A 323 ARG A 367 ARG A 370 TYR A 380
SITE 3 AC1 10 HOH A1003 HOH A1025
CRYST1 54.400 49.900 60.700 90.00 97.80 90.00 P 1 21 1 2
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 0.018382 0.000000 0.002518 0.00000
SCALE2 0.000000 0.020040 0.000000 0.00000
SCALE3 0.000000 0.000000 0.016628 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
