HEADER HORMONE 04-APR-08 2ZLA
TITLE 2-SUBSTITUTED-16-ENE-22-THIA-1ALPHA,25-DIHYDROXY-26,27-DIMETHYL-19-
TITLE 2 NORVITAMIN D3 ANALOGS: SYNTHESIS, BIOLOGICAL EVALUATION AND CRYSTAL
TITLE 3 STRUCTURE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: VITAMIN D3 RECEPTOR;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: VDR-LBD, UNP RESIDUES 116-423;
COMPND 5 SYNONYM: LIGAND BINDING DOMAIN OF VITAMIN D RECEPTOR, VDR, 1,25-
COMPND 6 DIHYDROXYVITAMIN D3 RECEPTOR, NUCLEAR RECEPTOR SUBFAMILY 1 GROUP I
COMPND 7 MEMBER 1;
COMPND 8 ENGINEERED: YES;
COMPND 9 MOL_ID: 2;
COMPND 10 MOLECULE: COACTIVATOR PEPTIDE DRIP;
COMPND 11 CHAIN: C;
COMPND 12 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 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET14B;
SOURCE 11 MOL_ID: 2;
SOURCE 12 SYNTHETIC: YES;
SOURCE 13 OTHER_DETAILS: PEPTIDE SYNTHESIS
KEYWDS PROTEIN-LIGAND COMPLEX, DNA-BINDING, METAL-BINDING, NUCLEUS,
KEYWDS 2 PHOSPHOPROTEIN, RECEPTOR, TRANSCRIPTION, TRANSCRIPTION REGULATION,
KEYWDS 3 ZINC, ZINC-FINGER, HORMONE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.SHIMIZU,Y.MIYAMOTO,M.NAKABAYASHI,H.MASUNO,T.IKURA,N.ITO
REVDAT 4 01-NOV-23 2ZLA 1 REMARK SEQADV
REVDAT 3 24-FEB-09 2ZLA 1 VERSN
REVDAT 2 12-AUG-08 2ZLA 1 JRNL
REVDAT 1 24-JUN-08 2ZLA 0
JRNL AUTH M.SHIMIZU,Y.MIYAMOTO,H.TAKAKU,M.MATSUO,M.NAKABAYASHI,
JRNL AUTH 2 H.MASUNO,N.UDAGAWA,H.F.DELUCA,T.IKURA,N.ITO
JRNL TITL 2-SUBSTITUTED-16-ENE-22-THIA-1ALPHA,25-DIHYDROXY-26,
JRNL TITL 2 27-DIMETHYL-19-NORVITAMIN D3 ANALOGS: SYNTHESIS, BIOLOGICAL
JRNL TITL 3 EVALUATION, AND CRYSTAL STRUCTURE
JRNL REF BIOORG.MED.CHEM. V. 16 6949 2008
JRNL REFN ISSN 0968-0896
JRNL PMID 18539034
JRNL DOI 10.1016/J.BMC.2008.05.043
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 38.45
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 143559.130
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 94.3
REMARK 3 NUMBER OF REFLECTIONS : 17332
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 SET) : 0.213
REMARK 3 FREE R VALUE : 0.263
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 9.900
REMARK 3 FREE R VALUE TEST SET COUNT : 1709
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.006
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.13
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 87.40
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2375
REMARK 3 BIN R VALUE (WORKING SET) : 0.2750
REMARK 3 BIN FREE R VALUE : 0.3110
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 10.10
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 267
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.019
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2001
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 34
REMARK 3 SOLVENT ATOMS : 176
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 17.60
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 39.80
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -14.18000
REMARK 3 B22 (A**2) : 13.60000
REMARK 3 B33 (A**2) : 0.58000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -8.19000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.25
REMARK 3 ESD FROM SIGMAA (A) : 0.22
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.32
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.24
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.006
REMARK 3 BOND ANGLES (DEGREES) : 1.100
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 18.80
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.780
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 1.500 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.340 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 2.190 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 3.130 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.38
REMARK 3 BSOL : 58.93
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 3 : ION.PARAM
REMARK 3 PARAMETER FILE 4 : LG3.PARAM
REMARK 3 PARAMETER FILE 5 : NULL
REMARK 3 TOPOLOGY FILE 1 : WATER.TOP
REMARK 3 TOPOLOGY FILE 3 : ION.TOP
REMARK 3 TOPOLOGY FILE 4 : LG3.TOP
REMARK 3 TOPOLOGY FILE 5 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2ZLA COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 11-APR-08.
REMARK 100 THE DEPOSITION ID IS D_1000028114.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 28-FEB-07
REMARK 200 TEMPERATURE (KELVIN) : 95
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PHOTON FACTORY
REMARK 200 BEAMLINE : BL-6A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.978
REMARK 200 MONOCHROMATOR : TRIANGULAR SI(111) WITH AN
REMARK 200 ASYMMETRIC ANGLE OF 7.8
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 22869
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.1
REMARK 200 DATA REDUNDANCY : 3.400
REMARK 200 R MERGE (I) : 0.04300
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 30.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.07
REMARK 200 COMPLETENESS FOR SHELL (%) : 93.6
REMARK 200 DATA REDUNDANCY IN SHELL : 2.90
REMARK 200 R MERGE FOR SHELL (I) : 0.30300
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.900
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: PDB ENTRY 1RJK
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 41.65
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.11
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1-0.4M FORMIC ACID, 15-20%
REMARK 280 POLYETHYLENE GLYCOL(PEG)4000, 0-20% ETHYLENE GLYCOL, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, 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 76.99250
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 21.00100
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 76.99250
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 21.00100
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: 11690 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -9.1 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 MET A 206
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 SER A 218
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 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 LEU A 124 87.83 75.38
REMARK 500 ASP A 279 25.53 -146.17
REMARK 500 CYS A 284 58.36 -104.77
REMARK 500 GLN A 343 -83.11 -95.47
REMARK 500 GLN A 374 18.39 56.23
REMARK 500 ASN C 626 51.53 84.66
REMARK 500 HIS C 627 75.26 -119.80
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 VDB A 500
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2ZL9 RELATED DB: PDB
REMARK 900 COMPLEX AMONG VDR-LBD, A LIGAND YI-III-690A, AND A COACTIVATOR
REMARK 900 PEPTIDE DRIP
REMARK 900 RELATED ID: 2ZLC RELATED DB: PDB
DBREF 2ZLA A 116 423 UNP P13053 VDR_RAT 116 423
DBREF 2ZLA C 625 637 PDB 2ZLA 2ZLA 625 637
SEQADV 2ZLA GLY A 106 UNP P13053 EXPRESSION TAG
SEQADV 2ZLA SER A 107 UNP P13053 EXPRESSION TAG
SEQADV 2ZLA HIS A 108 UNP P13053 EXPRESSION TAG
SEQADV 2ZLA MET A 109 UNP P13053 EXPRESSION TAG
SEQADV 2ZLA GLY A 110 UNP P13053 EXPRESSION TAG
SEQADV 2ZLA SER A 111 UNP P13053 EXPRESSION TAG
SEQADV 2ZLA PRO A 112 UNP P13053 EXPRESSION TAG
SEQADV 2ZLA ASN A 113 UNP P13053 EXPRESSION TAG
SEQADV 2ZLA SER A 114 UNP P13053 EXPRESSION TAG
SEQADV 2ZLA PRO A 115 UNP P13053 EXPRESSION TAG
SEQADV 2ZLA A UNP P13053 SER 165 DELETION
SEQADV 2ZLA A UNP P13053 TYR 166 DELETION
SEQADV 2ZLA A UNP P13053 SER 167 DELETION
SEQADV 2ZLA A UNP P13053 PRO 168 DELETION
SEQADV 2ZLA A UNP P13053 ARG 169 DELETION
SEQADV 2ZLA A UNP P13053 PRO 170 DELETION
SEQADV 2ZLA A UNP P13053 THR 171 DELETION
SEQADV 2ZLA A UNP P13053 LEU 172 DELETION
SEQADV 2ZLA A UNP P13053 SER 173 DELETION
SEQADV 2ZLA A UNP P13053 PHE 174 DELETION
SEQADV 2ZLA A UNP P13053 SER 175 DELETION
SEQADV 2ZLA A UNP P13053 GLY 176 DELETION
SEQADV 2ZLA A UNP P13053 ASN 177 DELETION
SEQADV 2ZLA A UNP P13053 SER 178 DELETION
SEQADV 2ZLA A UNP P13053 SER 179 DELETION
SEQADV 2ZLA A UNP P13053 SER 180 DELETION
SEQADV 2ZLA A UNP P13053 SER 181 DELETION
SEQADV 2ZLA A UNP P13053 SER 182 DELETION
SEQADV 2ZLA A UNP P13053 SER 183 DELETION
SEQADV 2ZLA A UNP P13053 ASP 184 DELETION
SEQADV 2ZLA A UNP P13053 LEU 185 DELETION
SEQADV 2ZLA A UNP P13053 TYR 186 DELETION
SEQADV 2ZLA A UNP P13053 THR 187 DELETION
SEQADV 2ZLA A UNP P13053 THR 188 DELETION
SEQADV 2ZLA A UNP P13053 SER 189 DELETION
SEQADV 2ZLA A UNP P13053 LEU 190 DELETION
SEQADV 2ZLA A UNP P13053 ASP 191 DELETION
SEQADV 2ZLA A UNP P13053 MET 192 DELETION
SEQADV 2ZLA A UNP P13053 MET 193 DELETION
SEQADV 2ZLA A UNP P13053 GLU 194 DELETION
SEQADV 2ZLA A UNP P13053 PRO 195 DELETION
SEQADV 2ZLA A UNP P13053 SER 196 DELETION
SEQADV 2ZLA A UNP P13053 GLY 197 DELETION
SEQADV 2ZLA A UNP P13053 PHE 198 DELETION
SEQADV 2ZLA A UNP P13053 SER 199 DELETION
SEQADV 2ZLA A UNP P13053 ASN 200 DELETION
SEQADV 2ZLA A UNP P13053 LEU 201 DELETION
SEQADV 2ZLA A UNP P13053 ASP 202 DELETION
SEQADV 2ZLA A UNP P13053 LEU 203 DELETION
SEQADV 2ZLA A UNP P13053 ASN 204 DELETION
SEQADV 2ZLA A UNP P13053 GLY 205 DELETION
SEQADV 2ZLA A UNP P13053 GLU 206 DELETION
SEQADV 2ZLA A UNP P13053 ASP 207 DELETION
SEQADV 2ZLA A UNP P13053 SER 208 DELETION
SEQADV 2ZLA A UNP P13053 ASP 209 DELETION
SEQADV 2ZLA A UNP P13053 ASP 210 DELETION
SEQADV 2ZLA A UNP P13053 PRO 211 DELETION
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 VDB A 500 34
HETNAM VDB (1R,2S,3R,5Z,7E)-17-{(1R)-1-[(2-ETHYL-2-HYDROXYBUTYL)
HETNAM 2 VDB SULFANYL]ETHYL}-2-(2-HYDROXYETHOXY)-9,10-SECOESTRA-5,
HETNAM 3 VDB 7,16-TRIENE-1,3-DIOL
HETSYN VDB (20R)-1ALPHA,25-DIHYDROXY-2BETA-(2-HYDROXYETHOXY)-16-
HETSYN 2 VDB ENE-22-THIA-26,27-DIMETHYL-19,24-DINORVITAMIN D3
FORMUL 3 VDB C28 H46 O5 S
FORMUL 4 HOH *176(H2 O)
HELIX 1 1 SER A 125 LYS A 141 1 17
HELIX 2 2 TYR A 147 PHE A 153 5 7
HELIX 3 3 MET A 222 MET A 243 1 22
HELIX 4 4 GLY A 246 LEU A 250 5 5
HELIX 5 5 THR A 251 SER A 271 1 21
HELIX 6 6 ASP A 292 LYS A 298 1 7
HELIX 7 7 THR A 302 LEU A 319 1 18
HELIX 8 8 HIS A 322 VAL A 335 1 14
HELIX 9 9 ASP A 344 HIS A 367 1 24
HELIX 10 10 GLN A 374 SER A 401 1 28
HELIX 11 11 GLN A 403 MET A 408 1 6
HELIX 12 12 THR A 411 GLY A 419 1 9
HELIX 13 13 HIS C 627 LYS C 635 1 9
SHEET 1 A 3 PHE A 275 THR A 276 0
SHEET 2 A 3 SER A 281 ASP A 283 -1 O SER A 281 N THR A 276
SHEET 3 A 3 LYS A 290 TYR A 291 -1 O TYR A 291 N TRP A 282
CISPEP 1 PRO A 369 PRO A 370 0 0.54
SITE 1 AC1 12 THR A 142 TYR A 143 ALA A 227 SER A 233
SITE 2 AC1 12 ARG A 270 SER A 271 SER A 274 TRP A 282
SITE 3 AC1 12 CYS A 284 HIS A 301 HIS A 393 LEU A 400
CRYST1 153.985 42.002 42.152 90.00 95.77 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 0.006494 0.000000 0.000656 0.00000
SCALE2 0.000000 0.023808 0.000000 0.00000
SCALE3 0.000000 0.000000 0.023844 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
