HEADER OXIDOREDUCTASE 04-FEB-94 1RAL
TITLE THREE-DIMENSIONAL STRUCTURE OF RAT LIVER 3ALPHA-HYDROXYSTEROID(SLASH)
TITLE 2 DIHYDRODIOL DEHYDROGENASE: A MEMBER OF THE ALDO-KETO REDUCTASE
TITLE 3 SUPERFAMILY
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 3-ALPHA-HYDROXYSTEROID DEHYDROGENASE;
COMPND 3 CHAIN: A;
COMPND 4 EC: 1.1.1.50;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;
SOURCE 3 ORGANISM_COMMON: NORWAY RAT;
SOURCE 4 ORGANISM_TAXID: 10116
KEYWDS OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR S.S.HOOG,J.E.PAWLOWSKI,P.M.ALZARI,T.M.PENNING,M.LEWIS
REVDAT 3 14-FEB-24 1RAL 1 REMARK
REVDAT 2 24-FEB-09 1RAL 1 VERSN
REVDAT 1 30-APR-94 1RAL 0
JRNL AUTH S.S.HOOG,J.E.PAWLOWSKI,P.M.ALZARI,T.M.PENNING,M.LEWIS
JRNL TITL THREE-DIMENSIONAL STRUCTURE OF RAT LIVER 3
JRNL TITL 2 ALPHA-HYDROXYSTEROID/DIHYDRODIOL DEHYDROGENASE: A MEMBER OF
JRNL TITL 3 THE ALDO-KETO REDUCTASE SUPERFAMILY.
JRNL REF PROC.NATL.ACAD.SCI.USA V. 91 2517 1994
JRNL REFN ISSN 0027-8424
JRNL PMID 8146147
JRNL DOI 10.1073/PNAS.91.7.2517
REMARK 2
REMARK 2 RESOLUTION. 3.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 10.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 1.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 5883
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING SET) : 0.220
REMARK 3 FREE R VALUE : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2471
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 0
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.019
REMARK 3 BOND ANGLES (DEGREES) : 3.800
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
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 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1RAL COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000175972.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : NULL
REMARK 200 RADIATION SOURCE : NULL
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : NULL
REMARK 200 WAVELENGTH OR RANGE (A) : NULL
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : NULL
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : NULL
REMARK 200 RESOLUTION RANGE HIGH (A) : NULL
REMARK 200 RESOLUTION RANGE LOW (A) : NULL
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : NULL
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
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: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: X-PLOR
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 47.14
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.33
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 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 71.65000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 71.65000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 25.65000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 44.75000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 25.65000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 44.75000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 71.65000
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 25.65000
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 44.75000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 71.65000
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 25.65000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 44.75000
REMARK 290 SMTRY3 8 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: 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 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 ARG A 223 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 225 CG CD CE NZ
REMARK 475
REMARK 475 ZERO OCCUPANCY RESIDUES
REMARK 475 THE FOLLOWING RESIDUES WERE MODELED WITH ZERO OCCUPANCY.
REMARK 475 THE LOCATION AND PROPERTIES OF THESE RESIDUES MAY NOT
REMARK 475 BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 475 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE)
REMARK 475 M RES C SSEQI
REMARK 475 SER A 221
REMARK 475 SER A 222
REMARK 475 ARG A 223
REMARK 475 ASP A 224
REMARK 475 LYS A 225
REMARK 475 THR A 226
REMARK 475 TRP A 227
REMARK 475 VAL A 228
REMARK 475 ASP A 229
REMARK 475 GLN A 230
REMARK 475 LYS A 231
REMARK 475 SER A 232
REMARK 475 PRO A 233
REMARK 475 VAL A 234
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 ASP A 2 CA - C - N ANGL. DEV. = -14.9 DEGREES
REMARK 500 LEU A 10 CA - CB - CG ANGL. DEV. = 14.1 DEGREES
REMARK 500 ARG A 47 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 TYR A 55 CB - CG - CD2 ANGL. DEV. = -4.0 DEGREES
REMARK 500 ILE A 79 CG1 - CB - CG2 ANGL. DEV. = -14.5 DEGREES
REMARK 500 LYS A 104 CA - CB - CG ANGL. DEV. = 16.3 DEGREES
REMARK 500 GLU A 149 CA - CB - CG ANGL. DEV. = 15.0 DEGREES
REMARK 500 CYS A 154 CA - CB - SG ANGL. DEV. = 11.3 DEGREES
REMARK 500 ARG A 171 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 LEU A 177 N - CA - CB ANGL. DEV. = -13.2 DEGREES
REMARK 500 LEU A 177 CA - CB - CG ANGL. DEV. = 16.5 DEGREES
REMARK 500 LYS A 183 CA - CB - CG ANGL. DEV. = 13.7 DEGREES
REMARK 500 TYR A 196 CB - CG - CD2 ANGL. DEV. = -3.8 DEGREES
REMARK 500 LEU A 236 CA - CB - CG ANGL. DEV. = 21.8 DEGREES
REMARK 500 ASN A 273 CA - CB - CG ANGL. DEV. = 14.6 DEGREES
REMARK 500 GLU A 279 CA - CB - CG ANGL. DEV. = 15.2 DEGREES
REMARK 500 ARG A 304 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 ARG A 304 NE - CZ - NH2 ANGL. DEV. = -4.5 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 SER A 3 -156.72 -108.76
REMARK 500 ILE A 4 -24.52 104.22
REMARK 500 ASN A 11 -64.04 17.35
REMARK 500 THR A 24 -155.98 -171.40
REMARK 500 PRO A 26 -159.04 -120.65
REMARK 500 ALA A 30 -34.05 69.52
REMARK 500 LYS A 31 -154.30 55.92
REMARK 500 GLU A 33 49.77 -107.29
REMARK 500 ALA A 41 -62.19 -108.08
REMARK 500 LEU A 54 -73.69 -55.08
REMARK 500 GLU A 58 -76.38 -2.86
REMARK 500 ARG A 66 29.94 -70.44
REMARK 500 SER A 67 -31.23 -130.94
REMARK 500 ILE A 69 54.40 -91.54
REMARK 500 GLU A 70 -59.46 -164.44
REMARK 500 ARG A 76 -53.36 -5.59
REMARK 500 SER A 87 -38.52 -36.46
REMARK 500 PHE A 89 6.43 -61.93
REMARK 500 GLN A 107 18.01 58.50
REMARK 500 ASP A 132 65.84 -67.82
REMARK 500 GLU A 133 -34.95 63.46
REMARK 500 HIS A 134 -169.24 -169.72
REMARK 500 LYS A 136 -142.16 -115.85
REMARK 500 LYS A 161 -23.91 -34.92
REMARK 500 VAL A 165 -166.54 -112.49
REMARK 500 SER A 166 144.18 -172.28
REMARK 500 CYS A 170 -35.59 -18.09
REMARK 500 LYS A 183 -63.91 -122.85
REMARK 500 VAL A 187 -74.50 -98.76
REMARK 500 HIS A 194 174.81 171.39
REMARK 500 LEU A 197 79.23 179.93
REMARK 500 GLN A 199 97.26 -67.58
REMARK 500 TYR A 205 -52.57 -167.73
REMARK 500 LYS A 209 41.71 -107.84
REMARK 500 ASP A 210 19.01 42.79
REMARK 500 SER A 221 -71.21 65.85
REMARK 500 SER A 222 -49.57 58.24
REMARK 500 ASP A 224 -63.96 66.81
REMARK 500 LYS A 225 94.07 40.68
REMARK 500 THR A 226 51.28 -68.29
REMARK 500 TRP A 227 4.56 -160.67
REMARK 500 ASP A 229 -51.74 -139.18
REMARK 500 SER A 232 -91.13 -170.33
REMARK 500 LEU A 236 46.47 -91.72
REMARK 500 ASP A 237 4.82 -162.30
REMARK 500 PRO A 239 -73.13 -44.79
REMARK 500 ALA A 245 44.96 -85.68
REMARK 500 LYS A 246 -44.76 -145.88
REMARK 500 GLN A 250 122.31 130.77
REMARK 500 THR A 251 140.25 -20.31
REMARK 500
REMARK 500 THIS ENTRY HAS 58 RAMACHANDRAN OUTLIERS.
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 SER A 232 PRO A 233 -141.05
REMARK 500 THR A 251 PRO A 252 -147.34
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1RAL A 1 308 UNP P23457 DIDH_RAT 1 308
SEQRES 1 A 308 MET ASP SER ILE SER LEU ARG VAL ALA LEU ASN ASP GLY
SEQRES 2 A 308 ASN PHE ILE PRO VAL LEU GLY PHE GLY THR THR VAL PRO
SEQRES 3 A 308 GLU LYS VAL ALA LYS ASP GLU VAL ILE LYS ALA THR LYS
SEQRES 4 A 308 ILE ALA ILE ASP ASN GLY PHE ARG HIS PHE ASP SER ALA
SEQRES 5 A 308 TYR LEU TYR GLU VAL GLU GLU GLU VAL GLY GLN ALA ILE
SEQRES 6 A 308 ARG SER LYS ILE GLU ASP GLY THR VAL LYS ARG GLU ASP
SEQRES 7 A 308 ILE PHE TYR THR SER LYS LEU TRP SER THR PHE HIS ARG
SEQRES 8 A 308 PRO GLU LEU VAL ARG THR CYS LEU GLU LYS THR LEU LYS
SEQRES 9 A 308 SER THR GLN LEU ASP TYR VAL ASP LEU TYR ILE ILE HIS
SEQRES 10 A 308 PHE PRO MET ALA LEU GLN PRO GLY ASP ILE PHE PHE PRO
SEQRES 11 A 308 ARG ASP GLU HIS GLY LYS LEU LEU PHE GLU THR VAL ASP
SEQRES 12 A 308 ILE CYS ASP THR TRP GLU ALA MET GLU LYS CYS LYS ASP
SEQRES 13 A 308 ALA GLY LEU ALA LYS SER ILE GLY VAL SER ASN PHE ASN
SEQRES 14 A 308 CYS ARG GLN LEU GLU ARG ILE LEU ASN LYS PRO GLY LEU
SEQRES 15 A 308 LYS TYR LYS PRO VAL CYS ASN GLN VAL GLU CYS HIS LEU
SEQRES 16 A 308 TYR LEU ASN GLN SER LYS MET LEU ASP TYR CYS LYS SER
SEQRES 17 A 308 LYS ASP ILE ILE LEU VAL SER TYR CYS THR LEU GLY SER
SEQRES 18 A 308 SER ARG ASP LYS THR TRP VAL ASP GLN LYS SER PRO VAL
SEQRES 19 A 308 LEU LEU ASP ASP PRO VAL LEU CYS ALA ILE ALA LYS LYS
SEQRES 20 A 308 TYR LYS GLN THR PRO ALA LEU VAL ALA LEU ARG TYR GLN
SEQRES 21 A 308 LEU GLN ARG GLY VAL VAL PRO LEU ILE ARG SER PHE ASN
SEQRES 22 A 308 ALA LYS ARG ILE LYS GLU LEU THR GLN VAL PHE GLU PHE
SEQRES 23 A 308 GLN LEU ALA SER GLU ASP MET LYS ALA LEU ASP GLY LEU
SEQRES 24 A 308 ASN ARG ASN PHE ARG TYR ASN ASN ALA
HELIX 1 1 VAL A 34 ASP A 43 1 10
HELIX 2 2 VAL A 57 GLY A 72 1 16
HELIX 3 3 LYS A 75 ILE A 79 5 5
HELIX 4 4 ARG A 91 GLU A 93 5 3
HELIX 5 5 LEU A 94 GLN A 107 1 14
HELIX 6 6 ASP A 143 ALA A 157 1 15
HELIX 7 7 ASN A 169 LEU A 177 1 9
HELIX 8 8 GLN A 199 LYS A 207 1 9
HELIX 9 9 SER A 208 ASP A 210 5 3
HELIX 10 10 VAL A 234 ASP A 237 5 4
HELIX 11 11 ASP A 238 TYR A 248 1 11
HELIX 12 12 PRO A 252 GLY A 264 1 13
HELIX 13 13 ASN A 273 GLU A 279 1 7
HELIX 14 14 LEU A 280 GLU A 285 5 6
HELIX 15 15 ALA A 289 ASP A 297 1 9
SHEET 1 A 2 ARG A 7 LEU A 10 0
SHEET 2 A 2 ASN A 14 PRO A 17 -1 N ASN A 14 O LEU A 10
SHEET 1 B 9 GLY A 20 GLY A 22 0
SHEET 2 B 9 HIS A 48 ASP A 50 1 O HIS A 48 N PHE A 21
SHEET 3 B 9 PHE A 80 LEU A 85 1 O PHE A 80 N PHE A 49
SHEET 4 B 9 LEU A 113 ILE A 116 1 N LEU A 113 O TYR A 81
SHEET 5 B 9 ILE A 163 SER A 166 1 N GLY A 164 O TYR A 114
SHEET 6 B 9 ASN A 189 GLU A 192 1 N GLN A 190 O VAL A 165
SHEET 7 B 9 VAL A 214 TYR A 216 1 O VAL A 214 N VAL A 191
SHEET 8 B 9 VAL A 266 ILE A 269 1 O VAL A 266 N SER A 215
SHEET 9 B 9 GLY A 20 GLY A 22 1 N GLY A 20 O PRO A 267
CRYST1 51.300 89.500 143.300 90.00 90.00 90.00 C 2 2 21 8
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 0.019493 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011173 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006978 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
