HEADER ALLERGEN 18-NOV-11 4A84
TITLE CRYSTAL STRUCTURE OF MAJOR BIRCH POLLEN ALLERGEN BET V 1 A F30V MUTANT
TITLE 2 IN COMPLEX WITH DEOXYCHOLATE.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MAJOR POLLEN ALLERGEN BET V 1-A;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: BET V 1 A, ALLERGEN BET V I-A, BET V 1-A;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BETULA PENDULA;
SOURCE 3 ORGANISM_COMMON: EUROPEAN WHITE BIRCH;
SOURCE 4 ORGANISM_TAXID: 3505;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR: PET-28B
KEYWDS ALLERGEN, PR-10 PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR S.KOFLER,H.BRANDSTETTER
REVDAT 3 20-DEC-23 4A84 1 REMARK
REVDAT 2 15-AUG-12 4A84 1 JRNL
REVDAT 1 30-MAY-12 4A84 0
JRNL AUTH S.KOFLER,C.ASAM,U.ECKHARD,M.WALLNER,F.FERREIRA,
JRNL AUTH 2 H.BRANDSTETTER
JRNL TITL CRYSTALLOGRAPHICALLY MAPPED LIGAND BINDING DIFFERS IN HIGH
JRNL TITL 2 AND LOW IGE BINDING ISOFORMS OF BIRCH POLLEN ALLERGEN BET V
JRNL TITL 3 1.
JRNL REF J.MOL.BIOL. V. 422 109 2012
JRNL REFN ISSN 0022-2836
JRNL PMID 22634284
JRNL DOI 10.1016/J.JMB.2012.05.016
REMARK 2
REMARK 2 RESOLUTION. 1.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.6.0117
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) : 1.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 37.89
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.1
REMARK 3 NUMBER OF REFLECTIONS : 20173
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) : 0.169
REMARK 3 R VALUE (WORKING SET) : 0.165
REMARK 3 FREE R VALUE : 0.243
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1069
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) : 1.50
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.54
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1483
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 96.21
REMARK 3 BIN R VALUE (WORKING SET) : 0.2590
REMARK 3 BIN FREE R VALUE SET COUNT : 65
REMARK 3 BIN FREE R VALUE : 0.4370
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1229
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 69
REMARK 3 SOLVENT ATOMS : 188
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 14.07
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.05000
REMARK 3 B22 (A**2) : -0.09000
REMARK 3 B33 (A**2) : -0.93000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.23000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.124
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.103
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.075
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.460
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.964
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.928
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1373 ; 0.014 ; 0.020
REMARK 3 BOND LENGTHS OTHERS (A): 933 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 1888 ; 1.846 ; 2.032
REMARK 3 BOND ANGLES OTHERS (DEGREES): 2324 ; 0.964 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 173 ; 5.806 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 56 ;35.184 ;25.714
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 229 ;13.098 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 3 ;35.442 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 225 ; 0.102 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1473 ; 0.008 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 242 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 395 ; 0.249 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 948 ; 0.194 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 661 ; 0.176 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): 681 ; 0.088 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 41 ; 0.179 ; 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): 71 ; 0.301 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 36 ; 0.160 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 6 ; 0.116 ; 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): 1373 ;10.855 ; 1.483
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 933 ; 5.691 ; 1.474
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1881 ;13.545 ; 2.182
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 461 ;17.541 ; 4.405
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1127 ;20.661 ; 8.245
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): 2306 ; 3.479 ; 3.000
REMARK 3 SPHERICITY; FREE ATOMS (A**2): 68 ;40.251 ; 5.000
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): 2389 ;11.815 ; 5.000
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 : 1.20
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. U VALUES REFINED INDIVIDUALLY
REMARK 4
REMARK 4 4A84 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 18-NOV-11.
REMARK 100 THE DEPOSITION ID IS D_1290050361.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-SEP-11
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID29
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.91841
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : IMOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 21271
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.500
REMARK 200 RESOLUTION RANGE LOW (A) : 32.490
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.3
REMARK 200 DATA REDUNDANCY : 3.100
REMARK 200 R MERGE (I) : 0.11000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 4.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.58
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.0
REMARK 200 DATA REDUNDANCY IN SHELL : 2.90
REMARK 200 R MERGE FOR SHELL (I) : 0.74000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.100
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 4A80
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 37.71
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.97
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 7
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 27.99000
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 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 400
REMARK 400 COMPOUND
REMARK 400 ENGINEERED RESIDUE IN CHAIN A, PHE 31 TO VAL
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 OG SER A 11 OG SER A 112 2.03
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 ASP A 125 48.58 -87.35
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 DXC A 1160
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DXC A 1161
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MPD A 1162
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1163
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1LLT RELATED DB: PDB
REMARK 900 BIRCH POLLEN ALLERGEN BET V 1 MUTANT E45S
REMARK 900 RELATED ID: 1FSK RELATED DB: PDB
REMARK 900 COMPLEX FORMATION BETWEEN A FAB FRAGMENT OF A MONOCLONALIGG
REMARK 900 ANTIBODY AND THE MAJOR ALLERGEN FROM BIRCH POLLEN BET V1
REMARK 900 RELATED ID: 1QMR RELATED DB: PDB
REMARK 900 BIRCH POLLEN ALLERGEN BET V 1 MUTANT N28T, K32Q, E45S, P108G
REMARK 900 RELATED ID: 1B6F RELATED DB: PDB
REMARK 900 BIRCH POLLEN ALLERGEN BET V 1
REMARK 900 RELATED ID: 4A80 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MAJOR BIRCH POLLEN ALLERGEN BET V 1 A IN
REMARK 900 COMPLEX WITH 8-ANILINONAPHTHALENE-1-SULFONATE (ANS)
REMARK 900 RELATED ID: 1BTV RELATED DB: PDB
REMARK 900 STRUCTURE OF BET V 1, NMR, 20 STRUCTURES
REMARK 900 RELATED ID: 1BV1 RELATED DB: PDB
REMARK 900 BIRCH POLLEN ALLERGEN BET V 1
REMARK 900 RELATED ID: 4A81 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MAJOR BIRCH POLLEN ALLERGEN BET V 1 A IN
REMARK 900 TERNARY COMPLEX WITH 8-ANILINONAPHTHALENE-1- SULFONATE (ANS) AND
REMARK 900 DEOXYCHOLIC ACID
REMARK 900 RELATED ID: 4A83 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MAJOR BIRCH POLLEN ALLERGEN BET V 1 A IN
REMARK 900 COMPLEX WITH DEOXYCHOLATE.
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE UNIPROT SEQUENCE IS FURTHER PROCESSED INTO A MATURE
REMARK 999 FORM. MATURE PROTEIN LOST ITS STARTING METHIONINE.
DBREF 4A84 A 1 159 UNP P15494 BEV1A_BETPN 2 160
SEQADV 4A84 VAL A 30 UNP P15494 PHE 31 ENGINEERED MUTATION
SEQRES 1 A 159 GLY VAL PHE ASN TYR GLU THR GLU THR THR SER VAL ILE
SEQRES 2 A 159 PRO ALA ALA ARG LEU PHE LYS ALA PHE ILE LEU ASP GLY
SEQRES 3 A 159 ASP ASN LEU VAL PRO LYS VAL ALA PRO GLN ALA ILE SER
SEQRES 4 A 159 SER VAL GLU ASN ILE GLU GLY ASN GLY GLY PRO GLY THR
SEQRES 5 A 159 ILE LYS LYS ILE SER PHE PRO GLU GLY PHE PRO PHE LYS
SEQRES 6 A 159 TYR VAL LYS ASP ARG VAL ASP GLU VAL ASP HIS THR ASN
SEQRES 7 A 159 PHE LYS TYR ASN TYR SER VAL ILE GLU GLY GLY PRO ILE
SEQRES 8 A 159 GLY ASP THR LEU GLU LYS ILE SER ASN GLU ILE LYS ILE
SEQRES 9 A 159 VAL ALA THR PRO ASP GLY GLY SER ILE LEU LYS ILE SER
SEQRES 10 A 159 ASN LYS TYR HIS THR LYS GLY ASP HIS GLU VAL LYS ALA
SEQRES 11 A 159 GLU GLN VAL LYS ALA SER LYS GLU MET GLY GLU THR LEU
SEQRES 12 A 159 LEU ARG ALA VAL GLU SER TYR LEU LEU ALA HIS SER ASP
SEQRES 13 A 159 ALA TYR ASN
HET DXC A1160 28
HET DXC A1161 28
HET MPD A1162 8
HET SO4 A1163 5
HETNAM DXC (3ALPHA,5BETA,12ALPHA)-3,12-DIHYDROXYCHOLAN-24-OIC ACID
HETNAM MPD (4S)-2-METHYL-2,4-PENTANEDIOL
HETNAM SO4 SULFATE ION
HETSYN DXC DEOXYCHOLIC ACID
FORMUL 2 DXC 2(C24 H40 O4)
FORMUL 4 MPD C6 H14 O2
FORMUL 5 SO4 O4 S 2-
FORMUL 6 HOH *188(H2 O)
HELIX 1 1 PRO A 14 ILE A 23 1 10
HELIX 2 2 ASP A 25 ALA A 34 1 10
HELIX 3 3 LYS A 129 HIS A 154 1 26
SHEET 1 AA 7 VAL A 2 SER A 11 0
SHEET 2 AA 7 SER A 112 THR A 122 -1 O SER A 112 N SER A 11
SHEET 3 AA 7 LEU A 95 ALA A 106 -1 N GLU A 96 O HIS A 121
SHEET 4 AA 7 LYS A 80 GLU A 87 -1 O TYR A 81 N ILE A 102
SHEET 5 AA 7 TYR A 66 ASP A 75 -1 O LYS A 68 N ILE A 86
SHEET 6 AA 7 ILE A 53 SER A 57 -1 O LYS A 54 N ASP A 69
SHEET 7 AA 7 SER A 40 GLU A 45 -1 O SER A 40 N SER A 57
SITE 1 AC1 11 PHE A 22 ILE A 23 VAL A 30 ASP A 69
SITE 2 AC1 11 TYR A 83 ILE A 98 ASN A 100 TYR A 120
SITE 3 AC1 11 SER A 136 LEU A 143 DXC A1161
SITE 1 AC2 11 PHE A 58 PHE A 62 PRO A 63 PHE A 64
SITE 2 AC2 11 PRO A 90 ILE A 98 GLN A 132 ALA A 135
SITE 3 AC2 11 DXC A1160 HOH A2187 HOH A2188
SITE 1 AC3 4 PHE A 62 ALA A 135 THR A 142 HOH A2056
SITE 1 AC4 5 GLU A 6 THR A 7 GLU A 8 LYS A 32
SITE 2 AC4 5 TYR A 150
CRYST1 32.560 55.980 37.970 90.00 93.69 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 0.030713 0.000000 0.001981 0.00000
SCALE2 0.000000 0.017864 0.000000 0.00000
SCALE3 0.000000 0.000000 0.026391 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
