HEADER TRANSFERASE 15-DEC-06 2OA7
TITLE MOUSE C14A GLUTATHIONE-S-TRANSFERASE MUTANT IN COMPLEX WITH S-HEXYL
TITLE 2 GLUTATHIONE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GLUTATHIONE S-TRANSFERASE P 1;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: GST YF-YF, GST-PIB, GST CLASS-PI, GST P1, PREADIPOCYTE
COMPND 5 GROWTH FACTOR;
COMPND 6 EC: 2.5.1.18;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: HOUSE MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 GENE: GSTP1, GSTPIB;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS ENZYME-LIGAND COMPLEX, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR O.J.KYRIELEIS,G.MCMANUS,T.J.MANTLE,A.R.KHAN
REVDAT 6 30-AUG-23 2OA7 1 REMARK
REVDAT 5 20-OCT-21 2OA7 1 REMARK SEQADV
REVDAT 4 24-JUL-19 2OA7 1 REMARK
REVDAT 3 18-OCT-17 2OA7 1 REMARK
REVDAT 2 24-FEB-09 2OA7 1 VERSN
REVDAT 1 30-JAN-07 2OA7 0
JRNL AUTH O.J.KYRIELEIS,G.MCMANUS,T.J.MANTLE,A.R.KHAN
JRNL TITL MOUSE C14A GLUTATHIONE-S-TRANSFERASE MUTANT IN COMPLEX WITH
JRNL TITL 2 S-HEXYL GLUTATHIONE
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
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 : ENGH & HUBER
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 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 91.7
REMARK 3 NUMBER OF REFLECTIONS : 25671
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) : 0.217
REMARK 3 FREE R VALUE : 0.261
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.400
REMARK 3 FREE R VALUE TEST SET COUNT : 1237
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 : 3306
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 52
REMARK 3 SOLVENT ATOMS : 233
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 18.22
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.93900
REMARK 3 B22 (A**2) : -0.40100
REMARK 3 B33 (A**2) : -1.53800
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.60000
REMARK 3 B23 (A**2) : 0.00000
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) : 0.007
REMARK 3 BOND ANGLES (DEGREES) : NULL
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : ISOTROPIC
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 1.137 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 1.658 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 1.838 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 2.467 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : 32.71
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 : CNS_TOPPAR:PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : CNS_TOPPAR:DNA-RNA_REP.PARAM
REMARK 3 PARAMETER FILE 3 : CNS_TOPPAR:WATER_REP.PARAM
REMARK 3 PARAMETER FILE 4 : CNS_TOPPAR:ION.PARAM
REMARK 3 PARAMETER FILE 5 : GTX.PARAM
REMARK 3 PARAMETER FILE 6 : NULL
REMARK 3 TOPOLOGY FILE 1 : CNS_TOPPAR:PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : CNS_TOPPAR:DNA-RNA.TOP
REMARK 3 TOPOLOGY FILE 3 : CNS_TOPPAR:WATER.TOP
REMARK 3 TOPOLOGY FILE 4 : CNS_TOPPAR:ION.TOP
REMARK 3 TOPOLOGY FILE 5 : GTX.TOP
REMARK 3 TOPOLOGY FILE 6 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2OA7 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 19-DEC-06.
REMARK 100 THE DEPOSITION ID IS D_1000040881.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 18-DEC-95
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : GRAPHITE
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000, DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 29547
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 91.7
REMARK 200 DATA REDUNDANCY : 2.400
REMARK 200 R MERGE (I) : 0.04700
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 28.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.17
REMARK 200 COMPLETENESS FOR SHELL (%) : 91.1
REMARK 200 DATA REDUNDANCY IN SHELL : 2.40
REMARK 200 R MERGE FOR SHELL (I) : 0.12000
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: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: PDB ENTRY 1GLP
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 58.58
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.97
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
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 66.30100
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 39.27050
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 66.30100
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 39.27050
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: 4310 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 17870 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -19.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
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 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 SER A 27 OG
REMARK 480 ASP A 36 OD1 OD2
REMARK 480 ASP A 59 OD1 OD2
REMARK 480 GLN A 83 OE1 NE2
REMARK 480 LYS A 120 CE NZ
REMARK 480 GLN A 147 CD OE1 NE2
REMARK 480 GLU A 197 OE1 OE2
REMARK 480 GLU B 31 OE1 OE2
REMARK 480 LEU B 42 CD1 CD2
REMARK 480 ASP B 59 OD1 OD2
REMARK 480 ASN B 113 OD1 ND2
REMARK 480 LYS B 120 NZ
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 GLN A 64 108.78 81.38
REMARK 500 ASN A 110 51.64 -163.25
REMARK 500 ALA A 141 -117.51 -108.71
REMARK 500 ASN A 204 -168.64 -121.37
REMARK 500 GLN B 64 107.55 73.88
REMARK 500 ASN B 110 41.92 -167.53
REMARK 500 ALA B 141 -123.47 -118.24
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 GTX A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GTX B 302
DBREF 2OA7 A 1 209 UNP P19157 GSTP1_MOUSE 1 209
DBREF 2OA7 B 1 209 UNP P19157 GSTP1_MOUSE 1 209
SEQADV 2OA7 ALA A 14 UNP P19157 CYS 14 ENGINEERED MUTATION
SEQADV 2OA7 ALA B 14 UNP P19157 CYS 14 ENGINEERED MUTATION
SEQRES 1 A 209 PRO PRO TYR THR ILE VAL TYR PHE PRO VAL ARG GLY ARG
SEQRES 2 A 209 ALA GLU ALA MET ARG MET LEU LEU ALA ASP GLN GLY GLN
SEQRES 3 A 209 SER TRP LYS GLU GLU VAL VAL THR ILE ASP THR TRP MET
SEQRES 4 A 209 GLN GLY LEU LEU LYS PRO THR CYS LEU TYR GLY GLN LEU
SEQRES 5 A 209 PRO LYS PHE GLU ASP GLY ASP LEU THR LEU TYR GLN SER
SEQRES 6 A 209 ASN ALA ILE LEU ARG HIS LEU GLY ARG SER LEU GLY LEU
SEQRES 7 A 209 TYR GLY LYS ASN GLN ARG GLU ALA ALA GLN MET ASP MET
SEQRES 8 A 209 VAL ASN ASP GLY VAL GLU ASP LEU ARG GLY LYS TYR VAL
SEQRES 9 A 209 THR LEU ILE TYR THR ASN TYR GLU ASN GLY LYS ASN ASP
SEQRES 10 A 209 TYR VAL LYS ALA LEU PRO GLY HIS LEU LYS PRO PHE GLU
SEQRES 11 A 209 THR LEU LEU SER GLN ASN GLN GLY GLY LYS ALA PHE ILE
SEQRES 12 A 209 VAL GLY ASP GLN ILE SER PHE ALA ASP TYR ASN LEU LEU
SEQRES 13 A 209 ASP LEU LEU LEU ILE HIS GLN VAL LEU ALA PRO GLY CYS
SEQRES 14 A 209 LEU ASP ASN PHE PRO LEU LEU SER ALA TYR VAL ALA ARG
SEQRES 15 A 209 LEU SER ALA ARG PRO LYS ILE LYS ALA PHE LEU SER SER
SEQRES 16 A 209 PRO GLU HIS VAL ASN ARG PRO ILE ASN GLY ASN GLY LYS
SEQRES 17 A 209 GLN
SEQRES 1 B 209 PRO PRO TYR THR ILE VAL TYR PHE PRO VAL ARG GLY ARG
SEQRES 2 B 209 ALA GLU ALA MET ARG MET LEU LEU ALA ASP GLN GLY GLN
SEQRES 3 B 209 SER TRP LYS GLU GLU VAL VAL THR ILE ASP THR TRP MET
SEQRES 4 B 209 GLN GLY LEU LEU LYS PRO THR CYS LEU TYR GLY GLN LEU
SEQRES 5 B 209 PRO LYS PHE GLU ASP GLY ASP LEU THR LEU TYR GLN SER
SEQRES 6 B 209 ASN ALA ILE LEU ARG HIS LEU GLY ARG SER LEU GLY LEU
SEQRES 7 B 209 TYR GLY LYS ASN GLN ARG GLU ALA ALA GLN MET ASP MET
SEQRES 8 B 209 VAL ASN ASP GLY VAL GLU ASP LEU ARG GLY LYS TYR VAL
SEQRES 9 B 209 THR LEU ILE TYR THR ASN TYR GLU ASN GLY LYS ASN ASP
SEQRES 10 B 209 TYR VAL LYS ALA LEU PRO GLY HIS LEU LYS PRO PHE GLU
SEQRES 11 B 209 THR LEU LEU SER GLN ASN GLN GLY GLY LYS ALA PHE ILE
SEQRES 12 B 209 VAL GLY ASP GLN ILE SER PHE ALA ASP TYR ASN LEU LEU
SEQRES 13 B 209 ASP LEU LEU LEU ILE HIS GLN VAL LEU ALA PRO GLY CYS
SEQRES 14 B 209 LEU ASP ASN PHE PRO LEU LEU SER ALA TYR VAL ALA ARG
SEQRES 15 B 209 LEU SER ALA ARG PRO LYS ILE LYS ALA PHE LEU SER SER
SEQRES 16 B 209 PRO GLU HIS VAL ASN ARG PRO ILE ASN GLY ASN GLY LYS
SEQRES 17 B 209 GLN
HET GTX A 301 26
HET GTX B 302 26
HETNAM GTX S-HEXYLGLUTATHIONE
FORMUL 3 GTX 2(C16 H30 N3 O6 S 1+)
FORMUL 5 HOH *233(H2 O)
HELIX 1 1 ALA A 14 GLN A 24 1 11
HELIX 2 2 THR A 34 MET A 39 1 6
HELIX 3 3 LEU A 43 CYS A 47 5 5
HELIX 4 4 GLN A 64 GLY A 77 1 14
HELIX 5 5 ASN A 82 ASN A 110 1 29
HELIX 6 6 ASN A 110 GLN A 135 1 26
HELIX 7 7 ASN A 136 LYS A 140 5 5
HELIX 8 8 SER A 149 ALA A 166 1 18
HELIX 9 9 PHE A 173 ARG A 186 1 14
HELIX 10 10 ARG A 186 SER A 195 1 10
HELIX 11 11 SER A 195 ARG A 201 1 7
HELIX 12 12 ALA B 14 GLN B 24 1 11
HELIX 13 13 THR B 34 MET B 39 1 6
HELIX 14 14 LEU B 43 CYS B 47 5 5
HELIX 15 15 GLN B 64 LEU B 76 1 13
HELIX 16 16 ASN B 82 ASN B 110 1 29
HELIX 17 17 ASN B 110 GLN B 135 1 26
HELIX 18 18 ASN B 136 LYS B 140 5 5
HELIX 19 19 SER B 149 ALA B 166 1 18
HELIX 20 20 PHE B 173 ARG B 186 1 14
HELIX 21 21 ARG B 186 SER B 194 1 9
HELIX 22 22 SER B 195 ASN B 200 1 6
SHEET 1 A 4 TRP A 28 VAL A 32 0
SHEET 2 A 4 TYR A 3 TYR A 7 1 N ILE A 5 O LYS A 29
SHEET 3 A 4 LYS A 54 ASP A 57 -1 O LYS A 54 N VAL A 6
SHEET 4 A 4 LEU A 60 TYR A 63 -1 O LEU A 62 N PHE A 55
SHEET 1 B 4 TRP B 28 VAL B 32 0
SHEET 2 B 4 TYR B 3 TYR B 7 1 N ILE B 5 O GLU B 31
SHEET 3 B 4 LYS B 54 ASP B 57 -1 O LYS B 54 N VAL B 6
SHEET 4 B 4 LEU B 60 TYR B 63 -1 O LEU B 62 N PHE B 55
CISPEP 1 PRO A 1 PRO A 2 0 1.08
CISPEP 2 LEU A 52 PRO A 53 0 0.30
CISPEP 3 PRO B 1 PRO B 2 0 1.01
CISPEP 4 LEU B 52 PRO B 53 0 0.30
SITE 1 AC1 16 PHE A 8 VAL A 10 ARG A 13 ILE A 35
SITE 2 AC1 16 LYS A 44 GLY A 50 GLN A 51 LEU A 52
SITE 3 AC1 16 GLN A 64 SER A 65 GLY A 205 HOH A 306
SITE 4 AC1 16 HOH A 316 HOH A 389 ASP B 98 HOH B 380
SITE 1 AC2 20 ILE A 35 ASP A 36 MET A 39 ASP A 98
SITE 2 AC2 20 PHE B 8 VAL B 10 ARG B 13 ILE B 35
SITE 3 AC2 20 TRP B 38 LYS B 44 GLN B 51 LEU B 52
SITE 4 AC2 20 PRO B 53 GLN B 64 SER B 65 GLY B 205
SITE 5 AC2 20 HOH B 303 HOH B 310 HOH B 311 HOH B 396
CRYST1 132.602 78.541 57.531 90.00 111.40 90.00 C 1 2 1 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 0.007541 0.000000 0.002955 0.00000
SCALE2 0.000000 0.012732 0.000000 0.00000
SCALE3 0.000000 0.000000 0.018669 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
