HEADER HORMONE/GROWTH FACTOR 22-JAN-00 1DVT
TITLE CRYSTAL STRUCTURE OF HUMAN TRANSTHYRETIN IN COMPLEX WITH FLURBIPROFEN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TRANSTHYRETIN;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: PREALBUMIN;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS THYROXINE TRANSPORT, SIGNALING PROTEIN, HORMONE-GROWTH FACTOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR T.KLABUNDE,H.M.PETRASSI,V.B.OZA,J.W.KELLY,J.C.SACCHETTINI
REVDAT 3 07-FEB-24 1DVT 1 REMARK
REVDAT 2 24-FEB-09 1DVT 1 VERSN
REVDAT 1 22-JAN-01 1DVT 0
JRNL AUTH T.KLABUNDE,H.M.PETRASSI,V.B.OZA,P.RAMAN,J.W.KELLY,
JRNL AUTH 2 J.C.SACCHETTINI
JRNL TITL RATIONAL DESIGN OF POTENT HUMAN TRANSTHYRETIN AMYLOID
JRNL TITL 2 DISEASE INHIBITORS.
JRNL REF NAT.STRUCT.BIOL. V. 7 312 2000
JRNL REFN ISSN 1072-8368
JRNL PMID 10742177
JRNL DOI 10.1038/74082
REMARK 2
REMARK 2 RESOLUTION. 1.90 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) : 1.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 8.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 90.5
REMARK 3 NUMBER OF REFLECTIONS : 17529
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOMLY CHOSEN SUBSET OF 10
REMARK 3 % OF THE OBSERVED REFLECTIONS
REMARK 3 R VALUE (WORKING SET) : 0.197
REMARK 3 FREE R VALUE : 0.220
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 1745
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 : 1771
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 18
REMARK 3 SOLVENT ATOMS : 57
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) : 0.006
REMARK 3 BOND ANGLES (DEGREES) : 1.261
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 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : 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: THE STRUCTURE CONTAINS TWO FLURBIPROFEN
REMARK 3 MOLECULES THAT BIND IN EACH OF TWO INDEPENDENT BINDING SITES OF
REMARK 3 THE TETRAMER. SINCE THE BINDING IS ALONG THE 2-FOLD
REMARK 3 CRYSTALLOGRAPHIC AXIS, AN OCCUPANCY OF 0.5 CORRESPONDS TO
REMARK 3 SATURATION OF EACH OF THE BINDING SITES.
REMARK 4
REMARK 4 1DVT COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 28-JAN-00.
REMARK 100 THE DEPOSITION ID IS D_1000010417.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 02-FEB-99
REMARK 200 TEMPERATURE (KELVIN) : 293
REMARK 200 PH : 7.4
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 RU200
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MACSCIENCE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 20907
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.850
REMARK 200 RESOLUTION RANGE LOW (A) : 10.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.8
REMARK 200 DATA REDUNDANCY : 3.700
REMARK 200 R MERGE (I) : 0.05800
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 10.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.85
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.95
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.8
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.35000
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: NULL
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 45.13
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.24
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: POTASSIUM CHLORIDE, POTASSIUM
REMARK 280 PHOSPHATE, AMMONIUM SULFATE, PH 7.4, VAPOR DIFFUSION, HANGING
REMARK 280 DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
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 21.69000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 42.78000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 21.69000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 42.78000
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 300 REMARK: THE BIOLOGICAL ASSEMBLE IS A TETRAMER CONSTRUCTED FROM THE
REMARK 300 DIMER (CHAIN A AND CHAIN B) AND A SYMMETRY MATE GENERATED BY THE
REMARK 300 TWO-FOLD.
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: TETRAMERIC
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 350 BIOMT1 2 -1.000000 0.000000 0.000000 43.38000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 85.56000
REMARK 350 BIOMT3 2 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 1
REMARK 465 PRO A 2
REMARK 465 THR A 3
REMARK 465 GLY A 4
REMARK 465 THR A 5
REMARK 465 GLY A 6
REMARK 465 GLU A 7
REMARK 465 SER A 8
REMARK 465 LYS A 9
REMARK 465 GLY B 1
REMARK 465 PRO B 2
REMARK 465 THR B 3
REMARK 465 GLY B 4
REMARK 465 THR B 5
REMARK 465 GLY B 6
REMARK 465 GLU B 7
REMARK 465 SER B 8
REMARK 465 LYS B 9
REMARK 465 ASN B 124
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 ASN A 98 19.98 56.96
REMARK 500 ASP B 99 -19.34 71.96
REMARK 500 SER B 100 87.43 -59.02
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 FLP A 125
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1BMZ RELATED DB: PDB
REMARK 900 HUMAN TRANSTHYRETIN (PREALBUMIN)
REMARK 900 RELATED ID: 1DVQ RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN TRANSTHYRETIN
REMARK 900 RELATED ID: 1DVS RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN TRANSTHYRETIN IN COMPLEX WITH RESVERATROL
REMARK 900 RELATED ID: 1DVU RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN TRANSTHYRETIN IN COMPLEX WITH
REMARK 900 DIBENZOFURAN-4,6-DICARBOXYLIC ACID
REMARK 900 RELATED ID: 1DVX RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN TRANSTHYRETIN IN COMPLEX WITH DICLOFENAC
REMARK 900 RELATED ID: 1DVY RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF TRANSTHYRETIN IN COMPLEX WITH N-(M-
REMARK 900 TRIFLUOROMETHYLPHENYL) PHENOXAZINE-4,6-DICARBOXYLIC ACID
REMARK 900 RELATED ID: 1DVZ RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN TRANSTHYRETIN IN COMPLEX WITH O-
REMARK 900 TRIFLUOROMETHYLPHENYL ANTHRANILIC ACID
DBREF 1DVT A 1 124 UNP P02766 TTHY_HUMAN 1 124
DBREF 1DVT B 1 124 UNP P02766 TTHY_HUMAN 1 124
SEQRES 1 A 124 GLY PRO THR GLY THR GLY GLU SER LYS CYS PRO LEU MET
SEQRES 2 A 124 VAL LYS VAL LEU ASP ALA VAL ARG GLY SER PRO ALA ILE
SEQRES 3 A 124 ASN VAL ALA VAL HIS VAL PHE ARG LYS ALA ALA ASP ASP
SEQRES 4 A 124 THR TRP GLU PRO PHE ALA SER GLY LYS THR SER GLU SER
SEQRES 5 A 124 GLY GLU LEU HIS GLY LEU THR THR GLU GLU GLN PHE VAL
SEQRES 6 A 124 GLU GLY ILE TYR LYS VAL GLU ILE ASP THR LYS SER TYR
SEQRES 7 A 124 TRP LYS ALA LEU GLY ILE SER PRO PHE HIS GLU HIS ALA
SEQRES 8 A 124 GLU VAL VAL PHE THR ALA ASN ASP SER GLY PRO ARG ARG
SEQRES 9 A 124 TYR THR ILE ALA ALA LEU LEU SER PRO TYR SER TYR SER
SEQRES 10 A 124 THR THR ALA VAL VAL THR ASN
SEQRES 1 B 124 GLY PRO THR GLY THR GLY GLU SER LYS CYS PRO LEU MET
SEQRES 2 B 124 VAL LYS VAL LEU ASP ALA VAL ARG GLY SER PRO ALA ILE
SEQRES 3 B 124 ASN VAL ALA VAL HIS VAL PHE ARG LYS ALA ALA ASP ASP
SEQRES 4 B 124 THR TRP GLU PRO PHE ALA SER GLY LYS THR SER GLU SER
SEQRES 5 B 124 GLY GLU LEU HIS GLY LEU THR THR GLU GLU GLN PHE VAL
SEQRES 6 B 124 GLU GLY ILE TYR LYS VAL GLU ILE ASP THR LYS SER TYR
SEQRES 7 B 124 TRP LYS ALA LEU GLY ILE SER PRO PHE HIS GLU HIS ALA
SEQRES 8 B 124 GLU VAL VAL PHE THR ALA ASN ASP SER GLY PRO ARG ARG
SEQRES 9 B 124 TYR THR ILE ALA ALA LEU LEU SER PRO TYR SER TYR SER
SEQRES 10 B 124 THR THR ALA VAL VAL THR ASN
HET FLP A 125 36
HETNAM FLP FLURBIPROFEN
FORMUL 3 FLP C15 H13 F O2
FORMUL 4 HOH *57(H2 O)
HELIX 1 1 ASP A 74 LEU A 82 1 9
HELIX 2 2 ASP B 74 LEU B 82 1 9
SHEET 1 A 8 SER A 23 PRO A 24 0
SHEET 2 A 8 LEU A 12 ASP A 18 -1 N ASP A 18 O SER A 23
SHEET 3 A 8 ARG A 104 SER A 112 1 O TYR A 105 N MET A 13
SHEET 4 A 8 SER A 115 THR A 123 -1 O SER A 115 N SER A 112
SHEET 5 A 8 SER B 115 THR B 123 -1 O TYR B 116 N THR A 118
SHEET 6 A 8 ARG B 104 SER B 112 -1 N ARG B 104 O THR B 123
SHEET 7 A 8 LEU B 12 ASP B 18 1 N MET B 13 O TYR B 105
SHEET 8 A 8 SER B 23 PRO B 24 -1 O SER B 23 N ASP B 18
SHEET 1 B 8 GLU A 54 LEU A 55 0
SHEET 2 B 8 LEU A 12 ASP A 18 -1 O VAL A 14 N LEU A 55
SHEET 3 B 8 ARG A 104 SER A 112 1 O TYR A 105 N MET A 13
SHEET 4 B 8 SER A 115 THR A 123 -1 O SER A 115 N SER A 112
SHEET 5 B 8 SER B 115 THR B 123 -1 O TYR B 116 N THR A 118
SHEET 6 B 8 ARG B 104 SER B 112 -1 N ARG B 104 O THR B 123
SHEET 7 B 8 LEU B 12 ASP B 18 1 N MET B 13 O TYR B 105
SHEET 8 B 8 GLU B 54 LEU B 55 -1 N LEU B 55 O VAL B 14
SHEET 1 C 8 TRP A 41 LYS A 48 0
SHEET 2 C 8 ALA A 29 LYS A 35 -1 N VAL A 30 O GLY A 47
SHEET 3 C 8 GLY A 67 ILE A 73 -1 O ILE A 68 N LYS A 35
SHEET 4 C 8 HIS A 88 ALA A 97 -1 O ALA A 91 N ILE A 73
SHEET 5 C 8 HIS B 88 ALA B 97 -1 N GLU B 89 O VAL A 94
SHEET 6 C 8 GLY B 67 ILE B 73 -1 O GLY B 67 N ALA B 97
SHEET 7 C 8 ALA B 29 LYS B 35 -1 O HIS B 31 N GLU B 72
SHEET 8 C 8 TRP B 41 LYS B 48 -1 N GLU B 42 O ARG B 34
SITE 1 AC1 14 LYS A 15 LEU A 17 ALA A 108 ALA A 109
SITE 2 AC1 14 LEU A 110 SER A 117 LYS B 15 LEU B 17
SITE 3 AC1 14 THR B 106 ALA B 108 ALA B 109 LEU B 110
SITE 4 AC1 14 SER B 117 THR B 119
CRYST1 43.380 85.560 64.880 90.00 90.00 90.00 P 21 21 2 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 0.023052 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011688 0.000000 0.00000
SCALE3 0.000000 0.000000 0.015413 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
