HEADER TRANSPORT PROTEIN 28-MAY-14 4TKW
TITLE CRYSTAL STRUCTURE OF HUMAN TRANSTHYRETIN LEU55PRO MUTANT
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TRANSTHYRETIN;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: UNP RESIDUES 29-147;
COMPND 5 SYNONYM: ATTR,PREALBUMIN,TBPA;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: TTR, PALB;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: ROSETTA (DE3) PLYSS;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET24
KEYWDS HUMAN TRANSTHYRETIN, AMYLOID, TRANSTHYRETIN, MUTANT, TRANSPORT
KEYWDS 2 PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR L.SAELICES,D.CASCIO,M.SAWAYA,D.S.EISENBERG
REVDAT 5 27-DEC-23 4TKW 1 REMARK
REVDAT 4 14-DEC-16 4TKW 1 TITLE
REVDAT 3 09-DEC-15 4TKW 1 JRNL
REVDAT 2 28-OCT-15 4TKW 1 JRNL
REVDAT 1 21-OCT-15 4TKW 0
JRNL AUTH L.SAELICES,L.M.JOHNSON,W.Y.LIANG,M.R.SAWAYA,D.CASCIO,
JRNL AUTH 2 P.RUCHALA,J.WHITELEGGE,L.JIANG,R.RIEK,D.S.EISENBERG
JRNL TITL UNCOVERING THE MECHANISM OF AGGREGATION OF HUMAN
JRNL TITL 2 TRANSTHYRETIN.
JRNL REF J.BIOL.CHEM. V. 290 28932 2015
JRNL REFN ESSN 1083-351X
JRNL PMID 26459562
JRNL DOI 10.1074/JBC.M115.659912
REMARK 2
REMARK 2 RESOLUTION. 1.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER 2.10.0
REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,
REMARK 3 : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,
REMARK 3 : WOMACK,MATTHEWS,TEN EYCK,TRONRUD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.87
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 3 NUMBER OF REFLECTIONS : 22488
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) : 0.195
REMARK 3 R VALUE (WORKING SET) : 0.195
REMARK 3 FREE R VALUE : 0.200
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1147
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 : 11
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 1.89
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.31
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 2857
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2094
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2718
REMARK 3 BIN R VALUE (WORKING SET) : 0.2091
REMARK 3 BIN FREE R VALUE : 0.2146
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.87
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 139
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 : 1725
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 55
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 28.82
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 37.42
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -7.85930
REMARK 3 B22 (A**2) : 7.02590
REMARK 3 B33 (A**2) : 0.83340
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.249
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : 0.119
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.101
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.120
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : 0.101
REMARK 3
REMARK 3 REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797
REMARK 3 CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.943
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.950
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 1773 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 2427 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 555 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : 26 ; 2.000 ; HARMONIC
REMARK 3 GENERAL PLANES : 266 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 1773 ; 20.000 ; HARMONIC
REMARK 3 BAD NON-BONDED CONTACTS : NULL ; NULL ; NULL
REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL
REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL
REMARK 3 CHIRAL IMPROPER TORSION : 246 ; 5.000 ; SEMIHARMONIC
REMARK 3 SUM OF OCCUPANCIES : NULL ; NULL ; NULL
REMARK 3 UTILITY DISTANCES : NULL ; NULL ; NULL
REMARK 3 UTILITY ANGLES : NULL ; NULL ; NULL
REMARK 3 UTILITY TORSION : NULL ; NULL ; NULL
REMARK 3 IDEAL-DIST CONTACT TERM : 1885 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 1.01
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.53
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 14.44
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 2
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: { A|* }
REMARK 3 ORIGIN FOR THE GROUP (A): 45.6775 29.6686 71.6278
REMARK 3 T TENSOR
REMARK 3 T11: -0.0479 T22: -0.0694
REMARK 3 T33: -0.0671 T12: -0.0072
REMARK 3 T13: 0.0069 T23: -0.0551
REMARK 3 L TENSOR
REMARK 3 L11: 1.9124 L22: 3.8790
REMARK 3 L33: 1.1678 L12: 0.4600
REMARK 3 L13: -0.1507 L23: 0.6101
REMARK 3 S TENSOR
REMARK 3 S11: -0.1218 S12: 0.2405 S13: -0.2155
REMARK 3 S21: -0.3054 S22: 0.0444 S23: -0.1286
REMARK 3 S31: 0.0669 S32: -0.1092 S33: 0.0775
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: { B|* }
REMARK 3 ORIGIN FOR THE GROUP (A): 42.4420 29.1576 91.0593
REMARK 3 T TENSOR
REMARK 3 T11: 0.0106 T22: -0.0644
REMARK 3 T33: -0.0393 T12: 0.0130
REMARK 3 T13: 0.0003 T23: 0.0090
REMARK 3 L TENSOR
REMARK 3 L11: 1.5207 L22: 2.1085
REMARK 3 L33: 0.7194 L12: -0.7048
REMARK 3 L13: 0.4080 L23: -0.1733
REMARK 3 S TENSOR
REMARK 3 S11: -0.0637 S12: 0.0358 S13: -0.0410
REMARK 3 S21: 0.2796 S22: -0.0187 S23: 0.1224
REMARK 3 S31: -0.0081 S32: 0.0238 S33: 0.0824
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4TKW COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-MAY-14.
REMARK 100 THE DEPOSITION ID IS D_1000201792.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-MAR-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 24-ID-C
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9792
REMARK 200 MONOCHROMATOR : SI (111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : PSI PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 22582
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800
REMARK 200 RESOLUTION RANGE LOW (A) : 19.870
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 200 DATA REDUNDANCY : 6.260
REMARK 200 R MERGE (I) : 0.08900
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 10.8400
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.85
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.2
REMARK 200 DATA REDUNDANCY IN SHELL : 5.69
REMARK 200 R MERGE FOR SHELL (I) : 1.12100
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.580
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 42.17
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.13
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% (W/V) PEG-1000, 0.1M IMIDAZOLE,
REMARK 280 0.2M CALCIUM ACETATE, PH 8.0, VAPOR DIFFUSION, TEMPERATURE 298K
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 21.53000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 42.20000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 21.53000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 42.20000
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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 6270 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 19260 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -44.0 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 350 BIOMT1 2 -1.000000 0.000000 0.000000 86.12000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 84.40000
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 LYS A 9
REMARK 465 PRO A 125
REMARK 465 LYS A 126
REMARK 465 GLU A 127
REMARK 465 HIS A 128
REMARK 465 HIS A 129
REMARK 465 HIS A 130
REMARK 465 HIS A 131
REMARK 465 HIS A 132
REMARK 465 HIS A 133
REMARK 465 LYS B 9
REMARK 465 PRO B 125
REMARK 465 LYS B 126
REMARK 465 GLU B 127
REMARK 465 HIS B 128
REMARK 465 HIS B 129
REMARK 465 HIS B 130
REMARK 465 HIS B 131
REMARK 465 HIS B 132
REMARK 465 HIS B 133
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 CYS A 10 SG
REMARK 470 LYS A 15 CD CE NZ
REMARK 470 ASP A 38 CG OD1 OD2
REMARK 470 GLU A 61 CG CD OE1 OE2
REMARK 470 GLU A 62 CG CD OE1 OE2
REMARK 470 GLU A 63 CG CD OE1 OE2
REMARK 470 GLU A 92 CG CD OE1 OE2
REMARK 470 ARG A 104 NE CZ NH1 NH2
REMARK 470 ASN A 124 CG OD1 ND2
REMARK 470 GLU B 61 CG CD OE1 OE2
REMARK 470 GLU B 63 CG CD OE1 OE2
REMARK 470 GLU B 92 CG CD OE1 OE2
REMARK 470 ASP B 99 CG OD1 OD2
REMARK 470 ARG B 104 CG CD NE CZ NH1 NH2
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 PHE B 44 -51.08 -121.68
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4TL4 RELATED DB: PDB
REMARK 900 RELATED ID: 4TL5 RELATED DB: PDB
REMARK 900 RELATED ID: 4TLK RELATED DB: PDB
REMARK 900 RELATED ID: 4TLS RELATED DB: PDB
DBREF 4TKW A 9 127 UNP P02766 TTHY_HUMAN 29 147
DBREF 4TKW B 9 127 UNP P02766 TTHY_HUMAN 29 147
SEQADV 4TKW PRO A 55 UNP P02766 LEU 75 ENGINEERED MUTATION
SEQADV 4TKW HIS A 128 UNP P02766 EXPRESSION TAG
SEQADV 4TKW HIS A 129 UNP P02766 EXPRESSION TAG
SEQADV 4TKW HIS A 130 UNP P02766 EXPRESSION TAG
SEQADV 4TKW HIS A 131 UNP P02766 EXPRESSION TAG
SEQADV 4TKW HIS A 132 UNP P02766 EXPRESSION TAG
SEQADV 4TKW HIS A 133 UNP P02766 EXPRESSION TAG
SEQADV 4TKW PRO B 55 UNP P02766 LEU 75 ENGINEERED MUTATION
SEQADV 4TKW HIS B 128 UNP P02766 EXPRESSION TAG
SEQADV 4TKW HIS B 129 UNP P02766 EXPRESSION TAG
SEQADV 4TKW HIS B 130 UNP P02766 EXPRESSION TAG
SEQADV 4TKW HIS B 131 UNP P02766 EXPRESSION TAG
SEQADV 4TKW HIS B 132 UNP P02766 EXPRESSION TAG
SEQADV 4TKW HIS B 133 UNP P02766 EXPRESSION TAG
SEQRES 1 A 125 LYS CYS PRO LEU MET VAL LYS VAL LEU ASP ALA VAL ARG
SEQRES 2 A 125 GLY SER PRO ALA ILE ASN VAL ALA VAL HIS VAL PHE ARG
SEQRES 3 A 125 LYS ALA ALA ASP ASP THR TRP GLU PRO PHE ALA SER GLY
SEQRES 4 A 125 LYS THR SER GLU SER GLY GLU PRO HIS GLY LEU THR THR
SEQRES 5 A 125 GLU GLU GLU PHE VAL GLU GLY ILE TYR LYS VAL GLU ILE
SEQRES 6 A 125 ASP THR LYS SER TYR TRP LYS ALA LEU GLY ILE SER PRO
SEQRES 7 A 125 PHE HIS GLU HIS ALA GLU VAL VAL PHE THR ALA ASN ASP
SEQRES 8 A 125 SER GLY PRO ARG ARG TYR THR ILE ALA ALA LEU LEU SER
SEQRES 9 A 125 PRO TYR SER TYR SER THR THR ALA VAL VAL THR ASN PRO
SEQRES 10 A 125 LYS GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 B 125 LYS CYS PRO LEU MET VAL LYS VAL LEU ASP ALA VAL ARG
SEQRES 2 B 125 GLY SER PRO ALA ILE ASN VAL ALA VAL HIS VAL PHE ARG
SEQRES 3 B 125 LYS ALA ALA ASP ASP THR TRP GLU PRO PHE ALA SER GLY
SEQRES 4 B 125 LYS THR SER GLU SER GLY GLU PRO HIS GLY LEU THR THR
SEQRES 5 B 125 GLU GLU GLU PHE VAL GLU GLY ILE TYR LYS VAL GLU ILE
SEQRES 6 B 125 ASP THR LYS SER TYR TRP LYS ALA LEU GLY ILE SER PRO
SEQRES 7 B 125 PHE HIS GLU HIS ALA GLU VAL VAL PHE THR ALA ASN ASP
SEQRES 8 B 125 SER GLY PRO ARG ARG TYR THR ILE ALA ALA LEU LEU SER
SEQRES 9 B 125 PRO TYR SER TYR SER THR THR ALA VAL VAL THR ASN PRO
SEQRES 10 B 125 LYS GLU HIS HIS HIS HIS HIS HIS
FORMUL 3 HOH *55(H2 O)
HELIX 1 AA1 ASP A 74 LEU A 82 1 9
HELIX 2 AA2 ASP B 74 LEU B 82 1 9
SHEET 1 AA1 8 SER A 23 PRO A 24 0
SHEET 2 AA1 8 LEU A 12 ASP A 18 -1 N ASP A 18 O SER A 23
SHEET 3 AA1 8 ARG A 104 SER A 112 1 O LEU A 111 N LEU A 17
SHEET 4 AA1 8 SER A 115 THR A 123 -1 O THR A 119 N ALA A 108
SHEET 5 AA1 8 SER B 115 THR B 123 -1 O TYR B 116 N THR A 118
SHEET 6 AA1 8 ARG B 104 SER B 112 -1 N ARG B 104 O THR B 123
SHEET 7 AA1 8 LEU B 12 ASP B 18 1 N MET B 13 O TYR B 105
SHEET 8 AA1 8 SER B 23 PRO B 24 -1 O SER B 23 N ASP B 18
SHEET 1 AA2 8 TRP A 41 LYS A 48 0
SHEET 2 AA2 8 ALA A 29 LYS A 35 -1 N VAL A 32 O ALA A 45
SHEET 3 AA2 8 GLY A 67 ILE A 73 -1 O GLU A 72 N HIS A 31
SHEET 4 AA2 8 HIS A 88 ALA A 97 -1 O ALA A 91 N ILE A 73
SHEET 5 AA2 8 ALA B 91 ALA B 97 -1 O VAL B 94 N GLU A 89
SHEET 6 AA2 8 GLY B 67 ILE B 73 -1 N ILE B 73 O ALA B 91
SHEET 7 AA2 8 ALA B 29 LYS B 35 -1 N HIS B 31 O GLU B 72
SHEET 8 AA2 8 TRP B 41 LYS B 48 -1 O ALA B 45 N VAL B 32
CRYST1 43.060 84.400 65.090 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 0.023223 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011848 0.000000 0.00000
SCALE3 0.000000 0.000000 0.015363 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
