HEADER TRANSPORT PROTEIN 30-MAY-14 4TLK
TITLE CRYSTAL STRUCTURE OF HUMAN TRANSTHYRETIN SER85PRO/GLU92PRO 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 4 27-DEC-23 4TLK 1 JRNL REMARK
REVDAT 3 09-DEC-15 4TLK 1 JRNL
REVDAT 2 28-OCT-15 4TLK 1 JRNL
REVDAT 1 21-OCT-15 4TLK 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. 1.44 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) : 1.44
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 63.38
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 41846
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) : 0.189
REMARK 3 R VALUE (WORKING SET) : 0.189
REMARK 3 FREE R VALUE : 0.201
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.030
REMARK 3 FREE R VALUE TEST SET COUNT : 2105
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 : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 1.44
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 1.48
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.79
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 2999
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2299
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2838
REMARK 3 BIN R VALUE (WORKING SET) : 0.2286
REMARK 3 BIN FREE R VALUE : 0.2525
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.37
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 161
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 : 1773
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 22
REMARK 3 SOLVENT ATOMS : 100
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 21.48
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 25.51
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.46310
REMARK 3 B22 (A**2) : -0.59520
REMARK 3 B33 (A**2) : -0.86800
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) : 0.190
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : 0.065
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.062
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.064
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : 0.062
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 : 0.958
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.953
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 1866 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 2550 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 613 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : 35 ; 2.000 ; HARMONIC
REMARK 3 GENERAL PLANES : 277 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 1866 ; 20.000 ; HARMONIC
REMARK 3 BAD NON-BONDED CONTACTS : 0 ; 5.000 ; SEMIHARMONIC
REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL
REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL
REMARK 3 CHIRAL IMPROPER TORSION : 251 ; 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 : 2156 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 1.05
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 4.07
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 15.65
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): 44.1138 29.8905 69.4463
REMARK 3 T TENSOR
REMARK 3 T11: -0.0232 T22: -0.0132
REMARK 3 T33: -0.0156 T12: -0.0089
REMARK 3 T13: 0.0013 T23: -0.0203
REMARK 3 L TENSOR
REMARK 3 L11: 0.5170 L22: 0.7525
REMARK 3 L33: 0.6232 L12: 0.2159
REMARK 3 L13: 0.2211 L23: 0.3485
REMARK 3 S TENSOR
REMARK 3 S11: -0.0445 S12: 0.0573 S13: -0.0656
REMARK 3 S21: -0.0857 S22: -0.0146 S23: 0.0093
REMARK 3 S31: 0.0076 S32: -0.0236 S33: 0.0591
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: { B|* }
REMARK 3 ORIGIN FOR THE GROUP (A): 41.6121 29.4204 89.0831
REMARK 3 T TENSOR
REMARK 3 T11: -0.0172 T22: -0.0228
REMARK 3 T33: -0.0125 T12: 0.0060
REMARK 3 T13: -0.0002 T23: 0.0173
REMARK 3 L TENSOR
REMARK 3 L11: 0.6673 L22: 0.5296
REMARK 3 L33: 0.7825 L12: -0.2577
REMARK 3 L13: 0.2138 L23: -0.2833
REMARK 3 S TENSOR
REMARK 3 S11: -0.0148 S12: -0.0275 S13: -0.1101
REMARK 3 S21: 0.0764 S22: -0.0173 S23: 0.0275
REMARK 3 S31: 0.0158 S32: 0.0137 S33: 0.0321
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4TLK 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_1000201822.
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 : NULL
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 48638
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.440
REMARK 200 RESOLUTION RANGE LOW (A) : 63.380
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.0
REMARK 200 DATA REDUNDANCY : 6.700
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 13.3400
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: 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 (%): 39.70
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.04
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, HANGING DROP,
REMARK 280 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 20.99000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 42.62000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 20.99000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 42.62000
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: 8740 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 19040 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -86.0 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 83.96000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 85.24000
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 O2 PEG B 203 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 305 LIES ON A SPECIAL POSITION.
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 MET A 13 CG SD CE
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NA A 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NA B 202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG B 203
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG B 204
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4TKW RELATED DB: PDB
REMARK 900 RELATED ID: 4TL4 RELATED DB: PDB
REMARK 900 RELATED ID: 4TL5 RELATED DB: PDB
REMARK 900 RELATED ID: 4TLS RELATED DB: PDB
DBREF 4TLK A 9 127 UNP P02766 TTHY_HUMAN 29 147
DBREF 4TLK B 9 127 UNP P02766 TTHY_HUMAN 29 147
SEQADV 4TLK PRO A 85 UNP P02766 SER 105 ENGINEERED MUTATION
SEQADV 4TLK PRO A 92 UNP P02766 GLU 112 ENGINEERED MUTATION
SEQADV 4TLK HIS A 128 UNP P02766 EXPRESSION TAG
SEQADV 4TLK HIS A 129 UNP P02766 EXPRESSION TAG
SEQADV 4TLK HIS A 130 UNP P02766 EXPRESSION TAG
SEQADV 4TLK HIS A 131 UNP P02766 EXPRESSION TAG
SEQADV 4TLK HIS A 132 UNP P02766 EXPRESSION TAG
SEQADV 4TLK HIS A 133 UNP P02766 EXPRESSION TAG
SEQADV 4TLK PRO B 85 UNP P02766 SER 105 ENGINEERED MUTATION
SEQADV 4TLK PRO B 92 UNP P02766 GLU 112 ENGINEERED MUTATION
SEQADV 4TLK HIS B 128 UNP P02766 EXPRESSION TAG
SEQADV 4TLK HIS B 129 UNP P02766 EXPRESSION TAG
SEQADV 4TLK HIS B 130 UNP P02766 EXPRESSION TAG
SEQADV 4TLK HIS B 131 UNP P02766 EXPRESSION TAG
SEQADV 4TLK HIS B 132 UNP P02766 EXPRESSION TAG
SEQADV 4TLK 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 LEU 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 PRO PRO
SEQRES 7 A 125 PHE HIS GLU HIS ALA PRO 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 LEU 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 PRO PRO
SEQRES 7 B 125 PHE HIS GLU HIS ALA PRO 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
HET NA A 201 1
HET GOL B 201 6
HET NA B 202 1
HET PEG B 203 7
HET PEG B 204 7
HETNAM NA SODIUM ION
HETNAM GOL GLYCEROL
HETNAM PEG DI(HYDROXYETHYL)ETHER
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 3 NA 2(NA 1+)
FORMUL 4 GOL C3 H8 O3
FORMUL 6 PEG 2(C4 H10 O3)
FORMUL 8 HOH *100(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 THR B 118 N TYR A 116
SHEET 6 AA1 8 ARG B 104 SER B 112 -1 N ALA B 108 O THR B 119
SHEET 7 AA1 8 LEU B 12 ASP B 18 1 N LEU B 17 O LEU B 111
SHEET 8 AA1 8 SER B 23 PRO B 24 -1 O SER B 23 N ASP B 18
SHEET 1 AA2 8 GLU A 54 LEU A 55 0
SHEET 2 AA2 8 LEU A 12 ASP A 18 -1 N VAL A 14 O LEU A 55
SHEET 3 AA2 8 ARG A 104 SER A 112 1 O LEU A 111 N LEU A 17
SHEET 4 AA2 8 SER A 115 THR A 123 -1 O THR A 119 N ALA A 108
SHEET 5 AA2 8 SER B 115 THR B 123 -1 O THR B 118 N TYR A 116
SHEET 6 AA2 8 ARG B 104 SER B 112 -1 N ALA B 108 O THR B 119
SHEET 7 AA2 8 LEU B 12 ASP B 18 1 N LEU B 17 O LEU B 111
SHEET 8 AA2 8 GLU B 54 LEU B 55 -1 O LEU B 55 N VAL B 14
SHEET 1 AA3 8 TRP A 41 LYS A 48 0
SHEET 2 AA3 8 ALA A 29 LYS A 35 -1 N VAL A 32 O ALA A 45
SHEET 3 AA3 8 GLY A 67 ILE A 73 -1 O GLU A 72 N HIS A 31
SHEET 4 AA3 8 HIS A 88 ALA A 97 -1 O VAL A 93 N VAL A 71
SHEET 5 AA3 8 HIS B 88 ALA B 97 -1 O VAL B 94 N GLU A 89
SHEET 6 AA3 8 GLY B 67 ILE B 73 -1 N TYR B 69 O PHE B 95
SHEET 7 AA3 8 ALA B 29 LYS B 35 -1 N HIS B 31 O GLU B 72
SHEET 8 AA3 8 TRP B 41 LYS B 48 -1 O ALA B 45 N VAL B 32
LINK O LEU A 12 NA NA A 201 1555 1555 3.03
LINK O LEU B 12 NA NA B 202 1555 1555 2.80
SITE 1 AC1 5 CYS A 10 PRO A 11 LEU A 12 LEU A 58
SITE 2 AC1 5 THR A 59
SITE 1 AC2 5 VAL A 20 GLY A 83 PRO A 85 HOH A 312
SITE 2 AC2 5 VAL B 20
SITE 1 AC3 5 CYS B 10 PRO B 11 LEU B 12 LEU B 58
SITE 2 AC3 5 THR B 59
SITE 1 AC4 4 LEU B 110 SER B 117 THR B 118 THR B 119
SITE 1 AC5 10 TRP A 41 LYS A 70 GLU A 72 HIS A 90
SITE 2 AC5 10 PRO A 92 TRP B 41 LYS B 70 GLU B 72
SITE 3 AC5 10 HIS B 90 PRO B 92
CRYST1 41.980 85.240 63.380 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 0.023821 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011732 0.000000 0.00000
SCALE3 0.000000 0.000000 0.015778 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
