HEADER TRANSPORT PROTEIN 23-APR-01 1IIK
TITLE CRYSTAL STRUCTURE OF THE TRANSTHYRETIN MUTANT TTR Y114C-DATA COLLECTED
TITLE 2 AT CRYO TEMPERATURE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TRANSTHYRETIN;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: TRANSTHYRETIN;
COMPND 5 SYNONYM: TBPA, TTR, ATTR;
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;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET3
KEYWDS GREEK KEY, BETA BARREL, TRANSPORT PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR T.ENEQVIST,A.OLOFSSON,Y.ANDO,E.LUNDGREN,A.E.SAUER-ERIKSSON
REVDAT 5 16-AUG-23 1IIK 1 REMARK
REVDAT 4 27-OCT-21 1IIK 1 REMARK SEQADV LINK
REVDAT 3 13-JUL-11 1IIK 1 VERSN
REVDAT 2 24-FEB-09 1IIK 1 VERSN
REVDAT 1 15-NOV-02 1IIK 0
JRNL AUTH T.ENEQVIST,A.OLOFSSON,Y.ANDO,T.MIYAKAWA,S.KATSURAGI,J.JASS,
JRNL AUTH 2 E.LUNDGREN,A.E.SAUER-ERIKSSON
JRNL TITL DISULFIDE-BOND FORMATION IN THE TRANSTHYRETIN MUTANT Y114C
JRNL TITL 2 PREVENTS AMYLOID FIBRIL FORMATION IN VIVO AND IN VITRO
JRNL REF BIOCHEMISTRY V. 41 13143 2002
JRNL REFN ISSN 0006-2960
JRNL PMID 12403615
JRNL DOI 10.1021/BI025800W
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.32
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 14658
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) : 0.197
REMARK 3 R VALUE (WORKING SET) : 0.192
REMARK 3 FREE R VALUE : 0.239
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 11.200
REMARK 3 FREE R VALUE TEST SET COUNT : 1649
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 : 24
REMARK 3 SOLVENT ATOMS : 198
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 14.10
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 16.41
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.27000
REMARK 3 B22 (A**2) : -0.06000
REMARK 3 B33 (A**2) : -0.21000
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 OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.220
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.184
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.174
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.067
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 DISTANCE RESTRAINTS. RMS SIGMA
REMARK 3 BOND LENGTH (A) : 0.009 ; 0.021
REMARK 3 ANGLE DISTANCE (A) : 1.256 ; 1.939
REMARK 3 INTRAPLANAR 1-4 DISTANCE (A) : NULL ; NULL
REMARK 3 H-BOND OR METAL COORDINATION (A) : NULL ; NULL
REMARK 3
REMARK 3 PLANE RESTRAINT (A) : 0.004 ; 0.020
REMARK 3 CHIRAL-CENTER RESTRAINT (A**3) : 0.075 ; 0.200
REMARK 3
REMARK 3 NON-BONDED CONTACT RESTRAINTS.
REMARK 3 SINGLE TORSION (A) : 3.895 ; 3.000
REMARK 3 MULTIPLE TORSION (A) : 17.749; 15.000
REMARK 3 H-BOND (X...Y) (A) : 0.162 ; 0.500
REMARK 3 H-BOND (X-H...Y) (A) : 0.223 ; 0.300
REMARK 3
REMARK 3 CONFORMATIONAL TORSION ANGLE RESTRAINTS.
REMARK 3 SPECIFIED (DEGREES) : NULL ; NULL
REMARK 3 PLANAR (DEGREES) : NULL ; NULL
REMARK 3 STAGGERED (DEGREES) : NULL ; NULL
REMARK 3 TRANSVERSE (DEGREES) : NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 0.731 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 1.399 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 1.849 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 3.129 ; 4.500
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: OCCUPANCY OF BME MOLECULES WERE REFINED
REMARK 3 AFTER STRUCTURAL OVERALL B-FACTOR REFINEMENT
REMARK 4
REMARK 4 1IIK COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-APR-01.
REMARK 100 THE DEPOSITION ID IS D_1000013301.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 30-OCT-00
REMARK 200 TEMPERATURE (KELVIN) : 110
REMARK 200 PH : 5.0
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 : ENRAF-NONIUS
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NI FILTER
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 : 16411
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.9
REMARK 200 DATA REDUNDANCY : 3.900
REMARK 200 R MERGE (I) : 0.07700
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.07
REMARK 200 COMPLETENESS FOR SHELL (%) : 94.8
REMARK 200 DATA REDUNDANCY IN SHELL : 3.80
REMARK 200 R MERGE FOR SHELL (I) : 0.27200
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.100
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: PDB ENTRY 1F41
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 43.53
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.18
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 40% PEG 550 MONOMETHYL ETHER, 0.1M
REMARK 280 SODIUM CITRATE, 0.1M AMMONIUM SULPHATE, 0.1% BME, PH 5.0, VAPOR
REMARK 280 DIFFUSION, HANGING DROP AT 298K, TEMPERATURE 298.0K
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 21.64400
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 42.64400
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 21.64400
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 42.64400
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 SECOND PART OF THE BIOLOGICAL ASSEMBLY IS GENERATED BY
REMARK 300 THE TWO FOLD AXIS: -X, -Y, Z.
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,PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 6770 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 19780 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -50.0 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 43.28800
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 85.28800
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 HOH A 915 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 996 LIES ON A SPECIAL POSITION.
REMARK 375 HOH B 915 LIES ON A SPECIAL POSITION.
REMARK 375 HOH B 947 LIES ON A SPECIAL POSITION.
REMARK 375 HOH B 995 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 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 LYS A 126
REMARK 465 GLU A 127
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 PRO B 125
REMARK 465 LYS B 126
REMARK 465 GLU B 127
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 HIS A 90 -179.92 -172.74
REMARK 500 PRO B 102 -175.73 -53.97
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 BME A 901
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BME B 902
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BME A 903
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BME A 904
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BME B 905
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BME B 906
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1III RELATED DB: PDB
REMARK 900 A SINGLE MUTANT TTR Y114C AT ROOM TEMPERATURE
REMARK 900 RELATED ID: 1IIM RELATED DB: PDB
REMARK 900 A DOUBLE MUTANT OF TRANSTHYRETIN
REMARK 900 RELATED ID: 1IIN RELATED DB: PDB
REMARK 900 A DOUBLE MUTANT OF TRANSTHYRETIN
DBREF 1IIK A 1 127 UNP P02766 TTHY_HUMAN 21 147
DBREF 1IIK B 1 127 UNP P02766 TTHY_HUMAN 21 147
SEQADV 1IIK CYS A 114 UNP P02766 TYR 134 ENGINEERED MUTATION
SEQADV 1IIK CYS B 114 UNP P02766 TYR 134 ENGINEERED MUTATION
SEQRES 1 A 127 GLY PRO THR GLY THR GLY GLU SER LYS CYS PRO LEU MET
SEQRES 2 A 127 VAL LYS VAL LEU ASP ALA VAL ARG GLY SER PRO ALA ILE
SEQRES 3 A 127 ASN VAL ALA VAL HIS VAL PHE ARG LYS ALA ALA ASP ASP
SEQRES 4 A 127 THR TRP GLU PRO PHE ALA SER GLY LYS THR SER GLU SER
SEQRES 5 A 127 GLY GLU LEU HIS GLY LEU THR THR GLU GLU GLU PHE VAL
SEQRES 6 A 127 GLU GLY ILE TYR LYS VAL GLU ILE ASP THR LYS SER TYR
SEQRES 7 A 127 TRP LYS ALA LEU GLY ILE SER PRO PHE HIS GLU HIS ALA
SEQRES 8 A 127 GLU VAL VAL PHE THR ALA ASN ASP SER GLY PRO ARG ARG
SEQRES 9 A 127 TYR THR ILE ALA ALA LEU LEU SER PRO CYS SER TYR SER
SEQRES 10 A 127 THR THR ALA VAL VAL THR ASN PRO LYS GLU
SEQRES 1 B 127 GLY PRO THR GLY THR GLY GLU SER LYS CYS PRO LEU MET
SEQRES 2 B 127 VAL LYS VAL LEU ASP ALA VAL ARG GLY SER PRO ALA ILE
SEQRES 3 B 127 ASN VAL ALA VAL HIS VAL PHE ARG LYS ALA ALA ASP ASP
SEQRES 4 B 127 THR TRP GLU PRO PHE ALA SER GLY LYS THR SER GLU SER
SEQRES 5 B 127 GLY GLU LEU HIS GLY LEU THR THR GLU GLU GLU PHE VAL
SEQRES 6 B 127 GLU GLY ILE TYR LYS VAL GLU ILE ASP THR LYS SER TYR
SEQRES 7 B 127 TRP LYS ALA LEU GLY ILE SER PRO PHE HIS GLU HIS ALA
SEQRES 8 B 127 GLU VAL VAL PHE THR ALA ASN ASP SER GLY PRO ARG ARG
SEQRES 9 B 127 TYR THR ILE ALA ALA LEU LEU SER PRO CYS SER TYR SER
SEQRES 10 B 127 THR THR ALA VAL VAL THR ASN PRO LYS GLU
HET BME A 901 4
HET BME A 903 4
HET BME A 904 4
HET BME B 902 4
HET BME B 905 4
HET BME B 906 4
HETNAM BME BETA-MERCAPTOETHANOL
FORMUL 3 BME 6(C2 H6 O S)
FORMUL 9 HOH *198(H2 O)
HELIX 1 1 ASP A 74 ALA A 81 1 8
HELIX 2 2 ASP B 74 LEU B 82 1 9
SHEET 1 A 4 TRP A 41 LYS A 48 0
SHEET 2 A 4 ALA A 29 LYS A 35 -1 N VAL A 30 O GLY A 47
SHEET 3 A 4 GLY A 67 ILE A 73 -1 O ILE A 68 N LYS A 35
SHEET 4 A 4 ALA A 91 ALA A 97 -1 O ALA A 91 N ILE A 73
SHEET 1 B 4 TRP B 41 LYS B 48 0
SHEET 2 B 4 ALA B 29 LYS B 35 -1 N VAL B 30 O GLY B 47
SHEET 3 B 4 GLY B 67 ILE B 73 -1 O ILE B 68 N LYS B 35
SHEET 4 B 4 ALA B 91 ALA B 97 -1 O ALA B 91 N ILE B 73
LINK SG CYS A 114 S2 BME A 901 1555 1555 2.00
LINK S2 BME A 903 S2 BME A 904 1555 1555 2.03
LINK C1 BME A 903 C2 BME A 904 1555 2665 1.56
LINK C1 BME A 903 O1 BME A 904 1555 2665 1.37
LINK C2 BME A 903 C1 BME A 904 1555 2665 1.49
LINK C2 BME A 903 S2 BME A 904 1555 2665 1.88
LINK O1 BME A 903 C1 BME A 904 1555 2665 1.45
LINK S2 BME A 903 C2 BME A 904 1555 2665 1.75
LINK C2 BME A 903 C1 BME A 904 2665 1555 1.49
LINK O1 BME A 903 C1 BME A 904 2665 1555 1.45
LINK S2 BME A 903 C2 BME A 904 2665 1555 1.75
LINK C1 BME A 903 C2 BME A 904 2665 1555 1.56
LINK C1 BME A 903 O1 BME A 904 2665 1555 1.37
LINK C2 BME A 903 S2 BME A 904 2665 1555 1.88
LINK SG CYS B 114 S2 BME B 902 1555 1555 1.93
LINK S2 BME B 905 S2 BME B 906 1555 1555 2.03
LINK C1 BME B 905 O1 BME B 906 1555 2665 1.42
LINK C2 BME B 905 C1 BME B 906 1555 2665 1.53
LINK C2 BME B 905 S2 BME B 906 1555 2665 1.72
LINK O1 BME B 905 C1 BME B 906 1555 2665 1.40
LINK S2 BME B 905 C2 BME B 906 1555 2665 1.92
LINK C2 BME B 905 C1 BME B 906 2665 1555 1.53
LINK O1 BME B 905 C1 BME B 906 2665 1555 1.40
LINK S2 BME B 905 C2 BME B 906 2665 1555 1.92
LINK C1 BME B 905 C2 BME B 906 2665 1555 1.51
LINK C1 BME B 905 O1 BME B 906 2665 1555 1.42
LINK C2 BME B 905 S2 BME B 906 2665 1555 1.72
LINK C1 BME B 905 C2 BME B 906 1555 2665 1.51
SITE 1 AC1 6 PHE A 87 CYS A 114 HOH A 959 ARG B 21
SITE 2 AC1 6 ALA B 120 VAL B 122
SITE 1 AC2 5 HOH A 953 PRO B 86 PHE B 87 PRO B 113
SITE 2 AC2 5 CYS B 114
SITE 1 AC3 5 ALA A 108 SER A 117 THR A 118 THR A 119
SITE 2 AC3 5 BME A 904
SITE 1 AC4 5 ALA A 108 SER A 117 THR A 118 THR A 119
SITE 2 AC4 5 BME A 903
SITE 1 AC5 4 SER B 117 THR B 118 THR B 119 BME B 906
SITE 1 AC6 4 SER B 117 THR B 118 THR B 119 BME B 905
CRYST1 43.288 85.288 64.781 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 0.023101 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011725 0.000000 0.00000
SCALE3 0.000000 0.000000 0.015437 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
