HEADER TRIOSEPHOSPHATE ISOMERASE 06-APR-99 1CI1
TITLE CRYSTAL STRUCTURE OF TRIOSEPHOSPHATE ISOMERASE FROM TRYPANOSOMA CRUZI
TITLE 2 IN HEXANE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN (TRIOSEPHOSPHATE ISOMERASE);
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: TIM;
COMPND 5 EC: 5.3.1.1;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: TRYPANOSOMA CRUZI;
SOURCE 3 ORGANISM_TAXID: 5693;
SOURCE 4 STRAIN: MEXICAN NINOA STRAIN;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL23(DE3);
SOURCE 8 EXPRESSION_SYSTEM_CELLULAR_LOCATION: CYTOPLASM;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET23A
KEYWDS TRIOSEPHOSPHATE ISOMERASE, TRYPANOSOMA CRUZI, ORGANIC SOLVENT,
KEYWDS 2 HEXANE, OLIGOMERIC PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR X.-G.GAO,E.MALDONDO,R.PEREZ-MONTFORT,M.T.DE GOMEZ-PUYOU,A.GOMEZ-
AUTHOR 2 PUYOU,A.RODRIGUEZ-ROMERO
REVDAT 6 09-AUG-23 1CI1 1 REMARK
REVDAT 5 20-NOV-19 1CI1 1 JRNL
REVDAT 4 13-JUL-11 1CI1 1 VERSN
REVDAT 3 24-FEB-09 1CI1 1 VERSN
REVDAT 2 01-APR-03 1CI1 1 JRNL
REVDAT 1 01-SEP-99 1CI1 0
JRNL AUTH X.G.GAO,E.MALDONADO,R.PEREZ-MONTFORT,G.GARZA-RAMOS,
JRNL AUTH 2 M.T.DE GOMEZ-PUYOU,A.GOMEZ-PUYOU,A.RODRIGUEZ-ROMERO
JRNL TITL CRYSTAL STRUCTURE OF TRIOSEPHOSPHATE ISOMERASE FROM
JRNL TITL 2 TRYPANOSOMA CRUZI IN HEXANE.
JRNL REF PROC.NATL.ACAD.SCI.USA V. 96 10062 1999
JRNL REFN ISSN 0027-8424
JRNL PMID 10468562
JRNL DOI 10.1073/PNAS.96.18.10062
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH E.MALDONADO,M.SORIANO-GARCIA,A.MORENO,N.CABRERA,
REMARK 1 AUTH 2 G.GARZA-RAMOS,M.DE GOMEZ-PUYOU,A.GOMEZ-PUYOU,
REMARK 1 AUTH 3 R.PEREZ-MONTFORT
REMARK 1 TITL DIFFERENCES IN THE INTERSUBUNIT CONTACTS IN TRIOSEPHOSPHATE
REMARK 1 TITL 2 ISOMERASE FROM TWO CLOSELY RELATED PATHOGENIC TRYPANOSOMES.
REMARK 1 REF J.MOL.BIOL. V. 283 193 1998
REMARK 1 REFN ISSN 0022-2836
REMARK 1 PMID 9761683
REMARK 1 DOI 10.1006/JMBI.1998.2094
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.851(ONLINE)
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 5.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 10000000.000
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0010
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 82.4
REMARK 3 NUMBER OF REFLECTIONS : 26956
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) : 0.181
REMARK 3 FREE R VALUE : 0.239
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2696
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.005
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.12
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 65.90
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 3197
REMARK 3 BIN R VALUE (WORKING SET) : 0.3090
REMARK 3 BIN FREE R VALUE : 0.3580
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 9.90
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 350
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.019
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3818
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 18
REMARK 3 SOLVENT ATOMS : 236
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 18.10
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 25.60
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.00000
REMARK 3 B22 (A**2) : 0.00000
REMARK 3 B33 (A**2) : 0.00000
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) : 0.21
REMARK 3 ESD FROM SIGMAA (A) : 0.32
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.27
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.35
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.006
REMARK 3 BOND ANGLES (DEGREES) : 1.200
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 25.00
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.640
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 1.560 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.210 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 3.000 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 4.580 ; 2.500
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 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : PARAM.HEX
REMARK 3 PARAMETER FILE 3 : NULL
REMARK 3 PARAMETER FILE 4 : NULL
REMARK 3 TOPOLOGY FILE 1 : TOPHCSDX.PRO
REMARK 3 TOPOLOGY FILE 2 : TOP.HEX
REMARK 3 TOPOLOGY FILE 3 : TOPH19.SOL
REMARK 3 TOPOLOGY FILE 4 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1CI1 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-APR-99.
REMARK 100 THE DEPOSITION ID IS D_1000000798.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 21-APR-98
REMARK 200 TEMPERATURE (KELVIN) : 291
REMARK 200 PH : 7.5
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 : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IIC
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 31766
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.950
REMARK 200 RESOLUTION RANGE LOW (A) : 25.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 84.4
REMARK 200 DATA REDUNDANCY : 3.600
REMARK 200 R MERGE (I) : 0.11600
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 4.6400
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) : 2.11
REMARK 200 COMPLETENESS FOR SHELL (%) : 65.5
REMARK 200 DATA REDUNDANCY IN SHELL : 3.40
REMARK 200 R MERGE FOR SHELL (I) : 0.11300
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.100
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: OTHER
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: PDB ENTRY 1TCD
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 47.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.32
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN WAS CRYSTALLIZED AT ROOM
REMARK 280 TEMPERATUTE BY VAPER DIFFUSION FROM 0.1 M NA HEPES PH7.5, 2%(V/V)
REMARK 280 PEG400 AND 2.0 M AMMONIUM SULFATE, THEN SOAKED IN ANHYDROUS N-
REMARK 280 HEXANE. , VAPOR DIFFUSION
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
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 21.82800
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 74.60550
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 38.82500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 74.60550
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 21.82800
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 38.82500
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,PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 3730 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 19380 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -11.0 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 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 MET A 1
REMARK 465 ALA A 2
REMARK 465 SER A 3
REMARK 465 MET B 1
REMARK 465 ALA B 2
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 LYS A 14 -147.16 51.49
REMARK 500 LYS A 177 73.05 -103.03
REMARK 500 PRO A 241 -8.11 -55.41
REMARK 500 LYS B 14 -149.80 50.91
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: CS
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: CATALYTIC SITE
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEX B 261
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEX B 262
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEX B 263
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE FIRST 3 N-TERMINAL RESIDUE WERE NOT
REMARK 999 BUILT INTO THE MODEL A AS THEY WERE NOT
REMARK 999 SEEEN IN THE DENSITY MAPS
REMARK 999 THE FIRST 2 N-TERMINAL RESIDUE WERE NOT
REMARK 999 BUILT INTO THE MODEL B AS THEY WERE NOT
REMARK 999 SEEN IN THE DENSITY MAPS
DBREF 1CI1 A 1 251 UNP P52270 TPIS_TRYCR 1 251
DBREF 1CI1 B 1 251 UNP P52270 TPIS_TRYCR 1 251
SEQRES 1 A 251 MET ALA SER LYS PRO GLN PRO ILE ALA ALA ALA ASN TRP
SEQRES 2 A 251 LYS CYS ASN GLY SER GLU SER LEU LEU VAL PRO LEU ILE
SEQRES 3 A 251 GLU THR LEU ASN ALA ALA THR PHE ASP HIS ASP VAL GLN
SEQRES 4 A 251 CYS VAL VAL ALA PRO THR PHE LEU HIS ILE PRO MET THR
SEQRES 5 A 251 LYS ALA ARG LEU THR ASN PRO LYS PHE GLN ILE ALA ALA
SEQRES 6 A 251 GLN ASN ALA ILE THR ARG SER GLY ALA PHE THR GLY GLU
SEQRES 7 A 251 VAL SER LEU GLN ILE LEU LYS ASP TYR GLY ILE SER TRP
SEQRES 8 A 251 VAL VAL LEU GLY HIS SER GLU ARG ARG LEU TYR TYR GLY
SEQRES 9 A 251 GLU THR ASN GLU ILE VAL ALA GLU LYS VAL ALA GLN ALA
SEQRES 10 A 251 CYS ALA ALA GLY PHE HIS VAL ILE VAL CYS VAL GLY GLU
SEQRES 11 A 251 THR ASN GLU GLU ARG GLU ALA GLY ARG THR ALA ALA VAL
SEQRES 12 A 251 VAL LEU THR GLN LEU ALA ALA VAL ALA GLN LYS LEU SER
SEQRES 13 A 251 LYS GLU ALA TRP SER ARG VAL VAL ILE ALA TYR GLU PRO
SEQRES 14 A 251 VAL TRP ALA ILE GLY THR GLY LYS VAL ALA THR PRO GLN
SEQRES 15 A 251 GLN ALA GLN GLU VAL HIS GLU LEU LEU ARG ARG TRP VAL
SEQRES 16 A 251 ARG SER LYS LEU GLY THR ASP ILE ALA ALA GLN LEU ARG
SEQRES 17 A 251 ILE LEU TYR GLY GLY SER VAL THR ALA LYS ASN ALA ARG
SEQRES 18 A 251 THR LEU TYR GLN MET ARG ASP ILE ASN GLY PHE LEU VAL
SEQRES 19 A 251 GLY GLY ALA SER LEU LYS PRO GLU PHE VAL GLU ILE ILE
SEQRES 20 A 251 GLU ALA THR LYS
SEQRES 1 B 251 MET ALA SER LYS PRO GLN PRO ILE ALA ALA ALA ASN TRP
SEQRES 2 B 251 LYS CYS ASN GLY SER GLU SER LEU LEU VAL PRO LEU ILE
SEQRES 3 B 251 GLU THR LEU ASN ALA ALA THR PHE ASP HIS ASP VAL GLN
SEQRES 4 B 251 CYS VAL VAL ALA PRO THR PHE LEU HIS ILE PRO MET THR
SEQRES 5 B 251 LYS ALA ARG LEU THR ASN PRO LYS PHE GLN ILE ALA ALA
SEQRES 6 B 251 GLN ASN ALA ILE THR ARG SER GLY ALA PHE THR GLY GLU
SEQRES 7 B 251 VAL SER LEU GLN ILE LEU LYS ASP TYR GLY ILE SER TRP
SEQRES 8 B 251 VAL VAL LEU GLY HIS SER GLU ARG ARG LEU TYR TYR GLY
SEQRES 9 B 251 GLU THR ASN GLU ILE VAL ALA GLU LYS VAL ALA GLN ALA
SEQRES 10 B 251 CYS ALA ALA GLY PHE HIS VAL ILE VAL CYS VAL GLY GLU
SEQRES 11 B 251 THR ASN GLU GLU ARG GLU ALA GLY ARG THR ALA ALA VAL
SEQRES 12 B 251 VAL LEU THR GLN LEU ALA ALA VAL ALA GLN LYS LEU SER
SEQRES 13 B 251 LYS GLU ALA TRP SER ARG VAL VAL ILE ALA TYR GLU PRO
SEQRES 14 B 251 VAL TRP ALA ILE GLY THR GLY LYS VAL ALA THR PRO GLN
SEQRES 15 B 251 GLN ALA GLN GLU VAL HIS GLU LEU LEU ARG ARG TRP VAL
SEQRES 16 B 251 ARG SER LYS LEU GLY THR ASP ILE ALA ALA GLN LEU ARG
SEQRES 17 B 251 ILE LEU TYR GLY GLY SER VAL THR ALA LYS ASN ALA ARG
SEQRES 18 B 251 THR LEU TYR GLN MET ARG ASP ILE ASN GLY PHE LEU VAL
SEQRES 19 B 251 GLY GLY ALA SER LEU LYS PRO GLU PHE VAL GLU ILE ILE
SEQRES 20 B 251 GLU ALA THR LYS
HET HEX B 261 6
HET HEX B 262 6
HET HEX B 263 6
HETNAM HEX HEXANE
FORMUL 3 HEX 3(C6 H14)
FORMUL 6 HOH *236(H2 O)
HELIX 1 1 GLU A 19 ALA A 31 1 13
HELIX 2 2 PHE A 46 ARG A 55 1 10
HELIX 3 3 LEU A 81 ASP A 86 1 6
HELIX 4 4 SER A 97 TYR A 102 1 6
HELIX 5 5 ASN A 107 ALA A 120 1 14
HELIX 6 6 ASN A 132 GLU A 136 1 5
HELIX 7 7 THR A 140 LYS A 154 1 15
HELIX 8 8 LYS A 157 ARG A 162 5 6
HELIX 9 9 VAL A 170 ALA A 172 5 3
HELIX 10 10 PRO A 181 LEU A 199 1 19
HELIX 11 11 THR A 201 GLN A 206 1 6
HELIX 12 12 ALA A 220 GLN A 225 1 6
HELIX 13 13 GLY A 236 LEU A 239 5 4
HELIX 14 14 PRO A 241 GLU A 248 5 8
HELIX 15 15 GLU B 19 ALA B 31 1 13
HELIX 16 16 PHE B 46 ARG B 55 1 10
HELIX 17 17 LEU B 81 ASP B 86 1 6
HELIX 18 18 SER B 97 TYR B 102 1 6
HELIX 19 19 ASN B 107 ALA B 119 1 13
HELIX 20 20 ASN B 132 GLU B 136 1 5
HELIX 21 21 THR B 140 LYS B 154 1 15
HELIX 22 22 LYS B 157 ARG B 162 5 6
HELIX 23 23 VAL B 170 THR B 175 1 6
HELIX 24 24 PRO B 181 LYS B 198 1 18
HELIX 25 25 THR B 201 GLN B 206 1 6
HELIX 26 26 ALA B 220 TYR B 224 1 5
HELIX 27 27 GLY B 236 LEU B 239 5 4
HELIX 28 28 PRO B 241 GLU B 248 5 8
SHEET 1 A 4 GLY A 231 VAL A 234 0
SHEET 2 A 4 PRO A 7 ASN A 12 1 N ILE A 8 O PHE A 232
SHEET 3 A 4 VAL A 38 ALA A 43 1 N GLN A 39 O PRO A 7
SHEET 4 A 4 PHE A 61 ALA A 64 1 N GLN A 62 O CYS A 40
SHEET 1 B 4 TRP A 91 LEU A 94 0
SHEET 2 B 4 HIS A 123 VAL A 128 1 N HIS A 123 O VAL A 92
SHEET 3 B 4 VAL A 163 GLU A 168 1 N VAL A 164 O VAL A 124
SHEET 4 B 4 ARG A 208 GLY A 212 1 N ARG A 208 O ILE A 165
SHEET 1 C 4 GLY B 231 VAL B 234 0
SHEET 2 C 4 PRO B 7 ASN B 12 1 N ILE B 8 O PHE B 232
SHEET 3 C 4 VAL B 38 ALA B 43 1 N GLN B 39 O PRO B 7
SHEET 4 C 4 PHE B 61 ILE B 63 1 N GLN B 62 O CYS B 40
SHEET 1 D 4 TRP B 91 LEU B 94 0
SHEET 2 D 4 HIS B 123 VAL B 128 1 N HIS B 123 O VAL B 92
SHEET 3 D 4 VAL B 163 TYR B 167 1 N VAL B 164 O VAL B 124
SHEET 4 D 4 ARG B 208 TYR B 211 1 N ARG B 208 O ILE B 165
SITE 1 CS 8 ASN A 12 LYS A 14 HIS A 96 GLU A 168
SITE 2 CS 8 ASN B 12 LYS B 14 HIS B 96 GLU B 168
SITE 1 AC1 3 ARG B 135 THR B 140 GLU B 186
SITE 1 AC2 8 ILE A 69 TYR A 103 GLY A 104 ILE A 109
SITE 2 AC2 8 LYS A 113 HOH A 289 TYR B 102 TYR B 103
SITE 1 AC3 3 PHE A 75 ARG A 139 TYR B 103
CRYST1 43.656 77.650 149.211 90.00 90.00 90.00 P 21 21 21 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 0.022906 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012878 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006702 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
