HEADER ISOMERASE(INTRAMOLECULAR OXIDOREDUCTASE)28-FEB-94 1TPF
TITLE COMPARISON OF THE STRUCTURES AND THE CRYSTAL CONTACTS OF
TITLE 2 TRYPANOSOMAL TRIOSEPHOSPHATE ISOMERASE IN FOUR DIFFERENT
TITLE 3 CRYSTAL FORMS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TRIOSEPHOSPHATE ISOMERASE;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 5.3.1.1;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: TRYPANOSOMA BRUCEI BRUCEI;
SOURCE 3 ORGANISM_TAXID: 5702;
SOURCE 4 STRAIN: BRUCEI
KEYWDS ISOMERASE(INTRAMOLECULAR OXIDOREDUCTASE)
EXPDTA X-RAY DIFFRACTION
AUTHOR K.V.RADHA KISHAN,J.PH.ZEELEN,R.K.WIERENGA
REVDAT 2 24-FEB-09 1TPF 1 VERSN
REVDAT 1 31-MAY-94 1TPF 0
JRNL AUTH K.V.KISHAN,J.P.ZEELEN,M.E.NOBLE,T.V.BORCHERT,
JRNL AUTH 2 R.K.WIERENGA
JRNL TITL COMPARISON OF THE STRUCTURES AND THE CRYSTAL
JRNL TITL 2 CONTACTS OF TRYPANOSOMAL TRIOSEPHOSPHATE ISOMERASE
JRNL TITL 3 IN FOUR DIFFERENT CRYSTAL FORMS.
JRNL REF PROTEIN SCI. V. 3 779 1994
JRNL REFN ISSN 0961-8368
JRNL PMID 8061607
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 1.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : TNT, X-PLOR
REMARK 3 AUTHORS : TRONRUD,TEN EYCK,MATTHEWS
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 32.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 36936
REMARK 3
REMARK 3 USING DATA ABOVE SIGMA CUTOFF.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING + TEST SET) : 0.199
REMARK 3 R VALUE (WORKING SET) : 0.199
REMARK 3 FREE R VALUE : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : NULL
REMARK 3
REMARK 3 USING ALL DATA, NO SIGMA CUTOFF.
REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : NULL
REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : NULL
REMARK 3 FREE R VALUE (NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : NULL
REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3774
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 16
REMARK 3 SOLVENT ATOMS : 158
REMARK 3
REMARK 3 WILSON B VALUE (FROM FCALC, A**2) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. RMS WEIGHT COUNT
REMARK 3 BOND LENGTHS (A) : NULL ; NULL ; NULL
REMARK 3 BOND ANGLES (DEGREES) : NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES (DEGREES) : NULL ; NULL ; NULL
REMARK 3 PSEUDOROTATION ANGLES (DEGREES) : NULL ; NULL ; NULL
REMARK 3 TRIGONAL CARBON PLANES (A) : NULL ; NULL ; NULL
REMARK 3 GENERAL PLANES (A) : NULL ; NULL ; NULL
REMARK 3 ISOTROPIC THERMAL FACTORS (A**2) : NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS (A) : NULL ; NULL ; NULL
REMARK 3
REMARK 3 INCORRECT CHIRAL-CENTERS (COUNT) : 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 RESTRAINT LIBRARIES.
REMARK 3 STEREOCHEMISTRY : NULL
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1TPF COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : NULL
REMARK 200 RADIATION SOURCE : NULL
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : NULL
REMARK 200 WAVELENGTH OR RANGE (A) : NULL
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : NULL
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : NULL
REMARK 200 RESOLUTION RANGE HIGH (A) : NULL
REMARK 200 RESOLUTION RANGE LOW (A) : NULL
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : NULL
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
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: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: X-PLOR
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 53.64
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.65
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,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
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
REMARK 350 TOTAL BURIED SURFACE AREA: 3990 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 19080 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -14.0 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 B 1
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 GLU A 53 CD GLU A 53 OE1 0.068
REMARK 500 GLU A 133 CD GLU A 133 OE1 0.077
REMARK 500 GLU B 77 CD GLU B 77 OE2 0.070
REMARK 500 GLU B 107 CD GLU B 107 OE2 0.070
REMARK 500 GLU B 167 CD GLU B 167 OE2 0.085
REMARK 500 GLU B 241 CD GLU B 241 OE2 0.072
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ASP A 36 CB - CG - OD1 ANGL. DEV. = -7.3 DEGREES
REMARK 500 ASP A 36 CB - CG - OD2 ANGL. DEV. = 6.2 DEGREES
REMARK 500 ASP A 111 CB - CG - OD2 ANGL. DEV. = -5.4 DEGREES
REMARK 500 ALA A 165 N - CA - CB ANGL. DEV. = 8.8 DEGREES
REMARK 500 ARG A 220 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 ASP A 244 CB - CG - OD1 ANGL. DEV. = -6.9 DEGREES
REMARK 500 ASP A 244 CB - CG - OD2 ANGL. DEV. = 6.0 DEGREES
REMARK 500 ASP B 36 CB - CG - OD1 ANGL. DEV. = -7.9 DEGREES
REMARK 500 ASP B 36 CB - CG - OD2 ANGL. DEV. = 7.4 DEGREES
REMARK 500 ASP B 111 CB - CG - OD2 ANGL. DEV. = -6.8 DEGREES
REMARK 500 ALA B 165 N - CA - CB ANGL. DEV. = 9.0 DEGREES
REMARK 500 ASP B 201 CB - CG - OD2 ANGL. DEV. = -5.4 DEGREES
REMARK 500 ARG B 220 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 ARG B 220 NE - CZ - NH2 ANGL. DEV. = -4.3 DEGREES
REMARK 500 ARG B 226 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 ASP B 227 CB - CG - OD2 ANGL. DEV. = -6.2 DEGREES
REMARK 500 ASP B 244 CB - CG - OD1 ANGL. DEV. = -8.2 DEGREES
REMARK 500 ASP B 244 CB - CG - OD2 ANGL. DEV. = 6.7 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
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 13 -151.03 59.72
REMARK 500 ASN A 66 167.41 177.57
REMARK 500 LYS B 3 97.07 34.30
REMARK 500 LYS B 13 -148.74 56.35
REMARK 500 ASN B 66 166.51 176.72
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH B 299 DISTANCE = 6.18 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS A 251
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS A 252
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS B 251
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS B 252
REMARK 999
REMARK 999 SEQUENCE
REMARK 999
REMARK 999 SEQUENCE ADVISORY NOTICE
REMARK 999 DIFFERENCE BETWEEN SWISS-PROT AND PDB SEQUENCE.
REMARK 999
REMARK 999 SWISS-PROT ENTRY NAME: TPIS_TRYBB
REMARK 999
REMARK 999 SWISS-PROT RESIDUE PDB SEQRES
REMARK 999
REMARK 999 NAME NUMBER NAME CHAIN SEQ/INSERT CODE
REMARK 999 ARG 203 ALA A 203
REMARK 999 ARG 203 ALA B 203
REMARK 999
REMARK 999 THE DISCREPANCY WITH THE AMINO ACID SEQUENCE AT 203 IS DUE
REMARK 999 TO THE CORRECT IDENTIFICATION OF THE SEQUENCE AFTER THE
REMARK 999 TPIS_TRYBB WAS SUBMITTED (REF: EUR. J. BIOCHEM., (1994),
REMARK 999 211, 703-710) ACCESSION NUMBER; EMBL: X03921, ID: TBTIM.
DBREF 1TPF A 1 250 UNP P04789 TPIS_TRYBB 1 250
DBREF 1TPF B 1 250 UNP P04789 TPIS_TRYBB 1 250
SEQRES 1 A 250 MET SER LYS PRO GLN PRO ILE ALA ALA ALA ASN TRP LYS
SEQRES 2 A 250 CYS ASN GLY SER GLN GLN SER LEU SER GLU LEU ILE ASP
SEQRES 3 A 250 LEU PHE ASN SER THR SER ILE ASN HIS ASP VAL GLN CYS
SEQRES 4 A 250 VAL VAL ALA SER THR PHE VAL HIS LEU ALA MET THR LYS
SEQRES 5 A 250 GLU ARG LEU SER HIS PRO LYS PHE VAL ILE ALA ALA GLN
SEQRES 6 A 250 ASN ALA ILE ALA LYS SER GLY ALA PHE THR GLY GLU VAL
SEQRES 7 A 250 SER LEU PRO ILE LEU LYS ASP PHE GLY VAL ASN TRP ILE
SEQRES 8 A 250 VAL LEU GLY HIS SER GLU ARG ARG ALA TYR TYR GLY GLU
SEQRES 9 A 250 THR ASN GLU ILE VAL ALA ASP LYS VAL ALA ALA ALA VAL
SEQRES 10 A 250 ALA SER GLY PHE MET VAL ILE ALA CYS ILE GLY GLU THR
SEQRES 11 A 250 LEU GLN GLU ARG GLU SER GLY ARG THR ALA VAL VAL VAL
SEQRES 12 A 250 LEU THR GLN ILE ALA ALA ILE ALA LYS LYS LEU LYS LYS
SEQRES 13 A 250 ALA ASP TRP ALA LYS VAL VAL ILE ALA TYR GLU PRO VAL
SEQRES 14 A 250 TRP ALA ILE GLY THR GLY LYS VAL ALA THR PRO GLN GLN
SEQRES 15 A 250 ALA GLN GLU ALA HIS ALA LEU ILE ARG SER TRP VAL SER
SEQRES 16 A 250 SER LYS ILE GLY ALA ASP VAL ALA GLY GLU LEU ARG ILE
SEQRES 17 A 250 LEU TYR GLY GLY SER VAL ASN GLY LYS ASN ALA ARG THR
SEQRES 18 A 250 LEU TYR GLN GLN ARG ASP VAL ASN GLY PHE LEU VAL GLY
SEQRES 19 A 250 GLY ALA SER LEU LYS PRO GLU PHE VAL ASP ILE ILE LYS
SEQRES 20 A 250 ALA THR GLN
SEQRES 1 B 250 MET SER LYS PRO GLN PRO ILE ALA ALA ALA ASN TRP LYS
SEQRES 2 B 250 CYS ASN GLY SER GLN GLN SER LEU SER GLU LEU ILE ASP
SEQRES 3 B 250 LEU PHE ASN SER THR SER ILE ASN HIS ASP VAL GLN CYS
SEQRES 4 B 250 VAL VAL ALA SER THR PHE VAL HIS LEU ALA MET THR LYS
SEQRES 5 B 250 GLU ARG LEU SER HIS PRO LYS PHE VAL ILE ALA ALA GLN
SEQRES 6 B 250 ASN ALA ILE ALA LYS SER GLY ALA PHE THR GLY GLU VAL
SEQRES 7 B 250 SER LEU PRO ILE LEU LYS ASP PHE GLY VAL ASN TRP ILE
SEQRES 8 B 250 VAL LEU GLY HIS SER GLU ARG ARG ALA TYR TYR GLY GLU
SEQRES 9 B 250 THR ASN GLU ILE VAL ALA ASP LYS VAL ALA ALA ALA VAL
SEQRES 10 B 250 ALA SER GLY PHE MET VAL ILE ALA CYS ILE GLY GLU THR
SEQRES 11 B 250 LEU GLN GLU ARG GLU SER GLY ARG THR ALA VAL VAL VAL
SEQRES 12 B 250 LEU THR GLN ILE ALA ALA ILE ALA LYS LYS LEU LYS LYS
SEQRES 13 B 250 ALA ASP TRP ALA LYS VAL VAL ILE ALA TYR GLU PRO VAL
SEQRES 14 B 250 TRP ALA ILE GLY THR GLY LYS VAL ALA THR PRO GLN GLN
SEQRES 15 B 250 ALA GLN GLU ALA HIS ALA LEU ILE ARG SER TRP VAL SER
SEQRES 16 B 250 SER LYS ILE GLY ALA ASP VAL ALA GLY GLU LEU ARG ILE
SEQRES 17 B 250 LEU TYR GLY GLY SER VAL ASN GLY LYS ASN ALA ARG THR
SEQRES 18 B 250 LEU TYR GLN GLN ARG ASP VAL ASN GLY PHE LEU VAL GLY
SEQRES 19 B 250 GLY ALA SER LEU LYS PRO GLU PHE VAL ASP ILE ILE LYS
SEQRES 20 B 250 ALA THR GLN
HET DMS A 251 4
HET DMS A 252 4
HET DMS B 251 4
HET DMS B 252 4
HETNAM DMS DIMETHYL SULFOXIDE
FORMUL 3 DMS 4(C2 H6 O S)
FORMUL 7 HOH *158(H2 O)
HELIX 1 1 SER A 17 SER A 30 1 14
HELIX 2 2 THR A 44 VAL A 46 5 3
HELIX 3 3 HIS A 47 LEU A 55 1 9
HELIX 4 4 SER A 79 PHE A 86 1 8
HELIX 5 5 HIS A 95 TYR A 102 1 8
HELIX 6 6 THR A 105 SER A 119 1 15
HELIX 7 7 THR A 130 SER A 136 1 7
HELIX 8 8 ARG A 138 LYS A 153 1 16
HELIX 9 9 LEU A 154 LEU A 154 5 1
HELIX 10 10 LYS A 155 ALA A 160 5 6
HELIX 11 11 PRO A 168 ILE A 172 5 5
HELIX 12 12 THR A 179 ILE A 198 1 20
HELIX 13 13 GLY A 199 LEU A 206 1 8
HELIX 14 14 ASN A 218 GLN A 225 1 8
HELIX 15 15 GLY A 234 PRO A 240 5 7
HELIX 16 16 GLU A 241 ALA A 248 1 8
HELIX 17 17 SER B 17 SER B 30 1 14
HELIX 18 18 THR B 44 VAL B 46 5 3
HELIX 19 19 HIS B 47 LEU B 55 1 9
HELIX 20 20 SER B 79 PHE B 86 1 8
HELIX 21 21 HIS B 95 TYR B 102 1 8
HELIX 22 22 THR B 105 SER B 119 1 15
HELIX 23 23 THR B 130 SER B 136 1 7
HELIX 24 24 ARG B 138 LYS B 153 1 16
HELIX 25 25 LEU B 154 LEU B 154 5 1
HELIX 26 26 LYS B 155 ALA B 160 5 6
HELIX 27 27 PRO B 168 ILE B 172 5 5
HELIX 28 28 THR B 179 ILE B 198 1 20
HELIX 29 29 GLY B 199 LEU B 206 1 8
HELIX 30 30 ASN B 218 GLN B 225 1 8
HELIX 31 31 GLY B 234 PRO B 240 5 7
HELIX 32 32 GLU B 241 ALA B 248 1 8
SHEET 1 A 9 ILE A 7 ASN A 11 0
SHEET 2 A 9 GLN A 38 ALA A 42 1 O GLN A 38 N ALA A 8
SHEET 3 A 9 PHE A 60 ALA A 64 1 O VAL A 61 N VAL A 41
SHEET 4 A 9 TRP A 90 LEU A 93 1 O TRP A 90 N ALA A 64
SHEET 5 A 9 MET A 122 ILE A 127 1 O MET A 122 N ILE A 91
SHEET 6 A 9 VAL A 162 TYR A 166 1 O VAL A 163 N ALA A 125
SHEET 7 A 9 ARG A 207 TYR A 210 1 O ARG A 207 N ILE A 164
SHEET 8 A 9 GLY A 230 VAL A 233 1 O GLY A 230 N TYR A 210
SHEET 9 A 9 ILE A 7 ASN A 11 1 O ILE A 7 N PHE A 231
SHEET 1 B 9 ILE B 7 ASN B 11 0
SHEET 2 B 9 GLN B 38 ALA B 42 1 O GLN B 38 N ALA B 8
SHEET 3 B 9 PHE B 60 ALA B 64 1 O VAL B 61 N VAL B 41
SHEET 4 B 9 TRP B 90 LEU B 93 1 O TRP B 90 N ALA B 64
SHEET 5 B 9 MET B 122 ILE B 127 1 O MET B 122 N ILE B 91
SHEET 6 B 9 VAL B 162 TYR B 166 1 N VAL B 163 O VAL B 123
SHEET 7 B 9 ARG B 207 TYR B 210 1 O ARG B 207 N ILE B 164
SHEET 8 B 9 GLY B 230 VAL B 233 1 O GLY B 230 N TYR B 210
SHEET 9 B 9 ILE B 7 ASN B 11 1 O ILE B 7 N PHE B 231
SITE 1 AC1 2 GLY A 235 HOH A 259
SITE 1 AC2 4 SER A 96 ALA A 100 TYR A 101 HOH A 263
SITE 1 AC3 4 GLY B 234 GLY B 235 HOH B 257 HOH B 296
SITE 1 AC4 3 SER B 96 GLU B 97 ALA B 100
CRYST1 48.080 53.450 64.710 92.27 74.63 116.74 P 1 2
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 0.020799 0.010479 -0.006715 0.00000
SCALE2 0.000000 0.020949 -0.001946 0.00000
SCALE3 0.000000 0.000000 0.016096 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
END
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