HEADER INTRAMOLECULAR OXIDOREDUCTASE 12-OCT-92 1TRE
TITLE THE STRUCTURE OF TRIOSEPHOSPHATE ISOMERASE FROM ESCHERICHIA COLI
TITLE 2 DETERMINED AT 2.6 ANGSTROM RESOLUTION
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: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562
KEYWDS INTRAMOLECULAR OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.E.M.NOBLE,R.K.WIERENGA
REVDAT 5 14-FEB-24 1TRE 1 REMARK
REVDAT 4 14-AUG-19 1TRE 1 REMARK
REVDAT 3 17-JUL-19 1TRE 1 REMARK
REVDAT 2 24-FEB-09 1TRE 1 VERSN
REVDAT 1 31-OCT-93 1TRE 0
JRNL AUTH M.E.NOBLE,J.P.ZEELEN,R.K.WIERENGA,V.MAINFROID,K.GORAJ,
JRNL AUTH 2 A.C.GOHIMONT,J.A.MARTIAL
JRNL TITL STRUCTURE OF TRIOSEPHOSPHATE ISOMERASE FROM ESCHERICHIA COLI
JRNL TITL 2 DETERMINED AT 2.6 A RESOLUTION.
JRNL REF ACTA CRYSTALLOGR.,SECT.D V. 49 403 1993
JRNL REFN ISSN 0907-4449
JRNL PMID 15299515
JRNL DOI 10.1107/S0907444993002628
REMARK 2
REMARK 2 RESOLUTION. 2.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : TNT
REMARK 3 AUTHORS : TRONRUD,TEN EYCK,MATTHEWS
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : NULL
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : NULL
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) : 0.119
REMARK 3 R VALUE (WORKING SET) : 0.119
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 : 3771
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 172
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 1TRE COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000176801.
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) : N
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 : IMAGE PLATE
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 (%): 44.53
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.22
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
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 33.84500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 75.65500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 23.39000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 75.65500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 33.84500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 23.39000
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: TIM IS A DIMERIC ENZYME. THERE IS ONE DIMER IN THE
REMARK 300 ASYMMETRIC UNIT. CHAIN A CONTAINS RESIDUES 3 - 257 AND
REMARK 300 CHAIN B CONTAINS RESIDUES 3 - 255.
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: 3290 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 19520 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -15.0 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 GLN B 256
REMARK 465 ALA B 257
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 23 CD GLU A 23 OE1 0.070
REMARK 500 GLU A 57 CD GLU A 57 OE1 0.070
REMARK 500 GLU A 109 CD GLU A 109 OE1 0.081
REMARK 500 GLU A 120 CD GLU A 120 OE1 0.076
REMARK 500 GLU A 131 CD GLU A 131 OE1 0.078
REMARK 500 GLU A 169 CD GLU A 169 OE2 0.073
REMARK 500 GLU A 205 CD GLU A 205 OE1 0.072
REMARK 500 GLU A 222 CD GLU A 222 OE1 0.072
REMARK 500 GLU B 23 CD GLU B 23 OE1 0.071
REMARK 500 GLU B 31 CD GLU B 31 OE1 0.073
REMARK 500 GLU B 46 CD GLU B 46 OE2 0.086
REMARK 500 GLU B 55 CD GLU B 55 OE2 0.067
REMARK 500 GLU B 106 CD GLU B 106 OE2 0.073
REMARK 500 GLU B 109 CD GLU B 109 OE1 0.082
REMARK 500 GLU B 120 CD GLU B 120 OE1 0.081
REMARK 500 GLU B 135 CD GLU B 135 OE1 0.084
REMARK 500 GLU B 137 CD GLU B 137 OE2 0.072
REMARK 500 GLU B 142 CD GLU B 142 OE2 0.072
REMARK 500 GLU B 162 CD GLU B 162 OE1 0.066
REMARK 500 GLU B 205 CD GLU B 205 OE1 0.082
REMARK 500 GLU B 222 CD GLU B 222 OE2 0.069
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 ARG A 18 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 TYR A 48 CB - CG - CD1 ANGL. DEV. = -3.7 DEGREES
REMARK 500 VAL A 68 CB - CA - C ANGL. DEV. = -11.7 DEGREES
REMARK 500 ARG A 101 CD - NE - CZ ANGL. DEV. = 8.8 DEGREES
REMARK 500 ARG A 101 NE - CZ - NH1 ANGL. DEV. = 7.7 DEGREES
REMARK 500 ARG A 101 NE - CZ - NH2 ANGL. DEV. = -5.8 DEGREES
REMARK 500 ASP A 150 CB - CG - OD2 ANGL. DEV. = -7.0 DEGREES
REMARK 500 ASP A 194 CB - CG - OD1 ANGL. DEV. = -6.0 DEGREES
REMARK 500 ASP A 194 CB - CG - OD2 ANGL. DEV. = 5.5 DEGREES
REMARK 500 ASP A 200 CB - CG - OD1 ANGL. DEV. = 6.6 DEGREES
REMARK 500 ASP A 228 CB - CG - OD1 ANGL. DEV. = -5.8 DEGREES
REMARK 500 ASP A 230 CB - CG - OD1 ANGL. DEV. = 5.6 DEGREES
REMARK 500 ASP A 230 CB - CG - OD2 ANGL. DEV. = -8.3 DEGREES
REMARK 500 ARG B 4 NE - CZ - NH1 ANGL. DEV. = -3.5 DEGREES
REMARK 500 ASP B 108 CB - CG - OD1 ANGL. DEV. = 7.3 DEGREES
REMARK 500 LEU B 127 CA - C - N ANGL. DEV. = -13.4 DEGREES
REMARK 500 LEU B 127 O - C - N ANGL. DEV. = 12.1 DEGREES
REMARK 500 ARG B 147 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 ASP B 150 CB - CG - OD2 ANGL. DEV. = -6.1 DEGREES
REMARK 500 ALA B 151 CB - CA - C ANGL. DEV. = 9.6 DEGREES
REMARK 500 ASP B 194 CB - CG - OD1 ANGL. DEV. = 5.8 DEGREES
REMARK 500 ASP B 194 CB - CG - OD2 ANGL. DEV. = -7.1 DEGREES
REMARK 500 ASP B 200 CB - CG - OD1 ANGL. DEV. = 5.7 DEGREES
REMARK 500 ASP B 200 CB - CG - OD2 ANGL. DEV. = -6.4 DEGREES
REMARK 500 ASP B 228 CB - CG - OD1 ANGL. DEV. = -5.4 DEGREES
REMARK 500 ASP B 230 CB - CG - OD1 ANGL. DEV. = -7.6 DEGREES
REMARK 500 ASP B 230 CB - CG - OD2 ANGL. DEV. = 6.8 DEGREES
REMARK 500 ASP B 242 CB - CG - OD1 ANGL. DEV. = -7.3 DEGREES
REMARK 500 ASP B 242 CB - CG - OD2 ANGL. DEV. = 6.9 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 -142.26 60.70
REMARK 500 ASN A 67 163.15 174.43
REMARK 500 THR A 141 -72.87 -36.54
REMARK 500 ASP A 200 95.79 -173.46
REMARK 500 LYS B 13 -137.56 46.05
REMARK 500 ALA B 36 -29.47 -161.47
REMARK 500 ASN B 69 -167.47 -107.81
REMARK 500 THR B 141 -76.35 -33.52
REMARK 500 THR B 176 12.71 -151.55
REMARK 500 ALA B 254 -78.73 -76.10
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 ARG A 18 -10.84
REMARK 500 HIS B 97 12.52
REMARK 500 GLN B 121 11.86
REMARK 500 GLU B 162 10.83
REMARK 500 THR B 181 -10.46
REMARK 500 GLN B 186 -10.58
REMARK 500 ALA B 220 -10.00
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1TRE A 3 257 UNP P0A858 TPIS_ECOLI 1 255
DBREF 1TRE B 3 257 UNP P0A858 TPIS_ECOLI 1 255
SEQRES 1 A 255 MET ARG HIS PRO LEU VAL MET GLY ASN TRP LYS LEU ASN
SEQRES 2 A 255 GLY SER ARG HIS MET VAL HIS GLU LEU VAL SER ASN LEU
SEQRES 3 A 255 ARG LYS GLU LEU ALA GLY VAL ALA GLY CYS ALA VAL ALA
SEQRES 4 A 255 ILE ALA PRO PRO GLU MET TYR ILE ASP MET ALA LYS ARG
SEQRES 5 A 255 GLU ALA GLU GLY SER HIS ILE MET LEU GLY ALA GLN ASN
SEQRES 6 A 255 VAL ASN LEU ASN LEU SER GLY ALA PHE THR GLY GLU THR
SEQRES 7 A 255 SER ALA ALA MET LEU LYS ASP ILE GLY ALA GLN TYR ILE
SEQRES 8 A 255 ILE ILE GLY HIS SER GLU ARG ARG THR TYR HIS LYS GLU
SEQRES 9 A 255 SER ASP GLU LEU ILE ALA LYS LYS PHE ALA VAL LEU LYS
SEQRES 10 A 255 GLU GLN GLY LEU THR PRO VAL LEU CYS ILE GLY GLU THR
SEQRES 11 A 255 GLU ALA GLU ASN GLU ALA GLY LYS THR GLU GLU VAL CYS
SEQRES 12 A 255 ALA ARG GLN ILE ASP ALA VAL LEU LYS THR GLN GLY ALA
SEQRES 13 A 255 ALA ALA PHE GLU GLY ALA VAL ILE ALA TYR GLU PRO VAL
SEQRES 14 A 255 TRP ALA ILE GLY THR GLY LYS SER ALA THR PRO ALA GLN
SEQRES 15 A 255 ALA GLN ALA VAL HIS LYS PHE ILE ARG ASP HIS ILE ALA
SEQRES 16 A 255 LYS VAL ASP ALA ASN ILE ALA GLU GLN VAL ILE ILE GLN
SEQRES 17 A 255 TYR GLY GLY SER VAL ASN ALA SER ASN ALA ALA GLU LEU
SEQRES 18 A 255 PHE ALA GLN PRO ASP ILE ASP GLY ALA LEU VAL GLY GLY
SEQRES 19 A 255 ALA SER LEU LYS ALA ASP ALA PHE ALA VAL ILE VAL LYS
SEQRES 20 A 255 ALA ALA GLU ALA ALA LYS GLN ALA
SEQRES 1 B 255 MET ARG HIS PRO LEU VAL MET GLY ASN TRP LYS LEU ASN
SEQRES 2 B 255 GLY SER ARG HIS MET VAL HIS GLU LEU VAL SER ASN LEU
SEQRES 3 B 255 ARG LYS GLU LEU ALA GLY VAL ALA GLY CYS ALA VAL ALA
SEQRES 4 B 255 ILE ALA PRO PRO GLU MET TYR ILE ASP MET ALA LYS ARG
SEQRES 5 B 255 GLU ALA GLU GLY SER HIS ILE MET LEU GLY ALA GLN ASN
SEQRES 6 B 255 VAL ASN LEU ASN LEU SER GLY ALA PHE THR GLY GLU THR
SEQRES 7 B 255 SER ALA ALA MET LEU LYS ASP ILE GLY ALA GLN TYR ILE
SEQRES 8 B 255 ILE ILE GLY HIS SER GLU ARG ARG THR TYR HIS LYS GLU
SEQRES 9 B 255 SER ASP GLU LEU ILE ALA LYS LYS PHE ALA VAL LEU LYS
SEQRES 10 B 255 GLU GLN GLY LEU THR PRO VAL LEU CYS ILE GLY GLU THR
SEQRES 11 B 255 GLU ALA GLU ASN GLU ALA GLY LYS THR GLU GLU VAL CYS
SEQRES 12 B 255 ALA ARG GLN ILE ASP ALA VAL LEU LYS THR GLN GLY ALA
SEQRES 13 B 255 ALA ALA PHE GLU GLY ALA VAL ILE ALA TYR GLU PRO VAL
SEQRES 14 B 255 TRP ALA ILE GLY THR GLY LYS SER ALA THR PRO ALA GLN
SEQRES 15 B 255 ALA GLN ALA VAL HIS LYS PHE ILE ARG ASP HIS ILE ALA
SEQRES 16 B 255 LYS VAL ASP ALA ASN ILE ALA GLU GLN VAL ILE ILE GLN
SEQRES 17 B 255 TYR GLY GLY SER VAL ASN ALA SER ASN ALA ALA GLU LEU
SEQRES 18 B 255 PHE ALA GLN PRO ASP ILE ASP GLY ALA LEU VAL GLY GLY
SEQRES 19 B 255 ALA SER LEU LYS ALA ASP ALA PHE ALA VAL ILE VAL LYS
SEQRES 20 B 255 ALA ALA GLU ALA ALA LYS GLN ALA
FORMUL 3 HOH *172(H2 O)
HELIX 1 1 SER A 17 ALA A 33 1 17
HELIX 2 2 TYR A 48 GLU A 57 1 10
HELIX 3 3 SER A 81 GLY A 89 1 9
HELIX 4 4 HIS A 97 HIS A 104 1 8
HELIX 5 5 SER A 107 GLN A 121 1 15
HELIX 6 6 THR A 132 ALA A 138 1 7
HELIX 7 7 LYS A 140 GLY A 157 1 18
HELIX 8 8 ALA A 158 GLU A 162 5 5
HELIX 9 9 PRO A 170 ILE A 174 5 5
HELIX 10 10 THR A 181 ALA A 201 1 21
HELIX 11 11 ASP A 200 VAL A 207 1 8
HELIX 12 12 ASN A 219 ALA A 225 1 7
HELIX 13 13 GLY A 235 LEU A 239 5 5
HELIX 14 14 LYS A 240 ALA A 254 1 15
HELIX 15 15 SER B 17 LEU B 32 1 16
HELIX 16 16 PRO B 45 MET B 47 5 3
HELIX 17 17 TYR B 48 GLU B 57 1 10
HELIX 18 18 SER B 81 GLY B 89 1 9
HELIX 19 19 HIS B 97 HIS B 104 1 8
HELIX 20 20 SER B 107 GLN B 121 1 15
HELIX 21 21 THR B 132 ALA B 138 1 7
HELIX 22 22 LYS B 140 GLY B 157 1 18
HELIX 23 23 ALA B 158 GLU B 162 5 5
HELIX 24 24 THR B 181 LYS B 198 1 18
HELIX 25 25 ASP B 200 GLU B 205 1 6
HELIX 26 26 ASN B 219 ALA B 225 1 7
HELIX 27 27 GLY B 235 LEU B 239 5 5
HELIX 28 28 LYS B 240 LYS B 255 1 16
SHEET 1 A 9 LEU A 7 ASN A 11 0
SHEET 2 A 9 ALA A 39 ALA A 43 1 O ALA A 39 N VAL A 8
SHEET 3 A 9 ILE A 61 ALA A 65 1 N MET A 62 O VAL A 40
SHEET 4 A 9 TYR A 92 ILE A 95 1 N TYR A 92 O LEU A 63
SHEET 5 A 9 THR A 124 ILE A 129 1 O THR A 124 N ILE A 93
SHEET 6 A 9 VAL A 165 TYR A 168 1 O VAL A 165 N LEU A 127
SHEET 7 A 9 ILE A 208 TYR A 211 1 O ILE A 208 N ILE A 166
SHEET 8 A 9 GLY A 231 VAL A 234 1 O GLY A 231 N TYR A 211
SHEET 9 A 9 LEU A 7 ASN A 11 1 O LEU A 7 N ALA A 232
SHEET 1 B 9 LEU B 7 ASN B 11 0
SHEET 2 B 9 ALA B 39 ALA B 43 1 O ALA B 39 N VAL B 8
SHEET 3 B 9 MET B 62 ALA B 65 1 N MET B 62 O VAL B 40
SHEET 4 B 9 TYR B 92 ILE B 95 1 O TYR B 92 N ALA B 65
SHEET 5 B 9 THR B 124 ILE B 129 1 O THR B 124 N ILE B 93
SHEET 6 B 9 VAL B 165 TYR B 168 1 O VAL B 165 N LEU B 127
SHEET 7 B 9 ILE B 208 TYR B 211 1 O ILE B 208 N ILE B 166
SHEET 8 B 9 GLY B 231 VAL B 234 1 O GLY B 231 N TYR B 211
SHEET 9 B 9 LEU B 7 ASN B 11 1 O LEU B 7 N ALA B 232
CRYST1 67.690 46.780 151.310 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 0.014773 0.000000 0.000000 0.00000
SCALE2 0.000000 0.021377 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006609 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
