HEADER TRANSFERASE 12-FEB-01 1I2Q
TITLE CRYSTAL STRUCTURE OF ESCHERICHIA COLI TRANSALDOLASE B MUTANT T156A
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TRANSALDOLASE B;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 2.2.1.2;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 GENE: TALB;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: LJ110;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PGSJ451
KEYWDS ALPHA-BETA BARREL, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR S.THORELL,J.JIA,G.SCHNEIDER
REVDAT 6 09-AUG-23 1I2Q 1 REMARK
REVDAT 5 27-OCT-21 1I2Q 1 SEQADV
REVDAT 4 04-OCT-17 1I2Q 1 REMARK
REVDAT 3 24-FEB-09 1I2Q 1 VERSN
REVDAT 2 01-APR-03 1I2Q 1 JRNL
REVDAT 1 09-MAY-01 1I2Q 0
JRNL AUTH U.SCHORKEN,S.THORELL,M.SCHURMANN,J.JIA,G.A.SPRENGER,
JRNL AUTH 2 G.SCHNEIDER
JRNL TITL IDENTIFICATION OF CATALYTICALLY IMPORTANT RESIDUES IN THE
JRNL TITL 2 ACTIVE SITE OF ESCHERICHIA COLI TRANSALDOLASE.
JRNL REF EUR.J.BIOCHEM. V. 268 2408 2001
JRNL REFN ISSN 0014-2956
JRNL PMID 11298760
JRNL DOI 10.1046/J.1432-1327.2001.02128.X
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH J.JIA,Y.LINDQVIST,G.SCHNEIDER,U.SCHOERKEN,H.SAHM,
REMARK 1 AUTH 2 G.A.SPRENGER
REMARK 1 TITL CRYSTALLIZATION AND PRELIMINARY X-RAY ANALYSIS OF
REMARK 1 TITL 2 RECOMBINANT TRANSALDOLASE B FROM ESCHERICHIA COLI
REMARK 1 REF ACTA CRYSTALLOGR.,SECT.D V. 52 192 1996
REMARK 1 REFN ISSN 0907-4449
REMARK 1 DOI 10.1107/S0907444995010365
REMARK 1 REFERENCE 2
REMARK 1 AUTH J.JIA,W.HUANG,U.SCHOERKEN,H.SAHM,G.A.SPRENGER,Y.LINDQVIST,
REMARK 1 AUTH 2 G.SCHNEIDER
REMARK 1 TITL CRYSTAL STRUCTURE OF TRANSALDOLASE B FROM ESCHERICHIA COLI
REMARK 1 TITL 2 SUGGESTS A CIRCULAR PERMUTATION OF THE ALPHA/BETA BARREL
REMARK 1 TITL 3 WITHIN THE CLASS I ALDOLASE FAMILY
REMARK 1 REF STRUCTURE V. 4 715 1996
REMARK 1 REFN ISSN 0969-2126
REMARK 1 DOI 10.1016/S0969-2126(96)00077-9
REMARK 1 REFERENCE 3
REMARK 1 AUTH J.JIA,U.SCHOERKEN,Y.LINDQVIST,G.A.SPRENGER,G.SCHNEIDER
REMARK 1 TITL CRYSTAL STRUCTURE OF THE REDUCED SCHIFF-BASE INTERMEDIATE
REMARK 1 TITL 2 COMPLEX OF TRANSALDOLASE B FROM ESCHERICHIA COLI:
REMARK 1 TITL 3 MECHANISTIC IMPLICATIONS FOR CLASS I ALDOLASES
REMARK 1 REF PROTEIN SCI. V. 6 119 1997
REMARK 1 REFN ISSN 0961-8368
REMARK 1 REFERENCE 4
REMARK 1 AUTH S.THORELL,P.GERGELY JR.,K.BANKI,A.PERL,G.SCHNEIDER
REMARK 1 TITL THE THREE-DIMENSIONAL STRUCTURE OF HUMAN TRANSALDOLASE
REMARK 1 REF FEBS LETT. V. 475 205 2000
REMARK 1 REFN ISSN 0014-5793
REMARK 1 DOI 10.1016/S0014-5793(00)01658-6
REMARK 2
REMARK 2 RESOLUTION. 2.05 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.05
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.60
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 2336424.040
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 90.2
REMARK 3 NUMBER OF REFLECTIONS : 47894
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) : 0.186
REMARK 3 FREE R VALUE : 0.207
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2429
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.004
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) : 2.05
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.18
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 82.00
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 6780
REMARK 3 BIN R VALUE (WORKING SET) : 0.2520
REMARK 3 BIN FREE R VALUE : 0.2660
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.90
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 346
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.014
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4936
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 317
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 17.70
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 33.20
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 2.68000
REMARK 3 B22 (A**2) : 5.97000
REMARK 3 B33 (A**2) : -8.65000
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) : 0.22
REMARK 3 ESD FROM SIGMAA (A) : 0.22
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) : 0.24
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.23
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.005
REMARK 3 BOND ANGLES (DEGREES) : 1.100
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 20.70
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.730
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) : 1.150 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 1.810 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 2.140 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 3.230 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.34
REMARK 3 BSOL : 53.16
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 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 3 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : WATER.TOP
REMARK 3 TOPOLOGY FILE 3 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1I2Q COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-FEB-01.
REMARK 100 THE DEPOSITION ID IS D_1000012829.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 12-NOV-97
REMARK 200 TEMPERATURE (KELVIN) : 293
REMARK 200 PH : 4.0
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 : RIGAKU RU200
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : GRAPHITE
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MAR
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 47894
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.050
REMARK 200 RESOLUTION RANGE LOW (A) : 47.500
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 90.3
REMARK 200 DATA REDUNDANCY : 3.900
REMARK 200 R MERGE (I) : 0.05400
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 14.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.05
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.10
REMARK 200 COMPLETENESS FOR SHELL (%) : 79.9
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.20600
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.450
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: PDB ENTRY 1ONR
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 58.44
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.96
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 6000, SODIUM CITRATE, PH 4.0,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
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 34.57150
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 65.51550
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 45.88000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 65.51550
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 34.57150
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 45.88000
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 DIMER IS GENERATED WITH A SYMMETRY MOLECULE FROM ONE OF
REMARK 300 THE MONOMERS IN THE ASYMMETRIC UNIT
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 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 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 SER A 135 48.31 -77.64
REMARK 500 SER A 226 83.35 58.28
REMARK 500 SER B 135 47.50 -77.97
REMARK 500 SER B 226 82.51 58.17
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1ONR RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF ESCHERICHIA COLI TRANSALDOLASE B
REMARK 900 RELATED ID: 1UCW RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF ESCHERICHIA COLI TRANSALDOLASE B IN COMPLEX
REMARK 900 WITH THE REDUCED SCHIFF-BASE INTERMEDIATE
REMARK 900 RELATED ID: 1F05 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN TRANSALDOLASE
REMARK 900 RELATED ID: 1I2N RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF ESCHERICHIA COLI TRANSALDOLASE B MUTANT E35A
REMARK 900 RELATED ID: 1I2O RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF ESCHERICHIA COLI TRANSALDOLASE B MUTANT E96A
REMARK 900 RELATED ID: 1I2P RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF ESCHERICHIA COLI TRANSALDOLASE B MUTANT D17A
REMARK 900 RELATED ID: 1I2R RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF ESCHERICHIA COLI TRANSALDOLASE B MUTANT S176A
DBREF 1I2Q A 2 317 UNP P0A870 TALB_ECOLI 1 316
DBREF 1I2Q B 2 317 UNP P0A870 TALB_ECOLI 1 316
SEQADV 1I2Q ALA A 156 UNP P0A870 THR 155 ENGINEERED MUTATION
SEQADV 1I2Q ALA B 156 UNP P0A870 THR 155 ENGINEERED MUTATION
SEQRES 1 A 316 THR ASP LYS LEU THR SER LEU ARG GLN TYR THR THR VAL
SEQRES 2 A 316 VAL ALA ASP THR GLY ASP ILE ALA ALA MET LYS LEU TYR
SEQRES 3 A 316 GLN PRO GLN ASP ALA THR THR ASN PRO SER LEU ILE LEU
SEQRES 4 A 316 ASN ALA ALA GLN ILE PRO GLU TYR ARG LYS LEU ILE ASP
SEQRES 5 A 316 ASP ALA VAL ALA TRP ALA LYS GLN GLN SER ASN ASP ARG
SEQRES 6 A 316 ALA GLN GLN ILE VAL ASP ALA THR ASP LYS LEU ALA VAL
SEQRES 7 A 316 ASN ILE GLY LEU GLU ILE LEU LYS LEU VAL PRO GLY ARG
SEQRES 8 A 316 ILE SER THR GLU VAL ASP ALA ARG LEU SER TYR ASP THR
SEQRES 9 A 316 GLU ALA SER ILE ALA LYS ALA LYS ARG LEU ILE LYS LEU
SEQRES 10 A 316 TYR ASN ASP ALA GLY ILE SER ASN ASP ARG ILE LEU ILE
SEQRES 11 A 316 LYS LEU ALA SER THR TRP GLN GLY ILE ARG ALA ALA GLU
SEQRES 12 A 316 GLN LEU GLU LYS GLU GLY ILE ASN CYS ASN LEU ALA LEU
SEQRES 13 A 316 LEU PHE SER PHE ALA GLN ALA ARG ALA CYS ALA GLU ALA
SEQRES 14 A 316 GLY VAL PHE LEU ILE SER PRO PHE VAL GLY ARG ILE LEU
SEQRES 15 A 316 ASP TRP TYR LYS ALA ASN THR ASP LYS LYS GLU TYR ALA
SEQRES 16 A 316 PRO ALA GLU ASP PRO GLY VAL VAL SER VAL SER GLU ILE
SEQRES 17 A 316 TYR GLN TYR TYR LYS GLU HIS GLY TYR GLU THR VAL VAL
SEQRES 18 A 316 MET GLY ALA SER PHE ARG ASN ILE GLY GLU ILE LEU GLU
SEQRES 19 A 316 LEU ALA GLY CYS ASP ARG LEU THR ILE ALA PRO ALA LEU
SEQRES 20 A 316 LEU LYS GLU LEU ALA GLU SER GLU GLY ALA ILE GLU ARG
SEQRES 21 A 316 LYS LEU SER TYR THR GLY GLU VAL LYS ALA ARG PRO ALA
SEQRES 22 A 316 ARG ILE THR GLU SER GLU PHE LEU TRP GLN HIS ASN GLN
SEQRES 23 A 316 ASP PRO MET ALA VAL ASP LYS LEU ALA GLU GLY ILE ARG
SEQRES 24 A 316 LYS PHE ALA ILE ASP GLN GLU LYS LEU GLU LYS MET ILE
SEQRES 25 A 316 GLY ASP LEU LEU
SEQRES 1 B 316 THR ASP LYS LEU THR SER LEU ARG GLN TYR THR THR VAL
SEQRES 2 B 316 VAL ALA ASP THR GLY ASP ILE ALA ALA MET LYS LEU TYR
SEQRES 3 B 316 GLN PRO GLN ASP ALA THR THR ASN PRO SER LEU ILE LEU
SEQRES 4 B 316 ASN ALA ALA GLN ILE PRO GLU TYR ARG LYS LEU ILE ASP
SEQRES 5 B 316 ASP ALA VAL ALA TRP ALA LYS GLN GLN SER ASN ASP ARG
SEQRES 6 B 316 ALA GLN GLN ILE VAL ASP ALA THR ASP LYS LEU ALA VAL
SEQRES 7 B 316 ASN ILE GLY LEU GLU ILE LEU LYS LEU VAL PRO GLY ARG
SEQRES 8 B 316 ILE SER THR GLU VAL ASP ALA ARG LEU SER TYR ASP THR
SEQRES 9 B 316 GLU ALA SER ILE ALA LYS ALA LYS ARG LEU ILE LYS LEU
SEQRES 10 B 316 TYR ASN ASP ALA GLY ILE SER ASN ASP ARG ILE LEU ILE
SEQRES 11 B 316 LYS LEU ALA SER THR TRP GLN GLY ILE ARG ALA ALA GLU
SEQRES 12 B 316 GLN LEU GLU LYS GLU GLY ILE ASN CYS ASN LEU ALA LEU
SEQRES 13 B 316 LEU PHE SER PHE ALA GLN ALA ARG ALA CYS ALA GLU ALA
SEQRES 14 B 316 GLY VAL PHE LEU ILE SER PRO PHE VAL GLY ARG ILE LEU
SEQRES 15 B 316 ASP TRP TYR LYS ALA ASN THR ASP LYS LYS GLU TYR ALA
SEQRES 16 B 316 PRO ALA GLU ASP PRO GLY VAL VAL SER VAL SER GLU ILE
SEQRES 17 B 316 TYR GLN TYR TYR LYS GLU HIS GLY TYR GLU THR VAL VAL
SEQRES 18 B 316 MET GLY ALA SER PHE ARG ASN ILE GLY GLU ILE LEU GLU
SEQRES 19 B 316 LEU ALA GLY CYS ASP ARG LEU THR ILE ALA PRO ALA LEU
SEQRES 20 B 316 LEU LYS GLU LEU ALA GLU SER GLU GLY ALA ILE GLU ARG
SEQRES 21 B 316 LYS LEU SER TYR THR GLY GLU VAL LYS ALA ARG PRO ALA
SEQRES 22 B 316 ARG ILE THR GLU SER GLU PHE LEU TRP GLN HIS ASN GLN
SEQRES 23 B 316 ASP PRO MET ALA VAL ASP LYS LEU ALA GLU GLY ILE ARG
SEQRES 24 B 316 LYS PHE ALA ILE ASP GLN GLU LYS LEU GLU LYS MET ILE
SEQRES 25 B 316 GLY ASP LEU LEU
FORMUL 3 HOH *317(H2 O)
HELIX 1 1 ASP A 3 ARG A 9 1 7
HELIX 2 2 ASP A 20 GLN A 28 1 9
HELIX 3 3 ASN A 35 ALA A 43 1 9
HELIX 4 4 GLN A 44 GLU A 47 5 4
HELIX 5 5 TYR A 48 SER A 63 1 16
HELIX 6 6 ASP A 65 LYS A 87 1 23
HELIX 7 7 ASP A 98 SER A 102 5 5
HELIX 8 8 ASP A 104 ALA A 122 1 19
HELIX 9 9 SER A 125 ASP A 127 5 3
HELIX 10 10 THR A 136 GLU A 149 1 14
HELIX 11 11 SER A 160 ALA A 170 1 11
HELIX 12 12 PHE A 178 THR A 190 1 13
HELIX 13 13 ALA A 196 GLU A 199 5 4
HELIX 14 14 ASP A 200 HIS A 216 1 17
HELIX 15 15 ASN A 229 LEU A 236 1 8
HELIX 16 16 ALA A 245 SER A 255 1 11
HELIX 17 17 THR A 277 ASN A 286 1 10
HELIX 18 18 ASP A 288 ASP A 315 1 28
HELIX 19 19 ASP B 3 ARG B 9 1 7
HELIX 20 20 ASP B 20 GLN B 28 1 9
HELIX 21 21 ASN B 35 ALA B 43 1 9
HELIX 22 22 GLN B 44 GLU B 47 5 4
HELIX 23 23 TYR B 48 SER B 63 1 16
HELIX 24 24 ASP B 65 LYS B 87 1 23
HELIX 25 25 ASP B 98 SER B 102 5 5
HELIX 26 26 ASP B 104 ALA B 122 1 19
HELIX 27 27 SER B 125 ASP B 127 5 3
HELIX 28 28 THR B 136 GLU B 149 1 14
HELIX 29 29 SER B 160 ALA B 170 1 11
HELIX 30 30 PHE B 178 THR B 190 1 13
HELIX 31 31 ALA B 196 GLU B 199 5 4
HELIX 32 32 ASP B 200 HIS B 216 1 17
HELIX 33 33 ASN B 229 GLU B 235 1 7
HELIX 34 34 ALA B 245 SER B 255 1 11
HELIX 35 35 THR B 277 ASN B 286 1 10
HELIX 36 36 ASP B 288 ASP B 315 1 28
SHEET 1 A 9 THR A 13 ASP A 17 0
SHEET 2 A 9 ASP A 31 THR A 33 1 O ASP A 31 N ALA A 16
SHEET 3 A 9 ILE A 93 GLU A 96 1 N SER A 94 O ALA A 32
SHEET 4 A 9 ILE A 129 ALA A 134 1 O LEU A 130 N THR A 95
SHEET 5 A 9 CYS A 153 LEU A 158 1 N ASN A 154 O ILE A 131
SHEET 6 A 9 LEU A 174 PRO A 177 1 O LEU A 174 N LEU A 155
SHEET 7 A 9 VAL A 221 GLY A 224 1 O VAL A 221 N ILE A 175
SHEET 8 A 9 ARG A 241 ILE A 244 1 N ARG A 241 O VAL A 222
SHEET 9 A 9 THR A 13 ASP A 17 1 O THR A 13 N LEU A 242
SHEET 1 B 9 THR B 13 ASP B 17 0
SHEET 2 B 9 ASP B 31 THR B 33 1 O ASP B 31 N ALA B 16
SHEET 3 B 9 ILE B 93 GLU B 96 1 N SER B 94 O ALA B 32
SHEET 4 B 9 ILE B 129 ALA B 134 1 O LEU B 130 N THR B 95
SHEET 5 B 9 CYS B 153 LEU B 158 1 N ASN B 154 O ILE B 131
SHEET 6 B 9 LEU B 174 PRO B 177 1 O LEU B 174 N LEU B 155
SHEET 7 B 9 VAL B 221 GLY B 224 1 O VAL B 221 N ILE B 175
SHEET 8 B 9 ARG B 241 ILE B 244 1 N ARG B 241 O VAL B 222
SHEET 9 B 9 THR B 13 ASP B 17 1 O THR B 13 N LEU B 242
CRYST1 69.143 91.760 131.031 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 0.014463 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010898 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007632 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
