HEADER TRANSFERASE 25-OCT-06 2E1D
TITLE CRYSTAL STRUCTURE OF MOUSE TRANSALDOLASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TRANSALDOLASE;
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: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: HOUSE MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 6 EXPRESSION_SYSTEM_PLASMID: PX050706-14;
SOURCE 7 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS
KEYWDS TRANSALDOLASE, PENTOSE PHOSPHATE PATHWAY, STRUCTURAL GENOMICS,
KEYWDS 2 NPPSFA, NATIONAL PROJECT ON PROTEIN STRUCTURAL AND FUNCTIONAL
KEYWDS 3 ANALYSES, RIKEN STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE, RSGI,
KEYWDS 4 TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR S.KISHISHITA,K.MURAYAMA,L.CHEN,Z.J.LIU,B.C.WANG,M.SHIROUZU,
AUTHOR 2 S.YOKOYAMA,RIKEN STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE (RSGI)
REVDAT 4 25-OCT-23 2E1D 1 REMARK
REVDAT 3 10-NOV-21 2E1D 1 REMARK SEQADV
REVDAT 2 24-FEB-09 2E1D 1 VERSN
REVDAT 1 13-NOV-07 2E1D 0
JRNL AUTH S.KISHISHITA,K.MURAYAMA,L.CHEN,Z.J.LIU,B.C.WANG,M.SHIROUZU,
JRNL AUTH 2 S.YOKOYAMA
JRNL TITL CRYSTAL STRUCTURE OF MOUSE TRANSALDOLASE
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1
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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 46.52
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 57309.480
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 97.4
REMARK 3 NUMBER OF REFLECTIONS : 43527
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) : 0.169
REMARK 3 FREE R VALUE : 0.211
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2186
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) : 2.13
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 89.30
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 6270
REMARK 3 BIN R VALUE (WORKING SET) : 0.2010
REMARK 3 BIN FREE R VALUE : 0.2430
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.40
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 361
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.013
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5004
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 8
REMARK 3 SOLVENT ATOMS : 654
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 13.50
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 25.30
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 2.01000
REMARK 3 B22 (A**2) : 2.89000
REMARK 3 B33 (A**2) : -4.90000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -3.98000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.18
REMARK 3 ESD FROM SIGMAA (A) : 0.13
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) : 0.18
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) : 20.60
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.740
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) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.38
REMARK 3 BSOL : 60.06
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 : ION.PARAM
REMARK 3 PARAMETER FILE 4 : SO3_XPLOR_PAR.TXT
REMARK 3 PARAMETER FILE 5 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : ION.TOP
REMARK 3 TOPOLOGY FILE 3 : SO3_XPLOR_TOP.TXT
REMARK 3 TOPOLOGY FILE 4 : NULL
REMARK 3 TOPOLOGY FILE 5 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2E1D COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 26-OCT-06.
REMARK 100 THE DEPOSITION ID IS D_1000026103.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 05-SEP-05
REMARK 200 TEMPERATURE (KELVIN) : 93
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 22-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97243
REMARK 200 MONOCHROMATOR : SI III
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 300 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 44262
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 200 DATA REDUNDANCY : 7.500
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.06100
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 34.3000
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) : 2.09
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.6
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.25500
REMARK 200 <I/SIGMA(I)> FOR SHELL : 6.950
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 1F05
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 46.87
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.32
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M MES, 21% PEG3350, PH 6.5, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 53.74400
REMARK 290 SMTRY3 2 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 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 GLY A 4
REMARK 465 SER A 5
REMARK 465 SER A 6
REMARK 465 GLY A 7
REMARK 465 SER A 8
REMARK 465 SER A 9
REMARK 465 GLY A 10
REMARK 465 MET A 11
REMARK 465 ALA A 333
REMARK 465 GLU A 334
REMARK 465 GLY B 4
REMARK 465 SER B 5
REMARK 465 SER B 6
REMARK 465 GLY B 7
REMARK 465 SER B 8
REMARK 465 SER B 9
REMARK 465 GLY B 10
REMARK 465 SER B 332
REMARK 465 ALA B 333
REMARK 465 GLU B 334
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 ASP A 108 123.03 -38.75
REMARK 500 SER A 145 48.90 -83.19
REMARK 500 SER A 187 71.84 -117.48
REMARK 500 VAL A 190 -56.39 -122.42
REMARK 500 SER A 237 101.95 70.82
REMARK 500 SER A 284 156.05 177.99
REMARK 500 LYS B 38 62.91 34.87
REMARK 500 SER B 145 47.73 -81.69
REMARK 500 SER B 187 72.41 -119.21
REMARK 500 SER B 237 104.09 66.29
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 SO3 A 3016
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO3 B 3017
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: MMT007100385.2 RELATED DB: TARGETDB
DBREF 2E1D A 11 334 UNP Q93092 TALDO_MOUSE 11 334
DBREF 2E1D B 11 334 UNP Q93092 TALDO_MOUSE 11 334
SEQADV 2E1D GLY A 4 UNP Q93092 EXPRESSION TAG
SEQADV 2E1D SER A 5 UNP Q93092 EXPRESSION TAG
SEQADV 2E1D SER A 6 UNP Q93092 EXPRESSION TAG
SEQADV 2E1D GLY A 7 UNP Q93092 EXPRESSION TAG
SEQADV 2E1D SER A 8 UNP Q93092 EXPRESSION TAG
SEQADV 2E1D SER A 9 UNP Q93092 EXPRESSION TAG
SEQADV 2E1D GLY A 10 UNP Q93092 EXPRESSION TAG
SEQADV 2E1D GLY A 210 UNP Q93092 GLU 210 ENGINEERED MUTATION
SEQADV 2E1D GLY B 4 UNP Q93092 EXPRESSION TAG
SEQADV 2E1D SER B 5 UNP Q93092 EXPRESSION TAG
SEQADV 2E1D SER B 6 UNP Q93092 EXPRESSION TAG
SEQADV 2E1D GLY B 7 UNP Q93092 EXPRESSION TAG
SEQADV 2E1D SER B 8 UNP Q93092 EXPRESSION TAG
SEQADV 2E1D SER B 9 UNP Q93092 EXPRESSION TAG
SEQADV 2E1D GLY B 10 UNP Q93092 EXPRESSION TAG
SEQADV 2E1D GLY B 210 UNP Q93092 GLU 210 ENGINEERED MUTATION
SEQRES 1 A 331 GLY SER SER GLY SER SER GLY MET GLU SER ALA LEU ASP
SEQRES 2 A 331 GLN LEU LYS GLN PHE THR THR VAL VAL ALA ASP THR GLY
SEQRES 3 A 331 ASP PHE ASN ALA ILE ASP GLU TYR LYS PRO GLN ASP ALA
SEQRES 4 A 331 THR THR ASN PRO SER LEU ILE LEU ALA ALA ALA GLN MET
SEQRES 5 A 331 PRO ALA TYR GLN GLU LEU VAL GLU GLU ALA ILE ALA TYR
SEQRES 6 A 331 GLY LYS LYS LEU GLY GLY PRO GLN GLU GLU GLN ILE LYS
SEQRES 7 A 331 ASN ALA ILE ASP LYS LEU PHE VAL LEU PHE GLY ALA GLU
SEQRES 8 A 331 ILE LEU LYS LYS ILE PRO GLY ARG VAL SER THR GLU VAL
SEQRES 9 A 331 ASP ALA ARG LEU SER PHE ASP LYS ASP ALA MET VAL ALA
SEQRES 10 A 331 ARG ALA ARG ARG LEU ILE GLU LEU TYR LYS GLU ALA GLY
SEQRES 11 A 331 VAL GLY LYS ASP ARG ILE LEU ILE LYS LEU SER SER THR
SEQRES 12 A 331 TRP GLU GLY ILE GLN ALA GLY LYS GLU LEU GLU GLU GLN
SEQRES 13 A 331 HIS GLY ILE HIS CYS ASN MET THR LEU LEU PHE SER PHE
SEQRES 14 A 331 ALA GLN ALA VAL ALA CYS ALA GLU ALA GLY VAL THR LEU
SEQRES 15 A 331 ILE SER PRO PHE VAL GLY ARG ILE LEU ASP TRP HIS VAL
SEQRES 16 A 331 ALA ASN THR ASP LYS LYS SER TYR GLU PRO GLN GLY ASP
SEQRES 17 A 331 PRO GLY VAL LYS SER VAL THR LYS ILE TYR ASN TYR TYR
SEQRES 18 A 331 LYS LYS PHE GLY TYR LYS THR ILE VAL MET GLY ALA SER
SEQRES 19 A 331 PHE ARG ASN THR GLY GLU ILE LYS ALA LEU ALA GLY CYS
SEQRES 20 A 331 ASP PHE LEU THR ILE SER PRO LYS LEU LEU GLY GLU LEU
SEQRES 21 A 331 LEU LYS ASP ASN SER LYS LEU ALA PRO ALA LEU SER VAL
SEQRES 22 A 331 LYS ALA ALA GLN THR SER ASP SER GLU LYS ILE HIS LEU
SEQRES 23 A 331 ASP GLU LYS ALA PHE ARG TRP LEU HIS ASN GLU ASP GLN
SEQRES 24 A 331 MET ALA VAL GLU LYS LEU SER ASP GLY ILE ARG LYS PHE
SEQRES 25 A 331 ALA ALA ASP ALA ILE LYS LEU GLU ARG MET LEU THR GLU
SEQRES 26 A 331 ARG MET PHE SER ALA GLU
SEQRES 1 B 331 GLY SER SER GLY SER SER GLY MET GLU SER ALA LEU ASP
SEQRES 2 B 331 GLN LEU LYS GLN PHE THR THR VAL VAL ALA ASP THR GLY
SEQRES 3 B 331 ASP PHE ASN ALA ILE ASP GLU TYR LYS PRO GLN ASP ALA
SEQRES 4 B 331 THR THR ASN PRO SER LEU ILE LEU ALA ALA ALA GLN MET
SEQRES 5 B 331 PRO ALA TYR GLN GLU LEU VAL GLU GLU ALA ILE ALA TYR
SEQRES 6 B 331 GLY LYS LYS LEU GLY GLY PRO GLN GLU GLU GLN ILE LYS
SEQRES 7 B 331 ASN ALA ILE ASP LYS LEU PHE VAL LEU PHE GLY ALA GLU
SEQRES 8 B 331 ILE LEU LYS LYS ILE PRO GLY ARG VAL SER THR GLU VAL
SEQRES 9 B 331 ASP ALA ARG LEU SER PHE ASP LYS ASP ALA MET VAL ALA
SEQRES 10 B 331 ARG ALA ARG ARG LEU ILE GLU LEU TYR LYS GLU ALA GLY
SEQRES 11 B 331 VAL GLY LYS ASP ARG ILE LEU ILE LYS LEU SER SER THR
SEQRES 12 B 331 TRP GLU GLY ILE GLN ALA GLY LYS GLU LEU GLU GLU GLN
SEQRES 13 B 331 HIS GLY ILE HIS CYS ASN MET THR LEU LEU PHE SER PHE
SEQRES 14 B 331 ALA GLN ALA VAL ALA CYS ALA GLU ALA GLY VAL THR LEU
SEQRES 15 B 331 ILE SER PRO PHE VAL GLY ARG ILE LEU ASP TRP HIS VAL
SEQRES 16 B 331 ALA ASN THR ASP LYS LYS SER TYR GLU PRO GLN GLY ASP
SEQRES 17 B 331 PRO GLY VAL LYS SER VAL THR LYS ILE TYR ASN TYR TYR
SEQRES 18 B 331 LYS LYS PHE GLY TYR LYS THR ILE VAL MET GLY ALA SER
SEQRES 19 B 331 PHE ARG ASN THR GLY GLU ILE LYS ALA LEU ALA GLY CYS
SEQRES 20 B 331 ASP PHE LEU THR ILE SER PRO LYS LEU LEU GLY GLU LEU
SEQRES 21 B 331 LEU LYS ASP ASN SER LYS LEU ALA PRO ALA LEU SER VAL
SEQRES 22 B 331 LYS ALA ALA GLN THR SER ASP SER GLU LYS ILE HIS LEU
SEQRES 23 B 331 ASP GLU LYS ALA PHE ARG TRP LEU HIS ASN GLU ASP GLN
SEQRES 24 B 331 MET ALA VAL GLU LYS LEU SER ASP GLY ILE ARG LYS PHE
SEQRES 25 B 331 ALA ALA ASP ALA ILE LYS LEU GLU ARG MET LEU THR GLU
SEQRES 26 B 331 ARG MET PHE SER ALA GLU
HET SO3 A3016 4
HET SO3 B3017 4
HETNAM SO3 SULFITE ION
FORMUL 3 SO3 2(O3 S 2-)
FORMUL 5 HOH *654(H2 O)
HELIX 1 1 SER A 13 LYS A 19 1 7
HELIX 2 2 ASP A 30 ILE A 34 5 5
HELIX 3 3 ASN A 45 GLN A 54 1 10
HELIX 4 4 MET A 55 ALA A 57 5 3
HELIX 5 5 TYR A 58 GLY A 73 1 16
HELIX 6 6 PRO A 75 ILE A 99 1 25
HELIX 7 7 ASP A 108 SER A 112 5 5
HELIX 8 8 ASP A 114 ALA A 132 1 19
HELIX 9 9 GLY A 135 ASP A 137 5 3
HELIX 10 10 THR A 146 GLY A 161 1 16
HELIX 11 11 SER A 171 GLY A 182 1 12
HELIX 12 12 VAL A 190 THR A 201 1 12
HELIX 13 13 GLU A 207 GLY A 210 5 4
HELIX 14 14 ASP A 211 PHE A 227 1 17
HELIX 15 15 ASN A 240 ALA A 246 1 7
HELIX 16 16 SER A 256 ASP A 266 1 11
HELIX 17 17 SER A 275 GLN A 280 1 6
HELIX 18 18 ASP A 290 GLU A 300 1 11
HELIX 19 19 ASP A 301 PHE A 331 1 31
HELIX 20 20 SER B 13 THR B 22 1 10
HELIX 21 21 ASP B 30 LYS B 38 5 9
HELIX 22 22 ASN B 45 ALA B 53 1 9
HELIX 23 23 GLN B 54 ALA B 57 5 4
HELIX 24 24 TYR B 58 GLY B 73 1 16
HELIX 25 25 PRO B 75 LYS B 97 1 23
HELIX 26 26 ASP B 108 SER B 112 5 5
HELIX 27 27 ASP B 114 ALA B 132 1 19
HELIX 28 28 GLY B 135 ASP B 137 5 3
HELIX 29 29 THR B 146 GLY B 161 1 16
HELIX 30 30 SER B 171 GLY B 182 1 12
HELIX 31 31 VAL B 190 THR B 201 1 12
HELIX 32 32 GLU B 207 GLY B 210 5 4
HELIX 33 33 ASP B 211 PHE B 227 1 17
HELIX 34 34 ASN B 240 ALA B 246 1 7
HELIX 35 35 SER B 256 ASP B 266 1 11
HELIX 36 36 SER B 275 THR B 281 1 7
HELIX 37 37 ASP B 290 GLU B 300 1 11
HELIX 38 38 ASP B 301 PHE B 331 1 31
SHEET 1 A 9 THR A 23 ASP A 27 0
SHEET 2 A 9 ASP A 41 THR A 43 1 O THR A 43 N ALA A 26
SHEET 3 A 9 VAL A 103 GLU A 106 1 O SER A 104 N ALA A 42
SHEET 4 A 9 ILE A 139 SER A 144 1 O LYS A 142 N THR A 105
SHEET 5 A 9 CYS A 164 LEU A 169 1 O ASN A 165 N ILE A 141
SHEET 6 A 9 LEU A 185 PRO A 188 1 O SER A 187 N MET A 166
SHEET 7 A 9 ILE A 232 GLY A 235 1 O ILE A 232 N ILE A 186
SHEET 8 A 9 PHE A 252 ILE A 255 1 O PHE A 252 N VAL A 233
SHEET 9 A 9 THR A 23 ASP A 27 1 N VAL A 25 O ILE A 255
SHEET 1 B 9 THR B 23 ASP B 27 0
SHEET 2 B 9 ASP B 41 THR B 43 1 O THR B 43 N ALA B 26
SHEET 3 B 9 VAL B 103 GLU B 106 1 O SER B 104 N ALA B 42
SHEET 4 B 9 ILE B 139 SER B 144 1 O LYS B 142 N THR B 105
SHEET 5 B 9 CYS B 164 LEU B 169 1 O ASN B 165 N ILE B 141
SHEET 6 B 9 LEU B 185 PRO B 188 1 O SER B 187 N MET B 166
SHEET 7 B 9 ILE B 232 GLY B 235 1 O ILE B 232 N ILE B 186
SHEET 8 B 9 PHE B 252 ILE B 255 1 O PHE B 252 N VAL B 233
SHEET 9 B 9 THR B 23 ASP B 27 1 N ASP B 27 O ILE B 255
SITE 1 AC1 5 ARG A 192 SER A 237 ARG A 239 HOH A3128
SITE 2 AC1 5 HOH A3262
SITE 1 AC2 4 ARG B 192 SER B 237 ARG B 239 HOH B3376
CRYST1 51.984 107.488 60.877 90.00 96.91 90.00 P 1 21 1 4
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 0.019237 0.000000 0.002330 0.00000
SCALE2 0.000000 0.009303 0.000000 0.00000
SCALE3 0.000000 0.000000 0.016547 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
