HEADER OXIDOREDUCTASE 26-JUL-03 1Q2X
TITLE CRYSTAL STRUCTURE OF THE E243D MUTANT OF ASPARTATE SEMIALDEHYDE
TITLE 2 DEHYDROGENASE FROM HAEMOPHILUS INFLUENZAE BOUND WITH SUBSTRATE
TITLE 3 ASPARTATE SEMIALDEHYDE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ASPARTATE-SEMIALDEHYDE DEHYDROGENASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: ASA DEHYDROGENASE, ASADH;
COMPND 5 EC: 1.2.1.11;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HAEMOPHILUS INFLUENZAE RD;
SOURCE 3 ORGANISM_TAXID: 71421;
SOURCE 4 STRAIN: KW20;
SOURCE 5 GENE: ASD;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET41
KEYWDS ENZYME, ASPARTATE SEMIALDEHYDE DEHYDROGENASE, TETRAHEDRAL
KEYWDS 2 INTERMEDIATE, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.BLANCO,R.A.MOORE,C.R.FAEHNLE,D.M.COE,R.E.VIOLA
REVDAT 5 16-AUG-23 1Q2X 1 REMARK
REVDAT 4 27-OCT-21 1Q2X 1 SEQADV LINK
REVDAT 3 13-JUL-11 1Q2X 1 VERSN
REVDAT 2 24-FEB-09 1Q2X 1 VERSN
REVDAT 1 27-JUL-04 1Q2X 0
JRNL AUTH J.BLANCO,R.A.MOORE,C.R.FAEHNLE,D.M.COE,R.E.VIOLA
JRNL TITL THE ROLE OF SUBSTRATE-BINDING GROUPS IN THE MECHANISM OF
JRNL TITL 2 ASPARTATE-BETA-SEMIALDEHYDE DEHYDROGENASE.
JRNL REF ACTA CRYSTALLOGR.,SECT.D V. 60 1388 2004
JRNL REFN ISSN 0907-4449
JRNL PMID 15272161
JRNL DOI 10.1107/S0907444904012971
REMARK 2
REMARK 2 RESOLUTION. 2.05 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.0
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) : 40.38
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 93.5
REMARK 3 NUMBER OF REFLECTIONS : 41039
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) : 0.238
REMARK 3 FREE R VALUE : 0.279
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.000
REMARK 3 FREE R VALUE TEST SET COUNT : 4124
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) (%) : 88.60
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 5838
REMARK 3 BIN R VALUE (WORKING SET) : 0.3410
REMARK 3 BIN FREE R VALUE : 0.3400
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 9.80
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 631
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 : 5522
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 212
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 14.40
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 32.40
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 4.75000
REMARK 3 B22 (A**2) : -13.99000
REMARK 3 B33 (A**2) : 9.24000
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) : 0.30
REMARK 3 ESD FROM SIGMAA (A) : 0.37
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) : 0.34
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.37
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.013
REMARK 3 BOND ANGLES (DEGREES) : 1.700
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 23.90
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.790
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 : 0.35
REMARK 3 BSOL : 20.61
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_NEW.PARAM
REMARK 3 PARAMETER FILE 2 : WATER.PARAM
REMARK 3 PARAMETER FILE 3 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN_NEW.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 1Q2X COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 31-JUL-03.
REMARK 100 THE DEPOSITION ID IS D_1000019848.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 18-JUL-02
REMARK 200 TEMPERATURE (KELVIN) : 90
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 19-BM
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : FLAT GRAPHITE CRYSTAL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : SBC-3
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : NULL
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.050
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 85.9
REMARK 200 DATA REDUNDANCY : 10.70
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.05500
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 19.1000
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) : 2.12
REMARK 200 COMPLETENESS FOR SHELL (%) : 94.5
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.24000
REMARK 200 <I/SIGMA(I)> FOR SHELL : 5.600
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: 1NWC
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 43.79
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.19
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20-24% PEG 3350, 0.2 M AMMONIUM
REMARK 280 ACETATE, 0.1 M TRIS, PH 8.5, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 298K
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 56.93100
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 300 REMARK: THE BIOLOGICAL ASSEMBLY IS A DIMER
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: 6910 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 27250 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -49.0 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 GLY A 41
REMARK 465 GLN A 42
REMARK 465 LYS A 43
REMARK 465 ALA A 44
REMARK 465 PRO A 45
REMARK 465 VAL A 46
REMARK 465 PHE A 47
REMARK 465 GLY A 48
REMARK 465 GLY A 49
REMARK 465 LYS A 50
REMARK 465 ASP A 51
REMARK 465 ALA A 52
REMARK 465 GLY A 53
REMARK 465 ASP A 54
REMARK 465 GLY B 41
REMARK 465 GLN B 42
REMARK 465 LYS B 43
REMARK 465 ALA B 44
REMARK 465 PRO B 45
REMARK 465 VAL B 46
REMARK 465 PHE B 47
REMARK 465 GLY B 48
REMARK 465 GLY B 49
REMARK 465 LYS B 50
REMARK 465 ASP B 51
REMARK 465 ALA B 52
REMARK 465 GLY B 53
REMARK 465 ASP B 54
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 LEU A 112 78.71 -177.61
REMARK 500 PRO A 229 43.04 -82.45
REMARK 500 ASP A 232 170.83 73.29
REMARK 500 LEU A 257 52.56 -104.60
REMARK 500 ASN A 310 64.65 -66.42
REMARK 500 LEU A 355 -90.54 -88.77
REMARK 500 ALA A 358 -80.18 -154.93
REMARK 500 LEU B 112 73.62 -175.51
REMARK 500 SER B 226 -159.88 -150.24
REMARK 500 PRO B 229 43.18 -81.06
REMARK 500 ASP B 232 171.48 74.55
REMARK 500 LEU B 257 53.08 -93.78
REMARK 500 ASN B 310 56.10 -65.64
REMARK 500 LEU B 319 55.15 -93.84
REMARK 500 LEU B 355 -93.17 -93.09
REMARK 500 ALA B 358 -77.53 -149.51
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1NWC RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF ASPARTATE SEMIALDEHYDE DEHYDROGENASE FROM
REMARK 900 HAEMOPHILUS INFLUENZAE
REMARK 900 RELATED ID: 1NWH RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF ASPARTATE SEMIALDEHYDE DEHYDROGENASE FROM
REMARK 900 HAEMOPHILUS INFLUENZAE AS A TETRAHEDRAL REACTION INTERMEDIATE
DBREF 1Q2X A 1 371 UNP P44801 DHAS_HAEIN 1 371
DBREF 1Q2X B 1 371 UNP P44801 DHAS_HAEIN 1 371
SEQADV 1Q2X HTI A 136 UNP P44801 CYS 136 MODIFIED RESIDUE
SEQADV 1Q2X ASP A 243 UNP P44801 GLU 243 ENGINEERED MUTATION
SEQADV 1Q2X HTI B 136 UNP P44801 CYS 136 MODIFIED RESIDUE
SEQADV 1Q2X ASP B 243 UNP P44801 GLU 243 ENGINEERED MUTATION
SEQRES 1 A 371 MET LYS ASN VAL GLY PHE ILE GLY TRP ARG GLY MET VAL
SEQRES 2 A 371 GLY SER VAL LEU MET ASP ARG MET SER GLN GLU ASN ASP
SEQRES 3 A 371 PHE GLU ASN LEU ASN PRO VAL PHE PHE THR THR SER GLN
SEQRES 4 A 371 ALA GLY GLN LYS ALA PRO VAL PHE GLY GLY LYS ASP ALA
SEQRES 5 A 371 GLY ASP LEU LYS SER ALA PHE ASP ILE GLU GLU LEU LYS
SEQRES 6 A 371 LYS LEU ASP ILE ILE VAL THR CYS GLN GLY GLY ASP TYR
SEQRES 7 A 371 THR ASN GLU VAL TYR PRO LYS LEU LYS ALA THR GLY TRP
SEQRES 8 A 371 ASP GLY TYR TRP VAL ASP ALA ALA SER ALA LEU ARG MET
SEQRES 9 A 371 LYS ASP ASP ALA ILE ILE VAL LEU ASP PRO VAL ASN GLN
SEQRES 10 A 371 HIS VAL ILE SER GLU GLY LEU LYS LYS GLY ILE LYS THR
SEQRES 11 A 371 PHE VAL GLY GLY ASN HTI THR VAL SER LEU MET LEU MET
SEQRES 12 A 371 ALA ILE GLY GLY LEU PHE GLU LYS ASP LEU VAL GLU TRP
SEQRES 13 A 371 ILE SER VAL ALA THR TYR GLN ALA ALA SER GLY ALA GLY
SEQRES 14 A 371 ALA LYS ASN MET ARG GLU LEU LEU SER GLN MET GLY LEU
SEQRES 15 A 371 LEU GLU GLN ALA VAL SER SER GLU LEU LYS ASP PRO ALA
SEQRES 16 A 371 SER SER ILE LEU ASP ILE GLU ARG LYS VAL THR ALA LYS
SEQRES 17 A 371 MET ARG ALA ASP ASN PHE PRO THR ASP ASN PHE GLY ALA
SEQRES 18 A 371 ALA LEU GLY GLY SER LEU ILE PRO TRP ILE ASP LYS LEU
SEQRES 19 A 371 LEU PRO GLU THR GLY GLN THR LYS ASP GLU TRP LYS GLY
SEQRES 20 A 371 TYR ALA GLU THR ASN LYS ILE LEU GLY LEU SER ASP ASN
SEQRES 21 A 371 PRO ILE PRO VAL ASP GLY LEU CYS VAL ARG ILE GLY ALA
SEQRES 22 A 371 LEU ARG CYS HIS SER GLN ALA PHE THR ILE LYS LEU LYS
SEQRES 23 A 371 LYS ASP LEU PRO LEU GLU GLU ILE GLU GLN ILE ILE ALA
SEQRES 24 A 371 SER HIS ASN GLU TRP VAL LYS VAL ILE PRO ASN ASP LYS
SEQRES 25 A 371 GLU ILE THR LEU ARG GLU LEU THR PRO ALA LYS VAL THR
SEQRES 26 A 371 GLY THR LEU SER VAL PRO VAL GLY ARG LEU ARG LYS LEU
SEQRES 27 A 371 ALA MET GLY PRO GLU TYR LEU ALA ALA PHE THR VAL GLY
SEQRES 28 A 371 ASP GLN LEU LEU TRP GLY ALA ALA GLU PRO VAL ARG ARG
SEQRES 29 A 371 ILE LEU LYS GLN LEU VAL ALA
SEQRES 1 B 371 MET LYS ASN VAL GLY PHE ILE GLY TRP ARG GLY MET VAL
SEQRES 2 B 371 GLY SER VAL LEU MET ASP ARG MET SER GLN GLU ASN ASP
SEQRES 3 B 371 PHE GLU ASN LEU ASN PRO VAL PHE PHE THR THR SER GLN
SEQRES 4 B 371 ALA GLY GLN LYS ALA PRO VAL PHE GLY GLY LYS ASP ALA
SEQRES 5 B 371 GLY ASP LEU LYS SER ALA PHE ASP ILE GLU GLU LEU LYS
SEQRES 6 B 371 LYS LEU ASP ILE ILE VAL THR CYS GLN GLY GLY ASP TYR
SEQRES 7 B 371 THR ASN GLU VAL TYR PRO LYS LEU LYS ALA THR GLY TRP
SEQRES 8 B 371 ASP GLY TYR TRP VAL ASP ALA ALA SER ALA LEU ARG MET
SEQRES 9 B 371 LYS ASP ASP ALA ILE ILE VAL LEU ASP PRO VAL ASN GLN
SEQRES 10 B 371 HIS VAL ILE SER GLU GLY LEU LYS LYS GLY ILE LYS THR
SEQRES 11 B 371 PHE VAL GLY GLY ASN HTI THR VAL SER LEU MET LEU MET
SEQRES 12 B 371 ALA ILE GLY GLY LEU PHE GLU LYS ASP LEU VAL GLU TRP
SEQRES 13 B 371 ILE SER VAL ALA THR TYR GLN ALA ALA SER GLY ALA GLY
SEQRES 14 B 371 ALA LYS ASN MET ARG GLU LEU LEU SER GLN MET GLY LEU
SEQRES 15 B 371 LEU GLU GLN ALA VAL SER SER GLU LEU LYS ASP PRO ALA
SEQRES 16 B 371 SER SER ILE LEU ASP ILE GLU ARG LYS VAL THR ALA LYS
SEQRES 17 B 371 MET ARG ALA ASP ASN PHE PRO THR ASP ASN PHE GLY ALA
SEQRES 18 B 371 ALA LEU GLY GLY SER LEU ILE PRO TRP ILE ASP LYS LEU
SEQRES 19 B 371 LEU PRO GLU THR GLY GLN THR LYS ASP GLU TRP LYS GLY
SEQRES 20 B 371 TYR ALA GLU THR ASN LYS ILE LEU GLY LEU SER ASP ASN
SEQRES 21 B 371 PRO ILE PRO VAL ASP GLY LEU CYS VAL ARG ILE GLY ALA
SEQRES 22 B 371 LEU ARG CYS HIS SER GLN ALA PHE THR ILE LYS LEU LYS
SEQRES 23 B 371 LYS ASP LEU PRO LEU GLU GLU ILE GLU GLN ILE ILE ALA
SEQRES 24 B 371 SER HIS ASN GLU TRP VAL LYS VAL ILE PRO ASN ASP LYS
SEQRES 25 B 371 GLU ILE THR LEU ARG GLU LEU THR PRO ALA LYS VAL THR
SEQRES 26 B 371 GLY THR LEU SER VAL PRO VAL GLY ARG LEU ARG LYS LEU
SEQRES 27 B 371 ALA MET GLY PRO GLU TYR LEU ALA ALA PHE THR VAL GLY
SEQRES 28 B 371 ASP GLN LEU LEU TRP GLY ALA ALA GLU PRO VAL ARG ARG
SEQRES 29 B 371 ILE LEU LYS GLN LEU VAL ALA
MODRES 1Q2X HTI A 136 CYS
MODRES 1Q2X HTI B 136 CYS
HET HTI A 136 14
HET HTI B 136 14
HETNAM HTI (4S)-4-{[(2S)-2-AMINO-3-OXOPROPYL]SULFANYL}-L-
HETNAM 2 HTI HOMOSERINE
FORMUL 1 HTI 2(C7 H14 N2 O5 S)
FORMUL 3 HOH *212(H2 O)
HELIX 1 1 GLY A 11 GLU A 24 1 14
HELIX 2 2 ASN A 25 LEU A 30 5 6
HELIX 3 3 ASP A 60 LYS A 66 1 7
HELIX 4 4 GLY A 75 ALA A 88 1 14
HELIX 5 5 LEU A 112 LYS A 125 1 14
HELIX 6 6 ASN A 135 ILE A 145 1 11
HELIX 7 7 ILE A 145 LYS A 151 1 7
HELIX 8 8 ALA A 164 ALA A 168 5 5
HELIX 9 9 GLY A 169 ALA A 186 1 18
HELIX 10 10 VAL A 187 ASP A 193 1 7
HELIX 11 11 SER A 197 ALA A 211 1 15
HELIX 12 12 THR A 241 GLY A 256 1 16
HELIX 13 13 PRO A 290 SER A 300 1 11
HELIX 14 14 ASP A 311 LEU A 319 1 9
HELIX 15 15 THR A 320 THR A 325 1 6
HELIX 16 16 ALA A 358 ALA A 371 1 14
HELIX 17 17 GLY B 11 GLU B 24 1 14
HELIX 18 18 ASN B 25 LEU B 30 5 6
HELIX 19 19 ASP B 60 LYS B 66 1 7
HELIX 20 20 GLY B 75 ALA B 88 1 14
HELIX 21 21 LEU B 112 GLY B 127 1 16
HELIX 22 22 ASN B 135 LYS B 151 1 17
HELIX 23 23 ALA B 164 ALA B 168 5 5
HELIX 24 24 GLY B 169 ALA B 186 1 18
HELIX 25 25 VAL B 187 ASP B 193 1 7
HELIX 26 26 SER B 197 ARG B 210 1 14
HELIX 27 27 THR B 241 LEU B 255 1 15
HELIX 28 28 PRO B 290 SER B 300 1 11
HELIX 29 29 ASP B 311 LEU B 319 1 9
HELIX 30 30 THR B 320 THR B 325 1 6
HELIX 31 31 ALA B 358 ALA B 371 1 14
SHEET 1 A 7 LYS A 56 SER A 57 0
SHEET 2 A 7 ASN A 31 THR A 36 1 N THR A 36 O LYS A 56
SHEET 3 A 7 ASN A 3 ILE A 7 1 N VAL A 4 O ASN A 31
SHEET 4 A 7 ILE A 69 THR A 72 1 O VAL A 71 N GLY A 5
SHEET 5 A 7 TYR A 94 ASP A 97 1 O VAL A 96 N ILE A 70
SHEET 6 A 7 THR A 130 GLY A 133 1 O PHE A 131 N TRP A 95
SHEET 7 A 7 ALA A 108 VAL A 111 1 N ILE A 109 O VAL A 132
SHEET 1 B 6 VAL A 264 LEU A 267 0
SHEET 2 B 6 VAL A 154 TYR A 162 1 N VAL A 159 O ASP A 265
SHEET 3 B 6 CYS A 276 LEU A 285 -1 O SER A 278 N TYR A 162
SHEET 4 B 6 TYR A 344 ASP A 352 -1 O ALA A 347 N PHE A 281
SHEET 5 B 6 VAL A 330 LYS A 337 -1 N GLY A 333 O PHE A 348
SHEET 6 B 6 VAL A 305 VAL A 307 1 N LYS A 306 O VAL A 332
SHEET 1 C 2 LEU A 227 ILE A 228 0
SHEET 2 C 2 ARG A 270 ILE A 271 -1 O ARG A 270 N ILE A 228
SHEET 1 D 7 LYS B 56 SER B 57 0
SHEET 2 D 7 ASN B 31 THR B 36 1 N THR B 36 O LYS B 56
SHEET 3 D 7 ASN B 3 ILE B 7 1 N VAL B 4 O VAL B 33
SHEET 4 D 7 ILE B 69 THR B 72 1 O VAL B 71 N GLY B 5
SHEET 5 D 7 TYR B 94 ASP B 97 1 O VAL B 96 N ILE B 70
SHEET 6 D 7 THR B 130 GLY B 133 1 O PHE B 131 N TRP B 95
SHEET 7 D 7 ALA B 108 VAL B 111 1 N ILE B 109 O VAL B 132
SHEET 1 E 6 VAL B 264 LEU B 267 0
SHEET 2 E 6 VAL B 154 TYR B 162 1 N VAL B 159 O LEU B 267
SHEET 3 E 6 CYS B 276 LEU B 285 -1 O ALA B 280 N ALA B 160
SHEET 4 E 6 GLY B 341 ASP B 352 -1 O ALA B 347 N PHE B 281
SHEET 5 E 6 VAL B 330 LEU B 338 -1 N LEU B 338 O TYR B 344
SHEET 6 E 6 VAL B 305 VAL B 307 1 N LYS B 306 O VAL B 332
SHEET 1 F 2 LEU B 227 ILE B 228 0
SHEET 2 F 2 ARG B 270 ILE B 271 -1 O ARG B 270 N ILE B 228
LINK C ASN A 135 N HTI A 136 1555 1555 1.33
LINK C HTI A 136 N THR A 137 1555 1555 1.34
LINK C ASN B 135 N HTI B 136 1555 1555 1.33
LINK C HTI B 136 N THR B 137 1555 1555 1.34
CRYST1 54.614 113.862 57.271 90.00 90.00 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 0.018310 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008783 0.000000 0.00000
SCALE3 0.000000 0.000000 0.017461 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
