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HEADER HYDROLASE 23-JUL-12 4G9E
TITLE CRYSTAL STRUCTURES OF N-ACYL HOMOSERINE LACTONASE AIDH COMPLEXED WITH
TITLE 2 N-BUTANOYL HOMOSERINE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ALPHA/BETA HYDROLASE FOLD PROTEIN;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: AHL-LACTONASE;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: OCHROBACTRUM;
SOURCE 3 ORGANISM_TAXID: 680275;
SOURCE 4 STRAIN: T63;
SOURCE 5 GENE: AIDH;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS ALPHA/BETA-HYDROLASE FOLD, AHL-LACTONASE, AHL-BINDING, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR D.C.LIANG,X.X.YAN,A.GAO
REVDAT 1 16-JAN-13 4G9E 0
JRNL AUTH A.GAO,G.Y.MEI,S.LIU,P.WANG,Q.TANG,Y.P.LIU,H.WEN,X.M.AN,
JRNL AUTH 2 L.Q.ZHANG,X.X.YAN,D.C.LIANG
JRNL TITL HIGH-RESOLUTION STRUCTURES OF AIDH COMPLEXES PROVIDE
JRNL TITL 2 INSIGHTS INTO A NOVEL CATALYTIC MECHANISM FOR N-ACYL
JRNL TITL 3 HOMOSERINE LACTONASE
JRNL REF ACTA CRYSTALLOGR.,SECT.D V. 69 82 2013
JRNL REFN ISSN 0907-4449
JRNL PMID 23275166
JRNL DOI 10.1107/S0907444912042369
REMARK 2
REMARK 2 RESOLUTION. 1.09 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.6.4_486)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-
REMARK 3 : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,
REMARK 3 : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL
REMARK 3 : MORIARTY,REETAL PAI,RANDY READ,JANE
REMARK 3 : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM
REMARK 3 : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,
REMARK 3 : LAURENT STORONI,TOM TERWILLIGER,PETER
REMARK 3 : ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.09
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 21.29
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.3
REMARK 3 NUMBER OF REFLECTIONS : 179678
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.129
REMARK 3 R VALUE (WORKING SET) : 0.127
REMARK 3 FREE R VALUE : 0.152
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.970
REMARK 3 FREE R VALUE TEST SET COUNT : 8930
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 21.2940 - 2.3440 0.94 16589 858 0.1374 0.1536
REMARK 3 2 2.3440 - 1.8609 0.99 17436 902 0.1211 0.1467
REMARK 3 3 1.8609 - 1.6257 1.00 17457 928 0.1114 0.1448
REMARK 3 4 1.6257 - 1.4771 0.99 17389 939 0.1016 0.1259
REMARK 3 5 1.4771 - 1.3713 0.99 17313 901 0.1058 0.1409
REMARK 3 6 1.3713 - 1.2904 0.98 17176 925 0.1110 0.1474
REMARK 3 7 1.2904 - 1.2258 0.98 17134 855 0.1166 0.1428
REMARK 3 8 1.2258 - 1.1725 0.97 16990 910 0.1339 0.1620
REMARK 3 9 1.1725 - 1.1273 0.96 16947 903 0.1661 0.1853
REMARK 3 10 1.1273 - 1.0884 0.93 16317 809 0.2232 0.2423
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 0.40
REMARK 3 SHRINKAGE RADIUS : 0.04
REMARK 3 K_SOL : 0.54
REMARK 3 B_SOL : 148.83
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.100
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 13.950
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 7.83
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 15.56
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 2.57270
REMARK 3 B22 (A**2) : -2.74080
REMARK 3 B33 (A**2) : -0.56360
REMARK 3 B12 (A**2) : -0.00000
REMARK 3 B13 (A**2) : 0.01200
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.005 4616
REMARK 3 ANGLE : 1.049 6290
REMARK 3 CHIRALITY : 0.073 657
REMARK 3 PLANARITY : 0.005 849
REMARK 3 DIHEDRAL : 12.031 1749
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4G9E COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 08-AUG-12.
REMARK 100 THE RCSB ID CODE IS RCSB073903.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 22-JUN-11
REMARK 200 TEMPERATURE (KELVIN) : 180
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRF
REMARK 200 BEAMLINE : BL17U
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9
REMARK 200 MONOCHROMATOR : GRAPHITE
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 179801
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.088
REMARK 200 RESOLUTION RANGE LOW (A) : 21.290
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 52.1
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.09
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.12
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
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 FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHENIX
REMARK 200 STARTING MODEL: 4G5X
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 33.24
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.84
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 25% PEG8000, 0.2M AMMONIUM ACETATE,
REMARK 280 0.01M MAGNESIUM ACETATE, 0.05M SODIUM CACODYLATE, 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 64.76150
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 A 1
REMARK 465 HIS A 277
REMARK 465 HIS A 278
REMARK 465 HIS A 279
REMARK 465 MET B 1
REMARK 465 THR B 2
REMARK 465 HIS B 277
REMARK 465 HIS B 278
REMARK 465 HIS B 279
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 ARG A 155 CG CD NE CZ NH1 NH2
REMARK 470 GLU B 47 OE2
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 ASP B 70 CB ASP B 70 CG -0.184
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 SER A 35 -154.71 -105.88
REMARK 500 SER A 102 -114.61 64.06
REMARK 500 ASN A 234 77.15 -151.17
REMARK 500 SER B 35 -155.42 -104.89
REMARK 500 SER B 102 -113.11 63.34
REMARK 500 GLU B 219 116.39 -38.93
REMARK 500 ASN B 234 79.28 -154.86
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 A 621 DISTANCE = 9.77 ANGSTROMS
REMARK 525 HOH A 624 DISTANCE = 8.56 ANGSTROMS
REMARK 525 HOH A 646 DISTANCE = 5.85 ANGSTROMS
REMARK 525 HOH A 663 DISTANCE = 9.70 ANGSTROMS
REMARK 525 HOH A 666 DISTANCE = 5.05 ANGSTROMS
REMARK 525 HOH A 693 DISTANCE = 5.15 ANGSTROMS
REMARK 525 HOH A 698 DISTANCE = 8.56 ANGSTROMS
REMARK 525 HOH A 744 DISTANCE = 5.33 ANGSTROMS
REMARK 525 HOH A 745 DISTANCE = 5.19 ANGSTROMS
REMARK 525 HOH A 767 DISTANCE = 7.71 ANGSTROMS
REMARK 525 HOH A 778 DISTANCE = 5.76 ANGSTROMS
REMARK 525 HOH A 786 DISTANCE = 7.15 ANGSTROMS
REMARK 525 HOH A 789 DISTANCE = 6.62 ANGSTROMS
REMARK 525 HOH A 798 DISTANCE = 6.99 ANGSTROMS
REMARK 525 HOH A 799 DISTANCE = 7.34 ANGSTROMS
REMARK 525 HOH A 812 DISTANCE = 9.59 ANGSTROMS
REMARK 525 HOH A 813 DISTANCE = 6.12 ANGSTROMS
REMARK 525 HOH A 819 DISTANCE = 5.83 ANGSTROMS
REMARK 525 HOH A 821 DISTANCE = 9.19 ANGSTROMS
REMARK 525 HOH A 822 DISTANCE = 6.21 ANGSTROMS
REMARK 525 HOH A 825 DISTANCE = 9.77 ANGSTROMS
REMARK 525 HOH A 826 DISTANCE = 8.10 ANGSTROMS
REMARK 525 HOH A 827 DISTANCE = 5.23 ANGSTROMS
REMARK 525 HOH A 830 DISTANCE = 5.29 ANGSTROMS
REMARK 525 HOH A 840 DISTANCE = 6.31 ANGSTROMS
REMARK 525 HOH A 841 DISTANCE = 6.11 ANGSTROMS
REMARK 525 HOH A 883 DISTANCE = 5.53 ANGSTROMS
REMARK 525 HOH B 626 DISTANCE = 7.28 ANGSTROMS
REMARK 525 HOH B 668 DISTANCE = 7.40 ANGSTROMS
REMARK 525 HOH B 747 DISTANCE = 7.74 ANGSTROMS
REMARK 525 HOH B 748 DISTANCE = 8.25 ANGSTROMS
REMARK 525 HOH B 759 DISTANCE = 5.14 ANGSTROMS
REMARK 525 HOH B 765 DISTANCE = 5.76 ANGSTROMS
REMARK 525 HOH B 766 DISTANCE = 9.55 ANGSTROMS
REMARK 525 HOH B 767 DISTANCE = 6.46 ANGSTROMS
REMARK 525 HOH B 768 DISTANCE = 7.98 ANGSTROMS
REMARK 525 HOH B 780 DISTANCE = 7.00 ANGSTROMS
REMARK 525 HOH B 781 DISTANCE = 5.94 ANGSTROMS
REMARK 525 HOH B 792 DISTANCE = 5.26 ANGSTROMS
REMARK 525 HOH B 794 DISTANCE = 6.39 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE C4L A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE C4L B 301
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4G5X RELATED DB: PDB
REMARK 900 RELATED ID: 4G8B RELATED DB: PDB
REMARK 900 RELATED ID: 4G8C RELATED DB: PDB
REMARK 900 RELATED ID: 4G8D RELATED DB: PDB
REMARK 900 RELATED ID: 4G9G RELATED DB: PDB
DBREF 4G9E A 1 271 UNP D2J2T6 D2J2T6_9RHIZ 1 271
DBREF 4G9E B 1 271 UNP D2J2T6 D2J2T6_9RHIZ 1 271
SEQADV 4G9E LEU A 272 UNP D2J2T6 EXPRESSION TAG
SEQADV 4G9E GLU A 273 UNP D2J2T6 EXPRESSION TAG
SEQADV 4G9E HIS A 274 UNP D2J2T6 EXPRESSION TAG
SEQADV 4G9E HIS A 275 UNP D2J2T6 EXPRESSION TAG
SEQADV 4G9E HIS A 276 UNP D2J2T6 EXPRESSION TAG
SEQADV 4G9E HIS A 277 UNP D2J2T6 EXPRESSION TAG
SEQADV 4G9E HIS A 278 UNP D2J2T6 EXPRESSION TAG
SEQADV 4G9E HIS A 279 UNP D2J2T6 EXPRESSION TAG
SEQADV 4G9E LEU B 272 UNP D2J2T6 EXPRESSION TAG
SEQADV 4G9E GLU B 273 UNP D2J2T6 EXPRESSION TAG
SEQADV 4G9E HIS B 274 UNP D2J2T6 EXPRESSION TAG
SEQADV 4G9E HIS B 275 UNP D2J2T6 EXPRESSION TAG
SEQADV 4G9E HIS B 276 UNP D2J2T6 EXPRESSION TAG
SEQADV 4G9E HIS B 277 UNP D2J2T6 EXPRESSION TAG
SEQADV 4G9E HIS B 278 UNP D2J2T6 EXPRESSION TAG
SEQADV 4G9E HIS B 279 UNP D2J2T6 EXPRESSION TAG
SEQRES 1 A 279 MET THR ILE ASN TYR HIS GLU LEU GLU THR SER HIS GLY
SEQRES 2 A 279 ARG ILE ALA VAL ARG GLU SER GLU GLY GLU GLY ALA PRO
SEQRES 3 A 279 LEU LEU MET ILE HIS GLY ASN SER SER SER GLY ALA ILE
SEQRES 4 A 279 PHE ALA PRO GLN LEU GLU GLY GLU ILE GLY LYS LYS TRP
SEQRES 5 A 279 ARG VAL ILE ALA PRO ASP LEU PRO GLY HIS GLY LYS SER
SEQRES 6 A 279 THR ASP ALA ILE ASP PRO ASP ARG SER TYR SER MET GLU
SEQRES 7 A 279 GLY TYR ALA ASP ALA MET THR GLU VAL MET GLN GLN LEU
SEQRES 8 A 279 GLY ILE ALA ASP ALA VAL VAL PHE GLY TRP SER LEU GLY
SEQRES 9 A 279 GLY HIS ILE GLY ILE GLU MET ILE ALA ARG TYR PRO GLU
SEQRES 10 A 279 MET ARG GLY LEU MET ILE THR GLY THR PRO PRO VAL ALA
SEQRES 11 A 279 ARG GLU GLU VAL GLY GLN GLY PHE LYS SER GLY PRO ASP
SEQRES 12 A 279 MET ALA LEU ALA GLY GLN GLU ILE PHE SER GLU ARG ASP
SEQRES 13 A 279 VAL GLU SER TYR ALA ARG SER THR CYS GLY GLU PRO PHE
SEQRES 14 A 279 GLU ALA SER LEU LEU ASP ILE VAL ALA ARG THR ASP GLY
SEQRES 15 A 279 ARG ALA ARG ARG ILE MET PHE GLU LYS PHE GLY SER GLY
SEQRES 16 A 279 THR GLY GLY ASN GLN ARG ASP ILE VAL ALA GLU ALA GLN
SEQRES 17 A 279 LEU PRO ILE ALA VAL VAL ASN GLY ARG ASP GLU PRO PHE
SEQRES 18 A 279 VAL GLU LEU ASP PHE VAL SER LYS VAL LYS PHE GLY ASN
SEQRES 19 A 279 LEU TRP GLU GLY LYS THR HIS VAL ILE ASP ASN ALA GLY
SEQRES 20 A 279 HIS ALA PRO PHE ARG GLU ALA PRO ALA GLU PHE ASP ALA
SEQRES 21 A 279 TYR LEU ALA ARG PHE ILE ARG ASP CYS THR GLN LEU GLU
SEQRES 22 A 279 HIS HIS HIS HIS HIS HIS
SEQRES 1 B 279 MET THR ILE ASN TYR HIS GLU LEU GLU THR SER HIS GLY
SEQRES 2 B 279 ARG ILE ALA VAL ARG GLU SER GLU GLY GLU GLY ALA PRO
SEQRES 3 B 279 LEU LEU MET ILE HIS GLY ASN SER SER SER GLY ALA ILE
SEQRES 4 B 279 PHE ALA PRO GLN LEU GLU GLY GLU ILE GLY LYS LYS TRP
SEQRES 5 B 279 ARG VAL ILE ALA PRO ASP LEU PRO GLY HIS GLY LYS SER
SEQRES 6 B 279 THR ASP ALA ILE ASP PRO ASP ARG SER TYR SER MET GLU
SEQRES 7 B 279 GLY TYR ALA ASP ALA MET THR GLU VAL MET GLN GLN LEU
SEQRES 8 B 279 GLY ILE ALA ASP ALA VAL VAL PHE GLY TRP SER LEU GLY
SEQRES 9 B 279 GLY HIS ILE GLY ILE GLU MET ILE ALA ARG TYR PRO GLU
SEQRES 10 B 279 MET ARG GLY LEU MET ILE THR GLY THR PRO PRO VAL ALA
SEQRES 11 B 279 ARG GLU GLU VAL GLY GLN GLY PHE LYS SER GLY PRO ASP
SEQRES 12 B 279 MET ALA LEU ALA GLY GLN GLU ILE PHE SER GLU ARG ASP
SEQRES 13 B 279 VAL GLU SER TYR ALA ARG SER THR CYS GLY GLU PRO PHE
SEQRES 14 B 279 GLU ALA SER LEU LEU ASP ILE VAL ALA ARG THR ASP GLY
SEQRES 15 B 279 ARG ALA ARG ARG ILE MET PHE GLU LYS PHE GLY SER GLY
SEQRES 16 B 279 THR GLY GLY ASN GLN ARG ASP ILE VAL ALA GLU ALA GLN
SEQRES 17 B 279 LEU PRO ILE ALA VAL VAL ASN GLY ARG ASP GLU PRO PHE
SEQRES 18 B 279 VAL GLU LEU ASP PHE VAL SER LYS VAL LYS PHE GLY ASN
SEQRES 19 B 279 LEU TRP GLU GLY LYS THR HIS VAL ILE ASP ASN ALA GLY
SEQRES 20 B 279 HIS ALA PRO PHE ARG GLU ALA PRO ALA GLU PHE ASP ALA
SEQRES 21 B 279 TYR LEU ALA ARG PHE ILE ARG ASP CYS THR GLN LEU GLU
SEQRES 22 B 279 HIS HIS HIS HIS HIS HIS
HET C4L A 301 13
HET C4L B 301 13
HETNAM C4L N-BUTANOYL-L-HOMOSERINE
FORMUL 3 C4L 2(C8 H15 N O4)
FORMUL 5 HOH *937(H2 O)
HELIX 1 1 SER A 36 ILE A 39 5 4
HELIX 2 2 PHE A 40 GLY A 46 1 7
HELIX 3 3 GLY A 46 LYS A 51 1 6
HELIX 4 4 ASP A 70 TYR A 75 1 6
HELIX 5 5 SER A 76 GLY A 92 1 17
HELIX 6 6 SER A 102 ILE A 112 1 11
HELIX 7 7 ALA A 130 GLU A 132 5 3
HELIX 8 8 GLU A 133 PHE A 138 1 6
HELIX 9 9 ASP A 143 GLN A 149 5 7
HELIX 10 10 SER A 153 GLY A 166 1 14
HELIX 11 11 GLU A 170 THR A 180 1 11
HELIX 12 12 ASP A 181 GLY A 195 1 15
HELIX 13 13 ASN A 199 ALA A 207 1 9
HELIX 14 14 GLU A 223 SER A 228 1 6
HELIX 15 15 LEU A 235 LYS A 239 5 5
HELIX 16 16 ALA A 249 ALA A 254 1 6
HELIX 17 17 ALA A 254 GLN A 271 1 18
HELIX 18 18 SER B 36 ILE B 39 5 4
HELIX 19 19 PHE B 40 GLY B 46 1 7
HELIX 20 20 GLY B 46 LYS B 51 1 6
HELIX 21 21 ASP B 70 TYR B 75 1 6
HELIX 22 22 SER B 76 GLY B 92 1 17
HELIX 23 23 SER B 102 TYR B 115 1 14
HELIX 24 24 ALA B 130 GLU B 132 5 3
HELIX 25 25 GLU B 133 PHE B 138 1 6
HELIX 26 26 GLY B 141 ALA B 147 1 7
HELIX 27 27 SER B 153 GLY B 166 1 14
HELIX 28 28 GLU B 170 THR B 180 1 11
HELIX 29 29 ASP B 181 GLY B 195 1 15
HELIX 30 30 ASN B 199 ALA B 207 1 9
HELIX 31 31 GLU B 223 SER B 228 1 6
HELIX 32 32 LEU B 235 LYS B 239 5 5
HELIX 33 33 ALA B 249 ALA B 254 1 6
HELIX 34 34 ALA B 254 LEU B 272 1 19
SHEET 1 A 8 ASN A 4 THR A 10 0
SHEET 2 A 8 GLY A 13 GLU A 19 -1 O GLU A 19 N ASN A 4
SHEET 3 A 8 TRP A 52 PRO A 57 -1 O ALA A 56 N ARG A 18
SHEET 4 A 8 GLY A 24 ILE A 30 1 N LEU A 27 O ILE A 55
SHEET 5 A 8 VAL A 97 TRP A 101 1 O PHE A 99 N LEU A 28
SHEET 6 A 8 GLY A 120 THR A 124 1 O MET A 122 N GLY A 100
SHEET 7 A 8 ILE A 211 GLY A 216 1 O ALA A 212 N ILE A 123
SHEET 8 A 8 HIS A 241 ILE A 243 1 O HIS A 241 N VAL A 213
SHEET 1 B 8 ASN B 4 THR B 10 0
SHEET 2 B 8 GLY B 13 GLU B 19 -1 O VAL B 17 N HIS B 6
SHEET 3 B 8 TRP B 52 PRO B 57 -1 O ALA B 56 N ARG B 18
SHEET 4 B 8 GLY B 24 ILE B 30 1 N LEU B 27 O ILE B 55
SHEET 5 B 8 VAL B 97 TRP B 101 1 O PHE B 99 N LEU B 28
SHEET 6 B 8 GLY B 120 THR B 124 1 O MET B 122 N GLY B 100
SHEET 7 B 8 ILE B 211 GLY B 216 1 O ALA B 212 N ILE B 123
SHEET 8 B 8 HIS B 241 ILE B 243 1 O HIS B 241 N VAL B 213
CISPEP 1 GLU A 167 PRO A 168 0 4.00
CISPEP 2 GLU B 167 PRO B 168 0 3.71
SITE 1 AC1 10 GLY A 32 ASN A 33 SER A 102 LEU A 103
SITE 2 AC1 10 MET A 144 ALA A 147 TYR A 160 PHE A 221
SITE 3 AC1 10 HIS A 248 HOH A 457
SITE 1 AC2 12 GLY B 32 ASN B 33 SER B 102 LEU B 103
SITE 2 AC2 12 MET B 144 ALA B 147 TYR B 160 MET B 188
SITE 3 AC2 12 PHE B 189 PHE B 221 HIS B 248 HOH B 576
CRYST1 42.164 129.523 44.312 90.00 111.00 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 0.023717 0.000000 0.009104 0.00000
SCALE2 0.000000 0.007721 0.000000 0.00000
SCALE3 0.000000 0.000000 0.024173 0.00000
TER 2194 HIS A 276
TER 4484 HIS B 276
MASTER 336 0 2 34 16 0 6 6 5179 2 26 44
END |