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HEADER HYDROLASE 23-OCT-08 2W22
TITLE ACTIVATION MECHANISM OF BACTERIAL THERMOALKALOPHILIC
TITLE 2 LIPASES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TRIACYLGLYCEROL LIPASE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RESIDUES 30-417;
COMPND 5 EC: 3.1.1.3;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: GEOBACILLUS THERMOCATENULATUS;
SOURCE 3 ORGANISM_TAXID: 33938;
SOURCE 4 STRAIN: DSM 730;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: DH5 ALPHA;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PT1;
SOURCE 9 OTHER_DETAILS: GERMAN COLLECTION OF MICROORGANISM (DSM) IN
SOURCE 10 BRAUNSCHWEIG
KEYWDS THERMOALKALOPHILIC LIPASES, HYDROLASE, OPEN CONFORMATION,
KEYWDS 2 ACTIVATION MECHANISM
EXPDTA X-RAY DIFFRACTION
AUTHOR C.CARRASCO-LOPEZ,C.GODOY,B.DE LAS RIVAS,G.FERNANDEZ-LORENTE,
AUTHOR 2 J.M.PALOMO,J.M.GUISAN,R.FERNANDEZ-LAFUENTE,J.A.HERMOSO
REVDAT 1 16-DEC-08 2W22 0
JRNL AUTH C.CARRASCO-LOPEZ,C.GODOY,B.DE LAS RIVAS,
JRNL AUTH 2 G.FERNANDEZ-LORENTE,J.M.PALOMO,J.M.GUISAN,
JRNL AUTH 3 R.FERNANDEZ-LAFUENTE,M.MARTINEZ-RIPOLL,J.A.HERMOSO
JRNL TITL ACTIVATION OF BACTERIAL THERMOALKALOPHILIC LIPASES
JRNL TITL 2 IS SPURRED BY DRAMATIC STRUCTURAL REARRANGEMENTS.
JRNL REF TO BE PUBLISHED
JRNL REFN
JRNL PMID 19056729
JRNL DOI 10.1074/JBC.M808268200
REMARK 2
REMARK 2 RESOLUTION. 2.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.2
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) : 2.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 45.18
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 2772100.41
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 30176
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) : 0.182
REMARK 3 FREE R VALUE : 0.226
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 7.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2112
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) : 2.20
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.34
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 85.90
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2840
REMARK 3 BIN FREE R VALUE : 0.3060
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 7.50
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.017
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3056
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 62
REMARK 3 SOLVENT ATOMS : 531
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 20.20
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 29.20
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -5.21000
REMARK 3 B22 (A**2) : 4.46000
REMARK 3 B33 (A**2) : 0.74000
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) : 0.27
REMARK 3 ESD FROM SIGMAA (A) : 0.31
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) : 0.32
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.32
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.005
REMARK 3 BOND ANGLES (DEGREES) : 1.20
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 22.80
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.76
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 : 56.08
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 : ION.PARAM
REMARK 3 PARAMETER FILE 3 : EGC_MOD.PAR
REMARK 3 PARAMETER FILE 4 : MPD_XPLOR.PAR
REMARK 3 PARAMETER FILE 5 : WATER_REP.PARAM
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : ION.TOP
REMARK 3 TOPOLOGY FILE 3 : WATER_REP.TOP
REMARK 3 TOPOLOGY FILE 4 : EGC_MOD.TOP
REMARK 3 TOPOLOGY FILE 5 : MPD_XPLOR.TOP
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: BULK SOLVENT MODEL USED
REMARK 4
REMARK 4 2W22 COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 23-OCT-08.
REMARK 100 THE PDBE ID CODE IS EBI-37947.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 21-APR-08
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : BM16
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.979234
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 37406
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.20
REMARK 200 RESOLUTION RANGE LOW (A) : 63.75
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NONE
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 4.1
REMARK 200 R MERGE (I) : 0.14
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 8.90
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.36
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 4.5
REMARK 200 R MERGE FOR SHELL (I) : 0.48
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.50
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 1JI3
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 62.36
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.27
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: SODIUM CITRATE 0.05 M, PH 5.6,
REMARK 280 MPD 13 % AND AMMONIUM ACETATE 0.2 M
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -X,Y,-Z
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z+1/2
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 X+1/2,-Y+1/2,-Z+1/2
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 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 36.53500
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 64.04000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 63.74500
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 36.53500
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 64.04000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 63.74500
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 36.53500
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 64.04000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 63.74500
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 36.53500
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 64.04000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 63.74500
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 GENERATING THE BIOMOLECULE
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: PQS
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 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 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 PRO A 199 C - N - CA ANGL. DEV. = 9.4 DEGREES
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 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 3 81.96 65.70
REMARK 500 PRO A 4 -174.99 -65.46
REMARK 500 LEU A 99 58.99 -142.06
REMARK 500 SER A 114 -123.73 44.32
REMARK 500 PHE A 181 -102.54 -123.85
REMARK 500 PRO A 199 -77.44 -31.22
REMARK 500 ARG A 272 45.28 -146.62
REMARK 500 ASN A 305 74.40 -158.26
REMARK 500 ASP A 311 -166.93 -101.33
REMARK 500 ILE A 320 -39.79 -132.87
REMARK 500 LYS A 330 -42.48 -136.69
REMARK 500 ASN A 368 80.49 -170.04
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 600
REMARK 600 HETEROGEN
REMARK 600 4S-2-METHYL-2,4-PENTANEDIOL (MPD): THIS COME FROM
REMARK 600 CRYSTALLIZATION CONDITIONS
REMARK 600 FRAGMENTS OF TRITON X-100 (EGC): TWO FRAGMENTS OF DIFFERENT
REMARK 600 SIZE ARE PRESENT IN THE STRUCTURE FROM PURIFICATION
REMARK 600 PROCEDURE.
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 EGC A 403
REMARK 610 EGC A 404
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 402 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 62 OD1
REMARK 620 2 HIS A 82 NE2 95.9
REMARK 620 3 HIS A 88 NE2 112.8 105.8
REMARK 620 4 ASP A 239 OD2 127.9 110.0 102.7
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EGC A 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EGC A 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MPD A 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MPD A 406
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MPD A 407
DBREF 2W22 A 1 1 PDB 2W22 2W22 1 1
DBREF 2W22 A 2 389 UNP Q59260 Q59260_9BACI 30 417
SEQADV 2W22 TYR A 355 UNP Q59260 CYS 383 CONFLICT
SEQRES 1 A 389 MET ALA SER PRO ARG ALA ASN ASP ALA PRO ILE VAL LEU
SEQRES 2 A 389 LEU HIS GLY PHE THR GLY TRP GLY ARG GLU GLU MET LEU
SEQRES 3 A 389 GLY PHE LYS TYR TRP GLY GLY VAL ARG GLY ASP ILE GLU
SEQRES 4 A 389 GLN TRP LEU ASN ASP ASN GLY TYR ARG THR TYR THR LEU
SEQRES 5 A 389 ALA VAL GLY PRO LEU SER SER ASN TRP ASP ARG ALA CYS
SEQRES 6 A 389 GLU ALA TYR ALA GLN LEU VAL GLY GLY THR VAL ASP TYR
SEQRES 7 A 389 GLY ALA ALA HIS ALA ALA LYS HIS GLY HIS ALA ARG PHE
SEQRES 8 A 389 GLY ARG THR TYR PRO GLY LEU LEU PRO GLU LEU LYS ARG
SEQRES 9 A 389 GLY GLY ARG VAL HIS ILE ILE ALA HIS SER GLN GLY GLY
SEQRES 10 A 389 GLN THR ALA ARG MET LEU VAL SER LEU LEU GLU ASN GLY
SEQRES 11 A 389 SER GLN GLU GLU ARG GLU TYR ALA LYS ALA HIS ASN VAL
SEQRES 12 A 389 SER LEU SER PRO LEU PHE GLU GLY GLY HIS HIS PHE VAL
SEQRES 13 A 389 LEU SER VAL THR THR ILE ALA THR PRO HIS ASP GLY THR
SEQRES 14 A 389 THR LEU VAL ASN MET VAL ASP PHE THR ASP ARG PHE PHE
SEQRES 15 A 389 ASP LEU GLN LYS ALA VAL LEU LYS ALA ALA ALA VAL ALA
SEQRES 16 A 389 SER ASN VAL PRO TYR THR SER GLN VAL TYR ASP PHE LYS
SEQRES 17 A 389 LEU ASP GLN TRP GLY LEU ARG ARG GLN PRO GLY GLU SER
SEQRES 18 A 389 PHE ASP HIS TYR PHE GLU ARG LEU LYS ARG SER PRO VAL
SEQRES 19 A 389 TRP THR SER THR ASP THR ALA ARG TYR ASP LEU SER ILE
SEQRES 20 A 389 PRO GLY ALA GLU LYS LEU ASN GLN TRP VAL GLN ALA SER
SEQRES 21 A 389 PRO ASN THR TYR TYR LEU SER PHE SER THR GLU ARG THR
SEQRES 22 A 389 HIS ARG GLY ALA LEU THR GLY ASN TYR TYR PRO GLU LEU
SEQRES 23 A 389 GLY MET ASN ALA PHE SER ALA VAL VAL CYS ALA PRO PHE
SEQRES 24 A 389 LEU GLY SER TYR ARG ASN GLU ALA LEU GLY ILE ASP ASP
SEQRES 25 A 389 ARG TRP LEU GLU ASN ASP GLY ILE VAL ASN THR VAL SER
SEQRES 26 A 389 MET ASN GLY PRO LYS ARG GLY SER SER ASP ARG ILE VAL
SEQRES 27 A 389 PRO TYR ASP GLY THR LEU LYS LYS GLY VAL TRP ASN ASP
SEQRES 28 A 389 MET GLY THR TYR ASN VAL ASP HIS LEU GLU VAL ILE GLY
SEQRES 29 A 389 VAL ASP PRO ASN PRO SER PHE ASP ILE ARG ALA PHE TYR
SEQRES 30 A 389 LEU ARG LEU ALA GLU GLN LEU ALA SER LEU ARG PRO
HET CA A 401 1
HET ZN A 402 1
HET EGC A 403 20
HET EGC A 404 16
HET MPD A 405 8
HET MPD A 406 8
HET MPD A 407 8
HETNAM MPD (4S)-2-METHYL-2,4-PENTANEDIOL
HETNAM ZN ZINC ION
HETNAM CA CALCIUM ION
HETNAM EGC 2-(2-{2-[2-(2-{2-[2-(2-{2-[4-(1,1,3,3-
HETNAM 2 EGC TETRAMETHYL-BUTYL)-PHENOXY]-ETHOXY}-ETHOXY)-ETHOXY]-
HETNAM 3 EGC ETHOXY}-ETHOXY)-ETHOXY]-ETHOXY}-ETHOXY)-
HETNAM 4 EGC ETHANOL
FORMUL 2 MPD 3(C6 H14 O2)
FORMUL 3 ZN ZN 2+
FORMUL 4 CA CA 2+
FORMUL 5 EGC 2(C32 H58 O10)
FORMUL 6 HOH *531(H2 O1)
HELIX 1 1 GLU A 24 PHE A 28 5 5
HELIX 2 2 GLY A 32 GLY A 36 5 5
HELIX 3 3 ASP A 37 ASN A 45 1 9
HELIX 4 4 SER A 59 GLY A 73 1 15
HELIX 5 5 GLY A 79 GLY A 87 1 9
HELIX 6 6 LEU A 99 GLY A 105 5 7
HELIX 7 7 GLN A 115 GLY A 130 1 16
HELIX 8 8 SER A 131 ASN A 142 1 12
HELIX 9 9 SER A 146 GLU A 150 5 5
HELIX 10 10 THR A 170 ASP A 179 1 10
HELIX 11 11 ASP A 183 SER A 196 1 14
HELIX 12 12 TYR A 200 TYR A 205 1 6
HELIX 13 13 LEU A 209 GLY A 213 5 5
HELIX 14 14 SER A 221 ARG A 231 1 11
HELIX 15 15 SER A 232 SER A 237 5 6
HELIX 16 16 THR A 240 SER A 246 1 7
HELIX 17 17 SER A 246 VAL A 257 1 12
HELIX 18 18 ASN A 289 CYS A 296 1 8
HELIX 19 19 CYS A 296 GLY A 301 1 6
HELIX 20 20 GLU A 306 GLY A 309 5 4
HELIX 21 21 ASP A 311 LEU A 315 5 5
HELIX 22 22 THR A 323 MET A 326 5 4
HELIX 23 23 LEU A 360 GLY A 364 5 5
HELIX 24 24 ASP A 372 SER A 386 1 15
SHEET 1 AA 7 THR A 49 LEU A 52 0
SHEET 2 AA 7 ILE A 11 LEU A 14 1 O ILE A 11 N TYR A 50
SHEET 3 AA 7 VAL A 108 HIS A 113 1 O HIS A 109 N VAL A 12
SHEET 4 AA 7 VAL A 156 ILE A 162 1 N LEU A 157 O VAL A 108
SHEET 5 AA 7 TYR A 264 THR A 270 1 O TYR A 264 N VAL A 159
SHEET 6 AA 7 TRP A 349 TYR A 355 1 O ASN A 350 N SER A 267
SHEET 7 AA 7 ILE A 337 PRO A 339 1 O VAL A 338 N ASP A 351
SHEET 1 AB 2 GLY A 74 ASP A 77 0
SHEET 2 AB 2 PHE A 91 TYR A 95 -1 N GLY A 92 O VAL A 76
SHEET 1 AC 2 THR A 273 ARG A 275 0
SHEET 2 AC 2 TYR A 282 PRO A 284 -1 O TYR A 283 N HIS A 274
LINK ZN ZN A 402 OD1 ASP A 62 1555 1555 2.13
LINK ZN ZN A 402 NE2 HIS A 82 1555 1555 2.21
LINK ZN ZN A 402 NE2 HIS A 88 1555 1555 2.29
LINK ZN ZN A 402 OD2 ASP A 239 1555 1555 2.11
SITE 1 AC1 5 GLY A 287 GLU A 361 ASP A 366 PRO A 367
SITE 2 AC1 5 HOH A2528
SITE 1 AC2 4 ASP A 62 HIS A 82 HIS A 88 ASP A 239
SITE 1 AC3 14 PHE A 17 LEU A 57 SER A 114 GLN A 115
SITE 2 AC3 14 LEU A 184 GLN A 185 VAL A 188 LEU A 189
SITE 3 AC3 14 THR A 240 ARG A 242 LEU A 245 ILE A 320
SITE 4 AC3 14 HIS A 359 HOH A2529
SITE 1 AC4 7 PHE A 17 THR A 18 MET A 174 THR A 178
SITE 2 AC4 7 LEU A 184 LEU A 360 HOH A2530
SITE 1 AC5 3 THR A 18 TYR A 205 PHE A 207
SITE 1 AC6 7 LYS A 139 ASN A 142 VAL A 143 GLU A 306
SITE 2 AC6 7 ALA A 307 GLY A 309 HOH A2299
SITE 1 AC7 4 ASN A 197 ARG A 216 VAL A 294 HOH A2531
CRYST1 73.070 128.080 127.490 90.00 90.00 90.00 I 2 2 2 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 0.013686 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007808 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007844 0.00000
TER 3057 PRO A 389
MASTER 355 0 7 24 11 0 13 6 3649 1 65 30
END |