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HEADER HYDROLASE 17-NOV-08 3FAK
TITLE STRUCTURAL AND FUNCTIONAL ANALYSIS OF A HORMONE-SENSITIVE
TITLE 2 LIPASE LIKE ESTE5 FROM A METAGENOME LIBRARY
CAVEAT 3FAK CHIRALITY ERROR AT CA CENTER OF ALA A 195
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ESTERASE/LIPASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: ESTE5;
COMPND 5 EC: 3.1.1.-;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: UNCULTURED BACTERIUM;
SOURCE 3 ORGANISM_TAXID: 77133;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: VECTOR;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET-21A;
SOURCE 9 OTHER_DETAILS: SOIL METAGGENOME LIBRARY
KEYWDS HSL, ESTE5, ESTERASE, LIPASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR K.Y.HWANG,K.H.NAM
REVDAT 1 10-FEB-09 3FAK 0
JRNL AUTH K.H.NAM,M.-Y.KIM,S.-J.KIM,A.PRIYADARSHI,W.H.LEE,
JRNL AUTH 2 K.Y.HWANG
JRNL TITL STRUCTURAL AND FUNCTIONAL ANALYSIS OF A NOVEL
JRNL TITL 2 ESTE5 BELONGING TO THE SUBFAMILY OF
JRNL TITL 3 HORMONE-SENSITIVE LIPASE
JRNL REF BIOCHEM.BIOPHYS.RES.COMMUN. V. 379 553 2009
JRNL REFN ISSN 0006-291X
JRNL PMID 19116143
JRNL DOI 10.1016/J.BBRC.2008.12.085
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 1.90 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 : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.79
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) (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 20076
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) : 0.214
REMARK 3 FREE R VALUE : 0.243
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 2206
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2241
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 2
REMARK 3 SOLVENT ATOMS : 195
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.011
REMARK 3 BOND ANGLES (DEGREES) : 2.10
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
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 : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : NULL
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 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE RESIDUES 194-197 ARE WITH HIGH
REMARK 3 RMSD, BUT THEY WERE BUILT DEPENDING ON ELECTRON-DENSITY MAP
REMARK 4
REMARK 4 3FAK COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 20-NOV-08.
REMARK 100 THE RCSB ID CODE IS RCSB050352.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 13-NOV-08
REMARK 200 TEMPERATURE (KELVIN) : 180
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PHOTON FACTORY
REMARK 200 BEAMLINE : BL-17A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.000
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 270
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 20076
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.9
REMARK 200 DATA REDUNDANCY : 5.600
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) : 1.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.97
REMARK 200 COMPLETENESS FOR SHELL (%) : 82.1
REMARK 200 DATA REDUNDANCY IN SHELL : 2.50
REMARK 200 R MERGE FOR SHELL (I) : 0.23200
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.520
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 2C7B
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 38.61
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.00
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M TRIS-HCL PH 7.5, 2.2M AMMONIUM
REMARK 280 SULFATE, 0.2M LITHIUM SULFATE, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 295K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y+1/2,X+1/2,Z+1/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+3/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+1/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+3/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-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 74.64100
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 30.49800
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 30.49800
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 37.32050
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 30.49800
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 30.49800
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 111.96150
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 30.49800
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 30.49800
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 37.32050
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 30.49800
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 30.49800
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 111.96150
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 74.64100
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: 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 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 -12
REMARK 465 ALA A -11
REMARK 465 SER A -10
REMARK 465 MET A -9
REMARK 465 THR A -8
REMARK 465 GLY A -7
REMARK 465 GLY A -6
REMARK 465 GLN A -5
REMARK 465 GLN A -4
REMARK 465 MET A -3
REMARK 465 GLY A -2
REMARK 465 ARG A -1
REMARK 465 GLY A 0
REMARK 465 LEU A 298
REMARK 465 ALA A 299
REMARK 465 ALA A 300
REMARK 465 ALA A 301
REMARK 465 LEU A 302
REMARK 465 GLU A 303
REMARK 465 HIS A 304
REMARK 465 HIS A 305
REMARK 465 HIS A 306
REMARK 465 HIS A 307
REMARK 465 HIS A 308
REMARK 465 HIS A 309
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 VAL A 46 CG1 - CB - CG2 ANGL. DEV. = 10.3 DEGREES
REMARK 500 ALA A 195 CB - CA - C ANGL. DEV. = -9.4 DEGREES
REMARK 500 ALA A 195 N - CA - CB ANGL. DEV. = -17.4 DEGREES
REMARK 500 ALA A 195 N - CA - C ANGL. DEV. = 55.5 DEGREES
REMARK 500 VAL A 194 CA - C - N ANGL. DEV. = -24.0 DEGREES
REMARK 500 GLY A 197 N - CA - C ANGL. DEV. = -32.2 DEGREES
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 PRO A 115 30.89 -96.21
REMARK 500 SER A 144 -120.46 57.58
REMARK 500 ASP A 237 50.80 -93.07
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 VAL A 194 ALA A 195 -94.36
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 VAL A 194 -21.16
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 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: (11X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500 M RES CSSEQI IMPROPER EXPECTED FOUND DETAILS
REMARK 500 VAL A 194 18.4 L L OUTSIDE RANGE
REMARK 500 ALA A 195 -1.0 L D EXPECTING SP3
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 CL A 310
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 311
DBREF 3FAK A 1 297 UNP Q0GMU2 Q0GMU2_9BACT 1 297
SEQADV 3FAK MET A -12 UNP Q0GMU2 INITIATING METHIONINE
SEQADV 3FAK ALA A -11 UNP Q0GMU2 EXPRESSION TAG
SEQADV 3FAK SER A -10 UNP Q0GMU2 EXPRESSION TAG
SEQADV 3FAK MET A -9 UNP Q0GMU2 EXPRESSION TAG
SEQADV 3FAK THR A -8 UNP Q0GMU2 EXPRESSION TAG
SEQADV 3FAK GLY A -7 UNP Q0GMU2 EXPRESSION TAG
SEQADV 3FAK GLY A -6 UNP Q0GMU2 EXPRESSION TAG
SEQADV 3FAK GLN A -5 UNP Q0GMU2 EXPRESSION TAG
SEQADV 3FAK GLN A -4 UNP Q0GMU2 EXPRESSION TAG
SEQADV 3FAK MET A -3 UNP Q0GMU2 EXPRESSION TAG
SEQADV 3FAK GLY A -2 UNP Q0GMU2 EXPRESSION TAG
SEQADV 3FAK ARG A -1 UNP Q0GMU2 EXPRESSION TAG
SEQADV 3FAK GLY A 0 UNP Q0GMU2 EXPRESSION TAG
SEQADV 3FAK LEU A 298 UNP Q0GMU2 EXPRESSION TAG
SEQADV 3FAK ALA A 299 UNP Q0GMU2 EXPRESSION TAG
SEQADV 3FAK ALA A 300 UNP Q0GMU2 EXPRESSION TAG
SEQADV 3FAK ALA A 301 UNP Q0GMU2 EXPRESSION TAG
SEQADV 3FAK LEU A 302 UNP Q0GMU2 EXPRESSION TAG
SEQADV 3FAK GLU A 303 UNP Q0GMU2 EXPRESSION TAG
SEQADV 3FAK HIS A 304 UNP Q0GMU2 EXPRESSION TAG
SEQADV 3FAK HIS A 305 UNP Q0GMU2 EXPRESSION TAG
SEQADV 3FAK HIS A 306 UNP Q0GMU2 EXPRESSION TAG
SEQADV 3FAK HIS A 307 UNP Q0GMU2 EXPRESSION TAG
SEQADV 3FAK HIS A 308 UNP Q0GMU2 EXPRESSION TAG
SEQADV 3FAK HIS A 309 UNP Q0GMU2 EXPRESSION TAG
SEQRES 1 A 322 MET ALA SER MET THR GLY GLY GLN GLN MET GLY ARG GLY
SEQRES 2 A 322 MET ALA GLY PRO GLU ILE VAL LYS LEU LYS LYS ILE LEU
SEQRES 3 A 322 ARG GLU LYS ALA VAL PRO PRO GLY THR GLU VAL PRO LEU
SEQRES 4 A 322 ASP VAL MET ARG LYS GLY MET GLU LYS VAL ALA PHE LYS
SEQRES 5 A 322 ALA ALA ASP ASP ILE GLN VAL GLU GLN VAL THR VAL ALA
SEQRES 6 A 322 GLY CYS ALA ALA GLU TRP VAL ARG ALA PRO GLY CYS GLN
SEQRES 7 A 322 ALA GLY LYS ALA ILE LEU TYR LEU HIS GLY GLY GLY TYR
SEQRES 8 A 322 VAL MET GLY SER ILE ASN THR HIS ARG SER MET VAL GLY
SEQRES 9 A 322 GLU ILE SER ARG ALA SER GLN ALA ALA ALA LEU LEU LEU
SEQRES 10 A 322 ASP TYR ARG LEU ALA PRO GLU HIS PRO PHE PRO ALA ALA
SEQRES 11 A 322 VAL GLU ASP GLY VAL ALA ALA TYR ARG TRP LEU LEU ASP
SEQRES 12 A 322 GLN GLY PHE LYS PRO GLN HIS LEU SER ILE SER GLY ASP
SEQRES 13 A 322 SER ALA GLY GLY GLY LEU VAL LEU ALA VAL LEU VAL SER
SEQRES 14 A 322 ALA ARG ASP GLN GLY LEU PRO MET PRO ALA SER ALA ILE
SEQRES 15 A 322 PRO ILE SER PRO TRP ALA ASP MET THR CYS THR ASN ASP
SEQRES 16 A 322 SER PHE LYS THR ARG ALA GLU ALA ASP PRO MET VAL ALA
SEQRES 17 A 322 PRO GLY GLY ILE ASN LYS MET ALA ALA ARG TYR LEU ASN
SEQRES 18 A 322 GLY ALA ASP ALA LYS HIS PRO TYR ALA SER PRO ASN PHE
SEQRES 19 A 322 ALA ASN LEU LYS GLY LEU PRO PRO LEU LEU ILE HIS VAL
SEQRES 20 A 322 GLY ARG ASP GLU VAL LEU LEU ASP ASP SER ILE LYS LEU
SEQRES 21 A 322 ASP ALA LYS ALA LYS ALA ASP GLY VAL LYS SER THR LEU
SEQRES 22 A 322 GLU ILE TRP ASP ASP MET ILE HIS VAL TRP HIS ALA PHE
SEQRES 23 A 322 HIS PRO MET LEU PRO GLU GLY LYS GLN ALA ILE VAL ARG
SEQRES 24 A 322 VAL GLY GLU PHE MET ARG GLU GLN TRP ALA ALA LEU ALA
SEQRES 25 A 322 ALA ALA LEU GLU HIS HIS HIS HIS HIS HIS
HET CL A 310 1
HET NA A 311 1
HETNAM CL CHLORIDE ION
HETNAM NA SODIUM ION
FORMUL 2 CL CL 1-
FORMUL 3 NA NA 1+
FORMUL 4 HOH *195(H2 O)
HELIX 1 1 GLY A 3 ALA A 17 1 15
HELIX 2 2 PRO A 25 VAL A 36 1 12
HELIX 3 3 SER A 82 GLN A 98 1 17
HELIX 4 4 PRO A 115 GLY A 132 1 18
HELIX 5 5 LYS A 134 GLN A 136 5 3
HELIX 6 6 SER A 144 GLN A 160 1 17
HELIX 7 7 ASP A 182 ARG A 187 1 6
HELIX 8 8 GLY A 197 ASN A 208 1 12
HELIX 9 9 SER A 218 ALA A 222 5 5
HELIX 10 10 LEU A 240 ASP A 254 1 15
HELIX 11 11 VAL A 269 HIS A 274 5 6
HELIX 12 12 LEU A 277 ALA A 297 1 21
SHEET 1 A 6 GLN A 45 VAL A 51 0
SHEET 2 A 6 CYS A 54 ARG A 60 -1 O ARG A 60 N GLN A 45
SHEET 3 A 6 ALA A 100 LEU A 104 -1 O ALA A 101 N VAL A 59
SHEET 4 A 6 ALA A 69 LEU A 73 1 N ILE A 70 O LEU A 102
SHEET 5 A 6 LEU A 138 ASP A 143 1 O SER A 139 N LEU A 71
SHEET 6 A 6 SER A 167 ILE A 171 1 O ILE A 171 N GLY A 142
SHEET 1 B 2 LEU A 230 GLY A 235 0
SHEET 2 B 2 SER A 258 TRP A 263 1 O GLU A 261 N ILE A 232
LINK NA NA A 311 O HOH A 564 1555 1555 2.81
CISPEP 1 ALA A 109 PRO A 110 0 0.12
CISPEP 2 PHE A 114 PRO A 115 0 0.01
CISPEP 3 ALA A 195 PRO A 196 0 2.59
SITE 1 AC1 5 ARG A 107 HIS A 112 ALA A 116 ALA A 117
SITE 2 AC1 5 TYR A 206
SITE 1 AC2 3 THR A 259 HOH A 549 HOH A 564
CRYST1 60.996 60.996 149.282 90.00 90.00 90.00 P 41 21 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 0.016395 0.000000 0.000000 0.00000
SCALE2 0.000000 0.016395 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006699 0.00000
TER 2242 ALA A 297
MASTER 356 0 2 12 8 0 3 6 2438 1 2 25
END |