HEADER HYDROLASE 28-MAR-09 3GTX
TITLE D71G/E101G MUTANT IN ORGANOPHOSPHORUS HYDROLASE FROM DEINOCOCCUS
TITLE 2 RADIODURANS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ORGANOPHOSPHORUS HYDROLASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: PHOSPHOTRIESTERASE, PUTATIVE;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: DEINOCOCCUS RADIODURANS;
SOURCE 3 ORGANISM_TAXID: 1299;
SOURCE 4 GENE: DR_0930;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS MUTANT, AMIDOHYDROLASE, ALPHA-BETA BARREL, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR R.HAWWA,S.LARSEN,K.RATIA,A.MESECAR
REVDAT 3 13-OCT-21 3GTX 1 REMARK SEQADV LINK
REVDAT 2 09-JUN-10 3GTX 1 JRNL
REVDAT 1 30-JUN-09 3GTX 0
JRNL AUTH R.HAWWA,S.D.LARSEN,K.RATIA,A.D.MESECAR
JRNL TITL STRUCTURE-BASED AND RANDOM MUTAGENESIS APPROACHES INCREASE
JRNL TITL 2 THE ORGANOPHOSPHATE-DEGRADING ACTIVITY OF A
JRNL TITL 3 PHOSPHOTRIESTERASE HOMOLOGUE FROM DEINOCOCCUS RADIODURANS.
JRNL REF J.MOL.BIOL. V. 393 36 2009
JRNL REFN ISSN 0022-2836
JRNL PMID 19631223
JRNL DOI 10.1016/J.JMB.2009.06.083
REMARK 2
REMARK 2 RESOLUTION. 1.62 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) : 1.62
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
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 : 49760
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING SET) : 0.242
REMARK 3 FREE R VALUE : 0.282
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 2642
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 : 2508
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 2
REMARK 3 SOLVENT ATOMS : 364
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) : 0.013
REMARK 3 BOND ANGLES (DEGREES) : 1.720
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: NULL
REMARK 4
REMARK 4 3GTX COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-APR-09.
REMARK 100 THE DEPOSITION ID IS D_1000052301.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 14-FEB-07
REMARK 200 TEMPERATURE (KELVIN) : 100
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 : 22-BM
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : NULL
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 52402
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.620
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.2
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.08700
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.62
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.72
REMARK 200 COMPLETENESS FOR SHELL (%) : 92.6
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.65900
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> 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: SOLVE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 59.31
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.02
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.8 M K-NA TARTRATE*3H20, 0.1 M TRIS,
REMARK 280 PH 8.5, 0.5% PEG 5000, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 289K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+2/3
REMARK 290 6555 -X,-X+Y,-Z+1/3
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 68.39333
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 136.78667
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 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 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 136.78667
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 68.39333
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3560 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 23500 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -70.0 KCAL/MOL
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 BIOMT1 2 -0.500000 -0.866025 0.000000 0.00000
REMARK 350 BIOMT2 2 -0.866025 0.500000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 68.39333
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
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 HIS A 85
REMARK 465 HIS A 86
REMARK 465 HIS A 87
REMARK 465 HIS A 88
REMARK 465 HIS A 89
REMARK 465 HIS A 90
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 OE2 GLU A 217 NH2 ARG A 264 2.16
REMARK 500
REMARK 500 REMARK: NULL
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 PHE A 326 N - CA - C ANGL. DEV. = -17.9 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 96 -114.53 -68.35
REMARK 500 ARG A 97 171.48 45.17
REMARK 500 SER A 99 -83.46 -174.53
REMARK 500 VAL A 335 -127.62 67.70
REMARK 500 ALA A 379 18.71 -69.17
REMARK 500
REMARK 500 REMARK: NULL
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 CO A 502 CO
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A 41 O
REMARK 620 2 TYR A 197 OH 84.0
REMARK 620 3 KCX A 243 OQ1 168.2 95.2
REMARK 620 4 HIS A 276 ND1 86.9 87.2 104.9
REMARK 620 5 HIS A 304 NE2 82.8 166.7 98.0 90.2
REMARK 620 6 HOH A 597 O 89.3 90.5 79.0 175.7 91.2
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CO A 501 CO
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 121 NE2
REMARK 620 2 HIS A 123 NE2 109.7
REMARK 620 3 KCX A 243 OQ2 99.7 88.6
REMARK 620 4 ASP A 364 OD1 82.2 88.5 176.9
REMARK 620 5 HOH A 597 O 109.6 138.9 96.1 85.5
REMARK 620 N 1 2 3 4
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CO A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CO A 502
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3GTF RELATED DB: PDB
REMARK 900 RELATED ID: 3GTH RELATED DB: PDB
REMARK 900 RELATED ID: 3GTI RELATED DB: PDB
REMARK 900 RELATED ID: 3GU1 RELATED DB: PDB
REMARK 900 RELATED ID: 3GU2 RELATED DB: PDB
REMARK 900 RELATED ID: 3GU9 RELATED DB: PDB
DBREF 3GTX A 101 423 UNP Q9RVU2 Q9RVU2_DEIRA 1 323
SEQADV 3GTX HIS A 85 UNP Q9RVU2 EXPRESSION TAG
SEQADV 3GTX HIS A 86 UNP Q9RVU2 EXPRESSION TAG
SEQADV 3GTX HIS A 87 UNP Q9RVU2 EXPRESSION TAG
SEQADV 3GTX HIS A 88 UNP Q9RVU2 EXPRESSION TAG
SEQADV 3GTX HIS A 89 UNP Q9RVU2 EXPRESSION TAG
SEQADV 3GTX HIS A 90 UNP Q9RVU2 EXPRESSION TAG
SEQADV 3GTX SER A 91 UNP Q9RVU2 EXPRESSION TAG
SEQADV 3GTX SER A 92 UNP Q9RVU2 EXPRESSION TAG
SEQADV 3GTX GLY A 93 UNP Q9RVU2 EXPRESSION TAG
SEQADV 3GTX LEU A 94 UNP Q9RVU2 EXPRESSION TAG
SEQADV 3GTX VAL A 95 UNP Q9RVU2 EXPRESSION TAG
SEQADV 3GTX PRO A 96 UNP Q9RVU2 EXPRESSION TAG
SEQADV 3GTX ARG A 97 UNP Q9RVU2 EXPRESSION TAG
SEQADV 3GTX GLY A 98 UNP Q9RVU2 EXPRESSION TAG
SEQADV 3GTX SER A 99 UNP Q9RVU2 EXPRESSION TAG
SEQADV 3GTX HIS A 100 UNP Q9RVU2 EXPRESSION TAG
SEQADV 3GTX GLY A 171 UNP Q9RVU2 ASP 71 ENGINEERED MUTATION
SEQADV 3GTX GLY A 201 UNP Q9RVU2 GLU 101 ENGINEERED MUTATION
SEQRES 1 A 339 HIS HIS HIS HIS HIS HIS SER SER GLY LEU VAL PRO ARG
SEQRES 2 A 339 GLY SER HIS MET THR ALA GLN THR VAL THR GLY ALA VAL
SEQRES 3 A 339 ALA ALA ALA GLN LEU GLY ALA THR LEU PRO HIS GLU HIS
SEQRES 4 A 339 VAL ILE PHE GLY TYR PRO GLY TYR ALA GLY ASP VAL THR
SEQRES 5 A 339 LEU GLY PRO PHE ASP HIS ALA ALA ALA LEU ALA SER CYS
SEQRES 6 A 339 THR GLU THR ALA ARG ALA LEU LEU ALA ARG GLY ILE GLN
SEQRES 7 A 339 THR VAL VAL ASP ALA THR PRO ASN GLY CYS GLY ARG ASN
SEQRES 8 A 339 PRO ALA PHE LEU ARG GLU VAL SER GLU ALA THR GLY LEU
SEQRES 9 A 339 GLN ILE LEU CYS ALA THR GLY PHE TYR TYR GLU GLY GLY
SEQRES 10 A 339 GLY ALA THR THR TYR PHE LYS PHE ARG ALA SER LEU GLY
SEQRES 11 A 339 ASP ALA GLU SER GLU ILE TYR GLU MET MET ARG THR GLU
SEQRES 12 A 339 VAL THR GLU GLY ILE ALA GLY THR GLY ILE ARG ALA GLY
SEQRES 13 A 339 VAL ILE KCX LEU ALA SER SER ARG ASP ALA ILE THR PRO
SEQRES 14 A 339 TYR GLU GLN LEU PHE PHE ARG ALA ALA ALA ARG VAL GLN
SEQRES 15 A 339 ARG GLU THR GLY VAL PRO ILE ILE THR HIS THR GLN GLU
SEQRES 16 A 339 GLY GLN GLN GLY PRO GLN GLN ALA GLU LEU LEU THR SER
SEQRES 17 A 339 LEU GLY ALA ASP PRO ALA ARG ILE MET ILE GLY HIS MET
SEQRES 18 A 339 ASP GLY ASN THR ASP PRO ALA TYR HIS ARG GLU THR LEU
SEQRES 19 A 339 ARG HIS GLY VAL SER ILE ALA PHE ASP ARG ILE GLY LEU
SEQRES 20 A 339 GLN GLY MET VAL GLY THR PRO THR ASP ALA GLU ARG LEU
SEQRES 21 A 339 SER VAL LEU THR THR LEU LEU GLY GLU GLY TYR ALA ASP
SEQRES 22 A 339 ARG LEU LEU LEU SER HIS ASP SER ILE TRP HIS TRP LEU
SEQRES 23 A 339 GLY ARG PRO PRO ALA ILE PRO GLU ALA ALA LEU PRO ALA
SEQRES 24 A 339 VAL LYS ASP TRP HIS PRO LEU HIS ILE SER ASP ASP ILE
SEQRES 25 A 339 LEU PRO ASP LEU ARG ARG ARG GLY ILE THR GLU GLU GLN
SEQRES 26 A 339 VAL GLY GLN MET THR VAL GLY ASN PRO ALA ARG LEU PHE
SEQRES 27 A 339 GLY
MODRES 3GTX KCX A 243 LYS LYSINE NZ-CARBOXYLIC ACID
HET KCX A 243 12
HET CO A 501 1
HET CO A 502 1
HETNAM KCX LYSINE NZ-CARBOXYLIC ACID
HETNAM CO COBALT (II) ION
FORMUL 1 KCX C7 H14 N2 O4
FORMUL 2 CO 2(CO 2+)
FORMUL 4 HOH *364(H2 O)
HELIX 1 1 ALA A 111 LEU A 115 5 5
HELIX 2 2 GLY A 130 VAL A 135 5 6
HELIX 3 3 ASP A 141 ARG A 159 1 19
HELIX 4 4 ASN A 175 GLY A 187 1 13
HELIX 5 5 THR A 204 GLY A 214 1 11
HELIX 6 6 ASP A 215 GLU A 230 1 16
HELIX 7 7 THR A 252 GLY A 270 1 19
HELIX 8 8 GLN A 282 LEU A 293 1 12
HELIX 9 9 ASP A 296 ALA A 298 5 3
HELIX 10 10 HIS A 304 ASN A 308 5 5
HELIX 11 11 ASP A 310 ARG A 319 1 10
HELIX 12 12 THR A 339 GLU A 353 1 15
HELIX 13 13 GLY A 354 ASP A 357 5 4
HELIX 14 14 PRO A 377 ALA A 379 5 3
HELIX 15 15 ALA A 380 ASP A 386 1 7
HELIX 16 16 LEU A 390 ASP A 395 1 6
HELIX 17 17 ASP A 395 ARG A 403 1 9
HELIX 18 18 THR A 406 VAL A 415 1 10
HELIX 19 19 VAL A 415 GLY A 423 1 9
SHEET 1 A 2 ALA A 103 THR A 105 0
SHEET 2 A 2 GLY A 108 VAL A 110 -1 O GLY A 108 N THR A 105
SHEET 1 B 4 GLN A 189 LEU A 191 0
SHEET 2 B 4 ILE A 161 ASP A 166 1 N ASP A 166 O LEU A 191
SHEET 3 B 4 ALA A 117 PHE A 126 1 N LEU A 119 O VAL A 165
SHEET 4 B 4 ILE A 366 TRP A 369 1 O TRP A 367 N HIS A 123
SHEET 1 C 6 ALA A 193 THR A 194 0
SHEET 2 C 6 VAL A 241 ALA A 245 1 O KCX A 243 N THR A 194
SHEET 3 C 6 ILE A 273 HIS A 276 1 O ILE A 274 N ILE A 242
SHEET 4 C 6 ILE A 300 ILE A 302 1 O MET A 301 N ILE A 273
SHEET 5 C 6 SER A 323 PHE A 326 1 O SER A 323 N ILE A 302
SHEET 6 C 6 LEU A 359 LEU A 361 1 O LEU A 360 N PHE A 326
LINK C ILE A 242 N KCX A 243 1555 1555 1.33
LINK C KCX A 243 N LEU A 244 1555 1555 1.35
LINK O HOH A 41 CO CO A 502 1555 1555 2.39
LINK NE2 HIS A 121 CO CO A 501 1555 1555 2.15
LINK NE2 HIS A 123 CO CO A 501 1555 1555 2.00
LINK OH TYR A 197 CO CO A 502 1555 1555 2.11
LINK OQ2 KCX A 243 CO CO A 501 1555 1555 2.06
LINK OQ1 KCX A 243 CO CO A 502 1555 1555 2.08
LINK ND1 HIS A 276 CO CO A 502 1555 1555 2.23
LINK NE2 HIS A 304 CO CO A 502 1555 1555 2.26
LINK OD1 ASP A 364 CO CO A 501 1555 1555 2.20
LINK CO CO A 501 O HOH A 597 1555 1555 1.72
LINK CO CO A 502 O HOH A 597 1555 1555 2.27
SITE 1 AC1 6 HIS A 121 HIS A 123 KCX A 243 ASP A 364
SITE 2 AC1 6 CO A 502 HOH A 597
SITE 1 AC2 7 HOH A 41 TYR A 197 KCX A 243 HIS A 276
SITE 2 AC2 7 HIS A 304 CO A 501 HOH A 597
CRYST1 61.030 61.030 205.180 90.00 90.00 120.00 P 31 2 1 6
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 0.016385 0.009460 0.000000 0.00000
SCALE2 0.000000 0.018920 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004874 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
