HEADER HYDROLASE 20-MAR-07 2P79
TITLE CRYSTAL STRUCTURE OF TTHB049 FROM THERMUS THERMOPHILUS HB8
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ALPHA-RIBAZOLE-5'-PHOSPHATE PHOSPHATASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: TTHB049 PROTEIN;
COMPND 5 EC: 3.1.3.73;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;
SOURCE 3 ORGANISM_TAXID: 300852;
SOURCE 4 STRAIN: HB8;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET-11A
KEYWDS THERMUS THERMOPHILUS HB8, STRUCTURAL GENOMICS, NPPSFA, NATIONAL
KEYWDS 2 PROJECT ON PROTEIN STRUCTURAL AND FUNCTIONAL ANALYSES, RIKEN
KEYWDS 3 STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE, RSGI, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.SUGAHARA,M.TAKETA,Y.KAGEYAMA,Y.MATSUURA,N.KUNISHIMA,RIKEN
AUTHOR 2 STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE (RSGI)
REVDAT 5 25-OCT-23 2P79 1 REMARK
REVDAT 4 10-NOV-21 2P79 1 REMARK SEQADV LINK
REVDAT 3 13-JUL-11 2P79 1 VERSN
REVDAT 2 24-FEB-09 2P79 1 VERSN
REVDAT 1 25-SEP-07 2P79 0
JRNL AUTH M.SUGAHARA,M.TAKETA,Y.KAGEYAMA,Y.MATSUURA,N.KUNISHIMA
JRNL TITL CRYSTAL STRUCTURE OF TTHB049 FROM THERMUS THERMOPHILUS HB8
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.75 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
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) : 1.75
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.53
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) (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 44086
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) : 0.203
REMARK 3 FREE R VALUE : 0.232
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 2187
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) : 1.75
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.81
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.90
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2390
REMARK 3 BIN FREE R VALUE : 0.2600
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 223
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 : 2694
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 25
REMARK 3 SOLVENT ATOMS : 362
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 18.10
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 21.50
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.91000
REMARK 3 B22 (A**2) : -1.38000
REMARK 3 B33 (A**2) : 0.47000
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) : 0.20
REMARK 3 ESD FROM SIGMAA (A) : 0.13
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) : 0.23
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.12
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 1.400
REMARK 3 BOND ANGLES (DEGREES) : 0.007
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : ANISOTROP
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 2P79 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 14-MAY-07.
REMARK 100 THE DEPOSITION ID IS D_1000042054.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 20-NOV-06
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.3
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SPRING-8
REMARK 200 BEAMLINE : BL26B1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0000
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RIGAKU JUPITER
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 44097
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.750
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 8.800
REMARK 200 R MERGE (I) : 0.07300
REMARK 200 R SYM (I) : 0.07100
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 7.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.75
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.81
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 8.90
REMARK 200 R MERGE FOR SHELL (I) : 0.34100
REMARK 200 R SYM FOR SHELL (I) : 0.32400
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.200
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: 1V37
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 55.33
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.75
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 2.75M NACL, 0.1M TRIS-HCL, PH 8.3, OIL
REMARK 280 -MICRO BATCH, TEMPERATURE 295K
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 42.47400
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 45.94300
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 55.48350
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 42.47400
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 45.94300
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 55.48350
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 42.47400
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 45.94300
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 55.48350
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 42.47400
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 45.94300
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 55.48350
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 300 REMARK: THE BIOLOGICAL ASSEMBLY IS A MONOMER IN THE ASYMMETRIC UNIT
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 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 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 GLY A 172
REMARK 465 GLU A 173
REMARK 465 GLU A 174
REMARK 465 ALA A 175
REMARK 465 THR A 176
REMARK 465 GLY A 177
REMARK 465 ASP B 171
REMARK 465 GLY B 172
REMARK 465 GLU B 173
REMARK 465 GLU B 174
REMARK 465 ALA B 175
REMARK 465 THR B 176
REMARK 465 GLY B 177
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH B 2037 O HOH B 2096 4555 2.10
REMARK 500
REMARK 500 REMARK: NULL
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 TRP A 160 NE1 TRP A 160 CE2 0.114
REMARK 500 TRP B 160 NE1 TRP B 160 CE2 0.114
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 THR A 132 -150.11 -145.11
REMARK 500 PRO A 161 50.30 -103.67
REMARK 500 ALA B 41 -40.27 -136.36
REMARK 500 THR B 132 -147.66 -145.78
REMARK 500 PRO B 161 42.87 -106.99
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 NA B2001 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ALA A 79 O
REMARK 620 2 GLU A 81 O 119.3
REMARK 620 3 ALA B 79 O 121.1 96.5
REMARK 620 4 GLU B 81 O 95.6 112.5 112.7
REMARK 620 5 HOH B2148 O 67.6 85.4 71.0 160.4
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 NA B 2001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 1001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 1002
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 1003
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 1004
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2P6M RELATED DB: PDB
REMARK 900 RELATED ID: 2P6O RELATED DB: PDB
REMARK 900 RELATED ID: 2P75 RELATED DB: PDB
REMARK 900 RELATED ID: 2P77 RELATED DB: PDB
REMARK 900 RELATED ID: 2P78 RELATED DB: PDB
REMARK 900 RELATED ID: TTK003000215.14 RELATED DB: TARGETDB
DBREF 2P79 A 1 177 UNP Q53WB3 Q53WB3_THET8 1 177
DBREF 2P79 B 1 177 UNP Q53WB3 Q53WB3_THET8 1 177
SEQADV 2P79 MET A 84 UNP Q53WB3 LEU 84 ENGINEERED MUTATION
SEQADV 2P79 MET B 84 UNP Q53WB3 LEU 84 ENGINEERED MUTATION
SEQRES 1 A 177 MET GLU LEU TRP LEU VAL ARG HIS GLY GLU THR LEU TRP
SEQRES 2 A 177 ASN ARG GLU GLY ARG LEU LEU GLY TRP THR ASP LEU PRO
SEQRES 3 A 177 LEU THR ALA GLU GLY GLU ALA GLN ALA ARG ARG LEU LYS
SEQRES 4 A 177 GLY ALA LEU PRO SER LEU PRO ALA PHE SER SER ASP LEU
SEQRES 5 A 177 LEU ARG ALA ARG ARG THR ALA GLU LEU ALA GLY PHE SER
SEQRES 6 A 177 PRO ARG LEU TYR PRO GLU LEU ARG GLU ILE HIS PHE GLY
SEQRES 7 A 177 ALA LEU GLU GLY ALA MET TRP GLU THR LEU ASP PRO ARG
SEQRES 8 A 177 TYR LYS GLU ALA LEU LEU ARG PHE GLN GLY PHE HIS PRO
SEQRES 9 A 177 PRO GLY GLY GLU SER LEU SER ALA PHE GLN GLU ARG VAL
SEQRES 10 A 177 PHE ARG PHE LEU GLU GLY LEU LYS ALA PRO ALA VAL LEU
SEQRES 11 A 177 PHE THR HIS GLY GLY VAL VAL ARG ALA VAL LEU ARG ALA
SEQRES 12 A 177 LEU GLY GLU ASP GLY LEU VAL PRO PRO GLY SER ALA VAL
SEQRES 13 A 177 ALA VAL ASP TRP PRO ARG ARG VAL LEU VAL ARG LEU ALA
SEQRES 14 A 177 LEU ASP GLY GLU GLU ALA THR GLY
SEQRES 1 B 177 MET GLU LEU TRP LEU VAL ARG HIS GLY GLU THR LEU TRP
SEQRES 2 B 177 ASN ARG GLU GLY ARG LEU LEU GLY TRP THR ASP LEU PRO
SEQRES 3 B 177 LEU THR ALA GLU GLY GLU ALA GLN ALA ARG ARG LEU LYS
SEQRES 4 B 177 GLY ALA LEU PRO SER LEU PRO ALA PHE SER SER ASP LEU
SEQRES 5 B 177 LEU ARG ALA ARG ARG THR ALA GLU LEU ALA GLY PHE SER
SEQRES 6 B 177 PRO ARG LEU TYR PRO GLU LEU ARG GLU ILE HIS PHE GLY
SEQRES 7 B 177 ALA LEU GLU GLY ALA MET TRP GLU THR LEU ASP PRO ARG
SEQRES 8 B 177 TYR LYS GLU ALA LEU LEU ARG PHE GLN GLY PHE HIS PRO
SEQRES 9 B 177 PRO GLY GLY GLU SER LEU SER ALA PHE GLN GLU ARG VAL
SEQRES 10 B 177 PHE ARG PHE LEU GLU GLY LEU LYS ALA PRO ALA VAL LEU
SEQRES 11 B 177 PHE THR HIS GLY GLY VAL VAL ARG ALA VAL LEU ARG ALA
SEQRES 12 B 177 LEU GLY GLU ASP GLY LEU VAL PRO PRO GLY SER ALA VAL
SEQRES 13 B 177 ALA VAL ASP TRP PRO ARG ARG VAL LEU VAL ARG LEU ALA
SEQRES 14 B 177 LEU ASP GLY GLU GLU ALA THR GLY
HET GOL A1001 6
HET GOL A1003 6
HET GOL A1004 6
HET NA B2001 1
HET GOL B1002 6
HETNAM GOL GLYCEROL
HETNAM NA SODIUM ION
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 3 GOL 4(C3 H8 O3)
FORMUL 6 NA NA 1+
FORMUL 8 HOH *362(H2 O)
HELIX 1 1 THR A 11 GLY A 17 1 7
HELIX 2 2 THR A 28 LYS A 39 1 12
HELIX 3 3 LEU A 52 ALA A 62 1 11
HELIX 4 4 PRO A 70 ARG A 73 5 4
HELIX 5 5 PHE A 77 GLU A 81 5 5
HELIX 6 6 MET A 84 LEU A 88 5 5
HELIX 7 7 ASP A 89 ARG A 98 1 10
HELIX 8 8 SER A 109 GLY A 123 1 15
HELIX 9 9 HIS A 133 LEU A 144 1 12
HELIX 10 10 THR B 11 GLY B 17 1 7
HELIX 11 11 THR B 28 LYS B 39 1 12
HELIX 12 12 LEU B 52 ALA B 62 1 11
HELIX 13 13 PRO B 70 ARG B 73 5 4
HELIX 14 14 PHE B 77 GLU B 81 5 5
HELIX 15 15 MET B 84 LEU B 88 5 5
HELIX 16 16 ASP B 89 PHE B 99 1 11
HELIX 17 17 SER B 109 LEU B 124 1 16
HELIX 18 18 HIS B 133 LEU B 144 1 12
SHEET 1 A 6 ARG A 67 LEU A 68 0
SHEET 2 A 6 ALA A 47 SER A 49 1 N ALA A 47 O ARG A 67
SHEET 3 A 6 ALA A 128 THR A 132 1 O PHE A 131 N PHE A 48
SHEET 4 A 6 GLU A 2 ARG A 7 1 N TRP A 4 O LEU A 130
SHEET 5 A 6 ALA A 155 ASP A 159 -1 O VAL A 156 N LEU A 5
SHEET 6 A 6 ARG A 163 LEU A 168 -1 O ARG A 163 N ASP A 159
SHEET 1 B 6 ARG B 67 LEU B 68 0
SHEET 2 B 6 ALA B 47 SER B 49 1 N SER B 49 O ARG B 67
SHEET 3 B 6 ALA B 128 THR B 132 1 O PHE B 131 N PHE B 48
SHEET 4 B 6 GLU B 2 ARG B 7 1 N TRP B 4 O LEU B 130
SHEET 5 B 6 ALA B 155 ASP B 159 -1 O VAL B 156 N LEU B 5
SHEET 6 B 6 ARG B 163 LEU B 168 -1 O ARG B 163 N ASP B 159
LINK O ALA A 79 NA NA B2001 8555 1555 2.38
LINK O GLU A 81 NA NA B2001 8555 1555 2.35
LINK O ALA B 79 NA NA B2001 1555 1555 2.30
LINK O GLU B 81 NA NA B2001 1555 1555 2.35
LINK NA NA B2001 O HOH B2148 1555 1555 2.66
CISPEP 1 TRP A 160 PRO A 161 0 -3.43
CISPEP 2 TRP B 160 PRO B 161 0 -0.54
SITE 1 AC1 5 ALA A 79 GLU A 81 ALA B 79 GLU B 81
SITE 2 AC1 5 HOH B2148
SITE 1 AC2 3 TYR A 69 PHE A 120 GLY A 123
SITE 1 AC3 5 PHE B 48 PHE B 120 GLY B 123 LEU B 124
SITE 2 AC3 5 HOH B2014
SITE 1 AC4 4 GLY A 101 SER A 111 HOH A1100 SER B 65
SITE 1 AC5 4 GLU A 74 GLY A 135 ARG A 138 HOH A1113
CRYST1 84.948 91.886 110.967 90.00 90.00 90.00 I 2 2 2 16
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 0.011772 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010883 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009012 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
