HEADER OXIDOREDUCTASE 28-FEB-07 2EGG
TITLE CRYSTAL STRUCTURE OF SHIKIMATE 5-DEHYDROGENASE (AROE) FROM GEOBACILLUS
TITLE 2 KAUSTOPHILUS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SHIKIMATE 5-DEHYDROGENASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: AROE;
COMPND 5 EC: 1.1.1.25;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: GEOBACILLUS KAUSTOPHILUS;
SOURCE 3 ORGANISM_TAXID: 1462;
SOURCE 4 GENE: AROE;
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 SHIKIMATE, DIMER, STRUCTURAL GENOMICS, NPPSFA, NATIONAL PROJECT ON
KEYWDS 2 PROTEIN STRUCTURAL AND FUNCTIONAL ANALYSES, RIKEN STRUCTURAL
KEYWDS 3 GENOMICS/PROTEOMICS INITIATIVE, RSGI, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR B.BAGAUTDINOV,N.KUNISHIMA,RIKEN STRUCTURAL GENOMICS/PROTEOMICS
AUTHOR 2 INITIATIVE (RSGI)
REVDAT 4 25-OCT-23 2EGG 1 REMARK SEQADV
REVDAT 3 24-JAN-18 2EGG 1 REMARK
REVDAT 2 24-FEB-09 2EGG 1 VERSN
REVDAT 1 18-MAR-08 2EGG 0
JRNL AUTH B.BAGAUTDINOV,N.KUNISHIMA
JRNL TITL CRYSTAL STRUCTURE OF SHIKIMATE 5-DEHYDROGENASE (AROE) FROM
JRNL TITL 2 GEOBACILLUS KAUSTOPHILUS
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.25 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) : 2.25
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 36.54
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) (%) : 99.1
REMARK 3 NUMBER OF REFLECTIONS : 39341
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) : 0.218
REMARK 3 FREE R VALUE : 0.255
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 1955
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) : 2.25
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.33
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.70
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2490
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 : 194
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.019
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3444
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 2
REMARK 3 SOLVENT ATOMS : 402
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 43.02
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 42.80
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.00000
REMARK 3 B22 (A**2) : 0.00000
REMARK 3 B33 (A**2) : 0.00000
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) : 0.20
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) : 0.23
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.006
REMARK 3 BOND ANGLES (DEGREES) : 1.200
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 22.80
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.880
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : OVERALL
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 2EGG COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 13-MAR-07.
REMARK 100 THE DEPOSITION ID IS D_1000026633.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 13-DEC-06
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.1
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : GRAPHITE
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 39341
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.250
REMARK 200 RESOLUTION RANGE LOW (A) : 45.810
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.1
REMARK 200 DATA REDUNDANCY : 4.800
REMARK 200 R MERGE (I) : 0.08000
REMARK 200 R SYM (I) : 0.06100
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 19.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.25
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.33
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.0
REMARK 200 DATA REDUNDANCY IN SHELL : 4.70
REMARK 200 R MERGE FOR SHELL (I) : 0.49800
REMARK 200 R SYM FOR SHELL (I) : 0.46200
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.200
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: 1WXD
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 61.43
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.19
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 2.5M NACL, 100MM IMIDAZOLE, PH 8.1,
REMARK 280 MICROBATCH
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 3
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 Z,X,Y
REMARK 290 6555 Z,-X,-Y
REMARK 290 7555 -Z,-X,Y
REMARK 290 8555 -Z,X,-Y
REMARK 290 9555 Y,Z,X
REMARK 290 10555 -Y,Z,-X
REMARK 290 11555 Y,-Z,-X
REMARK 290 12555 -Y,-Z,X
REMARK 290 13555 X+1/2,Y+1/2,Z+1/2
REMARK 290 14555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 15555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 16555 X+1/2,-Y+1/2,-Z+1/2
REMARK 290 17555 Z+1/2,X+1/2,Y+1/2
REMARK 290 18555 Z+1/2,-X+1/2,-Y+1/2
REMARK 290 19555 -Z+1/2,-X+1/2,Y+1/2
REMARK 290 20555 -Z+1/2,X+1/2,-Y+1/2
REMARK 290 21555 Y+1/2,Z+1/2,X+1/2
REMARK 290 22555 -Y+1/2,Z+1/2,-X+1/2
REMARK 290 23555 Y+1/2,-Z+1/2,-X+1/2
REMARK 290 24555 -Y+1/2,-Z+1/2,X+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 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY2 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY1 6 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY2 6 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY1 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY2 7 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY2 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY1 9 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 9 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY3 9 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 10 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 10 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY3 10 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 11 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 11 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY3 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 12 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 12 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY3 12 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 13 1.000000 0.000000 0.000000 85.69700
REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 85.69700
REMARK 290 SMTRY3 13 0.000000 0.000000 1.000000 85.69700
REMARK 290 SMTRY1 14 -1.000000 0.000000 0.000000 85.69700
REMARK 290 SMTRY2 14 0.000000 -1.000000 0.000000 85.69700
REMARK 290 SMTRY3 14 0.000000 0.000000 1.000000 85.69700
REMARK 290 SMTRY1 15 -1.000000 0.000000 0.000000 85.69700
REMARK 290 SMTRY2 15 0.000000 1.000000 0.000000 85.69700
REMARK 290 SMTRY3 15 0.000000 0.000000 -1.000000 85.69700
REMARK 290 SMTRY1 16 1.000000 0.000000 0.000000 85.69700
REMARK 290 SMTRY2 16 0.000000 -1.000000 0.000000 85.69700
REMARK 290 SMTRY3 16 0.000000 0.000000 -1.000000 85.69700
REMARK 290 SMTRY1 17 0.000000 0.000000 1.000000 85.69700
REMARK 290 SMTRY2 17 1.000000 0.000000 0.000000 85.69700
REMARK 290 SMTRY3 17 0.000000 1.000000 0.000000 85.69700
REMARK 290 SMTRY1 18 0.000000 0.000000 1.000000 85.69700
REMARK 290 SMTRY2 18 -1.000000 0.000000 0.000000 85.69700
REMARK 290 SMTRY3 18 0.000000 -1.000000 0.000000 85.69700
REMARK 290 SMTRY1 19 0.000000 0.000000 -1.000000 85.69700
REMARK 290 SMTRY2 19 -1.000000 0.000000 0.000000 85.69700
REMARK 290 SMTRY3 19 0.000000 1.000000 0.000000 85.69700
REMARK 290 SMTRY1 20 0.000000 0.000000 -1.000000 85.69700
REMARK 290 SMTRY2 20 1.000000 0.000000 0.000000 85.69700
REMARK 290 SMTRY3 20 0.000000 -1.000000 0.000000 85.69700
REMARK 290 SMTRY1 21 0.000000 1.000000 0.000000 85.69700
REMARK 290 SMTRY2 21 0.000000 0.000000 1.000000 85.69700
REMARK 290 SMTRY3 21 1.000000 0.000000 0.000000 85.69700
REMARK 290 SMTRY1 22 0.000000 -1.000000 0.000000 85.69700
REMARK 290 SMTRY2 22 0.000000 0.000000 1.000000 85.69700
REMARK 290 SMTRY3 22 -1.000000 0.000000 0.000000 85.69700
REMARK 290 SMTRY1 23 0.000000 1.000000 0.000000 85.69700
REMARK 290 SMTRY2 23 0.000000 0.000000 -1.000000 85.69700
REMARK 290 SMTRY3 23 -1.000000 0.000000 0.000000 85.69700
REMARK 290 SMTRY1 24 0.000000 -1.000000 0.000000 85.69700
REMARK 290 SMTRY2 24 0.000000 0.000000 -1.000000 85.69700
REMARK 290 SMTRY3 24 1.000000 0.000000 0.000000 85.69700
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2090 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 20340 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -32.4 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 12110 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 55150 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -138.6 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 350 BIOMT1 2 0.000000 0.000000 -1.000000 0.00000
REMARK 350 BIOMT2 2 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT1 3 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT2 3 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT3 3 -1.000000 0.000000 0.000000 0.00000
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A1152 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A1154 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A1236 LIES ON A SPECIAL POSITION.
REMARK 375 HOH B 406 LIES ON A SPECIAL POSITION.
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 GLY A 2
REMARK 465 SER A 3
REMARK 465 SER A 4
REMARK 465 HIS A 5
REMARK 465 HIS A 6
REMARK 465 HIS A 7
REMARK 465 HIS A 8
REMARK 465 HIS A 9
REMARK 465 HIS A 10
REMARK 465 SER A 11
REMARK 465 SER A 12
REMARK 465 GLY A 13
REMARK 465 GLU A 14
REMARK 465 ASN A 15
REMARK 465 LEU A 16
REMARK 465 TYR A 17
REMARK 465 PHE A 18
REMARK 465 GLN A 19
REMARK 465 MET B 1
REMARK 465 GLY B 2
REMARK 465 SER B 3
REMARK 465 SER B 4
REMARK 465 HIS B 5
REMARK 465 HIS B 6
REMARK 465 HIS B 7
REMARK 465 HIS B 8
REMARK 465 HIS B 9
REMARK 465 HIS B 10
REMARK 465 SER B 11
REMARK 465 SER B 12
REMARK 465 GLY B 13
REMARK 465 GLU B 14
REMARK 465 ASN B 15
REMARK 465 LEU B 16
REMARK 465 TYR B 17
REMARK 465 PHE B 18
REMARK 465 GLN B 19
REMARK 465 GLY B 20
REMARK 465 ILE B 144
REMARK 465 LEU B 145
REMARK 465 VAL B 146
REMARK 465 ILE B 147
REMARK 465 GLY B 148
REMARK 465 ALA B 149
REMARK 465 GLY B 150
REMARK 465 GLY B 151
REMARK 465 GLY B 152
REMARK 465 ALA B 153
REMARK 465 ARG B 154
REMARK 465 GLY B 155
REMARK 465 ILE B 156
REMARK 465 TYR B 157
REMARK 465 PHE B 158
REMARK 465 SER B 159
REMARK 465 LEU B 160
REMARK 465 LEU B 161
REMARK 465 SER B 162
REMARK 465 THR B 163
REMARK 465 ALA B 164
REMARK 465 ALA B 165
REMARK 465 GLU B 166
REMARK 465 ARG B 167
REMARK 465 ILE B 168
REMARK 465 ASP B 169
REMARK 465 MET B 170
REMARK 465 ALA B 171
REMARK 465 ASN B 172
REMARK 465 ARG B 173
REMARK 465 THR B 174
REMARK 465 VAL B 175
REMARK 465 GLU B 176
REMARK 465 LYS B 177
REMARK 465 ALA B 178
REMARK 465 GLU B 179
REMARK 465 ARG B 180
REMARK 465 LEU B 181
REMARK 465 VAL B 182
REMARK 465 ARG B 183
REMARK 465 GLU B 184
REMARK 465 GLY B 185
REMARK 465 ASP B 186
REMARK 465 GLU B 187
REMARK 465 ARG B 188
REMARK 465 ARG B 189
REMARK 465 SER B 190
REMARK 465 ALA B 191
REMARK 465 TYR B 192
REMARK 465 PHE B 193
REMARK 465 SER B 194
REMARK 465 LEU B 195
REMARK 465 ALA B 196
REMARK 465 GLU B 197
REMARK 465 ALA B 198
REMARK 465 GLU B 199
REMARK 465 THR B 200
REMARK 465 ARG B 201
REMARK 465 LEU B 202
REMARK 465 ALA B 203
REMARK 465 GLU B 204
REMARK 465 TYR B 205
REMARK 465 ASP B 206
REMARK 465 ILE B 207
REMARK 465 ILE B 208
REMARK 465 ILE B 209
REMARK 465 ASN B 210
REMARK 465 THR B 211
REMARK 465 THR B 212
REMARK 465 SER B 213
REMARK 465 VAL B 214
REMARK 465 GLY B 215
REMARK 465 MET B 216
REMARK 465 HIS B 217
REMARK 465 PRO B 218
REMARK 465 ARG B 219
REMARK 465 VAL B 220
REMARK 465 GLU B 221
REMARK 465 VAL B 222
REMARK 465 GLN B 223
REMARK 465 PRO B 224
REMARK 465 LEU B 225
REMARK 465 SER B 226
REMARK 465 LEU B 227
REMARK 465 GLU B 228
REMARK 465 ARG B 229
REMARK 465 LEU B 230
REMARK 465 ARG B 231
REMARK 465 PRO B 232
REMARK 465 GLY B 233
REMARK 465 VAL B 234
REMARK 465 ILE B 235
REMARK 465 VAL B 236
REMARK 465 PRO B 243
REMARK 465 LEU B 244
REMARK 465 GLU B 245
REMARK 465 THR B 246
REMARK 465 LYS B 247
REMARK 465 TRP B 248
REMARK 465 LEU B 249
REMARK 465 LYS B 250
REMARK 465 GLU B 251
REMARK 465 ALA B 252
REMARK 465 LYS B 253
REMARK 465 ALA B 254
REMARK 465 ARG B 255
REMARK 465 GLY B 256
REMARK 465 ALA B 257
REMARK 465 ARG B 258
REMARK 465 VAL B 259
REMARK 465 ARG B 297
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 ASN A 136 70.84 44.80
REMARK 500 ASP A 186 -60.45 -91.77
REMARK 500 GLU A 187 -1.95 81.93
REMARK 500 GLU A 221 23.35 -74.95
REMARK 500 PHE B 31 102.08 -160.73
REMARK 500 VAL B 33 -11.84 -144.79
REMARK 500 PRO B 52 92.51 -69.78
REMARK 500 ASP B 140 75.68 -64.43
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 1001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 1002
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: GKA001002524.1 RELATED DB: TARGETDB
DBREF 2EGG A 22 297 UNP Q5KWX7 Q5KWX7_GEOKA 1 276
DBREF 2EGG B 22 297 UNP Q5KWX7 Q5KWX7_GEOKA 1 276
SEQADV 2EGG MET A 1 UNP Q5KWX7 EXPRESSION TAG
SEQADV 2EGG GLY A 2 UNP Q5KWX7 EXPRESSION TAG
SEQADV 2EGG SER A 3 UNP Q5KWX7 EXPRESSION TAG
SEQADV 2EGG SER A 4 UNP Q5KWX7 EXPRESSION TAG
SEQADV 2EGG HIS A 5 UNP Q5KWX7 EXPRESSION TAG
SEQADV 2EGG HIS A 6 UNP Q5KWX7 EXPRESSION TAG
SEQADV 2EGG HIS A 7 UNP Q5KWX7 EXPRESSION TAG
SEQADV 2EGG HIS A 8 UNP Q5KWX7 EXPRESSION TAG
SEQADV 2EGG HIS A 9 UNP Q5KWX7 EXPRESSION TAG
SEQADV 2EGG HIS A 10 UNP Q5KWX7 EXPRESSION TAG
SEQADV 2EGG SER A 11 UNP Q5KWX7 EXPRESSION TAG
SEQADV 2EGG SER A 12 UNP Q5KWX7 EXPRESSION TAG
SEQADV 2EGG GLY A 13 UNP Q5KWX7 EXPRESSION TAG
SEQADV 2EGG GLU A 14 UNP Q5KWX7 EXPRESSION TAG
SEQADV 2EGG ASN A 15 UNP Q5KWX7 EXPRESSION TAG
SEQADV 2EGG LEU A 16 UNP Q5KWX7 EXPRESSION TAG
SEQADV 2EGG TYR A 17 UNP Q5KWX7 EXPRESSION TAG
SEQADV 2EGG PHE A 18 UNP Q5KWX7 EXPRESSION TAG
SEQADV 2EGG GLN A 19 UNP Q5KWX7 EXPRESSION TAG
SEQADV 2EGG GLY A 20 UNP Q5KWX7 EXPRESSION TAG
SEQADV 2EGG HIS A 21 UNP Q5KWX7 EXPRESSION TAG
SEQADV 2EGG MET B 1 UNP Q5KWX7 EXPRESSION TAG
SEQADV 2EGG GLY B 2 UNP Q5KWX7 EXPRESSION TAG
SEQADV 2EGG SER B 3 UNP Q5KWX7 EXPRESSION TAG
SEQADV 2EGG SER B 4 UNP Q5KWX7 EXPRESSION TAG
SEQADV 2EGG HIS B 5 UNP Q5KWX7 EXPRESSION TAG
SEQADV 2EGG HIS B 6 UNP Q5KWX7 EXPRESSION TAG
SEQADV 2EGG HIS B 7 UNP Q5KWX7 EXPRESSION TAG
SEQADV 2EGG HIS B 8 UNP Q5KWX7 EXPRESSION TAG
SEQADV 2EGG HIS B 9 UNP Q5KWX7 EXPRESSION TAG
SEQADV 2EGG HIS B 10 UNP Q5KWX7 EXPRESSION TAG
SEQADV 2EGG SER B 11 UNP Q5KWX7 EXPRESSION TAG
SEQADV 2EGG SER B 12 UNP Q5KWX7 EXPRESSION TAG
SEQADV 2EGG GLY B 13 UNP Q5KWX7 EXPRESSION TAG
SEQADV 2EGG GLU B 14 UNP Q5KWX7 EXPRESSION TAG
SEQADV 2EGG ASN B 15 UNP Q5KWX7 EXPRESSION TAG
SEQADV 2EGG LEU B 16 UNP Q5KWX7 EXPRESSION TAG
SEQADV 2EGG TYR B 17 UNP Q5KWX7 EXPRESSION TAG
SEQADV 2EGG PHE B 18 UNP Q5KWX7 EXPRESSION TAG
SEQADV 2EGG GLN B 19 UNP Q5KWX7 EXPRESSION TAG
SEQADV 2EGG GLY B 20 UNP Q5KWX7 EXPRESSION TAG
SEQADV 2EGG HIS B 21 UNP Q5KWX7 EXPRESSION TAG
SEQRES 1 A 297 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 297 GLU ASN LEU TYR PHE GLN GLY HIS MET GLU LYS VAL TYR
SEQRES 3 A 297 GLY LEU ILE GLY PHE PRO VAL GLU HIS SER LEU SER PRO
SEQRES 4 A 297 LEU MET HIS ASN ASP ALA PHE ALA ARG LEU GLY ILE PRO
SEQRES 5 A 297 ALA ARG TYR HIS LEU PHE SER VAL GLU PRO GLY GLN VAL
SEQRES 6 A 297 GLY ALA ALA ILE ALA GLY VAL ARG ALA LEU GLY ILE ALA
SEQRES 7 A 297 GLY VAL ASN VAL THR ILE PRO HIS LYS LEU ALA VAL ILE
SEQRES 8 A 297 PRO PHE LEU ASP GLU VAL ASP GLU HIS ALA ARG ARG ILE
SEQRES 9 A 297 GLY ALA VAL ASN THR ILE ILE ASN ASN ASP GLY ARG LEU
SEQRES 10 A 297 VAL GLY TYR ASN THR ASP GLY LEU GLY TYR VAL GLN ALA
SEQRES 11 A 297 LEU GLU GLU GLU MET ASN ILE THR LEU ASP GLY LYS ARG
SEQRES 12 A 297 ILE LEU VAL ILE GLY ALA GLY GLY GLY ALA ARG GLY ILE
SEQRES 13 A 297 TYR PHE SER LEU LEU SER THR ALA ALA GLU ARG ILE ASP
SEQRES 14 A 297 MET ALA ASN ARG THR VAL GLU LYS ALA GLU ARG LEU VAL
SEQRES 15 A 297 ARG GLU GLY ASP GLU ARG ARG SER ALA TYR PHE SER LEU
SEQRES 16 A 297 ALA GLU ALA GLU THR ARG LEU ALA GLU TYR ASP ILE ILE
SEQRES 17 A 297 ILE ASN THR THR SER VAL GLY MET HIS PRO ARG VAL GLU
SEQRES 18 A 297 VAL GLN PRO LEU SER LEU GLU ARG LEU ARG PRO GLY VAL
SEQRES 19 A 297 ILE VAL SER ASP ILE ILE TYR ASN PRO LEU GLU THR LYS
SEQRES 20 A 297 TRP LEU LYS GLU ALA LYS ALA ARG GLY ALA ARG VAL GLN
SEQRES 21 A 297 ASN GLY VAL GLY MET LEU VAL TYR GLN GLY ALA LEU ALA
SEQRES 22 A 297 PHE GLU LYS TRP THR GLY GLN TRP PRO ASP VAL ASN ARG
SEQRES 23 A 297 MET LYS GLN LEU VAL ILE GLU ALA LEU ARG ARG
SEQRES 1 B 297 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 B 297 GLU ASN LEU TYR PHE GLN GLY HIS MET GLU LYS VAL TYR
SEQRES 3 B 297 GLY LEU ILE GLY PHE PRO VAL GLU HIS SER LEU SER PRO
SEQRES 4 B 297 LEU MET HIS ASN ASP ALA PHE ALA ARG LEU GLY ILE PRO
SEQRES 5 B 297 ALA ARG TYR HIS LEU PHE SER VAL GLU PRO GLY GLN VAL
SEQRES 6 B 297 GLY ALA ALA ILE ALA GLY VAL ARG ALA LEU GLY ILE ALA
SEQRES 7 B 297 GLY VAL ASN VAL THR ILE PRO HIS LYS LEU ALA VAL ILE
SEQRES 8 B 297 PRO PHE LEU ASP GLU VAL ASP GLU HIS ALA ARG ARG ILE
SEQRES 9 B 297 GLY ALA VAL ASN THR ILE ILE ASN ASN ASP GLY ARG LEU
SEQRES 10 B 297 VAL GLY TYR ASN THR ASP GLY LEU GLY TYR VAL GLN ALA
SEQRES 11 B 297 LEU GLU GLU GLU MET ASN ILE THR LEU ASP GLY LYS ARG
SEQRES 12 B 297 ILE LEU VAL ILE GLY ALA GLY GLY GLY ALA ARG GLY ILE
SEQRES 13 B 297 TYR PHE SER LEU LEU SER THR ALA ALA GLU ARG ILE ASP
SEQRES 14 B 297 MET ALA ASN ARG THR VAL GLU LYS ALA GLU ARG LEU VAL
SEQRES 15 B 297 ARG GLU GLY ASP GLU ARG ARG SER ALA TYR PHE SER LEU
SEQRES 16 B 297 ALA GLU ALA GLU THR ARG LEU ALA GLU TYR ASP ILE ILE
SEQRES 17 B 297 ILE ASN THR THR SER VAL GLY MET HIS PRO ARG VAL GLU
SEQRES 18 B 297 VAL GLN PRO LEU SER LEU GLU ARG LEU ARG PRO GLY VAL
SEQRES 19 B 297 ILE VAL SER ASP ILE ILE TYR ASN PRO LEU GLU THR LYS
SEQRES 20 B 297 TRP LEU LYS GLU ALA LYS ALA ARG GLY ALA ARG VAL GLN
SEQRES 21 B 297 ASN GLY VAL GLY MET LEU VAL TYR GLN GLY ALA LEU ALA
SEQRES 22 B 297 PHE GLU LYS TRP THR GLY GLN TRP PRO ASP VAL ASN ARG
SEQRES 23 B 297 MET LYS GLN LEU VAL ILE GLU ALA LEU ARG ARG
HET CL A1001 1
HET CL A1002 1
HETNAM CL CHLORIDE ION
FORMUL 3 CL 2(CL 1-)
FORMUL 5 HOH *402(H2 O)
HELIX 1 1 LEU A 37 LEU A 49 1 13
HELIX 2 2 GLN A 64 GLY A 76 1 13
HELIX 3 3 VAL A 90 LEU A 94 5 5
HELIX 4 4 ASP A 98 GLY A 105 1 8
HELIX 5 5 THR A 122 MET A 135 1 14
HELIX 6 6 GLY A 150 SER A 162 1 13
HELIX 7 7 THR A 174 GLY A 185 1 12
HELIX 8 8 SER A 194 ARG A 201 1 8
HELIX 9 9 LEU A 202 TYR A 205 5 4
HELIX 10 10 THR A 246 ARG A 255 1 10
HELIX 11 11 GLY A 262 GLY A 279 1 18
HELIX 12 12 ASP A 283 ARG A 297 1 15
HELIX 13 13 LEU B 37 LEU B 49 1 13
HELIX 14 14 GLN B 64 GLY B 76 1 13
HELIX 15 15 VAL B 90 LEU B 94 5 5
HELIX 16 16 ASP B 98 GLY B 105 1 8
HELIX 17 17 THR B 122 MET B 135 1 14
HELIX 18 18 GLY B 262 GLY B 279 1 18
HELIX 19 19 ASP B 283 ARG B 296 1 14
SHEET 1 A 6 ALA A 53 SER A 59 0
SHEET 2 A 6 LYS A 24 GLY A 30 1 N LEU A 28 O PHE A 58
SHEET 3 A 6 GLY A 79 VAL A 82 1 O ASN A 81 N GLY A 27
SHEET 4 A 6 THR A 109 ASN A 113 -1 O ILE A 110 N VAL A 80
SHEET 5 A 6 ARG A 116 TYR A 120 -1 O TYR A 120 N THR A 109
SHEET 6 A 6 GLU A 96 VAL A 97 1 N GLU A 96 O GLY A 119
SHEET 1 B 6 TYR A 192 PHE A 193 0
SHEET 2 B 6 ARG A 167 ALA A 171 1 N MET A 170 O PHE A 193
SHEET 3 B 6 ARG A 143 ILE A 147 1 N ILE A 144 O ARG A 167
SHEET 4 B 6 ILE A 207 ASN A 210 1 O ILE A 209 N ILE A 147
SHEET 5 B 6 ILE A 235 ASP A 238 1 O SER A 237 N ILE A 208
SHEET 6 B 6 ARG A 258 GLN A 260 1 O ARG A 258 N VAL A 236
SHEET 1 C 6 ALA B 53 SER B 59 0
SHEET 2 C 6 LYS B 24 GLY B 30 1 N LEU B 28 O PHE B 58
SHEET 3 C 6 GLY B 79 VAL B 82 1 O ASN B 81 N ILE B 29
SHEET 4 C 6 THR B 109 ASN B 113 -1 O ILE B 110 N VAL B 80
SHEET 5 C 6 ARG B 116 TYR B 120 -1 O TYR B 120 N THR B 109
SHEET 6 C 6 GLU B 96 VAL B 97 1 N GLU B 96 O GLY B 119
CISPEP 1 PHE A 31 PRO A 32 0 0.50
CISPEP 2 ILE A 84 PRO A 85 0 -0.33
CISPEP 3 HIS A 217 PRO A 218 0 0.40
CISPEP 4 ASN A 242 PRO A 243 0 0.20
CISPEP 5 PHE B 31 PRO B 32 0 0.21
CISPEP 6 ILE B 84 PRO B 85 0 -0.09
SITE 1 AC1 2 MET A 265 GLN A 269
SITE 1 AC2 4 ASN A 113 ARG A 116 ARG A 180 HOH A1075
CRYST1 171.394 171.394 171.394 90.00 90.00 90.00 I 2 3 48
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 0.005835 0.000000 0.000000 0.00000
SCALE2 0.000000 0.005835 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005835 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
