HEADER TRANSFERASE 15-OCT-03 1R6L
TITLE CRYSTAL STRUCTURE OF THE TRNA PROCESSING ENZYME RNASE PH FROM
TITLE 2 PSEUDOMONAS AERUGINOSA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: RIBONUCLEASE PH;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: RNASE PH, TRNA NUCLEOTIDYLTRANSFERASE;
COMPND 5 EC: 2.7.7.56;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PSEUDOMONAS AERUGINOSA;
SOURCE 3 ORGANISM_TAXID: 287;
SOURCE 4 GENE: RPH;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: B834;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PQE30
KEYWDS BETA-ALPHA-BETA-ALPHA FOLD, HEXAMER, PHOSPHATE BOUND, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.M.CHOI,E.Y.PARK,J.H.KIM,S.K.CHANG,Y.CHO
REVDAT 3 13-JUL-11 1R6L 1 VERSN
REVDAT 2 24-FEB-09 1R6L 1 VERSN
REVDAT 1 17-FEB-04 1R6L 0
JRNL AUTH J.M.CHOI,E.Y.PARK,J.H.KIM,S.K.CHANG,Y.CHO
JRNL TITL PROBING THE FUNCTIONAL IMPORTANCE OF THE HEXAMERIC RING
JRNL TITL 2 STRUCTURE OF RNASE PH
JRNL REF J.BIOL.CHEM. V. 279 755 2004
JRNL REFN ISSN 0021-9258
JRNL PMID 14573594
JRNL DOI 10.1074/JBC.M309628200
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) : 26.01
REMARK 3 DATA CUTOFF (SIGMA(F)) : 1.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 1259160.300
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 98.6
REMARK 3 NUMBER OF REFLECTIONS : 21543
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) : 0.221
REMARK 3 FREE R VALUE : 0.244
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.900
REMARK 3 FREE R VALUE TEST SET COUNT : 1262
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.007
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) : 1.90
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.02
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 96.40
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 3272
REMARK 3 BIN R VALUE (WORKING SET) : 0.2390
REMARK 3 BIN FREE R VALUE : 0.2920
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.90
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 205
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.020
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1782
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 43
REMARK 3 SOLVENT ATOMS : 206
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 16.20
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 30.00
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.62000
REMARK 3 B22 (A**2) : 1.62000
REMARK 3 B33 (A**2) : -3.25000
REMARK 3 B12 (A**2) : 2.01000
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) : 0.23
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) : 0.27
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.19
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.006
REMARK 3 BOND ANGLES (DEGREES) : 1.30
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 23.20
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) : 1.450 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.100 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 2.270 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 3.270 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.41
REMARK 3 BSOL : 72.94
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 : SO4.PARAM
REMARK 3 PARAMETER FILE 3 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 4 : NHE.PARAM
REMARK 3 PARAMETER FILE 5 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : SO4.TOP
REMARK 3 TOPOLOGY FILE 3 : WATER.TOP
REMARK 3 TOPOLOGY FILE 4 : NHE.TOP
REMARK 3 TOPOLOGY FILE 5 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1R6L COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 20-OCT-03.
REMARK 100 THE RCSB ID CODE IS RCSB020499.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 28-MAY-03
REMARK 200 TEMPERATURE (KELVIN) : 103
REMARK 200 PH : 9.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PAL/PLS
REMARK 200 BEAMLINE : 6B
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9793, 0.9792, 0.9716
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL MONOCHROMATOR
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MACSCIENCE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 21859
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
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) : 1.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.97
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.6
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: MAD
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD
REMARK 200 SOFTWARE USED: SOLVE, RESOLVE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 48.80
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.42
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: AMMONIUM SULFATE, CHES, SODIUM
REMARK 280 CHLORIDE, PH 9.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: H 3 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z
REMARK 290 3555 -X+Y,-X,Z
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z
REMARK 290 6555 -X,-X+Y,-Z
REMARK 290 7555 X+2/3,Y+1/3,Z+1/3
REMARK 290 8555 -Y+2/3,X-Y+1/3,Z+1/3
REMARK 290 9555 -X+Y+2/3,-X+1/3,Z+1/3
REMARK 290 10555 Y+2/3,X+1/3,-Z+1/3
REMARK 290 11555 X-Y+2/3,-Y+1/3,-Z+1/3
REMARK 290 12555 -X+2/3,-X+Y+1/3,-Z+1/3
REMARK 290 13555 X+1/3,Y+2/3,Z+2/3
REMARK 290 14555 -Y+1/3,X-Y+2/3,Z+2/3
REMARK 290 15555 -X+Y+1/3,-X+2/3,Z+2/3
REMARK 290 16555 Y+1/3,X+2/3,-Z+2/3
REMARK 290 17555 X-Y+1/3,-Y+2/3,-Z+2/3
REMARK 290 18555 -X+1/3,-X+Y+2/3,-Z+2/3
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 0.00000
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 0.00000
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 0.00000
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 0.00000
REMARK 290 SMTRY1 7 1.000000 0.000000 0.000000 55.56950
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 32.08307
REMARK 290 SMTRY3 7 0.000000 0.000000 1.000000 38.61367
REMARK 290 SMTRY1 8 -0.500000 -0.866025 0.000000 55.56950
REMARK 290 SMTRY2 8 0.866025 -0.500000 0.000000 32.08307
REMARK 290 SMTRY3 8 0.000000 0.000000 1.000000 38.61367
REMARK 290 SMTRY1 9 -0.500000 0.866025 0.000000 55.56950
REMARK 290 SMTRY2 9 -0.866025 -0.500000 0.000000 32.08307
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 38.61367
REMARK 290 SMTRY1 10 -0.500000 0.866025 0.000000 55.56950
REMARK 290 SMTRY2 10 0.866025 0.500000 0.000000 32.08307
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 38.61367
REMARK 290 SMTRY1 11 1.000000 0.000000 0.000000 55.56950
REMARK 290 SMTRY2 11 0.000000 -1.000000 0.000000 32.08307
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 38.61367
REMARK 290 SMTRY1 12 -0.500000 -0.866025 0.000000 55.56950
REMARK 290 SMTRY2 12 -0.866025 0.500000 0.000000 32.08307
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 38.61367
REMARK 290 SMTRY1 13 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 64.16613
REMARK 290 SMTRY3 13 0.000000 0.000000 1.000000 77.22733
REMARK 290 SMTRY1 14 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 14 0.866025 -0.500000 0.000000 64.16613
REMARK 290 SMTRY3 14 0.000000 0.000000 1.000000 77.22733
REMARK 290 SMTRY1 15 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 15 -0.866025 -0.500000 0.000000 64.16613
REMARK 290 SMTRY3 15 0.000000 0.000000 1.000000 77.22733
REMARK 290 SMTRY1 16 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 16 0.866025 0.500000 0.000000 64.16613
REMARK 290 SMTRY3 16 0.000000 0.000000 -1.000000 77.22733
REMARK 290 SMTRY1 17 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 17 0.000000 -1.000000 0.000000 64.16613
REMARK 290 SMTRY3 17 0.000000 0.000000 -1.000000 77.22733
REMARK 290 SMTRY1 18 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 18 -0.866025 0.500000 0.000000 64.16613
REMARK 290 SMTRY3 18 0.000000 0.000000 -1.000000 77.22733
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 300 REMARK: THE BIOLOGICAL ASSEMBLY IS A HEXAMER GENERATED FROM THE
REMARK 300 MONOMER IN THE ASYMMETRIC UNIT BY THE OPERATIONS; (-Y, X-Y, Z ), (-
REMARK 300 X+Y, -X, Z), (Y, X, -Z), (X-Y, -Y , -Z) AND (-X, -X+Y, -Z)
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: HEXAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC
REMARK 350 SOFTWARE USED: PISA,PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 21840 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 55420 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -445.0 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 111.13900
REMARK 350 BIOMT2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 3 -0.500000 0.866025 0.000000 55.56950
REMARK 350 BIOMT2 3 -0.866025 -0.500000 0.000000 96.24920
REMARK 350 BIOMT3 3 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 4 -0.500000 0.866025 0.000000 55.56950
REMARK 350 BIOMT2 4 0.866025 0.500000 0.000000 -32.08307
REMARK 350 BIOMT3 4 0.000000 0.000000 -1.000000 -38.61367
REMARK 350 BIOMT1 5 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 5 0.000000 -1.000000 0.000000 64.16613
REMARK 350 BIOMT3 5 0.000000 0.000000 -1.000000 -38.61367
REMARK 350 BIOMT1 6 -0.500000 -0.866025 0.000000 111.13900
REMARK 350 BIOMT2 6 -0.866025 0.500000 0.000000 64.16613
REMARK 350 BIOMT3 6 0.000000 0.000000 -1.000000 -38.61367
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 54
REMARK 465 GLN A 55
REMARK 465 GLY A 56
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 49 -93.21 -56.45
REMARK 500 LEU A 52 -22.62 -152.72
REMARK 500 LYS A 83 140.39 174.94
REMARK 500 ASP A 123 47.06 -156.01
REMARK 500 GLN A 158 146.58 -171.36
REMARK 500 ASP A 175 79.98 62.24
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 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE
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: (10X,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 LYS A 23 24.7 L L OUTSIDE RANGE
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 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A2969 DISTANCE = 5.70 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1002
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1003
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1004
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1005
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1006
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NHE A 2854
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1R6M RELATED DB: PDB
REMARK 900 THE SAME PROTEIN COMPLEXED WITH PHOSPHATE
DBREF 1R6L A 1 239 UNP P50597 RNPH_PSEAE 1 239
SEQADV 1R6L MSE A 1 UNP P50597 MET 1 MODIFIED RESIDUE
SEQADV 1R6L MSE A 66 UNP P50597 MET 66 MODIFIED RESIDUE
SEQADV 1R6L MSE A 159 UNP P50597 MET 159 MODIFIED RESIDUE
SEQADV 1R6L MSE A 192 UNP P50597 MET 192 MODIFIED RESIDUE
SEQADV 1R6L MSE A 218 UNP P50597 MET 218 MODIFIED RESIDUE
SEQADV 1R6L MSE A 226 UNP P50597 MET 226 MODIFIED RESIDUE
SEQRES 1 A 239 MSE ASN ARG PRO SER GLY ARG ALA ALA ASP GLN LEU ARG
SEQRES 2 A 239 PRO ILE ARG ILE THR ARG HIS TYR THR LYS HIS ALA GLU
SEQRES 3 A 239 GLY SER VAL LEU VAL GLU PHE GLY ASP THR LYS VAL ILE
SEQRES 4 A 239 CYS THR VAL SER ALA GLU SER GLY VAL PRO ARG PHE LEU
SEQRES 5 A 239 LYS GLY GLN GLY GLN GLY TRP LEU THR ALA GLU TYR GLY
SEQRES 6 A 239 MSE LEU PRO ARG SER THR GLY GLU ARG ASN GLN ARG GLU
SEQRES 7 A 239 ALA SER ARG GLY LYS GLN GLY GLY ARG THR LEU GLU ILE
SEQRES 8 A 239 GLN ARG LEU ILE GLY ARG SER LEU ARG ALA ALA LEU ASP
SEQRES 9 A 239 LEU SER LYS LEU GLY GLU ASN THR LEU TYR ILE ASP CYS
SEQRES 10 A 239 ASP VAL ILE GLN ALA ASP GLY GLY THR ARG THR ALA SER
SEQRES 11 A 239 ILE THR GLY ALA THR VAL ALA LEU ILE ASP ALA LEU ALA
SEQRES 12 A 239 VAL LEU LYS LYS ARG GLY ALA LEU LYS GLY ASN PRO LEU
SEQRES 13 A 239 LYS GLN MSE VAL ALA ALA VAL SER VAL GLY ILE TYR GLN
SEQRES 14 A 239 GLY VAL PRO VAL LEU ASP LEU ASP TYR LEU GLU ASP SER
SEQRES 15 A 239 ALA ALA GLU THR ASP LEU ASN VAL VAL MSE THR ASP ALA
SEQRES 16 A 239 GLY GLY PHE ILE GLU VAL GLN GLY THR ALA GLU GLY ALA
SEQRES 17 A 239 PRO PHE ARG PRO ALA GLU LEU ASN ALA MSE LEU GLU LEU
SEQRES 18 A 239 ALA GLN GLN GLY MSE GLN GLU LEU PHE GLU LEU GLN ARG
SEQRES 19 A 239 ALA ALA LEU ALA GLU
MODRES 1R6L MSE A 1 MET SELENOMETHIONINE
MODRES 1R6L MSE A 66 MET SELENOMETHIONINE
MODRES 1R6L MSE A 159 MET SELENOMETHIONINE
MODRES 1R6L MSE A 192 MET SELENOMETHIONINE
MODRES 1R6L MSE A 218 MET SELENOMETHIONINE
MODRES 1R6L MSE A 226 MET SELENOMETHIONINE
HET MSE A 1 8
HET MSE A 66 8
HET MSE A 159 8
HET MSE A 192 8
HET MSE A 218 8
HET MSE A 226 8
HET SO4 A1001 5
HET SO4 A1002 5
HET SO4 A1003 5
HET SO4 A1004 5
HET SO4 A1005 5
HET SO4 A1006 5
HET NHE A2854 13
HETNAM MSE SELENOMETHIONINE
HETNAM SO4 SULFATE ION
HETNAM NHE 2-[N-CYCLOHEXYLAMINO]ETHANE SULFONIC ACID
HETSYN NHE N-CYCLOHEXYLTAURINE; CHES
FORMUL 1 MSE 6(C5 H11 N O2 SE)
FORMUL 2 SO4 6(O4 S 2-)
FORMUL 8 NHE C8 H17 N O3 S
FORMUL 9 HOH *206(H2 O)
HELIX 1 1 ARG A 77 GLY A 82 1 6
HELIX 2 2 GLY A 85 ALA A 102 1 18
HELIX 3 3 LEU A 103 LEU A 103 5 1
HELIX 4 4 ASP A 104 LEU A 108 5 5
HELIX 5 5 GLY A 125 ARG A 148 1 24
HELIX 6 6 ASP A 177 ALA A 184 1 8
HELIX 7 7 ARG A 211 ALA A 238 1 28
SHEET 1 A 5 ILE A 15 THR A 18 0
SHEET 2 A 5 GLY A 27 PHE A 33 -1 O GLU A 32 N ARG A 16
SHEET 3 A 5 THR A 36 SER A 46 -1 O CYS A 40 N VAL A 29
SHEET 4 A 5 ASN A 111 GLN A 121 -1 O GLN A 121 N LYS A 37
SHEET 5 A 5 TRP A 59 MSE A 66 1 N TRP A 59 O LEU A 113
SHEET 1 B 4 VAL A 171 LEU A 174 0
SHEET 2 B 4 VAL A 160 TYR A 168 -1 N GLY A 166 O VAL A 173
SHEET 3 B 4 THR A 186 THR A 193 -1 O LEU A 188 N VAL A 165
SHEET 4 B 4 PHE A 198 ALA A 205 -1 O ILE A 199 N VAL A 191
LINK C MSE A 1 N ASN A 2 1555 1555 1.33
LINK C GLY A 65 N MSE A 66 1555 1555 1.33
LINK C MSE A 66 N LEU A 67 1555 1555 1.33
LINK C GLN A 158 N MSE A 159 1555 1555 1.33
LINK C MSE A 159 N VAL A 160 1555 1555 1.33
LINK C VAL A 191 N MSE A 192 1555 1555 1.33
LINK C MSE A 192 N THR A 193 1555 1555 1.33
LINK C ALA A 217 N MSE A 218 1555 1555 1.33
LINK C MSE A 218 N LEU A 219 1555 1555 1.33
LINK C GLY A 225 N MSE A 226 1555 1555 1.33
LINK C MSE A 226 N GLN A 227 1555 1555 1.33
SITE 1 AC1 2 ARG A 81 LYS A 83
SITE 1 AC2 4 LYS A 37 NHE A2854 HOH A2888 HOH A2959
SITE 1 AC3 6 ARG A 87 GLY A 125 THR A 126 ARG A 127
SITE 2 AC3 6 HOH A2966 HOH A3057
SITE 1 AC4 6 ARG A 81 GLY A 85 GLY A 86 HOH A2904
SITE 2 AC4 6 HOH A2993 HOH A2997
SITE 1 AC5 6 SER A 5 ARG A 13 PRO A 14 GLY A 34
SITE 2 AC5 6 HOH A2859 HOH A2871
SITE 1 AC6 5 LYS A 23 ASP A 35 HOH A2918 HOH A2972
SITE 2 AC6 5 HOH A3051
SITE 1 AC7 7 THR A 18 TYR A 21 SO4 A1002 HOH A2860
SITE 2 AC7 7 HOH A2915 HOH A2927 HOH A2975
CRYST1 111.139 111.139 115.841 90.00 90.00 120.00 H 3 2 18
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 0.008998 0.005195 0.000000 0.00000
SCALE2 0.000000 0.010390 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008633 0.00000
HETATM 1 N MSE A 1 89.615 3.273 -39.632 1.00 42.75 N
HETATM 2 CA MSE A 1 88.931 4.151 -38.638 1.00 42.56 C
HETATM 3 C MSE A 1 89.880 5.252 -38.183 1.00 41.46 C
HETATM 4 O MSE A 1 90.852 4.991 -37.474 1.00 42.03 O
HETATM 5 CB MSE A 1 88.477 3.326 -37.427 1.00 43.87 C
HETATM 6 CG MSE A 1 87.598 4.069 -36.407 1.00 45.94 C
HETATM 7 SE MSE A 1 88.418 5.372 -35.438 1.00 45.97 SE
HETATM 8 CE MSE A 1 89.129 4.406 -34.124 1.00 41.36 C
(ATOM LINES ARE NOT SHOWN.)
END
