HEADER TRANSFERASE 16-NOV-07 3BED
TITLE MANNOSE/SORBOSE SPECIFIC IIA SUBUNIT OF PHOSPHOTRANSFERASE SYSTEM FROM
TITLE 2 ENTEROCOCCUS FAECALIS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PTS SYSTEM, IIA COMPONENT;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ENTEROCOCCUS FAECALIS;
SOURCE 3 ORGANISM_TAXID: 226185;
SOURCE 4 STRAIN: V583;
SOURCE 5 ATCC: 700802;
SOURCE 6 GENE: EF_0461;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PMCSG7
KEYWDS MANNOSE/SORBOSE, PHOSPHOTRANSFERASE SYSTEM, STRUCTURAL GENOMICS,
KEYWDS 2 APC28805, PSI-2, PROTEIN STRUCTURE INITIATIVE, MIDWEST CENTER FOR
KEYWDS 3 STRUCTURAL GENOMICS, MCSG, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.OSIPIUK,R.WU,S.MOY,A.JOACHIMIAK,MIDWEST CENTER FOR STRUCTURAL
AUTHOR 2 GENOMICS (MCSG)
REVDAT 3 13-JUL-11 3BED 1 VERSN
REVDAT 2 24-FEB-09 3BED 1 VERSN
REVDAT 1 27-NOV-07 3BED 0
SPRSDE 27-NOV-07 3BED 2IAC
JRNL AUTH J.OSIPIUK,R.WU,S.MOY,A.JOACHIMIAK
JRNL TITL X-RAY CRYSTAL STRUCTURE OF MANNOSE/SORBOSE SPECIFIC IIA
JRNL TITL 2 SUBUNIT OF PHOSPHOTRANSFERASE SYSTEM FROM ENTEROCOCCUS
JRNL TITL 3 FAECALIS.
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.45 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.45
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 37.50
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 79.8
REMARK 3 NUMBER OF REFLECTIONS : 34957
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 + TEST SET) : 0.159
REMARK 3 R VALUE (WORKING SET) : 0.157
REMARK 3 FREE R VALUE : 0.197
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1872
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.45
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.49
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1029
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 32.01
REMARK 3 BIN R VALUE (WORKING SET) : 0.1870
REMARK 3 BIN FREE R VALUE SET COUNT : 53
REMARK 3 BIN FREE R VALUE : 0.2830
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1876
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 330
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 20.70
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 24.16
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -2.25000
REMARK 3 B22 (A**2) : 3.39000
REMARK 3 B33 (A**2) : -2.44000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -1.24000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.104
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.081
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.046
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.626
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.969
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.955
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2068 ; 0.017 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2852 ; 1.805 ; 2.020
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 311 ; 6.276 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 66 ;41.374 ;27.576
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 372 ;14.699 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 5 ;11.128 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 371 ; 0.332 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1493 ; 0.007 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1196 ; 0.242 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 1485 ; 0.310 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 264 ; 0.184 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 58 ; 0.272 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 14 ; 0.187 ; 0.200
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 1433 ; 1.697 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2258 ; 2.136 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 699 ; 4.732 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 569 ; 5.418 ; 4.500
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): 2132 ; 4.065 ; 3.000
REMARK 3 SPHERICITY; FREE ATOMS (A**2): 330 ; 6.648 ; 3.000
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): 2025 ; 4.280 ; 3.000
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 3BED COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-NOV-07.
REMARK 100 THE RCSB ID CODE IS RCSB045414.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 06-FEB-06
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 19-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97920
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 36836
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.450
REMARK 200 RESOLUTION RANGE LOW (A) : 37.500
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 79.6
REMARK 200 DATA REDUNDANCY : 7.300
REMARK 200 R MERGE (I) : 0.11700
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 35.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.45
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.48
REMARK 200 COMPLETENESS FOR SHELL (%) : 31.8
REMARK 200 DATA REDUNDANCY IN SHELL : 4.30
REMARK 200 R MERGE FOR SHELL (I) : 0.35100
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.180
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: HKL-3000, SHELXD, MLPHARE, DM, SOLVE/RESOLVE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 42.33
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.13
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M CALCIUM CHLORIDE, 0.1 M HEPES
REMARK 280 BUFFER, 30% PEG 4000, PH 7.5, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 294K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
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+1/2,Y+1/2,Z
REMARK 290 4555 -X+1/2,Y+1/2,-Z
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 53.02950
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 18.75150
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 53.02950
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 18.75150
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
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: AUTHORS STATE THAT THE BIOLOGICAL UNIT OF THIS PROTEIN IS
REMARK 300 UNKNOWN.
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: 3260 ANGSTROM**2
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: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 8200 ANGSTROM**2
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 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 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 A 207 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 148 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 188 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 SER A -2
REMARK 465 ASN A -1
REMARK 465 ALA A 0
REMARK 465 ASP A 133
REMARK 465 GLU A 134
REMARK 465 GLU A 135
REMARK 465 GLU A 136
REMARK 465 PHE A 137
REMARK 465 GLU A 138
REMARK 465 GLU A 139
REMARK 465 SER B -2
REMARK 465 ASN B -1
REMARK 465 ALA B 0
REMARK 465 GLU B 130
REMARK 465 LEU B 131
REMARK 465 THR B 132
REMARK 465 ASP B 133
REMARK 465 GLU B 134
REMARK 465 GLU B 135
REMARK 465 GLU B 136
REMARK 465 PHE B 137
REMARK 465 GLU B 138
REMARK 465 GLU B 139
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 O HOH B 201 O HOH B 256 1.87
REMARK 500 O LYS B 54 O HOH B 283 2.15
REMARK 500 O HOH B 159 O HOH B 285 2.17
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 LEU A 128 CB - CG - CD1 ANGL. DEV. = 10.4 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 MLY A 2 -85.22 -72.19
REMARK 500 ASP B 30 33.30 -140.87
REMARK 500 MLY B 68 118.69 -31.90
REMARK 500 LEU B 92 120.38 -37.38
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 MLY A 2 -35.3 L D WRONG HAND
REMARK 500 GLU A 130 24.9 L L OUTSIDE RANGE
REMARK 500 MLY B 2 -1.0 L D WRONG HAND
REMARK 500 MLY B 68 14.6 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 A 263 DISTANCE = 5.93 ANGSTROMS
REMARK 525 HOH A 269 DISTANCE = 5.23 ANGSTROMS
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: APC28805 RELATED DB: TARGETDB
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 LYSINE RESIDUES OF THE PROTEIN WERE CHEMICALLY
REMARK 999 DIMETHYLATED AFTER PROTEIN PURIFICATION.
DBREF 3BED A 1 139 UNP Q838I6 Q838I6_ENTFA 1 139
DBREF 3BED B 1 139 UNP Q838I6 Q838I6_ENTFA 1 139
SEQADV 3BED SER A -2 UNP Q838I6 EXPRESSION TAG
SEQADV 3BED ASN A -1 UNP Q838I6 EXPRESSION TAG
SEQADV 3BED ALA A 0 UNP Q838I6 EXPRESSION TAG
SEQADV 3BED SER B -2 UNP Q838I6 EXPRESSION TAG
SEQADV 3BED ASN B -1 UNP Q838I6 EXPRESSION TAG
SEQADV 3BED ALA B 0 UNP Q838I6 EXPRESSION TAG
SEQRES 1 A 142 SER ASN ALA MSE MLY PRO LYS LEU ILE LEU MSE SER HIS
SEQRES 2 A 142 GLY ARG MSE ALA GLU GLU THR LEU ALA SER THR GLN MSE
SEQRES 3 A 142 ILE VAL GLY GLU LEU ALA ASP ALA ALA ILE VAL SER MSE
SEQRES 4 A 142 THR ALA GLU ASP GLY LEU SER GLY THR GLN ALA LYS LEU
SEQRES 5 A 142 ALA ALA ILE LEU LYS GLU ALA GLY ASN VAL PRO THR LEU
SEQRES 6 A 142 VAL LEU ALA ASP LEU MLY GLY GLY THR PRO CYS ASN VAL
SEQRES 7 A 142 ALA MSE MSE ALA MSE GLY THR TYR PRO GLN LEU ARG VAL
SEQRES 8 A 142 VAL ALA GLY LEU ASN LEU ALA MSE ALA ILE GLU ALA ALA
SEQRES 9 A 142 VAL SER PRO VAL GLU ASN VAL ASP GLU LEU ALA ALA TYR
SEQRES 10 A 142 LEU THR GLN ILE GLY GLN SER ALA VAL THR THR ILE ASP
SEQRES 11 A 142 LEU PRO GLU LEU THR ASP GLU GLU GLU PHE GLU GLU
SEQRES 1 B 142 SER ASN ALA MSE MLY PRO LYS LEU ILE LEU MSE SER HIS
SEQRES 2 B 142 GLY ARG MSE ALA GLU GLU THR LEU ALA SER THR GLN MSE
SEQRES 3 B 142 ILE VAL GLY GLU LEU ALA ASP ALA ALA ILE VAL SER MSE
SEQRES 4 B 142 THR ALA GLU ASP GLY LEU SER GLY THR GLN ALA LYS LEU
SEQRES 5 B 142 ALA ALA ILE LEU LYS GLU ALA GLY ASN VAL PRO THR LEU
SEQRES 6 B 142 VAL LEU ALA ASP LEU MLY GLY GLY THR PRO CYS ASN VAL
SEQRES 7 B 142 ALA MSE MSE ALA MSE GLY THR TYR PRO GLN LEU ARG VAL
SEQRES 8 B 142 VAL ALA GLY LEU ASN LEU ALA MSE ALA ILE GLU ALA ALA
SEQRES 9 B 142 VAL SER PRO VAL GLU ASN VAL ASP GLU LEU ALA ALA TYR
SEQRES 10 B 142 LEU THR GLN ILE GLY GLN SER ALA VAL THR THR ILE ASP
SEQRES 11 B 142 LEU PRO GLU LEU THR ASP GLU GLU GLU PHE GLU GLU
MODRES 3BED MSE A 1 MET SELENOMETHIONINE
MODRES 3BED MLY A 2 LYS N-DIMETHYL-LYSINE
MODRES 3BED MSE A 8 MET SELENOMETHIONINE
MODRES 3BED MSE A 13 MET SELENOMETHIONINE
MODRES 3BED MSE A 23 MET SELENOMETHIONINE
MODRES 3BED MSE A 36 MET SELENOMETHIONINE
MODRES 3BED MLY A 68 LYS N-DIMETHYL-LYSINE
MODRES 3BED MSE A 77 MET SELENOMETHIONINE
MODRES 3BED MSE A 78 MET SELENOMETHIONINE
MODRES 3BED MSE A 80 MET SELENOMETHIONINE
MODRES 3BED MSE A 96 MET SELENOMETHIONINE
MODRES 3BED MSE B 1 MET SELENOMETHIONINE
MODRES 3BED MLY B 2 LYS N-DIMETHYL-LYSINE
MODRES 3BED MSE B 8 MET SELENOMETHIONINE
MODRES 3BED MSE B 13 MET SELENOMETHIONINE
MODRES 3BED MSE B 23 MET SELENOMETHIONINE
MODRES 3BED MSE B 36 MET SELENOMETHIONINE
MODRES 3BED MLY B 68 LYS N-DIMETHYL-LYSINE
MODRES 3BED MSE B 77 MET SELENOMETHIONINE
MODRES 3BED MSE B 78 MET SELENOMETHIONINE
MODRES 3BED MSE B 80 MET SELENOMETHIONINE
MODRES 3BED MSE B 96 MET SELENOMETHIONINE
HET MSE A 1 16
HET MLY A 2 11
HET MSE A 8 8
HET MSE A 13 8
HET MSE A 23 8
HET MSE A 36 8
HET MLY A 68 11
HET MSE A 77 13
HET MSE A 78 8
HET MSE A 80 8
HET MSE A 96 13
HET MSE B 1 13
HET MLY B 2 11
HET MSE B 8 8
HET MSE B 13 8
HET MSE B 23 8
HET MSE B 36 8
HET MLY B 68 11
HET MSE B 77 8
HET MSE B 78 8
HET MSE B 80 8
HET MSE B 96 16
HETNAM MSE SELENOMETHIONINE
HETNAM MLY N-DIMETHYL-LYSINE
FORMUL 1 MSE 18(C5 H11 N O2 SE)
FORMUL 1 MLY 4(C8 H18 N2 O2)
FORMUL 3 HOH *330(H2 O)
HELIX 1 1 ARG A 12 GLY A 26 1 15
HELIX 2 2 ASP A 40 GLY A 57 1 18
HELIX 3 3 GLY A 70 MSE A 80 1 11
HELIX 4 4 ASN A 93 SER A 103 1 11
HELIX 5 5 ASN A 107 ALA A 122 1 16
HELIX 6 6 ARG B 12 GLY B 26 1 15
HELIX 7 7 GLU B 27 ALA B 29 5 3
HELIX 8 8 ASP B 40 GLY B 57 1 18
HELIX 9 9 GLY B 70 MSE B 80 1 11
HELIX 10 10 ASN B 93 SER B 103 1 11
HELIX 11 11 ASN B 107 ALA B 122 1 16
SHEET 1 A 5 ALA A 32 MSE A 36 0
SHEET 2 A 5 LYS A 4 HIS A 10 1 N SER A 9 O MSE A 36
SHEET 3 A 5 THR A 61 ALA A 65 1 O LEU A 62 N LYS A 4
SHEET 4 A 5 LEU A 86 ALA A 90 1 O VAL A 89 N ALA A 65
SHEET 5 A 5 THR B 124 THR B 125 -1 O THR B 124 N ALA A 90
SHEET 1 B 5 THR A 124 ILE A 126 0
SHEET 2 B 5 LEU B 86 ALA B 90 -1 O ALA B 90 N THR A 124
SHEET 3 B 5 THR B 61 ALA B 65 1 N ALA B 65 O VAL B 89
SHEET 4 B 5 LYS B 4 HIS B 10 1 N LYS B 4 O LEU B 62
SHEET 5 B 5 ALA B 32 MSE B 36 1 O ALA B 32 N LEU B 7
LINK C AMSE A 1 N MLY A 2 1555 1555 1.33
LINK C BMSE A 1 N MLY A 2 1555 1555 1.33
LINK C MLY A 2 N PRO A 3 1555 1555 1.33
LINK C LEU A 7 N MSE A 8 1555 1555 1.33
LINK C MSE A 8 N SER A 9 1555 1555 1.34
LINK C ARG A 12 N MSE A 13 1555 1555 1.34
LINK C MSE A 13 N ALA A 14 1555 1555 1.34
LINK C GLN A 22 N MSE A 23 1555 1555 1.33
LINK C MSE A 23 N ILE A 24 1555 1555 1.33
LINK C SER A 35 N MSE A 36 1555 1555 1.33
LINK C MSE A 36 N THR A 37 1555 1555 1.31
LINK C LEU A 67 N MLY A 68 1555 1555 1.30
LINK C MLY A 68 N GLY A 69 1555 1555 1.34
LINK C ALA A 76 N MSE A 77 1555 1555 1.34
LINK C MSE A 77 N MSE A 78 1555 1555 1.34
LINK C MSE A 78 N ALA A 79 1555 1555 1.32
LINK C ALA A 79 N MSE A 80 1555 1555 1.33
LINK C MSE A 80 N GLY A 81 1555 1555 1.34
LINK C ALA A 95 N MSE A 96 1555 1555 1.33
LINK C MSE A 96 N ALA A 97 1555 1555 1.33
LINK C MSE B 1 N MLY B 2 1555 1555 1.32
LINK C MLY B 2 N PRO B 3 1555 1555 1.35
LINK C LEU B 7 N MSE B 8 1555 1555 1.33
LINK C MSE B 8 N SER B 9 1555 1555 1.33
LINK C ARG B 12 N MSE B 13 1555 1555 1.34
LINK C MSE B 13 N ALA B 14 1555 1555 1.34
LINK C GLN B 22 N MSE B 23 1555 1555 1.34
LINK C MSE B 23 N ILE B 24 1555 1555 1.32
LINK C SER B 35 N MSE B 36 1555 1555 1.35
LINK C MSE B 36 N THR B 37 1555 1555 1.34
LINK C LEU B 67 N MLY B 68 1555 1555 1.35
LINK C MLY B 68 N GLY B 69 1555 1555 1.34
LINK C ALA B 76 N MSE B 77 1555 1555 1.33
LINK C MSE B 77 N MSE B 78 1555 1555 1.34
LINK C MSE B 78 N ALA B 79 1555 1555 1.34
LINK C ALA B 79 N MSE B 80 1555 1555 1.33
LINK C MSE B 80 N GLY B 81 1555 1555 1.34
LINK C ALA B 95 N AMSE B 96 1555 1555 1.33
LINK C ALA B 95 N BMSE B 96 1555 1555 1.33
LINK C AMSE B 96 N ALA B 97 1555 1555 1.33
LINK C BMSE B 96 N ALA B 97 1555 1555 1.34
CRYST1 106.059 37.503 76.993 90.00 121.49 90.00 C 1 2 1 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 0.009429 0.000000 0.005777 0.00000
SCALE2 0.000000 0.026665 0.000000 0.00000
SCALE3 0.000000 0.000000 0.015232 0.00000
HETATM 1 N AMSE A 1 -15.599 33.068 25.995 0.30 27.25 N
ANISOU 1 N AMSE A 1 3363 3534 3456 -42 0 -47 N
HETATM 2 N BMSE A 1 -15.722 33.084 26.405 0.30 25.71 N
ANISOU 2 N BMSE A 1 3181 3354 3231 -1 61 -72 N
HETATM 3 CA AMSE A 1 -16.503 34.242 25.978 0.30 27.52 C
ANISOU 3 CA AMSE A 1 3413 3555 3485 -45 -14 -62 C
HETATM 4 CA BMSE A 1 -16.587 34.234 26.044 0.30 25.89 C
ANISOU 4 CA BMSE A 1 3231 3338 3268 0 50 -51 C
HETATM 5 C AMSE A 1 -17.768 33.878 25.209 0.30 27.10 C
ANISOU 5 C AMSE A 1 3340 3510 3446 -60 -8 -61 C
HETATM 6 C BMSE A 1 -17.558 33.843 24.948 0.30 26.06 C
ANISOU 6 C BMSE A 1 3230 3409 3260 -53 39 -50 C
HETATM 7 O AMSE A 1 -18.262 32.755 25.338 0.30 27.97 O
ANISOU 7 O AMSE A 1 3479 3570 3579 -29 27 -74 O
HETATM 8 O BMSE A 1 -17.618 32.680 24.562 0.30 26.92 O
ANISOU 8 O BMSE A 1 3372 3527 3327 -32 98 -30 O
HETATM 9 CB AMSE A 1 -15.806 35.443 25.347 0.30 27.96 C
ANISOU 9 CB AMSE A 1 3472 3572 3576 -43 -24 -86 C
HETATM 10 CB BMSE A 1 -15.756 35.401 25.557 0.30 25.93 C
ANISOU 10 CB BMSE A 1 3260 3308 3282 20 35 -51 C
HETATM 11 CG AMSE A 1 -15.958 35.580 23.839 0.30 29.45 C
ANISOU 11 CG AMSE A 1 3646 3830 3713 -90 -122 -80 C
HETATM 12 CG BMSE A 1 -16.598 36.527 24.966 0.30 25.78 C
ANISOU 12 CG BMSE A 1 3187 3305 3303 27 -1 -14 C
HETATM 13 SE AMSE A 1 -14.669 34.634 22.750 0.24 32.87 SE
ANISOU 13 SE AMSE A 1 3609 4629 4250 -224 -255 -554 SE
HETATM 14 SE BMSE A 1 -15.715 37.531 23.562 0.24 25.31 SE
ANISOU 14 SE BMSE A 1 3106 3182 3326 75 135 -95 SE
HETATM 15 CE AMSE A 1 -13.525 36.183 22.495 0.30 30.67 C
ANISOU 15 CE AMSE A 1 3725 4019 3909 18 -106 -142 C
HETATM 16 CE BMSE A 1 -14.776 36.060 22.661 0.30 21.23 C
ANISOU 16 CE BMSE A 1 2878 2547 2641 -10 17 161 C
HETATM 17 N MLY A 2 -18.291 34.836 24.442 1.00 26.85 N
ANISOU 17 N MLY A 2 3313 3529 3357 -113 35 -63 N
HETATM 18 CA MLY A 2 -19.409 34.620 23.488 1.00 26.18 C
ANISOU 18 CA MLY A 2 3140 3569 3237 -109 75 -74 C
HETATM 19 CB MLY A 2 -20.536 33.983 24.278 1.00 26.67 C
ANISOU 19 CB MLY A 2 3218 3668 3247 -204 114 12 C
HETATM 20 CG MLY A 2 -21.819 33.661 23.539 1.00 28.88 C
ANISOU 20 CG MLY A 2 3376 3853 3742 -280 71 15 C
HETATM 21 CD MLY A 2 -22.486 32.747 24.585 1.00 29.25 C
ANISOU 21 CD MLY A 2 3722 3785 3608 -182 19 208 C
HETATM 22 CE MLY A 2 -23.929 32.350 24.333 1.00 30.81 C
ANISOU 22 CE MLY A 2 3968 3905 3834 -212 -7 61 C
HETATM 23 NZ MLY A 2 -24.126 31.051 25.033 1.00 29.18 N
ANISOU 23 NZ MLY A 2 3799 4058 3227 -389 -63 194 N
HETATM 24 CH1 MLY A 2 -25.139 30.154 24.481 1.00 14.56 C
ANISOU 24 CH1 MLY A 2 2298 1914 1316 -309 570 -281 C
HETATM 25 CH2 MLY A 2 -24.432 31.330 26.438 1.00 31.79 C
ANISOU 25 CH2 MLY A 2 4109 4223 3743 -307 39 -222 C
HETATM 26 C MLY A 2 -18.927 33.823 22.279 1.00 24.54 C
ANISOU 26 C MLY A 2 2979 3290 3052 -72 50 -91 C
HETATM 27 O MLY A 2 -19.028 32.573 22.224 1.00 25.09 O
ANISOU 27 O MLY A 2 3037 3395 3099 -139 120 13 O
(ATOM LINES ARE NOT SHOWN.)
END
