HEADER HYDROLASE 18-JAN-10 3LFU
TITLE CRYSTAL STRUCTURE OF E. COLI UVRD
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DNA HELICASE II;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: C-TERMINAL TRUNCATION (UNP RESIDUES 1-647);
COMPND 5 EC: 3.6.1.-;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 GENE: B3813, JW3786, MUTU, PDEB, RAD, RECL, UVRD;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS DNA HELICASE, SF1 HELICASE, ATP-BINDING, DNA DAMAGE, DNA REPAIR, DNA
KEYWDS 2 REPLICATION, DNA-BINDING, HELICASE, HYDROLASE, NUCLEOTIDE-BINDING,
KEYWDS 3 SOS RESPONSE
EXPDTA X-RAY DIFFRACTION
AUTHOR S.KOROLEV,G.WAKSMAN,T.M.LOHMAN
REVDAT 6 21-FEB-24 3LFU 1 REMARK
REVDAT 5 17-JUL-19 3LFU 1 REMARK
REVDAT 4 01-NOV-17 3LFU 1 REMARK
REVDAT 3 30-NOV-11 3LFU 1 JRNL VERSN
REVDAT 2 06-JUL-11 3LFU 1 JRNL
REVDAT 1 02-FEB-11 3LFU 0
JRNL AUTH H.JIA,S.KOROLEV,A.NIEDZIELA-MAJKA,N.K.MALUF,G.H.GAUSS,
JRNL AUTH 2 S.MYONG,T.HA,G.WAKSMAN,T.M.LOHMAN
JRNL TITL ROTATIONS OF THE 2B SUB-DOMAIN OF E. COLI UVRD
JRNL TITL 2 HELICASE/TRANSLOCASE COUPLED TO NUCLEOTIDE AND DNA BINDING.
JRNL REF J.MOL.BIOL. V. 411 633 2011
JRNL REFN ISSN 0022-2836
JRNL PMID 21704638
JRNL DOI 10.1016/J.JMB.2011.06.019
REMARK 2
REMARK 2 RESOLUTION. 1.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0102
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.54
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 91.0
REMARK 3 NUMBER OF REFLECTIONS : 67970
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) : 0.202
REMARK 3 R VALUE (WORKING SET) : 0.199
REMARK 3 FREE R VALUE : 0.248
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 3393
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) : 1.80
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.85
REMARK 3 REFLECTION IN BIN (WORKING SET) : 5193
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.98
REMARK 3 BIN R VALUE (WORKING SET) : 0.2700
REMARK 3 BIN FREE R VALUE SET COUNT : 250
REMARK 3 BIN FREE R VALUE : 0.3110
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5039
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 20
REMARK 3 SOLVENT ATOMS : 721
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 25.75
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.03000
REMARK 3 B22 (A**2) : 0.00000
REMARK 3 B33 (A**2) : -0.03000
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 OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.140
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.140
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.087
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.730
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.949
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.923
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 5143 ; 0.011 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 6944 ; 1.763 ; 1.954
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 628 ; 6.802 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 265 ;35.092 ;23.509
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 903 ;16.260 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 54 ;21.233 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 751 ; 0.180 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3932 ; 0.013 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
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): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
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): 3132 ; 1.554 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 4987 ; 2.577 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2011 ; 4.284 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1957 ; 6.297 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
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 : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3LFU COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-JAN-10.
REMARK 100 THE DEPOSITION ID IS D_1000057225.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-MAR-99
REMARK 200 TEMPERATURE (KELVIN) : 130
REMARK 200 PH : 9.1
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) : 0.99188
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : SBC-2
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK, HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 70609
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 94.0
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.06400
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) : 1.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.83
REMARK 200 COMPLETENESS FOR SHELL (%) : 86.0
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.22400
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 54.05
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.68
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.0 M (NH4)2SO4, PH 9.1, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 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+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 97.27150
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 29.36950
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 97.27150
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 29.36950
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
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 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A 1
REMARK 465 ASP A 2
REMARK 465 GLN A 160
REMARK 465 SER A 161
REMARK 465 TYR A 162
REMARK 465 GLY A 163
REMARK 465 TYR A 521
REMARK 465 ASN A 522
REMARK 465 GLU A 523
REMARK 465 GLU A 524
REMARK 465 ASP A 525
REMARK 465 ALA A 542
REMARK 465 ASP A 587
REMARK 465 GLU A 588
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 VAL A 3 CG1 CG2
REMARK 470 HIS A 157 CG ND1 CD2 CE1 NE2
REMARK 470 HIS A 158 CG ND1 CD2 CE1 NE2
REMARK 470 ILE A 159 CB CG1 CG2 CD1
REMARK 470 ASN A 164 CB CG OD1 ND2
REMARK 470 PRO A 165 CG CD
REMARK 470 GLU A 167 CG CD OE1 OE2
REMARK 470 GLN A 168 CG CD OE1 NE2
REMARK 470 SER A 520 OG
REMARK 470 GLU A 526 CG CD OE1 OE2
REMARK 470 GLU A 544 CB CG CD OE1 OE2
REMARK 470 GLN A 546 CB CG CD OE1 NE2
REMARK 470 ALA A 547 CB
REMARK 470 ASP A 548 CG OD1 OD2
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 SG CYS A 52 O HOH A 716 2.07
REMARK 500 ND1 HIS A 91 O HOH A 803 2.15
REMARK 500 O HOH A 832 O HOH A 1316 2.16
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ARG A 42 NE - CZ - NH1 ANGL. DEV. = 7.9 DEGREES
REMARK 500 ARG A 42 NE - CZ - NH2 ANGL. DEV. = -5.4 DEGREES
REMARK 500 ASP A 110 C - N - CA ANGL. DEV. = -15.2 DEGREES
REMARK 500 PRO A 165 N - CA - CB ANGL. DEV. = 7.6 DEGREES
REMARK 500 ARG A 211 NE - CZ - NH1 ANGL. DEV. = -3.4 DEGREES
REMARK 500 ARG A 211 NE - CZ - NH2 ANGL. DEV. = 3.1 DEGREES
REMARK 500 ASP A 220 CB - CG - OD1 ANGL. DEV. = 6.3 DEGREES
REMARK 500 ASP A 224 CB - CG - OD1 ANGL. DEV. = 6.5 DEGREES
REMARK 500 ARG A 278 NE - CZ - NH1 ANGL. DEV. = -6.6 DEGREES
REMARK 500 ARG A 278 NE - CZ - NH2 ANGL. DEV. = 4.2 DEGREES
REMARK 500 SER A 285 CB - CA - C ANGL. DEV. = 11.8 DEGREES
REMARK 500 LEU A 290 CB - CG - CD1 ANGL. DEV. = 12.2 DEGREES
REMARK 500 ARG A 361 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 ARG A 361 NE - CZ - NH2 ANGL. DEV. = -5.7 DEGREES
REMARK 500 LEU A 397 CB - CG - CD1 ANGL. DEV. = 10.2 DEGREES
REMARK 500 LEU A 437 CB - CG - CD1 ANGL. DEV. = 11.3 DEGREES
REMARK 500 LEU A 509 CB - CG - CD1 ANGL. DEV. = 10.4 DEGREES
REMARK 500 ARG A 596 CD - NE - CZ ANGL. DEV. = 8.8 DEGREES
REMARK 500 ARG A 596 NE - CZ - NH1 ANGL. DEV. = 7.0 DEGREES
REMARK 500 ARG A 596 NE - CZ - NH2 ANGL. DEV. = -9.2 DEGREES
REMARK 500 ARG A 618 CG - CD - NE ANGL. DEV. = -16.3 DEGREES
REMARK 500 ARG A 618 NE - CZ - NH2 ANGL. DEV. = -3.2 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 ASP A 110 55.84 -107.89
REMARK 500 ASP A 133 102.92 -59.80
REMARK 500 HIS A 157 -130.26 -93.60
REMARK 500 HIS A 158 -91.13 -95.80
REMARK 500 GLU A 497 73.86 -100.04
REMARK 500 LEU A 540 -80.49 -78.89
REMARK 500 GLU A 544 171.45 58.08
REMARK 500 GLN A 546 45.58 83.61
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 GLY A 273 ALA A 274 -128.28
REMARK 500 LEU A 528 MET A 529 131.97
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 ARG A 596 0.08 SIDE CHAIN
REMARK 500 ARG A 618 0.07 SIDE CHAIN
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 SO4 A 1000
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1002
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1003
DBREF 3LFU A 1 647 UNP P03018 UVRD_ECOLI 1 647
SEQRES 1 A 647 MET ASP VAL SER TYR LEU LEU ASP SER LEU ASN ASP LYS
SEQRES 2 A 647 GLN ARG GLU ALA VAL ALA ALA PRO ARG SER ASN LEU LEU
SEQRES 3 A 647 VAL LEU ALA GLY ALA GLY SER GLY LYS THR ARG VAL LEU
SEQRES 4 A 647 VAL HIS ARG ILE ALA TRP LEU MET SER VAL GLU ASN CYS
SEQRES 5 A 647 SER PRO TYR SER ILE MET ALA VAL THR PHE THR ASN LYS
SEQRES 6 A 647 ALA ALA ALA GLU MET ARG HIS ARG ILE GLY GLN LEU MET
SEQRES 7 A 647 GLY THR SER GLN GLY GLY MET TRP VAL GLY THR PHE HIS
SEQRES 8 A 647 GLY LEU ALA HIS ARG LEU LEU ARG ALA HIS HIS MET ASP
SEQRES 9 A 647 ALA ASN LEU PRO GLN ASP PHE GLN ILE LEU ASP SER GLU
SEQRES 10 A 647 ASP GLN LEU ARG LEU LEU LYS ARG LEU ILE LYS ALA MET
SEQRES 11 A 647 ASN LEU ASP GLU LYS GLN TRP PRO PRO ARG GLN ALA MET
SEQRES 12 A 647 TRP TYR ILE ASN SER GLN LYS ASP GLU GLY LEU ARG PRO
SEQRES 13 A 647 HIS HIS ILE GLN SER TYR GLY ASN PRO VAL GLU GLN THR
SEQRES 14 A 647 TRP GLN LYS VAL TYR GLN ALA TYR GLN GLU ALA CYS ASP
SEQRES 15 A 647 ARG ALA GLY LEU VAL ASP PHE ALA GLU LEU LEU LEU ARG
SEQRES 16 A 647 ALA HIS GLU LEU TRP LEU ASN LYS PRO HIS ILE LEU GLN
SEQRES 17 A 647 HIS TYR ARG GLU ARG PHE THR ASN ILE LEU VAL ASP GLU
SEQRES 18 A 647 PHE GLN ASP THR ASN ASN ILE GLN TYR ALA TRP ILE ARG
SEQRES 19 A 647 LEU LEU ALA GLY ASP THR GLY LYS VAL MET ILE VAL GLY
SEQRES 20 A 647 ASP ASP ASP GLN SER ILE TYR GLY TRP ARG GLY ALA GLN
SEQRES 21 A 647 VAL GLU ASN ILE GLN ARG PHE LEU ASN ASP PHE PRO GLY
SEQRES 22 A 647 ALA GLU THR ILE ARG LEU GLU GLN ASN TYR ARG SER THR
SEQRES 23 A 647 SER ASN ILE LEU SER ALA ALA ASN ALA LEU ILE GLU ASN
SEQRES 24 A 647 ASN ASN GLY ARG LEU GLY LYS LYS LEU TRP THR ASP GLY
SEQRES 25 A 647 ALA ASP GLY GLU PRO ILE SER LEU TYR CYS ALA PHE ASN
SEQRES 26 A 647 GLU LEU ASP GLU ALA ARG PHE VAL VAL ASN ARG ILE LYS
SEQRES 27 A 647 THR TRP GLN ASP ASN GLY GLY ALA LEU ALA GLU CYS ALA
SEQRES 28 A 647 ILE LEU TYR ARG SER ASN ALA GLN SER ARG VAL LEU GLU
SEQRES 29 A 647 GLU ALA LEU LEU GLN ALA SER MET PRO TYR ARG ILE TYR
SEQRES 30 A 647 GLY GLY MET ARG PHE PHE GLU ARG GLN GLU ILE LYS ASP
SEQRES 31 A 647 ALA LEU SER TYR LEU ARG LEU ILE ALA ASN ARG ASN ASP
SEQRES 32 A 647 ASP ALA ALA PHE GLU ARG VAL VAL ASN THR PRO THR ARG
SEQRES 33 A 647 GLY ILE GLY ASP ARG THR LEU ASP VAL VAL ARG GLN THR
SEQRES 34 A 647 SER ARG ASP ARG GLN LEU THR LEU TRP GLN ALA CYS ARG
SEQRES 35 A 647 GLU LEU LEU GLN GLU LYS ALA LEU ALA GLY ARG ALA ALA
SEQRES 36 A 647 SER ALA LEU GLN ARG PHE MET GLU LEU ILE ASP ALA LEU
SEQRES 37 A 647 ALA GLN GLU THR ALA ASP MET PRO LEU HIS VAL GLN THR
SEQRES 38 A 647 ASP ARG VAL ILE LYS ASP SER GLY LEU ARG THR MET TYR
SEQRES 39 A 647 GLU GLN GLU LYS GLY GLU LYS GLY GLN THR ARG ILE GLU
SEQRES 40 A 647 ASN LEU GLU GLU LEU VAL THR ALA THR ARG GLN PHE SER
SEQRES 41 A 647 TYR ASN GLU GLU ASP GLU ASP LEU MET PRO LEU GLN ALA
SEQRES 42 A 647 PHE LEU SER HIS ALA ALA LEU GLU ALA GLY GLU GLY GLN
SEQRES 43 A 647 ALA ASP THR TRP GLN ASP ALA VAL GLN LEU MET THR LEU
SEQRES 44 A 647 HIS SER ALA LYS GLY LEU GLU PHE PRO GLN VAL PHE ILE
SEQRES 45 A 647 VAL GLY MET GLU GLU GLY MET PHE PRO SER GLN MET SER
SEQRES 46 A 647 LEU ASP GLU GLY GLY ARG LEU GLU GLU GLU ARG ARG LEU
SEQRES 47 A 647 ALA TYR VAL GLY VAL THR ARG ALA MET GLN LYS LEU THR
SEQRES 48 A 647 LEU THR TYR ALA GLU THR ARG ARG LEU TYR GLY LYS GLU
SEQRES 49 A 647 VAL TYR HIS ARG PRO SER ARG PHE ILE GLY GLU LEU PRO
SEQRES 50 A 647 GLU GLU CYS VAL GLU GLU VAL ARG LEU ARG
HET SO4 A1000 5
HET SO4 A1001 5
HET SO4 A1002 5
HET SO4 A1003 5
HETNAM SO4 SULFATE ION
FORMUL 2 SO4 4(O4 S 2-)
FORMUL 6 HOH *721(H2 O)
HELIX 1 1 VAL A 3 ASP A 8 1 6
HELIX 2 2 ASN A 11 ALA A 19 1 9
HELIX 3 3 GLY A 34 VAL A 49 1 16
HELIX 4 4 SER A 53 TYR A 55 5 3
HELIX 5 5 THR A 63 GLY A 79 1 17
HELIX 6 6 PHE A 90 HIS A 101 1 12
HELIX 7 7 HIS A 102 ASN A 106 5 5
HELIX 8 8 ASP A 115 MET A 130 1 16
HELIX 9 9 PRO A 138 GLU A 152 1 15
HELIX 10 10 PRO A 165 GLY A 185 1 21
HELIX 11 11 PHE A 189 LYS A 203 1 15
HELIX 12 12 LYS A 203 PHE A 214 1 12
HELIX 13 13 GLU A 221 THR A 225 5 5
HELIX 14 14 ASN A 226 GLY A 238 1 13
HELIX 15 15 ASP A 248 SER A 252 5 5
HELIX 16 16 TYR A 254 GLY A 258 5 5
HELIX 17 17 GLU A 262 PHE A 271 1 10
HELIX 18 18 THR A 286 GLU A 298 1 13
HELIX 19 19 GLU A 326 ASN A 343 1 18
HELIX 20 20 ALA A 346 ALA A 348 5 3
HELIX 21 21 SER A 356 ALA A 358 5 3
HELIX 22 22 GLN A 359 ALA A 370 1 12
HELIX 23 23 ARG A 381 GLU A 384 5 4
HELIX 24 24 ARG A 385 ASN A 400 1 16
HELIX 25 25 ASP A 403 VAL A 411 1 9
HELIX 26 26 GLY A 419 ARG A 433 1 15
HELIX 27 27 THR A 436 GLU A 447 1 12
HELIX 28 28 ALA A 451 THR A 472 1 22
HELIX 29 29 PRO A 476 SER A 488 1 13
HELIX 30 30 GLY A 489 GLN A 496 1 8
HELIX 31 31 GLY A 499 SER A 520 1 22
HELIX 32 32 MET A 529 GLU A 541 1 13
HELIX 33 33 HIS A 560 LYS A 563 5 4
HELIX 34 34 ARG A 591 THR A 604 1 14
HELIX 35 35 SER A 630 LEU A 636 1 7
HELIX 36 36 PRO A 637 GLU A 639 5 3
SHEET 1 A 6 TRP A 86 THR A 89 0
SHEET 2 A 6 ILE A 57 THR A 61 1 N ALA A 59 O TRP A 86
SHEET 3 A 6 ASN A 216 VAL A 219 1 O LEU A 218 N VAL A 60
SHEET 4 A 6 LYS A 242 GLY A 247 1 O MET A 244 N ILE A 217
SHEET 5 A 6 LEU A 25 ALA A 29 1 N VAL A 27 O ILE A 245
SHEET 6 A 6 GLU A 275 LEU A 279 1 O ILE A 277 N LEU A 26
SHEET 1 B 2 GLN A 112 LEU A 114 0
SHEET 2 B 2 LEU A 186 ASP A 188 1 O VAL A 187 N LEU A 114
SHEET 1 C 6 TYR A 374 ILE A 376 0
SHEET 2 C 6 VAL A 554 THR A 558 1 O LEU A 556 N ARG A 375
SHEET 3 C 6 CYS A 350 TYR A 354 1 N CYS A 350 O GLN A 555
SHEET 4 C 6 PHE A 567 ILE A 572 1 O PHE A 571 N LEU A 353
SHEET 5 C 6 ALA A 606 LEU A 620 1 O MET A 607 N PHE A 567
SHEET 6 C 6 LYS A 623 TYR A 626 -1 O LYS A 623 N LEU A 620
SHEET 1 D 7 TYR A 374 ILE A 376 0
SHEET 2 D 7 VAL A 554 THR A 558 1 O LEU A 556 N ARG A 375
SHEET 3 D 7 CYS A 350 TYR A 354 1 N CYS A 350 O GLN A 555
SHEET 4 D 7 PHE A 567 ILE A 572 1 O PHE A 571 N LEU A 353
SHEET 5 D 7 ALA A 606 LEU A 620 1 O MET A 607 N PHE A 567
SHEET 6 D 7 ILE A 318 ASN A 325 1 N ALA A 323 O TYR A 614
SHEET 7 D 7 VAL A 641 GLU A 643 1 O GLU A 642 N ILE A 318
CISPEP 1 THR A 413 PRO A 414 0 -3.33
CISPEP 2 PHE A 580 PRO A 581 0 7.70
SITE 1 AC1 9 ALA A 31 GLY A 32 GLN A 251 ARG A 284
SITE 2 AC1 9 GLY A 564 ARG A 605 HOH A 856 HOH A 951
SITE 3 AC1 9 HOH A1341
SITE 1 AC2 8 THR A 63 ASN A 64 LYS A 65 ARG A 211
SITE 2 AC2 8 HOH A 779 HOH A 977 HOH A1090 HOH A1227
SITE 1 AC3 10 GLY A 34 LYS A 35 THR A 36 ARG A 37
SITE 2 AC3 10 ARG A 73 HOH A 839 HOH A 892 HOH A 908
SITE 3 AC3 10 HOH A1289 HOH A1295
SITE 1 AC4 7 LYS A 135 ARG A 460 HOH A 875 HOH A1066
SITE 2 AC4 7 HOH A1107 HOH A1238 HOH A1338
CRYST1 194.543 58.739 69.418 90.00 90.00 90.00 P 21 21 2 4
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 0.005140 0.000000 0.000000 0.00000
SCALE2 0.000000 0.017024 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014405 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
