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PDBsum entry 1iwg

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Membrane protein PDB id
1iwg
Jmol
Contents
Protein chain
1006 a.a. *
* Residue conservation analysis
HEADER    MEMBRANE PROTEIN                        15-MAY-02   1IWG
TITLE     CRYSTAL STRUCTURE OF BACTERIAL MULTIDRUG EFFLUX TRANSPORTER ACRB
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: ACRB;
COMPND   3 CHAIN: A;
COMPND   4 SYNONYM: MULTIDRUG EFFLUX PROTEIN;
COMPND   5 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE   3 ORGANISM_TAXID: 562;
SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI K12;
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 83333;
SOURCE   6 EXPRESSION_SYSTEM_STRAIN: K12;
SOURCE   7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PUC-118
KEYWDS    DRUG RESISTANCE, MULTIDRUG EFFLUX, TRANSPORTER, ANTIPORTER, MEMBRANE
KEYWDS   2 PROTEIN
EXPDTA    X-RAY DIFFRACTION
AUTHOR    S.MURAKAMI,R.NAKASHIMA,E.YAMASHITA,A.YAMAGUCHI
REVDAT   3   13-JUL-11 1IWG    1       VERSN
REVDAT   2   24-FEB-09 1IWG    1       VERSN
REVDAT   1   23-OCT-02 1IWG    0
JRNL        AUTH   S.MURAKAMI,R.NAKASHIMA,E.YAMASHITA,A.YAMAGUCHI
JRNL        TITL   CRYSTAL STRUCTURE OF BACTERIAL MULTIDRUG EFFLUX TRANSPORTER
JRNL        TITL 2 ACRB
JRNL        REF    NATURE                        V. 419   587 2002
JRNL        REFN                   ISSN 0028-0836
JRNL        PMID   12374972
JRNL        DOI    10.1038/NATURE01050
REMARK   2
REMARK   2 RESOLUTION.    3.50 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : CNS
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK   3               : READ,RICE,SIMONSON,WARREN
REMARK   3
REMARK   3  REFINEMENT TARGET : ENGH & HUBER
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.50
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 8.00
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)   (%) : NULL
REMARK   3   NUMBER OF REFLECTIONS             : 198425
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   CROSS-VALIDATION METHOD          : NULL
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM
REMARK   3   R VALUE            (WORKING SET) : 0.290
REMARK   3   FREE R VALUE                     : 0.355
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL
REMARK   3   FREE R VALUE TEST SET COUNT      : 9921
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) : NULL
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL
REMARK   3   BIN R VALUE           (WORKING SET) : NULL
REMARK   3   BIN FREE R VALUE                    : NULL
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 7639
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 0
REMARK   3   SOLVENT ATOMS            : 0
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : NULL
REMARK   3    B22 (A**2) : NULL
REMARK   3    B33 (A**2) : NULL
REMARK   3    B12 (A**2) : NULL
REMARK   3    B13 (A**2) : NULL
REMARK   3    B23 (A**2) : NULL
REMARK   3
REMARK   3  ESTIMATED COORDINATE ERROR.
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL
REMARK   3   ESD FROM SIGMAA              (A) : NULL
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL
REMARK   3
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.
REMARK   3   BOND LENGTHS                 (A) : NULL
REMARK   3   BOND ANGLES            (DEGREES) : NULL
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL MODEL : NULL
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 1IWG COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 21-MAY-02.
REMARK 100 THE RCSB ID CODE IS RCSB005340.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 10-FEB-01
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 6.1
REMARK 200  NUMBER OF CRYSTALS USED        : 4
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : SPRING-8
REMARK 200  BEAMLINE                       : BL44XU
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.900
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE
REMARK 200  DETECTOR MANUFACTURER          : MAC SCIENCE DIP-2040
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 198425
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.500
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.8
REMARK 200  DATA REDUNDANCY                : 7.500
REMARK 200  R MERGE                    (I) : 0.09000
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 11.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.50
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.63
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.6
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.10
REMARK 200  R MERGE FOR SHELL          (I) : 0.36500
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : 2.600
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MIR
REMARK 200 SOFTWARE USED: SOLVE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 73.07
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.57
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 2000, SODIUM PHOSPHATE, SODIUM
REMARK 280  CITRATE, GLYCEROL, DODECYL MALTOSIDE, PH 6.1, VAPOR DIFFUSION,
REMARK 280  SITTING DROP, TEMPERATURE 298K
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       72.26800
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       41.72395
REMARK 290   SMTRY3   7  0.000000  0.000000  1.000000      173.05933
REMARK 290   SMTRY1   8 -0.500000 -0.866025  0.000000       72.26800
REMARK 290   SMTRY2   8  0.866025 -0.500000  0.000000       41.72395
REMARK 290   SMTRY3   8  0.000000  0.000000  1.000000      173.05933
REMARK 290   SMTRY1   9 -0.500000  0.866025  0.000000       72.26800
REMARK 290   SMTRY2   9 -0.866025 -0.500000  0.000000       41.72395
REMARK 290   SMTRY3   9  0.000000  0.000000  1.000000      173.05933
REMARK 290   SMTRY1  10 -0.500000  0.866025  0.000000       72.26800
REMARK 290   SMTRY2  10  0.866025  0.500000  0.000000       41.72395
REMARK 290   SMTRY3  10  0.000000  0.000000 -1.000000      173.05933
REMARK 290   SMTRY1  11  1.000000  0.000000  0.000000       72.26800
REMARK 290   SMTRY2  11  0.000000 -1.000000  0.000000       41.72395
REMARK 290   SMTRY3  11  0.000000  0.000000 -1.000000      173.05933
REMARK 290   SMTRY1  12 -0.500000 -0.866025  0.000000       72.26800
REMARK 290   SMTRY2  12 -0.866025  0.500000  0.000000       41.72395
REMARK 290   SMTRY3  12  0.000000  0.000000 -1.000000      173.05933
REMARK 290   SMTRY1  13  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2  13  0.000000  1.000000  0.000000       83.44790
REMARK 290   SMTRY3  13  0.000000  0.000000  1.000000      346.11867
REMARK 290   SMTRY1  14 -0.500000 -0.866025  0.000000        0.00000
REMARK 290   SMTRY2  14  0.866025 -0.500000  0.000000       83.44790
REMARK 290   SMTRY3  14  0.000000  0.000000  1.000000      346.11867
REMARK 290   SMTRY1  15 -0.500000  0.866025  0.000000        0.00000
REMARK 290   SMTRY2  15 -0.866025 -0.500000  0.000000       83.44790
REMARK 290   SMTRY3  15  0.000000  0.000000  1.000000      346.11867
REMARK 290   SMTRY1  16 -0.500000  0.866025  0.000000        0.00000
REMARK 290   SMTRY2  16  0.866025  0.500000  0.000000       83.44790
REMARK 290   SMTRY3  16  0.000000  0.000000 -1.000000      346.11867
REMARK 290   SMTRY1  17  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2  17  0.000000 -1.000000  0.000000       83.44790
REMARK 290   SMTRY3  17  0.000000  0.000000 -1.000000      346.11867
REMARK 290   SMTRY1  18 -0.500000 -0.866025  0.000000        0.00000
REMARK 290   SMTRY2  18 -0.866025  0.500000  0.000000       83.44790
REMARK 290   SMTRY3  18  0.000000  0.000000 -1.000000      346.11867
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: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA,PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 18180 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 112580 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -78.0 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      144.53600
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       72.26800
REMARK 350   BIOMT2   3 -0.866025 -0.500000  0.000000      125.17185
REMARK 350   BIOMT3   3  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     PRO A     2
REMARK 465     ASN A     3
REMARK 465     PHE A     4
REMARK 465     PHE A     5
REMARK 465     ILE A     6
REMARK 465     PRO A   499
REMARK 465     ILE A   500
REMARK 465     ALA A   501
REMARK 465     LYS A   502
REMARK 465     GLY A   503
REMARK 465     ASP A   504
REMARK 465     HIS A   505
REMARK 465     GLY A   506
REMARK 465     GLU A   507
REMARK 465     GLY A   508
REMARK 465     LYS A   509
REMARK 465     LYS A   510
REMARK 465     GLY A   511
REMARK 465     PHE A   512
REMARK 465     ASP A   711
REMARK 465     THR A   860
REMARK 465     GLY A   861
REMARK 465     MET A   862
REMARK 465     SER A   863
REMARK 465     TYR A   864
REMARK 465     GLN A   865
REMARK 465     GLU A   866
REMARK 465     ARG A   867
REMARK 465     LEU A   868
REMARK 465     ASN A  1037
REMARK 465     GLU A  1038
REMARK 465     ASP A  1039
REMARK 465     ILE A  1040
REMARK 465     GLU A  1041
REMARK 465     HIS A  1042
REMARK 465     SER A  1043
REMARK 465     HIS A  1044
REMARK 465     THR A  1045
REMARK 465     VAL A  1046
REMARK 465     ASP A  1047
REMARK 465     HIS A  1048
REMARK 465     HIS A  1049
REMARK 465     HIS A  1050
REMARK 465     HIS A  1051
REMARK 465     HIS A  1052
REMARK 465     HIS A  1053
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    VAL A   946     N    LYS A   950              2.07
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE
REMARK 500   NE2  HIS A   525     NE2  HIS A   525     4556     2.10
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    LYS A 950   C   -  N   -  CA  ANGL. DEV. = -28.1 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    PRO A   9     -100.24    -53.81
REMARK 500    ILE A  10      -96.44      2.45
REMARK 500    PHE A  11      -63.65    -22.96
REMARK 500    LEU A  21      -77.68    -67.45
REMARK 500    ALA A  22      -47.98    -28.77
REMARK 500    LEU A  28       39.20    -75.56
REMARK 500    LYS A  29       17.77   -178.20
REMARK 500    ALA A  33     -173.98    -55.97
REMARK 500    GLN A  34     -148.16    -71.65
REMARK 500    THR A  37      109.98    -45.33
REMARK 500    TYR A  49       87.31   -164.16
REMARK 500    PRO A  50      111.63    -33.32
REMARK 500    ALA A  52      142.30    -29.59
REMARK 500    THR A  56      -70.39    -46.59
REMARK 500    THR A  60      -34.91   -139.39
REMARK 500    THR A  62      -87.99    -72.42
REMARK 500    GLN A  63      -37.56    -31.16
REMARK 500    ASN A  70      145.22   -170.95
REMARK 500    ASN A  74      136.63     64.50
REMARK 500    LEU A  75      129.15    170.69
REMARK 500    THR A  85        2.68    -66.60
REMARK 500    GLN A  89       85.11   -156.11
REMARK 500    VAL A 107      -15.54    -48.10
REMARK 500    PRO A 116       -6.15    -51.71
REMARK 500    GLN A 125     -159.36    -85.43
REMARK 500    SER A 133        4.13   -159.58
REMARK 500    SER A 134       43.45     19.02
REMARK 500    SER A 135      124.98   -178.62
REMARK 500    LEU A 137      -85.62   -165.63
REMARK 500    ASP A 146      -99.67    -64.39
REMARK 500    THR A 150      150.70    -36.56
REMARK 500    GLN A 151       23.92    -67.90
REMARK 500    GLU A 152      -32.53   -134.10
REMARK 500    ALA A 160       51.70   -144.19
REMARK 500    ASN A 161      -24.62    165.66
REMARK 500    ALA A 165      -72.15    -84.74
REMARK 500    SER A 167       14.90    -64.59
REMARK 500    ARG A 168      -28.58   -143.09
REMARK 500    SER A 170       87.27     -1.65
REMARK 500    PHE A 178       81.54    -68.78
REMARK 500    SER A 180      148.94   -174.38
REMARK 500    ALA A 183      147.28   -175.99
REMARK 500    ASN A 191      -70.13    -41.09
REMARK 500    LYS A 195       -0.97    -57.97
REMARK 500    GLN A 197       65.71     60.61
REMARK 500    LYS A 208       27.24    -68.51
REMARK 500    ALA A 209      -41.69   -138.57
REMARK 500    ALA A 212      145.30   -175.92
REMARK 500    LYS A 226      116.19    -33.32
REMARK 500    ALA A 236     -152.11   -109.81
REMARK 500
REMARK 500 THIS ENTRY HAS     159 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 650
REMARK 650 HELIX
REMARK 650 DETERMINATION METHOD: AUTHOR DETERMINED
REMARK 700
REMARK 700 SHEET
REMARK 700 DETERMINATION METHOD: AUTHOR DETERMINED
DBREF  1IWG A    1  1049  UNP    P31224   ACRB_ECOLI       1   1049
SEQADV 1IWG HIS A 1050  UNP  P31224              EXPRESSION TAG
SEQADV 1IWG HIS A 1051  UNP  P31224              EXPRESSION TAG
SEQADV 1IWG HIS A 1052  UNP  P31224              EXPRESSION TAG
SEQADV 1IWG HIS A 1053  UNP  P31224              EXPRESSION TAG
SEQRES   1 A 1053  MET PRO ASN PHE PHE ILE ASP ARG PRO ILE PHE ALA TRP
SEQRES   2 A 1053  VAL ILE ALA ILE ILE ILE MET LEU ALA GLY GLY LEU ALA
SEQRES   3 A 1053  ILE LEU LYS LEU PRO VAL ALA GLN TYR PRO THR ILE ALA
SEQRES   4 A 1053  PRO PRO ALA VAL THR ILE SER ALA SER TYR PRO GLY ALA
SEQRES   5 A 1053  ASP ALA LYS THR VAL GLN ASP THR VAL THR GLN VAL ILE
SEQRES   6 A 1053  GLU GLN ASN MET ASN GLY ILE ASP ASN LEU MET TYR MET
SEQRES   7 A 1053  SER SER ASN SER ASP SER THR GLY THR VAL GLN ILE THR
SEQRES   8 A 1053  LEU THR PHE GLU SER GLY THR ASP ALA ASP ILE ALA GLN
SEQRES   9 A 1053  VAL GLN VAL GLN ASN LYS LEU GLN LEU ALA MET PRO LEU
SEQRES  10 A 1053  LEU PRO GLN GLU VAL GLN GLN GLN GLY VAL SER VAL GLU
SEQRES  11 A 1053  LYS SER SER SER SER PHE LEU MET VAL VAL GLY VAL ILE
SEQRES  12 A 1053  ASN THR ASP GLY THR MET THR GLN GLU ASP ILE SER ASP
SEQRES  13 A 1053  TYR VAL ALA ALA ASN MET LYS ASP ALA ILE SER ARG THR
SEQRES  14 A 1053  SER GLY VAL GLY ASP VAL GLN LEU PHE GLY SER GLN TYR
SEQRES  15 A 1053  ALA MET ARG ILE TRP MET ASN PRO ASN GLU LEU ASN LYS
SEQRES  16 A 1053  PHE GLN LEU THR PRO VAL ASP VAL ILE THR ALA ILE LYS
SEQRES  17 A 1053  ALA GLN ASN ALA GLN VAL ALA ALA GLY GLN LEU GLY GLY
SEQRES  18 A 1053  THR PRO PRO VAL LYS GLY GLN GLN LEU ASN ALA SER ILE
SEQRES  19 A 1053  ILE ALA GLN THR ARG LEU THR SER THR GLU GLU PHE GLY
SEQRES  20 A 1053  LYS ILE LEU LEU LYS VAL ASN GLN ASP GLY SER ARG VAL
SEQRES  21 A 1053  LEU LEU ARG ASP VAL ALA LYS ILE GLU LEU GLY GLY GLU
SEQRES  22 A 1053  ASN TYR ASP ILE ILE ALA GLU PHE ASN GLY GLN PRO ALA
SEQRES  23 A 1053  SER GLY LEU GLY ILE LYS LEU ALA THR GLY ALA ASN ALA
SEQRES  24 A 1053  LEU ASP THR ALA ALA ALA ILE ARG ALA GLU LEU ALA LYS
SEQRES  25 A 1053  MET GLU PRO PHE PHE PRO SER GLY LEU LYS ILE VAL TYR
SEQRES  26 A 1053  PRO TYR ASP THR THR PRO PHE VAL LYS ILE SER ILE HIS
SEQRES  27 A 1053  GLU VAL VAL LYS THR LEU VAL GLU ALA ILE ILE LEU VAL
SEQRES  28 A 1053  PHE LEU VAL MET TYR LEU PHE LEU GLN ASN PHE ARG ALA
SEQRES  29 A 1053  THR LEU ILE PRO THR ILE ALA VAL PRO VAL VAL LEU LEU
SEQRES  30 A 1053  GLY THR PHE ALA VAL LEU ALA ALA PHE GLY PHE SER ILE
SEQRES  31 A 1053  ASN THR LEU THR MET PHE GLY MET VAL LEU ALA ILE GLY
SEQRES  32 A 1053  LEU LEU VAL ASP ASP ALA ILE VAL VAL VAL GLU ASN VAL
SEQRES  33 A 1053  GLU ARG VAL MET ALA GLU GLU GLY LEU PRO PRO LYS GLU
SEQRES  34 A 1053  ALA THR ARG LYS SER MET GLY GLN ILE GLN GLY ALA LEU
SEQRES  35 A 1053  VAL GLY ILE ALA MET VAL LEU SER ALA VAL PHE VAL PRO
SEQRES  36 A 1053  MET ALA PHE PHE GLY GLY SER THR GLY ALA ILE TYR ARG
SEQRES  37 A 1053  GLN PHE SER ILE THR ILE VAL SER ALA MET ALA LEU SER
SEQRES  38 A 1053  VAL LEU VAL ALA LEU ILE LEU THR PRO ALA LEU CYS ALA
SEQRES  39 A 1053  THR MET LEU LYS PRO ILE ALA LYS GLY ASP HIS GLY GLU
SEQRES  40 A 1053  GLY LYS LYS GLY PHE PHE GLY TRP PHE ASN ARG MET PHE
SEQRES  41 A 1053  GLU LYS SER THR HIS HIS TYR THR ASP SER VAL GLY GLY
SEQRES  42 A 1053  ILE LEU ARG SER THR GLY ARG TYR LEU VAL LEU TYR LEU
SEQRES  43 A 1053  ILE ILE VAL VAL GLY MET ALA TYR LEU PHE VAL ARG LEU
SEQRES  44 A 1053  PRO SER SER PHE LEU PRO ASP GLU ASP GLN GLY VAL PHE
SEQRES  45 A 1053  MET THR MET VAL GLN LEU PRO ALA GLY ALA THR GLN GLU
SEQRES  46 A 1053  ARG THR GLN LYS VAL LEU ASN GLU VAL THR HIS TYR TYR
SEQRES  47 A 1053  LEU THR LYS GLU LYS ASN ASN VAL GLU SER VAL PHE ALA
SEQRES  48 A 1053  VAL ASN GLY PHE GLY PHE ALA GLY ARG GLY GLN ASN THR
SEQRES  49 A 1053  GLY ILE ALA PHE VAL SER LEU LYS ASP TRP ALA ASP ARG
SEQRES  50 A 1053  PRO GLY GLU GLU ASN LYS VAL GLU ALA ILE THR MET ARG
SEQRES  51 A 1053  ALA THR ARG ALA PHE SER GLN ILE LYS ASP ALA MET VAL
SEQRES  52 A 1053  PHE ALA PHE ASN LEU PRO ALA ILE VAL GLU LEU GLY THR
SEQRES  53 A 1053  ALA THR GLY PHE ASP PHE GLU LEU ILE ASP GLN ALA GLY
SEQRES  54 A 1053  LEU GLY HIS GLU LYS LEU THR GLN ALA ARG ASN GLN LEU
SEQRES  55 A 1053  LEU ALA GLU ALA ALA LYS HIS PRO ASP MET LEU THR SER
SEQRES  56 A 1053  VAL ARG PRO ASN GLY LEU GLU ASP THR PRO GLN PHE LYS
SEQRES  57 A 1053  ILE ASP ILE ASP GLN GLU LYS ALA GLN ALA LEU GLY VAL
SEQRES  58 A 1053  SER ILE ASN ASP ILE ASN THR THR LEU GLY ALA ALA TRP
SEQRES  59 A 1053  GLY GLY SER TYR VAL ASN ASP PHE ILE ASP ARG GLY ARG
SEQRES  60 A 1053  VAL LYS LYS VAL TYR VAL MET SER GLU ALA LYS TYR ARG
SEQRES  61 A 1053  MET LEU PRO ASP ASP ILE GLY ASP TRP TYR VAL ARG ALA
SEQRES  62 A 1053  ALA ASP GLY GLN MET VAL PRO PHE SER ALA PHE SER SER
SEQRES  63 A 1053  SER ARG TRP GLU TYR GLY SER PRO ARG LEU GLU ARG TYR
SEQRES  64 A 1053  ASN GLY LEU PRO SER MET GLU ILE LEU GLY GLN ALA ALA
SEQRES  65 A 1053  PRO GLY LYS SER THR GLY GLU ALA MET GLU LEU MET GLU
SEQRES  66 A 1053  GLN LEU ALA SER LYS LEU PRO THR GLY VAL GLY TYR ASP
SEQRES  67 A 1053  TRP THR GLY MET SER TYR GLN GLU ARG LEU SER GLY ASN
SEQRES  68 A 1053  GLN ALA PRO SER LEU TYR ALA ILE SER LEU ILE VAL VAL
SEQRES  69 A 1053  PHE LEU CYS LEU ALA ALA LEU TYR GLU SER TRP SER ILE
SEQRES  70 A 1053  PRO PHE SER VAL MET LEU VAL VAL PRO LEU GLY VAL ILE
SEQRES  71 A 1053  GLY ALA LEU LEU ALA ALA THR PHE ARG GLY LEU THR ASN
SEQRES  72 A 1053  ASP VAL TYR PHE GLN VAL GLY LEU LEU THR THR ILE GLY
SEQRES  73 A 1053  LEU SER ALA LYS ASN ALA ILE LEU ILE VAL GLU PHE ALA
SEQRES  74 A 1053  LYS ASP LEU MET ASP LYS GLU GLY LYS GLY LEU ILE GLU
SEQRES  75 A 1053  ALA THR LEU ASP ALA VAL ARG MET ARG LEU ARG PRO ILE
SEQRES  76 A 1053  LEU MET THR SER LEU ALA PHE ILE LEU GLY VAL MET PRO
SEQRES  77 A 1053  LEU VAL ILE SER THR GLY ALA GLY SER GLY ALA GLN ASN
SEQRES  78 A 1053  ALA VAL GLY THR GLY VAL MET GLY GLY MET VAL THR ALA
SEQRES  79 A 1053  THR VAL LEU ALA ILE PHE PHE VAL PRO VAL PHE PHE VAL
SEQRES  80 A 1053  VAL VAL ARG ARG ARG PHE SER ARG LYS ASN GLU ASP ILE
SEQRES  81 A 1053  GLU HIS SER HIS THR VAL ASP HIS HIS HIS HIS HIS HIS
HELIX    1   1 ARG A    8  LEU A   28  1                                  21
HELIX    2   2 ASP A   53  ASP A   59  1                                   7
HELIX    3   3 VAL A   61  MET A   69  1                                   9
HELIX    4   4 ASP A   99  GLN A  108  1                                  10
HELIX    5   5 ASN A  109  ASN A  109  5                                   1
HELIX    6   6 LYS A  110  LEU A  118  5                                   9
HELIX    7   7 GLN A  120  GLN A  124  1                                   5
HELIX    8   8 GLU A  152  ALA A  159  1                                   8
HELIX    9   9 MET A  162  SER A  167  1                                   6
HELIX   10  10 ASN A  189  LYS A  195  1                                   7
HELIX   11  11 THR A  199  ASN A  211  1                                  13
HELIX   12  12 SER A  242  LYS A  248  1                                   7
HELIX   13  13 LEU A  262  VAL A  265  1                                   4
HELIX   14  14 ALA A  299  LEU A  310  1                                  12
HELIX   15  15 ALA A  311  LYS A  312  5                                   2
HELIX   16  16 MET A  313  PHE A  317  5                                   5
HELIX   17  17 THR A  329  LEU A  357  1                                  29
HELIX   18  18 ASN A  361  ALA A  385  1                                  25
HELIX   19  19 ASN A  391  GLU A  423  1                                  33
HELIX   20  20 PRO A  427  SER A  434  1                                   8
HELIX   21  21 GLN A  437  PHE A  458  1                                  22
HELIX   22  22 THR A  463  ALA A  485  1                                  23
HELIX   23  23 ILE A  487  MET A  496  1                                  10
HELIX   24  24 PHE A  513  HIS A  525  1                                  13
HELIX   25  25 HIS A  525  ARG A  536  1                                  12
HELIX   26  26 THR A  538  ARG A  558  1                                  21
HELIX   27  27 THR A  583  LYS A  601  1                                  19
HELIX   28  28 ASP A  633  ARG A  637  5                                   5
HELIX   29  29 LYS A  643  ILE A  658  1                                  16
HELIX   30  30 GLY A  691  HIS A  709  1                                  19
HELIX   31  31 ASP A  732  GLY A  740  1                                   9
HELIX   32  32 SER A  742  GLY A  755  1                                  14
HELIX   33  33 GLU A  776  ARG A  780  5                                   5
HELIX   34  34 LEU A  782  GLY A  787  5                                   6
HELIX   35  35 SER A  802  PHE A  804  5                                   3
HELIX   36  36 SER A  836  SER A  849  1                                  14
HELIX   37  37 GLN A  872  TYR A  892  1                                  21
HELIX   38  38 SER A  896  VAL A  901  1                                   6
HELIX   39  39 LEU A  903  ARG A  919  1                                  17
HELIX   40  40 ASP A  924  GLU A  956  1                                  33
HELIX   41  41 ILE A  961  MET A  970  1                                  10
HELIX   42  42 LEU A  972  ILE A  991  1                                  20
HELIX   43  43 SER A  997  ALA A 1018  1                                  22
HELIX   44  44 VAL A 1024  PHE A 1033  1                                  10
SHEET    1   A10 VAL A 127  LYS A 131  0
SHEET    2   A10 ALA A  42  SER A  48 -1
SHEET    3   A10 THR A  87  THR A  93 -1
SHEET    4   A10 TYR A  77  ASP A  83 -1
SHEET    5   A10 ARG A 815  TYR A 819 -1
SHEET    6   A10 LEU A 822  GLN A 830 -1
SHEET    7   A10 SER A 715  PRO A 718 -1
SHEET    8   A10 LEU A 822  GLN A 830 -1
SHEET    9   A10 GLY A 679  ASP A 686 -1
SHEET   10   A10 VAL A 855  ASP A 858 -1
SHEET    1   B10 LEU A 321  VAL A 324  0
SHEET    2   B10 PHE A 136  ASN A 144 -1
SHEET    3   B10 GLN A 284  LYS A 292 -1
SHEET    4   B10 ASP A 174  LEU A 177 -1
SHEET    5   B10 GLN A 284  LYS A 292 -1
SHEET    6   B10 ILE A 278  PHE A 281 -1
SHEET    7   B10 VAL A 606  VAL A 612 -1
SHEET    8   B10 ASN A 623  LEU A 631 -1
SHEET    9   B10 PHE A 572  GLN A 577 -1
SHEET   10   B10 ALA A 661  ASN A 667 -1
SHEET    1   C 6 ALA A 266  GLY A 272  0
SHEET    2   C 6 TYR A 182  MET A 188 -1
SHEET    3   C 6 ARG A 767  VAL A 773  1
SHEET    4   C 6 GLY A 756  TYR A 758 -1
SHEET    5   C 6 ARG A 767  VAL A 773 -1
SHEET    6   C 6 ASN A 760  ASP A 764 -1
SHEET    1   D 3 GLN A 218  GLY A 220  0
SHEET    2   D 3 ASN A 231  LEU A 240 -1
SHEET    3   D 3 ASN A 211  VAL A 214 -1
SHEET    1   E 2 LEU A 250  ASN A 254  0
SHEET    2   E 2 SER A 258  LEU A 261 -1
SHEET    1   F 2 THR A 724  ILE A 729  0
SHEET    2   F 2 SER A 807  GLY A 812 -1
SHEET    1   G 2 TYR A 790  ALA A 793  0
SHEET    2   G 2 GLN A 797  PRO A 800 -1
SHEET    1   H 2 GLY A 614  GLY A 616  0
SHEET    2   H 2 GLY A 619  GLY A 621 -1
CRYST1  144.536  144.536  519.178  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      0.006919  0.003995  0.000000        0.00000
SCALE2      0.000000  0.007989  0.000000        0.00000
SCALE3      0.000000  0.000000  0.001926        0.00000
      
PROCHECK
Go to PROCHECK summary
 References