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PDBsum entry 3e7h

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Top Page protein Protein-protein interface(s) links
Transferase PDB id
3e7h
Jmol
Contents
Protein chains
102 a.a.
Waters ×263
HEADER    TRANSFERASE                             18-AUG-08   3E7H
TITLE     THE CRYSTAL STRUCTURE OF THE BETA SUBUNIT OF THE DNA-
TITLE    2 DIRECTED RNA POLYMERASE FROM VIBRIO CHOLERAE O1 BIOVAR
TITLE    3 ELTOR
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: DNA-DIRECTED RNA POLYMERASE SUBUNIT BETA;
COMPND   3 CHAIN: A, B;
COMPND   4 SYNONYM: RNAP SUBUNIT BETA, TRANSCRIPTASE SUBUNIT BETA,
COMPND   5 RNA POLYMERASE SUBUNIT BETA;
COMPND   6 EC: 2.7.7.6;
COMPND   7 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: VIBRIO CHOLERAE;
SOURCE   3 ORGANISM_TAXID: 666;
SOURCE   4 STRAIN: STR. N16961 CHROMOSOME I;
SOURCE   5 GENE: RPOB, VC_0328;
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PMCSG7
KEYWDS    DNA-DIRECTED RNA POLYMERASE, STRUCTURAL GENOMICS, PSI, MCSG,
KEYWDS   2 PROTEIN STRUCTURE INITIATIVE, MIDWEST CENTER FOR STRUCTURAL
KEYWDS   3 GENOMICS, NUCLEOTIDYLTRANSFERASE, TRANSCRIPTION, TRANSFERASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    R.ZHANG,R.WU,L.FREEMAN,A.JOACHIMIAK,MIDWEST CENTER FOR
AUTHOR   2 STRUCTURAL GENOMICS (MCSG)
REVDAT   2   24-FEB-09 3E7H    1       VERSN
REVDAT   1   14-OCT-08 3E7H    0
JRNL        AUTH   R.ZHANG,R.WU,L.FREEMAN,A.JOACHIMIAK
JRNL        TITL   THE CRYSTAL STRUCTURE OF THE BETA SUBUNIT OF THE
JRNL        TITL 2 DNA-DIRECTED RNA POLYMERASE FROM VIBRIO CHOLERAE
JRNL        TITL 3 O1 BIOVAR ELTOR
JRNL        REF    TO BE PUBLISHED
JRNL        REFN
REMARK   1
REMARK   2
REMARK   2 RESOLUTION.    1.70 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 WITH PHASES
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.70
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 45.98
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0
REMARK   3   NUMBER OF REFLECTIONS             : 26715
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) : 0.183
REMARK   3   R VALUE            (WORKING SET) : 0.181
REMARK   3   FREE R VALUE                     : 0.229
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000
REMARK   3   FREE R VALUE TEST SET COUNT      : 1414
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) : 1.70
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.74
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1920
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.95
REMARK   3   BIN R VALUE           (WORKING SET) : 0.1780
REMARK   3   BIN FREE R VALUE SET COUNT          : 108
REMARK   3   BIN FREE R VALUE                    : 0.2770
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 1595
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 0
REMARK   3   SOLVENT ATOMS            : 263
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 21.00
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 20.76
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 0.19000
REMARK   3    B22 (A**2) : 0.19000
REMARK   3    B33 (A**2) : -0.38000
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): 0.135
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.104
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.063
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.122
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.959
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.936
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  1611 ; 0.015 ; 0.022
REMARK   3   BOND LENGTHS OTHERS               (A):  1080 ; 0.002 ; 0.020
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  2175 ; 1.471 ; 1.969
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  2647 ; 0.909 ; 3.000
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   201 ; 6.081 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    80 ;27.569 ;25.250
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   300 ;12.598 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    12 ;18.118 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   257 ; 0.079 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1789 ; 0.005 ; 0.020
REMARK   3   GENERAL PLANES OTHERS             (A):   303 ; 0.001 ; 0.020
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   262 ; 0.222 ; 0.200
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  1141 ; 0.199 ; 0.200
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):   780 ; 0.169 ; 0.200
REMARK   3   NON-BONDED TORSION OTHERS         (A):   912 ; 0.084 ; 0.200
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   190 ; 0.196 ; 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):    23 ; 0.230 ; 0.200
REMARK   3   SYMMETRY VDW OTHERS               (A):    80 ; 0.272 ; 0.200
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    31 ; 0.331 ; 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):  1303 ; 1.824 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):   412 ; 0.876 ; 1.500
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  1625 ; 2.300 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   680 ; 4.096 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   550 ; 5.823 ; 4.500
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  : 1
REMARK   3
REMARK   3   TLS GROUP : 1
REMARK   3    NUMBER OF COMPONENTS GROUP : 2
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   A     0        A   100
REMARK   3    RESIDUE RANGE :   B     0        B   100
REMARK   3    ORIGIN FOR THE GROUP (A):  36.3470  25.0380  44.1660
REMARK   3    T TENSOR
REMARK   3      T11:  -0.0090 T22:  -0.0077
REMARK   3      T33:  -0.0479 T12:  -0.0040
REMARK   3      T13:  -0.0131 T23:   0.0020
REMARK   3    L TENSOR
REMARK   3      L11:   0.1883 L22:   0.2098
REMARK   3      L33:   0.1915 L12:  -0.0014
REMARK   3      L13:  -0.0149 L23:   0.0469
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0160 S12:   0.0192 S13:   0.0016
REMARK   3      S21:   0.0004 S22:   0.0029 S23:  -0.0267
REMARK   3      S31:   0.0063 S32:  -0.0259 S33:   0.0131
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
REMARK   3  RIDING POSITIONS
REMARK   4
REMARK   4 3E7H COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 19-AUG-08.
REMARK 100 THE RCSB ID CODE IS RCSB048971.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 23-APR-08
REMARK 200  TEMPERATURE           (KELVIN) : NULL
REMARK 200  PH                             : 6.5
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) : 0.9794
REMARK 200  MONOCHROMATOR                  : SI 111 CHANNEL
REMARK 200  OPTICS                         : MIRRORS
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL3000
REMARK 200  DATA SCALING SOFTWARE          : HKL3000
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 26715
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.700
REMARK 200  RESOLUTION RANGE LOW       (A) : 45.980
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 1.0
REMARK 200  DATA REDUNDANCY                : 18.500
REMARK 200  R MERGE                    (I) : 0.08100
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 50.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.70
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.74
REMARK 200  COMPLETENESS FOR SHELL     (%) : 1.0
REMARK 200  DATA REDUNDANCY IN SHELL       : 17.50
REMARK 200  R MERGE FOR SHELL          (I) : 0.72700
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : 2.580
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: HIKL3000
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 54.01
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.67
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 25% PEG3350, 0.1M BIS-TRIS, PH6.5,
REMARK 280  0.2M NACL , VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,-Y,Z+1/2
REMARK 290       3555   -Y+1/2,X+1/2,Z+3/4
REMARK 290       4555   Y+1/2,-X+1/2,Z+1/4
REMARK 290       5555   -X+1/2,Y+1/2,-Z+3/4
REMARK 290       6555   X+1/2,-Y+1/2,-Z+1/4
REMARK 290       7555   Y,X,-Z
REMARK 290       8555   -Y,-X,-Z+1/2
REMARK 290
REMARK 290     WHERE NNN -> OPERATOR NUMBER
REMARK 290           MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       57.99050
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       32.51750
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       32.51750
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       86.98575
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       32.51750
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       32.51750
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       28.99525
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       32.51750
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       32.51750
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       86.98575
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       32.51750
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       32.51750
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       28.99525
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       57.99050
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: THIS PROTEIN EXISTED AS TETRAMER A2B2. THE SECOND PART
REMARK 300 OF THE BIOLOGICAL ASSEMBLY OF MOL. A/B IS GENERATED BY THE
REMARK 300 OPERATION: Y,X,-Z+1
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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 7700 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 20520 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -55.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 350   BIOMT1   2  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT2   2  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000      115.98100
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   102
REMARK 465     ALA B   101
REMARK 465     GLY B   102
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   N    ALA A     0     O    HOH A   154              1.95
REMARK 500   N    ALA B     0     O    HOH B   215              2.05
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   O    HOH A   108     O    HOH B   217     7556     1.80
REMARK 500   O    HOH A   158     O    HOH B   138     5545     1.94
REMARK 500   O    HOH A   164     O    HOH B   115     7556     2.11
REMARK 500   O    HOH A   249     O    HOH B   161     8665     2.13
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    ASP B   7   CB  -  CG  -  OD1 ANGL. DEV. =   5.4 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: APC87466.1   RELATED DB: TARGETDB
DBREF  3E7H A    1   102  UNP    Q9KV30   RPOB_VIBCH     228    329
DBREF  3E7H B    1   102  UNP    Q9KV30   RPOB_VIBCH     228    329
SEQADV 3E7H ALA A    0  UNP  Q9KV30              EXPRESSION TAG
SEQADV 3E7H ALA B    0  UNP  Q9KV30              EXPRESSION TAG
SEQRES   1 A  103  ALA VAL ASN PHE GLU VAL LYS ASP GLN THR LEU MET MET
SEQRES   2 A  103  GLU LEU VAL PRO GLU ARG LEU ARG GLY GLU THR ALA THR
SEQRES   3 A  103  PHE ASP ILE GLU ALA ASP GLY LYS VAL TYR VAL GLU LYS
SEQRES   4 A  103  GLY ARG ARG VAL THR ALA ARG HIS ILE ARG GLN LEU GLU
SEQRES   5 A  103  LYS ASP GLY VAL ASN PHE ILE GLU VAL PRO VAL GLU TYR
SEQRES   6 A  103  ILE VAL GLY LYS VAL SER ALA LYS ASP TYR VAL ASN GLU
SEQRES   7 A  103  ALA THR GLY GLU LEU ILE ILE THR ALA ASN GLN GLU ILE
SEQRES   8 A  103  SER LEU GLU ALA LEU ALA ASN LEU SER GLN ALA GLY
SEQRES   1 B  103  ALA VAL ASN PHE GLU VAL LYS ASP GLN THR LEU MET MET
SEQRES   2 B  103  GLU LEU VAL PRO GLU ARG LEU ARG GLY GLU THR ALA THR
SEQRES   3 B  103  PHE ASP ILE GLU ALA ASP GLY LYS VAL TYR VAL GLU LYS
SEQRES   4 B  103  GLY ARG ARG VAL THR ALA ARG HIS ILE ARG GLN LEU GLU
SEQRES   5 B  103  LYS ASP GLY VAL ASN PHE ILE GLU VAL PRO VAL GLU TYR
SEQRES   6 B  103  ILE VAL GLY LYS VAL SER ALA LYS ASP TYR VAL ASN GLU
SEQRES   7 B  103  ALA THR GLY GLU LEU ILE ILE THR ALA ASN GLN GLU ILE
SEQRES   8 B  103  SER LEU GLU ALA LEU ALA ASN LEU SER GLN ALA GLY
FORMUL   3  HOH   *263(H2 O)
HELIX    1   1 VAL A   15  ARG A   20  1                                   6
HELIX    2   2 THR A   43  ASP A   53  1                                  11
HELIX    3   3 PRO A   61  GLY A   67  5                                   7
HELIX    4   4 SER A   91  ALA A  101  1                                  11
HELIX    5   5 VAL B   15  ARG B   20  1                                   6
HELIX    6   6 THR B   43  ASP B   53  1                                  11
HELIX    7   7 PRO B   61  GLY B   67  5                                   7
HELIX    8   8 SER B   91  GLN B  100  1                                  10
SHEET    1   A 3 PHE A  57  VAL A  60  0
SHEET    2   A 3 VAL A   1  GLU A  13 -1  N  MET A  12   O  ILE A  58
SHEET    3   A 3 GLU A  81  ILE A  90 -1  O  THR A  85   N  LYS A   6
SHEET    1   B 2 ILE A  28  ALA A  30  0
SHEET    2   B 2 LYS A  33  VAL A  36 -1  O  TYR A  35   N  ILE A  28
SHEET    1   C 3 PHE B  57  VAL B  60  0
SHEET    2   C 3 VAL B   1  LEU B  14 -1  N  LEU B  10   O  VAL B  60
SHEET    3   C 3 VAL B  75  ILE B  90 -1  O  ILE B  83   N  THR B   9
SHEET    1   D 2 ILE B  28  ALA B  30  0
SHEET    2   D 2 LYS B  33  VAL B  36 -1  O  VAL B  36   N  ILE B  28
CRYST1   65.035   65.035  115.981  90.00  90.00  90.00 P 43 21 2    16
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      0.015376  0.000000  0.000000        0.00000
SCALE2      0.000000  0.015376  0.000000        0.00000
SCALE3      0.000000  0.000000  0.008622        0.00000
      
PROCHECK
Go to PROCHECK summary
 References