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PDBsum entry 2gih

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Top Page protein dna_rna metals Protein-protein interface(s) links
Hydrolase/DNA PDB id
2gih
Jmol
Contents
Protein chains
257 a.a.
DNA/RNA
Metals
_CA ×2
Waters ×363
HEADER    HYDROLASE/DNA                           28-MAR-06   2GIH
TITLE     Q138F HINCII BOUND TO COGNATE DNA GTCGAC AND CA2+
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: 5'-D(*GP*CP*CP*GP*GP*TP*CP*GP*AP*CP*CP*GP*GP*C)-
COMPND   3 3';
COMPND   4 CHAIN: E, F;
COMPND   5 ENGINEERED: YES;
COMPND   6 MOL_ID: 2;
COMPND   7 MOLECULE: TYPE II RESTRICTION ENZYME HINCII;
COMPND   8 CHAIN: A, B;
COMPND   9 SYNONYM: ENDONUCLEASE HINCII, R.HINCII;
COMPND  10 EC: 3.1.21.4;
COMPND  11 ENGINEERED: YES;
COMPND  12 MUTATION: YES
SOURCE    MOL_ID: 1;
SOURCE   2 SYNTHETIC: YES;
SOURCE   3 MOL_ID: 2;
SOURCE   4 ORGANISM_SCIENTIFIC: HAEMOPHILUS INFLUENZAE;
SOURCE   5 ORGANISM_TAXID: 727;
SOURCE   6 GENE: HINCIIR;
SOURCE   7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE   9 EXPRESSION_SYSTEM_STRAIN: ER2393;
SOURCE  10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE  11 EXPRESSION_SYSTEM_PLASMID: PCCR101HINCII.R
KEYWDS    PROTEIN DNA COMPLEX, INDIRECT READOUT, DNA INTERCALATION,
KEYWDS   2 ENDONUCLEASE, HYDROLASE/DNA COMPLEX
EXPDTA    X-RAY DIFFRACTION
AUTHOR    N.C.HORTON,H.K.JOSHI,C.ETZKORN,L.CHATWELL,J.BITINAITE
REVDAT   4   24-FEB-09 2GIH    1       VERSN
REVDAT   3   27-MAR-07 2GIH    1       TITLE  COMPND SOURCE DBREF
REVDAT   3 2                   1       SEQADV
REVDAT   2   29-AUG-06 2GIH    1       JRNL
REVDAT   1   18-JUL-06 2GIH    0
JRNL        AUTH   H.K.JOSHI,C.ETZKORN,L.CHATWELL,J.BITINAITE,
JRNL        AUTH 2 N.C.HORTON
JRNL        TITL   ALTERATION OF SEQUENCE SPECIFICITY OF THE TYPE II
JRNL        TITL 2 RESTRICTION ENDONUCLEASE HINCII THROUGH AN
JRNL        TITL 3 INDIRECT READOUT MECHANISM.
JRNL        REF    J.BIOL.CHEM.                  V. 281 23852 2006
JRNL        REFN                   ISSN 0021-9258
JRNL        PMID   16675462
JRNL        DOI    10.1074/JBC.M512339200
REMARK   1
REMARK   2
REMARK   2 RESOLUTION.    2.50 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) : 2.50
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.00
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 2.000
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             : 21318
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 5%
REMARK   3   R VALUE            (WORKING SET) : 0.190
REMARK   3   FREE R VALUE                     : 0.283
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL
REMARK   3   FREE R VALUE TEST SET COUNT      : 1086
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            : 4102
REMARK   3   NUCLEIC ACID ATOMS       : 568
REMARK   3   HETEROGEN ATOMS          : 2
REMARK   3   SOLVENT ATOMS            : 363
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 65.40
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) : 0.007
REMARK   3   BOND ANGLES            (DEGREES) : 1.33
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 2GIH COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-APR-06.
REMARK 100 THE RCSB ID CODE IS RCSB037159.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 20-FEB-05
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 7.5
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : SSRL
REMARK 200  BEAMLINE                       : BL9-2
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9
REMARK 200  MONOCHROMATOR                  : 180 FRAMES, 1 DEGREE
REMARK 200                                   OSCILLATION, 25 SEC PER FRAME
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : BLU-ICE
REMARK 200  DATA SCALING SOFTWARE          : CCP4 (SCALA)
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 28688
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.300
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.9
REMARK 200  DATA REDUNDANCY                : 7.000
REMARK 200  R MERGE                    (I) : 0.08600
REMARK 200  R SYM                      (I) : 0.08600
REMARK 200   FOR THE DATA SET  : 38.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.59
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL
REMARK 200  R MERGE FOR SHELL          (I) : 0.70300
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : 2.800
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 49.13
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.42
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 25% PEG 4K, 0.15 M NACL, 0.1 HEPES,
REMARK 280  PH 7.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 290K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 41
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -Y,X+1/2,Z+1/4
REMARK 290       3555   -X+1/2,-Y+1/2,Z+1/2
REMARK 290       4555   Y+1/2,-X,Z+3/4
REMARK 290       5555   X+1/2,Y+1/2,Z+1/2
REMARK 290       6555   -Y+1/2,X,Z+3/4
REMARK 290       7555   -X,-Y,Z
REMARK 290       8555   Y,-X+1/2,Z+1/4
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  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY2   2  1.000000  0.000000  0.000000       63.93050
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       20.31575
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000       63.93050
REMARK 290   SMTRY2   3  0.000000 -1.000000  0.000000       63.93050
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       40.63150
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       63.93050
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       60.94725
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       63.93050
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       63.93050
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       40.63150
REMARK 290   SMTRY1   6  0.000000 -1.000000  0.000000       63.93050
REMARK 290   SMTRY2   6  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       60.94725
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   7  0.000000 -1.000000  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       63.93050
REMARK 290   SMTRY3   8  0.000000  0.000000  1.000000       20.31575
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 300 REMARK: THE BIOLOGICAL ASSEMBLY IS A PROTEIN DIMER AND SINGLE
REMARK 300 DUPLEX OF DNA. THE ASYMMETRIC UNIT IS THE BIOLOGICAL ASSEMBLY.
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 APPLY THE FOLLOWING TO CHAINS: E, F, 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 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     PRO B    23
REMARK 465     LYS B    24
REMARK 465     SER B    25
REMARK 465     GLY B    26
REMARK 465     THR B    27
REMARK 465     LEU B    28
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     GLN A   9    CG   CD   OE1  NE2
REMARK 470     LYS A  24    CG   CD   CE   NZ
REMARK 470     SER A  50    OG
REMARK 470     ASP A 120    CG   OD1  OD2
REMARK 470     LYS A 135    CG   CD   CE   NZ
REMARK 470     LYS A 228    CG   CD   CE   NZ
REMARK 470     LEU A 258    CG   CD1  CD2
REMARK 470     GLN B   9    CB   CG   CD   OE1  NE2
REMARK 470     ASP B  10    CG   OD1  OD2
REMARK 470     LYS B  21    CG   CD   CE   NZ
REMARK 470     HIS B  31    CG   ND1  CD2  CE1  NE2
REMARK 470     GLU B  35    CG   CD   OE1  OE2
REMARK 470     LYS B  66    CG   CD   CE   NZ
REMARK 470     GLU B  74    CG   CD   OE1  OE2
REMARK 470     LYS B 108    CG   CD   CE   NZ
REMARK 470     LYS B 119    CG   CD   CE   NZ
REMARK 470     GLN B 121    CG   CD   OE1  NE2
REMARK 470     GLU B 178    CG   CD   OE1  OE2
REMARK 470     GLN B 240    CG   CD   OE1  NE2
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   407     O    HOH A   407     7655     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    LYS A  55   N   -  CA  -  C   ANGL. DEV. = -17.3 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    THR A  27     -160.65    -70.67
REMARK 500    LEU A  28        8.37   -160.10
REMARK 500    LEU A  49       40.35   -140.47
REMARK 500    ASN A  67       60.52   -117.65
REMARK 500    SER A  82      124.03   -179.19
REMARK 500    LYS A 135      -85.05    -96.87
REMARK 500    SER A 136      105.71     -8.33
REMARK 500    ASP A 162       24.17   -145.49
REMARK 500    VAL A 212      -42.50     98.43
REMARK 500    VAL A 250      -69.78   -103.23
REMARK 500    GLN B   9      -41.23    107.94
REMARK 500    ASN B  67       58.37   -146.73
REMARK 500    LEU B 104      138.41     59.20
REMARK 500    LYS B 119      110.70   -167.90
REMARK 500    GLN B 121       14.70     58.33
REMARK 500    ASP B 162       31.28   -148.80
REMARK 500    GLU B 178       43.53   -160.06
REMARK 500    SER B 196       -9.58    -56.49
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     DC E   7         0.06    SIDE_CHAIN
REMARK 500     DG E   8         0.05    SIDE_CHAIN
REMARK 500     DA F   9         0.06    SIDE_CHAIN
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 F 340        DISTANCE =  5.33 ANGSTROMS
REMARK 525    HOH B 443        DISTANCE =  6.19 ANGSTROMS
REMARK 525    HOH B 449        DISTANCE =  6.37 ANGSTROMS
REMARK 525    HOH B 451        DISTANCE =  6.64 ANGSTROMS
REMARK 525    HOH A 488        DISTANCE =  8.79 ANGSTROMS
REMARK 525    HOH B 502        DISTANCE =  6.61 ANGSTROMS
REMARK 525    HOH B 521        DISTANCE =  5.63 ANGSTROMS
REMARK 525    HOH B 538        DISTANCE =  5.98 ANGSTROMS
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620  (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620  SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              CA A 402  CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 114   OD2
REMARK 620 2 ASP A 127   OD2  79.6
REMARK 620 3 HOH F 365   O   127.7  75.3
REMARK 620 4 VAL A 128   O   107.1  96.0 120.4
REMARK 620 N                    1     2     3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              CA B 401  CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 127   OD1
REMARK 620 2 VAL B 128   O    81.6
REMARK 620 3 ASP B 114   OD1 117.4 131.8
REMARK 620 4 ASP B 114   OD2  95.2  98.1  40.4
REMARK 620 5  DG E   8   OP1  99.8 160.3  65.1 101.3
REMARK 620 N                    1     2     3     4
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 401
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 402
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2GIG   RELATED DB: PDB
REMARK 900 Q138F HINCII BOUND TO COGNATE DNA GTCGAC
REMARK 900 RELATED ID: 1TX3   RELATED DB: PDB
REMARK 900 WILD TYPE HINCII BOUND TO COGNATE DNA GTCGAC
REMARK 900 RELATED ID: 2GIE   RELATED DB: PDB
REMARK 900 RELATED ID: 2GII   RELATED DB: PDB
REMARK 900 RELATED ID: 2GIJ   RELATED DB: PDB
DBREF  2GIH A    2   258  UNP    P17743   T2C2_HAEIN       2    258
DBREF  2GIH B    2   258  UNP    P17743   T2C2_HAEIN       2    258
DBREF  2GIH E    1    14  PDB    2GIH     2GIH             1     14
DBREF  2GIH F    1    14  PDB    2GIH     2GIH             1     14
SEQADV 2GIH THR A  130  UNP  P17743    ARG   130 CONFLICT
SEQADV 2GIH PHE A  138  UNP  P17743    GLN   138 ENGINEERED
SEQADV 2GIH TRP A  173  UNP  P17743    SER   173 CONFLICT
SEQADV 2GIH THR B  130  UNP  P17743    ARG   130 CONFLICT
SEQADV 2GIH PHE B  138  UNP  P17743    GLN   138 ENGINEERED
SEQADV 2GIH TRP B  173  UNP  P17743    SER   173 CONFLICT
SEQRES   1 E   14   DG  DC  DC  DG  DG  DT  DC  DG  DA  DC  DC  DG  DG
SEQRES   2 E   14   DC
SEQRES   1 F   14   DG  DC  DC  DG  DG  DT  DC  DG  DA  DC  DC  DG  DG
SEQRES   2 F   14   DC
SEQRES   1 A  257  SER PHE ILE LYS PRO ILE TYR GLN ASP ILE ASN SER ILE
SEQRES   2 A  257  LEU ILE GLY GLN LYS VAL LYS ARG PRO LYS SER GLY THR
SEQRES   3 A  257  LEU SER GLY HIS ALA ALA GLY GLU PRO PHE GLU LYS LEU
SEQRES   4 A  257  VAL TYR LYS PHE LEU LYS GLU ASN LEU SER ASP LEU THR
SEQRES   5 A  257  PHE LYS GLN TYR GLU TYR LEU ASN ASP LEU PHE MET LYS
SEQRES   6 A  257  ASN PRO ALA ILE ILE GLY HIS GLU ALA ARG TYR LYS LEU
SEQRES   7 A  257  PHE ASN SER PRO THR LEU LEU PHE LEU LEU SER ARG GLY
SEQRES   8 A  257  LYS ALA ALA THR GLU ASN TRP SER ILE GLU ASN LEU PHE
SEQRES   9 A  257  GLU GLU LYS GLN ASN ASP THR ALA ASP ILE LEU LEU VAL
SEQRES  10 A  257  LYS ASP GLN PHE TYR GLU LEU LEU ASP VAL LYS THR ARG
SEQRES  11 A  257  ASN ILE SER LYS SER ALA PHE ALA PRO ASN ILE ILE SER
SEQRES  12 A  257  ALA TYR LYS LEU ALA GLN THR CYS ALA LYS MET ILE ASP
SEQRES  13 A  257  ASN LYS GLU PHE ASP LEU PHE ASP ILE ASN TYR LEU GLU
SEQRES  14 A  257  VAL ASP TRP GLU LEU ASN GLY GLU ASP LEU VAL CYS VAL
SEQRES  15 A  257  SER THR SER PHE ALA GLU LEU PHE LYS SER GLU PRO SER
SEQRES  16 A  257  GLU LEU TYR ILE ASN TRP ALA ALA ALA MET GLN ILE GLN
SEQRES  17 A  257  PHE HIS VAL ARG ASP LEU ASP GLN GLY PHE ASN GLY THR
SEQRES  18 A  257  ARG GLU GLU TRP ALA LYS SER TYR LEU LYS HIS PHE VAL
SEQRES  19 A  257  THR GLN ALA GLU GLN ARG ALA ILE SER MET ILE ASP LYS
SEQRES  20 A  257  PHE VAL LYS PRO PHE LYS LYS TYR ILE LEU
SEQRES   1 B  257  SER PHE ILE LYS PRO ILE TYR GLN ASP ILE ASN SER ILE
SEQRES   2 B  257  LEU ILE GLY GLN LYS VAL LYS ARG PRO LYS SER GLY THR
SEQRES   3 B  257  LEU SER GLY HIS ALA ALA GLY GLU PRO PHE GLU LYS LEU
SEQRES   4 B  257  VAL TYR LYS PHE LEU LYS GLU ASN LEU SER ASP LEU THR
SEQRES   5 B  257  PHE LYS GLN TYR GLU TYR LEU ASN ASP LEU PHE MET LYS
SEQRES   6 B  257  ASN PRO ALA ILE ILE GLY HIS GLU ALA ARG TYR LYS LEU
SEQRES   7 B  257  PHE ASN SER PRO THR LEU LEU PHE LEU LEU SER ARG GLY
SEQRES   8 B  257  LYS ALA ALA THR GLU ASN TRP SER ILE GLU ASN LEU PHE
SEQRES   9 B  257  GLU GLU LYS GLN ASN ASP THR ALA ASP ILE LEU LEU VAL
SEQRES  10 B  257  LYS ASP GLN PHE TYR GLU LEU LEU ASP VAL LYS THR ARG
SEQRES  11 B  257  ASN ILE SER LYS SER ALA PHE ALA PRO ASN ILE ILE SER
SEQRES  12 B  257  ALA TYR LYS LEU ALA GLN THR CYS ALA LYS MET ILE ASP
SEQRES  13 B  257  ASN LYS GLU PHE ASP LEU PHE ASP ILE ASN TYR LEU GLU
SEQRES  14 B  257  VAL ASP TRP GLU LEU ASN GLY GLU ASP LEU VAL CYS VAL
SEQRES  15 B  257  SER THR SER PHE ALA GLU LEU PHE LYS SER GLU PRO SER
SEQRES  16 B  257  GLU LEU TYR ILE ASN TRP ALA ALA ALA MET GLN ILE GLN
SEQRES  17 B  257  PHE HIS VAL ARG ASP LEU ASP GLN GLY PHE ASN GLY THR
SEQRES  18 B  257  ARG GLU GLU TRP ALA LYS SER TYR LEU LYS HIS PHE VAL
SEQRES  19 B  257  THR GLN ALA GLU GLN ARG ALA ILE SER MET ILE ASP LYS
SEQRES  20 B  257  PHE VAL LYS PRO PHE LYS LYS TYR ILE LEU
HET     CA  B 401       1
HET     CA  A 402       1
HETNAM      CA CALCIUM ION
FORMUL   5   CA    2(CA 2+)
FORMUL   7  HOH   *363(H2 O)
HELIX    1   1 ILE A    4  PRO A    6  5                                   3
HELIX    2   2 ILE A    7  ILE A   14  1                                   8
HELIX    3   3 GLY A   34  LEU A   49  1                                  16
HELIX    4   4 GLN A   56  ASN A   67  1                                  12
HELIX    5   5 GLY A   72  TYR A   77  1                                   6
HELIX    6   6 LYS A   78  ASN A   81  5                                   4
HELIX    7   7 SER A   82  SER A   90  1                                   9
HELIX    8   8 GLY A   92  TRP A   99  1                                   8
HELIX    9   9 ALA A  145  ASN A  158  1                                  14
HELIX   10  10 PHE A  191  SER A  193  5                                   3
HELIX   11  11 GLU A  194  LEU A  198  5                                   5
HELIX   12  12 THR A  222  VAL A  250  1                                  29
HELIX   13  13 PHE A  253  LEU A  258  1                                   6
HELIX   14  14 PHE B    3  TYR B    8  1                                   6
HELIX   15  15 ASP B   10  ILE B   16  1                                   7
HELIX   16  16 GLU B   35  LEU B   49  1                                  15
HELIX   17  17 GLN B   56  LYS B   66  1                                  11
HELIX   18  18 GLY B   72  LEU B   79  1                                   8
HELIX   19  19 SER B   82  SER B   90  1                                   9
HELIX   20  20 GLY B   92  TRP B   99  1                                   8
HELIX   21  21 ALA B  145  LYS B  159  1                                  15
HELIX   22  22 PHE B  191  SER B  193  5                                   3
HELIX   23  23 GLU B  194  LEU B  198  5                                   5
HELIX   24  24 HIS B  211  LEU B  215  5                                   5
HELIX   25  25 THR B  222  VAL B  250  1                                  29
HELIX   26  26 LYS B  251  LYS B  254  5                                   4
SHEET    1   A 6 LYS A  19  LYS A  21  0
SHEET    2   A 6 ASP A 179  GLU A 189 -1  O  LEU A 180   N  VAL A  20
SHEET    3   A 6 PHE A 164  ASN A 176 -1  N  GLU A 174   O  VAL A 181
SHEET    4   A 6 PHE A 122  ASN A 132  1  N  ARG A 131   O  TRP A 173
SHEET    5   A 6 ILE A 115  LYS A 119 -1  N  ILE A 115   O  LEU A 126
SHEET    6   A 6 THR A  53  LYS A  55 -1  N  PHE A  54   O  LEU A 116
SHEET    1   B 3 ASN A 141  SER A 144  0
SHEET    2   B 3 GLN A 207  GLN A 209 -1  O  ILE A 208   N  ILE A 142
SHEET    3   B 3 ILE A 200  ASN A 201 -1  N  ASN A 201   O  GLN A 207
SHEET    1   C 6 LYS B  19  VAL B  20  0
SHEET    2   C 6 LEU B 180  GLU B 189 -1  O  LEU B 180   N  VAL B  20
SHEET    3   C 6 PHE B 164  LEU B 175 -1  N  GLU B 174   O  VAL B 181
SHEET    4   C 6 TYR B 123  ASN B 132  1  N  LYS B 129   O  LEU B 169
SHEET    5   C 6 ILE B 115  VAL B 118 -1  N  ILE B 115   O  LEU B 126
SHEET    6   C 6 THR B  53  LYS B  55 -1  N  PHE B  54   O  LEU B 116
SHEET    1   D 3 ASN B 141  SER B 144  0
SHEET    2   D 3 GLN B 207  GLN B 209 -1  O  ILE B 208   N  ILE B 143
SHEET    3   D 3 ILE B 200  ASN B 201 -1  N  ASN B 201   O  GLN B 207
LINK        CA    CA A 402                 OD2 ASP A 114     1555   1555  2.20
LINK        CA    CA A 402                 OD2 ASP A 127     1555   1555  2.51
LINK        CA    CA A 402                 O   HOH F 365     1555   1555  2.33
LINK        CA    CA A 402                 O   VAL A 128     1555   1555  2.82
LINK        CA    CA B 401                 OD1 ASP B 127     1555   1555  2.62
LINK        CA    CA B 401                 O   VAL B 128     1555   1555  2.53
LINK        CA    CA B 401                 OD1 ASP B 114     1555   1555  3.35
LINK        CA    CA B 401                 OD2 ASP B 114     1555   1555  2.20
LINK        CA    CA B 401                 OP1  DG E   8     1555   1555  2.39
SITE     1 AC1  4 ASP B 114  ASP B 127  VAL B 128   DG E   8
SITE     1 AC2  4 ASP A 114  ASP A 127  VAL A 128  HOH F 365
CRYST1  127.861  127.861   81.263  90.00  90.00  90.00 I 41         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      0.007821  0.000000  0.000000        0.00000
SCALE2      0.000000  0.007821  0.000000        0.00000
SCALE3      0.000000  0.000000  0.012306        0.00000
      
PROCHECK
Go to PROCHECK summary
 References