spacer
spacer

PDBsum entry 2cfm

Go to PDB code: 
Top Page protein ligands metals links
Ligase PDB id
2cfm
Jmol
Contents
Protein chain
561 a.a.
Ligands
AMP
Metals
_MG
Waters ×450
HEADER    LIGASE                                  22-FEB-06   2CFM
TITLE     ATP-DEPENDENT DNA LIGASE FROM PYROCOCCUS FURIOSUS
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: THERMOSTABLE DNA LIGASE;
COMPND   3 CHAIN: A;
COMPND   4 SYNONYM: POLYDEOXYRIBONUCLEOTIDE SYNTHASE [ATP], PFU DNA
COMPND   5  LIGASE;
COMPND   6 EC: 6.5.1.1;
COMPND   7 ENGINEERED: YES;
COMPND   8 OTHER_DETAILS: AMP IS BOUND IN THE POCKET NON-COVALENTLY
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: PYROCOCCUS FURIOSUS;
SOURCE   3 ORGANISM_TAXID: 2261;
SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE   6 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE   7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PET21D
KEYWDS    LIGASE, PROTEIN-NUCLEOTIDE COMPLEX, CELL CYCLE, CELL
KEYWDS   2 DIVISION, DNA DAMAGE, DNA RECOMBINATION, DNA REPAIR, DNA
KEYWDS   3 REPLICATION, NUCLEOTIDE-BINDING
EXPDTA    X-RAY DIFFRACTION
AUTHOR    H.NISHIDA,Y.ISHINO,K.MORIKAWA
REVDAT   3   24-FEB-09 2CFM    1       VERSN
REVDAT   2   26-JUL-06 2CFM    1       JRNL
REVDAT   1   12-JUL-06 2CFM    0
JRNL        AUTH   H.NISHIDA,S.KIYONARI,Y.ISHINO,K.MORIKAWA
JRNL        TITL   THE CLOSED STRUCTURE OF AN ARCHAEAL DNA LIGASE
JRNL        TITL 2 FROM PYROCOCCUS FURIOSUS.
JRNL        REF    J.MOL.BIOL.                   V. 360   956 2006
JRNL        REFN                   ISSN 0022-2836
JRNL        PMID   16820169
JRNL        DOI    10.1016/J.JMB.2006.05.062
REMARK   2
REMARK   2 RESOLUTION.    1.8  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 : MAXIMUM LIKELIHOOD
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.00
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 1.000
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 99.4
REMARK   3   NUMBER OF REFLECTIONS             : 56943
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 SET) : 0.204
REMARK   3   FREE R VALUE                     : 0.231
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 7.00
REMARK   3   FREE R VALUE TEST SET COUNT      : 4051
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) : 1.80
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.88
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 98.50
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  (%) : 7.00
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            : 4295
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 152
REMARK   3   SOLVENT ATOMS            : 450
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) : 0.008
REMARK   3   BOND ANGLES            (DEGREES) : 1.39
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL MODEL : ISOTROPIC
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  PARAMETER FILE  2  : NULL
REMARK   3  TOPOLOGY FILE  1   : NULL
REMARK   3  TOPOLOGY FILE  2   : NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 2CFM COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 22-FEB-06.
REMARK 100 THE PDBE ID CODE IS EBI-27880.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 21-JUN-04
REMARK 200  TEMPERATURE           (KELVIN) : 100.0
REMARK 200  PH                             : 8.00
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : PHOTON FACTORY
REMARK 200  BEAMLINE                       : BL6B
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9797, 0.9791, 0.9787, 0.9587
REMARK 200  MONOCHROMATOR                  : SI 111 CHANNEL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE (RAXIS-IV)
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 56984
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.800
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.4
REMARK 200  DATA REDUNDANCY                : 3.400
REMARK 200  R MERGE                    (I) : 0.07000
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 11.7000
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) : 1.88
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.5
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.30
REMARK 200  R MERGE FOR SHELL          (I) : 0.32000
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: MAD
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD
REMARK 200 SOFTWARE USED: SHARP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 51.2
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.5
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: ETHANOL, PH 8, VAPOR DIFFUSION,
REMARK 280  HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,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       43.69950
REMARK 290   SMTRY3   2  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 GENERATING THE BIOMOLECULE
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: PQS
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 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     ARG A   2    CB   CG   CD   NE   CZ   NH1  NH2
REMARK 470     LYS A  99    CG   CD   CE   NZ
REMARK 470     GLN A 103    CG   CD   OE1  NE2
REMARK 470     LYS A 104    CG   CD   CE   NZ
REMARK 470     THR A 127    OG1  CG2
REMARK 470     GLU A 129    CG   CD   OE1  OE2
REMARK 470     LYS A 134    CG   CD   CE   NZ
REMARK 470     ARG A 276    CG   CD   NE   CZ   NH1  NH2
REMARK 470     LYS A 322    CG   CD   CE   NZ
REMARK 470     GLU A 327    CG   CD   OE1  OE2
REMARK 470     GLU A 330    CG   CD   OE1  OE2
REMARK 470     PRO A 514    CG   CD
REMARK 470     LYS A 515    CG   CD   CE   NZ
REMARK 470     TYR A 516    CG   CD1  CD2  CE1  CE2  CZ   OH
REMARK 470     ARG A 517    CG   CD   NE   CZ   NH1  NH2
REMARK 470     SER A 561    OG
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    GLN A 109   N   -  CA  -  C   ANGL. DEV. = -16.9 DEGREES
REMARK 500    ARG A 358   NE  -  CZ  -  NH1 ANGL. DEV. =   3.8 DEGREES
REMARK 500    ARG A 358   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.8 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 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    GLU A  55      -37.14     88.21
REMARK 500    LYS A 515      -74.10    -44.23
REMARK 500    ARG A 531       64.03   -115.21
REMARK 500    GLU A 560     -155.60     77.92
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    TYR A  43         0.08    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 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                              MG A1562  MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A2218   O
REMARK 620 2 HOH A2253   O    93.8
REMARK 620 3 HOH A2329   O    95.4 170.7
REMARK 620 4 HOH A2330   O    91.7  88.0  90.2
REMARK 620 5 HOH A2419   O    86.4  87.4  94.7 174.9
REMARK 620 6 HOH A2450   O   172.6  78.8  91.9  87.4  93.9
REMARK 620 N                    1     2     3     4     5
REMARK 700
REMARK 700 SHEET
REMARK 700 THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN
REMARK 700 ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW,
REMARK 700 TWO SHEETS ARE DEFINED.
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  MG A1562
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AMP A1563
DBREF  2CFM A    1   561  UNP    P56709   DNLI_PYRFU       1    561
SEQRES   1 A  561  MSE ARG TYR LEU GLU LEU ALA GLN LEU TYR GLN LYS LEU
SEQRES   2 A  561  GLU LYS THR THR MSE LYS LEU ILE LYS THR ARG LEU VAL
SEQRES   3 A  561  ALA ASP PHE LEU LYS LYS VAL PRO ASP ASP HIS LEU GLU
SEQRES   4 A  561  PHE ILE PRO TYR LEU ILE LEU GLY GLU VAL PHE PRO GLU
SEQRES   5 A  561  TRP ASP GLU ARG GLU LEU GLY VAL GLY GLU LYS LEU LEU
SEQRES   6 A  561  ILE LYS ALA VAL ALA MSE ALA THR GLY ILE ASP ALA LYS
SEQRES   7 A  561  GLU ILE GLU GLU SER VAL LYS ASP THR GLY ASP LEU GLY
SEQRES   8 A  561  GLU SER ILE ALA LEU ALA VAL LYS LYS LYS LYS GLN LYS
SEQRES   9 A  561  SER PHE PHE SER GLN PRO LEU THR ILE LYS ARG VAL TYR
SEQRES  10 A  561  GLN THR LEU VAL LYS VAL ALA GLU THR THR GLY GLU GLY
SEQRES  11 A  561  SER GLN ASP LYS LYS VAL LYS TYR LEU ALA ASP LEU PHE
SEQRES  12 A  561  MSE ASP ALA GLU PRO LEU GLU ALA LYS TYR LEU ALA ARG
SEQRES  13 A  561  THR ILE LEU GLY THR MSE ARG THR GLY VAL ALA GLU GLY
SEQRES  14 A  561  LEU LEU ARG ASP ALA ILE ALA MSE ALA PHE HIS VAL LYS
SEQRES  15 A  561  VAL GLU LEU VAL GLU ARG ALA TYR MSE LEU THR SER ASP
SEQRES  16 A  561  PHE GLY TYR VAL ALA LYS ILE ALA LYS LEU GLU GLY ASN
SEQRES  17 A  561  GLU GLY LEU ALA LYS VAL GLN VAL GLN LEU GLY LYS PRO
SEQRES  18 A  561  ILE LYS PRO MSE LEU ALA GLN GLN ALA ALA SER ILE ARG
SEQRES  19 A  561  ASP ALA LEU LEU GLU MSE GLY GLY GLU ALA GLU PHE GLU
SEQRES  20 A  561  ILE LYS TYR ASP GLY ALA ARG VAL GLN VAL HIS LYS ASP
SEQRES  21 A  561  GLY SER LYS ILE ILE VAL TYR SER ARG ARG LEU GLU ASN
SEQRES  22 A  561  VAL THR ARG ALA ILE PRO GLU ILE VAL GLU ALA LEU LYS
SEQRES  23 A  561  GLU ALA ILE ILE PRO GLU LYS ALA ILE VAL GLU GLY GLU
SEQRES  24 A  561  LEU VAL ALA ILE GLY GLU ASN GLY ARG PRO LEU PRO PHE
SEQRES  25 A  561  GLN TYR VAL LEU ARG ARG PHE ARG ARG LYS HIS ASN ILE
SEQRES  26 A  561  GLU GLU MSE MSE GLU LYS ILE PRO LEU GLU LEU ASN LEU
SEQRES  27 A  561  PHE ASP VAL LEU TYR VAL ASP GLY GLN SER LEU ILE ASP
SEQRES  28 A  561  THR LYS PHE ILE ASP ARG ARG ARG THR LEU GLU GLU ILE
SEQRES  29 A  561  ILE LYS GLN ASN GLU LYS ILE LYS VAL ALA GLU ASN LEU
SEQRES  30 A  561  ILE THR LYS LYS VAL GLU GLU ALA GLU ALA PHE TYR LYS
SEQRES  31 A  561  ARG ALA LEU GLU MSE GLY HIS GLU GLY LEU MSE ALA LYS
SEQRES  32 A  561  ARG LEU ASP ALA VAL TYR GLU PRO GLY ASN ARG GLY LYS
SEQRES  33 A  561  LYS TRP LEU LYS ILE LYS PRO THR MSE GLU ASN LEU ASP
SEQRES  34 A  561  LEU VAL ILE ILE GLY ALA GLU TRP GLY GLU GLY ARG ARG
SEQRES  35 A  561  ALA HIS LEU PHE GLY SER PHE ILE LEU GLY ALA TYR ASP
SEQRES  36 A  561  PRO GLU THR GLY GLU PHE LEU GLU VAL GLY LYS VAL GLY
SEQRES  37 A  561  SER GLY PHE THR ASP ASP ASP LEU VAL GLU PHE THR LYS
SEQRES  38 A  561  MSE LEU LYS PRO LEU ILE ILE LYS GLU GLU GLY LYS ARG
SEQRES  39 A  561  VAL TRP LEU GLN PRO LYS VAL VAL ILE GLU VAL THR TYR
SEQRES  40 A  561  GLN GLU ILE GLN LYS SER PRO LYS TYR ARG SER GLY PHE
SEQRES  41 A  561  ALA LEU ARG PHE PRO ARG PHE VAL ALA LEU ARG ASP ASP
SEQRES  42 A  561  LYS GLY PRO GLU ASP ALA ASP THR ILE GLU ARG ILE ALA
SEQRES  43 A  561  GLN LEU TYR GLU LEU GLN GLU LYS MSE LYS GLY LYS VAL
SEQRES  44 A  561  GLU SER
MODRES 2CFM MSE A    1  MET  SELENOMETHIONINE
MODRES 2CFM MSE A   18  MET  SELENOMETHIONINE
MODRES 2CFM MSE A   71  MET  SELENOMETHIONINE
MODRES 2CFM MSE A  144  MET  SELENOMETHIONINE
MODRES 2CFM MSE A  162  MET  SELENOMETHIONINE
MODRES 2CFM MSE A  177  MET  SELENOMETHIONINE
MODRES 2CFM MSE A  191  MET  SELENOMETHIONINE
MODRES 2CFM MSE A  225  MET  SELENOMETHIONINE
MODRES 2CFM MSE A  240  MET  SELENOMETHIONINE
MODRES 2CFM MSE A  328  MET  SELENOMETHIONINE
MODRES 2CFM MSE A  329  MET  SELENOMETHIONINE
MODRES 2CFM MSE A  395  MET  SELENOMETHIONINE
MODRES 2CFM MSE A  401  MET  SELENOMETHIONINE
MODRES 2CFM MSE A  425  MET  SELENOMETHIONINE
MODRES 2CFM MSE A  482  MET  SELENOMETHIONINE
MODRES 2CFM MSE A  555  MET  SELENOMETHIONINE
HET    MSE  A   1       8
HET    MSE  A  18       8
HET    MSE  A  71       8
HET    MSE  A 144       8
HET    MSE  A 162       8
HET    MSE  A 177       8
HET    MSE  A 191       8
HET    MSE  A 225       8
HET    MSE  A 240       8
HET    MSE  A 328       8
HET    MSE  A 329       8
HET    MSE  A 395       8
HET    MSE  A 401       8
HET    MSE  A 425       8
HET    MSE  A 482       8
HET    MSE  A 555       8
HET     MG  A1562       1
HET    AMP  A1563      23
HETNAM     MSE SELENOMETHIONINE
HETNAM      MG MAGNESIUM ION
HETNAM     AMP ADENOSINE MONOPHOSPHATE
FORMUL   1  MSE    16(C5 H11 N O2 SE)
FORMUL   2   MG    MG 2+
FORMUL   3  AMP    C10 H14 N5 O7 P
FORMUL   4  HOH   *450(H2 O1)
HELIX    1   1 ARG A    2  LYS A   15  1                                  14
HELIX    2   2 MSE A   18  VAL A   33  1                                  16
HELIX    3   3 PRO A   34  LEU A   38  5                                   5
HELIX    4   4 PHE A   40  LEU A   46  1                                   7
HELIX    5   5 GLY A   61  GLY A   74  1                                  14
HELIX    6   6 ASP A   76  GLY A   88  1                                  13
HELIX    7   7 ASP A   89  LYS A  102  1                                  14
HELIX    8   8 THR A  112  THR A  126  1                                  15
HELIX    9   9 GLY A  130  MSE A  144  1                                  15
HELIX   10  10 GLU A  147  GLY A  160  1                                  14
HELIX   11  11 ALA A  167  PHE A  179  1                                  13
HELIX   12  12 LYS A  182  SER A  194  1                                  13
HELIX   13  13 ASP A  195  VAL A  214  1                                  20
HELIX   14  14 SER A  232  MSE A  240  1                                   9
HELIX   15  15 VAL A  274  ALA A  277  5                                   4
HELIX   16  16 ILE A  278  ILE A  289  1                                  12
HELIX   17  17 PHE A  312  ARG A  321  1                                  10
HELIX   18  18 ASN A  324  ILE A  332  1                                   9
HELIX   19  19 LYS A  353  ILE A  365  1                                  13
HELIX   20  20 LYS A  381  MSE A  395  1                                  15
HELIX   21  21 GLU A  439  ALA A  443  5                                   5
HELIX   22  22 THR A  472  LYS A  484  1                                  13
HELIX   23  23 GLY A  535  ALA A  539  5                                   5
HELIX   24  24 THR A  541  LYS A  558  1                                  18
SHEET    1  AA 5 LEU A 226  ALA A 230  0
SHEET    2  AA 5 ARG A 414  ILE A 421  1  O  GLY A 415   N  GLN A 228
SHEET    3  AA 5 GLY A 399  LYS A 403 -1  O  LEU A 400   N  ILE A 421
SHEET    4  AA 5 ALA A 244  LYS A 249 -1  O  GLU A 245   N  LYS A 403
SHEET    5  AA 5 ASN A 376  THR A 379 -1  O  LEU A 377   N  PHE A 246
SHEET    1  AB 5 LYS A 263  TYR A 267  0
SHEET    2  AB 5 ALA A 253  ASP A 260 -1  O  GLN A 256   N  TYR A 267
SHEET    3  AB 5 LYS A 293  ALA A 302 -1  O  ALA A 294   N  LYS A 259
SHEET    4  AB 5 LEU A 334  VAL A 344 -1  O  GLU A 335   N  VAL A 301
SHEET    5  AB 5 ILE A 371  VAL A 373  1  O  LYS A 372   N  LEU A 338
SHEET    1  AC 5 LYS A 263  TYR A 267  0
SHEET    2  AC 5 ALA A 253  ASP A 260 -1  O  GLN A 256   N  TYR A 267
SHEET    3  AC 5 LYS A 293  ALA A 302 -1  O  ALA A 294   N  LYS A 259
SHEET    4  AC 5 LEU A 334  VAL A 344 -1  O  GLU A 335   N  VAL A 301
SHEET    5  AC 5 GLN A 347  SER A 348 -1  O  GLN A 347   N  VAL A 344
SHEET    1  AD 5 PHE A 461  VAL A 467  0
SHEET    2  AD 5 PHE A 446  TYR A 454 -1  O  PHE A 449   N  VAL A 467
SHEET    3  AD 5 LEU A 428  TRP A 437 -1  O  VAL A 431   N  GLY A 452
SHEET    4  AD 5 VAL A 502  THR A 506 -1  O  ILE A 503   N  LEU A 430
SHEET    5  AD 5 ARG A 526  LEU A 530 -1  O  ARG A 526   N  THR A 506
SHEET    1  AE 5 PHE A 461  VAL A 467  0
SHEET    2  AE 5 PHE A 446  TYR A 454 -1  O  PHE A 449   N  VAL A 467
SHEET    3  AE 5 LEU A 428  TRP A 437 -1  O  VAL A 431   N  GLY A 452
SHEET    4  AE 5 ARG A 494  LEU A 497 -1  O  VAL A 495   N  ALA A 435
SHEET    5  AE 5 ILE A 487  GLU A 491 -1  N  ILE A 488   O  TRP A 496
SHEET    1  AF 2 GLU A 509  GLN A 511  0
SHEET    2  AF 2 ALA A 521  ARG A 523 -1  O  ALA A 521   N  GLN A 511
LINK         C   MSE A   1                 N   ARG A   2     1555   1555  1.33
LINK         C   THR A  17                 N   MSE A  18     1555   1555  1.33
LINK         C   MSE A  18                 N   LYS A  19     1555   1555  1.32
LINK         C   ALA A  70                 N   MSE A  71     1555   1555  1.33
LINK         C   MSE A  71                 N   ALA A  72     1555   1555  1.32
LINK         C   PHE A 143                 N   MSE A 144     1555   1555  1.33
LINK         C   MSE A 144                 N   ASP A 145     1555   1555  1.33
LINK         C   THR A 161                 N   MSE A 162     1555   1555  1.33
LINK         C   MSE A 162                 N   ARG A 163     1555   1555  1.33
LINK         C   ALA A 176                 N   MSE A 177     1555   1555  1.33
LINK         C   MSE A 177                 N   ALA A 178     1555   1555  1.32
LINK         C   TYR A 190                 N   MSE A 191     1555   1555  1.33
LINK         C   MSE A 191                 N   LEU A 192     1555   1555  1.32
LINK         C   PRO A 224                 N   MSE A 225     1555   1555  1.33
LINK         C   MSE A 225                 N   LEU A 226     1555   1555  1.33
LINK         C   GLU A 239                 N   MSE A 240     1555   1555  1.32
LINK         C   MSE A 240                 N   GLY A 241     1555   1555  1.33
LINK         C   GLU A 327                 N   MSE A 328     1555   1555  1.33
LINK         C   MSE A 328                 N   MSE A 329     1555   1555  1.33
LINK         C   MSE A 329                 N   GLU A 330     1555   1555  1.33
LINK         C   GLU A 394                 N   MSE A 395     1555   1555  1.33
LINK         C   MSE A 395                 N   GLY A 396     1555   1555  1.33
LINK         C   LEU A 400                 N   MSE A 401     1555   1555  1.33
LINK         C   MSE A 401                 N   ALA A 402     1555   1555  1.32
LINK         C   THR A 424                 N   MSE A 425     1555   1555  1.33
LINK         C   MSE A 425                 N   GLU A 426     1555   1555  1.32
LINK         C   LYS A 481                 N   MSE A 482     1555   1555  1.32
LINK         C   MSE A 482                 N   LEU A 483     1555   1555  1.33
LINK         C   LYS A 554                 N   MSE A 555     1555   1555  1.33
LINK         C   MSE A 555                 N   LYS A 556     1555   1555  1.33
LINK        MG    MG A1562                 O   HOH A2253     1555   1555  2.19
LINK        MG    MG A1562                 O   HOH A2329     1555   1555  2.13
LINK        MG    MG A1562                 O   HOH A2330     1555   1555  2.23
LINK        MG    MG A1562                 O   HOH A2419     1555   1555  2.39
LINK        MG    MG A1562                 O   HOH A2450     1555   1555  2.21
LINK        MG    MG A1562                 O   HOH A2218     1555   1555  2.08
SITE     1 AC1  7 GLU A 299  HOH A2218  HOH A2253  HOH A2329
SITE     2 AC1  7 HOH A2330  HOH A2419  HOH A2450
SITE     1 AC2 20 LEU A 226  ALA A 227  GLU A 247  ILE A 248
SITE     2 AC2 20 LYS A 249  TYR A 250  ARG A 254  ARG A 269
SITE     3 AC2 20 GLU A 299  PHE A 339  MSE A 401  LYS A 403
SITE     4 AC2 20 LYS A 420  HOH A2233  HOH A2253  HOH A2356
SITE     5 AC2 20 HOH A2447  HOH A2448  HOH A2449  HOH A2450
CRYST1   60.866   87.399   62.648  90.00 109.22  90.00 P 1 21 1      2
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      0.016430  0.000000  0.005728        0.00000
SCALE2      0.000000  0.011442  0.000000        0.00000
SCALE3      0.000000  0.000000  0.016904        0.00000
      
PROCHECK
Go to PROCHECK summary
 References