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PDBsum entry 3cmu

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Top Page protein dna_rna ligands metals links
Recombination/DNA PDB id
3cmu
Jmol
Contents
Protein chain
1937 a.a.
DNA/RNA
Ligands
ALF ×6
ADP ×6
Metals
_MG ×6
HEADER    RECOMBINATION/DNA                       24-MAR-08   3CMU
TITLE     MECHANISM OF HOMOLOGOUS RECOMBINATION FROM THE RECA-
TITLE    2 SSDNA/DSDNA STRUCTURES
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: DNA (5'-
COMPND   3 D(*DTP*DTP*DTP*DTP*DTP*DTP*DTP*DTP*DTP*DTP*DTP*DTP*DTP*DTP*
COMPND   4 DTP*DTP*DTP*DT)-3');
COMPND   5 CHAIN: B;
COMPND   6 ENGINEERED: YES;
COMPND   7 MOL_ID: 2;
COMPND   8 MOLECULE: PROTEIN RECA;
COMPND   9 CHAIN: A;
COMPND  10 SYNONYM: RECOMBINASE A;
COMPND  11 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 SYNTHETIC: YES;
SOURCE   3 MOL_ID: 2;
SOURCE   4 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI
KEYWDS    HOMOLOGOUS RECOMBINATION, RECOMBINATION/DNA COMPLEX
EXPDTA    X-RAY DIFFRACTION
AUTHOR    N.P.PAVLETICH
REVDAT   3   24-FEB-09 3CMU    1       VERSN
REVDAT   2   01-JUL-08 3CMU    1       JRNL
REVDAT   1   20-MAY-08 3CMU    0
JRNL        AUTH   Z.CHEN,H.YANG,N.P.PAVLETICH
JRNL        TITL   MECHANISM OF HOMOLOGOUS RECOMBINATION FROM THE
JRNL        TITL 2 RECA-SSDNA/DSDNA STRUCTURES.
JRNL        REF    NATURE                        V. 453   489 2008
JRNL        REFN                   ISSN 0028-0836
JRNL        PMID   18497818
JRNL        DOI    10.1038/NATURE06971
REMARK   1
REMARK   2
REMARK   2 RESOLUTION.    4.20 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
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 4.20
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 12.00
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
REMARK   3   COMPLETENESS FOR RANGE        (%) : 80.7
REMARK   3   NUMBER OF REFLECTIONS             : 16125
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) : 0.276
REMARK   3   R VALUE            (WORKING SET) : 0.275
REMARK   3   FREE R VALUE                     : 0.298
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.300
REMARK   3   FREE R VALUE TEST SET COUNT      : 905
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) : 4.20
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 4.30
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 775
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 57.71
REMARK   3   BIN R VALUE           (WORKING SET) : 0.5030
REMARK   3   BIN FREE R VALUE SET COUNT          : 45
REMARK   3   BIN FREE R VALUE                    : 0.4980
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 14598
REMARK   3   NUCLEIC ACID ATOMS       : 297
REMARK   3   HETEROGEN ATOMS          : 198
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) : 194.78
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 15.22000
REMARK   3    B22 (A**2) : 15.22000
REMARK   3    B33 (A**2) : -22.82000
REMARK   3    B12 (A**2) : 7.61000
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): NULL
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 1.328
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 1.083
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 197.085
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.937
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.922
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 15346 ; 0.012 ; 0.022
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 20726 ; 1.441 ; 2.022
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1934 ; 5.831 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   599 ;35.914 ;25.409
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  2784 ;19.574 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    82 ;15.676 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  2378 ; 0.158 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 11046 ; 0.004 ; 0.020
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  7837 ; 0.245 ; 0.200
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A): 10209 ; 0.312 ; 0.200
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   692 ; 0.155 ; 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):   100 ; 0.426 ; 0.200
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     5 ; 0.372 ; 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):  9866 ; 1.089 ; 1.200
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 15234 ; 1.960 ; 1.800
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  6280 ; 1.577 ; 1.800
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  5492 ; 2.773 ; 3.000
REMARK   3
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL
REMARK   3
REMARK   3  NCS RESTRAINTS STATISTICS
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK   3
REMARK   3  TLS DETAILS
REMARK   3   NUMBER OF TLS GROUPS  : NULL
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED : BABINET MODEL WITH 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: NULL
REMARK   4
REMARK   4 3CMU COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 28-APR-08.
REMARK 100 THE RCSB ID CODE IS RCSB046965.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 01-OCT-06
REMARK 200  TEMPERATURE           (KELVIN) : NULL
REMARK 200  PH                             : 7.5
REMARK 200  NUMBER OF CRYSTALS USED        : NULL
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : APS
REMARK 200  BEAMLINE                       : 24-ID-C
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : NULL
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : NULL
REMARK 200  DETECTOR MANUFACTURER          : NULL
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200  DATA SCALING SOFTWARE          : NULL
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 16125
REMARK 200  RESOLUTION RANGE HIGH      (A) : 4.200
REMARK 200  RESOLUTION RANGE LOW       (A) : 40.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : NULL
REMARK 200  DATA REDUNDANCY                : NULL
REMARK 200  R MERGE                    (I) : NULL
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL
REMARK 200  R MERGE FOR SHELL          (I) : NULL
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 62.76
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.30
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: RECA6 FUSION PROTEIN WAS INCUBATED
REMARK 280  WITH A 3-FOLD MOLAR EXCESS OF SSDNA (DT)18 IN THE ORIGINAL
REMARK 280  PROTEIN BUFFER SUPPLEMENTED WITH 2 MM ADP, 10 MM MGCL2 AND 8
REMARK 280  MM ALF4, PH 6.0. CRYSTALS OF THE RECA6-(ADP-ALF4-MG)6-(DT)18
REMARK 280  COMPLEX WERE GROWN FROM 50 MM HEPES-NA+, 1.5% (W/V)
REMARK 280  POLYETHYLENE GLYCOL (PEG) 3350, 4% (W/V) POLYVINYLPYRROLIDONE
REMARK 280  K15 (PVP K15), 25% (V/V) 2-METHYL-2,4-PENTANDIOL (MPD), 10 MM
REMARK 280  DTT, PH 7.5.
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -Y,X-Y,Z+2/3
REMARK 290       3555   -X+Y,-X,Z+1/3
REMARK 290       4555   Y,X,-Z
REMARK 290       5555   X-Y,-Y,-Z+1/3
REMARK 290       6555   -X,-X+Y,-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      140.66667
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       70.33333
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       70.33333
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      140.66667
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 12480 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 72830 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -158.5 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, A
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465   M RES C SSSEQI
REMARK 465      DT B   999
REMARK 465      DT B  1000
REMARK 465      DT B  1001
REMARK 465     GLY A    26
REMARK 465     ALA A    27
REMARK 465     HIS A    28
REMARK 465     MET A    29
REMARK 465     GLY A    30
REMARK 465     GLU A    31
REMARK 465     ASP A    32
REMARK 465     ARG A    33
REMARK 465     SER A    34
REMARK 465     MET A    35
REMARK 465     ASP A    36
REMARK 465     SER A   329
REMARK 465     ASN A   330
REMARK 465     PRO A   331
REMARK 465     ASN A   332
REMARK 465     SER A   333
REMARK 465     THR A   334
REMARK 465     THR A   986
REMARK 465     GLY A   987
REMARK 465     SER A   988
REMARK 465     THR A   989
REMARK 465     GLY A   990
REMARK 465     SER A   991
REMARK 465     GLY A   992
REMARK 465     THR A   993
REMARK 465     THR A   994
REMARK 465     GLY A   995
REMARK 465     SER A   996
REMARK 465     THR A   997
REMARK 465     GLY A   998
REMARK 465     SER A   999
REMARK 465     MET A  1000
REMARK 465     THR A  1334
REMARK 465     THR A  1986
REMARK 465     GLY A  1987
REMARK 465     SER A  1988
REMARK 465     THR A  1989
REMARK 465     GLY A  1990
REMARK 465     SER A  1991
REMARK 465     MET A  1992
REMARK 465     GLY A  1993
REMARK 465     HIS A  1994
REMARK 465     THR A  1995
REMARK 465     THR A  1996
REMARK 465     GLY A  1997
REMARK 465     ALA A  1998
REMARK 465     MET A  1999
REMARK 465     SER A  2000
REMARK 465     THR A  2334
REMARK 465     THR A  2986
REMARK 465     GLY A  2987
REMARK 465     SER A  2988
REMARK 465     THR A  2989
REMARK 465     GLY A  2990
REMARK 465     SER A  2991
REMARK 465     MET A  2992
REMARK 465     ALA A  2993
REMARK 465     SER A  2994
REMARK 465     THR A  2995
REMARK 465     GLY A  2996
REMARK 465     SER A  2997
REMARK 465     THR A  2998
REMARK 465     GLY A  2999
REMARK 465     SER A  3000
REMARK 465     THR A  3334
REMARK 465     THR A  3989
REMARK 465     GLY A  3990
REMARK 465     ALA A  3991
REMARK 465     THR A  3992
REMARK 465     GLY A  3993
REMARK 465     ALA A  3994
REMARK 465     MET A  3995
REMARK 465     SER A  3996
REMARK 465     GLY A  3997
REMARK 465     ARG A  3998
REMARK 465     MET A  3999
REMARK 465     SER A  4000
REMARK 465     THR A  4334
REMARK 465     THR A  4987
REMARK 465     GLY A  4988
REMARK 465     SER A  4989
REMARK 465     THR A  4990
REMARK 465     GLY A  4991
REMARK 465     SER A  4992
REMARK 465     GLY A  4993
REMARK 465     SER A  4994
REMARK 465     SER A  4995
REMARK 465     THR A  4996
REMARK 465     GLY A  4997
REMARK 465     SER A  4998
REMARK 465     MET A  4999
REMARK 465     SER A  5000
REMARK 465     GLY A  5157
REMARK 465     GLU A  5158
REMARK 465     ILE A  5159
REMARK 465     GLY A  5160
REMARK 465     ASP A  5161
REMARK 465     SER A  5162
REMARK 465     HIS A  5163
REMARK 465     MET A  5197
REMARK 465     LYS A  5198
REMARK 465     ILE A  5199
REMARK 465     GLY A  5200
REMARK 465     VAL A  5201
REMARK 465     MET A  5202
REMARK 465     PHE A  5203
REMARK 465     GLY A  5204
REMARK 465     SER A  5329
REMARK 465     ASN A  5330
REMARK 465     PRO A  5331
REMARK 465     ASN A  5332
REMARK 465     SER A  5333
REMARK 465     THR A  5334
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      DT B1002    P    OP1  OP2
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  AL    ALF A  1501     O3B  ADP A  1502              1.85
REMARK 500  AL    ALF A  3501     O3B  ADP A  3502              1.87
REMARK 500  AL    ALF A  2501     O3B  ADP A  2502              1.87
REMARK 500  AL    ALF A  4501     O3B  ADP A  4502              1.87
REMARK 500   F2   ALF A  1501     O1B  ADP A  1502              1.88
REMARK 500  AL    ALF A   501     O3B  ADP A   502              1.89
REMARK 500   F3   ALF A   501     O3B  ADP A   502              1.90
REMARK 500   F3   ALF A  2501     O3B  ADP A  2502              1.91
REMARK 500   F2   ALF A  2501     O1B  ADP A  2502              1.95
REMARK 500   F2   ALF A  4501     O1B  ADP A  4502              1.96
REMARK 500   F2   ALF A  3501     O1B  ADP A  3502              1.98
REMARK 500   OE2  GLU A    96     F4   ALF A   501              1.99
REMARK 500   F3   ALF A  1501     O3B  ADP A  1502              2.01
REMARK 500   F3   ALF A  3501     O3B  ADP A  3502              2.01
REMARK 500   F2   ALF A   501     O1B  ADP A   502              2.02
REMARK 500   F3   ALF A  4501     O3B  ADP A  4502              2.05
REMARK 500  AL    ALF A  5501     O3B  ADP A  5502              2.08
REMARK 500   F3   ALF A  5501     O3B  ADP A  5502              2.14
REMARK 500   NZ   LYS A  1248     F1   ALF A   501              2.17
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   OD2  ASP A  1276     OE2  GLU A  5235     4556     2.08
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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   RES CSSEQI ATM2   DEVIATION
REMARK 500     DT B1002   C1'    DT B1002   N1      0.082
REMARK 500     DT B1002   N3     DT B1002   C4      0.053
REMARK 500     DT B1007   O3'    DT B1007   C3'    -0.043
REMARK 500     DT B1010   O3'    DT B1010   C3'    -0.037
REMARK 500     DT B1012   O3'    DT B1012   C3'    -0.047
REMARK 500     DT B1012   O3'    DT B1013   P      -0.073
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     DT B1002   N1  -  C1' -  C2' ANGL. DEV. =   9.5 DEGREES
REMARK 500     DT B1002   C5  -  C6  -  N1  ANGL. DEV. =   3.7 DEGREES
REMARK 500     DT B1002   N3  -  C4  -  O4  ANGL. DEV. =   5.4 DEGREES
REMARK 500     DT B1002   C5  -  C4  -  O4  ANGL. DEV. =  -4.9 DEGREES
REMARK 500     DT B1003   O4' -  C1' -  N1  ANGL. DEV. =   3.7 DEGREES
REMARK 500     DT B1003   N3  -  C4  -  O4  ANGL. DEV. =   4.4 DEGREES
REMARK 500     DT B1003   C5  -  C4  -  O4  ANGL. DEV. =  -4.8 DEGREES
REMARK 500     DT B1004   O5' -  C5' -  C4' ANGL. DEV. =  -5.0 DEGREES
REMARK 500     DT B1003   C3' -  O3' -  P   ANGL. DEV. =   9.1 DEGREES
REMARK 500     DT B1005   C4' -  C3' -  C2' ANGL. DEV. =  -4.4 DEGREES
REMARK 500     DT B1005   O4' -  C1' -  N1  ANGL. DEV. =   6.4 DEGREES
REMARK 500     DT B1006   O4' -  C1' -  N1  ANGL. DEV. =   3.2 DEGREES
REMARK 500     DT B1006   N3  -  C4  -  O4  ANGL. DEV. =   3.8 DEGREES
REMARK 500     DT B1006   C5  -  C4  -  O4  ANGL. DEV. =  -5.3 DEGREES
REMARK 500     DT B1005   C3' -  O3' -  P   ANGL. DEV. =   7.7 DEGREES
REMARK 500     DT B1007   O5' -  C5' -  C4' ANGL. DEV. =  -4.8 DEGREES
REMARK 500     DT B1008   C4' -  C3' -  C2' ANGL. DEV. =  -4.7 DEGREES
REMARK 500     DT B1008   O4' -  C1' -  N1  ANGL. DEV. =   6.2 DEGREES
REMARK 500     DT B1009   O4' -  C1' -  N1  ANGL. DEV. =   3.3 DEGREES
REMARK 500     DT B1009   N3  -  C4  -  O4  ANGL. DEV. =   4.0 DEGREES
REMARK 500     DT B1009   C5  -  C4  -  O4  ANGL. DEV. =  -5.4 DEGREES
REMARK 500     DT B1008   C3' -  O3' -  P   ANGL. DEV. =   8.0 DEGREES
REMARK 500     DT B1010   O5' -  C5' -  C4' ANGL. DEV. =  -5.3 DEGREES
REMARK 500     DT B1011   C4' -  C3' -  C2' ANGL. DEV. =  -4.7 DEGREES
REMARK 500     DT B1011   O4' -  C1' -  N1  ANGL. DEV. =   7.1 DEGREES
REMARK 500     DT B1012   O4' -  C1' -  N1  ANGL. DEV. =   3.6 DEGREES
REMARK 500     DT B1012   N3  -  C4  -  O4  ANGL. DEV. =   4.1 DEGREES
REMARK 500     DT B1012   C5  -  C4  -  O4  ANGL. DEV. =  -5.8 DEGREES
REMARK 500     DT B1011   C3' -  O3' -  P   ANGL. DEV. =   7.4 DEGREES
REMARK 500     DT B1012   C3' -  O3' -  P   ANGL. DEV. =  -9.4 DEGREES
REMARK 500     DT B1014   C4' -  C3' -  C2' ANGL. DEV. =  -4.3 DEGREES
REMARK 500     DT B1014   O4' -  C1' -  N1  ANGL. DEV. =   7.4 DEGREES
REMARK 500     DT B1015   O4' -  C1' -  N1  ANGL. DEV. =   3.3 DEGREES
REMARK 500     DT B1015   N3  -  C4  -  O4  ANGL. DEV. =   4.0 DEGREES
REMARK 500     DT B1015   C5  -  C4  -  O4  ANGL. DEV. =  -5.5 DEGREES
REMARK 500     DT B1014   C3' -  O3' -  P   ANGL. DEV. =   8.4 DEGREES
REMARK 500     DT B1016   O5' -  C5' -  C4' ANGL. DEV. =  -5.2 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500  M RES CSSEQI        PSI       PHI
REMARK 500    ALA A  98       30.48   -161.57
REMARK 500    SER A 145       97.66     78.60
REMARK 500    ASP A 161     -175.43    -58.45
REMARK 500    HIS A 163       60.03   -108.18
REMARK 500    GLU A 233       42.73    -88.12
REMARK 500    PHE A 255      -13.76     76.33
REMARK 500    GLU A 266      -39.90   -138.75
REMARK 500    VAL A 275      -72.28    -47.50
REMARK 500    LYS A1023      -78.73    -48.08
REMARK 500    VAL A1037       86.58    -63.90
REMARK 500    ALA A1098       30.47   -161.92
REMARK 500    SER A1145       97.27     78.75
REMARK 500    HIS A1163       68.64   -107.35
REMARK 500    GLU A1233       42.20    -88.09
REMARK 500    PHE A1255      -14.16     76.48
REMARK 500    GLU A1266      -39.65   -138.44
REMARK 500    VAL A1275      -73.35    -47.63
REMARK 500    SER A1329       43.15    -93.51
REMARK 500    ASN A1330       62.06    178.84
REMARK 500    LYS A2023      -78.58    -48.50
REMARK 500    ASP A2036      133.50    -38.40
REMARK 500    VAL A2037       83.54    -68.60
REMARK 500    ALA A2098       30.47   -161.65
REMARK 500    SER A2145       97.95     77.64
REMARK 500    HIS A2163       68.81   -107.95
REMARK 500    GLU A2233       42.38    -88.12
REMARK 500    PHE A2255      -13.79     75.57
REMARK 500    GLU A2266      -39.93   -138.35
REMARK 500    VAL A2275      -72.52    -47.44
REMARK 500    ASN A2330       62.68    179.34
REMARK 500    LYS A3023      -78.08    -48.58
REMARK 500    ASP A3036      131.74    -39.25
REMARK 500    VAL A3037       86.59    -66.00
REMARK 500    ALA A3098       30.93   -161.61
REMARK 500    SER A3145       97.99     78.19
REMARK 500    ALA A3147       -9.86    -58.02
REMARK 500    HIS A3163       68.67   -107.87
REMARK 500    GLU A3233       42.59    -88.39
REMARK 500    PHE A3255      -13.84     75.78
REMARK 500    GLU A3266      -39.98   -138.45
REMARK 500    VAL A3275      -72.22    -47.70
REMARK 500    SER A3329       43.63    -85.63
REMARK 500    ASN A3330       63.23    178.81
REMARK 500    LYS A4023      -79.01    -48.42
REMARK 500    ALA A4098       30.68   -162.05
REMARK 500    SER A4145       98.16     78.00
REMARK 500    ALA A4147       -9.45    -58.19
REMARK 500    HIS A4163       68.08   -107.59
REMARK 500    GLU A4233       43.39    -88.72
REMARK 500    PHE A4255      -14.08     76.79
REMARK 500    GLU A4266      -40.22   -138.42
REMARK 500    VAL A4275      -72.72    -47.66
REMARK 500    SER A4329       45.13    -94.35
REMARK 500    ASN A4330       62.34    178.70
REMARK 500    LYS A5023      -78.16    -48.31
REMARK 500    ASP A5036      134.01    -37.47
REMARK 500    VAL A5037       81.13    -69.22
REMARK 500    ALA A5098       30.56   -161.95
REMARK 500    SER A5145       97.45     78.76
REMARK 500    ALA A5147       -9.74    -58.05
REMARK 500    GLU A5233       42.77    -88.79
REMARK 500    PHE A5255      -14.16     76.88
REMARK 500    GLU A5266      -40.36   -138.15
REMARK 500    VAL A5275      -72.45    -47.65
REMARK 500
REMARK 500 REMARK: NULL
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 A 500  MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR A  73   OG1
REMARK 620 2 ADP A 502   O1B  83.8
REMARK 620 N                    1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MG A1500  MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR A1073   OG1
REMARK 620 2 ADP A1502   O1B  81.5
REMARK 620 N                    1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MG A2500  MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR A2073   OG1
REMARK 620 2 ADP A2502   O1B  88.2
REMARK 620 N                    1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MG A3500  MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR A3073   OG1
REMARK 620 2 ADP A3502   O1B  84.4
REMARK 620 N                    1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MG A4500  MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR A4073   OG1
REMARK 620 2 ADP A4502   O1B  82.0
REMARK 620 N                    1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MG A5500  MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR A5073   OG1
REMARK 620 2 ADP A5502   O1B  81.8
REMARK 620 N                    1
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 500
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ALF A 501
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1500
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ALF A 1501
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 2500
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ALF A 2501
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 3500
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ALF A 3501
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 4500
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ALF A 4501
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 5500
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ALF A 5501
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP A 502
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP A 1502
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP A 2502
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP A 3502
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP A 4502
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP A 5502
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3CMT   RELATED DB: PDB
REMARK 900 RELATED ID: 3CMV   RELATED DB: PDB
REMARK 900 RELATED ID: 3CMW   RELATED DB: PDB
REMARK 900 RELATED ID: 3CMX   RELATED DB: PDB
DBREF  3CMU B  999  1016  PDB    3CMT     3CMT             1     18
DBREF  3CMU A   30   334  UNP    P0A7G6   RECA_ECOLI      31    335
DBREF  3CMU A 1001  1334  UNP    P0A7G6   RECA_ECOLI       2    335
DBREF  3CMU A 2001  2334  UNP    P0A7G6   RECA_ECOLI       2    335
DBREF  3CMU A 3001  3334  UNP    P0A7G6   RECA_ECOLI       2    335
DBREF  3CMU A 4001  4334  UNP    P0A7G6   RECA_ECOLI       2    335
DBREF  3CMU A 5001  5334  UNP    P0A7G6   RECA_ECOLI       2    335
SEQADV 3CMU GLY A   26  UNP  P0A7G6              LINKER
SEQADV 3CMU ALA A   27  UNP  P0A7G6              LINKER
SEQADV 3CMU HIS A   28  UNP  P0A7G6              LINKER
SEQADV 3CMU MET A   29  UNP  P0A7G6              LINKER
SEQADV 3CMU THR A  986  UNP  P0A7G6              LINKER
SEQADV 3CMU GLY A  987  UNP  P0A7G6              LINKER
SEQADV 3CMU SER A  988  UNP  P0A7G6              LINKER
SEQADV 3CMU THR A  989  UNP  P0A7G6              LINKER
SEQADV 3CMU GLY A  990  UNP  P0A7G6              LINKER
SEQADV 3CMU SER A  991  UNP  P0A7G6              LINKER
SEQADV 3CMU GLY A  992  UNP  P0A7G6              LINKER
SEQADV 3CMU THR A  993  UNP  P0A7G6              LINKER
SEQADV 3CMU THR A  994  UNP  P0A7G6              LINKER
SEQADV 3CMU GLY A  995  UNP  P0A7G6              LINKER
SEQADV 3CMU SER A  996  UNP  P0A7G6              LINKER
SEQADV 3CMU THR A  997  UNP  P0A7G6              LINKER
SEQADV 3CMU GLY A  998  UNP  P0A7G6              LINKER
SEQADV 3CMU SER A  999  UNP  P0A7G6              LINKER
SEQADV 3CMU MET A 1000  UNP  P0A7G6              LINKER
SEQADV 3CMU THR A 1986  UNP  P0A7G6              LINKER
SEQADV 3CMU GLY A 1987  UNP  P0A7G6              LINKER
SEQADV 3CMU SER A 1988  UNP  P0A7G6              LINKER
SEQADV 3CMU THR A 1989  UNP  P0A7G6              LINKER
SEQADV 3CMU GLY A 1990  UNP  P0A7G6              LINKER
SEQADV 3CMU SER A 1991  UNP  P0A7G6              LINKER
SEQADV 3CMU MET A 1992  UNP  P0A7G6              LINKER
SEQADV 3CMU GLY A 1993  UNP  P0A7G6              LINKER
SEQADV 3CMU HIS A 1994  UNP  P0A7G6              LINKER
SEQADV 3CMU THR A 1995  UNP  P0A7G6              LINKER
SEQADV 3CMU THR A 1996  UNP  P0A7G6              LINKER
SEQADV 3CMU GLY A 1997  UNP  P0A7G6              LINKER
SEQADV 3CMU ALA A 1998  UNP  P0A7G6              LINKER
SEQADV 3CMU MET A 1999  UNP  P0A7G6              LINKER
SEQADV 3CMU SER A 2000  UNP  P0A7G6              LINKER
SEQADV 3CMU THR A 2986  UNP  P0A7G6              LINKER
SEQADV 3CMU GLY A 2987  UNP  P0A7G6              LINKER
SEQADV 3CMU SER A 2988  UNP  P0A7G6              LINKER
SEQADV 3CMU THR A 2989  UNP  P0A7G6              LINKER
SEQADV 3CMU GLY A 2990  UNP  P0A7G6              LINKER
SEQADV 3CMU SER A 2991  UNP  P0A7G6              LINKER
SEQADV 3CMU MET A 2992  UNP  P0A7G6              LINKER
SEQADV 3CMU ALA A 2993  UNP  P0A7G6              LINKER
SEQADV 3CMU SER A 2994  UNP  P0A7G6              LINKER
SEQADV 3CMU THR A 2995  UNP  P0A7G6              LINKER
SEQADV 3CMU GLY A 2996  UNP  P0A7G6              LINKER
SEQADV 3CMU SER A 2997  UNP  P0A7G6              LINKER
SEQADV 3CMU THR A 2998  UNP  P0A7G6              LINKER
SEQADV 3CMU GLY A 2999  UNP  P0A7G6              LINKER
SEQADV 3CMU SER A 3000  UNP  P0A7G6              LINKER
SEQADV 3CMU THR A 3989  UNP  P0A7G6              LINKER
SEQADV 3CMU GLY A 3990  UNP  P0A7G6              LINKER
SEQADV 3CMU ALA A 3991  UNP  P0A7G6              LINKER
SEQADV 3CMU THR A 3992  UNP  P0A7G6              LINKER
SEQADV 3CMU GLY A 3993  UNP  P0A7G6              LINKER
SEQADV 3CMU ALA A 3994  UNP  P0A7G6              LINKER
SEQADV 3CMU MET A 3995  UNP  P0A7G6              LINKER
SEQADV 3CMU SER A 3996  UNP  P0A7G6              LINKER
SEQADV 3CMU GLY A 3997  UNP  P0A7G6              LINKER
SEQADV 3CMU ARG A 3998  UNP  P0A7G6              LINKER
SEQADV 3CMU MET A 3999  UNP  P0A7G6              LINKER
SEQADV 3CMU SER A 4000  UNP  P0A7G6              LINKER
SEQADV 3CMU THR A 4987  UNP  P0A7G6              LINKER
SEQADV 3CMU GLY A 4988  UNP  P0A7G6              LINKER
SEQADV 3CMU SER A 4989  UNP  P0A7G6              LINKER
SEQADV 3CMU THR A 4990  UNP  P0A7G6              LINKER
SEQADV 3CMU GLY A 4991  UNP  P0A7G6              LINKER
SEQADV 3CMU SER A 4992  UNP  P0A7G6              LINKER
SEQADV 3CMU GLY A 4993  UNP  P0A7G6              LINKER
SEQADV 3CMU SER A 4994  UNP  P0A7G6              LINKER
SEQADV 3CMU SER A 4995  UNP  P0A7G6              LINKER
SEQADV 3CMU THR A 4996  UNP  P0A7G6              LINKER
SEQADV 3CMU GLY A 4997  UNP  P0A7G6              LINKER
SEQADV 3CMU SER A 4998  UNP  P0A7G6              LINKER
SEQADV 3CMU MET A 4999  UNP  P0A7G6              LINKER
SEQADV 3CMU SER A 5000  UNP  P0A7G6              LINKER
SEQRES   1 B   18   DT  DT  DT  DT  DT  DT  DT  DT  DT  DT  DT  DT  DT
SEQRES   2 B   18   DT  DT  DT  DT  DT
SEQRES   1 A 2050  GLY ALA HIS MET GLY GLU ASP ARG SER MET ASP VAL GLU
SEQRES   2 A 2050  THR ILE SER THR GLY SER LEU SER LEU ASP ILE ALA LEU
SEQRES   3 A 2050  GLY ALA GLY GLY LEU PRO MET GLY ARG ILE VAL GLU ILE
SEQRES   4 A 2050  TYR GLY PRO GLU SER SER GLY LYS THR THR LEU THR LEU
SEQRES   5 A 2050  GLN VAL ILE ALA ALA ALA GLN ARG GLU GLY LYS THR CYS
SEQRES   6 A 2050  ALA PHE ILE ASP ALA GLU HIS ALA LEU ASP PRO ILE TYR
SEQRES   7 A 2050  ALA ARG LYS LEU GLY VAL ASP ILE ASP ASN LEU LEU CYS
SEQRES   8 A 2050  SER GLN PRO ASP THR GLY GLU GLN ALA LEU GLU ILE CYS
SEQRES   9 A 2050  ASP ALA LEU ALA ARG SER GLY ALA VAL ASP VAL ILE VAL
SEQRES  10 A 2050  VAL ASP SER VAL ALA ALA LEU THR PRO LYS ALA GLU ILE
SEQRES  11 A 2050  GLU GLY GLU ILE GLY ASP SER HIS MET GLY LEU ALA ALA
SEQRES  12 A 2050  ARG MET MET SER GLN ALA MET ARG LYS LEU ALA GLY ASN
SEQRES  13 A 2050  LEU LYS GLN SER ASN THR LEU LEU ILE PHE ILE ASN GLN
SEQRES  14 A 2050  ILE ARG MET LYS ILE GLY VAL MET PHE GLY ASN PRO GLU
SEQRES  15 A 2050  THR THR THR GLY GLY ASN ALA LEU LYS PHE TYR ALA SER
SEQRES  16 A 2050  VAL ARG LEU ASP ILE ARG ARG ILE GLY ALA VAL LYS GLU
SEQRES  17 A 2050  GLY GLU ASN VAL VAL GLY SER GLU THR ARG VAL LYS VAL
SEQRES  18 A 2050  VAL LYS ASN LYS ILE ALA ALA PRO PHE LYS GLN ALA GLU
SEQRES  19 A 2050  PHE GLN ILE LEU TYR GLY GLU GLY ILE ASN PHE TYR GLY
SEQRES  20 A 2050  GLU LEU VAL ASP LEU GLY VAL LYS GLU LYS LEU ILE GLU
SEQRES  21 A 2050  LYS ALA GLY ALA TRP TYR SER TYR LYS GLY GLU LYS ILE
SEQRES  22 A 2050  GLY GLN GLY LYS ALA ASN ALA THR ALA TRP LEU LYS ASP
SEQRES  23 A 2050  ASN PRO GLU THR ALA LYS GLU ILE GLU LYS LYS VAL ARG
SEQRES  24 A 2050  GLU LEU LEU LEU SER ASN PRO ASN SER THR THR GLY SER
SEQRES  25 A 2050  THR GLY SER GLY THR THR GLY SER THR GLY SER MET ALA
SEQRES  26 A 2050  ILE ASP GLU ASN LYS GLN LYS ALA LEU ALA ALA ALA LEU
SEQRES  27 A 2050  GLY GLN ILE GLU LYS GLN PHE GLY LYS GLY SER ILE MET
SEQRES  28 A 2050  ARG LEU GLY GLU ASP ARG SER MET ASP VAL GLU THR ILE
SEQRES  29 A 2050  SER THR GLY SER LEU SER LEU ASP ILE ALA LEU GLY ALA
SEQRES  30 A 2050  GLY GLY LEU PRO MET GLY ARG ILE VAL GLU ILE TYR GLY
SEQRES  31 A 2050  PRO GLU SER SER GLY LYS THR THR LEU THR LEU GLN VAL
SEQRES  32 A 2050  ILE ALA ALA ALA GLN ARG GLU GLY LYS THR CYS ALA PHE
SEQRES  33 A 2050  ILE ASP ALA GLU HIS ALA LEU ASP PRO ILE TYR ALA ARG
SEQRES  34 A 2050  LYS LEU GLY VAL ASP ILE ASP ASN LEU LEU CYS SER GLN
SEQRES  35 A 2050  PRO ASP THR GLY GLU GLN ALA LEU GLU ILE CYS ASP ALA
SEQRES  36 A 2050  LEU ALA ARG SER GLY ALA VAL ASP VAL ILE VAL VAL ASP
SEQRES  37 A 2050  SER VAL ALA ALA LEU THR PRO LYS ALA GLU ILE GLU GLY
SEQRES  38 A 2050  GLU ILE GLY ASP SER HIS MET GLY LEU ALA ALA ARG MET
SEQRES  39 A 2050  MET SER GLN ALA MET ARG LYS LEU ALA GLY ASN LEU LYS
SEQRES  40 A 2050  GLN SER ASN THR LEU LEU ILE PHE ILE ASN GLN ILE ARG
SEQRES  41 A 2050  MET LYS ILE GLY VAL MET PHE GLY ASN PRO GLU THR THR
SEQRES  42 A 2050  THR GLY GLY ASN ALA LEU LYS PHE TYR ALA SER VAL ARG
SEQRES  43 A 2050  LEU ASP ILE ARG ARG ILE GLY ALA VAL LYS GLU GLY GLU
SEQRES  44 A 2050  ASN VAL VAL GLY SER GLU THR ARG VAL LYS VAL VAL LYS
SEQRES  45 A 2050  ASN LYS ILE ALA ALA PRO PHE LYS GLN ALA GLU PHE GLN
SEQRES  46 A 2050  ILE LEU TYR GLY GLU GLY ILE ASN PHE TYR GLY GLU LEU
SEQRES  47 A 2050  VAL ASP LEU GLY VAL LYS GLU LYS LEU ILE GLU LYS ALA
SEQRES  48 A 2050  GLY ALA TRP TYR SER TYR LYS GLY GLU LYS ILE GLY GLN
SEQRES  49 A 2050  GLY LYS ALA ASN ALA THR ALA TRP LEU LYS ASP ASN PRO
SEQRES  50 A 2050  GLU THR ALA LYS GLU ILE GLU LYS LYS VAL ARG GLU LEU
SEQRES  51 A 2050  LEU LEU SER ASN PRO ASN SER THR THR GLY SER THR GLY
SEQRES  52 A 2050  SER MET GLY HIS THR THR GLY ALA MET SER ALA ILE ASP
SEQRES  53 A 2050  GLU ASN LYS GLN LYS ALA LEU ALA ALA ALA LEU GLY GLN
SEQRES  54 A 2050  ILE GLU LYS GLN PHE GLY LYS GLY SER ILE MET ARG LEU
SEQRES  55 A 2050  GLY GLU ASP ARG SER MET ASP VAL GLU THR ILE SER THR
SEQRES  56 A 2050  GLY SER LEU SER LEU ASP ILE ALA LEU GLY ALA GLY GLY
SEQRES  57 A 2050  LEU PRO MET GLY ARG ILE VAL GLU ILE TYR GLY PRO GLU
SEQRES  58 A 2050  SER SER GLY LYS THR THR LEU THR LEU GLN VAL ILE ALA
SEQRES  59 A 2050  ALA ALA GLN ARG GLU GLY LYS THR CYS ALA PHE ILE ASP
SEQRES  60 A 2050  ALA GLU HIS ALA LEU ASP PRO ILE TYR ALA ARG LYS LEU
SEQRES  61 A 2050  GLY VAL ASP ILE ASP ASN LEU LEU CYS SER GLN PRO ASP
SEQRES  62 A 2050  THR GLY GLU GLN ALA LEU GLU ILE CYS ASP ALA LEU ALA
SEQRES  63 A 2050  ARG SER GLY ALA VAL ASP VAL ILE VAL VAL ASP SER VAL
SEQRES  64 A 2050  ALA ALA LEU THR PRO LYS ALA GLU ILE GLU GLY GLU ILE
SEQRES  65 A 2050  GLY ASP SER HIS MET GLY LEU ALA ALA ARG MET MET SER
SEQRES  66 A 2050  GLN ALA MET ARG LYS LEU ALA GLY ASN LEU LYS GLN SER
SEQRES  67 A 2050  ASN THR LEU LEU ILE PHE ILE ASN GLN ILE ARG MET LYS
SEQRES  68 A 2050  ILE GLY VAL MET PHE GLY ASN PRO GLU THR THR THR GLY
SEQRES  69 A 2050  GLY ASN ALA LEU LYS PHE TYR ALA SER VAL ARG LEU ASP
SEQRES  70 A 2050  ILE ARG ARG ILE GLY ALA VAL LYS GLU GLY GLU ASN VAL
SEQRES  71 A 2050  VAL GLY SER GLU THR ARG VAL LYS VAL VAL LYS ASN LYS
SEQRES  72 A 2050  ILE ALA ALA PRO PHE LYS GLN ALA GLU PHE GLN ILE LEU
SEQRES  73 A 2050  TYR GLY GLU GLY ILE ASN PHE TYR GLY GLU LEU VAL ASP
SEQRES  74 A 2050  LEU GLY VAL LYS GLU LYS LEU ILE GLU LYS ALA GLY ALA
SEQRES  75 A 2050  TRP TYR SER TYR LYS GLY GLU LYS ILE GLY GLN GLY LYS
SEQRES  76 A 2050  ALA ASN ALA THR ALA TRP LEU LYS ASP ASN PRO GLU THR
SEQRES  77 A 2050  ALA LYS GLU ILE GLU LYS LYS VAL ARG GLU LEU LEU LEU
SEQRES  78 A 2050  SER ASN PRO ASN SER THR THR GLY SER THR GLY SER MET
SEQRES  79 A 2050  ALA SER THR GLY SER THR GLY SER ALA ILE ASP GLU ASN
SEQRES  80 A 2050  LYS GLN LYS ALA LEU ALA ALA ALA LEU GLY GLN ILE GLU
SEQRES  81 A 2050  LYS GLN PHE GLY LYS GLY SER ILE MET ARG LEU GLY GLU
SEQRES  82 A 2050  ASP ARG SER MET ASP VAL GLU THR ILE SER THR GLY SER
SEQRES  83 A 2050  LEU SER LEU ASP ILE ALA LEU GLY ALA GLY GLY LEU PRO
SEQRES  84 A 2050  MET GLY ARG ILE VAL GLU ILE TYR GLY PRO GLU SER SER
SEQRES  85 A 2050  GLY LYS THR THR LEU THR LEU GLN VAL ILE ALA ALA ALA
SEQRES  86 A 2050  GLN ARG GLU GLY LYS THR CYS ALA PHE ILE ASP ALA GLU
SEQRES  87 A 2050  HIS ALA LEU ASP PRO ILE TYR ALA ARG LYS LEU GLY VAL
SEQRES  88 A 2050  ASP ILE ASP ASN LEU LEU CYS SER GLN PRO ASP THR GLY
SEQRES  89 A 2050  GLU GLN ALA LEU GLU ILE CYS ASP ALA LEU ALA ARG SER
SEQRES  90 A 2050  GLY ALA VAL ASP VAL ILE VAL VAL ASP SER VAL ALA ALA
SEQRES  91 A 2050  LEU THR PRO LYS ALA GLU ILE GLU GLY GLU ILE GLY ASP
SEQRES  92 A 2050  SER HIS MET GLY LEU ALA ALA ARG MET MET SER GLN ALA
SEQRES  93 A 2050  MET ARG LYS LEU ALA GLY ASN LEU LYS GLN SER ASN THR
SEQRES  94 A 2050  LEU LEU ILE PHE ILE ASN GLN ILE ARG MET LYS ILE GLY
SEQRES  95 A 2050  VAL MET PHE GLY ASN PRO GLU THR THR THR GLY GLY ASN
SEQRES  96 A 2050  ALA LEU LYS PHE TYR ALA SER VAL ARG LEU ASP ILE ARG
SEQRES  97 A 2050  ARG ILE GLY ALA VAL LYS GLU GLY GLU ASN VAL VAL GLY
SEQRES  98 A 2050  SER GLU THR ARG VAL LYS VAL VAL LYS ASN LYS ILE ALA
SEQRES  99 A 2050  ALA PRO PHE LYS GLN ALA GLU PHE GLN ILE LEU TYR GLY
SEQRES 100 A 2050  GLU GLY ILE ASN PHE TYR GLY GLU LEU VAL ASP LEU GLY
SEQRES 101 A 2050  VAL LYS GLU LYS LEU ILE GLU LYS ALA GLY ALA TRP TYR
SEQRES 102 A 2050  SER TYR LYS GLY GLU LYS ILE GLY GLN GLY LYS ALA ASN
SEQRES 103 A 2050  ALA THR ALA TRP LEU LYS ASP ASN PRO GLU THR ALA LYS
SEQRES 104 A 2050  GLU ILE GLU LYS LYS VAL ARG GLU LEU LEU LEU SER ASN
SEQRES 105 A 2050  PRO ASN SER THR THR GLY ALA THR GLY ALA MET SER GLY
SEQRES 106 A 2050  ARG MET SER ALA ILE ASP GLU ASN LYS GLN LYS ALA LEU
SEQRES 107 A 2050  ALA ALA ALA LEU GLY GLN ILE GLU LYS GLN PHE GLY LYS
SEQRES 108 A 2050  GLY SER ILE MET ARG LEU GLY GLU ASP ARG SER MET ASP
SEQRES 109 A 2050  VAL GLU THR ILE SER THR GLY SER LEU SER LEU ASP ILE
SEQRES 110 A 2050  ALA LEU GLY ALA GLY GLY LEU PRO MET GLY ARG ILE VAL
SEQRES 111 A 2050  GLU ILE TYR GLY PRO GLU SER SER GLY LYS THR THR LEU
SEQRES 112 A 2050  THR LEU GLN VAL ILE ALA ALA ALA GLN ARG GLU GLY LYS
SEQRES 113 A 2050  THR CYS ALA PHE ILE ASP ALA GLU HIS ALA LEU ASP PRO
SEQRES 114 A 2050  ILE TYR ALA ARG LYS LEU GLY VAL ASP ILE ASP ASN LEU
SEQRES 115 A 2050  LEU CYS SER GLN PRO ASP THR GLY GLU GLN ALA LEU GLU
SEQRES 116 A 2050  ILE CYS ASP ALA LEU ALA ARG SER GLY ALA VAL ASP VAL
SEQRES 117 A 2050  ILE VAL VAL ASP SER VAL ALA ALA LEU THR PRO LYS ALA
SEQRES 118 A 2050  GLU ILE GLU GLY GLU ILE GLY ASP SER HIS MET GLY LEU
SEQRES 119 A 2050  ALA ALA ARG MET MET SER GLN ALA MET ARG LYS LEU ALA
SEQRES 120 A 2050  GLY ASN LEU LYS GLN SER ASN THR LEU LEU ILE PHE ILE
SEQRES 121 A 2050  ASN GLN ILE ARG MET LYS ILE GLY VAL MET PHE GLY ASN
SEQRES 122 A 2050  PRO GLU THR THR THR GLY GLY ASN ALA LEU LYS PHE TYR
SEQRES 123 A 2050  ALA SER VAL ARG LEU ASP ILE ARG ARG ILE GLY ALA VAL
SEQRES 124 A 2050  LYS GLU GLY GLU ASN VAL VAL GLY SER GLU THR ARG VAL
SEQRES 125 A 2050  LYS VAL VAL LYS ASN LYS ILE ALA ALA PRO PHE LYS GLN
SEQRES 126 A 2050  ALA GLU PHE GLN ILE LEU TYR GLY GLU GLY ILE ASN PHE
SEQRES 127 A 2050  TYR GLY GLU LEU VAL ASP LEU GLY VAL LYS GLU LYS LEU
SEQRES 128 A 2050  ILE GLU LYS ALA GLY ALA TRP TYR SER TYR LYS GLY GLU
SEQRES 129 A 2050  LYS ILE GLY GLN GLY LYS ALA ASN ALA THR ALA TRP LEU
SEQRES 130 A 2050  LYS ASP ASN PRO GLU THR ALA LYS GLU ILE GLU LYS LYS
SEQRES 131 A 2050  VAL ARG GLU LEU LEU LEU SER ASN PRO ASN SER THR THR
SEQRES 132 A 2050  GLY SER THR GLY SER GLY SER SER THR GLY SER MET SER
SEQRES 133 A 2050  ALA ILE ASP GLU ASN LYS GLN LYS ALA LEU ALA ALA ALA
SEQRES 134 A 2050  LEU GLY GLN ILE GLU LYS GLN PHE GLY LYS GLY SER ILE
SEQRES 135 A 2050  MET ARG LEU GLY GLU ASP ARG SER MET ASP VAL GLU THR
SEQRES 136 A 2050  ILE SER THR GLY SER LEU SER LEU ASP ILE ALA LEU GLY
SEQRES 137 A 2050  ALA GLY GLY LEU PRO MET GLY ARG ILE VAL GLU ILE TYR
SEQRES 138 A 2050  GLY PRO GLU SER SER GLY LYS THR THR LEU THR LEU GLN
SEQRES 139 A 2050  VAL ILE ALA ALA ALA GLN ARG GLU GLY LYS THR CYS ALA
SEQRES 140 A 2050  PHE ILE ASP ALA GLU HIS ALA LEU ASP PRO ILE TYR ALA
SEQRES 141 A 2050  ARG LYS LEU GLY VAL ASP ILE ASP ASN LEU LEU CYS SER
SEQRES 142 A 2050  GLN PRO ASP THR GLY GLU GLN ALA LEU GLU ILE CYS ASP
SEQRES 143 A 2050  ALA LEU ALA ARG SER GLY ALA VAL ASP VAL ILE VAL VAL
SEQRES 144 A 2050  ASP SER VAL ALA ALA LEU THR PRO LYS ALA GLU ILE GLU
SEQRES 145 A 2050  GLY GLU ILE GLY ASP SER HIS MET GLY LEU ALA ALA ARG
SEQRES 146 A 2050  MET MET SER GLN ALA MET ARG LYS LEU ALA GLY ASN LEU
SEQRES 147 A 2050  LYS GLN SER ASN THR LEU LEU ILE PHE ILE ASN GLN ILE
SEQRES 148 A 2050  ARG MET LYS ILE GLY VAL MET PHE GLY ASN PRO GLU THR
SEQRES 149 A 2050  THR THR GLY GLY ASN ALA LEU LYS PHE TYR ALA SER VAL
SEQRES 150 A 2050  ARG LEU ASP ILE ARG ARG ILE GLY ALA VAL LYS GLU GLY
SEQRES 151 A 2050  GLU ASN VAL VAL GLY SER GLU THR ARG VAL LYS VAL VAL
SEQRES 152 A 2050  LYS ASN LYS ILE ALA ALA PRO PHE LYS GLN ALA GLU PHE
SEQRES 153 A 2050  GLN ILE LEU TYR GLY GLU GLY ILE ASN PHE TYR GLY GLU
SEQRES 154 A 2050  LEU VAL ASP LEU GLY VAL LYS GLU LYS LEU ILE GLU LYS
SEQRES 155 A 2050  ALA GLY ALA TRP TYR SER TYR LYS GLY GLU LYS ILE GLY
SEQRES 156 A 2050  GLN GLY LYS ALA ASN ALA THR ALA TRP LEU LYS ASP ASN
SEQRES 157 A 2050  PRO GLU THR ALA LYS GLU ILE GLU LYS LYS VAL ARG GLU
SEQRES 158 A 2050  LEU LEU LEU SER ASN PRO ASN SER THR
HET     MG  A 500       1
HET    ALF  A 501       5
HET     MG  A1500       1
HET    ALF  A1501       5
HET     MG  A2500       1
HET    ALF  A2501       5
HET     MG  A3500       1
HET    ALF  A3501       5
HET     MG  A4500       1
HET    ALF  A4501       5
HET     MG  A5500       1
HET    ALF  A5501       5
HET    ADP  A 502      27
HET    ADP  A1502      27
HET    ADP  A2502      27
HET    ADP  A3502      27
HET    ADP  A4502      27
HET    ADP  A5502      27
HETNAM      MG MAGNESIUM ION
HETNAM     ALF TETRAFLUOROALUMINATE ION
HETNAM     ADP ADENOSINE-5'-DIPHOSPHATE
FORMUL   3   MG    6(MG 2+)
FORMUL   4  ALF    6(AL F4 1-)
FORMUL  15  ADP    6(C10 H15 N5 O10 P2)
HELIX    1   1 SER A   44  GLY A   52  1                                   9
HELIX    2   2 GLY A   71  ARG A   85  1                                  15
HELIX    3   3 ASP A  100  LEU A  107  1                                   8
HELIX    4   4 THR A  121  GLY A  136  1                                  16
HELIX    5   5 SER A  145  LEU A  149  5                                   5
HELIX    6   6 PRO A  151  GLY A  157  1                                   7
HELIX    7   7 GLY A  165  GLN A  184  1                                  20
HELIX    8   8 GLY A  211  TYR A  218  1                                   8
HELIX    9   9 ASN A  269  GLU A  281  1                                  13
HELIX   10  10 GLY A  301  LYS A  310  1                                  10
HELIX   11  11 ASN A  312  LEU A  328  1                                  17
HELIX   12  12 ASN A 1005  GLY A 1022  1                                  18
HELIX   13  13 GLY A 1030  ASP A 1032  5                                   3
HELIX   14  14 SER A 1044  GLY A 1052  1                                   9
HELIX   15  15 GLY A 1071  ARG A 1085  1                                  15
HELIX   16  16 ASP A 1100  LEU A 1107  1                                   8
HELIX   17  17 THR A 1121  GLY A 1136  1                                  16
HELIX   18  18 SER A 1145  LEU A 1149  5                                   5
HELIX   19  19 PRO A 1151  GLY A 1157  1                                   7
HELIX   20  20 GLY A 1165  GLN A 1184  1                                  20
HELIX   21  21 GLY A 1211  TYR A 1218  1                                   8
HELIX   22  22 ASN A 1269  GLU A 1281  1                                  13
HELIX   23  23 GLY A 1301  LYS A 1310  1                                  10
HELIX   24  24 ASN A 1312  LEU A 1328  1                                  17
HELIX   25  25 ASN A 2005  GLY A 2022  1                                  18
HELIX   26  26 GLY A 2030  ASP A 2032  5                                   3
HELIX   27  27 SER A 2044  GLY A 2052  1                                   9
HELIX   28  28 GLY A 2071  ARG A 2085  1                                  15
HELIX   29  29 ASP A 2100  LEU A 2107  1                                   8
HELIX   30  30 THR A 2121  GLY A 2136  1                                  16
HELIX   31  31 SER A 2145  LEU A 2149  5                                   5
HELIX   32  32 PRO A 2151  GLY A 2157  1                                   7
HELIX   33  33 GLY A 2165  GLN A 2184  1                                  20
HELIX   34  34 GLY A 2211  TYR A 2218  1                                   8
HELIX   35  35 ASN A 2269  GLU A 2281  1                                  13
HELIX   36  36 GLY A 2301  LYS A 2310  1                                  10
HELIX   37  37 ASN A 2312  LEU A 2328  1                                  17
HELIX   38  38 ASN A 3005  GLY A 3022  1                                  18
HELIX   39  39 GLY A 3030  ASP A 3032  5                                   3
HELIX   40  40 SER A 3044  GLY A 3052  1                                   9
HELIX   41  41 GLY A 3071  ARG A 3085  1                                  15
HELIX   42  42 ASP A 3100  LEU A 3107  1                                   8
HELIX   43  43 THR A 3121  GLY A 3136  1                                  16
HELIX   44  44 SER A 3145  LEU A 3149  5                                   5
HELIX   45  45 PRO A 3151  GLY A 3157  1                                   7
HELIX   46  46 GLY A 3165  GLN A 3184  1                                  20
HELIX   47  47 GLY A 3211  TYR A 3218  1                                   8
HELIX   48  48 ASN A 3269  GLU A 3281  1                                  13
HELIX   49  49 GLY A 3301  LYS A 3310  1                                  10
HELIX   50  50 ASN A 3312  LEU A 3328  1                                  17
HELIX   51  51 ASN A 4005  GLY A 4022  1                                  18
HELIX   52  52 GLY A 4030  ASP A 4032  5                                   3
HELIX   53  53 SER A 4044  GLY A 4052  1                                   9
HELIX   54  54 GLY A 4071  ARG A 4085  1                                  15
HELIX   55  55 ASP A 4100  LEU A 4107  1                                   8
HELIX   56  56 THR A 4121  GLY A 4136  1                                  16
HELIX   57  57 SER A 4145  LEU A 4149  5                                   5
HELIX   58  58 PRO A 4151  GLY A 4157  1                                   7
HELIX   59  59 GLY A 4165  GLN A 4184  1                                  20
HELIX   60  60 GLY A 4211  TYR A 4218  1                                   8
HELIX   61  61 ASN A 4269  GLU A 4281  1                                  13
HELIX   62  62 GLY A 4301  LYS A 4310  1                                  10
HELIX   63  63 ASN A 4312  LEU A 4328  1                                  17
HELIX   64  64 ASN A 5005  GLY A 5022  1                                  18
HELIX   65  65 GLY A 5030  ASP A 5032  5                                   3
HELIX   66  66 SER A 5044  GLY A 5052  1                                   9
HELIX   67  67 GLY A 5071  ARG A 5085  1                                  15
HELIX   68  68 ASP A 5100  LEU A 5107  1                                   8
HELIX   69  69 THR A 5121  GLY A 5136  1                                  16
HELIX   70  70 SER A 5145  LEU A 5149  5                                   5
HELIX   71  71 PRO A 5151  GLU A 5156  1                                   6
HELIX   72  72 GLY A 5165  GLN A 5184  1                                  20
HELIX   73  73 GLY A 5211  TYR A 5218  1                                   8
HELIX   74  74 ASN A 5269  GLU A 5281  1                                  13
HELIX   75  75 GLY A 5301  LYS A 5310  1                                  10
HELIX   76  76 ASN A 5312  LEU A 5328  1                                  17
SHEET    1   A 2 THR A  39  ILE A  40  0
SHEET    2   A 2 LEU A  56  PRO A  57 -1  O  LEU A  56   N  ILE A  40
SHEET    1   B10 GLY A 267  ILE A 268  0
SHEET    2   B10 GLN A 257  LEU A 263 -1  N  LEU A 263   O  GLY A 267
SHEET    3   B10 ASN A 236  ASN A 249 -1  N  THR A 242   O  PHE A 260
SHEET    4   B10 ALA A 219  GLU A 233 -1  N  ARG A 222   O  VAL A 247
SHEET    5   B10 ILE A  61  TYR A  65  1  N  ILE A  61   O  SER A 220
SHEET    6   B10 LEU A 188  ASN A 193  1  O  PHE A 191   N  VAL A  62
SHEET    7   B10 VAL A 140  VAL A 143  1  N  ILE A 141   O  ILE A 190
SHEET    8   B10 CYS A  90  ILE A  93  1  N  ILE A  93   O  VAL A 142
SHEET    9   B10 LEU A 115  SER A 117  1  O  SER A 117   N  PHE A  92
SHEET   10   B10 ILE A1026  ARG A1028 -1  O  MET A1027   N  CYS A 116
SHEET    1   C 2 ARG A 196  MET A 197  0
SHEET    2   C 2 GLU A 207  THR A 208 -1  O  THR A 208   N  ARG A 196
SHEET    1   D 3 GLU A 285  ALA A 287  0
SHEET    2   D 3 TRP A 290  TYR A 293 -1  O  SER A 292   N  GLU A 285
SHEET    3   D 3 GLU A 296  GLN A 300 -1  O  GLU A 296   N  TYR A 293
SHEET    1   E 2 THR A1039  ILE A1040  0
SHEET    2   E 2 LEU A1056  PRO A1057 -1  O  LEU A1056   N  ILE A1040
SHEET    1   F10 GLY A1267  ILE A1268  0
SHEET    2   F10 GLN A1257  LEU A1263 -1  N  LEU A1263   O  GLY A1267
SHEET    3   F10 ASN A1236  ASN A1249 -1  N  THR A1242   O  PHE A1260
SHEET    4   F10 ALA A1219  GLU A1233 -1  N  ARG A1222   O  VAL A1247
SHEET    5   F10 ILE A1061  TYR A1065  1  N  ILE A1061   O  SER A1220
SHEET    6   F10 LEU A1188  ASN A1193  1  O  PHE A1191   N  VAL A1062
SHEET    7   F10 VAL A1140  VAL A1143  1  N  ILE A1141   O  ILE A1190
SHEET    8   F10 CYS A1090  ILE A1093  1  N  ILE A1093   O  VAL A1142
SHEET    9   F10 LEU A1115  SER A1117  1  O  SER A1117   N  PHE A1092
SHEET   10   F10 ILE A2026  ARG A2028 -1  O  MET A2027   N  CYS A1116
SHEET    1   G 2 ARG A1196  MET A1197  0
SHEET    2   G 2 GLU A1207  THR A1208 -1  O  THR A1208   N  ARG A1196
SHEET    1   H 3 GLU A1285  ALA A1287  0
SHEET    2   H 3 TRP A1290  TYR A1293 -1  O  SER A1292   N  GLU A1285
SHEET    3   H 3 GLU A1296  GLN A1300 -1  O  GLU A1296   N  TYR A1293
SHEET    1   I 2 THR A2039  ILE A2040  0
SHEET    2   I 2 LEU A2056  PRO A2057 -1  O  LEU A2056   N  ILE A2040
SHEET    1   J10 GLY A2267  ILE A2268  0
SHEET    2   J10 GLN A2257  LEU A2263 -1  N  LEU A2263   O  GLY A2267
SHEET    3   J10 ASN A2236  ASN A2249 -1  N  THR A2242   O  PHE A2260
SHEET    4   J10 ALA A2219  GLU A2233 -1  N  ASP A2224   O  LYS A2245
SHEET    5   J10 ILE A2061  TYR A2065  1  N  ILE A2061   O  SER A2220
SHEET    6   J10 LEU A2188  ASN A2193  1  O  PHE A2191   N  VAL A2062
SHEET    7   J10 VAL A2140  VAL A2143  1  N  VAL A2143   O  ILE A2192
SHEET    8   J10 CYS A2090  ILE A2093  1  N  ILE A2093   O  VAL A2142
SHEET    9   J10 LEU A2115  SER A2117  1  O  SER A2117   N  PHE A2092
SHEET   10   J10 ILE A3026  ARG A3028 -1  O  MET A3027   N  CYS A2116
SHEET    1   K 2 ARG A2196  MET A2197  0
SHEET    2   K 2 GLU A2207  THR A2208 -1  O  THR A2208   N  ARG A2196
SHEET    1   L 3 GLU A2285  ALA A2287  0
SHEET    2   L 3 TRP A2290  TYR A2293 -1  O  SER A2292   N  GLU A2285
SHEET    3   L 3 GLU A2296  GLN A2300 -1  O  GLU A2296   N  TYR A2293
SHEET    1   M 2 THR A3039  ILE A3040  0
SHEET    2   M 2 LEU A3056  PRO A3057 -1  O  LEU A3056   N  ILE A3040
SHEET    1   N10 GLY A3267  ILE A3268  0
SHEET    2   N10 GLN A3257  LEU A3263 -1  N  LEU A3263   O  GLY A3267
SHEET    3   N10 ASN A3236  ASN A3249 -1  N  THR A3242   O  PHE A3260
SHEET    4   N10 ALA A3219  GLU A3233 -1  N  ASP A3224   O  LYS A3245
SHEET    5   N10 ILE A3061  TYR A3065  1  N  ILE A3061   O  SER A3220
SHEET    6   N10 LEU A3188  ASN A3193  1  O  PHE A3191   N  VAL A3062
SHEET    7   N10 VAL A3140  VAL A3143  1  N  ILE A3141   O  ILE A3190
SHEET    8   N10 CYS A3090  ILE A3093  1  N  ILE A3093   O  VAL A3142
SHEET    9   N10 LEU A3115  SER A3117  1  O  SER A3117   N  PHE A3092
SHEET   10   N10 ILE A4026  ARG A4028 -1  O  MET A4027   N  CYS A3116
SHEET    1   O 2 ARG A3196  MET A3197  0
SHEET    2   O 2 GLU A3207  THR A3208 -1  O  THR A3208   N  ARG A3196
SHEET    1   P 3 GLU A3285  ALA A3287  0
SHEET    2   P 3 TRP A3290  TYR A3293 -1  O  SER A3292   N  GLU A3285
SHEET    3   P 3 GLU A3296  GLN A3300 -1  O  GLU A3296   N  TYR A3293
SHEET    1   Q 2 THR A4039  ILE A4040  0
SHEET    2   Q 2 LEU A4056  PRO A4057 -1  O  LEU A4056   N  ILE A4040
SHEET    1   R10 GLY A4267  ILE A4268  0
SHEET    2   R10 GLN A4257  LEU A4263 -1  N  LEU A4263   O  GLY A4267
SHEET    3   R10 ASN A4236  ASN A4249 -1  N  THR A4242   O  PHE A4260
SHEET    4   R10 ALA A4219  GLU A4233 -1  N  ASP A4224   O  LYS A4245
SHEET    5   R10 ILE A4061  TYR A4065  1  N  ILE A4061   O  SER A4220
SHEET    6   R10 LEU A4188  ASN A4193  1  O  PHE A4191   N  VAL A4062
SHEET    7   R10 VAL A4140  VAL A4143  1  N  ILE A4141   O  ILE A4190
SHEET    8   R10 CYS A4090  ILE A4093  1  N  ILE A4093   O  VAL A4142
SHEET    9   R10 LEU A4115  SER A4117  1  O  SER A4117   N  PHE A4092
SHEET   10   R10 ILE A5026  ARG A5028 -1  O  MET A5027   N  CYS A4116
SHEET    1   S 2 ILE A4195  MET A4197  0
SHEET    2   S 2 GLU A4207  THR A4209 -1  O  THR A4208   N  ARG A4196
SHEET    1   T 3 GLU A4285  ALA A4287  0
SHEET    2   T 3 TRP A4290  TYR A4293 -1  O  SER A4292   N  GLU A4285
SHEET    3   T 3 GLU A4296  GLN A4300 -1  O  GLU A4296   N  TYR A4293
SHEET    1   U 2 THR A5039  ILE A5040  0
SHEET    2   U 2 LEU A5056  PRO A5057 -1  O  LEU A5056   N  ILE A5040
SHEET    1   V 9 LEU A5115  SER A5117  0
SHEET    2   V 9 CYS A5090  ILE A5093  1  N  PHE A5092   O  SER A5117
SHEET    3   V 9 VAL A5140  VAL A5143  1  O  VAL A5142   N  ILE A5093
SHEET    4   V 9 LEU A5188  ASN A5193  1  O  ILE A5190   N  ILE A5141
SHEET    5   V 9 ILE A5061  TYR A5065  1  N  VAL A5062   O  PHE A5191
SHEET    6   V 9 ALA A5219  GLU A5233  1  O  SER A5220   N  ILE A5061
SHEET    7   V 9 ASN A5236  ASN A5249 -1  O  LYS A5245   N  ASP A5224
SHEET    8   V 9 GLN A5257  LEU A5263 -1  O  PHE A5260   N  THR A5242
SHEET    9   V 9 GLY A5267  ILE A5268 -1  O  GLY A5267   N  LEU A5263
SHEET    1   W 3 GLU A5285  ALA A5287  0
SHEET    2   W 3 TRP A5290  TYR A5293 -1  O  SER A5292   N  GLU A5285
SHEET    3   W 3 GLU A5296  GLN A5300 -1  O  GLU A5296   N  TYR A5293
LINK         OG1 THR A  73                MG    MG A 500     1555   1555  2.17
LINK         OG1 THR A1073                MG    MG A1500     1555   1555  2.13
LINK         OG1 THR A2073                MG    MG A2500     1555   1555  2.13
LINK         OG1 THR A3073                MG    MG A3500     1555   1555  2.14
LINK         OG1 THR A4073                MG    MG A4500     1555   1555  2.15
LINK         OG1 THR A5073                MG    MG A5500     1555   1555  2.30
LINK        MG    MG A 500                 O1B ADP A 502     1555   1555  2.20
LINK        MG    MG A1500                 O1B ADP A1502     1555   1555  2.19
LINK        MG    MG A2500                 O1B ADP A2502     1555   1555  2.20
LINK        MG    MG A3500                 O1B ADP A3502     1555   1555  2.22
LINK        MG    MG A4500                 O1B ADP A4502     1555   1555  2.21
LINK        MG    MG A5500                 O1B ADP A5502     1555   1555  2.25
SITE     1 AC1  4 THR A  73  GLU A  96  ASP A 144  LYS A1250
SITE     1 AC2  8 GLU A  68  SER A  69  LYS A  72  THR A  73
SITE     2 AC2  8 GLU A  96  PHE A1217  LYS A1248  LYS A1250
SITE     1 AC3  3 THR A1073  GLU A1096  LYS A2250
SITE     1 AC4  8 GLU A1068  SER A1069  LYS A1072  THR A1073
SITE     2 AC4  8 GLU A1096  PHE A2217  LYS A2248  LYS A2250
SITE     1 AC5  3 THR A2073  GLU A2096  LYS A3250
SITE     1 AC6  8 GLU A2068  SER A2069  LYS A2072  THR A2073
SITE     2 AC6  8 GLU A2096  PHE A3217  LYS A3248  LYS A3250
SITE     1 AC7  3 THR A3073  GLU A3096  LYS A4250
SITE     1 AC8  8 GLU A3068  SER A3069  LYS A3072  THR A3073
SITE     2 AC8  8 GLU A3096  PHE A4217  LYS A4248  LYS A4250
SITE     1 AC9  3 THR A4073  GLU A4096  LYS A5250
SITE     1 BC1  8 GLU A4068  SER A4069  LYS A4072  THR A4073
SITE     2 BC1  8 GLU A4096  PHE A5217  LYS A5248  LYS A5250
SITE     1 BC2  2 THR A5073  GLU A5096
SITE     1 BC3  5 GLU A5068  SER A5069  LYS A5072  THR A5073
SITE     2 BC3  5 GLU A5096
SITE     1 BC4 16 SER A  69  SER A  70  GLY A  71  LYS A  72
SITE     2 BC4 16 THR A  73  THR A  74  ASP A 100  TYR A 103
SITE     3 BC4 16 SER A 240  TYR A 264  ASN A1249  LYS A1250
SITE     4 BC4 16 ILE A1251  ALA A1252  ALA A1253  PRO A1254
SITE     1 BC5 16 SER A1069  SER A1070  GLY A1071  LYS A1072
SITE     2 BC5 16 THR A1073  THR A1074  ASP A1100  TYR A1103
SITE     3 BC5 16 SER A1240  TYR A1264  ASN A2249  LYS A2250
SITE     4 BC5 16 ILE A2251  ALA A2252  ALA A2253  PRO A2254
SITE     1 BC6 18 PRO A2067  GLU A2068  SER A2069  SER A2070
SITE     2 BC6 18 GLY A2071  LYS A2072  THR A2073  THR A2074
SITE     3 BC6 18 ASP A2100  TYR A2103  SER A2240  TYR A2264
SITE     4 BC6 18 ASN A3249  LYS A3250  ILE A3251  ALA A3252
SITE     5 BC6 18 ALA A3253  PRO A3254
SITE     1 BC7 16 SER A3069  SER A3070  GLY A3071  LYS A3072
SITE     2 BC7 16 THR A3073  THR A3074  ASP A3100  TYR A3103
SITE     3 BC7 16 SER A3240  TYR A3264  ASN A4249  LYS A4250
SITE     4 BC7 16 ILE A4251  ALA A4252  ALA A4253  PRO A4254
SITE     1 BC8 16 SER A4069  SER A4070  GLY A4071  LYS A4072
SITE     2 BC8 16 THR A4073  THR A4074  ASP A4100  TYR A4103
SITE     3 BC8 16 SER A4240  TYR A4264  ASN A5249  LYS A5250
SITE     4 BC8 16 ILE A5251  ALA A5252  ALA A5253  PRO A5254
SITE     1 BC9 11 GLU A5068  SER A5069  SER A5070  GLY A5071
SITE     2 BC9 11 LYS A5072  THR A5073  THR A5074  ASP A5100
SITE     3 BC9 11 TYR A5103  SER A5240  TYR A5264
CRYST1  156.000  156.000  211.000  90.00  90.00 120.00 P 32 2 1      6
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      0.006410  0.003701  0.000000        0.00000
SCALE2      0.000000  0.007402  0.000000        0.00000
SCALE3      0.000000  0.000000  0.004739        0.00000
      
PROCHECK
Go to PROCHECK summary
 References