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PDBsum entry 3r5x

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Top Page protein ligands metals Protein-protein interface(s) links
Ligase PDB id
3r5x
Jmol
Contents
Protein chains
302 a.a.
284 a.a.
Ligands
ATP ×4
EDO
ACY
Metals
_CA ×7
_MG
Waters ×750
HEADER    LIGASE                                  20-MAR-11   3R5X
TITLE     CRYSTAL STRUCTURE OF D-ALANINE--D-ALANINE LIGASE FROM BACILLUS
TITLE    2 ANTHRACIS COMPLEXED WITH ATP
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: D-ALANINE--D-ALANINE LIGASE;
COMPND   3 CHAIN: A, B, C, D;
COMPND   4 SYNONYM: D-ALA-D-ALA LIGASE, D-ALANYLALANINE SYNTHETASE;
COMPND   5 EC: 6.3.2.4;
COMPND   6 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: BACILLUS ANTHRACIS;
SOURCE   3 ORGANISM_COMMON: ANTHRAX,ANTHRAX BACTERIUM;
SOURCE   4 ORGANISM_TAXID: 1392;
SOURCE   5 STRAIN: AMES;
SOURCE   6 GENE: BAS2435, BA_2610, DDL, DDLB, GBAA_2610;
SOURCE   7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE   9 EXPRESSION_SYSTEM_STRAIN: BL21 MAGIC;
SOURCE  10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE  11 EXPRESSION_SYSTEM_PLASMID: PMCSG7
KEYWDS    ALPHA-BETA STRUCTURE, LIGASE, CYTOSOL, STRUCTURAL GENOMICS, CENTER
KEYWDS   2 FOR STRUCTURAL GENOMICS OF INFECTIOUS DISEASES, CSGID
EXPDTA    X-RAY DIFFRACTION
AUTHOR    Y.KIM,R.MULLIGAN,J.HASSEMAN,W.F.ANDERSON,A.JOACHIMIAK,CSGID
REVDAT   1   06-APR-11 3R5X    0
JRNL        AUTH   Y.KIM,J.HASSEMAN,W.F.ANDERSON,A.JOACHIMIAK,CSGID
JRNL        TITL   CRYSTAL STRUCTURE OF D-ALANINE--D-ALANINE LIGASE FROM
JRNL        TITL 2 BACILLUS ANTHRACIS COMPLEXED WITH ATP
JRNL        REF    TO BE PUBLISHED
JRNL        REFN
REMARK   2
REMARK   2 RESOLUTION.    2.00 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.7_650)
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-
REMARK   3               : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,
REMARK   3               : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL
REMARK   3               : MORIARTY,REETAL PAI,RANDY READ,JANE
REMARK   3               : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM
REMARK   3               : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,
REMARK   3               : LAURENT STORONI,TOM TERWILLIGER,PETER
REMARK   3               : ZWART
REMARK   3
REMARK   3    REFINEMENT TARGET : MLHL
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 32.77
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 0.000
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.8
REMARK   3   NUMBER OF REFLECTIONS             : 84091
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.180
REMARK   3   R VALUE            (WORKING SET) : 0.177
REMARK   3   FREE R VALUE                     : 0.221
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.040
REMARK   3   FREE R VALUE TEST SET COUNT      : 4235
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE
REMARK   3     1 32.7796 -  6.2089    0.87     2412   107  0.1687 0.1905
REMARK   3     2  6.2089 -  4.9336    0.99     2705   153  0.1571 0.1876
REMARK   3     3  4.9336 -  4.3115    0.99     2694   137  0.1252 0.1767
REMARK   3     4  4.3115 -  3.9180    0.99     2754   150  0.1348 0.1582
REMARK   3     5  3.9180 -  3.6376    0.98     2654   166  0.1543 0.1833
REMARK   3     6  3.6376 -  3.4234    0.98     2702   156  0.1670 0.2059
REMARK   3     7  3.4234 -  3.2521    0.98     2701   141  0.1780 0.1993
REMARK   3     8  3.2521 -  3.1106    0.98     2679   148  0.1801 0.2360
REMARK   3     9  3.1106 -  2.9910    0.98     2684   159  0.1916 0.2453
REMARK   3    10  2.9910 -  2.8878    0.98     2752   127  0.1825 0.2549
REMARK   3    11  2.8878 -  2.7976    0.98     2663   150  0.1782 0.2334
REMARK   3    12  2.7976 -  2.7176    0.98     2731   139  0.1828 0.2307
REMARK   3    13  2.7176 -  2.6461    0.98     2663   124  0.1878 0.2823
REMARK   3    14  2.6461 -  2.5816    0.98     2702   160  0.1946 0.2471
REMARK   3    15  2.5816 -  2.5229    0.98     2721   121  0.1908 0.2686
REMARK   3    16  2.5229 -  2.4693    0.98     2686   128  0.2076 0.2967
REMARK   3    17  2.4693 -  2.4199    0.98     2720   113  0.2059 0.2589
REMARK   3    18  2.4199 -  2.3742    0.98     2672   141  0.2000 0.2816
REMARK   3    19  2.3742 -  2.3318    0.97     2690   147  0.1960 0.2651
REMARK   3    20  2.3318 -  2.2923    0.98     2684   145  0.2070 0.2544
REMARK   3    21  2.2923 -  2.2554    0.97     2635   153  0.2198 0.2783
REMARK   3    22  2.2554 -  2.2207    0.97     2690   142  0.2379 0.3337
REMARK   3    23  2.2207 -  2.1880    0.97     2682   148  0.2333 0.2603
REMARK   3    24  2.1880 -  2.1572    0.97     2586   148  0.2388 0.2977
REMARK   3    25  2.1572 -  2.1281    0.97     2739   146  0.2520 0.3049
REMARK   3    26  2.1281 -  2.1004    0.97     2626   136  0.2668 0.3232
REMARK   3    27  2.1004 -  2.0742    0.96     2663   138  0.2709 0.2991
REMARK   3    28  2.0742 -  2.0492    0.95     2639   143  0.2876 0.3150
REMARK   3    29  2.0492 -  2.0254    0.94     2558   145  0.3060 0.3423
REMARK   3    30  2.0254 -  2.0000    0.86     2369   124  0.3177 0.3599
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL
REMARK   3   SOLVENT RADIUS     : 1.30
REMARK   3   SHRINKAGE RADIUS   : 1.06
REMARK   3   K_SOL              : 0.31
REMARK   3   B_SOL              : 48.25
REMARK   3
REMARK   3  ERROR ESTIMATES.
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.280
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : NULL
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 37.17
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 59.20
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : -1.02830
REMARK   3    B22 (A**2) : -2.21840
REMARK   3    B33 (A**2) : 3.24670
REMARK   3    B12 (A**2) : -2.26710
REMARK   3    B13 (A**2) : 5.57960
REMARK   3    B23 (A**2) : -16.28000
REMARK   3
REMARK   3  TWINNING INFORMATION.
REMARK   3   FRACTION: NULL
REMARK   3   OPERATOR: NULL
REMARK   3
REMARK   3  DEVIATIONS FROM IDEAL VALUES.
REMARK   3                 RMSD          COUNT
REMARK   3   BOND      :  0.010           9789
REMARK   3   ANGLE     :  1.284          13253
REMARK   3   CHIRALITY :  0.085           1511
REMARK   3   PLANARITY :  0.007           1677
REMARK   3   DIHEDRAL  : 16.867           3781
REMARK   3
REMARK   3  TLS DETAILS
REMARK   3   NUMBER OF TLS GROUPS  : 4
REMARK   3   TLS GROUP : 1
REMARK   3    SELECTION: CHAIN A
REMARK   3    ORIGIN FOR THE GROUP (A):  85.5771  74.3076  -4.7055
REMARK   3    T TENSOR
REMARK   3      T11:   0.3555 T22:   0.2563
REMARK   3      T33:   0.2836 T12:  -0.0067
REMARK   3      T13:   0.0193 T23:   0.0240
REMARK   3    L TENSOR
REMARK   3      L11:   0.8700 L22:   0.9611
REMARK   3      L33:   0.8950 L12:  -0.3988
REMARK   3      L13:  -0.4749 L23:   0.9726
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0092 S12:  -0.0262 S13:  -0.1838
REMARK   3      S21:   0.1956 S22:  -0.0200 S23:   0.1142
REMARK   3      S31:   0.1036 S32:   0.0133 S33:   0.0329
REMARK   3   TLS GROUP : 2
REMARK   3    SELECTION: CHAIN B
REMARK   3    ORIGIN FOR THE GROUP (A):  86.6655  96.9733  15.8858
REMARK   3    T TENSOR
REMARK   3      T11:   0.4671 T22:   0.3404
REMARK   3      T33:   0.2364 T12:  -0.0616
REMARK   3      T13:   0.0500 T23:  -0.0276
REMARK   3    L TENSOR
REMARK   3      L11:   1.0150 L22:   1.2412
REMARK   3      L33:   0.9114 L12:   0.0778
REMARK   3      L13:  -0.3054 L23:   1.2894
REMARK   3    S TENSOR
REMARK   3      S11:   0.1650 S12:  -0.2085 S13:   0.1591
REMARK   3      S21:   0.2689 S22:   0.0213 S23:   0.0727
REMARK   3      S31:  -0.1401 S32:   0.2373 S33:  -0.0415
REMARK   3   TLS GROUP : 3
REMARK   3    SELECTION: CHAIN C
REMARK   3    ORIGIN FOR THE GROUP (A):  46.0478  46.3889  43.2259
REMARK   3    T TENSOR
REMARK   3      T11:   0.2909 T22:   0.2646
REMARK   3      T33:   0.2957 T12:  -0.0394
REMARK   3      T13:   0.0364 T23:  -0.0337
REMARK   3    L TENSOR
REMARK   3      L11:   0.9525 L22:   0.9693
REMARK   3      L33:   2.0302 L12:   0.2950
REMARK   3      L13:   0.1611 L23:   0.9306
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0773 S12:   0.2627 S13:  -0.1927
REMARK   3      S21:  -0.0792 S22:   0.1580 S23:  -0.2333
REMARK   3      S31:   0.1446 S32:  -0.0480 S33:  -0.0382
REMARK   3   TLS GROUP : 4
REMARK   3    SELECTION: CHAIN D
REMARK   3    ORIGIN FOR THE GROUP (A):  57.3223  71.6588  55.5291
REMARK   3    T TENSOR
REMARK   3      T11:   0.1148 T22:   0.2415
REMARK   3      T33:   0.3796 T12:   0.0428
REMARK   3      T13:  -0.0408 T23:  -0.0586
REMARK   3    L TENSOR
REMARK   3      L11:   0.5574 L22:   1.4651
REMARK   3      L33:   1.3731 L12:   0.4179
REMARK   3      L13:   0.1194 L23:   0.7553
REMARK   3    S TENSOR
REMARK   3      S11:   0.0339 S12:   0.0695 S13:   0.2355
REMARK   3      S21:   0.0591 S22:   0.1062 S23:  -0.2309
REMARK   3      S31:   0.0628 S32:   0.0211 S33:  -0.0229
REMARK   3
REMARK   3  NCS DETAILS
REMARK   3   NUMBER OF NCS GROUPS : NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 3R5X COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-MAR-11.
REMARK 100 THE RCSB ID CODE IS RCSB064529.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 04-JUN-10
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 6.5
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : APS
REMARK 200  BEAMLINE                       : 19-ID
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97934
REMARK 200  MONOCHROMATOR                  : SI(111)
REMARK 200  OPTICS                         : MIRRORS
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-3000
REMARK 200  DATA SCALING SOFTWARE          : HKL-3000
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 84177
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.2
REMARK 200  DATA REDUNDANCY                : 2.100
REMARK 200  R MERGE                    (I) : NULL
REMARK 200  R SYM                      (I) : 0.08700
REMARK 200   FOR THE DATA SET  : 12.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.03
REMARK 200  COMPLETENESS FOR SHELL     (%) : 93.3
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.00
REMARK 200  R MERGE FOR SHELL          (I) : NULL
REMARK 200  R SYM FOR SHELL            (I) : 0.40800
REMARK 200   FOR SHELL         : 1.840
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SAD
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: HKL3000, SHELXS,MLPHARE,BUCCANEER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 48.55
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.39
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M BIS-TRIS PH 6.5, 20 % W/V
REMARK 280  POLYETHYLENE GLYCOL MONOMETHYL ETHER 5000, VAPOR DIFFUSION,
REMARK 280  SITTING DROP, TEMPERATURE 289K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,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
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3
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: 4130 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 26890 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -56.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
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: 4300 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 26280 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -61.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 11020 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 50580 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -138.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350   BIOMT1   2  1.000000  0.000000  0.000000      -48.21969
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000       25.22597
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000       88.50499
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     SER A   139
REMARK 465     GLY A   140
REMARK 465     GLY A   141
REMARK 465     SER A   142
REMARK 465     PHE A   304
REMARK 465     SER B    -2
REMARK 465     ASN B    -1
REMARK 465     GLY B   141
REMARK 465     SER B   142
REMARK 465     SER B   143
REMARK 465     VAL B   144
REMARK 465     ASP B   203
REMARK 465     TYR B   204
REMARK 465     ASN B   205
REMARK 465     ALA B   206
REMARK 465     LYS B   207
REMARK 465     TYR B   208
REMARK 465     ASP B   209
REMARK 465     ASP B   210
REMARK 465     ALA B   211
REMARK 465     PHE B   304
REMARK 465     SER C    -2
REMARK 465     ASN C    -1
REMARK 465     SER C   139
REMARK 465     GLY C   140
REMARK 465     GLY C   141
REMARK 465     SER C   142
REMARK 465     SER C   143
REMARK 465     VAL C   144
REMARK 465     ALA C   198
REMARK 465     ALA C   199
REMARK 465     GLU C   200
REMARK 465     PHE C   201
REMARK 465     PHE C   202
REMARK 465     ASP C   203
REMARK 465     TYR C   204
REMARK 465     ASN C   205
REMARK 465     ALA C   206
REMARK 465     LYS C   207
REMARK 465     TYR C   208
REMARK 465     ASP C   209
REMARK 465     ASP C   210
REMARK 465     ALA C   211
REMARK 465     SER C   212
REMARK 465     SER D    -2
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   O1G  ATP A   311     O    HOH A   646              2.17
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    CYS C 241   CB    CYS C 241   SG     -0.113
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    SER A  11     -136.59     50.07
REMARK 500    ASP A 203     -124.63     45.42
REMARK 500    VAL A 243      -61.79     73.88
REMARK 500    SER B  11     -137.76     55.82
REMARK 500    VAL B 243      -62.11     73.17
REMARK 500    SER C  11     -130.96     46.58
REMARK 500    VAL C 243      -59.15     70.00
REMARK 500    SER D  11     -131.18     47.49
REMARK 500    VAL D 243      -61.63     73.53
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 A 334        DISTANCE =  5.70 ANGSTROMS
REMARK 525    HOH A 336        DISTANCE =  7.54 ANGSTROMS
REMARK 525    HOH A 357        DISTANCE =  5.27 ANGSTROMS
REMARK 525    HOH C 347        DISTANCE =  5.34 ANGSTROMS
REMARK 525    HOH C 349        DISTANCE =  5.39 ANGSTROMS
REMARK 525    HOH D 307        DISTANCE =  5.31 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 310  CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ATP A 311   O2B
REMARK 620 2 GLU A 260   OE2  72.1
REMARK 620 3 ATP A 311   O2A  74.0  90.5
REMARK 620 4 ASP A 248   OD2 162.0  94.1 118.8
REMARK 620 5 HOH A 689   O    71.7  50.2 134.0  90.6
REMARK 620 N                    1     2     3     4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MG C 313  MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ARG C 299   O
REMARK 620 2 GLU C 302   O    82.7
REMARK 620 3 HOH C 667   O    92.7  69.8
REMARK 620 4 HOH C 668   O    72.3  92.3 158.3
REMARK 620 5 HOH C 669   O   138.5 132.2 118.0  83.0
REMARK 620 N                    1     2     3     4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              CA D 310  CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ATP D 311   O3A
REMARK 620 2 ASP D 248   OD2 166.1
REMARK 620 3 HOH D 528   O    83.7  99.7
REMARK 620 4 GLU D 260   OE2  86.3  80.2  90.6
REMARK 620 5 ATP D 311   O3B  57.7 109.9 121.8  49.5
REMARK 620 N                    1     2     3     4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              CA B 310  CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU B 260   OE2
REMARK 620 2 ASP B 248   OD2  87.4
REMARK 620 N                    1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              CA D 312  CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH D 542   O
REMARK 620 2 TYR D 208   O    82.4
REMARK 620 3 GLU D 200   OE1  87.0 127.3
REMARK 620 4 ASP D 203   OD2 170.2  89.4  93.9
REMARK 620 5 GLU D 200   OE2  82.3  77.2  50.3  90.8
REMARK 620 6 HOH D 543   O    84.5  71.8 157.7  97.9 147.6
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              CA C 312  CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU C 108   OE1
REMARK 620 2 GLU C 108   OE2  51.0
REMARK 620 3 HOH C 642   O    88.2  91.8
REMARK 620 N                    1     2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              CA C 310  CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP C 248   OD2
REMARK 620 2 HOH C 536   O    67.6
REMARK 620 3 GLU C 260   OE1  98.2 117.2
REMARK 620 4 ATP C 311   O1A 102.1  47.1  81.8
REMARK 620 5 ATP C 311   O2B 158.3  94.4  78.8  56.2
REMARK 620 N                    1     2     3     4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              CA B 312  CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLY B 281   O
REMARK 620 2 HOH B 626   O    78.9
REMARK 620 3 HOH B 628   O    74.4 102.2
REMARK 620 4 HOH B 627   O   133.6  77.4 149.8
REMARK 620 5 HOH B 630   O   145.0  77.1  86.3  64.0
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 A 310
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ATP A 311
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 310
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ATP B 311
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 312
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA C 310
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ATP C 311
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA C 312
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG C 313
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA D 310
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ATP D 311
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA D 312
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D 313
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACY D 314
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3R23   RELATED DB: PDB
REMARK 900 THE SAME PROTEIN APO-FORM
REMARK 900 RELATED ID: IDP01207   RELATED DB: TARGETDB
DBREF  3R5X A  313   304  UNP    Q81Q29   DDL_BACAN        1    304
DBREF  3R5X B    1   304  UNP    Q81Q29   DDL_BACAN        1    304
DBREF  3R5X C    1   304  UNP    Q81Q29   DDL_BACAN        1    304
DBREF  3R5X D    1   304  UNP    Q81Q29   DDL_BACAN        1    304
SEQADV 3R5X SER A   -2  UNP  Q81Q29              EXPRESSION TAG
SEQADV 3R5X ASN A   -1  UNP  Q81Q29              EXPRESSION TAG
SEQADV 3R5X ALA A    0  UNP  Q81Q29              EXPRESSION TAG
SEQADV 3R5X SER B   -2  UNP  Q81Q29              EXPRESSION TAG
SEQADV 3R5X ASN B   -1  UNP  Q81Q29              EXPRESSION TAG
SEQADV 3R5X ALA B    0  UNP  Q81Q29              EXPRESSION TAG
SEQADV 3R5X SER C   -2  UNP  Q81Q29              EXPRESSION TAG
SEQADV 3R5X ASN C   -1  UNP  Q81Q29              EXPRESSION TAG
SEQADV 3R5X ALA C    0  UNP  Q81Q29              EXPRESSION TAG
SEQADV 3R5X SER D   -2  UNP  Q81Q29              EXPRESSION TAG
SEQADV 3R5X ASN D   -1  UNP  Q81Q29              EXPRESSION TAG
SEQADV 3R5X ALA D    0  UNP  Q81Q29              EXPRESSION TAG
SEQRES   1 A  307  SER ASN ALA MSE ARG ILE GLY VAL ILE MSE GLY GLY VAL
SEQRES   2 A  307  SER SER GLU LYS GLN VAL SER ILE MSE THR GLY ASN GLU
SEQRES   3 A  307  MSE ILE ALA ASN LEU ASP LYS ASN LYS TYR GLU ILE VAL
SEQRES   4 A  307  PRO ILE THR LEU ASN GLU LYS MSE ASP LEU ILE GLU LYS
SEQRES   5 A  307  ALA LYS ASP ILE ASP PHE ALA LEU LEU ALA LEU HIS GLY
SEQRES   6 A  307  LYS TYR GLY GLU ASP GLY THR VAL GLN GLY THR LEU GLU
SEQRES   7 A  307  SER LEU GLY ILE PRO TYR SER GLY SER ASN MSE LEU SER
SEQRES   8 A  307  SER GLY ILE CYS MSE ASP LYS ASN ILE SER LYS LYS ILE
SEQRES   9 A  307  LEU ARG TYR GLU GLY ILE GLU THR PRO ASP TRP ILE GLU
SEQRES  10 A  307  LEU THR LYS MSE GLU ASP LEU ASN PHE ASP GLU LEU ASP
SEQRES  11 A  307  LYS LEU GLY PHE PRO LEU VAL VAL LYS PRO ASN SER GLY
SEQRES  12 A  307  GLY SER SER VAL GLY VAL LYS ILE VAL TYR ASP LYS ASP
SEQRES  13 A  307  GLU LEU ILE SER MSE LEU GLU THR VAL PHE GLU TRP ASP
SEQRES  14 A  307  SER GLU VAL VAL ILE GLU LYS TYR ILE LYS GLY GLU GLU
SEQRES  15 A  307  ILE THR CYS SER ILE PHE ASP GLY LYS GLN LEU PRO ILE
SEQRES  16 A  307  ILE SER ILE ARG HIS ALA ALA GLU PHE PHE ASP TYR ASN
SEQRES  17 A  307  ALA LYS TYR ASP ASP ALA SER THR ILE GLU GLU VAL ILE
SEQRES  18 A  307  GLU LEU PRO ALA GLU LEU LYS GLU ARG VAL ASN LYS ALA
SEQRES  19 A  307  SER LEU ALA CYS TYR LYS ALA LEU LYS CYS SER VAL TYR
SEQRES  20 A  307  ALA ARG VAL ASP MSE MSE VAL LYS ASP GLY ILE PRO TYR
SEQRES  21 A  307  VAL MSE GLU VAL ASN THR LEU PRO GLY MSE THR GLN ALA
SEQRES  22 A  307  SER LEU LEU PRO LYS SER ALA ASP ALA ALA GLY ILE HIS
SEQRES  23 A  307  TYR SER LYS LEU LEU ASP MSE ILE ILE GLU THR SER LEU
SEQRES  24 A  307  ARG VAL ARG LYS GLU GLU GLY PHE
SEQRES   1 B  307  SER ASN ALA MSE ARG ILE GLY VAL ILE MSE GLY GLY VAL
SEQRES   2 B  307  SER SER GLU LYS GLN VAL SER ILE MSE THR GLY ASN GLU
SEQRES   3 B  307  MSE ILE ALA ASN LEU ASP LYS ASN LYS TYR GLU ILE VAL
SEQRES   4 B  307  PRO ILE THR LEU ASN GLU LYS MSE ASP LEU ILE GLU LYS
SEQRES   5 B  307  ALA LYS ASP ILE ASP PHE ALA LEU LEU ALA LEU HIS GLY
SEQRES   6 B  307  LYS TYR GLY GLU ASP GLY THR VAL GLN GLY THR LEU GLU
SEQRES   7 B  307  SER LEU GLY ILE PRO TYR SER GLY SER ASN MSE LEU SER
SEQRES   8 B  307  SER GLY ILE CYS MSE ASP LYS ASN ILE SER LYS LYS ILE
SEQRES   9 B  307  LEU ARG TYR GLU GLY ILE GLU THR PRO ASP TRP ILE GLU
SEQRES  10 B  307  LEU THR LYS MSE GLU ASP LEU ASN PHE ASP GLU LEU ASP
SEQRES  11 B  307  LYS LEU GLY PHE PRO LEU VAL VAL LYS PRO ASN SER GLY
SEQRES  12 B  307  GLY SER SER VAL GLY VAL LYS ILE VAL TYR ASP LYS ASP
SEQRES  13 B  307  GLU LEU ILE SER MSE LEU GLU THR VAL PHE GLU TRP ASP
SEQRES  14 B  307  SER GLU VAL VAL ILE GLU LYS TYR ILE LYS GLY GLU GLU
SEQRES  15 B  307  ILE THR CYS SER ILE PHE ASP GLY LYS GLN LEU PRO ILE
SEQRES  16 B  307  ILE SER ILE ARG HIS ALA ALA GLU PHE PHE ASP TYR ASN
SEQRES  17 B  307  ALA LYS TYR ASP ASP ALA SER THR ILE GLU GLU VAL ILE
SEQRES  18 B  307  GLU LEU PRO ALA GLU LEU LYS GLU ARG VAL ASN LYS ALA
SEQRES  19 B  307  SER LEU ALA CYS TYR LYS ALA LEU LYS CYS SER VAL TYR
SEQRES  20 B  307  ALA ARG VAL ASP MSE MSE VAL LYS ASP GLY ILE PRO TYR
SEQRES  21 B  307  VAL MSE GLU VAL ASN THR LEU PRO GLY MSE THR GLN ALA
SEQRES  22 B  307  SER LEU LEU PRO LYS SER ALA ASP ALA ALA GLY ILE HIS
SEQRES  23 B  307  TYR SER LYS LEU LEU ASP MSE ILE ILE GLU THR SER LEU
SEQRES  24 B  307  ARG VAL ARG LYS GLU GLU GLY PHE
SEQRES   1 C  307  SER ASN ALA MSE ARG ILE GLY VAL ILE MSE GLY GLY VAL
SEQRES   2 C  307  SER SER GLU LYS GLN VAL SER ILE MSE THR GLY ASN GLU
SEQRES   3 C  307  MSE ILE ALA ASN LEU ASP LYS ASN LYS TYR GLU ILE VAL
SEQRES   4 C  307  PRO ILE THR LEU ASN GLU LYS MSE ASP LEU ILE GLU LYS
SEQRES   5 C  307  ALA LYS ASP ILE ASP PHE ALA LEU LEU ALA LEU HIS GLY
SEQRES   6 C  307  LYS TYR GLY GLU ASP GLY THR VAL GLN GLY THR LEU GLU
SEQRES   7 C  307  SER LEU GLY ILE PRO TYR SER GLY SER ASN MSE LEU SER
SEQRES   8 C  307  SER GLY ILE CYS MSE ASP LYS ASN ILE SER LYS LYS ILE
SEQRES   9 C  307  LEU ARG TYR GLU GLY ILE GLU THR PRO ASP TRP ILE GLU
SEQRES  10 C  307  LEU THR LYS MSE GLU ASP LEU ASN PHE ASP GLU LEU ASP
SEQRES  11 C  307  LYS LEU GLY PHE PRO LEU VAL VAL LYS PRO ASN SER GLY
SEQRES  12 C  307  GLY SER SER VAL GLY VAL LYS ILE VAL TYR ASP LYS ASP
SEQRES  13 C  307  GLU LEU ILE SER MSE LEU GLU THR VAL PHE GLU TRP ASP
SEQRES  14 C  307  SER GLU VAL VAL ILE GLU LYS TYR ILE LYS GLY GLU GLU
SEQRES  15 C  307  ILE THR CYS SER ILE PHE ASP GLY LYS GLN LEU PRO ILE
SEQRES  16 C  307  ILE SER ILE ARG HIS ALA ALA GLU PHE PHE ASP TYR ASN
SEQRES  17 C  307  ALA LYS TYR ASP ASP ALA SER THR ILE GLU GLU VAL ILE
SEQRES  18 C  307  GLU LEU PRO ALA GLU LEU LYS GLU ARG VAL ASN LYS ALA
SEQRES  19 C  307  SER LEU ALA CYS TYR LYS ALA LEU LYS CYS SER VAL TYR
SEQRES  20 C  307  ALA ARG VAL ASP MSE MSE VAL LYS ASP GLY ILE PRO TYR
SEQRES  21 C  307  VAL MSE GLU VAL ASN THR LEU PRO GLY MSE THR GLN ALA
SEQRES  22 C  307  SER LEU LEU PRO LYS SER ALA ASP ALA ALA GLY ILE HIS
SEQRES  23 C  307  TYR SER LYS LEU LEU ASP MSE ILE ILE GLU THR SER LEU
SEQRES  24 C  307  ARG VAL ARG LYS GLU GLU GLY PHE
SEQRES   1 D  307  SER ASN ALA MSE ARG ILE GLY VAL ILE MSE GLY GLY VAL
SEQRES   2 D  307  SER SER GLU LYS GLN VAL SER ILE MSE THR GLY ASN GLU
SEQRES   3 D  307  MSE ILE ALA ASN LEU ASP LYS ASN LYS TYR GLU ILE VAL
SEQRES   4 D  307  PRO ILE THR LEU ASN GLU LYS MSE ASP LEU ILE GLU LYS
SEQRES   5 D  307  ALA LYS ASP ILE ASP PHE ALA LEU LEU ALA LEU HIS GLY
SEQRES   6 D  307  LYS TYR GLY GLU ASP GLY THR VAL GLN GLY THR LEU GLU
SEQRES   7 D  307  SER LEU GLY ILE PRO TYR SER GLY SER ASN MSE LEU SER
SEQRES   8 D  307  SER GLY ILE CYS MSE ASP LYS ASN ILE SER LYS LYS ILE
SEQRES   9 D  307  LEU ARG TYR GLU GLY ILE GLU THR PRO ASP TRP ILE GLU
SEQRES  10 D  307  LEU THR LYS MSE GLU ASP LEU ASN PHE ASP GLU LEU ASP
SEQRES  11 D  307  LYS LEU GLY PHE PRO LEU VAL VAL LYS PRO ASN SER GLY
SEQRES  12 D  307  GLY SER SER VAL GLY VAL LYS ILE VAL TYR ASP LYS ASP
SEQRES  13 D  307  GLU LEU ILE SER MSE LEU GLU THR VAL PHE GLU TRP ASP
SEQRES  14 D  307  SER GLU VAL VAL ILE GLU LYS TYR ILE LYS GLY GLU GLU
SEQRES  15 D  307  ILE THR CYS SER ILE PHE ASP GLY LYS GLN LEU PRO ILE
SEQRES  16 D  307  ILE SER ILE ARG HIS ALA ALA GLU PHE PHE ASP TYR ASN
SEQRES  17 D  307  ALA LYS TYR ASP ASP ALA SER THR ILE GLU GLU VAL ILE
SEQRES  18 D  307  GLU LEU PRO ALA GLU LEU LYS GLU ARG VAL ASN LYS ALA
SEQRES  19 D  307  SER LEU ALA CYS TYR LYS ALA LEU LYS CYS SER VAL TYR
SEQRES  20 D  307  ALA ARG VAL ASP MSE MSE VAL LYS ASP GLY ILE PRO TYR
SEQRES  21 D  307  VAL MSE GLU VAL ASN THR LEU PRO GLY MSE THR GLN ALA
SEQRES  22 D  307  SER LEU LEU PRO LYS SER ALA ASP ALA ALA GLY ILE HIS
SEQRES  23 D  307  TYR SER LYS LEU LEU ASP MSE ILE ILE GLU THR SER LEU
SEQRES  24 D  307  ARG VAL ARG LYS GLU GLU GLY PHE
MODRES 3R5X MSE A  313  MET  SELENOMETHIONINE
MODRES 3R5X MSE A    7  MET  SELENOMETHIONINE
MODRES 3R5X MSE A   19  MET  SELENOMETHIONINE
MODRES 3R5X MSE A   24  MET  SELENOMETHIONINE
MODRES 3R5X MSE A   44  MET  SELENOMETHIONINE
MODRES 3R5X MSE A   86  MET  SELENOMETHIONINE
MODRES 3R5X MSE A   93  MET  SELENOMETHIONINE
MODRES 3R5X MSE A  118  MET  SELENOMETHIONINE
MODRES 3R5X MSE A  158  MET  SELENOMETHIONINE
MODRES 3R5X MSE A  249  MET  SELENOMETHIONINE
MODRES 3R5X MSE A  250  MET  SELENOMETHIONINE
MODRES 3R5X MSE A  259  MET  SELENOMETHIONINE
MODRES 3R5X MSE A  267  MET  SELENOMETHIONINE
MODRES 3R5X MSE A  290  MET  SELENOMETHIONINE
MODRES 3R5X MSE B    1  MET  SELENOMETHIONINE
MODRES 3R5X MSE B    7  MET  SELENOMETHIONINE
MODRES 3R5X MSE B   19  MET  SELENOMETHIONINE
MODRES 3R5X MSE B   24  MET  SELENOMETHIONINE
MODRES 3R5X MSE B   44  MET  SELENOMETHIONINE
MODRES 3R5X MSE B   86  MET  SELENOMETHIONINE
MODRES 3R5X MSE B   93  MET  SELENOMETHIONINE
MODRES 3R5X MSE B  118  MET  SELENOMETHIONINE
MODRES 3R5X MSE B  158  MET  SELENOMETHIONINE
MODRES 3R5X MSE B  249  MET  SELENOMETHIONINE
MODRES 3R5X MSE B  250  MET  SELENOMETHIONINE
MODRES 3R5X MSE B  259  MET  SELENOMETHIONINE
MODRES 3R5X MSE B  267  MET  SELENOMETHIONINE
MODRES 3R5X MSE B  290  MET  SELENOMETHIONINE
MODRES 3R5X MSE C    1  MET  SELENOMETHIONINE
MODRES 3R5X MSE C    7  MET  SELENOMETHIONINE
MODRES 3R5X MSE C   19  MET  SELENOMETHIONINE
MODRES 3R5X MSE C   24  MET  SELENOMETHIONINE
MODRES 3R5X MSE C   44  MET  SELENOMETHIONINE
MODRES 3R5X MSE C   86  MET  SELENOMETHIONINE
MODRES 3R5X MSE C   93  MET  SELENOMETHIONINE
MODRES 3R5X MSE C  118  MET  SELENOMETHIONINE
MODRES 3R5X MSE C  158  MET  SELENOMETHIONINE
MODRES 3R5X MSE C  249  MET  SELENOMETHIONINE
MODRES 3R5X MSE C  250  MET  SELENOMETHIONINE
MODRES 3R5X MSE C  259  MET  SELENOMETHIONINE
MODRES 3R5X MSE C  267  MET  SELENOMETHIONINE
MODRES 3R5X MSE C  290  MET  SELENOMETHIONINE
MODRES 3R5X MSE D    1  MET  SELENOMETHIONINE
MODRES 3R5X MSE D    7  MET  SELENOMETHIONINE
MODRES 3R5X MSE D   19  MET  SELENOMETHIONINE
MODRES 3R5X MSE D   24  MET  SELENOMETHIONINE
MODRES 3R5X MSE D   44  MET  SELENOMETHIONINE
MODRES 3R5X MSE D   86  MET  SELENOMETHIONINE
MODRES 3R5X MSE D   93  MET  SELENOMETHIONINE
MODRES 3R5X MSE D  118  MET  SELENOMETHIONINE
MODRES 3R5X MSE D  158  MET  SELENOMETHIONINE
MODRES 3R5X MSE D  249  MET  SELENOMETHIONINE
MODRES 3R5X MSE D  250  MET  SELENOMETHIONINE
MODRES 3R5X MSE D  259  MET  SELENOMETHIONINE
MODRES 3R5X MSE D  267  MET  SELENOMETHIONINE
MODRES 3R5X MSE D  290  MET  SELENOMETHIONINE
HET    MSE  A 313       8
HET    MSE  A   7       8
HET    MSE  A  19       8
HET    MSE  A  24       8
HET    MSE  A  44       8
HET    MSE  A  86       8
HET    MSE  A  93       8
HET    MSE  A 118       8
HET    MSE  A 158       8
HET    MSE  A 249       8
HET    MSE  A 250       8
HET    MSE  A 259      16
HET    MSE  A 267       8
HET    MSE  A 290       8
HET    MSE  B   1       8
HET    MSE  B   7       8
HET    MSE  B  19       8
HET    MSE  B  24       8
HET    MSE  B  44       8
HET    MSE  B  86       8
HET    MSE  B  93       8
HET    MSE  B 118       8
HET    MSE  B 158       8
HET    MSE  B 249       8
HET    MSE  B 250       8
HET    MSE  B 259      16
HET    MSE  B 267       8
HET    MSE  B 290       8
HET    MSE  C   1       8
HET    MSE  C   7       8
HET    MSE  C  19       8
HET    MSE  C  24       8
HET    MSE  C  44       8
HET    MSE  C  86      16
HET    MSE  C  93       8
HET    MSE  C 118       8
HET    MSE  C 158       8
HET    MSE  C 249       8
HET    MSE  C 250       8
HET    MSE  C 259      16
HET    MSE  C 267       8
HET    MSE  C 290       8
HET    MSE  D   1       8
HET    MSE  D   7       8
HET    MSE  D  19      16
HET    MSE  D  24       8
HET    MSE  D  44       8
HET    MSE  D  86      16
HET    MSE  D  93       8
HET    MSE  D 118       8
HET    MSE  D 158      16
HET    MSE  D 249       8
HET    MSE  D 250      16
HET    MSE  D 259       8
HET    MSE  D 267       8
HET    MSE  D 290       8
HET     CA  A 310       1
HET    ATP  A 311      31
HET     CA  B 310       1
HET    ATP  B 311      31
HET     CA  B 312       1
HET     CA  C 310       1
HET    ATP  C 311      31
HET     CA  C 312       1
HET     MG  C 313       1
HET     CA  D 310       1
HET    ATP  D 311      31
HET     CA  D 312       1
HET    EDO  D 313       4
HET    ACY  D 314       4
HETNAM     MSE SELENOMETHIONINE
HETNAM      CA CALCIUM ION
HETNAM     ATP ADENOSINE-5'-TRIPHOSPHATE
HETNAM      MG MAGNESIUM ION
HETNAM     EDO 1,2-ETHANEDIOL
HETNAM     ACY ACETIC ACID
HETSYN     EDO ETHYLENE GLYCOL
FORMUL   1  MSE    56(C5 H11 N O2 SE)
FORMUL   5   CA    7(CA 2+)
FORMUL   6  ATP    4(C10 H16 N5 O13 P3)
FORMUL  13   MG    MG 2+
FORMUL  17  EDO    C2 H6 O2
FORMUL  18  ACY    C2 H4 O2
FORMUL  19  HOH   *750(H2 O)
HELIX    1   1 VAL A   10  LEU A   28  1                                  19
HELIX    2   2 GLU A   42  MSE A   44  5                                   3
HELIX    3   3 ASP A   45  ALA A   50  1                                   6
HELIX    4   4 GLY A   62  ASP A   67  1                                   6
HELIX    5   5 GLY A   68  GLY A   78  1                                  11
HELIX    6   6 ASN A   85  ASP A   94  1                                  10
HELIX    7   7 ASP A   94  GLU A  105  1                                  12
HELIX    8   8 ASN A  122  GLY A  130  1                                   9
HELIX    9   9 ASP A  151  ASP A  166  1                                  16
HELIX   10  10 PRO A  221  LEU A  239  1                                  19
HELIX   11  11 SER A  271  ALA A  280  1                                  10
HELIX   12  12 HIS A  283  GLY A  303  1                                  21
HELIX   13  13 VAL B   10  LEU B   28  1                                  19
HELIX   14  14 GLU B   42  MSE B   44  5                                   3
HELIX   15  15 ASP B   45  ALA B   50  1                                   6
HELIX   16  16 LYS B   51  ILE B   53  5                                   3
HELIX   17  17 GLY B   62  ASP B   67  1                                   6
HELIX   18  18 GLY B   68  LEU B   77  1                                  10
HELIX   19  19 ASN B   85  ASP B   94  1                                  10
HELIX   20  20 ASP B   94  GLU B  105  1                                  12
HELIX   21  21 ASN B  122  GLY B  130  1                                   9
HELIX   22  22 ASP B  151  ASP B  166  1                                  16
HELIX   23  23 PRO B  221  LEU B  239  1                                  19
HELIX   24  24 SER B  271  ALA B  280  1                                  10
HELIX   25  25 HIS B  283  GLY B  303  1                                  21
HELIX   26  26 VAL C   10  LEU C   28  1                                  19
HELIX   27  27 GLU C   42  MSE C   44  5                                   3
HELIX   28  28 ASP C   45  ALA C   50  1                                   6
HELIX   29  29 LYS C   51  ILE C   53  5                                   3
HELIX   30  30 GLY C   62  ASP C   67  1                                   6
HELIX   31  31 GLY C   68  LEU C   77  1                                  10
HELIX   32  32 ASN C   85  ASP C   94  1                                  10
HELIX   33  33 ASP C   94  GLU C  105  1                                  12
HELIX   34  34 ASN C  122  GLY C  130  1                                   9
HELIX   35  35 ASP C  151  ASP C  166  1                                  16
HELIX   36  36 PRO C  221  LEU C  239  1                                  19
HELIX   37  37 SER C  271  ALA C  280  1                                  10
HELIX   38  38 HIS C  283  GLU C  302  1                                  20
HELIX   39  39 VAL D   10  LEU D   28  1                                  19
HELIX   40  40 GLU D   42  MSE D   44  5                                   3
HELIX   41  41 ASP D   45  ALA D   50  1                                   6
HELIX   42  42 GLY D   62  ASP D   67  1                                   6
HELIX   43  43 GLY D   68  LEU D   77  1                                  10
HELIX   44  44 ASN D   85  ASP D   94  1                                  10
HELIX   45  45 ASP D   94  GLU D  105  1                                  12
HELIX   46  46 ASN D  122  GLY D  130  1                                   9
HELIX   47  47 ASP D  151  ASP D  166  1                                  16
HELIX   48  48 ALA D  198  PHE D  202  5                                   5
HELIX   49  49 PRO D  221  LEU D  239  1                                  19
HELIX   50  50 SER D  271  ALA D  280  1                                  10
HELIX   51  51 HIS D  283  GLU D  302  1                                  20
SHEET    1   A 3 TYR A  33  THR A  39  0
SHEET    2   A 3 MSE A 313  MSE A   7  1  N  MSE A   7   O  ILE A  38
SHEET    3   A 3 PHE A  55  LEU A  58  1  O  PHE A  55   N  GLY A   4
SHEET    1   B 4 TRP A 112  THR A 116  0
SHEET    2   B 4 GLU A 168  LYS A 173 -1  O  ILE A 171   N  ILE A 113
SHEET    3   B 4 LEU A 133  PRO A 137 -1  N  LYS A 136   O  VAL A 170
SHEET    4   B 4 LYS A 147  VAL A 149 -1  O  LYS A 147   N  VAL A 135
SHEET    1   C 4 LYS A 188  GLN A 189  0
SHEET    2   C 4 GLU A 178  PHE A 185 -1  N  PHE A 185   O  LYS A 188
SHEET    3   C 4 ILE A 193  PHE A 202 -1  O  ILE A 195   N  GLU A 179
SHEET    4   C 4 ASN A 205  VAL A 217 -1  O  ILE A 214   N  ARG A 196
SHEET    1   D 4 LYS A 188  GLN A 189  0
SHEET    2   D 4 GLU A 178  PHE A 185 -1  N  PHE A 185   O  LYS A 188
SHEET    3   D 4 TYR A 244  LYS A 252 -1  O  VAL A 251   N  GLU A 178
SHEET    4   D 4 ILE A 255  ASN A 262 -1  O  ASN A 262   N  ARG A 246
SHEET    1   E 3 TYR B  33  THR B  39  0
SHEET    2   E 3 MSE B   1  MSE B   7  1  N  ILE B   3   O  VAL B  36
SHEET    3   E 3 PHE B  55  LEU B  58  1  O  LEU B  57   N  GLY B   4
SHEET    1   F 4 TRP B 112  THR B 116  0
SHEET    2   F 4 GLU B 168  LYS B 173 -1  O  VAL B 169   N  LEU B 115
SHEET    3   F 4 LEU B 133  PRO B 137 -1  N  VAL B 134   O  GLU B 172
SHEET    4   F 4 ILE B 148  VAL B 149 -1  O  VAL B 149   N  LEU B 133
SHEET    1   G 4 LYS B 188  GLN B 189  0
SHEET    2   G 4 GLU B 178  PHE B 185 -1  N  PHE B 185   O  LYS B 188
SHEET    3   G 4 ILE B 193  HIS B 197 -1  O  ILE B 195   N  GLU B 179
SHEET    4   G 4 THR B 213  VAL B 217 -1  O  GLU B 216   N  SER B 194
SHEET    1   H 4 LYS B 188  GLN B 189  0
SHEET    2   H 4 GLU B 178  PHE B 185 -1  N  PHE B 185   O  LYS B 188
SHEET    3   H 4 TYR B 244  LYS B 252 -1  O  VAL B 247   N  CYS B 182
SHEET    4   H 4 ILE B 255  ASN B 262 -1  O  ASN B 262   N  ARG B 246
SHEET    1   I 3 TYR C  33  LEU C  40  0
SHEET    2   I 3 MSE C   1  GLY C   8  1  N  MSE C   7   O  ILE C  38
SHEET    3   I 3 PHE C  55  LEU C  58  1  O  LEU C  57   N  GLY C   4
SHEET    1   J 4 TRP C 112  THR C 116  0
SHEET    2   J 4 GLU C 168  LYS C 173 -1  O  ILE C 171   N  ILE C 113
SHEET    3   J 4 LEU C 133  PRO C 137 -1  N  LYS C 136   O  VAL C 170
SHEET    4   J 4 LYS C 147  VAL C 149 -1  O  VAL C 149   N  LEU C 133
SHEET    1   K 4 LYS C 188  GLN C 189  0
SHEET    2   K 4 GLU C 178  PHE C 185 -1  N  PHE C 185   O  LYS C 188
SHEET    3   K 4 ILE C 193  ARG C 196 -1  O  ILE C 195   N  GLU C 179
SHEET    4   K 4 ILE C 214  VAL C 217 -1  O  GLU C 216   N  SER C 194
SHEET    1   L 4 LYS C 188  GLN C 189  0
SHEET    2   L 4 GLU C 178  PHE C 185 -1  N  PHE C 185   O  LYS C 188
SHEET    3   L 4 TYR C 244  LYS C 252 -1  O  ALA C 245   N  ILE C 184
SHEET    4   L 4 ILE C 255  ASN C 262 -1  O  ASN C 262   N  ARG C 246
SHEET    1   M 3 TYR D  33  LEU D  40  0
SHEET    2   M 3 MSE D   1  GLY D   8  1  N  MSE D   7   O  LEU D  40
SHEET    3   M 3 PHE D  55  LEU D  58  1  O  LEU D  57   N  GLY D   4
SHEET    1   N 4 TRP D 112  THR D 116  0
SHEET    2   N 4 GLU D 168  LYS D 173 -1  O  VAL D 169   N  LEU D 115
SHEET    3   N 4 LEU D 133  PRO D 137 -1  N  LYS D 136   O  VAL D 170
SHEET    4   N 4 LYS D 147  VAL D 149 -1  O  VAL D 149   N  LEU D 133
SHEET    1   O 4 LYS D 188  GLN D 189  0
SHEET    2   O 4 GLU D 178  PHE D 185 -1  N  PHE D 185   O  LYS D 188
SHEET    3   O 4 ILE D 193  ARG D 196 -1  O  ILE D 193   N  THR D 181
SHEET    4   O 4 ILE D 214  VAL D 217 -1  O  GLU D 216   N  SER D 194
SHEET    1   P 4 LYS D 188  GLN D 189  0
SHEET    2   P 4 GLU D 178  PHE D 185 -1  N  PHE D 185   O  LYS D 188
SHEET    3   P 4 TYR D 244  LYS D 252 -1  O  VAL D 247   N  CYS D 182
SHEET    4   P 4 ILE D 255  ASN D 262 -1  O  ASN D 262   N  ARG D 246
LINK         C   ALA A   0                 N   MSE A 313     1555   1555  1.33
LINK         C   MSE A 313                 N   ARG A   2     1555   1555  1.33
LINK         C   ILE A   6                 N   MSE A   7     1555   1555  1.33
LINK         C   MSE A   7                 N   GLY A   8     1555   1555  1.33
LINK         C   ILE A  18                 N   MSE A  19     1555   1555  1.33
LINK         C   MSE A  19                 N   THR A  20     1555   1555  1.33
LINK         C   GLU A  23                 N   MSE A  24     1555   1555  1.33
LINK         C   MSE A  24                 N   ILE A  25     1555   1555  1.32
LINK         C   LYS A  43                 N   MSE A  44     1555   1555  1.32
LINK         C   MSE A  44                 N   ASP A  45     1555   1555  1.34
LINK         C   ASN A  85                 N   MSE A  86     1555   1555  1.34
LINK         C   MSE A  86                 N   LEU A  87     1555   1555  1.33
LINK         C   CYS A  92                 N   MSE A  93     1555   1555  1.32
LINK         C   MSE A  93                 N   ASP A  94     1555   1555  1.32
LINK         C   LYS A 117                 N   MSE A 118     1555   1555  1.33
LINK         C   MSE A 118                 N   GLU A 119     1555   1555  1.32
LINK         C   SER A 157                 N   MSE A 158     1555   1555  1.33
LINK         C   MSE A 158                 N   LEU A 159     1555   1555  1.33
LINK         C   ASP A 248                 N   MSE A 249     1555   1555  1.34
LINK         C   MSE A 249                 N   MSE A 250     1555   1555  1.33
LINK         C   MSE A 250                 N   VAL A 251     1555   1555  1.34
LINK         C   VAL A 258                 N  AMSE A 259     1555   1555  1.33
LINK         C   VAL A 258                 N  BMSE A 259     1555   1555  1.33
LINK         C  AMSE A 259                 N   GLU A 260     1555   1555  1.33
LINK         C  BMSE A 259                 N   GLU A 260     1555   1555  1.33
LINK         C   GLY A 266                 N   MSE A 267     1555   1555  1.32
LINK         C   MSE A 267                 N   THR A 268     1555   1555  1.32
LINK         C   ASP A 289                 N   MSE A 290     1555   1555  1.33
LINK         C   MSE A 290                 N   ILE A 291     1555   1555  1.33
LINK         C   ALA B   0                 N   MSE B   1     1555   1555  1.33
LINK         C   MSE B   1                 N   ARG B   2     1555   1555  1.33
LINK         C   ILE B   6                 N   MSE B   7     1555   1555  1.32
LINK         C   MSE B   7                 N   GLY B   8     1555   1555  1.33
LINK         C   ILE B  18                 N   MSE B  19     1555   1555  1.33
LINK         C   MSE B  19                 N   THR B  20     1555   1555  1.33
LINK         C   GLU B  23                 N   MSE B  24     1555   1555  1.33
LINK         C   MSE B  24                 N   ILE B  25     1555   1555  1.33
LINK         C   LYS B  43                 N   MSE B  44     1555   1555  1.33
LINK         C   MSE B  44                 N   ASP B  45     1555   1555  1.33
LINK         C   ASN B  85                 N   MSE B  86     1555   1555  1.33
LINK         C   MSE B  86                 N   LEU B  87     1555   1555  1.33
LINK         C   CYS B  92                 N   MSE B  93     1555   1555  1.32
LINK         C   MSE B  93                 N   ASP B  94     1555   1555  1.33
LINK         C   LYS B 117                 N   MSE B 118     1555   1555  1.33
LINK         C   MSE B 118                 N   GLU B 119     1555   1555  1.33
LINK         C   SER B 157                 N   MSE B 158     1555   1555  1.33
LINK         C   MSE B 158                 N   LEU B 159     1555   1555  1.32
LINK         C   ASP B 248                 N   MSE B 249     1555   1555  1.33
LINK         C   MSE B 249                 N   MSE B 250     1555   1555  1.33
LINK         C   MSE B 250                 N   VAL B 251     1555   1555  1.33
LINK         C   VAL B 258                 N  AMSE B 259     1555   1555  1.33
LINK         C   VAL B 258                 N  BMSE B 259     1555   1555  1.33
LINK         C  AMSE B 259                 N   GLU B 260     1555   1555  1.33
LINK         C  BMSE B 259                 N   GLU B 260     1555   1555  1.33
LINK         C   GLY B 266                 N   MSE B 267     1555   1555  1.32
LINK         C   MSE B 267                 N   THR B 268     1555   1555  1.33
LINK         C   ASP B 289                 N   MSE B 290     1555   1555  1.34
LINK         C   MSE B 290                 N   ILE B 291     1555   1555  1.33
LINK         C   ALA C   0                 N   MSE C   1     1555   1555  1.33
LINK         C   MSE C   1                 N   ARG C   2     1555   1555  1.33
LINK         C   ILE C   6                 N   MSE C   7     1555   1555  1.32
LINK         C   MSE C   7                 N   GLY C   8     1555   1555  1.33
LINK         C   ILE C  18                 N   MSE C  19     1555   1555  1.33
LINK         C   MSE C  19                 N   THR C  20     1555   1555  1.33
LINK         C   GLU C  23                 N   MSE C  24     1555   1555  1.34
LINK         C   MSE C  24                 N   ILE C  25     1555   1555  1.32
LINK         C   LYS C  43                 N   MSE C  44     1555   1555  1.34
LINK         C   MSE C  44                 N   ASP C  45     1555   1555  1.32
LINK         C   ASN C  85                 N  AMSE C  86     1555   1555  1.33
LINK         C   ASN C  85                 N  BMSE C  86     1555   1555  1.33
LINK         C  AMSE C  86                 N   LEU C  87     1555   1555  1.33
LINK         C  BMSE C  86                 N   LEU C  87     1555   1555  1.33
LINK         C   CYS C  92                 N   MSE C  93     1555   1555  1.33
LINK         C   MSE C  93                 N   ASP C  94     1555   1555  1.34
LINK         C   LYS C 117                 N   MSE C 118     1555   1555  1.33
LINK         C   MSE C 118                 N   GLU C 119     1555   1555  1.33
LINK         C   SER C 157                 N   MSE C 158     1555   1555  1.33
LINK         C   MSE C 158                 N   LEU C 159     1555   1555  1.32
LINK         C   ASP C 248                 N   MSE C 249     1555   1555  1.33
LINK         C   MSE C 249                 N   MSE C 250     1555   1555  1.33
LINK         C   MSE C 250                 N   VAL C 251     1555   1555  1.33
LINK         C   VAL C 258                 N  AMSE C 259     1555   1555  1.33
LINK         C   VAL C 258                 N  BMSE C 259     1555   1555  1.34
LINK         C  AMSE C 259                 N   GLU C 260     1555   1555  1.33
LINK         C  BMSE C 259                 N   GLU C 260     1555   1555  1.33
LINK         C   GLY C 266                 N   MSE C 267     1555   1555  1.32
LINK         C   MSE C 267                 N   THR C 268     1555   1555  1.32
LINK         C   ASP C 289                 N   MSE C 290     1555   1555  1.33
LINK         C   MSE C 290                 N   ILE C 291     1555   1555  1.34
LINK         C   ALA D   0                 N   MSE D   1     1555   1555  1.32
LINK         C   MSE D   1                 N   ARG D   2     1555   1555  1.33
LINK         C   ILE D   6                 N   MSE D   7     1555   1555  1.33
LINK         C   MSE D   7                 N   GLY D   8     1555   1555  1.33
LINK         C   ILE D  18                 N  AMSE D  19     1555   1555  1.34
LINK         C   ILE D  18                 N  BMSE D  19     1555   1555  1.33
LINK         C  AMSE D  19                 N   THR D  20     1555   1555  1.33
LINK         C  BMSE D  19                 N   THR D  20     1555   1555  1.33
LINK         C   GLU D  23                 N   MSE D  24     1555   1555  1.33
LINK         C   MSE D  24                 N   ILE D  25     1555   1555  1.32
LINK         C   LYS D  43                 N   MSE D  44     1555   1555  1.33
LINK         C   MSE D  44                 N   ASP D  45     1555   1555  1.34
LINK         C   ASN D  85                 N  AMSE D  86     1555   1555  1.33
LINK         C   ASN D  85                 N  BMSE D  86     1555   1555  1.33
LINK         C  AMSE D  86                 N   LEU D  87     1555   1555  1.32
LINK         C  BMSE D  86                 N   LEU D  87     1555   1555  1.33
LINK         C   CYS D  92                 N   MSE D  93     1555   1555  1.33
LINK         C   MSE D  93                 N   ASP D  94     1555   1555  1.34
LINK         C   LYS D 117                 N   MSE D 118     1555   1555  1.33
LINK         C   MSE D 118                 N   GLU D 119     1555   1555  1.33
LINK         C   SER D 157                 N  AMSE D 158     1555   1555  1.33
LINK         C   SER D 157                 N  BMSE D 158     1555   1555  1.33
LINK         C  AMSE D 158                 N   LEU D 159     1555   1555  1.33
LINK         C  BMSE D 158                 N   LEU D 159     1555   1555  1.34
LINK         C   ASP D 248                 N   MSE D 249     1555   1555  1.33
LINK         C   MSE D 249                 N  AMSE D 250     1555   1555  1.33
LINK         C   MSE D 249                 N  BMSE D 250     1555   1555  1.33
LINK         C  AMSE D 250                 N   VAL D 251     1555   1555  1.33
LINK         C  BMSE D 250                 N   VAL D 251     1555   1555  1.33
LINK         C   VAL D 258                 N   MSE D 259     1555   1555  1.33
LINK         C   MSE D 259                 N   GLU D 260     1555   1555  1.33
LINK         C   GLY D 266                 N   MSE D 267     1555   1555  1.32
LINK         C   MSE D 267                 N   THR D 268     1555   1555  1.33
LINK         C   ASP D 289                 N   MSE D 290     1555   1555  1.33
LINK         C   MSE D 290                 N   ILE D 291     1555   1555  1.33
LINK        CA    CA A 310                 O2B ATP A 311     1555   1555  2.10
LINK         OE2 GLU A 260                CA    CA A 310     1555   1555  2.15
LINK        CA    CA A 310                 O2A ATP A 311     1555   1555  2.16
LINK         OD2 ASP A 248                CA    CA A 310     1555   1555  2.19
LINK         O   ARG C 299                MG    MG C 313     1555   1555  2.29
LINK        CA    CA D 310                 O3A ATP D 311     1555   1555  2.30
LINK         OD2 ASP D 248                CA    CA D 310     1555   1555  2.32
LINK        CA    CA D 310                 O   HOH D 528     1555   1555  2.34
LINK         OE2 GLU B 260                CA    CA B 310     1555   1555  2.38
LINK        CA    CA D 312                 O   HOH D 542     1555   1555  2.42
LINK         OD2 ASP B 248                CA    CA B 310     1555   1555  2.44
LINK         OE2 GLU D 260                CA    CA D 310     1555   1555  2.46
LINK         O   TYR D 208                CA    CA D 312     1555   1555  2.48
LINK         OE1 GLU C 108                CA    CA C 312     1555   1555  2.53
LINK         OD2 ASP C 248                CA    CA C 310     1555   1555  2.55
LINK         OE1 GLU D 200                CA    CA D 312     1555   1555  2.55
LINK         O   GLU C 302                MG    MG C 313     1555   1555  2.56
LINK         OD2AASP D 203                CA    CA D 312     1555   1555  2.58
LINK         OE2 GLU D 200                CA    CA D 312     1555   1555  2.59
LINK         OE2 GLU C 108                CA    CA C 312     1555   1555  2.64
LINK        CA    CA C 312                 O   HOH C 642     1555   1555  2.64
LINK        MG    MG C 313                 O   HOH C 667     1555   1555  2.64
LINK         O   GLY B 281                CA    CA B 312     1555   1555  2.64
LINK        CA    CA D 312                 O   HOH D 543     1555   1555  2.65
LINK        MG    MG C 313                 O   HOH C 668     1555   1555  2.67
LINK        CA    CA B 312                 O   HOH B 626     1555   1555  2.71
LINK        CA    CA B 312                 O   HOH B 628     1555   1555  2.72
LINK        CA    CA C 310                 O   HOH C 536     1555   1555  2.72
LINK         OE1 GLU C 260                CA    CA C 310     1555   1555  2.73
LINK        CA    CA C 310                 O1A ATP C 311     1555   1555  2.78
LINK        CA    CA C 310                 O2B ATP C 311     1555   1555  2.78
LINK        CA    CA B 312                 O   HOH B 627     1555   1555  2.79
LINK        MG    MG C 313                 O   HOH C 669     1555   1555  2.80
LINK         OD2BASP D 203                CA    CA D 312     1555   1555  2.87
LINK        CA    CA A 310                 O   HOH A 689     1555   1555  3.00
LINK        CA    CA B 312                 O   HOH B 630     1555   1555  3.01
LINK        CA    CA D 310                 O3B ATP D 311     1555   1555  3.03
CISPEP   1 PHE A  131    PRO A  132          0        -3.74
CISPEP   2 PHE B  131    PRO B  132          0        -6.14
CISPEP   3 PHE C  131    PRO C  132          0        -4.01
CISPEP   4 PHE D  131    PRO D  132          0        -3.27
SITE     1 AC1  4 ASP A 248  GLU A 260  ATP A 311  HOH A 689
SITE     1 AC2 18 LYS A  95  VAL A 134  LYS A 136  VAL A 146
SITE     2 AC2 18 GLU A 172  LYS A 173  TYR A 174  ILE A 175
SITE     3 AC2 18 GLU A 179  MSE A 259  GLU A 260  ASN A 262
SITE     4 AC2 18  CA A 310  HOH A 383  HOH A 408  HOH A 645
SITE     5 AC2 18 HOH A 646  HOH A 689
SITE     1 AC3  3 ASP B 248  GLU B 260  ATP B 311
SITE     1 AC4 17 GLU B  66  LYS B  95  VAL B 134  LYS B 136
SITE     2 AC4 17 GLY B 145  VAL B 146  GLU B 172  LYS B 173
SITE     3 AC4 17 TYR B 174  ILE B 175  GLU B 179  MSE B 250
SITE     4 AC4 17 MSE B 259  GLU B 260  ASN B 262   CA B 310
SITE     5 AC4 17 HOH B 742
SITE     1 AC5  7 ASN A  31  HOH A 629  GLY B 281  HOH B 626
SITE     2 AC5  7 HOH B 627  HOH B 628  HOH B 630
SITE     1 AC6  5 ARG C 246  ASP C 248  GLU C 260  ATP C 311
SITE     2 AC6  5 HOH C 536
SITE     1 AC7 16 LYS C  63  LYS C  95  VAL C 134  LYS C 136
SITE     2 AC7 16 VAL C 146  GLU C 172  LYS C 173  TYR C 174
SITE     3 AC7 16 ILE C 175  GLU C 179  MSE C 250  MSE C 259
SITE     4 AC7 16 GLU C 260   CA C 310  HOH C 536  HOH C 538
SITE     1 AC8  5 PHE A 131  HOH A 439  HOH A 641  GLU C 108
SITE     2 AC8  5 HOH C 642
SITE     1 AC9  5 ARG C 299  GLU C 302  HOH C 667  HOH C 668
SITE     2 AC9  5 HOH C 669
SITE     1 BC1  6 ASP A 203  HOH A 335  ASP D 248  GLU D 260
SITE     2 BC1  6 ATP D 311  HOH D 528
SITE     1 BC2 26 PHE A 201  ASP A 203  HOH A 335  HOH A 379
SITE     2 BC2 26 HOH A 545  LYS D  95  VAL D 134  LYS D 136
SITE     3 BC2 26 VAL D 146  GLU D 172  LYS D 173  TYR D 174
SITE     4 BC2 26 ILE D 175  GLU D 179  MSE D 250  MSE D 259
SITE     5 BC2 26 GLU D 260  ASN D 262   CA D 310  HOH D 336
SITE     6 BC2 26 HOH D 424  HOH D 434  HOH D 528  HOH D 567
SITE     7 BC2 26 HOH D 621  HOH D 671
SITE     1 BC3  6 ASP A 253  GLU D 200  ASP D 203  TYR D 208
SITE     2 BC3  6 HOH D 542  HOH D 543
SITE     1 BC4  5 GLU D  75  ARG D 299  GLU D 302  PHE D 304
SITE     2 BC4  5 HOH D 747
SITE     1 BC5  2 ASP D 111  HOH D 432
CRYST1   56.336   68.992   92.387  73.36  84.96  75.46 P 1           4
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      0.017751 -0.004603 -0.000316        0.00000
SCALE2      0.000000  0.014974 -0.004268        0.00000
SCALE3      0.000000  0.000000  0.011299        0.00000
      
PROCHECK
Go to PROCHECK summary
 References