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PDBsum entry 2yid

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Top Page protein ligands metals Protein-protein interface(s) links
Lyase PDB id
2yid
Jmol
Contents
Protein chains
844 a.a.
Ligands
TD7 ×4
Metals
_CA ×4
_MG ×4
Waters ×730
HEADER    LYASE                                   11-MAY-11   2YID
TITLE     CRYSTAL STRUCTURE OF THE SUCA DOMAIN OF MYCOBACTERIUM
TITLE    2 SMEGMATIS ALPHA-KETOGLUTARATE DECARBOXYLASE IN COMPLEX
TITLE    3 WITH THE ENAMINE-THDP INTERMEDIATE
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: 2-OXOGLUTARATE DECARBOXYLASE;
COMPND   3 CHAIN: A, B, C, D;
COMPND   4 FRAGMENT: RESIDUES 361-1227;
COMPND   5 SYNONYM: 2-OXOGLUTARATE CARBOXY-LYASE, ALPHA-KETOGLUTARATE
COMPND   6  DECARBOXYLASE, KDH;
COMPND   7 EC: 4.1.1.71;
COMPND   8 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM SMEGMATIS;
SOURCE   3 ORGANISM_TAXID: 1772;
SOURCE   4 STRAIN: MC2155;
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE   8 EXPRESSION_SYSTEM_VARIANT: PLYSS;
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE  10 EXPRESSION_SYSTEM_VECTOR: PET-28A
KEYWDS    LYASE, THDP-COVALENT ADDUCT
EXPDTA    X-RAY DIFFRACTION
AUTHOR    T.WAGNER,M.BELLINZONI,A.M.WEHENKEL,H.M.O'HARE,P.M.ALZARI
REVDAT   2   12-OCT-11 2YID    1       JRNL   REMARK VERSN
REVDAT   1   15-JUN-11 2YID    0
JRNL        AUTH   T.WAGNER,M.BELLINZONI,A.M.WEHENKEL,H.M.O'HARE,
JRNL        AUTH 2 P.M.ALZARI
JRNL        TITL   FUNCTIONAL PLASTICITY AND ALLOSTERIC REGULATION OF
JRNL        TITL 2 ALPHA-KETOGLUTARATE DECARBOXYLASE IN CENTRAL
JRNL        TITL 3 MYCOBACTERIAL METABOLISM.
JRNL        REF    CHEM.BIOL.                    V.  18  1011 2011
JRNL        REFN                   ISSN 1074-5521
JRNL        PMID   21867916
JRNL        DOI    10.1016/J.CHEMBIOL.2011.06.004
REMARK   2
REMARK   2 RESOLUTION.    2.25 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : BUSTER 2.11.1
REMARK   3   AUTHORS     : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,
REMARK   3               : PACIOREK,ROVERSI,SMART,VONRHEIN,WOMACK,
REMARK   3               : MATTHEWS,TEN EYCK,TRONRUD
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.25
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 32.94
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.0
REMARK   3   COMPLETENESS FOR RANGE        (%) : 95.71
REMARK   3   NUMBER OF REFLECTIONS             : 179896
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)  : 0.1935
REMARK   3   R VALUE            (WORKING SET)  : 0.1920
REMARK   3   FREE R VALUE                      : 0.2234
REMARK   3   FREE R VALUE TEST SET SIZE   (%)  : 5.04
REMARK   3   FREE R VALUE TEST SET COUNT       : 9062
REMARK   3   ESTIMATED ERROR OF FREE R VALUE   : NULL
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED               : 20
REMARK   3   BIN RESOLUTION RANGE HIGH   (ANGSTROMS) : 2.25
REMARK   3   BIN RESOLUTION RANGE LOW    (ANGSTROMS) : 2.31
REMARK   3   BIN COMPLETENESS (WORKING+TEST)     (%) : 95.71
REMARK   3   REFLECTIONS IN BIN (WORKING + TEST SET) : 13137
REMARK   3   BIN R VALUE        (WORKING + TEST SET) : 0.2147
REMARK   3   REFLECTIONS IN BIN        (WORKING SET) : 12469
REMARK   3   BIN R VALUE               (WORKING SET) : 0.2129
REMARK   3   BIN FREE R VALUE                        : 0.2488
REMARK   3   BIN FREE R VALUE TEST SET SIZE      (%) : 5.08
REMARK   3   BIN FREE R VALUE TEST SET COUNT         : 668
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE     : NULL
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 26117
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 140
REMARK   3   SOLVENT ATOMS            : 730
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 30.43
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 33.53
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : -0.8828
REMARK   3    B22 (A**2) : 4.5879
REMARK   3    B33 (A**2) : -3.7051
REMARK   3    B12 (A**2) : 1.1116
REMARK   3    B13 (A**2) : -0.4018
REMARK   3    B23 (A**2) : 0.5883
REMARK   3
REMARK   3  ESTIMATED COORDINATE ERROR.
REMARK   3   ESD FROM LUZZATI PLOT                    (A) : 0.295
REMARK   3   DPI (BLOW EQ-10) BASED ON R VALUE        (A) : 0.251
REMARK   3   DPI (BLOW EQ-9) BASED ON FREE R VALUE    (A) : 0.190
REMARK   3   DPI (CRUICKSHANK) BASED ON R VALUE       (A) : 0.268
REMARK   3   DPI (CRUICKSHANK) BASED ON FREE R VALUE  (A) : 0.197
REMARK   3
REMARK   3   REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797
REMARK   3               CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601
REMARK   3
REMARK   3  CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.9262
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.9014
REMARK   3
REMARK   3   NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK   3   TERM                          COUNT    WEIGHT   FUNCTION.
REMARK   3    BOND LENGTHS              : 26777  ; 2.00   ; HARMONIC
REMARK   3    BOND ANGLES               : 36320  ; 2.00   ; HARMONIC
REMARK   3    TORSION ANGLES            : 12397  ; 2.00   ; SINUSOIDAL
REMARK   3    TRIGONAL CARBON PLANES    : 700    ; 2.00   ; HARMONIC
REMARK   3    GENERAL PLANES            : 3959   ; 5.00   ; HARMONIC
REMARK   3    ISOTROPIC THERMAL FACTORS : 26777  ; 20.00  ; HARMONIC
REMARK   3    BAD NON-BONDED CONTACTS   : 3      ; 5.00   ; SEMIHARMONIC
REMARK   3    IMPROPER TORSIONS         : NULL   ; NULL   ; NULL
REMARK   3    PSEUDOROTATION ANGLES     : NULL   ; NULL   ; NULL
REMARK   3    CHIRAL IMPROPER TORSION   : 3454   ; 5.00   ; SEMIHARMONIC
REMARK   3    SUM OF OCCUPANCIES        : NULL   ; NULL   ; NULL
REMARK   3    UTILITY DISTANCES         : NULL   ; NULL   ; NULL
REMARK   3    UTILITY ANGLES            : NULL   ; NULL   ; NULL
REMARK   3    UTILITY TORSION           : NULL   ; NULL   ; NULL
REMARK   3    IDEAL-DIST CONTACT TERM   : 32619  ; 4.00   ; SEMIHARMONIC
REMARK   3
REMARK   3   RMS DEVIATIONS FROM IDEAL VALUES.
REMARK   3    BOND LENGTHS                       (A) : 0.010
REMARK   3    BOND ANGLES                  (DEGREES) : 1.01
REMARK   3    PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.22
REMARK   3    OTHER TORSION ANGLES         (DEGREES) : 2.83
REMARK   3
REMARK   3  TLS DETAILS
REMARK   3   NUMBER OF TLS GROUPS  : 4
REMARK   3
REMARK   3   TLS GROUP : 1
REMARK   3    SELECTION: CHAIN A
REMARK   3    ORIGIN FOR THE GROUP (A):   10.4136   -0.6089   -7.2293
REMARK   3    T TENSOR
REMARK   3     T11:   -0.0633 T22:   -0.0981
REMARK   3     T33:   -0.1430 T12:    0.0802
REMARK   3     T13:   -0.0112 T23:   -0.0238
REMARK   3    L TENSOR
REMARK   3     L11:    0.4626 L22:    0.8696
REMARK   3     L33:    0.3503 L12:    0.0359
REMARK   3     L13:    0.0264 L23:    0.0890
REMARK   3    S TENSOR
REMARK   3     S11:    0.0274 S12:    0.0464 S13:    0.0125
REMARK   3     S21:   -0.0565 S22:   -0.0386 S23:   -0.0417
REMARK   3     S31:    0.0917 S32:    0.0920 S33:    0.0112
REMARK   3
REMARK   3   TLS GROUP : 2
REMARK   3    SELECTION: CHAIN B
REMARK   3    ORIGIN FOR THE GROUP (A):   -9.8627    0.5680    8.9737
REMARK   3    T TENSOR
REMARK   3     T11:   -0.0292 T22:   -0.1260
REMARK   3     T33:   -0.0854 T12:    0.0467
REMARK   3     T13:   -0.0054 T23:   -0.0589
REMARK   3    L TENSOR
REMARK   3     L11:    0.3503 L22:    0.6865
REMARK   3     L33:    0.4986 L12:   -0.2198
REMARK   3     L13:    0.1325 L23:   -0.2141
REMARK   3    S TENSOR
REMARK   3     S11:   -0.0015 S12:   -0.0027 S13:    0.0203
REMARK   3     S21:    0.0628 S22:   -0.0121 S23:    0.1350
REMARK   3     S31:    0.0327 S32:    0.0079 S33:    0.0136
REMARK   3
REMARK   3   TLS GROUP : 3
REMARK   3    SELECTION: CHAIN C
REMARK   3    ORIGIN FOR THE GROUP (A):   24.1561   33.8547  -79.8119
REMARK   3    T TENSOR
REMARK   3     T11:   -0.0546 T22:   -0.1089
REMARK   3     T33:   -0.0941 T12:    0.0317
REMARK   3     T13:   -0.0267 T23:   -0.0118
REMARK   3    L TENSOR
REMARK   3     L11:    0.2549 L22:    0.8413
REMARK   3     L33:    0.4698 L12:   -0.0527
REMARK   3     L13:    0.0322 L23:    0.2334
REMARK   3    S TENSOR
REMARK   3     S11:   -0.0156 S12:    0.0249 S13:    0.0744
REMARK   3     S21:   -0.0543 S22:    0.0060 S23:   -0.0760
REMARK   3     S31:    0.0098 S32:    0.0221 S33:    0.0095
REMARK   3
REMARK   3   TLS GROUP: 4
REMARK   3    SELECTION: CHAIN D
REMARK   3    ORIGIN FOR THE GROUP (A):    5.6370   25.4353  -64.0960
REMARK   3    T TENSOR
REMARK   3     T11:   -0.0800 T22:   -0.1165
REMARK   3     T33:   -0.1126 T12:    0.0184
REMARK   3     T13:    0.0159 T23:   -0.0189
REMARK   3    L TENSOR
REMARK   3     L11:    0.5163 L22:    0.9142
REMARK   3     L33:    0.3668 L12:   -0.2729
REMARK   3     L13:    0.1098 L23:   -0.0230
REMARK   3    S TENSOR
REMARK   3     S11:   -0.0445 S12:   -0.0424 S13:   -0.0058
REMARK   3     S21:    0.1239 S22:    0.0054 S23:    0.1480
REMARK   3     S31:    0.0493 S32:   -0.0478 S33:    0.0391
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: NCS REPRESENTATION : RESTRAINT LSSR
REMARK   3  (-AUTONCS) IDEAL-DIST CONTACT TERM CONTACT SETUP. RESIDUE TYPES
REMARK   3  WITHOUT CCP4 ATOM TYPE IN LIBRARY=MG CA. NUMBER OF ATOMS WITH
REMARK   3  PROPER CCP4 ATOM TYPE=26979. NUMBER WITH APPROX DEFAULT CCP4 ATOM
REMARK   3  TYPE=0. NUMBER TREATED BY BAD NON-BONDED CONTACTS=8.
REMARK   4
REMARK   4 2YID COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 12-MAY-11.
REMARK 100 THE PDBE ID CODE IS EBI-48268.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 20-NOV-10
REMARK 200  TEMPERATURE           (KELVIN) : 110
REMARK 200  PH                             : 7.6
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : SOLEIL
REMARK 200  BEAMLINE                       : PROXIMA 1
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9801
REMARK 200  MONOCHROMATOR                  : CHANNEL CUT MONOCHROMATOR
REMARK 200                                   CRYSTAL
REMARK 200  OPTICS                         : KIRKPATRICK-BAEZ PAIR OF
REMARK 200                                   BI-MORPH MIRRORS
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : ADSC
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200  DATA SCALING SOFTWARE          : SCALA
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 179918
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.25
REMARK 200  RESOLUTION RANGE LOW       (A) : 41.90
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 95.7
REMARK 200  DATA REDUNDANCY                : 2.0
REMARK 200  R MERGE                    (I) : 0.10
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 6.90
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.25
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.37
REMARK 200  COMPLETENESS FOR SHELL     (%) : 94.6
REMARK 200  DATA REDUNDANCY IN SHELL       : 1.9
REMARK 200  R MERGE FOR SHELL          (I) : 0.48
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : 2.00
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 2YIC
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 54.6
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.71
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 52% MPD, 20 MM SODIUM ACETATE,
REMARK 280  5% 1,3-PROPANEDIOL.
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
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: 11170 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 57230 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -52.1 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: 11330 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 57860 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -54.1 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 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465   M RES C SSSEQI
REMARK 465     GLY A   360
REMARK 465     PHE A   397
REMARK 465     ARG A   398
REMARK 465     SER A   399
REMARK 465     HIS A   400
REMARK 465     PRO A   401
REMARK 465     ASP A   402
REMARK 465     LEU A   403
REMARK 465     ASP A   404
REMARK 465     VAL A   405
REMARK 465     ASN A   406
REMARK 465     SER A   407
REMARK 465     HIS A   408
REMARK 465     GLY A   409
REMARK 465     GLY A   423
REMARK 465     PHE A   424
REMARK 465     ALA A   425
REMARK 465     GLY A   426
REMARK 465     GLU A   811
REMARK 465     LYS A   812
REMARK 465     HIS A   813
REMARK 465     PRO A   828
REMARK 465     SER A   829
REMARK 465     LYS A   830
REMARK 465     GLY B   360
REMARK 465     ASP B   361
REMARK 465     SER B   362
REMARK 465     ILE B   363
REMARK 465     GLU B   364
REMARK 465     ASN B   394
REMARK 465     THR B   395
REMARK 465     ARG B   396
REMARK 465     PHE B   397
REMARK 465     ARG B   398
REMARK 465     SER B   399
REMARK 465     HIS B   400
REMARK 465     PRO B   401
REMARK 465     ASP B   402
REMARK 465     LEU B   403
REMARK 465     ASP B   404
REMARK 465     VAL B   405
REMARK 465     ASN B   406
REMARK 465     SER B   407
REMARK 465     HIS B   408
REMARK 465     GLY B   409
REMARK 465     LEU B   410
REMARK 465     THR B   411
REMARK 465     LEU B   412
REMARK 465     ASP B   422
REMARK 465     GLY B   423
REMARK 465     PHE B   424
REMARK 465     ALA B   425
REMARK 465     PRO B   567
REMARK 465     SER B   568
REMARK 465     GLN B   569
REMARK 465     GLY C   360
REMARK 465     ASP C   361
REMARK 465     SER C   362
REMARK 465     ILE C   363
REMARK 465     SER C   399
REMARK 465     HIS C   400
REMARK 465     PRO C   401
REMARK 465     ASP C   402
REMARK 465     LEU C   403
REMARK 465     ASP C   404
REMARK 465     VAL C   405
REMARK 465     ASN C   406
REMARK 465     SER C   407
REMARK 465     HIS C   408
REMARK 465     ASP C   422
REMARK 465     GLY C   423
REMARK 465     PHE C   424
REMARK 465     ALA C   425
REMARK 465     GLY C   426
REMARK 465     VAL C   427
REMARK 465     GLN C   428
REMARK 465     ASP C   632
REMARK 465     ASN C   633
REMARK 465     PRO C   828
REMARK 465     SER C   829
REMARK 465     GLY D   360
REMARK 465     SER D   399
REMARK 465     HIS D   400
REMARK 465     PRO D   401
REMARK 465     ASP D   402
REMARK 465     LEU D   403
REMARK 465     ASP D   404
REMARK 465     VAL D   405
REMARK 465     ASN D   406
REMARK 465     SER D   407
REMARK 465     HIS D   408
REMARK 465     GLY D   409
REMARK 465     PHE D   424
REMARK 465     ALA D   425
REMARK 465     SER D   829
REMARK 465     LYS D   830
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     ASP A 361    CG   OD1  OD2
REMARK 470     SER A 362    OG
REMARK 470     ILE A 363    CG1  CG2  CD1
REMARK 470     GLU A 364    CG   CD   OE1  OE2
REMARK 470     LYS A 366    CG   CD   CE   NZ
REMARK 470     THR A 395    OG1  CG2
REMARK 470     THR A 411    OG1  CG2
REMARK 470     LEU A 412    CG   CD1  CD2
REMARK 470     TRP A 413    CG   CD1  CD2  NE1  CE2  CE3  CZ2  CZ3
REMARK 470     TRP A 413    CH2
REMARK 470     ARG A 417    CG   CD   NE   CZ   NH1  NH2
REMARK 470     LYS A 420    CG   CD   CE   NZ
REMARK 470     VAL A 427    CG1  CG2
REMARK 470     GLN A 428    CG   CD   OE1  NE2
REMARK 470     ARG A 429    CG   CD   NE   CZ   NH1  NH2
REMARK 470     LYS A 470    CG   CD   CE   NZ
REMARK 470     ASP A 472    CG   OD1  OD2
REMARK 470     LYS A 473    CG   CD   CE   NZ
REMARK 470     LEU A 565    CG   CD1  CD2
REMARK 470     ASN A 566    CG   OD1  ND2
REMARK 470     SER A 568    OG
REMARK 470     GLN A 569    CG   CD   OE1  NE2
REMARK 470     HIS A 571    CG   ND1  CD2  CE1  NE2
REMARK 470     LYS A 767    CG   CD   CE   NZ
REMARK 470     ARG A 802    CG   CD   NE   CZ   NH1  NH2
REMARK 470     ARG A 808    CG   CD   NE   CZ   NH1  NH2
REMARK 470     GLU A 809    CG   CD   OE1  OE2
REMARK 470     GLU A 814    CG   CD   OE1  OE2
REMARK 470     ILE A 815    CG1  CG2  CD1
REMARK 470     GLU A 816    CG   CD   OE1  OE2
REMARK 470     GLU A 852    CG   CD   OE1  OE2
REMARK 470     LYS A 942    CG   CD   CE   NZ
REMARK 470     ASP A1101    CG   OD1  OD2
REMARK 470     GLU A1103    CG   CD   OE1  OE2
REMARK 470     ARG A1149    CG   CD   NE   CZ   NH1  NH2
REMARK 470     LYS A1162    CG   CD   CE   NZ
REMARK 470     ASP B 365    CG   OD1  OD2
REMARK 470     LYS B 366    CG   CD   CE   NZ
REMARK 470     ARG B 369    CG   CD   NE   CZ   NH1  NH2
REMARK 470     TRP B 413    CG   CD1  CD2  NE1  CE2  CE3  CZ2  CZ3
REMARK 470     TRP B 413    CH2
REMARK 470     ARG B 417    CG   CD   NE   CZ   NH1  NH2
REMARK 470     LYS B 420    CG   CD   CE   NZ
REMARK 470     VAL B 427    CG1  CG2
REMARK 470     GLN B 428    CG   CD   OE1  NE2
REMARK 470     ARG B 429    CG   CD   NE   CZ   NH1  NH2
REMARK 470     ARG B 445    CG   CD   NE   CZ   NH1  NH2
REMARK 470     ASP B 472    CG   OD1  OD2
REMARK 470     LYS B 473    CG   CD   CE   NZ
REMARK 470     LYS B 772    CG   CD   CE   NZ
REMARK 470     GLN B 797    CG   CD   OE1  NE2
REMARK 470     LYS B 812    CG   CD   CE   NZ
REMARK 470     GLU B 814    CG   CD   OE1  OE2
REMARK 470     ILE B 815    CG1  CG2  CD1
REMARK 470     GLN B 826    CG   CD   OE1  NE2
REMARK 470     ILE B 827    CG1  CG2  CD1
REMARK 470     SER B 829    OG
REMARK 470     LYS B 830    CG   CD   CE   NZ
REMARK 470     LYS B 837    CG   CD   CE   NZ
REMARK 470     GLU B 852    CG   CD   OE1  OE2
REMARK 470     ARG B1083    CG   CD   NE   CZ   NH1  NH2
REMARK 470     LYS B1089    CG   CD   CE   NZ
REMARK 470     ARG B1091    CG   CD   NE   CZ   NH1  NH2
REMARK 470     GLU B1103    CG   CD   OE1  OE2
REMARK 470     ARG B1149    CG   CD   NE   CZ   NH1  NH2
REMARK 470     GLU B1186    CG   CD   OE1  OE2
REMARK 470     LYS B1212    CG   CD   CE   NZ
REMARK 470     GLU C 364    CG   CD   OE1  OE2
REMARK 470     ASP C 365    CG   OD1  OD2
REMARK 470     LYS C 366    CG   CD   CE   NZ
REMARK 470     GLU C 372    CG   CD   OE1  OE2
REMARK 470     ARG C 398    CG   CD   NE   CZ   NH1  NH2
REMARK 470     THR C 411    OG1  CG2
REMARK 470     LEU C 412    CG   CD1  CD2
REMARK 470     TRP C 413    CG   CD1  CD2  NE1  CE2  CE3  CZ2  CZ3
REMARK 470     TRP C 413    CH2
REMARK 470     LYS C 420    CG   CD   CE   NZ
REMARK 470     ARG C 429    CG   CD   NE   CZ   NH1  NH2
REMARK 470     LYS C 431    CG   CD   CE   NZ
REMARK 470     ARG C 461    CG   CD   NE   CZ   NH1  NH2
REMARK 470     LYS C 470    CG   CD   CE   NZ
REMARK 470     LYS C 473    CG   CD   CE   NZ
REMARK 470     SER C 568    OG
REMARK 470     GLN C 569    CG   CD   OE1  NE2
REMARK 470     SER C 631    OG
REMARK 470     ARG C 634    CG   CD   NE   CZ   NH1  NH2
REMARK 470     LYS C 767    CD   CE   NZ
REMARK 470     GLN C 799    CG   CD   OE1  NE2
REMARK 470     GLU C 806    CG   CD   OE1  OE2
REMARK 470     LYS C 812    CG   CD   CE   NZ
REMARK 470     GLU C 814    CG   CD   OE1  OE2
REMARK 470     ILE C 815    CG1  CG2  CD1
REMARK 470     GLU C 816    CG   CD   OE1  OE2
REMARK 470     GLN C 825    CG   CD   OE1  NE2
REMARK 470     ILE C 827    CG1  CG2  CD1
REMARK 470     LYS C 830    CG   CD   CE   NZ
REMARK 470     GLU C 852    CG   CD   OE1  OE2
REMARK 470     LYS C 942    CG   CD   CE   NZ
REMARK 470     LYS C1089    CG   CD   CE   NZ
REMARK 470     GLU C1103    CG   CD   OE1  OE2
REMARK 470     ASP D 361    CG   OD1  OD2
REMARK 470     SER D 362    OG
REMARK 470     ILE D 363    CG1  CG2  CD1
REMARK 470     GLU D 364    CG   CD   OE1  OE2
REMARK 470     LYS D 366    CG   CD   CE   NZ
REMARK 470     ARG D 369    CG   CD   NE   CZ   NH1  NH2
REMARK 470     ARG D 398    CG   CD   NE   CZ   NH1  NH2
REMARK 470     THR D 411    OG1  CG2
REMARK 470     LEU D 412    CG   CD1  CD2
REMARK 470     TRP D 413    CG   CD1  CD2  NE1  CE2  CE3  CZ2  CZ3
REMARK 470     TRP D 413    CH2
REMARK 470     ARG D 417    CG   CD   NE   CZ   NH1  NH2
REMARK 470     LYS D 420    CG   CD   CE   NZ
REMARK 470     ASP D 422    CG   OD1  OD2
REMARK 470     VAL D 427    CG1  CG2
REMARK 470     GLN D 428    CG   CD   OE1  NE2
REMARK 470     LYS D 430    CG   CD   CE   NZ
REMARK 470     LYS D 470    CG   CD   CE   NZ
REMARK 470     ASP D 472    CG   OD1  OD2
REMARK 470     LYS D 473    CG   CD   CE   NZ
REMARK 470     HIS D 571    CG   ND1  CD2  CE1  NE2
REMARK 470     ARG D 664    CG   CD   NE   CZ   NH1  NH2
REMARK 470     ARG D 768    CG   CD   NE   CZ   NH1  NH2
REMARK 470     LYS D 772    CG   CD   CE   NZ
REMARK 470     GLU D 790    CG   CD   OE1  OE2
REMARK 470     GLN D 799    CG   CD   OE1  NE2
REMARK 470     ARG D 808    CG   CD   NE   CZ   NH1  NH2
REMARK 470     GLU D 809    CG   CD   OE1  OE2
REMARK 470     GLU D 814    CG   CD   OE1  OE2
REMARK 470     ILE D 827    CG1  CG2  CD1
REMARK 470     ASP D1101    CG   OD1  OD2
REMARK 470     GLU D1103    CG   CD   OE1  OE2
REMARK 470     ARG D1150    CG   CD   NE   CZ   NH1  NH2
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    ARG A 445     -118.09   -104.02
REMARK 500    TYR A 451      -11.11   -150.45
REMARK 500    GLU A 468       34.57    -90.40
REMARK 500    PRO A 538     -150.54    -86.00
REMARK 500    ARG A 540      105.56    -55.44
REMARK 500    HIS A 605      101.42    -56.44
REMARK 500    GLU A 607       -7.64     80.39
REMARK 500    ASN A 633       46.19    -96.40
REMARK 500    SER A 636        7.54    -66.36
REMARK 500    PHE A 682     -104.86     61.77
REMARK 500    CYS A 741     -154.26   -143.16
REMARK 500    GLN A 826      -61.15   -102.38
REMARK 500    PHE A 991      -62.61   -120.13
REMARK 500    THR A1021      -48.84   -131.08
REMARK 500    LYS A1070      -76.25   -128.60
REMARK 500    TYR A1158       75.84   -117.11
REMARK 500    ARG B 445     -116.51   -105.25
REMARK 500    TYR B 451      -10.91   -151.10
REMARK 500    GLU B 468       36.69    -91.65
REMARK 500    TYR B 500       60.59   -114.49
REMARK 500    PRO B 538     -151.06    -86.48
REMARK 500    ARG B 540      105.72    -56.38
REMARK 500    HIS B 605      102.67    -54.84
REMARK 500    GLU B 607       -6.03     75.45
REMARK 500    ASN B 633       43.46    -95.30
REMARK 500    SER B 636        0.71    -63.68
REMARK 500    PHE B 682     -104.38     61.83
REMARK 500    CYS B 741     -155.57   -144.38
REMARK 500    PHE B 991      -61.70   -120.76
REMARK 500    THR B1021      -46.84   -133.74
REMARK 500    LYS B1070      -75.09   -128.14
REMARK 500    TYR B1158       74.95   -115.77
REMARK 500    ARG C 445     -119.00   -104.20
REMARK 500    TYR C 451      -12.50   -153.73
REMARK 500    GLU C 468       34.10    -91.02
REMARK 500    PRO C 538     -150.44    -86.93
REMARK 500    ARG C 540      105.27    -56.20
REMARK 500    HIS C 605      101.20    -51.33
REMARK 500    GLU C 607       -8.26     72.42
REMARK 500    GLU C 629       45.93   -106.89
REMARK 500    PHE C 682     -103.89     61.38
REMARK 500    CYS C 741     -155.76   -151.01
REMARK 500    PHE C 991      -61.45   -120.24
REMARK 500    THR C1021      -47.21   -130.36
REMARK 500    LYS C1070      -76.27   -128.70
REMARK 500    SER C1088     -169.79   -124.81
REMARK 500    GLU C1103       44.10   -109.58
REMARK 500    TYR C1158       75.11   -116.75
REMARK 500    PHE D 397       58.90    -95.36
REMARK 500    ARG D 445     -119.08   -104.94
REMARK 500
REMARK 500 THIS ENTRY HAS      64 RAMACHANDRAN OUTLIERS.
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 A2002  MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 645   OD1
REMARK 620 2 ASN A 678   OD1  85.5
REMARK 620 3 ILE A 680   O    91.2  85.0
REMARK 620 4 TD7 A2001   O3B 171.7  96.0  97.0
REMARK 620 5 TD7 A2001   O2A  81.0 165.8  91.0  98.0
REMARK 620 6 HOH A3047   O    80.3  87.6 169.1  91.7  94.3
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MG B2002  MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 645   OD1
REMARK 620 2 ASN B 678   OD1  86.4
REMARK 620 3 ILE B 680   O    92.3  83.8
REMARK 620 4 TD7 B2001   O3B 174.1  93.9  93.6
REMARK 620 5 TD7 B2001   O2A  85.6 168.1  87.7  94.8
REMARK 620 6 HOH B3050   O    83.5  90.1 172.8  90.6  97.8
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MG C2002  MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 TD7 C2001   O3B
REMARK 620 2 TD7 C2001   O2A  91.2
REMARK 620 3 HOH C3062   O    84.8  91.7
REMARK 620 4 ASP C 645   OD1 166.0  81.2  83.7
REMARK 620 5 ASN C 678   OD1  97.8 170.9  90.4  90.3
REMARK 620 6 ILE C 680   O    96.3  88.6 178.8  95.2  89.2
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MG D2002  MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 TD7 D2001   O3B
REMARK 620 2 TD7 D2001   O2A  96.7
REMARK 620 3 HOH D3038   O    88.8  92.7
REMARK 620 4 ILE D 680   O   101.8  91.8 167.9
REMARK 620 5 ASP D 645   OD1 165.4  79.6  77.3  92.4
REMARK 620 6 ASN D 678   OD1  98.9 164.0  83.9  88.7  84.3
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              CA A2003  CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A1004   OD2
REMARK 620 2 HOH A3154   O    72.7
REMARK 620 3 ASP A1004   OD1  52.2 114.0
REMARK 620 4 ASP A1058   OD1 150.7  78.6 151.9
REMARK 620 5 ILE A1060   O    94.7  79.5  72.9  85.8
REMARK 620 6 HOH A3153   O   121.1 164.3  74.4  88.2  91.2
REMARK 620 7 HIS A1055   O    90.9  86.1 123.1  81.1 162.2 100.4
REMARK 620 N                    1     2     3     4     5     6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              CA B2003  CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH B3128   O
REMARK 620 2 ASP B1004   OD2  65.7
REMARK 620 3 HIS B1055   O    90.8  90.4
REMARK 620 4 ASP B1058   OD1  90.7 155.2  82.0
REMARK 620 5 ASP B1004   OD1 107.8  52.4 120.0 150.0
REMARK 620 6 ILE B1060   O    81.9  97.1 166.2  86.3  73.6
REMARK 620 7 HOH B3127   O   166.6 124.7  97.3  79.9  77.4  87.9
REMARK 620 N                    1     2     3     4     5     6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              CA C2003  CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH C3177   O
REMARK 620 2 ASP C1004   OD1  77.0
REMARK 620 3 ASP C1004   OD2 124.3  53.3
REMARK 620 4 HIS C1055   O    94.8 122.2  92.2
REMARK 620 5 ASP C1058   OD1  81.6 149.8 153.8  80.4
REMARK 620 6 ILE C1060   O    90.3  74.1  97.8 163.6  85.0
REMARK 620 7 HOH C3178   O   156.0 119.9  78.9  89.9  76.0  79.4
REMARK 620 N                    1     2     3     4     5     6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              CA D2003  CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP D1058   OD1
REMARK 620 2 ILE D1060   O    88.0
REMARK 620 3 HOH D3100   O    88.8  84.8
REMARK 620 4 HOH D3101   O    89.9  82.0 166.8
REMARK 620 5 HIS D1055   O    84.1 167.0 105.3  87.7
REMARK 620 6 ASP D1004   OD1 152.0  71.1  71.4 104.8 119.5
REMARK 620 7 ASP D1004   OD2 153.2  92.8 117.9  63.8  89.7  49.9
REMARK 620 N                    1     2     3     4     5     6
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TD7 A2001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  MG A2002
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CA A2003
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TD7 B2001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  MG B2002
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CA B2003
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TD7 C2001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  MG C2002
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CA C2003
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TD7 D2001
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  MG D2002
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CA D2003
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2XT8   RELATED DB: PDB
REMARK 900  CRYSTAL STRUCTURE OF MYCOBACTERIUM SMEGMATIS ALPHA-
REMARK 900  KETOGLUTARATE DECARBOXYLASE HOMOHEXAMER IN COMPLEX WITH
REMARK 900  GARA (MONOCLINIC FORM)
REMARK 900 RELATED ID: 2Y0P   RELATED DB: PDB
REMARK 900  CRYSTAL STRUCTURE OF THE SUCA DOMAIN OF MYCOBACTERIUM
REMARK 900  SMEGMATIS ALPHA-KETOGLUTARATE DECARBOXYLASE IN COMPLEX
REMARK 900  WITH THE ENAMINE-THDP INTERMEDIATE AND ACETYL-COA
REMARK 900 RELATED ID: 2XTA   RELATED DB: PDB
REMARK 900  CRYSTAL STRUCTURE OF THE SUCA DOMAIN OF MYCOBACTERIUM
REMARK 900  SMEGMATIS ALPHA-KETOGLUTARATE DECARBOXYLASE IN COMPLEX
REMARK 900  WITH ACETYL-COA (TRICLINIC FORM)
REMARK 900 RELATED ID: 2XT9   RELATED DB: PDB
REMARK 900  CRYSTAL STRUCTURE OF MYCOBACTERIUM SMEGMATIS ALPHA-
REMARK 900  KETOGLUTARATE DECARBOXYLASE IN COMPLEX WITH GARA
REMARK 900 RELATED ID: 2XT6   RELATED DB: PDB
REMARK 900  CRYSTAL STRUCTURE OF MYCOBACTERIUM SMEGMATIS ALPHA-
REMARK 900  KETOGLUTARATE DECARBOXYLASE HOMODIMER (ORTHORHOMBIC FORM)
REMARK 900 RELATED ID: 2YIC   RELATED DB: PDB
REMARK 900  CRYSTAL STRUCTURE OF THE SUCA DOMAIN OF MYCOBACTERIUM
REMARK 900  SMEGMATIS ALPHA-KETOGLUTARATE DECARBOXYLASE (TRICLINIC FORM)
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 FIRST GLY RESIDUE IS A PURIFICATION TAG LEFTOVER (TEV
REMARK 999 CLEAVAGE SITE).
DBREF  2YID A  361  1227  UNP    A0R2B1   KGD_MYCS2      361   1227
DBREF  2YID B  361  1227  UNP    A0R2B1   KGD_MYCS2      361   1227
DBREF  2YID C  361  1227  UNP    A0R2B1   KGD_MYCS2      361   1227
DBREF  2YID D  361  1227  UNP    A0R2B1   KGD_MYCS2      361   1227
SEQADV 2YID GLY A  360  UNP  A0R2B1              EXPRESSION TAG
SEQADV 2YID GLY B  360  UNP  A0R2B1              EXPRESSION TAG
SEQADV 2YID GLY C  360  UNP  A0R2B1              EXPRESSION TAG
SEQADV 2YID GLY D  360  UNP  A0R2B1              EXPRESSION TAG
SEQRES   1 A  868  GLY ASP SER ILE GLU ASP LYS ASN ALA ARG VAL ILE GLU
SEQRES   2 A  868  LEU ILE ALA ALA TYR ARG ASN ARG GLY HIS LEU MET ALA
SEQRES   3 A  868  ASP ILE ASP PRO LEU ARG LEU ASP ASN THR ARG PHE ARG
SEQRES   4 A  868  SER HIS PRO ASP LEU ASP VAL ASN SER HIS GLY LEU THR
SEQRES   5 A  868  LEU TRP ASP LEU ASP ARG GLU PHE LYS VAL ASP GLY PHE
SEQRES   6 A  868  ALA GLY VAL GLN ARG LYS LYS LEU ARG ASP ILE LEU SER
SEQRES   7 A  868  VAL LEU ARG ASP ALA TYR CYS ARG HIS VAL GLY VAL GLU
SEQRES   8 A  868  TYR THR HIS ILE LEU GLU PRO GLU GLN GLN ARG TRP ILE
SEQRES   9 A  868  GLN GLU ARG VAL GLU THR LYS HIS ASP LYS PRO THR VAL
SEQRES  10 A  868  ALA GLU GLN LYS TYR ILE LEU SER LYS LEU ASN ALA ALA
SEQRES  11 A  868  GLU ALA PHE GLU THR PHE LEU GLN THR LYS TYR VAL GLY
SEQRES  12 A  868  GLN LYS ARG PHE SER LEU GLU GLY ALA GLU THR VAL ILE
SEQRES  13 A  868  PRO MET MET ASP ALA VAL ILE ASP GLN CYS ALA GLU HIS
SEQRES  14 A  868  GLY LEU ASP GLU VAL VAL ILE ALA MET PRO HIS ARG GLY
SEQRES  15 A  868  ARG LEU ASN VAL LEU ALA ASN ILE VAL GLY LYS PRO TYR
SEQRES  16 A  868  SER GLN ILE PHE SER GLU PHE GLU GLY ASN LEU ASN PRO
SEQRES  17 A  868  SER GLN ALA HIS GLY SER GLY ASP VAL LYS TYR HIS LEU
SEQRES  18 A  868  GLY ALA THR GLY THR TYR ILE GLN MET PHE GLY ASP ASN
SEQRES  19 A  868  ASP ILE GLU VAL SER LEU THR ALA ASN PRO SER HIS LEU
SEQRES  20 A  868  GLU ALA VAL ASP PRO VAL LEU GLU GLY LEU VAL ARG ALA
SEQRES  21 A  868  LYS GLN ASP LEU LEU ASP THR GLY GLU GLU GLY SER ASP
SEQRES  22 A  868  ASN ARG PHE SER VAL VAL PRO LEU MET LEU HIS GLY ASP
SEQRES  23 A  868  ALA ALA PHE ALA GLY GLN GLY VAL VAL ALA GLU THR LEU
SEQRES  24 A  868  ASN LEU ALA LEU LEU ARG GLY TYR ARG THR GLY GLY THR
SEQRES  25 A  868  ILE HIS ILE VAL VAL ASN ASN GLN ILE GLY PHE THR THR
SEQRES  26 A  868  ALA PRO THR ASP SER ARG SER SER GLU TYR CYS THR ASP
SEQRES  27 A  868  VAL ALA LYS MET ILE GLY ALA PRO ILE PHE HIS VAL ASN
SEQRES  28 A  868  GLY ASP ASP PRO GLU ALA CYS ALA TRP VAL ALA ARG LEU
SEQRES  29 A  868  ALA VAL ASP PHE ARG GLN ALA PHE LYS LYS ASP VAL VAL
SEQRES  30 A  868  ILE ASP MET LEU CYS TYR ARG ARG ARG GLY HIS ASN GLU
SEQRES  31 A  868  GLY ASP ASP PRO SER MET THR GLN PRO TYR MET TYR ASP
SEQRES  32 A  868  VAL ILE ASP THR LYS ARG GLY SER ARG LYS ALA TYR THR
SEQRES  33 A  868  GLU ALA LEU ILE GLY ARG GLY ASP ILE SER MET LYS GLU
SEQRES  34 A  868  ALA GLU ASP ALA LEU ARG ASP TYR GLN GLY GLN LEU GLU
SEQRES  35 A  868  ARG VAL PHE ASN GLU VAL ARG GLU LEU GLU LYS HIS GLU
SEQRES  36 A  868  ILE GLU PRO SER GLU SER VAL GLU ALA ASP GLN GLN ILE
SEQRES  37 A  868  PRO SER LYS LEU ALA THR ALA VAL ASP LYS ALA MET LEU
SEQRES  38 A  868  GLN ARG ILE GLY ASP ALA HIS LEU ALA LEU PRO GLU GLY
SEQRES  39 A  868  PHE THR VAL HIS PRO ARG VAL ARG PRO VAL LEU GLU LYS
SEQRES  40 A  868  ARG ARG GLU MET ALA TYR GLU GLY ARG ILE ASP TRP ALA
SEQRES  41 A  868  PHE ALA GLU LEU LEU ALA LEU GLY SER LEU ILE ALA GLU
SEQRES  42 A  868  GLY LYS LEU VAL ARG LEU SER GLY GLN ASP THR GLN ARG
SEQRES  43 A  868  GLY THR PHE THR GLN ARG HIS ALA VAL ILE VAL ASP ARG
SEQRES  44 A  868  LYS THR GLY GLU GLU PHE THR PRO LEU GLN LEU LEU ALA
SEQRES  45 A  868  THR ASN PRO ASP GLY THR PRO THR GLY GLY LYS PHE LEU
SEQRES  46 A  868  VAL TYR ASN SER ALA LEU SER GLU PHE ALA ALA VAL GLY
SEQRES  47 A  868  PHE GLU TYR GLY TYR SER VAL GLY ASN PRO ASP ALA MET
SEQRES  48 A  868  VAL LEU TRP GLU ALA GLN PHE GLY ASP PHE VAL ASN GLY
SEQRES  49 A  868  ALA GLN SER ILE ILE ASP GLU PHE ILE SER SER GLY GLU
SEQRES  50 A  868  ALA LYS TRP GLY GLN LEU SER ASP VAL VAL LEU LEU LEU
SEQRES  51 A  868  PRO HIS GLY HIS GLU GLY GLN GLY PRO ASP HIS THR SER
SEQRES  52 A  868  GLY ARG ILE GLU ARG PHE LEU GLN LEU TRP ALA GLU GLY
SEQRES  53 A  868  SER MET THR ILE ALA MET PRO SER THR PRO ALA ASN TYR
SEQRES  54 A  868  PHE HIS LEU LEU ARG ARG HIS GLY LYS ASP GLY ILE GLN
SEQRES  55 A  868  ARG PRO LEU ILE VAL PHE THR PRO LYS SER MET LEU ARG
SEQRES  56 A  868  ASN LYS ALA ALA VAL SER ASP ILE ARG ASP PHE THR GLU
SEQRES  57 A  868  SER LYS PHE ARG SER VAL LEU GLU GLU PRO MET TYR THR
SEQRES  58 A  868  ASP GLY GLU GLY ASP ARG ASN LYS VAL THR ARG LEU LEU
SEQRES  59 A  868  LEU THR SER GLY LYS ILE TYR TYR GLU LEU ALA ALA ARG
SEQRES  60 A  868  LYS ALA LYS GLU ASN ARG GLU ASP VAL ALA ILE VAL ARG
SEQRES  61 A  868  ILE GLU GLN LEU ALA PRO LEU PRO ARG ARG ARG LEU ALA
SEQRES  62 A  868  GLU THR LEU ASP ARG TYR PRO ASN VAL LYS GLU LYS PHE
SEQRES  63 A  868  TRP VAL GLN GLU GLU PRO ALA ASN GLN GLY ALA TRP PRO
SEQRES  64 A  868  SER PHE GLY LEU THR LEU PRO GLU ILE LEU PRO ASP HIS
SEQRES  65 A  868  PHE THR GLY LEU LYS ARG ILE SER ARG ARG ALA MET SER
SEQRES  66 A  868  ALA PRO SER SER GLY SER SER LYS VAL HIS ALA VAL GLU
SEQRES  67 A  868  GLN GLN GLU ILE LEU ASP THR ALA PHE GLY
SEQRES   1 B  868  GLY ASP SER ILE GLU ASP LYS ASN ALA ARG VAL ILE GLU
SEQRES   2 B  868  LEU ILE ALA ALA TYR ARG ASN ARG GLY HIS LEU MET ALA
SEQRES   3 B  868  ASP ILE ASP PRO LEU ARG LEU ASP ASN THR ARG PHE ARG
SEQRES   4 B  868  SER HIS PRO ASP LEU ASP VAL ASN SER HIS GLY LEU THR
SEQRES   5 B  868  LEU TRP ASP LEU ASP ARG GLU PHE LYS VAL ASP GLY PHE
SEQRES   6 B  868  ALA GLY VAL GLN ARG LYS LYS LEU ARG ASP ILE LEU SER
SEQRES   7 B  868  VAL LEU ARG ASP ALA TYR CYS ARG HIS VAL GLY VAL GLU
SEQRES   8 B  868  TYR THR HIS ILE LEU GLU PRO GLU GLN GLN ARG TRP ILE
SEQRES   9 B  868  GLN GLU ARG VAL GLU THR LYS HIS ASP LYS PRO THR VAL
SEQRES  10 B  868  ALA GLU GLN LYS TYR ILE LEU SER LYS LEU ASN ALA ALA
SEQRES  11 B  868  GLU ALA PHE GLU THR PHE LEU GLN THR LYS TYR VAL GLY
SEQRES  12 B  868  GLN LYS ARG PHE SER LEU GLU GLY ALA GLU THR VAL ILE
SEQRES  13 B  868  PRO MET MET ASP ALA VAL ILE ASP GLN CYS ALA GLU HIS
SEQRES  14 B  868  GLY LEU ASP GLU VAL VAL ILE ALA MET PRO HIS ARG GLY
SEQRES  15 B  868  ARG LEU ASN VAL LEU ALA ASN ILE VAL GLY LYS PRO TYR
SEQRES  16 B  868  SER GLN ILE PHE SER GLU PHE GLU GLY ASN LEU ASN PRO
SEQRES  17 B  868  SER GLN ALA HIS GLY SER GLY ASP VAL LYS TYR HIS LEU
SEQRES  18 B  868  GLY ALA THR GLY THR TYR ILE GLN MET PHE GLY ASP ASN
SEQRES  19 B  868  ASP ILE GLU VAL SER LEU THR ALA ASN PRO SER HIS LEU
SEQRES  20 B  868  GLU ALA VAL ASP PRO VAL LEU GLU GLY LEU VAL ARG ALA
SEQRES  21 B  868  LYS GLN ASP LEU LEU ASP THR GLY GLU GLU GLY SER ASP
SEQRES  22 B  868  ASN ARG PHE SER VAL VAL PRO LEU MET LEU HIS GLY ASP
SEQRES  23 B  868  ALA ALA PHE ALA GLY GLN GLY VAL VAL ALA GLU THR LEU
SEQRES  24 B  868  ASN LEU ALA LEU LEU ARG GLY TYR ARG THR GLY GLY THR
SEQRES  25 B  868  ILE HIS ILE VAL VAL ASN ASN GLN ILE GLY PHE THR THR
SEQRES  26 B  868  ALA PRO THR ASP SER ARG SER SER GLU TYR CYS THR ASP
SEQRES  27 B  868  VAL ALA LYS MET ILE GLY ALA PRO ILE PHE HIS VAL ASN
SEQRES  28 B  868  GLY ASP ASP PRO GLU ALA CYS ALA TRP VAL ALA ARG LEU
SEQRES  29 B  868  ALA VAL ASP PHE ARG GLN ALA PHE LYS LYS ASP VAL VAL
SEQRES  30 B  868  ILE ASP MET LEU CYS TYR ARG ARG ARG GLY HIS ASN GLU
SEQRES  31 B  868  GLY ASP ASP PRO SER MET THR GLN PRO TYR MET TYR ASP
SEQRES  32 B  868  VAL ILE ASP THR LYS ARG GLY SER ARG LYS ALA TYR THR
SEQRES  33 B  868  GLU ALA LEU ILE GLY ARG GLY ASP ILE SER MET LYS GLU
SEQRES  34 B  868  ALA GLU ASP ALA LEU ARG ASP TYR GLN GLY GLN LEU GLU
SEQRES  35 B  868  ARG VAL PHE ASN GLU VAL ARG GLU LEU GLU LYS HIS GLU
SEQRES  36 B  868  ILE GLU PRO SER GLU SER VAL GLU ALA ASP GLN GLN ILE
SEQRES  37 B  868  PRO SER LYS LEU ALA THR ALA VAL ASP LYS ALA MET LEU
SEQRES  38 B  868  GLN ARG ILE GLY ASP ALA HIS LEU ALA LEU PRO GLU GLY
SEQRES  39 B  868  PHE THR VAL HIS PRO ARG VAL ARG PRO VAL LEU GLU LYS
SEQRES  40 B  868  ARG ARG GLU MET ALA TYR GLU GLY ARG ILE ASP TRP ALA
SEQRES  41 B  868  PHE ALA GLU LEU LEU ALA LEU GLY SER LEU ILE ALA GLU
SEQRES  42 B  868  GLY LYS LEU VAL ARG LEU SER GLY GLN ASP THR GLN ARG
SEQRES  43 B  868  GLY THR PHE THR GLN ARG HIS ALA VAL ILE VAL ASP ARG
SEQRES  44 B  868  LYS THR GLY GLU GLU PHE THR PRO LEU GLN LEU LEU ALA
SEQRES  45 B  868  THR ASN PRO ASP GLY THR PRO THR GLY GLY LYS PHE LEU
SEQRES  46 B  868  VAL TYR ASN SER ALA LEU SER GLU PHE ALA ALA VAL GLY
SEQRES  47 B  868  PHE GLU TYR GLY TYR SER VAL GLY ASN PRO ASP ALA MET
SEQRES  48 B  868  VAL LEU TRP GLU ALA GLN PHE GLY ASP PHE VAL ASN GLY
SEQRES  49 B  868  ALA GLN SER ILE ILE ASP GLU PHE ILE SER SER GLY GLU
SEQRES  50 B  868  ALA LYS TRP GLY GLN LEU SER ASP VAL VAL LEU LEU LEU
SEQRES  51 B  868  PRO HIS GLY HIS GLU GLY GLN GLY PRO ASP HIS THR SER
SEQRES  52 B  868  GLY ARG ILE GLU ARG PHE LEU GLN LEU TRP ALA GLU GLY
SEQRES  53 B  868  SER MET THR ILE ALA MET PRO SER THR PRO ALA ASN TYR
SEQRES  54 B  868  PHE HIS LEU LEU ARG ARG HIS GLY LYS ASP GLY ILE GLN
SEQRES  55 B  868  ARG PRO LEU ILE VAL PHE THR PRO LYS SER MET LEU ARG
SEQRES  56 B  868  ASN LYS ALA ALA VAL SER ASP ILE ARG ASP PHE THR GLU
SEQRES  57 B  868  SER LYS PHE ARG SER VAL LEU GLU GLU PRO MET TYR THR
SEQRES  58 B  868  ASP GLY GLU GLY ASP ARG ASN LYS VAL THR ARG LEU LEU
SEQRES  59 B  868  LEU THR SER GLY LYS ILE TYR TYR GLU LEU ALA ALA ARG
SEQRES  60 B  868  LYS ALA LYS GLU ASN ARG GLU ASP VAL ALA ILE VAL ARG
SEQRES  61 B  868  ILE GLU GLN LEU ALA PRO LEU PRO ARG ARG ARG LEU ALA
SEQRES  62 B  868  GLU THR LEU ASP ARG TYR PRO ASN VAL LYS GLU LYS PHE
SEQRES  63 B  868  TRP VAL GLN GLU GLU PRO ALA ASN GLN GLY ALA TRP PRO
SEQRES  64 B  868  SER PHE GLY LEU THR LEU PRO GLU ILE LEU PRO ASP HIS
SEQRES  65 B  868  PHE THR GLY LEU LYS ARG ILE SER ARG ARG ALA MET SER
SEQRES  66 B  868  ALA PRO SER SER GLY SER SER LYS VAL HIS ALA VAL GLU
SEQRES  67 B  868  GLN GLN GLU ILE LEU ASP THR ALA PHE GLY
SEQRES   1 C  868  GLY ASP SER ILE GLU ASP LYS ASN ALA ARG VAL ILE GLU
SEQRES   2 C  868  LEU ILE ALA ALA TYR ARG ASN ARG GLY HIS LEU MET ALA
SEQRES   3 C  868  ASP ILE ASP PRO LEU ARG LEU ASP ASN THR ARG PHE ARG
SEQRES   4 C  868  SER HIS PRO ASP LEU ASP VAL ASN SER HIS GLY LEU THR
SEQRES   5 C  868  LEU TRP ASP LEU ASP ARG GLU PHE LYS VAL ASP GLY PHE
SEQRES   6 C  868  ALA GLY VAL GLN ARG LYS LYS LEU ARG ASP ILE LEU SER
SEQRES   7 C  868  VAL LEU ARG ASP ALA TYR CYS ARG HIS VAL GLY VAL GLU
SEQRES   8 C  868  TYR THR HIS ILE LEU GLU PRO GLU GLN GLN ARG TRP ILE
SEQRES   9 C  868  GLN GLU ARG VAL GLU THR LYS HIS ASP LYS PRO THR VAL
SEQRES  10 C  868  ALA GLU GLN LYS TYR ILE LEU SER LYS LEU ASN ALA ALA
SEQRES  11 C  868  GLU ALA PHE GLU THR PHE LEU GLN THR LYS TYR VAL GLY
SEQRES  12 C  868  GLN LYS ARG PHE SER LEU GLU GLY ALA GLU THR VAL ILE
SEQRES  13 C  868  PRO MET MET ASP ALA VAL ILE ASP GLN CYS ALA GLU HIS
SEQRES  14 C  868  GLY LEU ASP GLU VAL VAL ILE ALA MET PRO HIS ARG GLY
SEQRES  15 C  868  ARG LEU ASN VAL LEU ALA ASN ILE VAL GLY LYS PRO TYR
SEQRES  16 C  868  SER GLN ILE PHE SER GLU PHE GLU GLY ASN LEU ASN PRO
SEQRES  17 C  868  SER GLN ALA HIS GLY SER GLY ASP VAL LYS TYR HIS LEU
SEQRES  18 C  868  GLY ALA THR GLY THR TYR ILE GLN MET PHE GLY ASP ASN
SEQRES  19 C  868  ASP ILE GLU VAL SER LEU THR ALA ASN PRO SER HIS LEU
SEQRES  20 C  868  GLU ALA VAL ASP PRO VAL LEU GLU GLY LEU VAL ARG ALA
SEQRES  21 C  868  LYS GLN ASP LEU LEU ASP THR GLY GLU GLU GLY SER ASP
SEQRES  22 C  868  ASN ARG PHE SER VAL VAL PRO LEU MET LEU HIS GLY ASP
SEQRES  23 C  868  ALA ALA PHE ALA GLY GLN GLY VAL VAL ALA GLU THR LEU
SEQRES  24 C  868  ASN LEU ALA LEU LEU ARG GLY TYR ARG THR GLY GLY THR
SEQRES  25 C  868  ILE HIS ILE VAL VAL ASN ASN GLN ILE GLY PHE THR THR
SEQRES  26 C  868  ALA PRO THR ASP SER ARG SER SER GLU TYR CYS THR ASP
SEQRES  27 C  868  VAL ALA LYS MET ILE GLY ALA PRO ILE PHE HIS VAL ASN
SEQRES  28 C  868  GLY ASP ASP PRO GLU ALA CYS ALA TRP VAL ALA ARG LEU
SEQRES  29 C  868  ALA VAL ASP PHE ARG GLN ALA PHE LYS LYS ASP VAL VAL
SEQRES  30 C  868  ILE ASP MET LEU CYS TYR ARG ARG ARG GLY HIS ASN GLU
SEQRES  31 C  868  GLY ASP ASP PRO SER MET THR GLN PRO TYR MET TYR ASP
SEQRES  32 C  868  VAL ILE ASP THR LYS ARG GLY SER ARG LYS ALA TYR THR
SEQRES  33 C  868  GLU ALA LEU ILE GLY ARG GLY ASP ILE SER MET LYS GLU
SEQRES  34 C  868  ALA GLU ASP ALA LEU ARG ASP TYR GLN GLY GLN LEU GLU
SEQRES  35 C  868  ARG VAL PHE ASN GLU VAL ARG GLU LEU GLU LYS HIS GLU
SEQRES  36 C  868  ILE GLU PRO SER GLU SER VAL GLU ALA ASP GLN GLN ILE
SEQRES  37 C  868  PRO SER LYS LEU ALA THR ALA VAL ASP LYS ALA MET LEU
SEQRES  38 C  868  GLN ARG ILE GLY ASP ALA HIS LEU ALA LEU PRO GLU GLY
SEQRES  39 C  868  PHE THR VAL HIS PRO ARG VAL ARG PRO VAL LEU GLU LYS
SEQRES  40 C  868  ARG ARG GLU MET ALA TYR GLU GLY ARG ILE ASP TRP ALA
SEQRES  41 C  868  PHE ALA GLU LEU LEU ALA LEU GLY SER LEU ILE ALA GLU
SEQRES  42 C  868  GLY LYS LEU VAL ARG LEU SER GLY GLN ASP THR GLN ARG
SEQRES  43 C  868  GLY THR PHE THR GLN ARG HIS ALA VAL ILE VAL ASP ARG
SEQRES  44 C  868  LYS THR GLY GLU GLU PHE THR PRO LEU GLN LEU LEU ALA
SEQRES  45 C  868  THR ASN PRO ASP GLY THR PRO THR GLY GLY LYS PHE LEU
SEQRES  46 C  868  VAL TYR ASN SER ALA LEU SER GLU PHE ALA ALA VAL GLY
SEQRES  47 C  868  PHE GLU TYR GLY TYR SER VAL GLY ASN PRO ASP ALA MET
SEQRES  48 C  868  VAL LEU TRP GLU ALA GLN PHE GLY ASP PHE VAL ASN GLY
SEQRES  49 C  868  ALA GLN SER ILE ILE ASP GLU PHE ILE SER SER GLY GLU
SEQRES  50 C  868  ALA LYS TRP GLY GLN LEU SER ASP VAL VAL LEU LEU LEU
SEQRES  51 C  868  PRO HIS GLY HIS GLU GLY GLN GLY PRO ASP HIS THR SER
SEQRES  52 C  868  GLY ARG ILE GLU ARG PHE LEU GLN LEU TRP ALA GLU GLY
SEQRES  53 C  868  SER MET THR ILE ALA MET PRO SER THR PRO ALA ASN TYR
SEQRES  54 C  868  PHE HIS LEU LEU ARG ARG HIS GLY LYS ASP GLY ILE GLN
SEQRES  55 C  868  ARG PRO LEU ILE VAL PHE THR PRO LYS SER MET LEU ARG
SEQRES  56 C  868  ASN LYS ALA ALA VAL SER ASP ILE ARG ASP PHE THR GLU
SEQRES  57 C  868  SER LYS PHE ARG SER VAL LEU GLU GLU PRO MET TYR THR
SEQRES  58 C  868  ASP GLY GLU GLY ASP ARG ASN LYS VAL THR ARG LEU LEU
SEQRES  59 C  868  LEU THR SER GLY LYS ILE TYR TYR GLU LEU ALA ALA ARG
SEQRES  60 C  868  LYS ALA LYS GLU ASN ARG GLU ASP VAL ALA ILE VAL ARG
SEQRES  61 C  868  ILE GLU GLN LEU ALA PRO LEU PRO ARG ARG ARG LEU ALA
SEQRES  62 C  868  GLU THR LEU ASP ARG TYR PRO ASN VAL LYS GLU LYS PHE
SEQRES  63 C  868  TRP VAL GLN GLU GLU PRO ALA ASN GLN GLY ALA TRP PRO
SEQRES  64 C  868  SER PHE GLY LEU THR LEU PRO GLU ILE LEU PRO ASP HIS
SEQRES  65 C  868  PHE THR GLY LEU LYS ARG ILE SER ARG ARG ALA MET SER
SEQRES  66 C  868  ALA PRO SER SER GLY SER SER LYS VAL HIS ALA VAL GLU
SEQRES  67 C  868  GLN GLN GLU ILE LEU ASP THR ALA PHE GLY
SEQRES   1 D  868  GLY ASP SER ILE GLU ASP LYS ASN ALA ARG VAL ILE GLU
SEQRES   2 D  868  LEU ILE ALA ALA TYR ARG ASN ARG GLY HIS LEU MET ALA
SEQRES   3 D  868  ASP ILE ASP PRO LEU ARG LEU ASP ASN THR ARG PHE ARG
SEQRES   4 D  868  SER HIS PRO ASP LEU ASP VAL ASN SER HIS GLY LEU THR
SEQRES   5 D  868  LEU TRP ASP LEU ASP ARG GLU PHE LYS VAL ASP GLY PHE
SEQRES   6 D  868  ALA GLY VAL GLN ARG LYS LYS LEU ARG ASP ILE LEU SER
SEQRES   7 D  868  VAL LEU ARG ASP ALA TYR CYS ARG HIS VAL GLY VAL GLU
SEQRES   8 D  868  TYR THR HIS ILE LEU GLU PRO GLU GLN GLN ARG TRP ILE
SEQRES   9 D  868  GLN GLU ARG VAL GLU THR LYS HIS ASP LYS PRO THR VAL
SEQRES  10 D  868  ALA GLU GLN LYS TYR ILE LEU SER LYS LEU ASN ALA ALA
SEQRES  11 D  868  GLU ALA PHE GLU THR PHE LEU GLN THR LYS TYR VAL GLY
SEQRES  12 D  868  GLN LYS ARG PHE SER LEU GLU GLY ALA GLU THR VAL ILE
SEQRES  13 D  868  PRO MET MET ASP ALA VAL ILE ASP GLN CYS ALA GLU HIS
SEQRES  14 D  868  GLY LEU ASP GLU VAL VAL ILE ALA MET PRO HIS ARG GLY
SEQRES  15 D  868  ARG LEU ASN VAL LEU ALA ASN ILE VAL GLY LYS PRO TYR
SEQRES  16 D  868  SER GLN ILE PHE SER GLU PHE GLU GLY ASN LEU ASN PRO
SEQRES  17 D  868  SER GLN ALA HIS GLY SER GLY ASP VAL LYS TYR HIS LEU
SEQRES  18 D  868  GLY ALA THR GLY THR TYR ILE GLN MET PHE GLY ASP ASN
SEQRES  19 D  868  ASP ILE GLU VAL SER LEU THR ALA ASN PRO SER HIS LEU
SEQRES  20 D  868  GLU ALA VAL ASP PRO VAL LEU GLU GLY LEU VAL ARG ALA
SEQRES  21 D  868  LYS GLN ASP LEU LEU ASP THR GLY GLU GLU GLY SER ASP
SEQRES  22 D  868  ASN ARG PHE SER VAL VAL PRO LEU MET LEU HIS GLY ASP
SEQRES  23 D  868  ALA ALA PHE ALA GLY GLN GLY VAL VAL ALA GLU THR LEU
SEQRES  24 D  868  ASN LEU ALA LEU LEU ARG GLY TYR ARG THR GLY GLY THR
SEQRES  25 D  868  ILE HIS ILE VAL VAL ASN ASN GLN ILE GLY PHE THR THR
SEQRES  26 D  868  ALA PRO THR ASP SER ARG SER SER GLU TYR CYS THR ASP
SEQRES  27 D  868  VAL ALA LYS MET ILE GLY ALA PRO ILE PHE HIS VAL ASN
SEQRES  28 D  868  GLY ASP ASP PRO GLU ALA CYS ALA TRP VAL ALA ARG LEU
SEQRES  29 D  868  ALA VAL ASP PHE ARG GLN ALA PHE LYS LYS ASP VAL VAL
SEQRES  30 D  868  ILE ASP MET LEU CYS TYR ARG ARG ARG GLY HIS ASN GLU
SEQRES  31 D  868  GLY ASP ASP PRO SER MET THR GLN PRO TYR MET TYR ASP
SEQRES  32 D  868  VAL ILE ASP THR LYS ARG GLY SER ARG LYS ALA TYR THR
SEQRES  33 D  868  GLU ALA LEU ILE GLY ARG GLY ASP ILE SER MET LYS GLU
SEQRES  34 D  868  ALA GLU ASP ALA LEU ARG ASP TYR GLN GLY GLN LEU GLU
SEQRES  35 D  868  ARG VAL PHE ASN GLU VAL ARG GLU LEU GLU LYS HIS GLU
SEQRES  36 D  868  ILE GLU PRO SER GLU SER VAL GLU ALA ASP GLN GLN ILE
SEQRES  37 D  868  PRO SER LYS LEU ALA THR ALA VAL ASP LYS ALA MET LEU
SEQRES  38 D  868  GLN ARG ILE GLY ASP ALA HIS LEU ALA LEU PRO GLU GLY
SEQRES  39 D  868  PHE THR VAL HIS PRO ARG VAL ARG PRO VAL LEU GLU LYS
SEQRES  40 D  868  ARG ARG GLU MET ALA TYR GLU GLY ARG ILE ASP TRP ALA
SEQRES  41 D  868  PHE ALA GLU LEU LEU ALA LEU GLY SER LEU ILE ALA GLU
SEQRES  42 D  868  GLY LYS LEU VAL ARG LEU SER GLY GLN ASP THR GLN ARG
SEQRES  43 D  868  GLY THR PHE THR GLN ARG HIS ALA VAL ILE VAL ASP ARG
SEQRES  44 D  868  LYS THR GLY GLU GLU PHE THR PRO LEU GLN LEU LEU ALA
SEQRES  45 D  868  THR ASN PRO ASP GLY THR PRO THR GLY GLY LYS PHE LEU
SEQRES  46 D  868  VAL TYR ASN SER ALA LEU SER GLU PHE ALA ALA VAL GLY
SEQRES  47 D  868  PHE GLU TYR GLY TYR SER VAL GLY ASN PRO ASP ALA MET
SEQRES  48 D  868  VAL LEU TRP GLU ALA GLN PHE GLY ASP PHE VAL ASN GLY
SEQRES  49 D  868  ALA GLN SER ILE ILE ASP GLU PHE ILE SER SER GLY GLU
SEQRES  50 D  868  ALA LYS TRP GLY GLN LEU SER ASP VAL VAL LEU LEU LEU
SEQRES  51 D  868  PRO HIS GLY HIS GLU GLY GLN GLY PRO ASP HIS THR SER
SEQRES  52 D  868  GLY ARG ILE GLU ARG PHE LEU GLN LEU TRP ALA GLU GLY
SEQRES  53 D  868  SER MET THR ILE ALA MET PRO SER THR PRO ALA ASN TYR
SEQRES  54 D  868  PHE HIS LEU LEU ARG ARG HIS GLY LYS ASP GLY ILE GLN
SEQRES  55 D  868  ARG PRO LEU ILE VAL PHE THR PRO LYS SER MET LEU ARG
SEQRES  56 D  868  ASN LYS ALA ALA VAL SER ASP ILE ARG ASP PHE THR GLU
SEQRES  57 D  868  SER LYS PHE ARG SER VAL LEU GLU GLU PRO MET TYR THR
SEQRES  58 D  868  ASP GLY GLU GLY ASP ARG ASN LYS VAL THR ARG LEU LEU
SEQRES  59 D  868  LEU THR SER GLY LYS ILE TYR TYR GLU LEU ALA ALA ARG
SEQRES  60 D  868  LYS ALA LYS GLU ASN ARG GLU ASP VAL ALA ILE VAL ARG
SEQRES  61 D  868  ILE GLU GLN LEU ALA PRO LEU PRO ARG ARG ARG LEU ALA
SEQRES  62 D  868  GLU THR LEU ASP ARG TYR PRO ASN VAL LYS GLU LYS PHE
SEQRES  63 D  868  TRP VAL GLN GLU GLU PRO ALA ASN GLN GLY ALA TRP PRO
SEQRES  64 D  868  SER PHE GLY LEU THR LEU PRO GLU ILE LEU PRO ASP HIS
SEQRES  65 D  868  PHE THR GLY LEU LYS ARG ILE SER ARG ARG ALA MET SER
SEQRES  66 D  868  ALA PRO SER SER GLY SER SER LYS VAL HIS ALA VAL GLU
SEQRES  67 D  868  GLN GLN GLU ILE LEU ASP THR ALA PHE GLY
HET    TD7  A2001      33
HET     MG  A2002       1
HET     CA  A2003       1
HET    TD7  B2001      33
HET     MG  B2002       1
HET     CA  B2003       1
HET    TD7  C2001      33
HET     MG  C2002       1
HET     CA  C2003       1
HET    TD7  D2001      33
HET     MG  D2002       1
HET     CA  D2003       1
HETNAM     TD7 (4E)-4-{3-[(4-AMINO-2-METHYLPYRIMIDIN-5-YL)
HETNAM   2 TD7  METHYL]-5-(2-{[(S)-HYDROXY(PHOSPHONOOXY)
HETNAM   3 TD7  PHOSPHORYL]OXY}ETHYL)-4-METHYL-1,3-THIAZOL-2(3H)-
HETNAM   4 TD7  YLIDENE}-4-HYDROXYBUTANOIC ACID
HETNAM      MG MAGNESIUM ION
HETNAM      CA CALCIUM ION
FORMUL   5  TD7    4(C16 H24 N4 O10 P2 S)
FORMUL   6   MG    4(MG 2+)
FORMUL   7   CA    4(CA 2+)
FORMUL   8  HOH   *730(H2 O)
HELIX    1   1 SER A  362  GLY A  381  1                                  20
HELIX    2   2 HIS A  382  MET A  384  5                                   3
HELIX    3   3 TRP A  413  ASP A  416  5                                   4
HELIX    4   4 LEU A  432  CYS A  444  1                                  13
HELIX    5   5 GLU A  456  GLU A  468  1                                  13
HELIX    6   6 THR A  475  TYR A  500  1                                  26
HELIX    7   7 THR A  513  HIS A  528  1                                  16
HELIX    8   8 GLY A  541  ILE A  549  1                                   9
HELIX    9   9 PRO A  553  GLU A  562  1                                  10
HELIX   10  10 ASN A  566  HIS A  571  1                                   6
HELIX   11  11 VAL A  576  LEU A  580  5                                   5
HELIX   12  12 VAL A  609  LEU A  624  1                                  16
HELIX   13  13 ASP A  645  GLN A  651  1                                   7
HELIX   14  14 GLN A  651  ASN A  659  1                                   9
HELIX   15  15 ALA A  685  ARG A  690  1                                   6
HELIX   16  16 THR A  696  GLY A  703  5                                   8
HELIX   17  17 ASP A  713  LYS A  732  1                                  20
HELIX   18  18 ASP A  752  THR A  756  5                                   5
HELIX   19  19 GLN A  757  ASP A  765  1                                   9
HELIX   20  20 GLY A  769  ARG A  781  1                                  13
HELIX   21  21 SER A  785  GLU A  809  1                                  25
HELIX   22  22 VAL A  821  GLN A  825  5                                   5
HELIX   23  23 ASP A  836  HIS A  847  1                                  12
HELIX   24  24 VAL A  860  GLY A  874  1                                  15
HELIX   25  25 ASP A  877  GLU A  892  1                                  16
HELIX   26  26 THR A  925  ALA A  931  5                                   7
HELIX   27  27 GLU A  952  ASN A  966  1                                  15
HELIX   28  28 PHE A  977  GLY A  983  5                                   7
HELIX   29  29 ALA A  984  PHE A  991  1                                   8
HELIX   30  30 SER A  994  GLY A 1000  1                                   7
HELIX   31  31 ARG A 1024  TRP A 1032  1                                   9
HELIX   32  32 THR A 1044  ASP A 1058  1                                  15
HELIX   33  33 LYS A 1070  ASN A 1075  5                                   6
HELIX   34  34 ASP A 1081  GLU A 1087  1                                   7
HELIX   35  35 GLU A 1096  ASP A 1101  1                                   6
HELIX   36  36 LYS A 1118  ASN A 1131  1                                  14
HELIX   37  37 PRO A 1147  ASP A 1156  1                                  10
HELIX   38  38 ALA A 1176  THR A 1193  1                                  18
HELIX   39  39 SER A 1210  PHE A 1226  1                                  17
HELIX   40  40 ASP B  365  GLY B  381  1                                  17
HELIX   41  41 HIS B  382  MET B  384  5                                   3
HELIX   42  42 LEU B  432  CYS B  444  1                                  13
HELIX   43  43 GLU B  456  GLU B  468  1                                  13
HELIX   44  44 THR B  475  TYR B  500  1                                  26
HELIX   45  45 THR B  513  HIS B  528  1                                  16
HELIX   46  46 GLY B  541  ILE B  549  1                                   9
HELIX   47  47 PRO B  553  GLU B  562  1                                  10
HELIX   48  48 VAL B  576  LEU B  580  5                                   5
HELIX   49  49 VAL B  609  LEU B  624  1                                  16
HELIX   50  50 ASP B  645  GLN B  651  1                                   7
HELIX   51  51 GLN B  651  ASN B  659  1                                   9
HELIX   52  52 ALA B  685  ARG B  690  1                                   6
HELIX   53  53 THR B  696  GLY B  703  5                                   8
HELIX   54  54 ASP B  713  LYS B  732  1                                  20
HELIX   55  55 ASP B  752  THR B  756  5                                   5
HELIX   56  56 GLN B  757  ASP B  765  1                                   9
HELIX   57  57 GLY B  769  ARG B  781  1                                  13
HELIX   58  58 SER B  785  GLU B  809  1                                  25
HELIX   59  59 VAL B  821  GLN B  825  5                                   5
HELIX   60  60 ASP B  836  HIS B  847  1                                  12
HELIX   61  61 VAL B  860  GLY B  874  1                                  15
HELIX   62  62 ASP B  877  GLU B  892  1                                  16
HELIX   63  63 THR B  925  ALA B  931  5                                   7
HELIX   64  64 GLU B  952  ASN B  966  1                                  15
HELIX   65  65 PHE B  977  GLY B  983  5                                   7
HELIX   66  66 ALA B  984  PHE B  991  1                                   8
HELIX   67  67 SER B  994  GLY B 1000  1                                   7
HELIX   68  68 ARG B 1024  TRP B 1032  1                                   9
HELIX   69  69 THR B 1044  ASP B 1058  1                                  15
HELIX   70  70 LYS B 1070  ASN B 1075  5                                   6
HELIX   71  71 ILE B 1082  GLU B 1087  1                                   6
HELIX   72  72 GLU B 1096  ASP B 1101  1                                   6
HELIX   73  73 ASP B 1105  VAL B 1109  5                                   5
HELIX   74  74 LYS B 1118  ASN B 1131  1                                  14
HELIX   75  75 PRO B 1147  ASP B 1156  1                                  10
HELIX   76  76 ALA B 1176  LEU B 1188  1                                  13
HELIX   77  77 LEU B 1188  THR B 1193  1                                   6
HELIX   78  78 SER B 1210  PHE B 1226  1                                  17
HELIX   79  79 ASP C  365  GLY C  381  1                                  17
HELIX   80  80 HIS C  382  MET C  384  5                                   3
HELIX   81  81 ASP C  393  ARG C  398  5                                   6
HELIX   82  82 TRP C  413  ASP C  416  5                                   4
HELIX   83  83 LEU C  432  CYS C  444  1                                  13
HELIX   84  84 GLU C  456  GLU C  468  1                                  13
HELIX   85  85 THR C  475  TYR C  500  1                                  26
HELIX   86  86 THR C  513  HIS C  528  1                                  16
HELIX   87  87 GLY C  541  ILE C  549  1                                   9
HELIX   88  88 PRO C  553  GLY C  563  1                                  11
HELIX   89  89 ASN C  566  HIS C  571  1                                   6
HELIX   90  90 VAL C  576  LEU C  580  5                                   5
HELIX   91  91 VAL C  609  ASP C  625  1                                  17
HELIX   92  92 ASP C  645  GLN C  651  1                                   7
HELIX   93  93 GLN C  651  ASN C  659  1                                   9
HELIX   94  94 ALA C  685  ARG C  690  1                                   6
HELIX   95  95 THR C  696  GLY C  703  5                                   8
HELIX   96  96 ASP C  713  LYS C  732  1                                  20
HELIX   97  97 ASP C  752  THR C  756  5                                   5
HELIX   98  98 GLN C  757  ASP C  765  1                                   9
HELIX   99  99 GLY C  769  ARG C  781  1                                  13
HELIX  100 100 SER C  785  GLU C  809  1                                  25
HELIX  101 101 VAL C  821  GLN C  825  5                                   5
HELIX  102 102 ASP C  836  HIS C  847  1                                  12
HELIX  103 103 VAL C  860  GLY C  874  1                                  15
HELIX  104 104 ASP C  877  GLU C  892  1                                  16
HELIX  105 105 THR C  925  ALA C  931  5                                   7
HELIX  106 106 GLU C  952  ASN C  966  1                                  15
HELIX  107 107 PHE C  977  GLY C  983  5                                   7
HELIX  108 108 ALA C  984  PHE C  991  1                                   8
HELIX  109 109 SER C  994  GLY C 1000  1                                   7
HELIX  110 110 ARG C 1024  TRP C 1032  1                                   9
HELIX  111 111 THR C 1044  ASP C 1058  1                                  15
HELIX  112 112 LYS C 1070  ASN C 1075  5                                   6
HELIX  113 113 ASP C 1081  GLU C 1087  1                                   7
HELIX  114 114 GLU C 1096  ASP C 1101  1                                   6
HELIX  115 115 ASP C 1105  VAL C 1109  5                                   5
HELIX  116 116 LYS C 1118  ASN C 1131  1                                  14
HELIX  117 117 PRO C 1147  ASP C 1156  1                                  10
HELIX  118 118 ALA C 1176  THR C 1193  1                                  18
HELIX  119 119 SER C 1210  PHE C 1226  1                                  17
HELIX  120 120 SER D  362  GLY D  381  1                                  20
HELIX  121 121 HIS D  382  MET D  384  5                                   3
HELIX  122 122 ASP D  393  ARG D  398  5                                   6
HELIX  123 123 TRP D  413  ASP D  416  5                                   4
HELIX  124 124 LEU D  432  CYS D  444  1                                  13
HELIX  125 125 GLU D  456  GLU D  468  1                                  13
HELIX  126 126 THR D  475  TYR D  500  1                                  26
HELIX  127 127 THR D  513  HIS D  528  1                                  16
HELIX  128 128 GLY D  541  ILE D  549  1                                   9
HELIX  129 129 PRO D  553  GLU D  562  1                                  10
HELIX  130 130 ASN D  566  HIS D  571  1                                   6
HELIX  131 131 VAL D  576  LEU D  580  5                                   5
HELIX  132 132 VAL D  609  LEU D  624  1                                  16
HELIX  133 133 ASP D  645  GLN D  651  1                                   7
HELIX  134 134 GLN D  651  ASN D  659  1                                   9
HELIX  135 135 ALA D  685  ARG D  690  1                                   6
HELIX  136 136 THR D  696  GLY D  703  5                                   8
HELIX  137 137 ASP D  713  LYS D  732  1                                  20
HELIX  138 138 ASP D  752  THR D  756  5                                   5
HELIX  139 139 GLN D  757  ASP D  765  1                                   9
HELIX  140 140 GLY D  769  ARG D  781  1                                  13
HELIX  141 141 SER D  785  GLU D  809  1                                  25
HELIX  142 142 VAL D  821  GLN D  825  5                                   5
HELIX  143 143 ASP D  836  HIS D  847  1                                  12
HELIX  144 144 VAL D  860  GLY D  874  1                                  15
HELIX  145 145 ASP D  877  GLU D  892  1                                  16
HELIX  146 146 THR D  925  ALA D  931  5                                   7
HELIX  147 147 GLU D  952  ASN D  966  1                                  15
HELIX  148 148 PHE D  977  GLY D  983  5                                   7
HELIX  149 149 ALA D  984  PHE D  991  1                                   8
HELIX  150 150 SER D  994  GLY D 1000  1                                   7
HELIX  151 151 ARG D 1024  TRP D 1032  1                                   9
HELIX  152 152 THR D 1044  ASP D 1058  1                                  15
HELIX  153 153 LYS D 1070  ASN D 1075  5                                   6
HELIX  154 154 ASP D 1081  GLU D 1087  1                                   7
HELIX  155 155 GLU D 1096  ASP D 1101  1                                   6
HELIX  156 156 ASP D 1105  VAL D 1109  5                                   5
HELIX  157 157 LYS D 1118  ASN D 1131  1                                  14
HELIX  158 158 PRO D 1147  ASP D 1156  1                                  10
HELIX  159 159 ALA D 1176  THR D 1193  1                                  18
HELIX  160 160 SER D 1210  PHE D 1226  1                                  17
SHEET    1  AA 2 GLU A 418  VAL A 421  0
SHEET    2  AA 2 GLN A 428  LYS A 431 -1  O  GLN A 428   N  VAL A 421
SHEET    1  AB 8 VAL A 447  GLU A 450  0
SHEET    2  AB 8 ILE A 706  ASN A 710 -1  O  ILE A 706   N  GLU A 450
SHEET    3  AB 8 VAL A 735  LEU A 740  1  O  VAL A 736   N  PHE A 707
SHEET    4  AB 8 ILE A 672  ASN A 677  1  O  HIS A 673   N  ILE A 737
SHEET    5  AB 8 VAL A 637  GLY A 644  1  O  PRO A 639   N  ILE A 672
SHEET    6  AB 8 GLU A 532  ALA A 536  1  O  GLU A 532   N  VAL A 638
SHEET    7  AB 8 ASP A 594  LEU A 599  1  O  GLU A 596   N  VAL A 533
SHEET    8  AB 8 ALA A 582  ILE A 587 -1  O  ALA A 582   N  LEU A 599
SHEET    1  AC 7 LYS A 942  ASN A 947  0
SHEET    2  AC 7 LEU A 895  GLY A 900  1  O  VAL A 896   N  LEU A 944
SHEET    3  AC 7 MET A 970  GLU A 974  1  O  MET A 970   N  ARG A 897
SHEET    4  AC 7 VAL A1006  PRO A1010  1  O  VAL A1006   N  TRP A 973
SHEET    5  AC 7 LEU A1064  THR A1068  1  O  LEU A1064   N  LEU A1007
SHEET    6  AC 7 THR A1038  ALA A1040  1  O  THR A1038   N  ILE A1065
SHEET    7  AC 7 GLN A1142  ALA A1144 -1  N  LEU A1143   O  ILE A1039
SHEET    1  AD 2 ILE A 915  VAL A 916  0
SHEET    2  AD 2 GLU A 923  PHE A 924 -1  O  PHE A 924   N  ILE A 915
SHEET    1  AE 5 VAL A1093  LEU A1094  0
SHEET    2  AE 5 VAL A1135  ILE A1140 -1  O  ARG A1139   N  LEU A1094
SHEET    3  AE 5 ARG A1111  THR A1115  1  O  ARG A1111   N  ALA A1136
SHEET    4  AE 5 GLU A1163  PRO A1171  1  O  GLU A1163   N  LEU A1112
SHEET    5  AE 5 LYS A1196  ARG A1200  1  O  LYS A1196   N  TRP A1166
SHEET    1  BA 2 GLU B 418  VAL B 421  0
SHEET    2  BA 2 GLN B 428  LYS B 431 -1  O  GLN B 428   N  VAL B 421
SHEET    1  BB 8 VAL B 447  GLU B 450  0
SHEET    2  BB 8 ILE B 706  ASN B 710 -1  O  ILE B 706   N  GLU B 450
SHEET    3  BB 8 VAL B 735  LEU B 740  1  O  VAL B 736   N  PHE B 707
SHEET    4  BB 8 ILE B 672  ASN B 677  1  O  HIS B 673   N  ILE B 737
SHEET    5  BB 8 VAL B 637  GLY B 644  1  O  PRO B 639   N  ILE B 672
SHEET    6  BB 8 GLU B 532  ALA B 536  1  O  GLU B 532   N  VAL B 638
SHEET    7  BB 8 ASP B 594  LEU B 599  1  O  GLU B 596   N  VAL B 533
SHEET    8  BB 8 ALA B 582  ILE B 587 -1  O  ALA B 582   N  LEU B 599
SHEET    1  BC 7 LYS B 942  ASN B 947  0
SHEET    2  BC 7 LEU B 895  GLY B 900  1  O  VAL B 896   N  LEU B 944
SHEET    3  BC 7 MET B 970  GLU B 974  1  O  MET B 970   N  ARG B 897
SHEET    4  BC 7 VAL B1006  PRO B1010  1  O  VAL B1006   N  TRP B 973
SHEET    5  BC 7 LEU B1064  THR B1068  1  O  LEU B1064   N  LEU B1007
SHEET    6  BC 7 THR B1038  ALA B1040  1  O  THR B1038   N  ILE B1065
SHEET    7  BC 7 GLN B1142  ALA B1144 -1  N  LEU B1143   O  ILE B1039
SHEET    1  BD 2 ILE B 915  VAL B 916  0
SHEET    2  BD 2 GLU B 923  PHE B 924 -1  O  PHE B 924   N  ILE B 915
SHEET    1  BE 5 VAL B1093  LEU B1094  0
SHEET    2  BE 5 VAL B1135  ILE B1140 -1  O  ARG B1139   N  LEU B1094
SHEET    3  BE 5 ARG B1111  THR B1115  1  O  ARG B1111   N  ALA B1136
SHEET    4  BE 5 GLU B1163  PRO B1171  1  O  GLU B1163   N  LEU B1112
SHEET    5  BE 5 LYS B1196  ARG B1200  1  O  LYS B1196   N  TRP B1166
SHEET    1  CA 2 GLU C 418  PHE C 419  0
SHEET    2  CA 2 LYS C 430  LYS C 431 -1  O  LYS C 430   N  PHE C 419
SHEET    1  CB 8 VAL C 447  GLU C 450  0
SHEET    2  CB 8 ILE C 706  ASN C 710 -1  O  ILE C 706   N  GLU C 450
SHEET    3  CB 8 VAL C 735  LEU C 740  1  O  VAL C 736   N  PHE C 707
SHEET    4  CB 8 ILE C 672  ASN C 677  1  O  HIS C 673   N  ILE C 737
SHEET    5  CB 8 VAL C 637  GLY C 644  1  O  PRO C 639   N  ILE C 672
SHEET    6  CB 8 GLU C 532  ALA C 536  1  O  GLU C 532   N  VAL C 638
SHEET    7  CB 8 ASP C 594  LEU C 599  1  O  GLU C 596   N  VAL C 533
SHEET    8  CB 8 ALA C 582  ILE C 587 -1  O  ALA C 582   N  LEU C 599
SHEET    1  CC 7 LYS C 942  ASN C 947  0
SHEET    2  CC 7 LEU C 895  GLY C 900  1  O  VAL C 896   N  LEU C 944
SHEET    3  CC 7 MET C 970  GLU C 974  1  O  MET C 970   N  ARG C 897
SHEET    4  CC 7 VAL C1006  PRO C1010  1  O  VAL C1006   N  TRP C 973
SHEET    5  CC 7 LEU C1064  THR C1068  1  O  LEU C1064   N  LEU C1007
SHEET    6  CC 7 THR C1038  ALA C1040  1  O  THR C1038   N  ILE C1065
SHEET    7  CC 7 GLN C1142  ALA C1144 -1  N  LEU C1143   O  ILE C1039
SHEET    1  CD 2 ILE C 915  VAL C 916  0
SHEET    2  CD 2 GLU C 923  PHE C 924 -1  O  PHE C 924   N  ILE C 915
SHEET    1  CE 5 VAL C1093  LEU C1094  0
SHEET    2  CE 5 VAL C1135  ILE C1140 -1  O  ARG C1139   N  LEU C1094
SHEET    3  CE 5 ARG C1111  THR C1115  1  O  ARG C1111   N  ALA C1136
SHEET    4  CE 5 GLU C1163  PRO C1171  1  O  GLU C1163   N  LEU C1112
SHEET    5  CE 5 LYS C1196  ARG C1200  1  O  LYS C1196   N  TRP C1166
SHEET    1  DA 2 GLU D 418  ASP D 422  0
SHEET    2  DA 2 VAL D 427  LYS D 431 -1  O  GLN D 428   N  VAL D 421
SHEET    1  DB 8 VAL D 447  GLU D 450  0
SHEET    2  DB 8 ILE D 706  ASN D 710 -1  O  ILE D 706   N  GLU D 450
SHEET    3  DB 8 VAL D 735  LEU D 740  1  O  VAL D 736   N  PHE D 707
SHEET    4  DB 8 ILE D 672  ASN D 677  1  O  HIS D 673   N  ILE D 737
SHEET    5  DB 8 VAL D 637  GLY D 644  1  O  PRO D 639   N  ILE D 672
SHEET    6  DB 8 GLU D 532  ALA D 536  1  O  GLU D 532   N  VAL D 638
SHEET    7  DB 8 ASP D 594  LEU D 599  1  O  GLU D 596   N  VAL D 533
SHEET    8  DB 8 ALA D 582  ILE D 587 -1  O  ALA D 582   N  LEU D 599
SHEET    1  DC 7 LYS D 942  ASN D 947  0
SHEET    2  DC 7 LEU D 895  GLY D 900  1  O  VAL D 896   N  LEU D 944
SHEET    3  DC 7 MET D 970  GLU D 974  1  O  MET D 970   N  ARG D 897
SHEET    4  DC 7 VAL D1006  PRO D1010  1  O  VAL D1006   N  TRP D 973
SHEET    5  DC 7 LEU D1064  THR D1068  1  O  LEU D1064   N  LEU D1007
SHEET    6  DC 7 THR D1038  ALA D1040  1  O  THR D1038   N  ILE D1065
SHEET    7  DC 7 GLN D1142  ALA D1144 -1  N  LEU D1143   O  ILE D1039
SHEET    1  DD 2 ILE D 915  VAL D 916  0
SHEET    2  DD 2 GLU D 923  PHE D 924 -1  O  PHE D 924   N  ILE D 915
SHEET    1  DE 5 VAL D1093  LEU D1094  0
SHEET    2  DE 5 VAL D1135  ILE D1140 -1  O  ARG D1139   N  LEU D1094
SHEET    3  DE 5 ARG D1111  THR D1115  1  O  ARG D1111   N  ALA D1136
SHEET    4  DE 5 GLU D1163  PRO D1171  1  O  GLU D1163   N  LEU D1112
SHEET    5  DE 5 LYS D1196  ARG D1200  1  O  LYS D1196   N  TRP D1166
LINK         O3B TD7 A2001                MG    MG A2002     1555   1555  2.01
LINK         O2A TD7 A2001                MG    MG A2002     1555   1555  1.99
LINK        MG    MG A2002                 OD1 ASP A 645     1555   1555  2.14
LINK        MG    MG A2002                 OD1 ASN A 678     1555   1555  1.99
LINK        MG    MG A2002                 O   ILE A 680     1555   1555  2.09
LINK        MG    MG A2002                 O   HOH A3047     1555   1555  2.22
LINK        CA    CA A2003                 OD2 ASP A1004     1555   1555  2.46
LINK        CA    CA A2003                 O   HOH A3154     1555   1555  2.40
LINK        CA    CA A2003                 OD1 ASP A1004     1555   1555  2.55
LINK        CA    CA A2003                 OD1 ASP A1058     1555   1555  2.45
LINK        CA    CA A2003                 O   ILE A1060     1555   1555  2.30
LINK        CA    CA A2003                 O   HOH A3153     1555   1555  2.61
LINK        CA    CA A2003                 O   HIS A1055     1555   1555  2.38
LINK         O3B TD7 B2001                MG    MG B2002     1555   1555  2.20
LINK         O2A TD7 B2001                MG    MG B2002     1555   1555  1.94
LINK        MG    MG B2002                 O   HOH B3050     1555   1555  2.15
LINK        MG    MG B2002                 OD1 ASN B 678     1555   1555  2.02
LINK        MG    MG B2002                 O   ILE B 680     1555   1555  2.12
LINK        MG    MG B2002                 OD1 ASP B 645     1555   1555  2.07
LINK        CA    CA B2003                 O   HOH B3127     1555   1555  2.33
LINK        CA    CA B2003                 O   ILE B1060     1555   1555  2.27
LINK        CA    CA B2003                 O   HOH B3128     1555   1555  2.43
LINK        CA    CA B2003                 OD1 ASP B1004     1555   1555  2.56
LINK        CA    CA B2003                 OD1 ASP B1058     1555   1555  2.43
LINK        CA    CA B2003                 O   HIS B1055     1555   1555  2.41
LINK        CA    CA B2003                 OD2 ASP B1004     1555   1555  2.43
LINK         O3B TD7 C2001                MG    MG C2002     1555   1555  2.05
LINK         O2A TD7 C2001                MG    MG C2002     1555   1555  2.10
LINK        MG    MG C2002                 OD1 ASP C 645     1555   1555  2.04
LINK        MG    MG C2002                 OD1 ASN C 678     1555   1555  1.92
LINK        MG    MG C2002                 O   HOH C3062     1555   1555  2.25
LINK        MG    MG C2002                 O   ILE C 680     1555   1555  2.05
LINK        CA    CA C2003                 OD1 ASP C1004     1555   1555  2.52
LINK        CA    CA C2003                 OD2 ASP C1004     1555   1555  2.37
LINK        CA    CA C2003                 O   HIS C1055     1555   1555  2.39
LINK        CA    CA C2003                 OD1 ASP C1058     1555   1555  2.48
LINK        CA    CA C2003                 O   ILE C1060     1555   1555  2.28
LINK        CA    CA C2003                 O   HOH C3177     1555   1555  2.48
LINK        CA    CA C2003                 O   HOH C3178     1555   1555  2.45
LINK         O2A TD7 D2001                MG    MG D2002     1555   1555  2.06
LINK         O3B TD7 D2001                MG    MG D2002     1555   1555  1.95
LINK        MG    MG D2002                 OD1 ASN D 678     1555   1555  1.97
LINK        MG    MG D2002                 OD1 ASP D 645     1555   1555  2.18
LINK        MG    MG D2002                 O   ILE D 680     1555   1555  2.00
LINK        MG    MG D2002                 O   HOH D3038     1555   1555  2.23
LINK        CA    CA D2003                 O   ILE D1060     1555   1555  2.30
LINK        CA    CA D2003                 O   HOH D3100     1555   1555  2.38
LINK        CA    CA D2003                 O   HOH D3101     1555   1555  2.50
LINK        CA    CA D2003                 O   HIS D1055     1555   1555  2.34
LINK        CA    CA D2003                 OD1 ASP D1004     1555   1555  2.65
LINK        CA    CA D2003                 OD2 ASP D1004     1555   1555  2.54
LINK        CA    CA D2003                 OD1 ASP D1058     1555   1555  2.36
CISPEP   1 ALA A 1144    PRO A 1145          0        -3.97
CISPEP   2 ALA B 1144    PRO B 1145          0        -5.57
CISPEP   3 ALA C 1144    PRO C 1145          0        -5.66
CISPEP   4 ALA D 1144    PRO D 1145          0        -4.62
SITE     1 AC1 29 PHE A 506  HIS A 539  ARG A 540  TYR A 578
SITE     2 AC1 29 HIS A 579  SER A 604  HIS A 605  LEU A 606
SITE     3 AC1 29 GLY A 644  ASP A 645  ALA A 646  ALA A 647
SITE     4 AC1 29 GLN A 651  ASN A 678  ILE A 680  GLY A 681
SITE     5 AC1 29 HIS A 747   MG A2002  HOH A3022  HOH A3024
SITE     6 AC1 29 HOH A3046  HOH A3047  HOH A3203  GLN B 901
SITE     7 AC1 29 LEU B 950  GLU B 952  GLN B 976  PHE B 980
SITE     8 AC1 29 HIS B1020
SITE     1 AC2  5 ASP A 645  ASN A 678  ILE A 680  TD7 A2001
SITE     2 AC2  5 HOH A3047
SITE     1 AC3  6 ASP A1004  HIS A1055  ASP A1058  ILE A1060
SITE     2 AC3  6 HOH A3153  HOH A3154
SITE     1 AC4 28 GLN A 901  LEU A 950  GLU A 952  GLN A 976
SITE     2 AC4 28 PHE A 980  HIS A1020  PHE B 506  HIS B 539
SITE     3 AC4 28 ARG B 540  TYR B 578  HIS B 579  SER B 604
SITE     4 AC4 28 HIS B 605  LEU B 606  GLY B 644  ASP B 645
SITE     5 AC4 28 ALA B 646  ALA B 647  ASN B 678  ILE B 680
SITE     6 AC4 28 GLY B 681  HIS B 747   MG B2002  HOH B3027
SITE     7 AC4 28 HOH B3028  HOH B3049  HOH B3050  HOH B3065
SITE     1 AC5  5 ASP B 645  ASN B 678  ILE B 680  TD7 B2001
SITE     2 AC5  5 HOH B3050
SITE     1 AC6  6 ASP B1004  HIS B1055  ASP B1058  ILE B1060
SITE     2 AC6  6 HOH B3127  HOH B3128
SITE     1 AC7 28 HIS C 539  ARG C 540  TYR C 578  HIS C 579
SITE     2 AC7 28 SER C 604  HIS C 605  LEU C 606  GLY C 644
SITE     3 AC7 28 ASP C 645  ALA C 646  ALA C 647  GLN C 651
SITE     4 AC7 28 ASN C 678  ILE C 680  GLY C 681  HIS C 747
SITE     5 AC7 28  MG C2002  HOH C3031  HOH C3032  HOH C3034
SITE     6 AC7 28 HOH C3061  HOH C3062  GLN D 901  LEU D 950
SITE     7 AC7 28 GLU D 952  GLN D 976  PHE D 980  HIS D1020
SITE     1 AC8  5 ASP C 645  ASN C 678  ILE C 680  TD7 C2001
SITE     2 AC8  5 HOH C3062
SITE     1 AC9  6 ASP C1004  HIS C1055  ASP C1058  ILE C1060
SITE     2 AC9  6 HOH C3177  HOH C3178
SITE     1 BC1 28 GLN C 901  LEU C 950  GLU C 952  GLN C 976
SITE     2 BC1 28 PHE C 980  HIS C1020  HIS D 539  ARG D 540
SITE     3 BC1 28 TYR D 578  HIS D 579  SER D 604  HIS D 605
SITE     4 BC1 28 LEU D 606  GLY D 644  ASP D 645  ALA D 646
SITE     5 BC1 28 ALA D 647  GLN D 651  ASN D 678  ILE D 680
SITE     6 BC1 28 GLY D 681  HIS D 747   MG D2002  HOH D3018
SITE     7 BC1 28 HOH D3019  HOH D3021  HOH D3037  HOH D3038
SITE     1 BC2  5 ASP D 645  ASN D 678  ILE D 680  TD7 D2001
SITE     2 BC2  5 HOH D3038
SITE     1 BC3  6 ASP D1004  HIS D1055  ASP D1058  ILE D1060
SITE     2 BC3  6 HOH D3100  HOH D3101
CRYST1   79.843   82.287  163.478  99.23  99.03 100.63 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      0.012525  0.002351  0.002497        0.00000
SCALE2      0.000000  0.012365  0.002459        0.00000
SCALE3      0.000000  0.000000  0.006315        0.00000
MTRIX1   1 -0.257700  0.137200  0.956400       -0.24500    1
MTRIX2   1  0.134300 -0.975200  0.176100       -0.26560    1
MTRIX3   1  0.956900  0.173800  0.232800        0.28540    1
MTRIX1   2  0.199800  0.218400 -0.955200      -77.81780    1
MTRIX2   2  0.225500 -0.958900 -0.172100       12.56750    1
MTRIX3   2 -0.953500 -0.181100 -0.240900        3.02250    1
MTRIX1   3 -0.932800 -0.360200 -0.005200       24.56720    1
MTRIX2   3 -0.360200  0.932900 -0.005000      -22.69670    1
MTRIX3   3  0.006600 -0.002800 -1.000000      -71.29410    1
      
PROCHECK
Go to PROCHECK summary
 References