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PDBsum entry 2yzm

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Ligase PDB id
2yzm
Jmol
Contents
Protein chains
319 a.a.
Ligands
DAL ×3
Waters ×266
HEADER    LIGASE                                  06-MAY-07   2YZM
TITLE     STRUCTURE OF D-ALANINE:D-ALANINE LIGASE WITH SUBSTRATE FROM THERMUS
TITLE    2 THERMOPHILUS HB8
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: D-ALANINE--D-ALANINE LIGASE;
COMPND   3 CHAIN: A, B, C;
COMPND   4 EC: 6.3.2.4;
COMPND   5 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;
SOURCE   3 ORGANISM_TAXID: 300852;
SOURCE   4 STRAIN: HB8;
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE   7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PET-11A
KEYWDS    D-ALANINE:D-ALANINE LIGASE, CELL SHAPE, PEPTIDOGLYCAN SYNTHESIS,
KEYWDS   2 STRUCTURAL GENOMICS, NPPSFA, NATIONAL PROJECT ON PROTEIN STRUCTURAL
KEYWDS   3 AND FUNCTIONAL ANALYSES, RIKEN STRUCTURAL GENOMICS/PROTEOMICS
KEYWDS   4 INITIATIVE, RSGI, LIGASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    Y.KITAMURA,S.YOKOYAMA,S.KURAMITSU,RIKEN STRUCTURAL
AUTHOR   2 GENOMICS/PROTEOMICS INITIATIVE (RSGI)
REVDAT   3   13-JUL-11 2YZM    1       VERSN
REVDAT   2   24-FEB-09 2YZM    1       VERSN
REVDAT   1   06-NOV-07 2YZM    0
JRNL        AUTH   Y.KITAMURA,S.YOKOYAMA,S.KURAMITSU
JRNL        TITL   STRUCTURE OF D-ALANINE:D-ALANINE LIGASE WITH SUBSTRATE FROM
JRNL        TITL 2 THERMUS THERMOPHILUS HB8
JRNL        REF    TO BE PUBLISHED
JRNL        REFN
REMARK   2
REMARK   2 RESOLUTION.    2.21 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : CNS 1.1
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK   3               : READ,RICE,SIMONSON,WARREN
REMARK   3
REMARK   3  REFINEMENT TARGET : NULL
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.21
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 44.16
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 180293.600
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 97.8
REMARK   3   NUMBER OF REFLECTIONS             : 60810
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM
REMARK   3   R VALUE            (WORKING SET) : 0.224
REMARK   3   FREE R VALUE                     : 0.266
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.200
REMARK   3   FREE R VALUE TEST SET COUNT      : 6174
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.003
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : 6
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.20
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.34
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 84.90
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 7915
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2510
REMARK   3   BIN FREE R VALUE                    : 0.3170
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 10.20
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 895
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.011
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 7192
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 18
REMARK   3   SOLVENT ATOMS            : 266
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 20.30
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 31.80
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : -1.08000
REMARK   3    B22 (A**2) : 2.59000
REMARK   3    B33 (A**2) : -1.51000
REMARK   3    B12 (A**2) : 0.00000
REMARK   3    B13 (A**2) : 4.84000
REMARK   3    B23 (A**2) : 0.00000
REMARK   3
REMARK   3  ESTIMATED COORDINATE ERROR.
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.28
REMARK   3   ESD FROM SIGMAA              (A) : 0.18
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00
REMARK   3
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.35
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.27
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.
REMARK   3   BOND LENGTHS                 (A) : 0.006
REMARK   3   BOND ANGLES            (DEGREES) : 1.30
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 24.10
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.01
REMARK   3
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL
REMARK   3
REMARK   3  BULK SOLVENT MODELING.
REMARK   3   METHOD USED : FLAT MODEL
REMARK   3   KSOL        : 0.34
REMARK   3   BSOL        : 34.90
REMARK   3
REMARK   3  NCS MODEL : NULL
REMARK   3
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL
REMARK   3
REMARK   3  PARAMETER FILE  1  : PROTEIN_REP.PARAM
REMARK   3  PARAMETER FILE  2  : WATER_REP.PARAM
REMARK   3  PARAMETER FILE  3  : DAL_XPLOR.PARAM
REMARK   3  PARAMETER FILE  4  : NULL
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP
REMARK   3  TOPOLOGY FILE  2   : WATER.TOP
REMARK   3  TOPOLOGY FILE  3   : DAL_XPLOR.TOP
REMARK   3  TOPOLOGY FILE  4   : NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 2YZM COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 27-JUL-07.
REMARK 100 THE RCSB ID CODE IS RCSB027334.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 30-SEP-05
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 5.4
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : SPRING-8
REMARK 200  BEAMLINE                       : BL26B2
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0
REMARK 200  MONOCHROMATOR                  : FIXED EXIT SI DOUBLE CRYSTAL
REMARK 200                                   MONOCHROMATOR
REMARK 200  OPTICS                         : A FIXED EXIT SI DOUBLE CRYSTAL
REMARK 200                                   MONOCHROMATOR FOLLOWED BY A TWO
REMARK 200                                   DIMENSIONAL FOCUSING MIRROR WHICH
REMARK 200                                   IS COATED IN RHODIUM.
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU JUPITER 210
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 61811
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.200
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9
REMARK 200  DATA REDUNDANCY                : 7.200
REMARK 200  R MERGE                    (I) : 0.04500
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 36.2900
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.28
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.9
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.90
REMARK 200  R MERGE FOR SHELL          (I) : 0.22700
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : 9.080
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: 2YZG
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 58.76
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.98
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 14% PEG 4000, 0.1M MG CHLORIDE, 0.1M
REMARK 280  MES PH 5.4, D-ALANINE, PH 5.4, VAPOR DIFFUSION, HANGING DROP,
REMARK 280  TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,Y,-Z
REMARK 290       3555   X+1/2,Y+1/2,Z
REMARK 290       4555   -X+1/2,Y+1/2,-Z
REMARK 290
REMARK 290     WHERE NNN -> OPERATOR NUMBER
REMARK 290           MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       83.35250
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       27.92450
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       83.35250
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       27.92450
REMARK 290   SMTRY3   4  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: 26130 ANGSTROM**2
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: 2690 ANGSTROM**2
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C
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   BIOMT1   2 -1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   2  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     TYR B   223
REMARK 465     ASP B   224
REMARK 465     TYR B   225
REMARK 465     GLU B   226
REMARK 465     THR B   227
REMARK 465     LYS B   228
REMARK 465     TYR B   229
REMARK 465     PHE C   222
REMARK 465     TYR C   223
REMARK 465     ASP C   224
REMARK 465     TYR C   225
REMARK 465     GLU C   226
REMARK 465     THR C   227
REMARK 465     LYS C   228
REMARK 465     TYR C   229
REMARK 465     THR C   230
REMARK 465     PRO C   231
REMARK 465     GLY C   232
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   O    GLY B   204     O    ARG B   264              2.13
REMARK 500   O    GLY A   204     O    ARG A   264              2.15
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    PRO A  29       34.30    -77.95
REMARK 500    ALA A  57      136.76   -176.63
REMARK 500    LEU A  80       64.57   -105.32
REMARK 500    VAL A 206      -55.78     64.67
REMARK 500    LYS A 228     -131.93     57.29
REMARK 500    ALA A 267      143.27    174.17
REMARK 500    PRO B  29       34.62    -74.30
REMARK 500    ALA B  57      145.61   -173.97
REMARK 500    LEU B  80       42.59    -97.22
REMARK 500    PRO B 145        0.47    -67.24
REMARK 500    PHE B 169       -7.15    -58.12
REMARK 500    ASP B 183      129.03   -178.95
REMARK 500    GLU B 184        0.22    -64.61
REMARK 500    VAL B 206      -57.70     65.00
REMARK 500    ARG B 264      -64.08    -99.22
REMARK 500    ALA B 267      141.70   -178.75
REMARK 500    GLU B 275       67.93     32.92
REMARK 500    PRO C  29       32.93    -81.49
REMARK 500    ALA C  57      141.42   -172.18
REMARK 500    LEU C  80       49.94   -109.11
REMARK 500    PRO C 145        8.68    -69.57
REMARK 500    SER C 159     -162.68   -117.59
REMARK 500    VAL C 206      -55.92     67.74
REMARK 500    ALA C 267      140.74    176.27
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE
REMARK 500 M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS
REMARK 500    ARG A 264        24.3      L          L   OUTSIDE RANGE
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DAL A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DAL B 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DAL C 403
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2YZG   RELATED DB: PDB
REMARK 900 RELATED ID: TTK003001114.2   RELATED DB: TARGETDB
DBREF  2YZM A    1   319  UNP    Q5SHZ3   Q5SHZ3_THET8     1    319
DBREF  2YZM B    1   319  UNP    Q5SHZ3   Q5SHZ3_THET8     1    319
DBREF  2YZM C    1   319  UNP    Q5SHZ3   Q5SHZ3_THET8     1    319
SEQRES   1 A  319  MET ARG VAL LEU LEU ILE ALA GLY GLY VAL SER PRO GLU
SEQRES   2 A  319  HIS GLU VAL SER LEU LEU SER ALA GLU GLY VAL LEU ARG
SEQRES   3 A  319  HIS ILE PRO PHE PRO THR ASP LEU ALA VAL ILE ALA GLN
SEQRES   4 A  319  ASP GLY ARG TRP LEU LEU GLY GLU LYS ALA LEU THR ALA
SEQRES   5 A  319  LEU GLU ALA LYS ALA ALA PRO GLU GLY GLU HIS PRO PHE
SEQRES   6 A  319  PRO PRO PRO LEU SER TRP GLU ARG TYR ASP VAL VAL PHE
SEQRES   7 A  319  PRO LEU LEU HIS GLY ARG PHE GLY GLU ASP GLY THR VAL
SEQRES   8 A  319  GLN GLY PHE LEU GLU LEU LEU GLY LYS PRO TYR VAL GLY
SEQRES   9 A  319  ALA GLY VAL ALA ALA SER ALA LEU CYS MET ASP LYS ASP
SEQRES  10 A  319  LEU SER LYS ARG VAL LEU ALA GLN ALA GLY VAL PRO VAL
SEQRES  11 A  319  VAL PRO TRP VAL ALA VAL ARG LYS GLY GLU PRO PRO VAL
SEQRES  12 A  319  VAL PRO PHE ASP PRO PRO PHE PHE VAL LYS PRO ALA ASN
SEQRES  13 A  319  THR GLY SER SER VAL GLY ILE SER ARG VAL GLU ARG PHE
SEQRES  14 A  319  GLN ASP LEU GLU ALA ALA LEU ALA LEU ALA PHE ARG TYR
SEQRES  15 A  319  ASP GLU LYS ALA VAL VAL GLU LYS ALA LEU SER PRO VAL
SEQRES  16 A  319  ARG GLU LEU GLU VAL GLY VAL LEU GLY ASN VAL PHE GLY
SEQRES  17 A  319  GLU ALA SER PRO VAL GLY GLU VAL ARG TYR GLU ALA PRO
SEQRES  18 A  319  PHE TYR ASP TYR GLU THR LYS TYR THR PRO GLY ARG ALA
SEQRES  19 A  319  GLU LEU LEU ILE PRO ALA PRO LEU ASP PRO GLY THR GLN
SEQRES  20 A  319  GLU THR VAL GLN GLU LEU ALA LEU LYS ALA TYR LYS VAL
SEQRES  21 A  319  LEU GLY VAL ARG GLY MET ALA ARG VAL ASP PHE PHE LEU
SEQRES  22 A  319  ALA GLU GLY GLU LEU TYR LEU ASN GLU LEU ASN THR ILE
SEQRES  23 A  319  PRO GLY PHE THR PRO THR SER MET TYR PRO ARG LEU PHE
SEQRES  24 A  319  GLU ALA GLY GLY VAL ALA TYR PRO GLU LEU LEU ARG ARG
SEQRES  25 A  319  LEU VAL GLU LEU ALA LEU THR
SEQRES   1 B  319  MET ARG VAL LEU LEU ILE ALA GLY GLY VAL SER PRO GLU
SEQRES   2 B  319  HIS GLU VAL SER LEU LEU SER ALA GLU GLY VAL LEU ARG
SEQRES   3 B  319  HIS ILE PRO PHE PRO THR ASP LEU ALA VAL ILE ALA GLN
SEQRES   4 B  319  ASP GLY ARG TRP LEU LEU GLY GLU LYS ALA LEU THR ALA
SEQRES   5 B  319  LEU GLU ALA LYS ALA ALA PRO GLU GLY GLU HIS PRO PHE
SEQRES   6 B  319  PRO PRO PRO LEU SER TRP GLU ARG TYR ASP VAL VAL PHE
SEQRES   7 B  319  PRO LEU LEU HIS GLY ARG PHE GLY GLU ASP GLY THR VAL
SEQRES   8 B  319  GLN GLY PHE LEU GLU LEU LEU GLY LYS PRO TYR VAL GLY
SEQRES   9 B  319  ALA GLY VAL ALA ALA SER ALA LEU CYS MET ASP LYS ASP
SEQRES  10 B  319  LEU SER LYS ARG VAL LEU ALA GLN ALA GLY VAL PRO VAL
SEQRES  11 B  319  VAL PRO TRP VAL ALA VAL ARG LYS GLY GLU PRO PRO VAL
SEQRES  12 B  319  VAL PRO PHE ASP PRO PRO PHE PHE VAL LYS PRO ALA ASN
SEQRES  13 B  319  THR GLY SER SER VAL GLY ILE SER ARG VAL GLU ARG PHE
SEQRES  14 B  319  GLN ASP LEU GLU ALA ALA LEU ALA LEU ALA PHE ARG TYR
SEQRES  15 B  319  ASP GLU LYS ALA VAL VAL GLU LYS ALA LEU SER PRO VAL
SEQRES  16 B  319  ARG GLU LEU GLU VAL GLY VAL LEU GLY ASN VAL PHE GLY
SEQRES  17 B  319  GLU ALA SER PRO VAL GLY GLU VAL ARG TYR GLU ALA PRO
SEQRES  18 B  319  PHE TYR ASP TYR GLU THR LYS TYR THR PRO GLY ARG ALA
SEQRES  19 B  319  GLU LEU LEU ILE PRO ALA PRO LEU ASP PRO GLY THR GLN
SEQRES  20 B  319  GLU THR VAL GLN GLU LEU ALA LEU LYS ALA TYR LYS VAL
SEQRES  21 B  319  LEU GLY VAL ARG GLY MET ALA ARG VAL ASP PHE PHE LEU
SEQRES  22 B  319  ALA GLU GLY GLU LEU TYR LEU ASN GLU LEU ASN THR ILE
SEQRES  23 B  319  PRO GLY PHE THR PRO THR SER MET TYR PRO ARG LEU PHE
SEQRES  24 B  319  GLU ALA GLY GLY VAL ALA TYR PRO GLU LEU LEU ARG ARG
SEQRES  25 B  319  LEU VAL GLU LEU ALA LEU THR
SEQRES   1 C  319  MET ARG VAL LEU LEU ILE ALA GLY GLY VAL SER PRO GLU
SEQRES   2 C  319  HIS GLU VAL SER LEU LEU SER ALA GLU GLY VAL LEU ARG
SEQRES   3 C  319  HIS ILE PRO PHE PRO THR ASP LEU ALA VAL ILE ALA GLN
SEQRES   4 C  319  ASP GLY ARG TRP LEU LEU GLY GLU LYS ALA LEU THR ALA
SEQRES   5 C  319  LEU GLU ALA LYS ALA ALA PRO GLU GLY GLU HIS PRO PHE
SEQRES   6 C  319  PRO PRO PRO LEU SER TRP GLU ARG TYR ASP VAL VAL PHE
SEQRES   7 C  319  PRO LEU LEU HIS GLY ARG PHE GLY GLU ASP GLY THR VAL
SEQRES   8 C  319  GLN GLY PHE LEU GLU LEU LEU GLY LYS PRO TYR VAL GLY
SEQRES   9 C  319  ALA GLY VAL ALA ALA SER ALA LEU CYS MET ASP LYS ASP
SEQRES  10 C  319  LEU SER LYS ARG VAL LEU ALA GLN ALA GLY VAL PRO VAL
SEQRES  11 C  319  VAL PRO TRP VAL ALA VAL ARG LYS GLY GLU PRO PRO VAL
SEQRES  12 C  319  VAL PRO PHE ASP PRO PRO PHE PHE VAL LYS PRO ALA ASN
SEQRES  13 C  319  THR GLY SER SER VAL GLY ILE SER ARG VAL GLU ARG PHE
SEQRES  14 C  319  GLN ASP LEU GLU ALA ALA LEU ALA LEU ALA PHE ARG TYR
SEQRES  15 C  319  ASP GLU LYS ALA VAL VAL GLU LYS ALA LEU SER PRO VAL
SEQRES  16 C  319  ARG GLU LEU GLU VAL GLY VAL LEU GLY ASN VAL PHE GLY
SEQRES  17 C  319  GLU ALA SER PRO VAL GLY GLU VAL ARG TYR GLU ALA PRO
SEQRES  18 C  319  PHE TYR ASP TYR GLU THR LYS TYR THR PRO GLY ARG ALA
SEQRES  19 C  319  GLU LEU LEU ILE PRO ALA PRO LEU ASP PRO GLY THR GLN
SEQRES  20 C  319  GLU THR VAL GLN GLU LEU ALA LEU LYS ALA TYR LYS VAL
SEQRES  21 C  319  LEU GLY VAL ARG GLY MET ALA ARG VAL ASP PHE PHE LEU
SEQRES  22 C  319  ALA GLU GLY GLU LEU TYR LEU ASN GLU LEU ASN THR ILE
SEQRES  23 C  319  PRO GLY PHE THR PRO THR SER MET TYR PRO ARG LEU PHE
SEQRES  24 C  319  GLU ALA GLY GLY VAL ALA TYR PRO GLU LEU LEU ARG ARG
SEQRES  25 C  319  LEU VAL GLU LEU ALA LEU THR
HET    DAL  A 401       6
HET    DAL  B 402       6
HET    DAL  C 403       6
HETNAM     DAL D-ALANINE
FORMUL   4  DAL    3(C3 H7 N O2)
FORMUL   7  HOH   *266(H2 O)
HELIX    1   1 GLU A   13  ILE A   28  1                                  16
HELIX    2   2 LEU A   45  LYS A   56  1                                  12
HELIX    3   3 SER A   70  TYR A   74  5                                   5
HELIX    4   4 GLY A   89  LEU A   98  1                                  10
HELIX    5   5 GLY A  106  MET A  114  1                                   9
HELIX    6   6 ASP A  115  ALA A  126  1                                  12
HELIX    7   7 ARG A  168  GLN A  170  5                                   3
HELIX    8   8 ASP A  171  PHE A  180  1                                  10
HELIX    9   9 ASP A  243  GLY A  262  1                                  20
HELIX   10  10 SER A  293  GLY A  302  1                                  10
HELIX   11  11 ALA A  305  LEU A  318  1                                  14
HELIX   12  12 GLU B   13  ILE B   28  1                                  16
HELIX   13  13 LEU B   45  LYS B   56  1                                  12
HELIX   14  14 SER B   70  TYR B   74  5                                   5
HELIX   15  15 GLY B   89  GLY B   99  1                                  11
HELIX   16  16 GLY B  106  MET B  114  1                                   9
HELIX   17  17 ASP B  115  GLY B  127  1                                  13
HELIX   18  18 ASP B  171  PHE B  180  1                                  10
HELIX   19  19 ASP B  243  GLY B  262  1                                  20
HELIX   20  20 SER B  293  GLY B  302  1                                  10
HELIX   21  21 ALA B  305  THR B  319  1                                  15
HELIX   22  22 GLU C   13  ARG C   26  1                                  14
HELIX   23  23 LEU C   45  LYS C   56  1                                  12
HELIX   24  24 SER C   70  TYR C   74  5                                   5
HELIX   25  25 GLY C   89  GLY C   99  1                                  11
HELIX   26  26 GLY C  106  MET C  114  1                                   9
HELIX   27  27 ASP C  115  ALA C  126  1                                  12
HELIX   28  28 ASP C  171  PHE C  180  1                                  10
HELIX   29  29 ASP C  243  GLY C  262  1                                  20
HELIX   30  30 SER C  293  GLY C  302  1                                  10
HELIX   31  31 ALA C  305  ALA C  317  1                                  13
SHEET    1   A 4 TRP A  43  LEU A  44  0
SHEET    2   A 4 THR A  32  ILE A  37 -1  N  VAL A  36   O  LEU A  44
SHEET    3   A 4 VAL A   3  GLY A   8  1  N  LEU A   5   O  ASP A  33
SHEET    4   A 4 VAL A  76  LEU A  80  1  O  PHE A  78   N  LEU A   4
SHEET    1   B 4 TRP A 133  ARG A 137  0
SHEET    2   B 4 LYS A 185  LYS A 190 -1  O  ALA A 186   N  VAL A 136
SHEET    3   B 4 PHE A 150  PRO A 154 -1  N  PHE A 151   O  GLU A 189
SHEET    4   B 4 SER A 164  VAL A 166 -1  O  VAL A 166   N  PHE A 150
SHEET    1   C 5 ARG A 233  LEU A 237  0
SHEET    2   C 5 GLU A 209  GLU A 219 -1  N  ARG A 217   O  GLU A 235
SHEET    3   C 5 ARG A 196  LEU A 203 -1  N  GLU A 199   O  GLY A 214
SHEET    4   C 5 MET A 266  ALA A 274 -1  O  PHE A 271   N  LEU A 198
SHEET    5   C 5 GLU A 277  ASN A 284 -1  O  GLU A 282   N  ASP A 270
SHEET    1   D 2 PHE A 222  ASP A 224  0
SHEET    2   D 2 LYS A 228  THR A 230 -1  O  LYS A 228   N  ASP A 224
SHEET    1   E 4 TRP B  43  LEU B  44  0
SHEET    2   E 4 THR B  32  ILE B  37 -1  N  VAL B  36   O  LEU B  44
SHEET    3   E 4 VAL B   3  GLY B   8  1  N  LEU B   5   O  ASP B  33
SHEET    4   E 4 VAL B  76  PRO B  79  1  O  PHE B  78   N  LEU B   4
SHEET    1   F 4 TRP B 133  ARG B 137  0
SHEET    2   F 4 LYS B 185  LYS B 190 -1  O  ALA B 186   N  VAL B 136
SHEET    3   F 4 PHE B 150  PRO B 154 -1  N  PHE B 151   O  GLU B 189
SHEET    4   F 4 SER B 164  VAL B 166 -1  O  VAL B 166   N  PHE B 150
SHEET    1   G 5 ALA B 234  LEU B 237  0
SHEET    2   G 5 GLU B 209  TYR B 218 -1  N  GLU B 215   O  LEU B 237
SHEET    3   G 5 ARG B 196  LEU B 203 -1  N  GLU B 199   O  GLY B 214
SHEET    4   G 5 MET B 266  ALA B 274 -1  O  PHE B 271   N  LEU B 198
SHEET    5   G 5 GLU B 277  ASN B 284 -1  O  GLU B 282   N  ASP B 270
SHEET    1   H 4 TRP C  43  LEU C  44  0
SHEET    2   H 4 THR C  32  ILE C  37 -1  N  VAL C  36   O  LEU C  44
SHEET    3   H 4 VAL C   3  GLY C   8  1  N  LEU C   5   O  ASP C  33
SHEET    4   H 4 VAL C  76  LEU C  80  1  O  PHE C  78   N  LEU C   4
SHEET    1   I 4 TRP C 133  ARG C 137  0
SHEET    2   I 4 LYS C 185  LYS C 190 -1  O  ALA C 186   N  VAL C 136
SHEET    3   I 4 PHE C 150  PRO C 154 -1  N  PHE C 151   O  GLU C 189
SHEET    4   I 4 SER C 164  VAL C 166 -1  O  VAL C 166   N  PHE C 150
SHEET    1   J 5 ALA C 234  LEU C 237  0
SHEET    2   J 5 GLU C 209  TYR C 218 -1  N  GLU C 215   O  LEU C 237
SHEET    3   J 5 ARG C 196  LEU C 203 -1  N  GLU C 199   O  GLY C 214
SHEET    4   J 5 MET C 266  ALA C 274 -1  O  PHE C 271   N  LEU C 198
SHEET    5   J 5 GLU C 277  ASN C 284 -1  O  GLU C 282   N  ASP C 270
CISPEP   1 PHE A   65    PRO A   66          0        -0.16
CISPEP   2 PRO A  148    PRO A  149          0         0.09
CISPEP   3 SER A  193    PRO A  194          0        -0.25
CISPEP   4 ILE A  238    PRO A  239          0        -0.36
CISPEP   5 PHE B   65    PRO B   66          0        -0.17
CISPEP   6 PRO B  148    PRO B  149          0        -0.10
CISPEP   7 SER B  193    PRO B  194          0         0.05
CISPEP   8 ILE B  238    PRO B  239          0        -0.05
CISPEP   9 PHE C   65    PRO C   66          0        -0.06
CISPEP  10 PRO C  148    PRO C  149          0         0.02
CISPEP  11 SER C  193    PRO C  194          0        -0.16
CISPEP  12 ILE C  238    PRO C  239          0        -0.21
SITE     1 AC1  8 GLU A  13  HIS A  82  GLY A  83  GLU A  87
SITE     2 AC1  8 THR A 157  ASN A 284  HOH A 428  HOH A 476
SITE     1 AC2  8 GLU B  13  GLY B  83  GLU B  87  MET B 114
SITE     2 AC2  8 GLY B 158  GLU B 282  ASN B 284  HOH B 453
SITE     1 AC3  7 GLU C  13  HIS C  82  GLY C  83  GLU C  87
SITE     2 AC3  7 GLY C 158  GLU C 282  ASN C 284
CRYST1  166.705   55.849  141.387  90.00 109.34  90.00 C 1 2 1      12
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      0.005999  0.000000  0.002105        0.00000
SCALE2      0.000000  0.017905  0.000000        0.00000
SCALE3      0.000000  0.000000  0.007496        0.00000
      
PROCHECK
Go to PROCHECK summary
 References