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PDBsum entry 3e5n

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Ligase PDB id
3e5n
Jmol
Contents
Protein chain
340 a.a.
Waters ×142
HEADER    LIGASE                                  14-AUG-08   3E5N
TITLE     CRYSTAL STRUCUTRE OF D-ALANINE-D-ALANINE LIGASE FROM
TITLE    2 XANTHOMONAS ORYZAE PV. ORYZAE KACC10331
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: D-ALANINE-D-ALANINE LIGASE A;
COMPND   3 CHAIN: A;
COMPND   4 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: XANTHOMONAS ORYZAE PV. ORYZAE;
SOURCE   3 ORGANISM_TAXID: 342109;
SOURCE   4 STRAIN: MAFF 311018;
SOURCE   5 GENE: XOO0324;
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PET15B
KEYWDS    BACTERIAL BLIGHT, D-ALANINE-D-ALANINE LIGASE, PIP (PLANT-
KEYWDS   2 INDUCIBLE PROMOTER) BOX PEPTIDOGLYCAN BIOSYNTHESIS
KEYWDS   3 XANTHOMONAS ORYZAE PV. ORYZAE, ATP-BINDING, CELL SHAPE,
KEYWDS   4 CELL WALL BIOGENESIS/DEGRADATION, CYTOPLASM, LIGASE,
KEYWDS   5 MAGNESIUM, MANGANESE, METAL-BINDING, NUCLEOTIDE-BINDING,
KEYWDS   6 PEPTIDOGLYCAN SYNTHESIS
EXPDTA    X-RAY DIFFRACTION
AUTHOR    T.N.T.DOAN,J.K.KIM,H.S.KIM,Y.J.AHN,J.G.KIM,B.M.LEE,L.W.KANG
REVDAT   1   18-AUG-09 3E5N    0
JRNL        AUTH   T.N.T.DOAN,J.K.KIM,H.S.KIM,Y.J.AHN,J.G.KIM,B.M.LEE,
JRNL        AUTH 2 L.W.KANG
JRNL        TITL   CRYSTAL STRUCUTRE OF D-ALANINE-D-ALANINE LIGASE
JRNL        TITL 2 FROM XANTHOMONAS ORYZAE PV. ORYZAE KACC10331
JRNL        REF    TO BE PUBLISHED
JRNL        REFN
REMARK   1
REMARK   2
REMARK   2 RESOLUTION.    2.00 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.2.0019
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON
REMARK   3
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 38.21
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.9
REMARK   3   NUMBER OF REFLECTIONS             : 22572
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) : 0.199
REMARK   3   R VALUE            (WORKING SET) : 0.196
REMARK   3   FREE R VALUE                     : 0.265
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100
REMARK   3   FREE R VALUE TEST SET COUNT      : 1217
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : 20
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.00
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.05
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1623
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.88
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2110
REMARK   3   BIN FREE R VALUE SET COUNT          : 83
REMARK   3   BIN FREE R VALUE                    : 0.2870
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 2582
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 0
REMARK   3   SOLVENT ATOMS            : 142
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 36.89
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : -0.08000
REMARK   3    B22 (A**2) : -0.08000
REMARK   3    B33 (A**2) : 0.17000
REMARK   3    B12 (A**2) : 0.00000
REMARK   3    B13 (A**2) : 0.00000
REMARK   3    B23 (A**2) : 0.00000
REMARK   3
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.
REMARK   3   ESU BASED ON R VALUE                            (A): NULL
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.187
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.133
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 10.343
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.954
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.915
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2625 ; 0.022 ; 0.022
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3568 ; 2.002 ; 1.963
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   341 ; 6.996 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   118 ;36.137 ;23.814
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   430 ;19.717 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    23 ;20.097 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   420 ; 0.176 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1992 ; 0.009 ; 0.020
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1223 ; 0.247 ; 0.200
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  1773 ; 0.311 ; 0.200
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   162 ; 0.193 ; 0.200
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    59 ; 0.243 ; 0.200
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     5 ; 0.232 ; 0.200
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  1748 ; 1.814 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2706 ; 2.686 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   974 ; 3.935 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   860 ; 5.682 ; 4.500
REMARK   3
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  2722 ; 2.834 ; 3.000
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):   142 ;10.371 ; 3.000
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  2582 ; 5.027 ; 3.000
REMARK   3
REMARK   3  NCS RESTRAINTS STATISTICS
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK   3
REMARK   3  TLS DETAILS
REMARK   3   NUMBER OF TLS GROUPS  : NULL
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED : MASK
REMARK   3   PARAMETERS FOR MASK CALCULATION
REMARK   3   VDW PROBE RADIUS   : 1.20
REMARK   3   ION PROBE RADIUS   : 0.80
REMARK   3   SHRINKAGE RADIUS   : 0.80
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE
REMARK   3  RIDING POSITIONS
REMARK   4
REMARK   4 3E5N COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 19-AUG-08.
REMARK 100 THE RCSB ID CODE IS RCSB048905.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 23-MAY-08
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 7.5
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : PHOTON FACTORY
REMARK 200  BEAMLINE                       : BL-17A
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.00000
REMARK 200  MONOCHROMATOR                  : FLAT SI(111) CRYSTALS
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 270
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 23816
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9
REMARK 200  DATA REDUNDANCY                : NULL
REMARK 200  R MERGE                    (I) : NULL
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.10
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.9
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL
REMARK 200  R MERGE FOR SHELL          (I) : NULL
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASES
REMARK 200 STARTING MODEL: PDB ENTRY 2NMP
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 38.68
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.01
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 15%(W/V) PEG4000, 0.1M TRIS, PH8.5,
REMARK 280  0.2M MGCL2, 0.3M DIMETHYLETHYL-(3-SULFOPROPYL)-AMMONIUM,
REMARK 280  PH7.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 287K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,-Y,Z+1/2
REMARK 290       3555   -Y+1/2,X+1/2,Z+3/4
REMARK 290       4555   Y+1/2,-X+1/2,Z+1/4
REMARK 290       5555   -X+1/2,Y+1/2,-Z+3/4
REMARK 290       6555   X+1/2,-Y+1/2,-Z+1/4
REMARK 290       7555   Y,X,-Z
REMARK 290       8555   -Y,-X,-Z+1/2
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       48.80050
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       41.52150
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       41.52150
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       73.20075
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       41.52150
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       41.52150
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       24.40025
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       41.52150
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       41.52150
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       73.20075
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       41.52150
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       41.52150
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       24.40025
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       48.80050
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3660 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 28300 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -24.3 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 350   BIOMT1   2  0.000000 -1.000000  0.000000        0.00000
REMARK 350   BIOMT2   2 -1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000      -48.80050
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     MET A   -18
REMARK 465     GLY A   -17
REMARK 465     HIS A   -16
REMARK 465     HIS A   -15
REMARK 465     HIS A   -14
REMARK 465     HIS A   -13
REMARK 465     HIS A   -12
REMARK 465     HIS A   -11
REMARK 465     HIS A   -10
REMARK 465     SER A    -9
REMARK 465     SER A    -8
REMARK 465     GLU A    -7
REMARK 465     ASN A    -6
REMARK 465     LEU A    -5
REMARK 465     TYR A    -4
REMARK 465     PHE A    -3
REMARK 465     GLN A    -2
REMARK 465     GLY A    -1
REMARK 465     HIS A     0
REMARK 465     MET A     1
REMARK 465     PRO A    92
REMARK 465     GLU A    93
REMARK 465     HIS A   250
REMARK 465     ASP A   251
REMARK 465     ALA A   252
REMARK 465     PHE A   253
REMARK 465     TYR A   254
REMARK 465     SER A   255
REMARK 465     TYR A   256
REMARK 465     ALA A   257
REMARK 465     THR A   258
REMARK 465     LYS A   259
REMARK 465     TYR A   260
REMARK 465     ILE A   261
REMARK 465     SER A   262
REMARK 465     GLU A   263
REMARK 465     HIS A   264
REMARK 465     GLY A   265
REMARK 465     ALA A   266
REMARK 465     ARG A   361
REMARK 465     SER A   362
REMARK 465     ALA A   363
REMARK 465     VAL A   364
REMARK 465     GLU A   365
REMARK 465     LEU A   366
REMARK 465     HIS A   367
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    HOH A   398     O    HOH A   439              2.12
REMARK 500   NE   ARG A    25     O    HOH A   425              2.17
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3
REMARK 500    ASP A  44   CB  -  CG  -  OD1 ANGL. DEV. = -10.3 DEGREES
REMARK 500    ARG A 146   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.3 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500  M RES CSSEQI        PSI       PHI
REMARK 500    ASP A  32      107.08    -55.39
REMARK 500    ASP A  44      164.33    -46.81
REMARK 500    SER A  56       43.52   -149.59
REMARK 500    GLN A 189     -160.29     75.13
REMARK 500    SER A 192      -78.16     79.58
REMARK 500    ASN A 236      -96.10   -100.31
REMARK 500    ASP A 308      -49.85    162.05
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500                                 MODEL     OMEGA
REMARK 500 ASN A  188     GLN A  189                 -146.28
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 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: (11X,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 163        22.8      L          L   OUTSIDE RANGE
REMARK 500     ILE A 175        22.2      L          L   OUTSIDE RANGE
REMARK 500     VAL A 233        22.2      L          L   OUTSIDE RANGE
REMARK 500     ALA A 307        23.3      L          L   OUTSIDE RANGE
REMARK 500     VAL A 312        23.2      L          L   OUTSIDE RANGE
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525  M RES CSSEQI
REMARK 525    HOH A 447        DISTANCE =  7.08 ANGSTROMS
REMARK 525    HOH A 500        DISTANCE =  8.29 ANGSTROMS
DBREF  3E5N A    1   367  UNP    Q2P8P8   Q2P8P8_XANOM     1    367
SEQADV 3E5N MET A  -18  UNP  Q2P8P8              EXPRESSION TAG
SEQADV 3E5N GLY A  -17  UNP  Q2P8P8              EXPRESSION TAG
SEQADV 3E5N HIS A  -16  UNP  Q2P8P8              EXPRESSION TAG
SEQADV 3E5N HIS A  -15  UNP  Q2P8P8              EXPRESSION TAG
SEQADV 3E5N HIS A  -14  UNP  Q2P8P8              EXPRESSION TAG
SEQADV 3E5N HIS A  -13  UNP  Q2P8P8              EXPRESSION TAG
SEQADV 3E5N HIS A  -12  UNP  Q2P8P8              EXPRESSION TAG
SEQADV 3E5N HIS A  -11  UNP  Q2P8P8              EXPRESSION TAG
SEQADV 3E5N HIS A  -10  UNP  Q2P8P8              EXPRESSION TAG
SEQADV 3E5N SER A   -9  UNP  Q2P8P8              EXPRESSION TAG
SEQADV 3E5N SER A   -8  UNP  Q2P8P8              EXPRESSION TAG
SEQADV 3E5N GLU A   -7  UNP  Q2P8P8              EXPRESSION TAG
SEQADV 3E5N ASN A   -6  UNP  Q2P8P8              EXPRESSION TAG
SEQADV 3E5N LEU A   -5  UNP  Q2P8P8              EXPRESSION TAG
SEQADV 3E5N TYR A   -4  UNP  Q2P8P8              EXPRESSION TAG
SEQADV 3E5N PHE A   -3  UNP  Q2P8P8              EXPRESSION TAG
SEQADV 3E5N GLN A   -2  UNP  Q2P8P8              EXPRESSION TAG
SEQADV 3E5N GLY A   -1  UNP  Q2P8P8              EXPRESSION TAG
SEQADV 3E5N HIS A    0  UNP  Q2P8P8              EXPRESSION TAG
SEQADV 3E5N VAL A  327  UNP  Q2P8P8    MET   327 CONFLICT
SEQRES   1 A  386  MET GLY HIS HIS HIS HIS HIS HIS HIS SER SER GLU ASN
SEQRES   2 A  386  LEU TYR PHE GLN GLY HIS MET ARG LYS ILE ARG VAL GLY
SEQRES   3 A  386  LEU ILE PHE GLY GLY LYS SER ALA GLU HIS GLU VAL SER
SEQRES   4 A  386  LEU GLN SER ALA ARG ASN ILE LEU ASP ALA LEU ASP PRO
SEQRES   5 A  386  GLN ARG PHE GLU PRO VAL LEU ILE GLY ILE ASP LYS GLN
SEQRES   6 A  386  GLY GLN TRP HIS VAL ASN ASP PRO ASP SER PHE LEU LEU
SEQRES   7 A  386  HIS ALA ASP ASP PRO ALA ARG ILE ALA LEU HIS ARG SER
SEQRES   8 A  386  GLY ARG GLY VAL ALA LEU LEU PRO GLY ALA GLN GLN GLN
SEQRES   9 A  386  GLN LEU ARG PRO ILE GLN PRO GLU GLN ALA LEU ALA GLN
SEQRES  10 A  386  ILE ASP VAL VAL PHE PRO ILE VAL HIS GLY THR LEU GLY
SEQRES  11 A  386  GLU ASP GLY SER LEU GLN GLY LEU LEU ARG MET ALA ASN
SEQRES  12 A  386  LEU PRO PHE VAL GLY SER GLY VAL LEU GLY SER ALA VAL
SEQRES  13 A  386  ALA MET ASP LYS ASP MET ALA LYS ARG VAL LEU ARG ASP
SEQRES  14 A  386  ALA ARG LEU ALA VAL ALA PRO PHE VAL CYS PHE ASP ARG
SEQRES  15 A  386  HIS THR ALA ALA HIS ALA ASP VAL ASP THR LEU ILE ALA
SEQRES  16 A  386  GLN LEU GLY LEU PRO LEU PHE VAL LYS PRO ALA ASN GLN
SEQRES  17 A  386  GLY SER SER VAL GLY VAL SER GLN VAL ARG THR ALA ASP
SEQRES  18 A  386  ALA PHE ALA ALA ALA LEU ALA LEU ALA LEU ALA TYR ASP
SEQRES  19 A  386  HIS LYS VAL LEU VAL GLU ALA ALA VAL ALA GLY ARG GLU
SEQRES  20 A  386  ILE GLU CYS ALA VAL LEU GLY ASN ALA VAL PRO HIS ALA
SEQRES  21 A  386  SER VAL CYS GLY GLU VAL VAL VAL HIS ASP ALA PHE TYR
SEQRES  22 A  386  SER TYR ALA THR LYS TYR ILE SER GLU HIS GLY ALA GLU
SEQRES  23 A  386  ILE VAL ILE PRO ALA ASP ILE ASP ALA GLN THR GLN GLN
SEQRES  24 A  386  ARG ILE GLN GLN ILE ALA VAL GLN ALA TYR GLN ALA LEU
SEQRES  25 A  386  GLY CYS ALA GLY MET ALA ARG VAL ASP VAL PHE LEU CYS
SEQRES  26 A  386  ALA ASP GLY ARG ILE VAL ILE ASN GLU VAL ASN THR LEU
SEQRES  27 A  386  PRO GLY PHE THR ARG ILE SER VAL TYR PRO LYS LEU TRP
SEQRES  28 A  386  GLN ALA SER GLY LEU ASP TYR ARG GLY LEU ILE THR ARG
SEQRES  29 A  386  LEU ILE GLU LEU ALA LEU GLU ARG HIS THR ASP ASP GLN
SEQRES  30 A  386  LEU LEU ARG SER ALA VAL GLU LEU HIS
FORMUL   2  HOH   *142(H2 O)
HELIX    1   1 GLU A   16  LEU A   31  1                                  16
HELIX    2   2 ASP A   53  SER A   56  5                                   4
HELIX    3   3 GLY A  108  ASP A  113  1                                   6
HELIX    4   4 GLY A  114  ALA A  123  1                                  10
HELIX    5   5 GLY A  131  ASP A  140  1                                  10
HELIX    6   6 ASP A  140  ALA A  151  1                                  12
HELIX    7   7 ARG A  163  ALA A  167  1                                   5
HELIX    8   8 ASP A  170  GLY A  179  1                                  10
HELIX    9   9 THR A  200  ASP A  202  5                                   3
HELIX   10  10 ALA A  203  LEU A  212  1                                  10
HELIX   11  11 ASP A  275  GLY A  294  1                                  20
HELIX   12  12 SER A  326  ALA A  334  1                                   9
HELIX   13  13 ASP A  338  LEU A  360  1                                  23
SHEET    1   A 4 TRP A  49  ASN A  52  0
SHEET    2   A 4 PHE A  36  ILE A  43 -1  N  GLY A  42   O  HIS A  50
SHEET    3   A 4 ILE A   4  GLY A  11  1  N  PHE A  10   O  ILE A  43
SHEET    4   A 4 VAL A 101  VAL A 106  1  O  ILE A 105   N  ILE A   9
SHEET    1   B 2 LEU A  58  LEU A  59  0
SHEET    2   B 2 ALA A  68  LEU A  69 -1  O  ALA A  68   N  LEU A  59
SHEET    1   C 2 VAL A  76  LEU A  78  0
SHEET    2   C 2 LEU A  87  PRO A  89 -1  O  ARG A  88   N  ALA A  77
SHEET    1   D 4 PHE A 158  ASP A 162  0
SHEET    2   D 4 LYS A 217  ALA A 222 -1  O  VAL A 218   N  PHE A 161
SHEET    3   D 4 LEU A 182  PRO A 186 -1  N  LYS A 185   O  LEU A 219
SHEET    4   D 4 SER A 196  VAL A 198 -1  O  VAL A 198   N  LEU A 182
SHEET    1   E 5 ILE A 268  VAL A 269  0
SHEET    2   E 5 HIS A 240  VAL A 247 -1  N  GLU A 246   O  VAL A 269
SHEET    3   E 5 ARG A 227  LEU A 234 -1  N  LEU A 234   O  HIS A 240
SHEET    4   E 5 MET A 298  LEU A 305 -1  O  ALA A 299   N  VAL A 233
SHEET    5   E 5 ILE A 311  ASN A 317 -1  O  ASN A 317   N  ARG A 300
CISPEP   1 LEU A  180    PRO A  181          0         6.97
CISPEP   2 ILE A  270    PRO A  271          0        -9.03
CISPEP   3 ALA A  307    ASP A  308          0        -7.22
CISPEP   4 ASP A  308    GLY A  309          0       -26.78
CRYST1   83.043   83.043   97.601  90.00  90.00  90.00 P 43 21 2     8
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      0.012042  0.000000  0.000000        0.00000
SCALE2      0.000000  0.012042  0.000000        0.00000
SCALE3      0.000000  0.000000  0.010246        0.00000
      
PROCHECK
Go to PROCHECK summary
 References