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PDBsum entry 3k3p

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Ligase PDB id
3k3p
Jmol
Contents
Protein chains
317 a.a.
Waters ×150
HEADER    LIGASE                                  03-OCT-09   3K3P
TITLE     CRYSTAL STRUCTURE OF THE APO FORM OF D-ALANINE:D-ALANINE LIGASE (DDL)
TITLE    2 FROM STREPTOCOCCUS MUTANS
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: D-ALANINE--D-ALANINE LIGASE;
COMPND   3 CHAIN: A, B;
COMPND   4 SYNONYM: D-ALANYLALANINE SYNTHETASE, D-ALA-D-ALA LIGASE;
COMPND   5 EC: 6.3.2.4;
COMPND   6 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: STREPTOCOCCUS MUTANS;
SOURCE   3 ORGANISM_TAXID: 1309;
SOURCE   4 STRAIN: UA159;
SOURCE   5 GENE: DDL;
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET28A(+)
KEYWDS    D-ALANYL-ALANINE SYNTHETASE, ATP-BINDING, CELL SHAPE, CELL WALL
KEYWDS   2 BIOGENESIS/DEGRADATION, LIGASE, MAGNESIUM, MANGANESE, METAL-BINDING,
KEYWDS   3 NUCLEOTIDE-BINDING, PEPTIDOGLYCAN SYNTHESIS
EXPDTA    X-RAY DIFFRACTION
AUTHOR    Y.LU
REVDAT   1   15-SEP-10 3K3P    0
JRNL        AUTH   Y.LU,H.XU,X.ZHAO
JRNL        TITL   CRYSTAL STRUCTURE OF THE APO FORM OF D-ALANINE:D-ALANINE
JRNL        TITL 2 LIGASE (DDL) FROM STREPTOCOCCUS MUTANS
JRNL        REF    PROTEIN PEPT.LETT.            V.  17  1053 2010
JRNL        REFN                   ISSN 0929-8665
JRNL        PMID   20522004
REMARK   2
REMARK   2 RESOLUTION.    2.23 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) : 2.23
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 17.58
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.9
REMARK   3   NUMBER OF REFLECTIONS             : 37611
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                     : 0.248
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100
REMARK   3   FREE R VALUE TEST SET COUNT      : 1921
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) : 2.23
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.29
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2628
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.71
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2420
REMARK   3   BIN FREE R VALUE SET COUNT          : 141
REMARK   3   BIN FREE R VALUE                    : 0.3340
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 4930
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 0
REMARK   3   SOLVENT ATOMS            : 150
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 29.14
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 0.00000
REMARK   3    B22 (A**2) : 0.00000
REMARK   3    B33 (A**2) : 0.00000
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): 0.256
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.212
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): NULL
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.945
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.916
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  5001 ; 0.023 ; 0.022
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  6766 ; 1.930 ; 1.991
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   625 ; 7.000 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   208 ;36.461 ;25.577
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   909 ;15.943 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    20 ;23.728 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   804 ; 0.125 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3648 ; 0.009 ; 0.020
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  2232 ; 0.215 ; 0.200
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  3421 ; 0.313 ; 0.200
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   232 ; 0.149 ; 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):    42 ; 0.227 ; 0.200
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     6 ; 0.122 ; 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):  3156 ; 1.170 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  5118 ; 2.105 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1845 ; 3.155 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1648 ; 4.752 ; 4.500
REMARK   3
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL
REMARK   3
REMARK   3  NCS RESTRAINTS STATISTICS
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK   3
REMARK   3  TLS DETAILS
REMARK   3   NUMBER OF TLS GROUPS  : NULL
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED : 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 RIDING
REMARK   3  POSITIONS
REMARK   4
REMARK   4 3K3P COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 06-OCT-09.
REMARK 100 THE RCSB ID CODE IS RCSB055506.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 27-DEC-08
REMARK 200  TEMPERATURE           (KELVIN) : 110
REMARK 200  PH                             : 7.0
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : N
REMARK 200  RADIATION SOURCE               : SEALED TUBE
REMARK 200  BEAMLINE                       : NULL
REMARK 200  X-RAY GENERATOR MODEL          : OXFORD DIFFRACTION ENHANCE ULTRA
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.54056
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : OXFORD ONYX CCD
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : CRYSALISPRO
REMARK 200  DATA SCALING SOFTWARE          : SCALA
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 37656
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.230
REMARK 200  RESOLUTION RANGE LOW       (A) : 68.850
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.8
REMARK 200  DATA REDUNDANCY                : 3.600
REMARK 200  R MERGE                    (I) : 0.09200
REMARK 200  R SYM                      (I) : 0.09200
REMARK 200   FOR THE DATA SET  : 16.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.23
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.35
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.8
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.50
REMARK 200  R MERGE FOR SHELL          (I) : 0.60500
REMARK 200  R SYM FOR SHELL            (I) : 0.60500
REMARK 200   FOR SHELL         : 1.200
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 2I87
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 47.72
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.35
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.05M MAGNESIUM SULFATE, 0.05M HEPES,
REMARK 280  1.2M LITHIUM SULFATE, PH 7.0, VAPOR DIFFUSION, HANGING DROP,
REMARK 280  TEMPERATURE 289K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -Y,X-Y,Z+2/3
REMARK 290       3555   -X+Y,-X,Z+1/3
REMARK 290
REMARK 290     WHERE NNN -> OPERATOR NUMBER
REMARK 290           MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   2 -0.500000 -0.866025  0.000000        0.00000
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       72.93333
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       36.46667
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: 3120 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 26290 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -15.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 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   -33
REMARK 465     GLY A   -32
REMARK 465     SER A   -31
REMARK 465     SER A   -30
REMARK 465     HIS A   -29
REMARK 465     HIS A   -28
REMARK 465     HIS A   -27
REMARK 465     HIS A   -26
REMARK 465     HIS A   -25
REMARK 465     HIS A   -24
REMARK 465     SER A   -23
REMARK 465     SER A   -22
REMARK 465     GLY A   -21
REMARK 465     LEU A   -20
REMARK 465     VAL A   -19
REMARK 465     PRO A   -18
REMARK 465     ARG A   -17
REMARK 465     GLY A   -16
REMARK 465     SER A   -15
REMARK 465     HIS A   -14
REMARK 465     MET A   -13
REMARK 465     ALA A   -12
REMARK 465     SER A   -11
REMARK 465     MET A   -10
REMARK 465     THR A    -9
REMARK 465     GLY A    -8
REMARK 465     GLY A    -7
REMARK 465     GLN A    -6
REMARK 465     GLN A    -5
REMARK 465     MET A    -4
REMARK 465     GLY A    -3
REMARK 465     ARG A    -2
REMARK 465     GLY A    -1
REMARK 465     SER A     0
REMARK 465     MET A     1
REMARK 465     SER A     2
REMARK 465     GLU A    61
REMARK 465     THR A    62
REMARK 465     MET A   177
REMARK 465     GLY A   178
REMARK 465     SER A   179
REMARK 465     SER A   180
REMARK 465     VAL A   181
REMARK 465     GLY A   182
REMARK 465     LYS A   237
REMARK 465     ASP A   238
REMARK 465     VAL A   239
REMARK 465     ALA A   240
REMARK 465     PHE A   241
REMARK 465     TYR A   242
REMARK 465     ASP A   243
REMARK 465     TYR A   244
REMARK 465     GLU A   245
REMARK 465     ALA A   246
REMARK 465     LYS A   247
REMARK 465     TYR A   248
REMARK 465     ILE A   249
REMARK 465     ASP A   250
REMARK 465     ASN A   251
REMARK 465     LYS A   252
REMARK 465     ILE A   253
REMARK 465     GLN A   311
REMARK 465     TRP A   312
REMARK 465     HIS A   347
REMARK 465     LEU A   348
REMARK 465     VAL A   349
REMARK 465     MET B   -33
REMARK 465     GLY B   -32
REMARK 465     SER B   -31
REMARK 465     SER B   -30
REMARK 465     HIS B   -29
REMARK 465     HIS B   -28
REMARK 465     HIS B   -27
REMARK 465     HIS B   -26
REMARK 465     HIS B   -25
REMARK 465     HIS B   -24
REMARK 465     SER B   -23
REMARK 465     SER B   -22
REMARK 465     GLY B   -21
REMARK 465     LEU B   -20
REMARK 465     VAL B   -19
REMARK 465     PRO B   -18
REMARK 465     ARG B   -17
REMARK 465     GLY B   -16
REMARK 465     SER B   -15
REMARK 465     HIS B   -14
REMARK 465     MET B   -13
REMARK 465     ALA B   -12
REMARK 465     SER B   -11
REMARK 465     MET B   -10
REMARK 465     THR B    -9
REMARK 465     GLY B    -8
REMARK 465     GLY B    -7
REMARK 465     GLN B    -6
REMARK 465     GLN B    -5
REMARK 465     MET B    -4
REMARK 465     GLY B    -3
REMARK 465     ARG B    -2
REMARK 465     GLY B    -1
REMARK 465     SER B     0
REMARK 465     MET B     1
REMARK 465     SER B     2
REMARK 465     GLU B    61
REMARK 465     THR B    62
REMARK 465     MET B   177
REMARK 465     GLY B   178
REMARK 465     SER B   179
REMARK 465     SER B   180
REMARK 465     VAL B   181
REMARK 465     LYS B   237
REMARK 465     ASP B   238
REMARK 465     VAL B   239
REMARK 465     ALA B   240
REMARK 465     PHE B   241
REMARK 465     TYR B   242
REMARK 465     ASP B   243
REMARK 465     TYR B   244
REMARK 465     GLU B   245
REMARK 465     ALA B   246
REMARK 465     LYS B   247
REMARK 465     TYR B   248
REMARK 465     ILE B   249
REMARK 465     ASP B   250
REMARK 465     ASN B   251
REMARK 465     LYS B   252
REMARK 465     ILE B   253
REMARK 465     GLN B   311
REMARK 465     TRP B   312
REMARK 465     HIS B   347
REMARK 465     LEU B   348
REMARK 465     VAL B   349
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480   M RES C SSEQI ATOMS
REMARK 480     SER B   60   OG
DBREF  3K3P A    1   349  UNP    P95803   DDL_STRMU        1    349
DBREF  3K3P B    1   349  UNP    P95803   DDL_STRMU        1    349
SEQADV 3K3P MET A  -33  UNP  P95803              EXPRESSION TAG
SEQADV 3K3P GLY A  -32  UNP  P95803              EXPRESSION TAG
SEQADV 3K3P SER A  -31  UNP  P95803              EXPRESSION TAG
SEQADV 3K3P SER A  -30  UNP  P95803              EXPRESSION TAG
SEQADV 3K3P HIS A  -29  UNP  P95803              EXPRESSION TAG
SEQADV 3K3P HIS A  -28  UNP  P95803              EXPRESSION TAG
SEQADV 3K3P HIS A  -27  UNP  P95803              EXPRESSION TAG
SEQADV 3K3P HIS A  -26  UNP  P95803              EXPRESSION TAG
SEQADV 3K3P HIS A  -25  UNP  P95803              EXPRESSION TAG
SEQADV 3K3P HIS A  -24  UNP  P95803              EXPRESSION TAG
SEQADV 3K3P SER A  -23  UNP  P95803              EXPRESSION TAG
SEQADV 3K3P SER A  -22  UNP  P95803              EXPRESSION TAG
SEQADV 3K3P GLY A  -21  UNP  P95803              EXPRESSION TAG
SEQADV 3K3P LEU A  -20  UNP  P95803              EXPRESSION TAG
SEQADV 3K3P VAL A  -19  UNP  P95803              EXPRESSION TAG
SEQADV 3K3P PRO A  -18  UNP  P95803              EXPRESSION TAG
SEQADV 3K3P ARG A  -17  UNP  P95803              EXPRESSION TAG
SEQADV 3K3P GLY A  -16  UNP  P95803              EXPRESSION TAG
SEQADV 3K3P SER A  -15  UNP  P95803              EXPRESSION TAG
SEQADV 3K3P HIS A  -14  UNP  P95803              EXPRESSION TAG
SEQADV 3K3P MET A  -13  UNP  P95803              EXPRESSION TAG
SEQADV 3K3P ALA A  -12  UNP  P95803              EXPRESSION TAG
SEQADV 3K3P SER A  -11  UNP  P95803              EXPRESSION TAG
SEQADV 3K3P MET A  -10  UNP  P95803              EXPRESSION TAG
SEQADV 3K3P THR A   -9  UNP  P95803              EXPRESSION TAG
SEQADV 3K3P GLY A   -8  UNP  P95803              EXPRESSION TAG
SEQADV 3K3P GLY A   -7  UNP  P95803              EXPRESSION TAG
SEQADV 3K3P GLN A   -6  UNP  P95803              EXPRESSION TAG
SEQADV 3K3P GLN A   -5  UNP  P95803              EXPRESSION TAG
SEQADV 3K3P MET A   -4  UNP  P95803              EXPRESSION TAG
SEQADV 3K3P GLY A   -3  UNP  P95803              EXPRESSION TAG
SEQADV 3K3P ARG A   -2  UNP  P95803              EXPRESSION TAG
SEQADV 3K3P GLY A   -1  UNP  P95803              EXPRESSION TAG
SEQADV 3K3P SER A    0  UNP  P95803              EXPRESSION TAG
SEQADV 3K3P MET B  -33  UNP  P95803              EXPRESSION TAG
SEQADV 3K3P GLY B  -32  UNP  P95803              EXPRESSION TAG
SEQADV 3K3P SER B  -31  UNP  P95803              EXPRESSION TAG
SEQADV 3K3P SER B  -30  UNP  P95803              EXPRESSION TAG
SEQADV 3K3P HIS B  -29  UNP  P95803              EXPRESSION TAG
SEQADV 3K3P HIS B  -28  UNP  P95803              EXPRESSION TAG
SEQADV 3K3P HIS B  -27  UNP  P95803              EXPRESSION TAG
SEQADV 3K3P HIS B  -26  UNP  P95803              EXPRESSION TAG
SEQADV 3K3P HIS B  -25  UNP  P95803              EXPRESSION TAG
SEQADV 3K3P HIS B  -24  UNP  P95803              EXPRESSION TAG
SEQADV 3K3P SER B  -23  UNP  P95803              EXPRESSION TAG
SEQADV 3K3P SER B  -22  UNP  P95803              EXPRESSION TAG
SEQADV 3K3P GLY B  -21  UNP  P95803              EXPRESSION TAG
SEQADV 3K3P LEU B  -20  UNP  P95803              EXPRESSION TAG
SEQADV 3K3P VAL B  -19  UNP  P95803              EXPRESSION TAG
SEQADV 3K3P PRO B  -18  UNP  P95803              EXPRESSION TAG
SEQADV 3K3P ARG B  -17  UNP  P95803              EXPRESSION TAG
SEQADV 3K3P GLY B  -16  UNP  P95803              EXPRESSION TAG
SEQADV 3K3P SER B  -15  UNP  P95803              EXPRESSION TAG
SEQADV 3K3P HIS B  -14  UNP  P95803              EXPRESSION TAG
SEQADV 3K3P MET B  -13  UNP  P95803              EXPRESSION TAG
SEQADV 3K3P ALA B  -12  UNP  P95803              EXPRESSION TAG
SEQADV 3K3P SER B  -11  UNP  P95803              EXPRESSION TAG
SEQADV 3K3P MET B  -10  UNP  P95803              EXPRESSION TAG
SEQADV 3K3P THR B   -9  UNP  P95803              EXPRESSION TAG
SEQADV 3K3P GLY B   -8  UNP  P95803              EXPRESSION TAG
SEQADV 3K3P GLY B   -7  UNP  P95803              EXPRESSION TAG
SEQADV 3K3P GLN B   -6  UNP  P95803              EXPRESSION TAG
SEQADV 3K3P GLN B   -5  UNP  P95803              EXPRESSION TAG
SEQADV 3K3P MET B   -4  UNP  P95803              EXPRESSION TAG
SEQADV 3K3P GLY B   -3  UNP  P95803              EXPRESSION TAG
SEQADV 3K3P ARG B   -2  UNP  P95803              EXPRESSION TAG
SEQADV 3K3P GLY B   -1  UNP  P95803              EXPRESSION TAG
SEQADV 3K3P SER B    0  UNP  P95803              EXPRESSION TAG
SEQRES   1 A  383  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES   2 A  383  LEU VAL PRO ARG GLY SER HIS MET ALA SER MET THR GLY
SEQRES   3 A  383  GLY GLN GLN MET GLY ARG GLY SER MET SER LYS GLU THR
SEQRES   4 A  383  LEU VAL LEU LEU TYR GLY GLY ARG SER ALA GLU ARG ASP
SEQRES   5 A  383  VAL SER VAL LEU SER ALA GLU SER VAL MET ARG ALA ILE
SEQRES   6 A  383  ASN TYR ASP ASN PHE LEU VAL LYS THR TYR PHE ILE THR
SEQRES   7 A  383  GLN ALA GLY ASP PHE ILE LYS THR GLN GLU PHE ASP SER
SEQRES   8 A  383  GLN PRO SER GLU THR ASP LYS LEU MET THR ASN ASP THR
SEQRES   9 A  383  ILE ILE ALA SER GLN LYS ILE LYS PRO SER ASP ILE TYR
SEQRES  10 A  383  GLU GLU GLU ALA VAL VAL PHE PRO VAL LEU HIS GLY PRO
SEQRES  11 A  383  MET GLY GLU ASP GLY SER ILE GLN GLY PHE LEU GLU VAL
SEQRES  12 A  383  LEU LYS MET PRO TYR VAL GLY THR ASN ILE LEU SER SER
SEQRES  13 A  383  SER VAL ALA MET ASP LYS ILE THR THR ASN GLN VAL LEU
SEQRES  14 A  383  GLU SER ALA THR THR ILE PRO GLN VAL ALA TYR VAL ALA
SEQRES  15 A  383  LEU ILE GLU GLY GLU PRO LEU GLU SER LYS LEU ALA GLU
SEQRES  16 A  383  VAL GLU GLU LYS LEU ILE TYR PRO VAL PHE VAL LYS PRO
SEQRES  17 A  383  ALA ASN MET GLY SER SER VAL GLY ILE SER LYS ALA GLU
SEQRES  18 A  383  ASN ARG THR ASP LEU LYS GLN ALA ILE ALA LEU ALA LEU
SEQRES  19 A  383  LYS TYR ASP SER ARG VAL LEU ILE GLU GLN GLY VAL ASP
SEQRES  20 A  383  ALA ARG GLU ILE GLU VAL GLY ILE LEU GLY ASN THR ASP
SEQRES  21 A  383  VAL LYS THR THR LEU PRO GLY GLU ILE VAL LYS ASP VAL
SEQRES  22 A  383  ALA PHE TYR ASP TYR GLU ALA LYS TYR ILE ASP ASN LYS
SEQRES  23 A  383  ILE THR MET ALA ILE PRO ALA GLU ILE ASP PRO VAL ILE
SEQRES  24 A  383  VAL GLU LYS MET ARG ASP TYR ALA ALA THR ALA PHE ARG
SEQRES  25 A  383  THR LEU GLY CYS CYS GLY LEU SER ARG CYS ASP PHE PHE
SEQRES  26 A  383  LEU THR GLU ASP GLY LYS VAL TYR LEU ASN GLU LEU ASN
SEQRES  27 A  383  THR MET PRO GLY PHE THR GLN TRP SER MET TYR PRO LEU
SEQRES  28 A  383  LEU TRP GLU ASN MET GLY LEU SER TYR SER VAL LEU ILE
SEQRES  29 A  383  GLU GLU LEU VAL SER LEU ALA LYS GLU MET PHE ASP LYS
SEQRES  30 A  383  ARG GLU SER HIS LEU VAL
SEQRES   1 B  383  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES   2 B  383  LEU VAL PRO ARG GLY SER HIS MET ALA SER MET THR GLY
SEQRES   3 B  383  GLY GLN GLN MET GLY ARG GLY SER MET SER LYS GLU THR
SEQRES   4 B  383  LEU VAL LEU LEU TYR GLY GLY ARG SER ALA GLU ARG ASP
SEQRES   5 B  383  VAL SER VAL LEU SER ALA GLU SER VAL MET ARG ALA ILE
SEQRES   6 B  383  ASN TYR ASP ASN PHE LEU VAL LYS THR TYR PHE ILE THR
SEQRES   7 B  383  GLN ALA GLY ASP PHE ILE LYS THR GLN GLU PHE ASP SER
SEQRES   8 B  383  GLN PRO SER GLU THR ASP LYS LEU MET THR ASN ASP THR
SEQRES   9 B  383  ILE ILE ALA SER GLN LYS ILE LYS PRO SER ASP ILE TYR
SEQRES  10 B  383  GLU GLU GLU ALA VAL VAL PHE PRO VAL LEU HIS GLY PRO
SEQRES  11 B  383  MET GLY GLU ASP GLY SER ILE GLN GLY PHE LEU GLU VAL
SEQRES  12 B  383  LEU LYS MET PRO TYR VAL GLY THR ASN ILE LEU SER SER
SEQRES  13 B  383  SER VAL ALA MET ASP LYS ILE THR THR ASN GLN VAL LEU
SEQRES  14 B  383  GLU SER ALA THR THR ILE PRO GLN VAL ALA TYR VAL ALA
SEQRES  15 B  383  LEU ILE GLU GLY GLU PRO LEU GLU SER LYS LEU ALA GLU
SEQRES  16 B  383  VAL GLU GLU LYS LEU ILE TYR PRO VAL PHE VAL LYS PRO
SEQRES  17 B  383  ALA ASN MET GLY SER SER VAL GLY ILE SER LYS ALA GLU
SEQRES  18 B  383  ASN ARG THR ASP LEU LYS GLN ALA ILE ALA LEU ALA LEU
SEQRES  19 B  383  LYS TYR ASP SER ARG VAL LEU ILE GLU GLN GLY VAL ASP
SEQRES  20 B  383  ALA ARG GLU ILE GLU VAL GLY ILE LEU GLY ASN THR ASP
SEQRES  21 B  383  VAL LYS THR THR LEU PRO GLY GLU ILE VAL LYS ASP VAL
SEQRES  22 B  383  ALA PHE TYR ASP TYR GLU ALA LYS TYR ILE ASP ASN LYS
SEQRES  23 B  383  ILE THR MET ALA ILE PRO ALA GLU ILE ASP PRO VAL ILE
SEQRES  24 B  383  VAL GLU LYS MET ARG ASP TYR ALA ALA THR ALA PHE ARG
SEQRES  25 B  383  THR LEU GLY CYS CYS GLY LEU SER ARG CYS ASP PHE PHE
SEQRES  26 B  383  LEU THR GLU ASP GLY LYS VAL TYR LEU ASN GLU LEU ASN
SEQRES  27 B  383  THR MET PRO GLY PHE THR GLN TRP SER MET TYR PRO LEU
SEQRES  28 B  383  LEU TRP GLU ASN MET GLY LEU SER TYR SER VAL LEU ILE
SEQRES  29 B  383  GLU GLU LEU VAL SER LEU ALA LYS GLU MET PHE ASP LYS
SEQRES  30 B  383  ARG GLU SER HIS LEU VAL
FORMUL   3  HOH   *150(H2 O)
HELIX    1   1 GLU A   16  ILE A   31  1                                  16
HELIX    2   2 ILE A   72  SER A   74  5                                   3
HELIX    3   3 LYS A   78  TYR A   83  5                                   6
HELIX    4   4 GLY A  101  LEU A  110  1                                  10
HELIX    5   5 ASN A  118  ASP A  127  1                                  10
HELIX    6   6 ASP A  127  THR A  139  1                                  13
HELIX    7   7 PRO A  154  LEU A  166  1                                  13
HELIX    8   8 ASN A  188  ASP A  203  1                                  16
HELIX    9   9 ASP A  262  LEU A  280  1                                  19
HELIX   10  10 SER A  313  MET A  322  1                                  10
HELIX   11  11 SER A  325  SER A  346  1                                  22
HELIX   12  12 GLU B   16  ILE B   31  1                                  16
HELIX   13  13 ILE B   72  SER B   74  5                                   3
HELIX   14  14 LYS B   78  TYR B   83  5                                   6
HELIX   15  15 GLY B  101  LEU B  110  1                                  10
HELIX   16  16 ASN B  118  ASP B  127  1                                  10
HELIX   17  17 ASP B  127  THR B  139  1                                  13
HELIX   18  18 PRO B  154  LEU B  166  1                                  13
HELIX   19  19 ASN B  188  ASP B  203  1                                  16
HELIX   20  20 ASP B  262  GLY B  281  1                                  20
HELIX   21  21 SER B  313  MET B  322  1                                  10
HELIX   22  22 SER B  325  SER B  346  1                                  22
SHEET    1   A 5 LYS A  76  ILE A  77  0
SHEET    2   A 5 PHE A  49  PHE A  55 -1  N  PHE A  49   O  ILE A  77
SHEET    3   A 5 PHE A  36  ILE A  43 -1  N  PHE A  42   O  ILE A  50
SHEET    4   A 5 GLU A   4  GLY A  11  1  N  LEU A   6   O  LYS A  39
SHEET    5   A 5 VAL A  88  VAL A  92  1  O  VAL A  92   N  LEU A   9
SHEET    1   B 4 TYR A 146  ILE A 150  0
SHEET    2   B 4 ARG A 205  GLN A 210 -1  O  VAL A 206   N  LEU A 149
SHEET    3   B 4 VAL A 170  PRO A 174 -1  N  LYS A 173   O  LEU A 207
SHEET    4   B 4 SER A 184  ALA A 186 -1  O  SER A 184   N  VAL A 172
SHEET    1   C 3 LYS A 228  THR A 229  0
SHEET    2   C 3 ARG A 215  GLY A 223 -1  N  LEU A 222   O  LYS A 228
SHEET    3   C 3 GLY A 233  ILE A 235 -1  O  GLY A 233   N  GLU A 218
SHEET    1   D 4 LYS A 228  THR A 229  0
SHEET    2   D 4 ARG A 215  GLY A 223 -1  N  LEU A 222   O  LYS A 228
SHEET    3   D 4 GLY A 284  LEU A 292 -1  O  PHE A 290   N  ILE A 217
SHEET    4   D 4 VAL A 298  ASN A 304 -1  O  GLU A 302   N  ASP A 289
SHEET    1   E 5 LYS B  76  ILE B  77  0
SHEET    2   E 5 PHE B  49  PHE B  55 -1  N  PHE B  49   O  ILE B  77
SHEET    3   E 5 PHE B  36  ILE B  43 -1  N  PHE B  42   O  ILE B  50
SHEET    4   E 5 GLU B   4  GLY B  11  1  N  GLU B   4   O  LEU B  37
SHEET    5   E 5 VAL B  88  VAL B  92  1  O  PHE B  90   N  VAL B   7
SHEET    1   F 4 TYR B 146  ILE B 150  0
SHEET    2   F 4 ARG B 205  GLN B 210 -1  O  VAL B 206   N  LEU B 149
SHEET    3   F 4 VAL B 170  PRO B 174 -1  N  PHE B 171   O  GLU B 209
SHEET    4   F 4 SER B 184  ALA B 186 -1  O  ALA B 186   N  VAL B 170
SHEET    1   G 3 LYS B 228  THR B 229  0
SHEET    2   G 3 ARG B 215  GLY B 223 -1  N  LEU B 222   O  LYS B 228
SHEET    3   G 3 GLY B 233  ILE B 235 -1  O  GLY B 233   N  GLU B 218
SHEET    1   H 4 LYS B 228  THR B 229  0
SHEET    2   H 4 ARG B 215  GLY B 223 -1  N  LEU B 222   O  LYS B 228
SHEET    3   H 4 GLY B 284  LEU B 292 -1  O  PHE B 290   N  ILE B 217
SHEET    4   H 4 VAL B 298  ASN B 304 -1  O  ASN B 304   N  ARG B 287
CISPEP   1 TYR A  168    PRO A  169          0        -1.54
CISPEP   2 ILE A  257    PRO A  258          0        -2.65
CISPEP   3 TYR B  168    PRO B  169          0        -6.08
CISPEP   4 ILE B  257    PRO B  258          0        -3.94
CRYST1   79.502   79.502  109.400  90.00  90.00 120.00 P 32          6
ORIGX1      1.000000  0.000000  0.000000        0.00000
ORIGX2      0.000000  1.000000  0.000000        0.00000
ORIGX3      0.000000  0.000000  1.000000        0.00000
SCALE1      0.012578  0.007262  0.000000        0.00000
SCALE2      0.000000  0.014524  0.000000        0.00000
SCALE3      0.000000  0.000000  0.009141        0.00000
      
PROCHECK
Go to PROCHECK summary
 References