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PDBsum entry 3tw5

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Top Page protein ligands Protein-protein interface(s) links
Transferase PDB id
3tw5
Jmol
Contents
Protein chains
344 a.a.
Ligands
CXS ×2
HEADER    TRANSFERASE                             21-SEP-11   3TW5
TITLE     CRYSTAL STRUCTURE OF THE GP42 TRANSGLUTAMINASE FROM PHYTOPHTHORA SOJAE
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: TRANSGLUTAMINASE ELICITOR;
COMPND   3 CHAIN: A, B;
COMPND   4 FRAGMENT: TRANSGLUTAMINASE DOMAIN;
COMPND   5 EC: 2.3.2.13;
COMPND   6 ENGINEERED: YES;
COMPND   7 MUTATION: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: PHYTOPHTHORA SOJAE;
SOURCE   3 ORGANISM_TAXID: 67593;
SOURCE   4 EXPRESSION_SYSTEM: PICHIA PASTORIS;
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 4922;
SOURCE   6 EXPRESSION_SYSTEM_STRAIN: GS115;
SOURCE   7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PPIC9K
KEYWDS    CYSTEINE PROTEASE, CONVERGENT EVOLUTION, INNATE IMMUNITY, PATHOGEN-
KEYWDS   2 ASSOCIATED MOLECULAR PATTERN (PAMP), PHYTOPHTHORA, TRANGLUTAMINASE,
KEYWDS   3 TRANSFERASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    K.REISS,E.KIRCHNER,G.ZOCHER,T.STEHLE
REVDAT   3   21-DEC-11 3TW5    1       JRNL
REVDAT   2   26-OCT-11 3TW5    1       JRNL
REVDAT   1   12-OCT-11 3TW5    0
JRNL        AUTH   K.REISS,E.KIRCHNER,M.GIJZEN,G.ZOCHER,B.LOFFELHARDT,
JRNL        AUTH 2 T.NURNBERGER,T.STEHLE,F.BRUNNER
JRNL        TITL   STRUCTURAL AND PHYLOGENETIC ANALYSES OF THE GP42
JRNL        TITL 2 TRANSGLUTAMINASE FROM PHYTOPHTHORA SOJAE REVEAL AN
JRNL        TITL 3 EVOLUTIONARY RELATIONSHIP BETWEEN OOMYCETES AND MARINE
JRNL        TITL 4 VIBRIO BACTERIA.
JRNL        REF    J.BIOL.CHEM.                  V. 286 42585 2011
JRNL        REFN                   ISSN 0021-9258
JRNL        PMID   21994936
JRNL        DOI    10.1074/JBC.M111.290544
REMARK   2
REMARK   2 RESOLUTION.    2.95 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.5.0109
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) : 2.95
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.00
REMARK   3   DATA CUTOFF            (SIGMA(F)) : -3.000
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.6
REMARK   3   NUMBER OF REFLECTIONS             : 30288
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) : 0.216
REMARK   3   R VALUE            (WORKING SET) : 0.215
REMARK   3   FREE R VALUE                     : 0.234
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000
REMARK   3   FREE R VALUE TEST SET COUNT      : 1594
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) : 2.95
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.03
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2220
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 98.16
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2940
REMARK   3   BIN FREE R VALUE SET COUNT          : 121
REMARK   3   BIN FREE R VALUE                    : 0.3630
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 5227
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 28
REMARK   3   SOLVENT ATOMS            : 0
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 42.40
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 45.92
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : -1.75000
REMARK   3    B22 (A**2) : -1.75000
REMARK   3    B33 (A**2) : 2.62000
REMARK   3    B12 (A**2) : -0.87000
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): 0.296
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.221
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 12.137
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.917
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.899
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  5403 ; 0.006 ; 0.022
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  7383 ; 0.889 ; 1.943
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   684 ; 4.461 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   224 ;36.281 ;25.179
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   783 ;13.377 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):     8 ; 9.963 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   808 ; 0.060 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  4140 ; 0.003 ; 0.021
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL
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):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL
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):  3412 ; 0.341 ; 2.000
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  5463 ; 0.616 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1991 ; 0.304 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1920 ; 0.529 ; 3.000
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 : 1
REMARK   3
REMARK   3  NCS GROUP NUMBER               : 1
REMARK   3     CHAIN NAMES                    : A B
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE
REMARK   3           1     A    163       A     528      4
REMARK   3           1     B    163       B     528      4
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT
REMARK   3   MEDIUM POSITIONAL  1    A    (A):   2604 ;  0.24 ;  0.50
REMARK   3   MEDIUM THERMAL     1    B (A**2):   2604 ;  0.12 ;  2.00
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   : 1.40
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 3TW5 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-OCT-11.
REMARK 100 THE RCSB ID CODE IS RCSB067994.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 28-JUN-10; 25-FEB-10
REMARK 200  TEMPERATURE           (KELVIN) : 100; 100
REMARK 200  PH                             : 11.0
REMARK 200  NUMBER OF CRYSTALS USED        : 2
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y; Y
REMARK 200  RADIATION SOURCE               : SLS; SLS
REMARK 200  BEAMLINE                       : X06DA; X06DA
REMARK 200  X-RAY GENERATOR MODEL          : NULL; NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M; M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0; 1.255
REMARK 200  MONOCHROMATOR                  : SI(111); SI(111)
REMARK 200  OPTICS                         : NULL; NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD; CCD
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 225 MM CCD; MARMOSAIC
REMARK 200                                   225 MM CCD
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200  DATA SCALING SOFTWARE          : XSCALE
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 31882
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.950
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.4
REMARK 200  DATA REDUNDANCY                : 3.700
REMARK 200  R MERGE                    (I) : 0.14000
REMARK 200  R SYM                      (I) : 0.09000
REMARK 200   FOR THE DATA SET  : 15.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.95
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.03
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.2
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.70
REMARK 200  R MERGE FOR SHELL          (I) : 66.00000
REMARK 200  R SYM FOR SHELL            (I) : 58.30000
REMARK 200   FOR SHELL         : 2.750
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH; MAD
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SIRAS
REMARK 200 SOFTWARE USED: SHARP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 73.87
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.71
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.6M AMMONIUM SULFATE, 0.2M LITHIUM
REMARK 280  SULFATE, 0.1M N-CYCLOHEXYL-3-AMINOPROPANESULFONIC ACID (CAPS), PH
REMARK 280  11.0, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 62 2 2
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       4555   -X,-Y,Z
REMARK 290       5555   Y,-X+Y,Z+2/3
REMARK 290       6555   X-Y,X,Z+1/3
REMARK 290       7555   Y,X,-Z+2/3
REMARK 290       8555   X-Y,-Y,-Z
REMARK 290       9555   -X,-X+Y,-Z+1/3
REMARK 290      10555   -Y,-X,-Z+2/3
REMARK 290      11555   -X+Y,Y,-Z
REMARK 290      12555   X,X-Y,-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       91.53333
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       45.76667
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       91.53333
REMARK 290   SMTRY1   6  0.500000 -0.866025  0.000000        0.00000
REMARK 290   SMTRY2   6  0.866025  0.500000  0.000000        0.00000
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       45.76667
REMARK 290   SMTRY1   7 -0.500000  0.866025  0.000000        0.00000
REMARK 290   SMTRY2   7  0.866025  0.500000  0.000000        0.00000
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       91.53333
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   9 -0.500000 -0.866025  0.000000        0.00000
REMARK 290   SMTRY2   9 -0.866025  0.500000  0.000000        0.00000
REMARK 290   SMTRY3   9  0.000000  0.000000 -1.000000       45.76667
REMARK 290   SMTRY1  10  0.500000 -0.866025  0.000000        0.00000
REMARK 290   SMTRY2  10 -0.866025 -0.500000  0.000000        0.00000
REMARK 290   SMTRY3  10  0.000000  0.000000 -1.000000       91.53333
REMARK 290   SMTRY1  11 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2  11  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3  11  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1  12  0.500000  0.866025  0.000000        0.00000
REMARK 290   SMTRY2  12  0.866025 -0.500000  0.000000        0.00000
REMARK 290   SMTRY3  12  0.000000  0.000000 -1.000000       45.76667
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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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     ALA A   339
REMARK 465     ARG A   340
REMARK 465     PHE A   341
REMARK 465     ASN A   342
REMARK 465     GLY A   343
REMARK 465     GLY A   344
REMARK 465     THR A   345
REMARK 465     ASP A   346
REMARK 465     THR A   347
REMARK 465     THR A   348
REMARK 465     ASP A   349
REMARK 465     GLU A   350
REMARK 465     TYR A   351
REMARK 465     GLY A   352
REMARK 465     ARG A   353
REMARK 465     HIS A   354
REMARK 465     SER A   355
REMARK 465     ASN A   356
REMARK 465     ASN A   357
REMARK 465     ALA A   358
REMARK 465     TYR A   359
REMARK 465     ARG A   360
REMARK 465     ALA A   529
REMARK 465     ALA B   339
REMARK 465     ARG B   340
REMARK 465     PHE B   341
REMARK 465     ASN B   342
REMARK 465     GLY B   343
REMARK 465     GLY B   344
REMARK 465     THR B   345
REMARK 465     ASP B   346
REMARK 465     THR B   347
REMARK 465     THR B   348
REMARK 465     ASP B   349
REMARK 465     GLU B   350
REMARK 465     TYR B   351
REMARK 465     GLY B   352
REMARK 465     ARG B   353
REMARK 465     HIS B   354
REMARK 465     SER B   355
REMARK 465     ASN B   356
REMARK 465     ASN B   357
REMARK 465     ALA B   358
REMARK 465     TYR B   359
REMARK 465     ARG B   360
REMARK 465     ALA B   529
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     LYS A 180    CG   CD   CE   NZ
REMARK 470     LYS A 186    CG   CD   CE   NZ
REMARK 470     LYS A 235    CG   CD   CE   NZ
REMARK 470     LYS A 243    CG   CD   CE   NZ
REMARK 470     LYS A 254    CG   CD   CE   NZ
REMARK 470     LYS A 255    CG   CD   CE   NZ
REMARK 470     LYS A 308    CG   CD   CE   NZ
REMARK 470     ARG A 331    CG   CD   NE   CZ   NH1  NH2
REMARK 470     LYS B 180    CG   CD   CE   NZ
REMARK 470     LYS B 186    CG   CD   CE   NZ
REMARK 470     GLN B 217    CG   CD   OE1  NE2
REMARK 470     LYS B 243    CG   CD   CE   NZ
REMARK 470     LYS B 244    CG   CD   CE   NZ
REMARK 470     LYS B 254    CG   CD   CE   NZ
REMARK 470     LYS B 255    CG   CD   CE   NZ
REMARK 470     ASP B 260    CG   OD1  OD2
REMARK 470     LYS B 277    CG   CD   CE   NZ
REMARK 470     LYS B 308    CG   CD   CE   NZ
REMARK 470     ARG B 331    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    TRP A 204       69.23     36.39
REMARK 500    SER A 210     -128.07     44.53
REMARK 500    ALA A 388        6.87     59.02
REMARK 500    ASN A 426      108.54   -164.32
REMARK 500    ASP A 490       75.77   -109.02
REMARK 500    ASP B 209       42.91     71.79
REMARK 500    SER B 210     -129.74     47.60
REMARK 500    ASN B 426      108.08   -160.75
REMARK 500    TYR B 485     -137.13     51.57
REMARK 500    ASN B 505        6.00     80.67
REMARK 500    CYS B 527       73.18     57.18
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 CXS A 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CXS A 530
DBREF  3TW5 A  163   529  UNP    Q6Q475   Q6Q475_9STRA   163    529
DBREF  3TW5 B  163   529  UNP    Q6Q475   Q6Q475_9STRA   163    529
SEQADV 3TW5 SER A  290  UNP  Q6Q475    CYS   290 ENGINEERED MUTATION
SEQADV 3TW5 SER B  290  UNP  Q6Q475    CYS   290 ENGINEERED MUTATION
SEQRES   1 A  367  GLU ALA ASN GLY ASN GLN ASP ILE ALA LYS LEU GLU ALA
SEQRES   2 A  367  TYR PHE GLY THR LYS MET GLU MET THR LEU LYS ASP LEU
SEQRES   3 A  367  PRO THR VAL GLY VAL HIS THR PRO SER PRO TRP ALA GLY
SEQRES   4 A  367  PRO TYR TRP PRO THR TYR GLN ASP SER ILE ASN VAL GLN
SEQRES   5 A  367  TRP SER GLN GLY GLN PRO SER ALA ALA GLU LYS TYR ALA
SEQRES   6 A  367  LYS ALA PHE GLY LYS ASP VAL LYS THR PHE MET ASP ALA
SEQRES   7 A  367  VAL SER LYS LYS ASN GLY ILE ASP SER GLN SER GLY ARG
SEQRES   8 A  367  LYS LYS CYS SER SER ASP ASP ASP CYS SER THR LEU THR
SEQRES   9 A  367  ASP GLY SER SER CYS SER ILE ARG THR GLY LYS THR SER
SEQRES  10 A  367  GLY TYR CYS ILE PRO THR TRP PHE GLY ILE SER HIS ALA
SEQRES  11 A  367  TRP SER PRO ALA ALA ILE LEU GLU THR GLU PRO LYS CYS
SEQRES  12 A  367  PRO VAL LYS HIS ASN GLY VAL THR PHE GLN PRO MET ASP
SEQRES  13 A  367  LEU LYS ALA LEU VAL SER LEU VAL TYR ASP GLY ALA ARG
SEQRES  14 A  367  VAL GLN THR VAL PHE THR GLY ALA ARG PHE ASN GLY GLY
SEQRES  15 A  367  THR ASP THR THR ASP GLU TYR GLY ARG HIS SER ASN ASN
SEQRES  16 A  367  ALA TYR ARG ASP LEU ASN PRO ALA TYR PHE HIS ILE ALA
SEQRES  17 A  367  SER ALA ASN ILE LEU GLY LYS LEU ASN SER THR PHE VAL
SEQRES  18 A  367  ALA ASP VAL THR ALA GLY ALA GLU VAL TRP ASN GLN PRO
SEQRES  19 A  367  VAL ARG GLY PHE LYS VAL TYR GLU GLN THR GLU MET THR
SEQRES  20 A  367  LEU GLU GLU GLY ALA GLN THR PHE TYR GLY LEU GLU ALA
SEQRES  21 A  367  TYR PRO TRP ASN ALA ALA ALA LYS SER LEU VAL TYR VAL
SEQRES  22 A  367  LYS SER ARG LEU SER TRP ILE TYR GLU THR TYR THR ASP
SEQRES  23 A  367  GLY GLY LEU VAL SER SER GLY GLN ILE ASP LYS PHE THR
SEQRES  24 A  367  THR GLY GLN TYR TYR TYR TYR LEU LEU GLU LEU ASP ASP
SEQRES  25 A  367  ALA GLY GLU ILE ILE GLY GLY GLU TRP VAL TYR GLY SER
SEQRES  26 A  367  ASP ASP ASP HIS PRO ASP PHE LEU TRP LEU PRO LYS ALA
SEQRES  27 A  367  LYS PRO ALA ALA ASN THR VAL THR SER VAL GLY LEU SER
SEQRES  28 A  367  TYR ALA ASP VAL SER MET LEU LEU LYS LYS SER ALA ALA
SEQRES  29 A  367  CYS THR ALA
SEQRES   1 B  367  GLU ALA ASN GLY ASN GLN ASP ILE ALA LYS LEU GLU ALA
SEQRES   2 B  367  TYR PHE GLY THR LYS MET GLU MET THR LEU LYS ASP LEU
SEQRES   3 B  367  PRO THR VAL GLY VAL HIS THR PRO SER PRO TRP ALA GLY
SEQRES   4 B  367  PRO TYR TRP PRO THR TYR GLN ASP SER ILE ASN VAL GLN
SEQRES   5 B  367  TRP SER GLN GLY GLN PRO SER ALA ALA GLU LYS TYR ALA
SEQRES   6 B  367  LYS ALA PHE GLY LYS ASP VAL LYS THR PHE MET ASP ALA
SEQRES   7 B  367  VAL SER LYS LYS ASN GLY ILE ASP SER GLN SER GLY ARG
SEQRES   8 B  367  LYS LYS CYS SER SER ASP ASP ASP CYS SER THR LEU THR
SEQRES   9 B  367  ASP GLY SER SER CYS SER ILE ARG THR GLY LYS THR SER
SEQRES  10 B  367  GLY TYR CYS ILE PRO THR TRP PHE GLY ILE SER HIS ALA
SEQRES  11 B  367  TRP SER PRO ALA ALA ILE LEU GLU THR GLU PRO LYS CYS
SEQRES  12 B  367  PRO VAL LYS HIS ASN GLY VAL THR PHE GLN PRO MET ASP
SEQRES  13 B  367  LEU LYS ALA LEU VAL SER LEU VAL TYR ASP GLY ALA ARG
SEQRES  14 B  367  VAL GLN THR VAL PHE THR GLY ALA ARG PHE ASN GLY GLY
SEQRES  15 B  367  THR ASP THR THR ASP GLU TYR GLY ARG HIS SER ASN ASN
SEQRES  16 B  367  ALA TYR ARG ASP LEU ASN PRO ALA TYR PHE HIS ILE ALA
SEQRES  17 B  367  SER ALA ASN ILE LEU GLY LYS LEU ASN SER THR PHE VAL
SEQRES  18 B  367  ALA ASP VAL THR ALA GLY ALA GLU VAL TRP ASN GLN PRO
SEQRES  19 B  367  VAL ARG GLY PHE LYS VAL TYR GLU GLN THR GLU MET THR
SEQRES  20 B  367  LEU GLU GLU GLY ALA GLN THR PHE TYR GLY LEU GLU ALA
SEQRES  21 B  367  TYR PRO TRP ASN ALA ALA ALA LYS SER LEU VAL TYR VAL
SEQRES  22 B  367  LYS SER ARG LEU SER TRP ILE TYR GLU THR TYR THR ASP
SEQRES  23 B  367  GLY GLY LEU VAL SER SER GLY GLN ILE ASP LYS PHE THR
SEQRES  24 B  367  THR GLY GLN TYR TYR TYR TYR LEU LEU GLU LEU ASP ASP
SEQRES  25 B  367  ALA GLY GLU ILE ILE GLY GLY GLU TRP VAL TYR GLY SER
SEQRES  26 B  367  ASP ASP ASP HIS PRO ASP PHE LEU TRP LEU PRO LYS ALA
SEQRES  27 B  367  LYS PRO ALA ALA ASN THR VAL THR SER VAL GLY LEU SER
SEQRES  28 B  367  TYR ALA ASP VAL SER MET LEU LEU LYS LYS SER ALA ALA
SEQRES  29 B  367  CYS THR ALA
HET    CXS  A   1      14
HET    CXS  A 530      14
HETNAM     CXS 3-CYCLOHEXYL-1-PROPYLSULFONIC ACID
FORMUL   3  CXS    2(C9 H19 N O3 S)
HELIX    1   1 GLY A  166  GLY A  178  1                                  13
HELIX    2   2 THR A  184  LEU A  188  5                                   5
HELIX    3   3 PRO A  205  VAL A  213  5                                   9
HELIX    4   4 SER A  221  PHE A  230  1                                  10
HELIX    5   5 ASP A  233  ASN A  245  1                                  13
HELIX    6   6 GLY A  246  SER A  251  5                                   6
HELIX    7   7 SER A  258  LEU A  265  5                                   8
HELIX    8   8 ILE A  289  GLU A  300  1                                  12
HELIX    9   9 GLN A  315  ALA A  330  1                                  16
HELIX   10  10 ASN A  363  LYS A  377  1                                  15
HELIX   11  11 THR A  409  GLY A  419  1                                  11
HELIX   12  12 GLY A  455  LYS A  459  5                                   5
HELIX   13  13 SER A  513  CYS A  527  1                                  15
HELIX   14  14 GLY B  166  GLY B  178  1                                  13
HELIX   15  15 THR B  184  LEU B  188  5                                   5
HELIX   16  16 PRO B  205  VAL B  213  5                                   9
HELIX   17  17 SER B  221  PHE B  230  1                                  10
HELIX   18  18 ASP B  233  ASN B  245  1                                  13
HELIX   19  19 GLY B  246  SER B  251  5                                   6
HELIX   20  20 SER B  258  SER B  263  5                                   6
HELIX   21  21 ILE B  289  GLU B  300  1                                  12
HELIX   22  22 GLN B  315  GLY B  329  1                                  15
HELIX   23  23 ASN B  363  LYS B  377  1                                  15
HELIX   24  24 THR B  409  GLY B  419  1                                  11
HELIX   25  25 GLY B  450  GLY B  455  1                                   6
HELIX   26  26 GLN B  456  LYS B  459  5                                   4
HELIX   27  27 TYR B  485  ASP B  489  5                                   5
HELIX   28  28 SER B  513  CYS B  527  1                                  15
SHEET    1   A 5 VAL A 191  VAL A 193  0
SHEET    2   A 5 ASN A 394  MET A 408 -1  O  PHE A 400   N  GLY A 192
SHEET    3   A 5 VAL A 383  ASP A 385 -1  N  ALA A 384   O  GLN A 395
SHEET    4   A 5 LEU A 495  PRO A 498 -1  O  TRP A 496   N  VAL A 383
SHEET    5   A 5 THR A 334  THR A 337 -1  N  VAL A 335   O  LEU A 497
SHEET    1   B 5 VAL A 191  VAL A 193  0
SHEET    2   B 5 ASN A 394  MET A 408 -1  O  PHE A 400   N  GLY A 192
SHEET    3   B 5 SER A 431  ILE A 442 -1  O  SER A 440   N  ARG A 398
SHEET    4   B 5 THR A 461  LEU A 472 -1  O  TYR A 468   N  VAL A 435
SHEET    5   B 5 ILE A 478  TRP A 483 -1  O  GLY A 480   N  GLU A 471
SHEET    1   C 3 LYS A 255  CYS A 256  0
SHEET    2   C 3 GLY A 280  PRO A 284 -1  O  GLY A 280   N  CYS A 256
SHEET    3   C 3 SER A 269  SER A 272 -1  N  SER A 272   O  TYR A 281
SHEET    1   D 2 VAL A 307  HIS A 309  0
SHEET    2   D 2 VAL A 312  PHE A 314 -1  O  PHE A 314   N  VAL A 307
SHEET    1   E 5 VAL B 191  VAL B 193  0
SHEET    2   E 5 ASN B 394  MET B 408 -1  O  PHE B 400   N  GLY B 192
SHEET    3   E 5 VAL B 383  ASP B 385 -1  N  ALA B 384   O  GLN B 395
SHEET    4   E 5 LEU B 495  PRO B 498 -1  O  TRP B 496   N  VAL B 383
SHEET    5   E 5 THR B 334  THR B 337 -1  N  VAL B 335   O  LEU B 497
SHEET    1   F 5 VAL B 191  VAL B 193  0
SHEET    2   F 5 ASN B 394  MET B 408 -1  O  PHE B 400   N  GLY B 192
SHEET    3   F 5 SER B 431  ILE B 442 -1  O  SER B 440   N  GLY B 399
SHEET    4   F 5 THR B 461  LEU B 472 -1  O  TYR B 466   N  SER B 437
SHEET    5   F 5 ILE B 478  TRP B 483 -1  O  GLY B 480   N  GLU B 471
SHEET    1   G 3 LYS B 255  CYS B 256  0
SHEET    2   G 3 GLY B 280  PRO B 284 -1  O  GLY B 280   N  CYS B 256
SHEET    3   G 3 SER B 269  SER B 272 -1  N  SER B 272   O  TYR B 281
SHEET    1   H 2 VAL B 307  HIS B 309  0
SHEET    2   H 2 VAL B 312  PHE B 314 -1  O  PHE B 314   N  VAL B 307
SSBOND   1 CYS A  256    CYS A  271                          1555   1555  2.04
SSBOND   2 CYS A  262    CYS A  282                          1555   1555  2.03
SSBOND   3 CYS A  305    CYS A  527                          1555   1555  2.04
SSBOND   4 CYS B  256    CYS B  271                          1555   1555  2.04
SSBOND   5 CYS B  262    CYS B  282                          1555   1555  2.02
SSBOND   6 CYS B  305    CYS B  527                          1555   1555  2.04
CISPEP   1 THR A  195    PRO A  196          0        -2.11
CISPEP   2 THR B  195    PRO B  196          0        -2.20
SITE     1 AC1  6 GLU A 404  LYS B 232  PHE B 237  SER B 509
SITE     2 AC1  6 VAL B 510  GLY B 511
SITE     1 AC2 11 LYS A 232  PHE A 237  ALA A 240  VAL A 507
SITE     2 AC2 11 SER A 509  VAL A 510  GLY A 511  GLU B 404
SITE     3 AC2 11 THR B 406  PHE B 417  TYR B 485
CRYST1  195.480  195.480  137.300  90.00  90.00 120.00 P 62 2 2     24
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      0.005116  0.002954  0.000000        0.00000
SCALE2      0.000000  0.005907  0.000000        0.00000
SCALE3      0.000000  0.000000  0.007283        0.00000
      
PROCHECK
Go to PROCHECK summary
 References