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PDBsum entry 3iu0

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Transferase PDB id
3iu0
Jmol
Contents
Protein chain
354 a.a.
Waters ×150
HEADER    TRANSFERASE                             28-AUG-09   3IU0
TITLE     STRUCTURAL BASIS FOR ZYMOGEN ACTIVATION AND SUBSTRATE BINDING OF
TITLE    2 TRANSGLUTAMINASE FROM STREPTOMYCES MOBARAENSE
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: PROTEIN-GLUTAMINE GAMMA-GLUTAMYLTRANSFERASE;
COMPND   3 CHAIN: A;
COMPND   4 SYNONYM: TRANSGLUTAMINASE, TGASE, MTG, MICROBIAL TRANSGLUTAMINASE
COMPND   5 ZYMOGEN;
COMPND   6 EC: 2.3.2.13;
COMPND   7 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: STREPTOMYCES MOBARAENSIS;
SOURCE   3 ORGANISM_COMMON: STREPTOVERTICILLIUM MOBARAENSE;
SOURCE   4 ORGANISM_TAXID: 35621;
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE   7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PET21D
KEYWDS    MTGASE, ZYMOGEN, PRO-ENZYME,CROSS-LINKING, TRANSFERASE,
KEYWDS   2 ACYLTRANSFERASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    T.T.LI
REVDAT   1   15-SEP-10 3IU0    0
JRNL        AUTH   M.YANG,J.M.WANG,T.K.WU,T.T.LI
JRNL        TITL   STRUCTURAL BASIS FOR ZYMOGEN ACTIVATION AND SUBSTRATE
JRNL        TITL 2 BINDING OF TRANSGLUTAMINASE FROM STREPTOMYCES MOBARAENSE
JRNL        REF    TO BE PUBLISHED
JRNL        REFN
REMARK   2
REMARK   2 RESOLUTION.    1.90 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 WITH PHASES
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.13
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0
REMARK   3   NUMBER OF REFLECTIONS             : 26318
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) : 0.213
REMARK   3   R VALUE            (WORKING SET) : 0.210
REMARK   3   FREE R VALUE                     : 0.244
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.088
REMARK   3   FREE R VALUE TEST SET COUNT      : 2953
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) : 1.90
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.95
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1891
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.91
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2120
REMARK   3   BIN FREE R VALUE SET COUNT          : 214
REMARK   3   BIN FREE R VALUE                    : 0.2700
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 2777
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) : 27.70
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 28.61
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 0.01500
REMARK   3    B22 (A**2) : 0.00400
REMARK   3    B33 (A**2) : -0.01900
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): 0.185
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.160
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.098
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.246
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.945
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.929
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2855 ; 0.010 ; 0.021
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3879 ; 1.056 ; 1.922
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   352 ; 5.142 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   156 ;33.947 ;23.462
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   413 ;14.278 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    26 ;14.940 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   382 ; 0.079 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2328 ; 0.004 ; 0.021
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1252 ; 0.183 ; 0.200
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  1940 ; 0.299 ; 0.200
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   193 ; 0.094 ; 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):    30 ; 0.189 ; 0.200
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    11 ; 0.098 ; 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):  1763 ; 0.542 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2802 ; 1.017 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1092 ; 1.554 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1077 ; 2.579 ; 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 : BABINET MODEL WITH 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: NULL
REMARK   4
REMARK   4 3IU0 COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 01-SEP-09.
REMARK 100 THE RCSB ID CODE IS RCSB054862.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : NULL
REMARK 200  TEMPERATURE           (KELVIN) : 180.0
REMARK 200  PH                             : 5.0
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : N
REMARK 200  RADIATION SOURCE               : ROTATING ANODE
REMARK 200  BEAMLINE                       : NULL
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU RUH3R
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418
REMARK 200  MONOCHROMATOR                  : BLUE-OPTICS
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : NULL
REMARK 200  DETECTOR MANUFACTURER          : NULL
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 29327
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.900
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0
REMARK 200  DATA REDUNDANCY                : 8.200
REMARK 200  R MERGE                    (I) : 0.04300
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 39.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.99
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.9
REMARK 200  DATA REDUNDANCY IN SHELL       : 8.00
REMARK 200  R MERGE FOR SHELL          (I) : 0.23800
REMARK 200  R SYM FOR SHELL            (I) : 0.23800
REMARK 200   FOR SHELL         : 8.100
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 1IU4
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 41.20
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.09
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% PEG8000, 50MM NACL, 1MM EDTA, 1MM
REMARK 280  BETA-MERCAPTOETHANOL, 0.01% NAN3, 100MM CACODYLIC ACID, PH5.0 AND
REMARK 280  2% GLYCEROL, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X+1/2,-Y,Z+1/2
REMARK 290       3555   -X,Y+1/2,-Z+1/2
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       32.16650
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       41.98450
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       33.56150
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       41.98450
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       32.16650
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       33.56150
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000
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: 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 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     ASP A     2
REMARK 465     ASN A     3
REMARK 465     GLY A     4
REMARK 465     ALA A     5
REMARK 465     GLY A     6
REMARK 465     GLU A     7
REMARK 465     GLU A     8
REMARK 465     PRO A    34
REMARK 465     ALA A    35
REMARK 465     ALA A    36
REMARK 465     SER A    37
REMARK 465     SER A    38
REMARK 465     ALA A    39
REMARK 465     GLY A    40
REMARK 465     PRO A    41
REMARK 465     SER A    42
REMARK 465     PHE A    43
REMARK 465     ARG A    44
REMARK 465     ALA A    45
REMARK 465     PRO A    46
REMARK 465     ASP A    47
REMARK 465     SER A    48
REMARK 465     HIS A   378
REMARK 465     HIS A   379
REMARK 465     HIS A   380
REMARK 465     HIS A   381
REMARK 465     HIS A   382
REMARK 465     HIS A   383
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     THR A   9    OG1  CG2
REMARK 470     LYS A  10    CG   CD   CE   NZ
REMARK 470     ARG A  94    CG   CD   NE   CZ   NH1  NH2
REMARK 470     ARG A 125    CG   CD   NE   CZ   NH1  NH2
REMARK 470     GLU A 139    CG   CD   OE1  OE2
REMARK 470     LYS A 141    CG   CD   CE   NZ
REMARK 470     ASN A 142    CG   OD1  ND2
REMARK 470     ARG A 144    CG   CD   NE   CZ   NH1  NH2
REMARK 470     LYS A 167    CG   CD   CE   NZ
REMARK 470     GLN A 170    CG   CD   OE1  NE2
REMARK 470     ARG A 181    CG   CD   NE   CZ   NH1  NH2
REMARK 470     LYS A 198    CG   CD   CE   NZ
REMARK 470     ASN A 204    CG   OD1  ND2
REMARK 470     ASP A 211    CG   OD1  OD2
REMARK 470     ARG A 229    CG   CD   NE   CZ   NH1  NH2
REMARK 470     LYS A 262    CG   CD   CE   NZ
REMARK 470     GLU A 295    CG   CD   OE1  OE2
REMARK 470     LYS A 371    CG   CD   CE   NZ
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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   RES CSSEQI ATM2   DEVIATION
REMARK 500    CYS A 110   CB    CYS A 110   SG      0.224
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    CYS A 110   CA  -  CB  -  SG  ANGL. DEV. =   9.0 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    ALA A 307       54.40   -152.36
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1IU4   RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MICROBIAL TRANSGLUTAMINASE FROM
REMARK 900 STREPTOVERTICILLIUM MOBARAENSE
DBREF  3IU0 A    2   377  UNP    P81453   TGAS_STRMB      32    407
SEQADV 3IU0 HIS A  378  UNP  P81453              EXPRESSION TAG
SEQADV 3IU0 HIS A  379  UNP  P81453              EXPRESSION TAG
SEQADV 3IU0 HIS A  380  UNP  P81453              EXPRESSION TAG
SEQADV 3IU0 HIS A  381  UNP  P81453              EXPRESSION TAG
SEQADV 3IU0 HIS A  382  UNP  P81453              EXPRESSION TAG
SEQADV 3IU0 HIS A  383  UNP  P81453              EXPRESSION TAG
SEQRES   1 A  382  ASP ASN GLY ALA GLY GLU GLU THR LYS SER TYR ALA GLU
SEQRES   2 A  382  THR TYR ARG LEU THR ALA ASP ASP VAL ALA ASN ILE ASN
SEQRES   3 A  382  ALA LEU ASN GLU SER ALA PRO ALA ALA SER SER ALA GLY
SEQRES   4 A  382  PRO SER PHE ARG ALA PRO ASP SER ASP ASP ARG VAL THR
SEQRES   5 A  382  PRO PRO ALA GLU PRO LEU ASP ARG MET PRO ASP PRO TYR
SEQRES   6 A  382  ARG PRO SER TYR GLY ARG ALA GLU THR VAL VAL ASN ASN
SEQRES   7 A  382  TYR ILE ARG LYS TRP GLN GLN VAL TYR SER HIS ARG ASP
SEQRES   8 A  382  GLY ARG LYS GLN GLN MET THR GLU GLU GLN ARG GLU TRP
SEQRES   9 A  382  LEU SER TYR GLY CYS VAL GLY VAL THR TRP VAL ASN SER
SEQRES  10 A  382  GLY GLN TYR PRO THR ASN ARG LEU ALA PHE ALA SER PHE
SEQRES  11 A  382  ASP GLU ASP ARG PHE LYS ASN GLU LEU LYS ASN GLY ARG
SEQRES  12 A  382  PRO ARG SER GLY GLU THR ARG ALA GLU PHE GLU GLY ARG
SEQRES  13 A  382  VAL ALA LYS GLU SER PHE ASP GLU GLU LYS GLY PHE GLN
SEQRES  14 A  382  ARG ALA ARG GLU VAL ALA SER VAL MET ASN ARG ALA LEU
SEQRES  15 A  382  GLU ASN ALA HIS ASP GLU SER ALA TYR LEU ASP ASN LEU
SEQRES  16 A  382  LYS LYS GLU LEU ALA ASN GLY ASN ASP ALA LEU ARG ASN
SEQRES  17 A  382  GLU ASP ALA ARG SER PRO PHE TYR SER ALA LEU ARG ASN
SEQRES  18 A  382  THR PRO SER PHE LYS GLU ARG ASN GLY GLY ASN HIS ASP
SEQRES  19 A  382  PRO SER ARG MET LYS ALA VAL ILE TYR SER LYS HIS PHE
SEQRES  20 A  382  TRP SER GLY GLN ASP ARG SER SER SER ALA ASP LYS ARG
SEQRES  21 A  382  LYS TYR GLY ASP PRO ASP ALA PHE ARG PRO ALA PRO GLY
SEQRES  22 A  382  THR GLY LEU VAL ASP MET SER ARG ASP ARG ASN ILE PRO
SEQRES  23 A  382  ARG SER PRO THR SER PRO GLY GLU GLY PHE VAL ASN PHE
SEQRES  24 A  382  ASP TYR GLY TRP PHE GLY ALA GLN THR GLU ALA ASP ALA
SEQRES  25 A  382  ASP LYS THR VAL TRP THR HIS GLY ASN HIS TYR HIS ALA
SEQRES  26 A  382  PRO ASN GLY SER LEU GLY ALA MET HIS VAL TYR GLU SER
SEQRES  27 A  382  LYS PHE ARG ASN TRP SER GLU GLY TYR SER ASP PHE ASP
SEQRES  28 A  382  ARG GLY ALA TYR VAL ILE THR PHE ILE PRO LYS SER TRP
SEQRES  29 A  382  ASN THR ALA PRO ASP LYS VAL LYS GLN GLY TRP PRO HIS
SEQRES  30 A  382  HIS HIS HIS HIS HIS
FORMUL   2  HOH   *150(H2 O)
HELIX    1   1 SER A   11  ARG A   17  1                                   7
HELIX    2   2 THR A   19  SER A   32  1                                  14
HELIX    3   3 VAL A   77  VAL A   87  1                                  11
HELIX    4   4 THR A   99  SER A  107  1                                   9
HELIX    5   5 VAL A  111  GLY A  119  1                                   9
HELIX    6   6 ASP A  132  GLY A  143  1                                  12
HELIX    7   7 THR A  150  SER A  162  1                                  13
HELIX    8   8 ASP A  164  GLU A  184  1                                  21
HELIX    9   9 ASP A  188  GLY A  203  1                                  16
HELIX   10  10 ASP A  205  GLU A  210  5                                   6
HELIX   11  11 SER A  214  ALA A  219  1                                   6
HELIX   12  12 THR A  223  GLU A  228  1                                   6
HELIX   13  13 ASP A  235  SER A  237  5                                   3
HELIX   14  14 SER A  257  GLY A  264  1                                   8
HELIX   15  15 ASP A  312  LYS A  315  5                                   4
HELIX   16  16 PHE A  341  GLU A  346  1                                   6
SHEET    1   A 3 ARG A  72  VAL A  76  0
SHEET    2   A 3 HIS A 335  LYS A 340 -1  O  GLU A 338   N  ALA A  73
SHEET    3   A 3 VAL A 317  GLY A 321 -1  N  HIS A 320   O  TYR A 337
SHEET    1   B 5 LEU A 277  VAL A 278  0
SHEET    2   B 5 ALA A 127  PHE A 128 -1  N  ALA A 127   O  VAL A 278
SHEET    3   B 5 ARG A 353  PRO A 362 -1  O  TYR A 356   N  PHE A 128
SHEET    4   B 5 MET A 239  PHE A 248 -1  N  VAL A 242   O  THR A 359
SHEET    5   B 5 ASP A 301  GLY A 306 -1  O  GLY A 306   N  ILE A 243
CRYST1   64.333   67.123   83.969  90.00  90.00  90.00 P 21 21 21    4
ORIGX1      1.000000  0.000000  0.000000        0.00000
ORIGX2      0.000000  1.000000  0.000000        0.00000
ORIGX3      0.000000  0.000000  1.000000        0.00000
SCALE1      0.015544  0.000000  0.000000        0.00000
SCALE2      0.000000  0.014898  0.000000        0.00000
SCALE3      0.000000  0.000000  0.011909        0.00000
      
PROCHECK
Go to PROCHECK summary
 References