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PDBsum entry 3s3s

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Transferase/transferase inhibitor PDB id
3s3s
Jmol
Contents
Protein chain
620 a.a.
Ligands
PHQ-XW1-VAL-PRO-
LEU
SO4 ×6
Waters ×153
HEADER    TRANSFERASE/TRANSFERASE INHIBITOR       18-MAY-11   3S3S
TITLE     TRANSGLUTAMINASE 2 IN COMPLEX WITH A NOVEL INHIBITOR
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: PROTEIN-GLUTAMINE GAMMA-GLUTAMYLTRANSFERASE 2;
COMPND   3 CHAIN: A;
COMPND   4 FRAGMENT: UNP RESIDUES 2-687;
COMPND   5 SYNONYM: TISSUE TRANSGLUTAMINASE, TRANSGLUTAMINASE C, TG(C), TGC,
COMPND   6 TGASE C, TRANSGLUTAMINASE H, TGASE H, TRANSGLUTAMINASE-2, TGASE-2;
COMPND   7 EC: 2.3.2.13;
COMPND   8 ENGINEERED: YES;
COMPND   9 MOL_ID: 2;
COMPND  10 MOLECULE: PEPTIDE INHIBITOR;
COMPND  11 CHAIN: B;
COMPND  12 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE   3 ORGANISM_COMMON: HUMAN;
SOURCE   4 ORGANISM_TAXID: 9606;
SOURCE   5 GENE: TGM2;
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE   8 MOL_ID: 2;
SOURCE   9 SYNTHETIC: YES;
SOURCE  10 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;
SOURCE  11 ORGANISM_TAXID: 32630
KEYWDS    TRANSGLUTAMINASE, TRANSFERASE-TRANSFERASE INHIBITOR COMPLEX
EXPDTA    X-RAY DIFFRACTION
AUTHOR    I.LINDEMANN,A.HEINE,G.KLEBE
REVDAT   1   06-JUN-12 3S3S    0
JRNL        AUTH   I.LINDEMANN,J.BOETTCHER,K.OERTEL,J.WEBER,M.HILS,
JRNL        AUTH 2 R.PASTERNACK,A.HEINE,G.KLEBE
JRNL        TITL   INHIBITORS OF TRANSGLUTAMINASE 2: A THERAPEUTIC OPTION IN
JRNL        TITL 2 CELIAC DISEASE
JRNL        REF    TO BE PUBLISHED
JRNL        REFN
REMARK   2
REMARK   2 RESOLUTION.    2.30 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.7_650)
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-
REMARK   3               : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,
REMARK   3               : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL
REMARK   3               : MORIARTY,REETAL PAI,RANDY READ,JANE
REMARK   3               : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM
REMARK   3               : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,
REMARK   3               : LAURENT STORONI,TOM TERWILLIGER,PETER
REMARK   3               : ZWART
REMARK   3
REMARK   3    REFINEMENT TARGET : ML
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 48.03
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 0.000
REMARK   3   COMPLETENESS FOR RANGE        (%) : 89.0
REMARK   3   NUMBER OF REFLECTIONS             : 32911
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.230
REMARK   3   R VALUE            (WORKING SET) : 0.227
REMARK   3   FREE R VALUE                     : 0.296
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.010
REMARK   3   FREE R VALUE TEST SET COUNT      : 1649
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE
REMARK   3     1 48.0442 -  5.2648    0.87     2818   134  0.2552 0.2976
REMARK   3     2  5.2648 -  4.1796    0.77     2305   120  0.2049 0.2572
REMARK   3     3  4.1796 -  3.6515    0.87     2575   158  0.2031 0.2906
REMARK   3     4  3.6515 -  3.3177    0.93     2710   149  0.2148 0.2851
REMARK   3     5  3.3177 -  3.0800    0.95     2749   153  0.2241 0.3111
REMARK   3     6  3.0800 -  2.8984    0.95     2754   144  0.2201 0.2961
REMARK   3     7  2.8984 -  2.7532    0.95     2728   130  0.2251 0.3297
REMARK   3     8  2.7532 -  2.6334    0.94     2717   152  0.2252 0.3343
REMARK   3     9  2.6334 -  2.5320    0.93     2673   125  0.2294 0.2616
REMARK   3    10  2.5320 -  2.4447    0.92     2624   158  0.2489 0.3550
REMARK   3    11  2.4447 -  2.3682    0.87     2509   127  0.2659 0.3210
REMARK   3    12  2.3682 -  2.3005    0.74     2100    99  0.2700 0.3432
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL
REMARK   3   SOLVENT RADIUS     : 1.20
REMARK   3   SHRINKAGE RADIUS   : 0.95
REMARK   3   K_SOL              : 0.36
REMARK   3   B_SOL              : 62.50
REMARK   3
REMARK   3  ERROR ESTIMATES.
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.320
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 28.950
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 9.16390
REMARK   3    B22 (A**2) : 9.16390
REMARK   3    B33 (A**2) : -18.32790
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  TWINNING INFORMATION.
REMARK   3   FRACTION: NULL
REMARK   3   OPERATOR: NULL
REMARK   3
REMARK   3  DEVIATIONS FROM IDEAL VALUES.
REMARK   3                 RMSD          COUNT
REMARK   3   BOND      :  0.008           4957
REMARK   3   ANGLE     :  1.054           6752
REMARK   3   CHIRALITY :  0.066            765
REMARK   3   PLANARITY :  0.005            865
REMARK   3   DIHEDRAL  : 14.919           1753
REMARK   3
REMARK   3  TLS DETAILS
REMARK   3   NUMBER OF TLS GROUPS  : NULL
REMARK   3
REMARK   3  NCS DETAILS
REMARK   3   NUMBER OF NCS GROUPS : NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 3S3S COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-JUN-11.
REMARK 100 THE RCSB ID CODE IS RCSB065724.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 21-OCT-10
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 7.0
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : BESSY
REMARK 200  BEAMLINE                       : 14.2
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.91841
REMARK 200  MONOCHROMATOR                  : DOUBLE CRYSTAL MONOCHROMATOR KMC
REMARK 200                                   -2
REMARK 200  OPTICS                         : MIRRORS
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : RAYONIX MX-225
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 34641
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.300
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0
REMARK 200  DATA REDUNDANCY                : 7.000
REMARK 200  R MERGE                    (I) : NULL
REMARK 200  R SYM                      (I) : 0.07500
REMARK 200   FOR THE DATA SET  : 23.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.35
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.80
REMARK 200  R MERGE FOR SHELL          (I) : NULL
REMARK 200  R SYM FOR SHELL            (I) : 0.34500
REMARK 200   FOR SHELL         : 3.500
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 2Q3Z
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 50.93
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.51
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 3.0 M AMM. SULFATE, 0.1 M HEPES, VAPOR
REMARK 280  DIFFUSION, SITTING DROP, TEMPERATURE 289K, PH 7.0
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 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+1/4
REMARK 290       4555   Y+1/2,-X+1/2,Z+3/4
REMARK 290       5555   -X+1/2,Y+1/2,-Z+1/4
REMARK 290       6555   X+1/2,-Y+1/2,-Z+3/4
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      155.17000
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       35.71950
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       35.71950
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       77.58500
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       35.71950
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       35.71950
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000      232.75500
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       35.71950
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       35.71950
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       77.58500
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       35.71950
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       35.71950
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000      232.75500
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      155.17000
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 300 REMARK: THE MAIN POLYMERIC PROTEIN-GLUTAMINE GAMMA-
REMARK 300 GLUTAMYLTRANSFERASE 2 IS A MONOMER IN THE ABSENCE OF THE PEPTIDE
REMARK 300 INHIBITOR
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 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 400
REMARK 400 COMPOUND
REMARK 400 THE UNREACTED FORM OF THE PEPTIDE INHIBITOR, CHAIN B HAS A DOUBLE
REMARK 400 BOND BETWEEN C15 AND C17 OF THE AMINOACID XW1. UPON REACTION WITH
REMARK 400 PROTEIN, A COVALENT BOND BETWEEN C15 AND SG OF CYS 277 CHAIN A IS
REMARK 400 FORMED
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    -6
REMARK 465     ALA A    -5
REMARK 465     HIS A    -4
REMARK 465     HIS A    -3
REMARK 465     HIS A    -2
REMARK 465     HIS A    -1
REMARK 465     HIS A     0
REMARK 465     ASP A   232
REMARK 465     GLY A   239
REMARK 465     ARG A   240
REMARK 465     TRP A   241
REMARK 465     ASP A   242
REMARK 465     ASN A   243
REMARK 465     ASN A   244
REMARK 465     TYR A   245
REMARK 465     GLY A   246
REMARK 465     ASP A   247
REMARK 465     GLY A   248
REMARK 465     VAL A   249
REMARK 465     SER A   250
REMARK 465     PRO A   251
REMARK 465     MET A   252
REMARK 465     HIS A   267
REMARK 465     GLY A   268
REMARK 465     CYS A   269
REMARK 465     GLN A   270
REMARK 465     ARG A   271
REMARK 465     VAL A   272
REMARK 465     LYS A   273
REMARK 465     TYR A   274
REMARK 465     GLY A   275
REMARK 465     GLN A   276
REMARK 465     ASP A   306
REMARK 465     GLN A   307
REMARK 465     ASN A   308
REMARK 465     ASN A   318
REMARK 465     GLU A   319
REMARK 465     PHE A   320
REMARK 465     GLY A   321
REMARK 465     GLU A   322
REMARK 465     ILE A   323
REMARK 465     GLN A   324
REMARK 465     GLY A   325
REMARK 465     ASP A   326
REMARK 465     LYS A   327
REMARK 465     GLN A   362
REMARK 465     GLU A   363
REMARK 465     LYS A   364
REMARK 465     SER A   365
REMARK 465     GLU A   366
REMARK 465     GLY A   367
REMARK 465     THR A   368
REMARK 465     TYR A   369
REMARK 465     GLN A   407
REMARK 465     ASP A   408
REMARK 465     ASP A   409
REMARK 465     GLY A   410
REMARK 465     SER A   411
REMARK 465     VAL A   412
REMARK 465     HIS A   413
REMARK 465     LEU A   462
REMARK 465     ASN A   463
REMARK 465     LYS A   464
REMARK 465     LEU A   465
REMARK 465     ALA A   466
REMARK 465     GLU A   467
REMARK 465     LYS A   468
REMARK 465     GLU A   469
REMARK 465     GLU A   470
REMARK 465     THR A   471
REMARK 465     ILE A   684
REMARK 465     GLY A   685
REMARK 465     PRO A   686
REMARK 465     ALA A   687
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     ARG A  28    CG   CD   NE   CZ   NH1  NH2
REMARK 470     GLU A  29    CG   CD   OE1  OE2
REMARK 470     LYS A  30    CG   CD   CE   NZ
REMARK 470     GLU A  85    CG   CD   OE1  OE2
REMARK 470     ASP A  97    CG   OD1  OD2
REMARK 470     GLU A 120    CG   CD   OE1  OE2
REMARK 470     LYS A 173    CG   CD   CE   NZ
REMARK 470     LYS A 176    CG   CD   CE   NZ
REMARK 470     ILE A 178    CG1  CG2  CD1
REMARK 470     ASP A 233    CG   OD1  OD2
REMARK 470     GLN A 234    CG   CD   OE1  NE2
REMARK 470     ARG A 317    CG   CD   NE   CZ   NH1  NH2
REMARK 470     LYS A 414    CG   CD   CE   NZ
REMARK 470     ARG A 433    CG   CD   NE   CZ   NH1  NH2
REMARK 470     GLU A 501    CG   CD   OE1  OE2
REMARK 470     GLU A 549    CG   CD   OE1  OE2
REMARK 470     LYS A 550    CG   CD   CE   NZ
REMARK 470     GLU A 557    CG   CD   OE1  OE2
REMARK 470     ILE A 572    CG1  CG2  CD1
REMARK 470     ARG A 592    CG   CD   NE   CZ   NH1  NH2
REMARK 470     GLU A 596    CG   CD   OE1  OE2
REMARK 470     LYS A 598    CG   CD   CE   NZ
REMARK 470     LYS A 600    CG   CD   CE   NZ
REMARK 470     ARG A 601    CG   CD   NE   CZ   NH1  NH2
REMARK 470     LYS A 602    CG   CD   CE   NZ
REMARK 470     GLU A 631    CG   CD   OE1  OE2
REMARK 470     LYS A 634    CG   CD   CE   NZ
REMARK 470     MET A 652    CG   SD   CE
REMARK 470     LEU A 655    CG   CD1  CD2
REMARK 470     LEU A 657    CG   CD1  CD2
REMARK 470     MET A 659    CG   SD   CE
REMARK 470     LYS A 674    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    VAL B   3   C     PRO B   4   N       0.151
REMARK 500    LEU B   5   C     LEU B   5   O       0.126
REMARK 500    PRO B   4   C     LEU B   5   N       0.141
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    TYR A 125      -10.25     92.12
REMARK 500    GLN A 169     -157.16   -149.28
REMARK 500    ASN A 206       80.39   -172.90
REMARK 500    CYS A 230       89.85    -65.04
REMARK 500    GLN A 234      -42.50     73.66
REMARK 500    GLU A 329       56.27   -108.62
REMARK 500    ILE A 405       67.19   -102.63
REMARK 500    ASN A 573       47.96     81.18
REMARK 500    PRO A 597       77.60    -62.08
REMARK 500    GLN A 599      -11.36    -46.08
REMARK 500    LYS A 600      -97.81    -70.14
REMARK 500    LYS A 602      111.87     70.36
REMARK 500    LEU A 629      -63.15   -129.45
REMARK 500    PRO A 656      100.69    -31.09
REMARK 500    LEU A 657      -77.75    -48.52
REMARK 500    HIS A 658     -131.31   -118.28
REMARK 500    MET A 659      -65.73   -100.59
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 SO4 A 688
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 689
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 690
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 691
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 692
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 693
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN B OF PEPTIDE INHIBITOR
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2Q3Z   RELATED DB: PDB
REMARK 900 TRANSGLUTAMINASE 2 UNDERGOES A LARGE CONFORMATIONAL CHANGE
REMARK 900 UPON ACTIVATION
REMARK 900 RELATED ID: 3S3J   RELATED DB: PDB
REMARK 900 TRANSGLUTAMINASE 2 IN COMPLEX WITH A NOVEL INHIBITOR
REMARK 900 RELATED ID: 3S3P   RELATED DB: PDB
REMARK 900 TRANSGLUTAMINASE 2 IN COMPLEX WITH A NOVEL INHIBITOR
DBREF  3S3S A    2   687  UNP    P21980   TGM2_HUMAN       2    687
DBREF  3S3S B    1     5  PDB    3S3S     3S3S             1      5
SEQADV 3S3S MET A   -6  UNP  P21980              INITIATING METHIONINE
SEQADV 3S3S ALA A   -5  UNP  P21980              EXPRESSION TAG
SEQADV 3S3S HIS A   -4  UNP  P21980              EXPRESSION TAG
SEQADV 3S3S HIS A   -3  UNP  P21980              EXPRESSION TAG
SEQADV 3S3S HIS A   -2  UNP  P21980              EXPRESSION TAG
SEQADV 3S3S HIS A   -1  UNP  P21980              EXPRESSION TAG
SEQADV 3S3S HIS A    0  UNP  P21980              EXPRESSION TAG
SEQADV 3S3S HIS A    1  UNP  P21980              EXPRESSION TAG
SEQRES   1 A  694  MET ALA HIS HIS HIS HIS HIS HIS ALA GLU GLU LEU VAL
SEQRES   2 A  694  LEU GLU ARG CYS ASP LEU GLU LEU GLU THR ASN GLY ARG
SEQRES   3 A  694  ASP HIS HIS THR ALA ASP LEU CYS ARG GLU LYS LEU VAL
SEQRES   4 A  694  VAL ARG ARG GLY GLN PRO PHE TRP LEU THR LEU HIS PHE
SEQRES   5 A  694  GLU GLY ARG ASN TYR GLU ALA SER VAL ASP SER LEU THR
SEQRES   6 A  694  PHE SER VAL VAL THR GLY PRO ALA PRO SER GLN GLU ALA
SEQRES   7 A  694  GLY THR LYS ALA ARG PHE PRO LEU ARG ASP ALA VAL GLU
SEQRES   8 A  694  GLU GLY ASP TRP THR ALA THR VAL VAL ASP GLN GLN ASP
SEQRES   9 A  694  CYS THR LEU SER LEU GLN LEU THR THR PRO ALA ASN ALA
SEQRES  10 A  694  PRO ILE GLY LEU TYR ARG LEU SER LEU GLU ALA SER THR
SEQRES  11 A  694  GLY TYR GLN GLY SER SER PHE VAL LEU GLY HIS PHE ILE
SEQRES  12 A  694  LEU LEU PHE ASN ALA TRP CYS PRO ALA ASP ALA VAL TYR
SEQRES  13 A  694  LEU ASP SER GLU GLU GLU ARG GLN GLU TYR VAL LEU THR
SEQRES  14 A  694  GLN GLN GLY PHE ILE TYR GLN GLY SER ALA LYS PHE ILE
SEQRES  15 A  694  LYS ASN ILE PRO TRP ASN PHE GLY GLN PHE GLU ASP GLY
SEQRES  16 A  694  ILE LEU ASP ILE CYS LEU ILE LEU LEU ASP VAL ASN PRO
SEQRES  17 A  694  LYS PHE LEU LYS ASN ALA GLY ARG ASP CYS SER ARG ARG
SEQRES  18 A  694  SER SER PRO VAL TYR VAL GLY ARG VAL VAL SER GLY MET
SEQRES  19 A  694  VAL ASN CYS ASN ASP ASP GLN GLY VAL LEU LEU GLY ARG
SEQRES  20 A  694  TRP ASP ASN ASN TYR GLY ASP GLY VAL SER PRO MET SER
SEQRES  21 A  694  TRP ILE GLY SER VAL ASP ILE LEU ARG ARG TRP LYS ASN
SEQRES  22 A  694  HIS GLY CYS GLN ARG VAL LYS TYR GLY GLN CYS TRP VAL
SEQRES  23 A  694  PHE ALA ALA VAL ALA CYS THR VAL LEU ARG CYS LEU GLY
SEQRES  24 A  694  ILE PRO THR ARG VAL VAL THR ASN TYR ASN SER ALA HIS
SEQRES  25 A  694  ASP GLN ASN SER ASN LEU LEU ILE GLU TYR PHE ARG ASN
SEQRES  26 A  694  GLU PHE GLY GLU ILE GLN GLY ASP LYS SER GLU MET ILE
SEQRES  27 A  694  TRP ASN PHE HIS CYS TRP VAL GLU SER TRP MET THR ARG
SEQRES  28 A  694  PRO ASP LEU GLN PRO GLY TYR GLU GLY TRP GLN ALA LEU
SEQRES  29 A  694  ASP PRO THR PRO GLN GLU LYS SER GLU GLY THR TYR CYS
SEQRES  30 A  694  CYS GLY PRO VAL PRO VAL ARG ALA ILE LYS GLU GLY ASP
SEQRES  31 A  694  LEU SER THR LYS TYR ASP ALA PRO PHE VAL PHE ALA GLU
SEQRES  32 A  694  VAL ASN ALA ASP VAL VAL ASP TRP ILE GLN GLN ASP ASP
SEQRES  33 A  694  GLY SER VAL HIS LYS SER ILE ASN ARG SER LEU ILE VAL
SEQRES  34 A  694  GLY LEU LYS ILE SER THR LYS SER VAL GLY ARG ASP GLU
SEQRES  35 A  694  ARG GLU ASP ILE THR HIS THR TYR LYS TYR PRO GLU GLY
SEQRES  36 A  694  SER SER GLU GLU ARG GLU ALA PHE THR ARG ALA ASN HIS
SEQRES  37 A  694  LEU ASN LYS LEU ALA GLU LYS GLU GLU THR GLY MET ALA
SEQRES  38 A  694  MET ARG ILE ARG VAL GLY GLN SER MET ASN MET GLY SER
SEQRES  39 A  694  ASP PHE ASP VAL PHE ALA HIS ILE THR ASN ASN THR ALA
SEQRES  40 A  694  GLU GLU TYR VAL CYS ARG LEU LEU LEU CYS ALA ARG THR
SEQRES  41 A  694  VAL SER TYR ASN GLY ILE LEU GLY PRO GLU CYS GLY THR
SEQRES  42 A  694  LYS TYR LEU LEU ASN LEU ASN LEU GLU PRO PHE SER GLU
SEQRES  43 A  694  LYS SER VAL PRO LEU CYS ILE LEU TYR GLU LYS TYR ARG
SEQRES  44 A  694  ASP CYS LEU THR GLU SER ASN LEU ILE LYS VAL ARG ALA
SEQRES  45 A  694  LEU LEU VAL GLU PRO VAL ILE ASN SER TYR LEU LEU ALA
SEQRES  46 A  694  GLU ARG ASP LEU TYR LEU GLU ASN PRO GLU ILE LYS ILE
SEQRES  47 A  694  ARG ILE LEU GLY GLU PRO LYS GLN LYS ARG LYS LEU VAL
SEQRES  48 A  694  ALA GLU VAL SER LEU GLN ASN PRO LEU PRO VAL ALA LEU
SEQRES  49 A  694  GLU GLY CYS THR PHE THR VAL GLU GLY ALA GLY LEU THR
SEQRES  50 A  694  GLU GLU GLN LYS THR VAL GLU ILE PRO ASP PRO VAL GLU
SEQRES  51 A  694  ALA GLY GLU GLU VAL LYS VAL ARG MET ASP LEU LEU PRO
SEQRES  52 A  694  LEU HIS MET GLY LEU HIS LYS LEU VAL VAL ASN PHE GLU
SEQRES  53 A  694  SER ASP LYS LEU LYS ALA VAL LYS GLY PHE ARG ASN VAL
SEQRES  54 A  694  ILE ILE GLY PRO ALA
SEQRES   1 B    5  PHQ XW1 VAL PRO LEU
MODRES 3S3S XW1 B    2  ALA
HET    PHQ  B   1      10
HET    XW1  B   2      13
HET    SO4  A 688       5
HET    SO4  A 689       5
HET    SO4  A 690       5
HET    SO4  A 691       5
HET    SO4  A 692       5
HET    SO4  A 693       5
HETNAM     PHQ BENZYL CHLOROCARBONATE
HETNAM     XW1 (2S)-2-AMINO-7-ETHOXY-7-OXOHEPTANOIC ACID
HETNAM     SO4 SULFATE ION
FORMUL   2  PHQ    C8 H7 CL O2
FORMUL   2  XW1    C9 H17 N O4
FORMUL   3  SO4    6(O4 S 2-)
FORMUL   9  HOH   *153(H2 O)
HELIX    1   1 GLU A   13  HIS A   21  1                                   9
HELIX    2   2 THR A   23  CYS A   27  5                                   5
HELIX    3   3 SER A  152  VAL A  160  1                                   9
HELIX    4   4 GLY A  188  VAL A  199  1                                  12
HELIX    5   5 ASN A  200  ASN A  206  1                                   7
HELIX    6   6 ASN A  206  ARG A  214  1                                   9
HELIX    7   7 SER A  216  VAL A  228  1                                  13
HELIX    8   8 SER A  257  ASN A  266  1                                  10
HELIX    9   9 CYS A  277  GLY A  292  1                                  16
HELIX   10  10 ASN A  310  ARG A  317  1                                   8
HELIX   11  11 VAL A  376  GLU A  381  1                                   6
HELIX   12  12 ASP A  389  ASN A  398  1                                  10
HELIX   13  13 ILE A  439  LYS A  444  1                                   6
HELIX   14  14 SER A  449  HIS A  461  1                                  13
HELIX   15  15 LEU A  547  ARG A  552  1                                   6
HELIX   16  16 ASP A  553  LEU A  555  5                                   3
SHEET    1   A 4 VAL A   6  ASP A  11  0
SHEET    2   A 4 PHE A  39  GLU A  46 -1  O  GLU A  46   N  VAL A   6
SHEET    3   A 4 THR A  99  THR A 105 -1  O  LEU A 102   N  LEU A  41
SHEET    4   A 4 THR A  89  GLN A  95 -1  N  THR A  91   O  GLN A 103
SHEET    1   B 5 LEU A  31  ARG A  34  0
SHEET    2   B 5 GLY A 127  LEU A 138  1  O  ILE A 136   N  VAL A  33
SHEET    3   B 5 GLY A 113  THR A 123 -1  N  LEU A 117   O  GLY A 133
SHEET    4   B 5 ASP A  55  THR A  63 -1  N  SER A  56   O  SER A 122
SHEET    5   B 5 LYS A  74  PRO A  78 -1  O  PHE A  77   N  PHE A  59
SHEET    1   C 2 GLN A 164  GLY A 170  0
SHEET    2   C 2 ILE A 175  ASN A 181 -1  O  LYS A 176   N  GLN A 169
SHEET    1   D 6 VAL A 374  PRO A 375  0
SHEET    2   D 6 GLY A 353  LEU A 357 -1  N  ALA A 356   O  VAL A 374
SHEET    3   D 6 PHE A 334  MET A 342 -1  N  VAL A 338   O  LEU A 357
SHEET    4   D 6 THR A 295  ALA A 304 -1  N  ASN A 300   O  HIS A 335
SHEET    5   D 6 LEU A 420  LYS A 429 -1  O  ILE A 421   N  SER A 303
SHEET    6   D 6 ARG A 436  ASP A 438 -1  O  GLU A 437   N  THR A 428
SHEET    1   E 6 SER A 415  ILE A 416  0
SHEET    2   E 6 ASP A 400  TRP A 404 -1  N  ASP A 403   O  SER A 415
SHEET    3   E 6 SER A 574  TYR A 583  1  O  TYR A 575   N  ASP A 400
SHEET    4   E 6 LEU A 560  GLU A 569 -1  N  ILE A 561   O  LEU A 582
SHEET    5   E 6 TYR A 503  VAL A 514 -1  N  ARG A 512   O  LYS A 562
SHEET    6   E 6 LEU A 520  LEU A 534 -1  O  LYS A 527   N  LEU A 509
SHEET    1   F 3 MET A 473  ARG A 478  0
SHEET    2   F 3 PHE A 489  ASN A 497 -1  O  THR A 496   N  ALA A 474
SHEET    3   F 3 SER A 538  ILE A 546 -1  O  ILE A 546   N  PHE A 489
SHEET    1   G 3 LYS A 590  LEU A 594  0
SHEET    2   G 3 LEU A 603  GLN A 610 -1  O  VAL A 604   N  LEU A 594
SHEET    3   G 3 GLU A 647  LEU A 654 -1  O  LEU A 654   N  LEU A 603
SHEET    1   H 4 LYS A 634  ILE A 638  0
SHEET    2   H 4 CYS A 620  GLU A 625 -1  N  CYS A 620   O  ILE A 638
SHEET    3   H 4 HIS A 662  GLU A 669 -1  O  VAL A 665   N  GLU A 625
SHEET    4   H 4 VAL A 676  VAL A 682 -1  O  ARG A 680   N  LEU A 664
LINK         SG  CYS A 277                 C15 XW1 B   2     1555   1555  1.78
LINK         C1  PHQ B   1                 N   XW1 B   2     1555   1555  1.45
LINK         C   XW1 B   2                 N   VAL B   3     1555   1555  1.48
CISPEP   1 GLY A  372    PRO A  373          0         2.67
CISPEP   2 LYS A  387    TYR A  388          0        -0.17
SITE     1 AC1  2 LYS A 202  ARG A 222
SITE     1 AC2  3 LYS A 202  ARG A 209  TYR A 219
SITE     1 AC3  1 ARG A  80
SITE     1 AC4  5 ARG A  80  ASP A  81  ALA A  82  HOH A 764
SITE     2 AC4  5 HOH A 815
SITE     1 AC5  3 ARG A 478  VAL A 479  ARG A 580
SITE     1 AC6  4 SER A  68  GLN A  69  LYS A  74  HOH A 838
SITE     1 AC7 12 GLN A 169  GLY A 170  CYS A 277  SER A 303
SITE     2 AC7 12 MET A 330  ILE A 331  TRP A 332  ASN A 333
SITE     3 AC7 12 PHE A 334  HIS A 335  THR A 360  ASN A 517
CRYST1   71.439   71.439  310.340  90.00  90.00  90.00 P 41 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      0.013998  0.000000  0.000000        0.00000
SCALE2      0.000000  0.013998  0.000000        0.00000
SCALE3      0.000000  0.000000  0.003222        0.00000
      
PROCHECK
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 References