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PDBsum entry 1nug

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Top Page protein metals Protein-protein interface(s) links
Transferase PDB id
1nug
Jmol
Contents
Protein chain
675 a.a. *
Metals
_MG ×2
_CL ×4
_CA ×4
Waters ×809
* Residue conservation analysis
HEADER    TRANSFERASE                             31-JAN-03   1NUG
TITLE     ROLE OF CALCIUM IONS IN THE ACTIVATION AND ACTIVITY OF THE
TITLE    2 TRANSGLUTAMINASE 3 ENZYME (2 CALCIUMS, 1 MG, INACTIVE FORM)
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: PROTEIN-GLUTAMINE GLUTAMYLTRANSFERASE E;
COMPND   3 CHAIN: A, B;
COMPND   4 SYNONYM: TGASE E, TGE, TGE, TRANSGLUTAMINASE 3;
COMPND   5 EC: 2.3.2.13;
COMPND   6 ENGINEERED: YES;
COMPND   7 MUTATION: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE   3 ORGANISM_COMMON: HUMAN;
SOURCE   4 ORGANISM_TAXID: 9606;
SOURCE   5 GENE: TGM3;
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE   7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE   9 EXPRESSION_SYSTEM_CELL_LINE: SF9;
SOURCE  10 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;
SOURCE  11 EXPRESSION_SYSTEM_VECTOR: PET 11A VECTOR (NOVAGEN) PVL1392
SOURCE  12 (INVITROGEN);
SOURCE  13 EXPRESSION_SYSTEM_PLASMID: BAC-N_BLUE, INVITROGEN
KEYWDS    TRANSGLUTAMINASE 3, X-RAY CRYSTALLOGRAPHY, METALLOENZYME,
KEYWDS   2 CALCIUM ION, TRANSFERASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    B.AHVAZI
REVDAT   3   24-FEB-09 1NUG    1       VERSN
REVDAT   2   01-JUL-03 1NUG    1       JRNL
REVDAT   1   22-APR-03 1NUG    0
JRNL        AUTH   B.AHVAZI,K.M.BOESHANS,W.IDLER,U.BAXA,P.M.STEINERT
JRNL        TITL   ROLES OF CALCIUM IONS IN THE ACTIVATION AND
JRNL        TITL 2 ACTIVITY OF THE TRANSGLUTAMINASE 3 ENZYME
JRNL        REF    J.BIOL.CHEM.                  V. 278 23834 2003
JRNL        REFN                   ISSN 0021-9258
JRNL        PMID   12679341
JRNL        DOI    10.1074/JBC.M301162200
REMARK   1
REMARK   1 REFERENCE 1
REMARK   1  AUTH   B.AHVAZI,H.C.KIM,S.H.KEE,Z.NEMES,P.M.STEINERT
REMARK   1  TITL   THREE-DIMENSIONAL STRUCTURE OF THE HUMAN
REMARK   1  TITL 2 TRANSGLUTAMINASE 3 ENZYME:BINDING OF CALCIUM IONS
REMARK   1  TITL 3 CHANGES STRUCTURE FOR ACTIVATION
REMARK   1  REF    EMBO J.                       V.  21  2055 2002
REMARK   1  REFN                   ISSN 0261-4189
REMARK   1  DOI    10.1093/EMBOJ/21.9.2055
REMARK   1 REFERENCE 2
REMARK   1  AUTH   H.C.KIM,Z.NEMES,W.W.IDLER,C.C.HYDE,P.M.STEINERT,
REMARK   1  AUTH 2 B.AHVAZI
REMARK   1  TITL   CRYSTALLIZATION AND PRELIMINARY X-RAY ANALYSIS OF
REMARK   1  TITL 2 HUMAN TRANSGLUTAMINASE 3 FROM ZYMOGEN TO ACTIVE
REMARK   1  TITL 3 FORM
REMARK   1  REF    J.STRUCT.BIOL.                V. 135    73 2001
REMARK   1  REFN                   ISSN 1047-8477
REMARK   1  DOI    10.1006/JSBI.2001.4384
REMARK   2
REMARK   2 RESOLUTION.    2.40 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : CNS 1.0
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,
REMARK   3               : READ,RICE,SIMONSON,WARREN
REMARK   3
REMARK   3  REFINEMENT TARGET : ENGH & HUBER
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 10.2
REMARK   3   NUMBER OF REFLECTIONS             : 59772
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 SET) : 0.194
REMARK   3   FREE R VALUE                     : 0.248
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL
REMARK   3   FREE R VALUE TEST SET COUNT      : 6071
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.003
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.40
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.55
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 9.60
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2680
REMARK   3   BIN FREE R VALUE                    : 0.3260
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 854
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.011
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 10567
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 10
REMARK   3   SOLVENT ATOMS            : 809
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 18.10
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 24.40
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : -7.64000
REMARK   3    B22 (A**2) : 10.65000
REMARK   3    B33 (A**2) : -3.00000
REMARK   3    B12 (A**2) : -2.76000
REMARK   3    B13 (A**2) : -1.79000
REMARK   3    B23 (A**2) : 0.76000
REMARK   3
REMARK   3  ESTIMATED COORDINATE ERROR.
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.26
REMARK   3   ESD FROM SIGMAA              (A) : 0.32
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00
REMARK   3
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.34
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.39
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.
REMARK   3   BOND LENGTHS                 (A) : 0.006
REMARK   3   BOND ANGLES            (DEGREES) : NULL
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 25.60
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.78
REMARK   3
REMARK   3  ISOTROPIC THERMAL MODEL : ISOTROPIC
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL
REMARK   3
REMARK   3  BULK SOLVENT MODELING.
REMARK   3   METHOD USED : NULL
REMARK   3   KSOL        : NULL
REMARK   3   BSOL        : NULL
REMARK   3
REMARK   3  NCS MODEL : NULL
REMARK   3
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL
REMARK   3
REMARK   3  PARAMETER FILE  1  : NULL
REMARK   3  TOPOLOGY FILE  1   : NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 1NUG COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-FEB-03.
REMARK 100 THE RCSB ID CODE IS RCSB018215.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 22-AUG-02; 24-AUG-02
REMARK 200  TEMPERATURE           (KELVIN) : 100; NULL
REMARK 200  PH                             : 7.5
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : N; Y
REMARK 200  RADIATION SOURCE               : ROTATING ANODE; NSLS
REMARK 200  BEAMLINE                       : NULL; X9B
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU RU200; NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M; NULL
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418; 0.92
REMARK 200  MONOCHROMATOR                  : SI 111 CHANNEL; NULL
REMARK 200  OPTICS                         : MIRRORS; MIRRORS
REMARK 200
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE; CCD
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS IIC; ADSC
REMARK 200                                   QUANTUM 4
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 65766
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.400
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 10.2
REMARK 200  DATA REDUNDANCY                : NULL
REMARK 200  R MERGE                    (I) : NULL
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.55
REMARK 200  COMPLETENESS FOR SHELL     (%) : 97.7
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL
REMARK 200  R MERGE FOR SHELL          (I) : NULL
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH; NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: PDB ENTRY 1L9N
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 57.05
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.86
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM NACL, 100 MM NAHEPES (PH
REMARK 280  7.5) 4-8% PEG 4K, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE
REMARK 280  288K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,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
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 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 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 400
REMARK 400 COMPOUND
REMARK 400 THE ENZYME WAS PROTEOLYZED WITH DISPASE I
REMARK 400 FOR ACTIVATION, MONOQ PURIFIED AND ACTIVATED
REMARK 400 WITH CACL2. THE MGCL2 AND ATP SALT WAS USED
REMARK 400 TO INHIBIT THE ACTIVITY.
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     ASN A   462
REMARK 465     THR A   463
REMARK 465     PRO A   464
REMARK 465     PHE A   465
REMARK 465     ALA A   466
REMARK 465     ALA A   467
REMARK 465     THR A   468
REMARK 465     SER A   469
REMARK 465     SER A   470
REMARK 465     MET A   471
REMARK 465     GLY A   472
REMARK 465     LEU A   473
REMARK 465     GLU A   474
REMARK 465     THR A   475
REMARK 465     GLU A   476
REMARK 465     GLU A   477
REMARK 465     GLN A   478
REMARK 465     LYS B   460
REMARK 465     PRO B   461
REMARK 465     ASN B   462
REMARK 465     THR B   463
REMARK 465     PRO B   464
REMARK 465     PHE B   465
REMARK 465     ALA B   466
REMARK 465     ALA B   467
REMARK 465     THR B   468
REMARK 465     SER B   469
REMARK 465     SER B   470
REMARK 465     MET B   471
REMARK 465     GLY B   472
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    LEU B 637   CA  -  CB  -  CG  ANGL. DEV. =  14.7 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    SER A  76     -138.72    -97.67
REMARK 500    ASN A  77      -41.80   -150.98
REMARK 500    VAL A 155      -49.26   -134.38
REMARK 500    ASP A 183       -3.43     68.99
REMARK 500    ASP A 201       89.11   -153.49
REMARK 500    ARG A 209        8.18    -69.85
REMARK 500    ASP A 227      -29.23     67.74
REMARK 500    ASN A 229       30.61     71.86
REMARK 500    ASP A 303       38.51   -159.36
REMARK 500    ARG A 304       69.82     28.06
REMARK 500    LYS A 321       83.53    -56.30
REMARK 500    GLN A 357      -63.72   -105.75
REMARK 500    ASP A 378       58.75    -99.02
REMARK 500    ASN A 393       39.91   -140.41
REMARK 500    VAL A 530      -67.19   -103.99
REMARK 500    ARG A 587      118.11   -164.55
REMARK 500    PHE A 658      148.29   -178.45
REMARK 500    SER B  76     -163.87   -120.98
REMARK 500    SER B  80     -149.44    -80.04
REMARK 500    TRP B  83      108.40     79.23
REMARK 500    VAL B 155      -53.37   -130.86
REMARK 500    ASP B 183       -8.97     70.88
REMARK 500    ASP B 227      -20.70     63.86
REMARK 500    ASP B 228       21.66   -150.20
REMARK 500    ASN B 235      116.08   -163.70
REMARK 500    HIS B 300       73.18   -117.10
REMARK 500    ASP B 303       40.84   -160.61
REMARK 500    ARG B 304       86.92     10.66
REMARK 500    ASN B 305       12.57   -148.70
REMARK 500    PHE B 329      148.31   -173.61
REMARK 500    GLN B 357      -71.51   -121.11
REMARK 500    VAL B 379        8.26    -67.74
REMARK 500    ASN B 393       43.91   -141.84
REMARK 500    SER B 445      159.74    -48.67
REMARK 500    GLU B 479      128.66    -38.68
REMARK 500    VAL B 530      -60.33    -99.58
REMARK 500    PRO B 544      124.85    -38.01
REMARK 500    ARG B 587      114.80   -169.83
REMARK 500    ASP B 626       59.03     37.75
REMARK 500    LYS B 651       -0.04     66.46
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620  (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620  SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              CA A 703  CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN A 226   O
REMARK 620 2 ASN A 224   OD1  93.5
REMARK 620 3 ALA A 221   O   167.4  84.3
REMARK 620 4 ASP A 228   OD2  89.5 161.9  88.9
REMARK 620 5 HOH A 957   O    75.0  89.2  92.5  74.4
REMARK 620 6 ASN A 224   O   110.9  67.9  79.8 127.3 156.3
REMARK 620 7 ASP A 228   OD1  78.9 148.6 109.2  49.4 117.4  86.3
REMARK 620 N                    1     2     3     4     5     6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              CA A 704  CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SER A 415   O
REMARK 620 2 HOH A1027   O    79.1
REMARK 620 3 HOH A 851   O    74.9  85.6
REMARK 620 4 GLU A 443   OE1  74.8 153.9  87.9
REMARK 620 5 GLU A 448   OE2 118.0  96.0 167.1  95.9
REMARK 620 6 GLU A 443   OE2 116.2 154.4  79.5  46.6  94.2
REMARK 620 7 ASN A 393   OD1 160.8  92.0  87.5 112.9  79.6  66.8
REMARK 620 N                    1     2     3     4     5     6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MG A 705  MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SER A 307   O
REMARK 620 2 HOH A 993   O    97.9
REMARK 620 3 HOH A1013   O    74.0  83.4
REMARK 620 4 ASP A 303   OD2 147.4 114.7 108.4
REMARK 620 5 ASN A 305   OD1  74.1 168.7 101.6  73.6
REMARK 620 6 ASP A 301   OD2  87.1  95.3 160.6  89.8  76.6
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              CA B 703  CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH B 972   O
REMARK 620 2 ASP B 228   OD2  74.7
REMARK 620 3 ASN B 226   O    71.8  94.0
REMARK 620 4 ASN B 224   OD1  85.3 154.8  94.2
REMARK 620 5 ASN B 224   O   155.0 125.9 115.7  70.7
REMARK 620 6 ALA B 221   O    88.7  86.7 159.5  77.5  79.5
REMARK 620 7 ASP B 228   OD1 112.7  48.7  78.3 156.4  92.3 116.3
REMARK 620 N                    1     2     3     4     5     6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              CA B 704  CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU B 448   OE2
REMARK 620 2 GLU B 443   OE1  81.6
REMARK 620 3 SER B 415   O   112.6  78.4
REMARK 620 4 HOH B 978   O    97.7 165.6  88.7
REMARK 620 5 HOH B 805   O   168.0  98.8  79.0  84.8
REMARK 620 6 GLU B 443   OE2  93.3  50.2 118.2 144.0  78.1
REMARK 620 7 ASN B 393   OD1  76.8 117.8 163.0  75.7  92.7  73.7
REMARK 620 N                    1     2     3     4     5     6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MG B 705  MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 303   OD2
REMARK 620 2 SER B 307   O   130.5
REMARK 620 3 ASN B 305   OD1  54.4  76.3
REMARK 620 4 ASP B 301   OD2  67.1  94.6  70.2
REMARK 620 N                    1     2     3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 701
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 702
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 703
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 704
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 705
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 701
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 702
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 703
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 704
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 705
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1L9M   RELATED DB: PDB
REMARK 900 ZYMOGEN TRANSGLUTAMINASE 3
REMARK 900 RELATED ID: 1L9N   RELATED DB: PDB
REMARK 900 ACTIVE TRANSGLUTAMINASE 3
REMARK 900 RELATED ID: 1NUD   RELATED DB: PDB
REMARK 900 TRANSGLUTAMINASE 3 ENZYME (3 CALCIUMS, ACTIVE FORM)
REMARK 900 RELATED ID: 1NUF   RELATED DB: PDB
REMARK 900 TRANSGLUTAMINASE 3 ENZYME (1 CALCIUM, INACTIVE FORM)
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE FOLLOWING RESIDUES ARE NOTED AS CONFLICTS
REMARK 999 IN THE SWISS-PROT DATABASE: K562R, G654R (SEQUENCE
REMARK 999 DATABASE NUMBERING).
REMARK 999 ACCORDING TO THE AUTHOR, RESIDUE 251 (SEQUENCE
REMARK 999 DATABASE NUMBERING) IS ASP AND DOES NOT REPRESENT
REMARK 999 A MUTATION BUT A MISTAKE IN THE SWISS-PROT DATABASE.
DBREF  1NUG A    1   692  UNP    Q08188   TGM3_HUMAN       2    693
DBREF  1NUG B    1   692  UNP    Q08188   TGM3_HUMAN       2    693
SEQADV 1NUG ASP A  250  UNP  Q08188    ASN   251 SEE REMARK 999
SEQADV 1NUG LEU A  264  UNP  Q08188    PHE   265 ENGINEERED
SEQADV 1NUG ARG A  561  UNP  Q08188    LYS   562 SEE REMARK 999
SEQADV 1NUG ARG A  653  UNP  Q08188    GLY   654 SEE REMARK 999
SEQADV 1NUG ASP B  250  UNP  Q08188    ASN   251 SEE REMARK 999
SEQADV 1NUG LEU B  264  UNP  Q08188    PHE   265 ENGINEERED
SEQADV 1NUG ARG B  561  UNP  Q08188    LYS   562 SEE REMARK 999
SEQADV 1NUG ARG B  653  UNP  Q08188    GLY   654 SEE REMARK 999
SEQRES   1 A  692  ALA ALA LEU GLY VAL GLN SER ILE ASN TRP GLN THR ALA
SEQRES   2 A  692  PHE ASN ARG GLN ALA HIS HIS THR ASP LYS PHE SER SER
SEQRES   3 A  692  GLN GLU LEU ILE LEU ARG ARG GLY GLN ASN PHE GLN VAL
SEQRES   4 A  692  LEU MET ILE MET ASN LYS GLY LEU GLY SER ASN GLU ARG
SEQRES   5 A  692  LEU GLU PHE ILE VAL SER THR GLY PRO TYR PRO SER GLU
SEQRES   6 A  692  SER ALA MET THR LYS ALA VAL PHE PRO LEU SER ASN GLY
SEQRES   7 A  692  SER SER GLY GLY TRP SER ALA VAL LEU GLN ALA SER ASN
SEQRES   8 A  692  GLY ASN THR LEU THR ILE SER ILE SER SER PRO ALA SER
SEQRES   9 A  692  ALA PRO ILE GLY ARG TYR THR MET ALA LEU GLN ILE PHE
SEQRES  10 A  692  SER GLN GLY GLY ILE SER SER VAL LYS LEU GLY THR PHE
SEQRES  11 A  692  ILE LEU LEU PHE ASN PRO TRP LEU ASN VAL ASP SER VAL
SEQRES  12 A  692  PHE MET GLY ASN HIS ALA GLU ARG GLU GLU TYR VAL GLN
SEQRES  13 A  692  GLU ASP ALA GLY ILE ILE PHE VAL GLY SER THR ASN ARG
SEQRES  14 A  692  ILE GLY MET ILE GLY TRP ASN PHE GLY GLN PHE GLU GLU
SEQRES  15 A  692  ASP ILE LEU SER ILE CYS LEU SER ILE LEU ASP ARG SER
SEQRES  16 A  692  LEU ASN PHE ARG ARG ASP ALA ALA THR ASP VAL ALA SER
SEQRES  17 A  692  ARG ASN ASP PRO LYS TYR VAL GLY ARG VAL LEU SER ALA
SEQRES  18 A  692  MET ILE ASN SER ASN ASP ASP ASN GLY VAL LEU ALA GLY
SEQRES  19 A  692  ASN TRP SER GLY THR TYR THR GLY GLY ARG ASP PRO ARG
SEQRES  20 A  692  SER TRP ASP GLY SER VAL GLU ILE LEU LYS ASN TRP LYS
SEQRES  21 A  692  LYS SER GLY LEU SER PRO VAL ARG TYR GLY GLN CYS TRP
SEQRES  22 A  692  VAL PHE ALA GLY THR LEU ASN THR ALA LEU ARG SER LEU
SEQRES  23 A  692  GLY ILE PRO SER ARG VAL ILE THR ASN PHE ASN SER ALA
SEQRES  24 A  692  HIS ASP THR ASP ARG ASN LEU SER VAL ASP VAL TYR TYR
SEQRES  25 A  692  ASP PRO MET GLY ASN PRO LEU ASP LYS GLY SER ASP SER
SEQRES  26 A  692  VAL TRP ASN PHE HIS VAL TRP ASN GLU GLY TRP PHE VAL
SEQRES  27 A  692  ARG SER ASP LEU GLY PRO SER TYR GLY GLY TRP GLN VAL
SEQRES  28 A  692  LEU ASP ALA THR PRO GLN GLU ARG SER GLN GLY VAL PHE
SEQRES  29 A  692  GLN CYS GLY PRO ALA SER VAL ILE GLY VAL ARG GLU GLY
SEQRES  30 A  692  ASP VAL GLN LEU ASN PHE ASP MET PRO PHE ILE PHE ALA
SEQRES  31 A  692  GLU VAL ASN ALA ASP ARG ILE THR TRP LEU TYR ASP ASN
SEQRES  32 A  692  THR THR GLY LYS GLN TRP LYS ASN SER VAL ASN SER HIS
SEQRES  33 A  692  THR ILE GLY ARG TYR ILE SER THR LYS ALA VAL GLY SER
SEQRES  34 A  692  ASN ALA ARG MET ASP VAL THR ASP LYS TYR LYS TYR PRO
SEQRES  35 A  692  GLU GLY SER ASP GLN GLU ARG GLN VAL PHE GLN LYS ALA
SEQRES  36 A  692  LEU GLY LYS LEU LYS PRO ASN THR PRO PHE ALA ALA THR
SEQRES  37 A  692  SER SER MET GLY LEU GLU THR GLU GLU GLN GLU PRO SER
SEQRES  38 A  692  ILE ILE GLY LYS LEU LYS VAL ALA GLY MET LEU ALA VAL
SEQRES  39 A  692  GLY LYS GLU VAL ASN LEU VAL LEU LEU LEU LYS ASN LEU
SEQRES  40 A  692  SER ARG ASP THR LYS THR VAL THR VAL ASN MET THR ALA
SEQRES  41 A  692  TRP THR ILE ILE TYR ASN GLY THR LEU VAL HIS GLU VAL
SEQRES  42 A  692  TRP LYS ASP SER ALA THR MET SER LEU ASP PRO GLU GLU
SEQRES  43 A  692  GLU ALA GLU HIS PRO ILE LYS ILE SER TYR ALA GLN TYR
SEQRES  44 A  692  GLU ARG TYR LEU LYS SER ASP ASN MET ILE ARG ILE THR
SEQRES  45 A  692  ALA VAL CYS LYS VAL PRO ASP GLU SER GLU VAL VAL VAL
SEQRES  46 A  692  GLU ARG ASP ILE ILE LEU ASP ASN PRO THR LEU THR LEU
SEQRES  47 A  692  GLU VAL LEU ASN GLU ALA ARG VAL ARG LYS PRO VAL ASN
SEQRES  48 A  692  VAL GLN MET LEU PHE SER ASN PRO LEU ASP GLU PRO VAL
SEQRES  49 A  692  ARG ASP CYS VAL LEU MET VAL GLU GLY SER GLY LEU LEU
SEQRES  50 A  692  LEU GLY ASN LEU LYS ILE ASP VAL PRO THR LEU GLY PRO
SEQRES  51 A  692  LYS GLU ARG SER ARG VAL ARG PHE ASP ILE LEU PRO SER
SEQRES  52 A  692  ARG SER GLY THR LYS GLN LEU LEU ALA ASP PHE SER CYS
SEQRES  53 A  692  ASN LYS PHE PRO ALA ILE LYS ALA MET LEU SER ILE ASP
SEQRES  54 A  692  VAL ALA GLU
SEQRES   1 B  692  ALA ALA LEU GLY VAL GLN SER ILE ASN TRP GLN THR ALA
SEQRES   2 B  692  PHE ASN ARG GLN ALA HIS HIS THR ASP LYS PHE SER SER
SEQRES   3 B  692  GLN GLU LEU ILE LEU ARG ARG GLY GLN ASN PHE GLN VAL
SEQRES   4 B  692  LEU MET ILE MET ASN LYS GLY LEU GLY SER ASN GLU ARG
SEQRES   5 B  692  LEU GLU PHE ILE VAL SER THR GLY PRO TYR PRO SER GLU
SEQRES   6 B  692  SER ALA MET THR LYS ALA VAL PHE PRO LEU SER ASN GLY
SEQRES   7 B  692  SER SER GLY GLY TRP SER ALA VAL LEU GLN ALA SER ASN
SEQRES   8 B  692  GLY ASN THR LEU THR ILE SER ILE SER SER PRO ALA SER
SEQRES   9 B  692  ALA PRO ILE GLY ARG TYR THR MET ALA LEU GLN ILE PHE
SEQRES  10 B  692  SER GLN GLY GLY ILE SER SER VAL LYS LEU GLY THR PHE
SEQRES  11 B  692  ILE LEU LEU PHE ASN PRO TRP LEU ASN VAL ASP SER VAL
SEQRES  12 B  692  PHE MET GLY ASN HIS ALA GLU ARG GLU GLU TYR VAL GLN
SEQRES  13 B  692  GLU ASP ALA GLY ILE ILE PHE VAL GLY SER THR ASN ARG
SEQRES  14 B  692  ILE GLY MET ILE GLY TRP ASN PHE GLY GLN PHE GLU GLU
SEQRES  15 B  692  ASP ILE LEU SER ILE CYS LEU SER ILE LEU ASP ARG SER
SEQRES  16 B  692  LEU ASN PHE ARG ARG ASP ALA ALA THR ASP VAL ALA SER
SEQRES  17 B  692  ARG ASN ASP PRO LYS TYR VAL GLY ARG VAL LEU SER ALA
SEQRES  18 B  692  MET ILE ASN SER ASN ASP ASP ASN GLY VAL LEU ALA GLY
SEQRES  19 B  692  ASN TRP SER GLY THR TYR THR GLY GLY ARG ASP PRO ARG
SEQRES  20 B  692  SER TRP ASP GLY SER VAL GLU ILE LEU LYS ASN TRP LYS
SEQRES  21 B  692  LYS SER GLY LEU SER PRO VAL ARG TYR GLY GLN CYS TRP
SEQRES  22 B  692  VAL PHE ALA GLY THR LEU ASN THR ALA LEU ARG SER LEU
SEQRES  23 B  692  GLY ILE PRO SER ARG VAL ILE THR ASN PHE ASN SER ALA
SEQRES  24 B  692  HIS ASP THR ASP ARG ASN LEU SER VAL ASP VAL TYR TYR
SEQRES  25 B  692  ASP PRO MET GLY ASN PRO LEU ASP LYS GLY SER ASP SER
SEQRES  26 B  692  VAL TRP ASN PHE HIS VAL TRP ASN GLU GLY TRP PHE VAL
SEQRES  27 B  692  ARG SER ASP LEU GLY PRO SER TYR GLY GLY TRP GLN VAL
SEQRES  28 B  692  LEU ASP ALA THR PRO GLN GLU ARG SER GLN GLY VAL PHE
SEQRES  29 B  692  GLN CYS GLY PRO ALA SER VAL ILE GLY VAL ARG GLU GLY
SEQRES  30 B  692  ASP VAL GLN LEU ASN PHE ASP MET PRO PHE ILE PHE ALA
SEQRES  31 B  692  GLU VAL ASN ALA ASP ARG ILE THR TRP LEU TYR ASP ASN
SEQRES  32 B  692  THR THR GLY LYS GLN TRP LYS ASN SER VAL ASN SER HIS
SEQRES  33 B  692  THR ILE GLY ARG TYR ILE SER THR LYS ALA VAL GLY SER
SEQRES  34 B  692  ASN ALA ARG MET ASP VAL THR ASP LYS TYR LYS TYR PRO
SEQRES  35 B  692  GLU GLY SER ASP GLN GLU ARG GLN VAL PHE GLN LYS ALA
SEQRES  36 B  692  LEU GLY LYS LEU LYS PRO ASN THR PRO PHE ALA ALA THR
SEQRES  37 B  692  SER SER MET GLY LEU GLU THR GLU GLU GLN GLU PRO SER
SEQRES  38 B  692  ILE ILE GLY LYS LEU LYS VAL ALA GLY MET LEU ALA VAL
SEQRES  39 B  692  GLY LYS GLU VAL ASN LEU VAL LEU LEU LEU LYS ASN LEU
SEQRES  40 B  692  SER ARG ASP THR LYS THR VAL THR VAL ASN MET THR ALA
SEQRES  41 B  692  TRP THR ILE ILE TYR ASN GLY THR LEU VAL HIS GLU VAL
SEQRES  42 B  692  TRP LYS ASP SER ALA THR MET SER LEU ASP PRO GLU GLU
SEQRES  43 B  692  GLU ALA GLU HIS PRO ILE LYS ILE SER TYR ALA GLN TYR
SEQRES  44 B  692  GLU ARG TYR LEU LYS SER ASP ASN MET ILE ARG ILE THR
SEQRES  45 B  692  ALA VAL CYS LYS VAL PRO ASP GLU SER GLU VAL VAL VAL
SEQRES  46 B  692  GLU ARG ASP ILE ILE LEU ASP ASN PRO THR LEU THR LEU
SEQRES  47 B  692  GLU VAL LEU ASN GLU ALA ARG VAL ARG LYS PRO VAL ASN
SEQRES  48 B  692  VAL GLN MET LEU PHE SER ASN PRO LEU ASP GLU PRO VAL
SEQRES  49 B  692  ARG ASP CYS VAL LEU MET VAL GLU GLY SER GLY LEU LEU
SEQRES  50 B  692  LEU GLY ASN LEU LYS ILE ASP VAL PRO THR LEU GLY PRO
SEQRES  51 B  692  LYS GLU ARG SER ARG VAL ARG PHE ASP ILE LEU PRO SER
SEQRES  52 B  692  ARG SER GLY THR LYS GLN LEU LEU ALA ASP PHE SER CYS
SEQRES  53 B  692  ASN LYS PHE PRO ALA ILE LYS ALA MET LEU SER ILE ASP
SEQRES  54 B  692  VAL ALA GLU
HET     CL  A 701       1
HET     CL  A 702       1
HET     CA  A 703       1
HET     CA  A 704       1
HET     MG  A 705       1
HET     CL  B 701       1
HET     CL  B 702       1
HET     CA  B 703       1
HET     CA  B 704       1
HET     MG  B 705       1
HETNAM      CL CHLORIDE ION
HETNAM      CA CALCIUM ION
HETNAM      MG MAGNESIUM ION
FORMUL   3   CL    4(CL 1-)
FORMUL   5   CA    4(CA 2+)
FORMUL   7   MG    2(MG 2+)
FORMUL  13  HOH   *809(H2 O)
HELIX    1   1 GLN A   11  HIS A   19  1                                   9
HELIX    2   2 ASN A  147  GLN A  156  1                                  10
HELIX    3   3 ASP A  183  ASP A  193  1                                  11
HELIX    4   4 SER A  195  ASP A  201  1                                   7
HELIX    5   5 ASP A  201  ARG A  209  1                                   9
HELIX    6   6 ASP A  211  ILE A  223  1                                  13
HELIX    7   7 ASP A  245  TRP A  249  5                                   5
HELIX    8   8 SER A  252  SER A  262  1                                  11
HELIX    9   9 GLN A  271  GLY A  287  1                                  17
HELIX   10  10 GLY A  343  GLY A  347  5                                   5
HELIX   11  11 VAL A  371  GLY A  377  1                                   7
HELIX   12  12 ASP A  384  ALA A  394  1                                  11
HELIX   13  13 VAL A  435  LYS A  440  1                                   6
HELIX   14  14 SER A  445  LYS A  460  1                                  16
HELIX   15  15 SER A  555  ARG A  561  1                                   7
HELIX   16  16 GLN B   11  HIS B   19  1                                   9
HELIX   17  17 ASN B  147  VAL B  155  1                                   9
HELIX   18  18 ASP B  183  ASP B  193  1                                  11
HELIX   19  19 SER B  195  ASP B  201  1                                   7
HELIX   20  20 ASP B  201  SER B  208  1                                   8
HELIX   21  21 ASP B  211  ILE B  223  1                                  13
HELIX   22  22 SER B  252  SER B  262  1                                  11
HELIX   23  23 GLN B  271  LEU B  286  1                                  16
HELIX   24  24 GLY B  343  GLY B  347  5                                   5
HELIX   25  25 VAL B  371  GLY B  377  1                                   7
HELIX   26  26 ASP B  384  ALA B  394  1                                  11
HELIX   27  27 VAL B  435  LYS B  440  1                                   6
HELIX   28  28 ASP B  446  LEU B  459  1                                  14
HELIX   29  29 SER B  555  ARG B  561  1                                   7
SHEET    1   A 9 VAL A   5  ASN A   9  0
SHEET    2   A 9 PHE A  37  MET A  43 -1  O  LEU A  40   N  ASN A   9
SHEET    3   A 9 THR A  94  SER A 100 -1  O  LEU A  95   N  MET A  41
SHEET    4   A 9 SER A  84  ASN A  91 -1  N  VAL A  86   O  SER A  98
SHEET    5   A 9 LYS A  70  SER A  76  1  N  SER A  76   O  ALA A  85
SHEET    6   A 9 ARG A  52  THR A  59 -1  N  PHE A  55   O  PHE A  73
SHEET    7   A 9 GLY A 108  SER A 118 -1  O  ALA A 113   N  ILE A  56
SHEET    8   A 9 GLY A 121  LEU A 133 -1  O  GLY A 128   N  MET A 112
SHEET    9   A 9 ILE A  30  ARG A  32  1  N  LEU A  31   O  ILE A 131
SHEET    1   B 2 ALA A 159  GLY A 165  0
SHEET    2   B 2 ILE A 170  ASN A 176 -1  O  GLY A 171   N  VAL A 164
SHEET    1   C 2 LEU A 232  GLY A 234  0
SHEET    2   C 2 VAL A 267  GLY A 270  1  O  VAL A 267   N  ALA A 233
SHEET    1   D 6 ALA A 369  SER A 370  0
SHEET    2   D 6 GLY A 348  LEU A 352 -1  N  VAL A 351   O  ALA A 369
SHEET    3   D 6 VAL A 326  PHE A 337 -1  N  ASN A 333   O  LEU A 352
SHEET    4   D 6 SER A 290  ALA A 299 -1  N  ASN A 295   O  HIS A 330
SHEET    5   D 6 ARG A 420  LYS A 425 -1  O  SER A 423   N  THR A 294
SHEET    6   D 6 ARG A 432  ASP A 434 -1  O  MET A 433   N  THR A 424
SHEET    1   E 3 SER A 307  TYR A 312  0
SHEET    2   E 3 ASP A 395  TYR A 401  1  O  TRP A 399   N  VAL A 310
SHEET    3   E 3 GLN A 408  ASN A 414 -1  O  ASN A 411   N  THR A 398
SHEET    1   F 3 ILE A 482  VAL A 488  0
SHEET    2   F 3 VAL A 498  ASN A 506 -1  O  LEU A 503   N  LYS A 485
SHEET    3   F 3 GLU A 547  ILE A 554 -1  O  ILE A 554   N  VAL A 498
SHEET    1   G 4 LEU A 529  LEU A 542  0
SHEET    2   G 4 LYS A 512  ILE A 523 -1  N  VAL A 516   O  ALA A 538
SHEET    3   G 4 MET A 568  LYS A 576 -1  O  ARG A 570   N  TRP A 521
SHEET    4   G 4 VAL A 583  ILE A 590 -1  O  VAL A 583   N  CYS A 575
SHEET    1   H 3 LEU A 596  VAL A 600  0
SHEET    2   H 3 VAL A 610  SER A 617 -1  O  LEU A 615   N  THR A 597
SHEET    3   H 3 ARG A 653  ILE A 660 -1  O  SER A 654   N  PHE A 616
SHEET    1   I 4 ASN A 640  VAL A 645  0
SHEET    2   I 4 CYS A 627  GLU A 632 -1  N  VAL A 631   O  LEU A 641
SHEET    3   I 4 GLY A 666  SER A 675 -1  O  LEU A 671   N  GLU A 632
SHEET    4   I 4 ILE A 682  VAL A 690 -1  O  ILE A 688   N  LYS A 668
SHEET    1   J 9 VAL B   5  ASN B   9  0
SHEET    2   J 9 PHE B  37  MET B  43 -1  O  LEU B  40   N  ASN B   9
SHEET    3   J 9 THR B  94  SER B 100 -1  O  ILE B  97   N  VAL B  39
SHEET    4   J 9 SER B  84  ASN B  91 -1  N  ASN B  91   O  THR B  94
SHEET    5   J 9 LYS B  70  SER B  76  1  N  SER B  76   O  ALA B  85
SHEET    6   J 9 ARG B  52  THR B  59 -1  N  PHE B  55   O  PHE B  73
SHEET    7   J 9 GLY B 108  SER B 118 -1  O  GLN B 115   N  GLU B  54
SHEET    8   J 9 GLY B 121  LEU B 133 -1  O  LEU B 127   N  MET B 112
SHEET    9   J 9 ILE B  30  ARG B  32  1  N  LEU B  31   O  ILE B 131
SHEET    1   K 2 ALA B 159  SER B 166  0
SHEET    2   K 2 ARG B 169  ASN B 176 -1  O  GLY B 171   N  VAL B 164
SHEET    1   L 2 LEU B 232  GLY B 234  0
SHEET    2   L 2 VAL B 267  GLY B 270  1  O  GLY B 270   N  ALA B 233
SHEET    1   M 6 ALA B 369  SER B 370  0
SHEET    2   M 6 GLY B 348  LEU B 352 -1  N  VAL B 351   O  ALA B 369
SHEET    3   M 6 VAL B 326  PHE B 337 -1  N  GLY B 335   O  GLN B 350
SHEET    4   M 6 SER B 290  ALA B 299 -1  N  ASN B 295   O  HIS B 330
SHEET    5   M 6 ARG B 420  LYS B 425 -1  O  SER B 423   N  THR B 294
SHEET    6   M 6 ARG B 432  ASP B 434 -1  O  MET B 433   N  THR B 424
SHEET    1   N 3 SER B 307  TYR B 312  0
SHEET    2   N 3 ASP B 395  TYR B 401  1  O  TRP B 399   N  VAL B 310
SHEET    3   N 3 GLN B 408  ASN B 414 -1  O  ASN B 411   N  THR B 398
SHEET    1   O 3 ILE B 482  VAL B 488  0
SHEET    2   O 3 VAL B 498  ASN B 506 -1  O  LEU B 503   N  LYS B 485
SHEET    3   O 3 GLU B 547  ILE B 554 -1  O  ILE B 554   N  VAL B 498
SHEET    1   P 4 LEU B 529  LEU B 542  0
SHEET    2   P 4 LYS B 512  ILE B 523 -1  N  MET B 518   O  ASP B 536
SHEET    3   P 4 MET B 568  VAL B 577 -1  O  ARG B 570   N  TRP B 521
SHEET    4   P 4 GLU B 580  ILE B 590 -1  O  VAL B 583   N  CYS B 575
SHEET    1   Q 3 LEU B 596  VAL B 600  0
SHEET    2   Q 3 VAL B 610  SER B 617 -1  O  GLN B 613   N  GLU B 599
SHEET    3   Q 3 ARG B 653  ILE B 660 -1  O  SER B 654   N  PHE B 616
SHEET    1   R 4 LEU B 637  VAL B 645  0
SHEET    2   R 4 CYS B 627  GLY B 633 -1  N  CYS B 627   O  VAL B 645
SHEET    3   R 4 GLY B 666  CYS B 676 -1  O  LEU B 671   N  GLU B 632
SHEET    4   R 4 PHE B 679  VAL B 690 -1  O  ILE B 682   N  PHE B 674
LINK        CA    CA A 703                 O   ASN A 226     1555   1555  2.38
LINK        CA    CA A 703                 OD1 ASN A 224     1555   1555  2.34
LINK        CA    CA A 703                 O   ALA A 221     1555   1555  2.35
LINK        CA    CA A 703                 OD2 ASP A 228     1555   1555  2.76
LINK        CA    CA A 703                 O   HOH A 957     1555   1555  2.52
LINK        CA    CA A 703                 O   ASN A 224     1555   1555  2.42
LINK        CA    CA A 703                 OD1 ASP A 228     1555   1555  2.48
LINK        CA    CA A 704                 O   SER A 415     1555   1555  2.30
LINK        CA    CA A 704                 O   HOH A1027     1555   1555  2.48
LINK        CA    CA A 704                 O   HOH A 851     1555   1555  2.72
LINK        CA    CA A 704                 OE1 GLU A 443     1555   1555  2.74
LINK        CA    CA A 704                 OE2 GLU A 448     1555   1555  2.82
LINK        CA    CA A 704                 OE2 GLU A 443     1555   1555  2.80
LINK        CA    CA A 704                 OD1 ASN A 393     1555   1555  2.57
LINK        MG    MG A 705                 O   SER A 307     1555   1555  2.47
LINK        MG    MG A 705                 O   HOH A 993     1555   1555  2.86
LINK        MG    MG A 705                 O   HOH A1013     1555   1555  2.63
LINK        MG    MG A 705                 OD2 ASP A 303     1555   1555  2.20
LINK        MG    MG A 705                 OD1 ASN A 305     1555   1555  2.56
LINK        MG    MG A 705                 OD2 ASP A 301     1555   1555  2.22
LINK        CA    CA B 703                 O   HOH B 972     1555   1555  2.60
LINK        CA    CA B 703                 OD2 ASP B 228     1555   1555  2.82
LINK        CA    CA B 703                 O   ASN B 226     1555   1555  2.32
LINK        CA    CA B 703                 OD1 ASN B 224     1555   1555  2.49
LINK        CA    CA B 703                 O   ASN B 224     1555   1555  2.38
LINK        CA    CA B 703                 O   ALA B 221     1555   1555  2.45
LINK        CA    CA B 703                 OD1 ASP B 228     1555   1555  2.48
LINK        CA    CA B 704                 OE2 GLU B 448     1555   1555  2.85
LINK        CA    CA B 704                 OE1 GLU B 443     1555   1555  2.74
LINK        CA    CA B 704                 O   SER B 415     1555   1555  2.42
LINK        CA    CA B 704                 O   HOH B 978     1555   1555  2.18
LINK        CA    CA B 704                 O   HOH B 805     1555   1555  2.76
LINK        CA    CA B 704                 OE2 GLU B 443     1555   1555  2.37
LINK        CA    CA B 704                 OD1 ASN B 393     1555   1555  2.43
LINK        MG    MG B 705                 OD2 ASP B 303     1555   1555  2.37
LINK        MG    MG B 705                 O   SER B 307     1555   1555  2.15
LINK        MG    MG B 705                 OD1 ASN B 305     1555   1555  2.91
LINK        MG    MG B 705                 OD2 ASP B 301     1555   1555  2.45
CISPEP   1 ARG A  268    TYR A  269          0        -0.38
CISPEP   2 GLY A  367    PRO A  368          0         1.36
CISPEP   3 ASN A  382    PHE A  383          0         0.08
CISPEP   4 ARG B  268    TYR B  269          0        -0.71
CISPEP   5 GLY B  367    PRO B  368          0         1.53
CISPEP   6 ASN B  382    PHE B  383          0         0.07
SITE     1 AC1  4 ASP A 183  LEU A 185  SER A 186  HOH A 763
SITE     1 AC2  4 ARG B 169  ARG B 587  ILE B 589  ILE B 590
SITE     1 AC3  5 ALA A 221  ASN A 224  ASN A 226  ASP A 228
SITE     2 AC3  5 HOH A 957
SITE     1 AC4  7 ASN A 393  SER A 415  GLU A 443  GLU A 448
SITE     2 AC4  7 ARG A 449  HOH A 851  HOH A1027
SITE     1 AC5  6 ASP A 301  ASP A 303  ASN A 305  SER A 307
SITE     2 AC5  6 HOH A 993  HOH A1013
SITE     1 AC6  4 ASP B 183  SER B 186  HOH B 768  HOH B 929
SITE     1 AC7  4 ARG A 169  ARG A 587  ILE A 590  HOH A 999
SITE     1 AC8  5 ALA B 221  ASN B 224  ASN B 226  ASP B 228
SITE     2 AC8  5 HOH B 972
SITE     1 AC9  6 ASN B 393  SER B 415  GLU B 443  GLU B 448
SITE     2 AC9  6 HOH B 805  HOH B 978
SITE     1 BC1  4 ASP B 301  ASP B 303  ASN B 305  SER B 307
CRYST1   57.510   66.810  116.530  97.24  90.28  98.36 P 1           2
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      0.017388  0.002555  0.000416        0.00000
SCALE2      0.000000  0.015129  0.001954        0.00000
SCALE3      0.000000  0.000000  0.008653        0.00000
      
PROCHECK
Go to PROCHECK summary
 References