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PDBsum entry 1l9m

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Top Page protein metals Protein-protein interface(s) links
Transferase PDB id
1l9m
Jmol
Contents
Protein chain
675 a.a. *
Metals
_CA ×2
_BR ×2
_CL ×2
Waters ×901
* Residue conservation analysis
HEADER    TRANSFERASE                             26-MAR-02   1L9M
TITLE     THREE-DIMENSIONAL STRUCTURE OF THE HUMAN TRANSGLUTAMINASE 3
TITLE    2 ENZYME: BINDING OF CALCIUM IONS CHANGE STRUCTURE FOR
TITLE    3 ACTIVATION
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: PROTEIN-GLUTAMINE GLUTAMYLTRANSFERASE E3;
COMPND   3 CHAIN: A, B;
COMPND   4 SYNONYM: TRANSGLUTAMINASE 3, TGM3, TGASE E3;
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 TISSUE: FORESKIN;
SOURCE   6 GENE: TGM3;
SOURCE   7 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE   8 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;
SOURCE   9 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE  10 EXPRESSION_SYSTEM_STRAIN: BACULOVIRUS SYSTEM;
SOURCE  11 EXPRESSION_SYSTEM_CELL_LINE: SF9;
SOURCE  12 EXPRESSION_SYSTEM_VECTOR_TYPE: PET 11A VECTOR(NOVAGEN)
SOURCE  13 PVL1392 (INVITROGEN);
SOURCE  14 EXPRESSION_SYSTEM_PLASMID: BAC-N-BLUE, INVITROGEN
KEYWDS    ACTIVATION, CALCIUM BINDING, TRANSGLUTAMINASE, X-RAY
KEYWDS   2 STRUCTURE, TRANSFERASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    B.AHVAZI
REVDAT   5   24-FEB-09 1L9M    1       VERSN
REVDAT   4   07-SEP-04 1L9M    1       REMARK
REVDAT   3   30-SEP-03 1L9M    1       JRNL   DBREF
REVDAT   2   06-NOV-02 1L9M    1       AUTHOR
REVDAT   1   29-MAY-02 1L9M    0
JRNL        AUTH   B.AHVAZI,H.C.KIM,S.H.KEE,Z.NEMES,P.M.STEINERT
JRNL        TITL   THREE-DIMENSIONAL STRUCTURE OF THE HUMAN
JRNL        TITL 2 TRANSGLUTAMINASE 3 ENZYME: BINDING OF CALCIUM IONS
JRNL        TITL 3 CHANGES STRUCTURE FOR ACTIVATION.
JRNL        REF    EMBO J.                       V.  21  2055 2002
JRNL        REFN                   ISSN 0261-4189
JRNL        PMID   11980702
JRNL        DOI    10.1093/EMBOJ/21.9.2055
REMARK   1
REMARK   1 REFERENCE 1
REMARK   1  AUTH   V.C.YEE,L.C.PEDERSEN,I.LE TRONG,P.D.BISHOP,
REMARK   1  AUTH 2 R.E.STENKAMP,D.C.TELLER
REMARK   1  TITL   TWO NON-PROLINE CIS PEPTIDE BONDS MAY BE IMPORTANT
REMARK   1  TITL 2 FOR FACTOR XIII FUNCTION
REMARK   1  REF    FEBS LETT.                    V. 423   291 1998
REMARK   1  REFN                   ISSN 0014-5793
REMARK   1  DOI    10.1016/S0014-5793(98)00098-2
REMARK   1 REFERENCE 2
REMARK   1  AUTH   M.S.WEISS,H.J.METZNER,R.HILGENFELD
REMARK   1  TITL   THREE-DIMENSIONAL STRUCTURE OF A TRANSGLUTAMINASE:
REMARK   1  TITL 2 HUMAN BLOOD COAGULATION FACTOR XII
REMARK   1  REF    PROC.NATL.ACAD.SCI.USA        V.  91  7296 1994
REMARK   1  REFN                   ISSN 0027-8424
REMARK   2
REMARK   2 RESOLUTION.    2.10 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) : 2.10
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)   (%) : NULL
REMARK   3   NUMBER OF REFLECTIONS             : 72799
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) : 0.182
REMARK   3   FREE R VALUE                     : 0.225
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL
REMARK   3   FREE R VALUE TEST SET COUNT      : 7350
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL
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) : 2.10
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.34
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 9.70
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2480
REMARK   3   BIN FREE R VALUE                    : 0.2960
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 1055
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.009
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 10580
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 6
REMARK   3   SOLVENT ATOMS            : 901
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 15.20
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 26.30
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : -3.03000
REMARK   3    B22 (A**2) : 6.12000
REMARK   3    B33 (A**2) : -3.09000
REMARK   3    B12 (A**2) : -2.78000
REMARK   3    B13 (A**2) : -0.56000
REMARK   3    B23 (A**2) : 1.32000
REMARK   3
REMARK   3  ESTIMATED COORDINATE ERROR.
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.23
REMARK   3   ESD FROM SIGMAA              (A) : 0.24
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) : 0.30
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.32
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.
REMARK   3   BOND LENGTHS                 (A) : 0.006
REMARK   3   BOND ANGLES            (DEGREES) : 1.24
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 25.54
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.74
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) : 0.860 ; NULL
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 1.480 ; NULL
REMARK   3   SIDE-CHAIN BOND              (A**2) : 1.190 ; NULL
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 1.790 ; 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: NCS TWO FOLD AVERAGING WAS EMPLOYED
REMARK   3  DURING REFINEMENT
REMARK   4
REMARK   4 1L9M COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 29-MAR-02.
REMARK 100 THE RCSB ID CODE IS RCSB015768.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 15-AUG-99; 26-JUL-00
REMARK 200  TEMPERATURE           (KELVIN) : 100; NULL
REMARK 200  PH                             : 8.5
REMARK 200  NUMBER OF CRYSTALS USED        : 3
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 : DENZO
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 75013
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.100
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     (%) : 93.0
REMARK 200  DATA REDUNDANCY                : NULL
REMARK 200  R MERGE                    (I) : NULL
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 11.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 20.00
REMARK 200  COMPLETENESS FOR SHELL     (%) : 93.0
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 1GGT
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 57.51
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.89
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 4%(W/V) PEG 20K, 100 MM TRIS_HCL(PH
REMARK 280  8.5), VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 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
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465   M RES C SSSEQI
REMARK 465     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     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 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    GLN A  11       51.30     39.67
REMARK 500    SER A  26      159.61    -48.61
REMARK 500    SER A  80     -111.53    -80.74
REMARK 500    ARG A 169      108.40   -164.63
REMARK 500    ASP A 183       -4.93     69.79
REMARK 500    ASP A 201       89.14   -162.90
REMARK 500    ASN A 229      100.48   -169.27
REMARK 500    ARG A 304       54.85     37.17
REMARK 500    LYS A 321       90.53    -58.74
REMARK 500    VAL A 379        1.04    -69.26
REMARK 500    ALA A 394      151.93    -46.61
REMARK 500    TYR A 421       46.27     38.13
REMARK 500    VAL A 530      -63.50    -94.69
REMARK 500    ARG A 607       13.58     58.43
REMARK 500    SER B  80     -144.60   -141.23
REMARK 500    ARG B 169      106.95   -166.26
REMARK 500    ASP B 183      -12.80     67.55
REMARK 500    VAL B 231      -71.69    -87.23
REMARK 500    ASN B 235      109.35   -166.15
REMARK 500    ASP B 301      -93.90    -97.06
REMARK 500    THR B 302       40.82     36.13
REMARK 500    GLN B 357      -66.06   -127.22
REMARK 500    HIS B 416       15.53   -143.93
REMARK 500    LEU B 459      -87.23    -79.49
REMARK 500    GLU B 474       58.93   -115.81
REMARK 500    THR B 475      116.40    -33.79
REMARK 500    GLU B 477     -163.39    -66.44
REMARK 500    GLU B 479      131.92    -37.65
REMARK 500    SER B 481      -42.60     74.15
REMARK 500    SER B 508     -134.11    -73.05
REMARK 500    ARG B 509       48.35   -176.85
REMARK 500    THR B 511      105.46     63.57
REMARK 500    ASP B 536      170.23    177.04
REMARK 500    GLU B 545       -8.26     65.49
REMARK 500    GLU B 580      136.70   -173.64
REMARK 500    ASN B 602      176.99    178.16
REMARK 500    LYS B 651        7.74     57.21
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 702  CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN A 226   O
REMARK 620 2 ALA A 221   O   160.5
REMARK 620 3 ASN A 224   OD1  98.6  85.2
REMARK 620 4 HOH A 784   O    94.1  74.0 148.7
REMARK 620 5 HOH A 977   O    83.4  77.4  90.8  62.3
REMARK 620 6 ASN A 224   O   113.3  86.2  73.7 126.5 158.4
REMARK 620 7 ASN A 229   O    79.8 104.9 154.4  56.2 114.1  83.4
REMARK 620 N                    1     2     3     4     5     6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              CA B 705  CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN B 224   O
REMARK 620 2 ASN B 224   OD1  78.7
REMARK 620 3 ASN B 226   N    74.7  61.9
REMARK 620 4 ALA B 221   O    87.2  88.5 147.5
REMARK 620 5 ASN B 226   O   118.1  99.7  53.0 154.4
REMARK 620 6 HOH B1001   O   164.5  94.3 114.4  78.8  76.5
REMARK 620 7 ASN B 229   O    86.4 161.0 103.0 102.6  77.0 102.9
REMARK 620 N                    1     2     3     4     5     6
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BR A 700
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 701
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 702
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BR B 703
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 704
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 705
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1L9M   RELATED DB: PDB
REMARK 900 ZYMOGEN TRANSGLUTAMINSE 3
REMARK 900 RELATED ID: 1L9N   RELATED DB: PDB
REMARK 900 THE ACTIVATED FORM BOUND TO CALCIUM IONS
REMARK 999
REMARK 999 THE FOLLOWING RESIDUES ARE NOTED AS CONFLICTS IN THE SWISS-PROT
REMARK 999 DATABASE: K12T, K561R, G654R. ACCORDING TO THE AUTHOR, RESIDUE
REMARK 999 250 IS ASP AND DOES NOT REPRESENT A MUTATION BUT A MISTAKE IN
REMARK 999 THE SWISS-PROT DATABASE.
DBREF  1L9M A    1   692  UNP    Q08188   TGM3_HUMAN       2    693
DBREF  1L9M B    1   692  UNP    Q08188   TGM3_HUMAN       2    693
SEQADV 1L9M ASP A  250  UNP  Q08188    ASN   251 SEE REMARK 999
SEQADV 1L9M LEU A  264  UNP  Q08188    PHE   265 ENGINEERED
SEQADV 1L9M ARG A  561  UNP  Q08188    LYS   562 SEE REMARK 999
SEQADV 1L9M ARG A  653  UNP  Q08188    GLY   654 SEE REMARK 999
SEQADV 1L9M ASP B  250  UNP  Q08188    ASN   251 SEE REMARK 999
SEQADV 1L9M LEU B  264  UNP  Q08188    PHE   265 ENGINEERED
SEQADV 1L9M ARG B  561  UNP  Q08188    LYS   562 SEE REMARK 999
SEQADV 1L9M 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     BR  A 700       1
HET     CL  A 701       1
HET     CA  A 702       1
HET     BR  B 703       1
HET     CL  B 704       1
HET     CA  B 705       1
HETNAM      BR BROMIDE ION
HETNAM      CL CHLORIDE ION
HETNAM      CA CALCIUM ION
FORMUL   3   BR    2(BR 1-)
FORMUL   4   CL    2(CL 1-)
FORMUL   5   CA    2(CA 2+)
FORMUL   9  HOH   *901(H2 O)
HELIX    1   1 GLN A   11  HIS A   19  1                                   9
HELIX    2   2 ASN A  147  VAL A  155  1                                   9
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  SER A  208  1                                   8
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 GLY A  251  SER A  262  1                                  12
HELIX    9   9 GLN A  271  GLY A  287  1                                  17
HELIX   10  10 VAL A  371  GLY A  377  1                                   7
HELIX   11  11 ASP A  384  ALA A  394  1                                  11
HELIX   12  12 VAL A  435  LYS A  440  1                                   6
HELIX   13  13 SER A  445  LYS A  460  1                                  16
HELIX   14  14 SER A  555  GLU A  560  1                                   6
HELIX   15  15 GLN B   11  HIS B   19  1                                   9
HELIX   16  16 ASN B  147  VAL B  155  1                                   9
HELIX   17  17 ASP B  183  ASP B  193  1                                  11
HELIX   18  18 SER B  195  ASP B  201  1                                   7
HELIX   19  19 ASP B  201  SER B  208  1                                   8
HELIX   20  20 ASP B  211  ILE B  223  1                                  13
HELIX   21  21 ASP B  245  TRP B  249  5                                   5
HELIX   22  22 SER B  252  SER B  262  1                                  11
HELIX   23  23 GLN B  271  GLY B  287  1                                  17
HELIX   24  24 VAL B  371  GLU B  376  1                                   6
HELIX   25  25 ASP B  384  ALA B  394  1                                  11
HELIX   26  26 VAL B  435  LYS B  440  1                                   6
HELIX   27  27 SER B  445  LYS B  460  1                                  16
HELIX   28  28 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  ILE A  97   N  VAL A  39
SHEET    4   A 9 SER A  84  ASN A  91 -1  N  SER A  84   O  SER A 100
SHEET    5   A 9 LYS A  70  SER A  76  1  N  SER A  76   O  LEU A  87
SHEET    6   A 9 ARG A  52  SER A  58 -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  SER A 123   N  ILE A 116
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  SER A 166  0
SHEET    2   B 2 ARG A 169  ASN A 176 -1  O  ILE A 173   N  ILE A 162
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 TRP A 349  LEU A 352 -1  N  VAL A 351   O  ALA A 369
SHEET    3   D 6 VAL A 326  TRP A 336 -1  N  GLY A 335   O  GLN A 350
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  ASP A 402  1  O  TRP A 399   N  VAL A 310
SHEET    3   E 3 LYS A 407  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 LEU A 641  VAL A 645  0
SHEET    2   I 4 CYS A 627  GLU A 632 -1  N  CYS A 627   O  VAL A 645
SHEET    3   I 4 GLY A 666  CYS A 676 -1  O  LEU A 671   N  GLU A 632
SHEET    4   I 4 PHE A 679  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  SER B  84   O  SER B 100
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  SER B  58 -1  N  PHE B  55   O  PHE B  73
SHEET    7   J 9 GLY B 108  SER B 118 -1  O  PHE B 117   N  ARG B  52
SHEET    8   J 9 GLY B 121  LEU B 133 -1  O  SER B 123   N  ILE B 116
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  ASN B 333   O  LEU B 352
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  ARG B 420   N  PHE B 296
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  ASP B 402  1  O  TRP B 399   N  VAL B 310
SHEET    3   N 3 LYS B 407  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  ALA B 548   N  LEU B 504
SHEET    1   P 4 LEU B 529  LEU B 542  0
SHEET    2   P 4 LYS B 512  ILE B 523 -1  N  VAL B 516   O  ALA B 538
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  LEU B 615   N  THR B 597
SHEET    3   Q 3 ARG B 653  ILE B 660 -1  O  VAL B 656   N  MET B 614
SHEET    1   R 4 LEU B 641  VAL B 645  0
SHEET    2   R 4 CYS B 627  GLU B 632 -1  N  LEU B 629   O  ILE B 643
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 688   N  LYS B 668
LINK        CA    CA A 702                 O   ASN A 226     1555   1555  2.56
LINK        CA    CA A 702                 O   ALA A 221     1555   1555  2.50
LINK        CA    CA A 702                 OD1 ASN A 224     1555   1555  2.36
LINK        CA    CA A 702                 O   HOH A 784     1555   1555  3.35
LINK        CA    CA A 702                 O   HOH A 977     1555   1555  2.40
LINK        CA    CA A 702                 O   ASN A 224     1555   1555  2.50
LINK        CA    CA A 702                 O   ASN A 229     1555   1555  2.77
LINK        CA    CA B 705                 O   ASN B 224     1555   1555  2.36
LINK        CA    CA B 705                 OD1 ASN B 224     1555   1555  2.35
LINK        CA    CA B 705                 N   ASN B 226     1555   1555  3.34
LINK        CA    CA B 705                 O   ALA B 221     1555   1555  2.43
LINK        CA    CA B 705                 O   ASN B 226     1555   1555  2.61
LINK        CA    CA B 705                 O   HOH B1001     1555   1555  2.37
LINK        CA    CA B 705                 O   ASN B 229     1555   1555  2.62
CISPEP   1 ARG A  268    TYR A  269          0        -0.21
CISPEP   2 GLY A  367    PRO A  368          0         0.16
CISPEP   3 ASN A  382    PHE A  383          0        -0.62
CISPEP   4 ARG B  268    TYR B  269          0        -0.10
CISPEP   5 GLY B  367    PRO B  368          0         1.73
CISPEP   6 ASN B  382    PHE B  383          0         0.10
SITE     1 AC1  4 ARG A 169  ARG A 587  ILE A 589  ILE A 590
SITE     1 AC2  2 ASP A 183  SER A 186
SITE     1 AC3  5 ALA A 221  ASN A 224  ASN A 226  ASN A 229
SITE     2 AC3  5 HOH A 977
SITE     1 AC4  5 ARG B 169  ARG B 587  ILE B 589  ILE B 590
SITE     2 AC4  5 HOH B1093
SITE     1 AC5  3 ASP B 183  SER B 186  HOH B 773
SITE     1 AC6  6 ALA B 221  ASN B 224  SER B 225  ASN B 226
SITE     2 AC6  6 ASN B 229  HOH B1001
CRYST1   57.709   67.515  116.208  97.24  90.15  98.67 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      0.017328  0.002642  0.000386        0.00000
SCALE2      0.000000  0.014983  0.001932        0.00000
SCALE3      0.000000  0.000000  0.008677        0.00000
      
PROCHECK
Go to PROCHECK summary
 References