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PDBsum entry 1sgx

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Top Page protein ligands metals Protein-protein interface(s) links
Transferase PDB id
1sgx
Jmol
Contents
Protein chains
675 a.a. *
Ligands
5GP ×2
Metals
_CA ×4
_MG ×2
Waters ×861
* Residue conservation analysis
HEADER    TRANSFERASE                             24-FEB-04   1SGX
OBSLTE     02-MAR-11 1SGX
TITLE     CRYSTAL STRUCTURE OF TRANSGLUTAMINASE 3 IN COMPLEX WITH BOUND GMP:
TITLE    2 STRUCTURAL BASIS FOR ALTERATION IN NUCLEOTIDE SPECIFICITY
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 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_CELL_LINE: SF9;
SOURCE  11 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;
SOURCE  12 EXPRESSION_SYSTEM_PLASMID: PET 11A VECTOR (NOVAGEN), PVL1392
SOURCE  13 (INVITROGEN), BAC-N-BLUE (INVITROGEN);
SOURCE  14 OTHER_DETAILS: SEE REFERENCE 5 BELOW
KEYWDS    TRANSGLUTAMINASE, GMP, CALCUIM BINDING, FLUORESCENCE, MODELING,
KEYWDS   2 PHAMACOPHORE CRYTSAL STRUCTURE, TRANSFERASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    B.AHVAZI
REVDAT   5   11-APR-12 1SGX    1       REMARK
REVDAT   4   02-MAR-11 1SGX    1       OBSLTE
REVDAT   3   24-FEB-09 1SGX    1       VERSN
REVDAT   2   19-APR-05 1SGX    1       JRNL
REVDAT   1   27-APR-04 1SGX    0
JRNL        AUTH   B.AHVAZI,K.M.BOESHANS,P.M.STEINERT
JRNL        TITL   ERRATUM: CRYSTAL STRUCTURE OF TRANSGLUTAMINASE 3 IN COMPLEX
JRNL        TITL 2 WITH GMP: STRUCTURAL BASIS FOR NUCLEOTIDE SPECIFICITY
JRNL        REF    J.BIOL.CHEM.                  V. 282 15312 2007
JRNL        REFN                   ISSN 0021-9258
REMARK   1
REMARK   1 REFERENCE 1
REMARK   1  AUTH   B.AHVAZI,K.M.BOESHANS,P.M.STEINERT
REMARK   1  TITL   CRYSTAL STRUCTURE OF TRANSGLUTAMINASE 3 IN COMPLEX WITH GMP:
REMARK   1  TITL 2 STRUCTURAL BASIS FOR NUCLEOTIDE SPECIFICITY
REMARK   1  REF    J.BIOL.CHEM.                  V. 279 26716 2004
REMARK   1  REFN                   ISSN 0021-9258
REMARK   1  PMID   15084592
REMARK   1  DOI    10.1074/JBC.M403481200
REMARK   1 REFERENCE 2
REMARK   1  AUTH   B.AHVAZI,K.M.BOESHANS,W.IDLER,U.BAXA,P.M.STEINERT,
REMARK   1  AUTH 2 F.RASTINEJAD
REMARK   1  TITL   STRUCTURAL BASIS FOR THE COORDINATED REGULATION OF
REMARK   1  TITL 2 TRANSGLUTMINASE 3 BY GUANINE NUCLEOTIDES AND
REMARK   1  TITL 3 CALCIUM/MAGNESIUM
REMARK   1  REF    J.BIOL.CHEM.                  V. 279  7180 2004
REMARK   1  REFN                   ISSN 0021-9258
REMARK   1  DOI    10.1074/JBC.M312310200
REMARK   1 REFERENCE 3
REMARK   1  AUTH   B.AHVAZI,P.M.STEINERT
REMARK   1  TITL   A MODEL FOR THE REACTION MECHANISM OF THE TRANSGLUTAMINASE 3
REMARK   1  TITL 2 ENZYME
REMARK   1  REF    EXP.MOL.MED.                  V.  35   228 2003
REMARK   1  REFN                   ISSN 1226-3613
REMARK   1 REFERENCE 4
REMARK   1  AUTH   B.AHVAZI,K.M.BOESHANS,W.IDLER,U.BAXA,P.M.STEINERT
REMARK   1  TITL   ROLES OF CALCIUM IONS IN THE ACTIVATION AND ACTIVITY OF THE
REMARK   1  TITL 2 TRANSGLUTAMINASE 3 ENZYME
REMARK   1  REF    J.BIOL.CHEM.                  V. 278 23834 2003
REMARK   1  REFN                   ISSN 0021-9258
REMARK   1  DOI    10.1074/JBC.M301162200
REMARK   1 REFERENCE 5
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 TRANSGLUTAMINASE 3
REMARK   1  TITL 2 ENZYME: BINDING OF CALCIUM IONS CHANGE STRUCTURE FOR
REMARK   1  TITL 3 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 6
REMARK   1  AUTH   H.C.KIM,Z.NEMES,W.W.IDLER,C.C.HYDE,P.M.STEINERT,B.AHVAZI
REMARK   1  TITL   CRYSTALLIZATION AND PRELIMINARY X-RAY ANALYSIS OF HUMAN
REMARK   1  TITL 2 TRANSGLUTAMINASE 3 FROM ZYMOGEN TO ACTIVE 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.    2.00 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : CNS 0.9
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) : 2.00
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             : 104830
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) : 0.206
REMARK   3   FREE R VALUE                     : 0.241
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL
REMARK   3   FREE R VALUE TEST SET COUNT      : 9826
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) : 2.00
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.13
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 9.40
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2720
REMARK   3   BIN FREE R VALUE                    : 0.3060
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 1361
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.008
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          : 54
REMARK   3   SOLVENT ATOMS            : 861
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 23.20
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : -6.92000
REMARK   3    B22 (A**2) : 9.36000
REMARK   3    B33 (A**2) : -2.44000
REMARK   3    B12 (A**2) : -2.32000
REMARK   3    B13 (A**2) : 0.39000
REMARK   3    B23 (A**2) : 0.58000
REMARK   3
REMARK   3  ESTIMATED COORDINATE ERROR.
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.24
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) : 0.29
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.26
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) : 25.40
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.75
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:
REMARK   3  CHAIN A (1-692) DISORDER FROM 462-478 AND CHAIN B (1-692)
REMARK   3  DISORDER FROM 460-472, NCS RTWO FOLD AVERAGING WAS
REMARK   3  EMPLOYED DURING REFINEMENT
REMARK   4
REMARK   4 1SGX COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK   5
REMARK   5 THE ENTRY IS OBSOLETED DUE TO PAPER RETRACTION
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-MAR-04.
REMARK 100 THE RCSB ID CODE IS RCSB021698.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 26-APR-03; 26-APR-03
REMARK 200  TEMPERATURE           (KELVIN) : 100; NULL
REMARK 200  PH                             : 7.0
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; 0.97946
REMARK 200  MONOCHROMATOR                  : SI 111 CHANNEL; NULL
REMARK 200  OPTICS                         : NULL; NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE; CCD
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS IV; ADSC QUANTUM 4
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 97639
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000
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     (%) : 90.3
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) : 2.00
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.07
REMARK 200  COMPLETENESS FOR SHELL     (%) : 81.7
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 1RLL AND 1RLN
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 57.14
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.87
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 4-10% (W/V) PEG 6000, 100 MM NA-HEPES
REMARK 280  PH 7.0, 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, 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 300 REMARK: THE BIOLOGICAL ASSEMBLY IS A MONOMER
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 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: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE
REMARK 500   O    HOH A  1408     O    HOH B  1515     1444     2.16
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    GLN A  11       52.93     38.73
REMARK 500    SER A  76     -158.94   -120.64
REMARK 500    TRP A  83      113.40     69.32
REMARK 500    VAL A 155      -54.09   -127.08
REMARK 500    ARG A 169       89.40   -163.47
REMARK 500    ASP A 183       -9.04     74.01
REMARK 500    ASP A 201       88.81   -163.06
REMARK 500    ASP A 227      -26.75     62.32
REMARK 500    ASN A 235      114.33   -160.31
REMARK 500    LYS A 321       91.52    -55.64
REMARK 500    ASN A 393       28.66   -147.12
REMARK 500    VAL A 530      -60.98    -98.94
REMARK 500    GLU A 545       -2.66     68.81
REMARK 500    ARG A 587      123.07   -173.35
REMARK 500    ARG A 607       12.45     57.05
REMARK 500    TYR B  62       59.45   -140.19
REMARK 500    SER B  76     -159.50   -142.29
REMARK 500    SER B  80     -146.76   -118.88
REMARK 500    TRP B  83      133.00     74.94
REMARK 500    VAL B 155      -53.85   -128.30
REMARK 500    ARG B 169       83.74   -165.32
REMARK 500    ASP B 183       -8.26     69.13
REMARK 500    ASP B 201       87.68   -152.14
REMARK 500    ASP B 227      -27.74     63.75
REMARK 500    ASN B 235      117.90   -162.91
REMARK 500    ARG B 304       78.56     21.14
REMARK 500    VAL B 379        5.15    -69.85
REMARK 500    ASN B 393       25.13   -145.77
REMARK 500    VAL B 530      -66.05   -100.78
REMARK 500    GLU B 545       -2.04     68.76
REMARK 500    ARG B 607       13.31     59.68
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS
REMARK 500    CYS B 272        25.0      L          L   OUTSIDE RANGE
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525  M RES CSSEQI
REMARK 525    HOH B1834        DISTANCE =  5.01 ANGSTROMS
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 A1001  CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN A 224   OD1
REMARK 620 2 ASN A 226   O    92.2
REMARK 620 3 ALA A 221   O    79.8 165.1
REMARK 620 4 ASP A 228   OD2 157.4  94.0  89.0
REMARK 620 5 HOH A1272   O    75.0  78.0  87.8  85.1
REMARK 620 6 ASN A 224   O    71.3 107.6  81.9 126.7 146.0
REMARK 620 7 ASP A 228   OD1 151.2  77.6 115.1  51.2 127.4  86.0
REMARK 620 N                    1     2     3     4     5     6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              CA A1002  CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SER A 415   O
REMARK 620 2 HOH A1345   O    86.0
REMARK 620 3 HOH A1161   O    78.5  90.8
REMARK 620 4 GLU A 443   OE1  75.9 158.5  96.6
REMARK 620 5 GLU A 448   OE2 113.6  86.7 167.5  90.1
REMARK 620 6 GLU A 443   OE2 119.1 150.5  80.3  50.9  95.8
REMARK 620 7 ASN A 393   OD1 157.1  76.0  87.7 124.3  79.7  75.6
REMARK 620 N                    1     2     3     4     5     6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MG A1011  MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN A 305   OD1
REMARK 620 2 SER A 307   O    76.2
REMARK 620 3 HOH A1101   O    81.4  78.9
REMARK 620 4 HOH A1309   O   172.3 105.2 106.3
REMARK 620 5 ASP A 303   OD2  84.6 158.6  89.2  95.1
REMARK 620 6 ASP A 301   OD2  85.2 101.2 166.1  87.1  86.1
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              CA B1501  CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH B1786   O
REMARK 620 2 ASP B 228   OD2  88.2
REMARK 620 3 ASN B 226   O    75.1  96.2
REMARK 620 4 ALA B 221   O    89.4  81.5 164.5
REMARK 620 5 ASN B 224   OD1  77.1 157.5  96.3  81.5
REMARK 620 6 ASP B 228   OD1 127.2  51.9  76.6 112.8 149.9
REMARK 620 7 ASN B 224   O   148.6 120.3 111.1  82.9  71.8  83.5
REMARK 620 N                    1     2     3     4     5     6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              CA B1502  CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU B 448   OE2
REMARK 620 2 SER B 415   O   113.1
REMARK 620 3 GLU B 443   OE1  87.6  79.5
REMARK 620 4 HOH B1792   O    82.5  86.9 158.5
REMARK 620 5 HOH B1615   O   168.1  78.1  98.9  94.5
REMARK 620 6 ASN B 393   OD1  72.8 161.9 118.3  76.8  95.3
REMARK 620 7 GLU B 443   OE2  93.6 123.7  51.9 147.4  82.8  71.3
REMARK 620 N                    1     2     3     4     5     6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MG B1511  MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 303   OD1
REMARK 620 2 SER B 307   O   151.5
REMARK 620 3 ASN B 305   OD1  72.2  84.0
REMARK 620 4 HOH B1696   O   107.7  98.9 167.4
REMARK 620 5 ASP B 301   OD2  94.7  96.6  80.2  87.2
REMARK 620 N                    1     2     3     4
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 1001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 1002
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1011
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 1501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 1502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 1511
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 5GP A 904
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 5GP B 914
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1RLL   RELATED DB: PDB
REMARK 900 TRANSGLUTAMINASE 3 INHIBITED BY GDP
REMARK 900 RELATED ID: 1RLN   RELATED DB: PDB
REMARK 900 TRANSGLUTAMINASE 3 INHIBITED BY GTPGAMMAS
DBREF  1SGX A    1   692  UNP    Q08188   TGM3_HUMAN       2    693
DBREF  1SGX B    1   692  UNP    Q08188   TGM3_HUMAN       2    693
SEQADV 1SGX LEU A  264  UNP  Q08188    PHE   265 ENGINEERED
SEQADV 1SGX LEU B  264  UNP  Q08188    PHE   265 ENGINEERED
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 ASN 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 ASN 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     CA  A1001       1
HET     CA  A1002       1
HET     MG  A1011       1
HET     CA  B1501       1
HET     CA  B1502       1
HET     MG  B1511       1
HET    5GP  A 904      24
HET    5GP  B 914      24
HETNAM      CA CALCIUM ION
HETNAM      MG MAGNESIUM ION
HETNAM     5GP GUANOSINE-5'-MONOPHOSPHATE
FORMUL   3   CA    4(CA 2+)
FORMUL   5   MG    2(MG 2+)
FORMUL   9  5GP    2(C10 H14 N5 O8 P)
FORMUL  11  HOH   *861(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 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  GLU A  560  1                                   6
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 ASP B  245  TRP B  249  5                                   5
HELIX   23  23 SER B  252  SER B  262  1                                  11
HELIX   24  24 GLN B  271  GLY B  287  1                                  17
HELIX   25  25 GLY B  343  GLY B  347  5                                   5
HELIX   26  26 VAL B  371  GLU B  376  1                                   6
HELIX   27  27 ASP B  384  ALA B  394  1                                  11
HELIX   28  28 VAL B  435  LYS B  440  1                                   6
HELIX   29  29 SER B  445  LEU B  459  1                                  15
HELIX   30  30 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  99   N  PHE A  37
SHEET    4   A 9 SER A  84  ASN A  91 -1  N  ALA A  89   O  THR A  96
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  SER A 166  0
SHEET    2   B 2 ARG A 169  ASN A 176 -1  O  TRP A 175   N  GLY A 160
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  SER A 298   O  TRP A 327
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 414   N  ARG A 396
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  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  VAL A 690   N  GLY A 666
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  99   N  PHE B  37
SHEET    4   J 9 SER B  84  ASN B  91 -1  N  ALA B  89   O  THR B  96
SHEET    5   J 9 LYS B  70  SER B  76  1  N  SER B  76   O  LEU B  87
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  ALA B 113   N  ILE B  56
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  VAL B 267   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  ILE B 293   O  TRP B 332
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  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 414   N  ARG B 396
SHEET    1   O 2 ARG B 359  SER B 360  0
SHEET    2   O 2 VAL B 363  PHE B 364 -1  O  VAL B 363   N  SER B 360
SHEET    1   P 3 ILE B 482  VAL B 488  0
SHEET    2   P 3 VAL B 498  ASN B 506 -1  O  LEU B 503   N  LYS B 485
SHEET    3   P 3 GLU B 547  ILE B 554 -1  O  ILE B 554   N  VAL B 498
SHEET    1   Q 4 LEU B 529  LEU B 542  0
SHEET    2   Q 4 LYS B 512  ILE B 523 -1  N  LYS B 512   O  LEU B 542
SHEET    3   Q 4 MET B 568  LYS B 576 -1  O  ARG B 570   N  TRP B 521
SHEET    4   Q 4 VAL B 583  ILE B 590 -1  O  VAL B 583   N  CYS B 575
SHEET    1   R 3 LEU B 596  VAL B 600  0
SHEET    2   R 3 VAL B 610  SER B 617 -1  O  LEU B 615   N  THR B 597
SHEET    3   R 3 ARG B 653  ILE B 660 -1  O  SER B 654   N  PHE B 616
SHEET    1   S 4 LEU B 641  VAL B 645  0
SHEET    2   S 4 CYS B 627  GLU B 632 -1  N  VAL B 631   O  LEU B 641
SHEET    3   S 4 GLY B 666  SER B 675 -1  O  ASP B 673   N  MET B 630
SHEET    4   S 4 ILE B 682  VAL B 690 -1  O  ILE B 688   N  LYS B 668
LINK        CA    CA A1001                 OD1 ASN A 224     1555   1555  2.40
LINK        CA    CA A1001                 O   ASN A 226     1555   1555  2.38
LINK        CA    CA A1001                 O   ALA A 221     1555   1555  2.40
LINK        CA    CA A1001                 OD2 ASP A 228     1555   1555  2.69
LINK        CA    CA A1001                 O   HOH A1272     1555   1555  2.41
LINK        CA    CA A1001                 O   ASN A 224     1555   1555  2.34
LINK        CA    CA A1001                 OD1 ASP A 228     1555   1555  2.34
LINK        CA    CA A1002                 O   SER A 415     1555   1555  2.28
LINK        CA    CA A1002                 O   HOH A1345     1555   1555  2.36
LINK        CA    CA A1002                 O   HOH A1161     1555   1555  2.51
LINK        CA    CA A1002                 OE1 GLU A 443     1555   1555  2.60
LINK        CA    CA A1002                 OE2 GLU A 448     1555   1555  2.59
LINK        CA    CA A1002                 OE2 GLU A 443     1555   1555  2.51
LINK        CA    CA A1002                 OD1 ASN A 393     1555   1555  2.35
LINK        MG    MG A1011                 OD1 ASN A 305     1555   1555  2.39
LINK        MG    MG A1011                 O   SER A 307     1555   1555  2.30
LINK        MG    MG A1011                 O   HOH A1101     1555   1555  2.53
LINK        MG    MG A1011                 O   HOH A1309     1555   1555  2.50
LINK        MG    MG A1011                 OD2 ASP A 303     1555   1555  2.14
LINK        MG    MG A1011                 OD2 ASP A 301     1555   1555  2.14
LINK        CA    CA B1501                 O   HOH B1786     1555   1555  2.50
LINK        CA    CA B1501                 OD2 ASP B 228     1555   1555  2.59
LINK        CA    CA B1501                 O   ASN B 226     1555   1555  2.32
LINK        CA    CA B1501                 O   ALA B 221     1555   1555  2.30
LINK        CA    CA B1501                 OD1 ASN B 224     1555   1555  2.23
LINK        CA    CA B1501                 OD1 ASP B 228     1555   1555  2.43
LINK        CA    CA B1501                 O   ASN B 224     1555   1555  2.38
LINK        CA    CA B1502                 OE2 GLU B 448     1555   1555  2.74
LINK        CA    CA B1502                 O   SER B 415     1555   1555  2.28
LINK        CA    CA B1502                 OE1 GLU B 443     1555   1555  2.48
LINK        CA    CA B1502                 O   HOH B1792     1555   1555  2.20
LINK        CA    CA B1502                 O   HOH B1615     1555   1555  2.29
LINK        CA    CA B1502                 OD1 ASN B 393     1555   1555  2.51
LINK        CA    CA B1502                 OE2 GLU B 443     1555   1555  2.54
LINK        MG    MG B1511                 OD1 ASP B 303     1555   1555  2.44
LINK        MG    MG B1511                 O   SER B 307     1555   1555  2.25
LINK        MG    MG B1511                 OD1 ASN B 305     1555   1555  2.23
LINK        MG    MG B1511                 O   HOH B1696     1555   1555  2.65
LINK        MG    MG B1511                 OD2 ASP B 301     1555   1555  2.21
CISPEP   1 ARG A  268    TYR A  269          0         0.03
CISPEP   2 GLY A  367    PRO A  368          0         1.42
CISPEP   3 ASN A  382    PHE A  383          0         0.03
CISPEP   4 ARG B  268    TYR B  269          0        -0.68
CISPEP   5 GLY B  367    PRO B  368          0         1.60
CISPEP   6 ASN B  382    PHE B  383          0        -0.08
SITE     1 AC1  5 ALA A 221  ASN A 224  ASN A 226  ASP A 228
SITE     2 AC1  5 HOH A1272
SITE     1 AC2  6 ASN A 393  SER A 415  GLU A 443  GLU A 448
SITE     2 AC2  6 HOH A1161  HOH A1345
SITE     1 AC3  6 ASP A 301  ASP A 303  ASN A 305  SER A 307
SITE     2 AC3  6 HOH A1101  HOH A1309
SITE     1 AC4  5 ALA B 221  ASN B 224  ASN B 226  ASP B 228
SITE     2 AC4  5 HOH B1786
SITE     1 AC5  6 ASN B 393  SER B 415  GLU B 443  GLU B 448
SITE     2 AC5  6 HOH B1615  HOH B1792
SITE     1 AC6  5 ASP B 301  ASP B 303  ASN B 305  SER B 307
SITE     2 AC6  5 HOH B1696
SITE     1 AC7  8 ARG A 169  LYS A 487  VAL A 488  LEU A 492
SITE     2 AC7  8 ARG A 587  ILE A 589  ILE A 590  HOH A1420
SITE     1 AC8 10 ASN B 168  ARG B 169  LYS B 487  VAL B 488
SITE     2 AC8 10 LEU B 492  ARG B 587  ILE B 589  ILE B 590
SITE     3 AC8 10 HOH B1685  HOH B1801
CRYST1   57.420   66.940  116.720  97.35  90.08  98.38 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      0.017416  0.002565  0.000360        0.00000
SCALE2      0.000000  0.015100  0.001972        0.00000
SCALE3      0.000000  0.000000  0.008640        0.00000
      
PROCHECK
Go to PROCHECK summary
 References